pmid	termid	name	comment
PMID:10022828	GO:0110085	mitotic actomyosin contractile ring	(comment: establishment, but not maintenance, of ring localization requires F-actin (assayed using latrunculin A))
PMID:10022828	GO:0110085	mitotic actomyosin contractile ring	(comment: establishment, but not maintenance, of ring localization requires F-actin (assayed using latrunculin A))
PMID:10022921	FYPO:0003773	normal level of transposon-encoded protein in cell	(comment: assayed using Tf1 transposon Gag and IN)
PMID:10022921	FYPO:0003775	decreased transposon-derived cDNA recombination	(comment: assayed using Tf1 transposon plasmid construct)
PMID:10022921	FYPO:0000593	decreased transposition	(comment: assayed using Tf1 transposon plasmid construct)
PMID:10022921	FYPO:0003774	normal level of transposon-derived cDNA in cell	(comment: assayed using Tf1 transposon)
PMID:10022921	FYPO:0003772	normal transposon gene mRNA level	(comment: assayed using Tf1 transposon)
PMID:10087262	FYPO:0006802	dispersed filamentous actin	(Fig. 1a) 'delocalized actin'
PMID:10087262	FYPO:0002720	sensitive to beta-glucanase [has_severity] high	(Fig. 1c)
PMID:10087262	FYPO:0002060	viable vegetative cell population	(comment CHECK - IMPORTANT pck2delta rescues ags1 ox defect, we cant do this genetic interaction type in new interface)
PMID:10087262	GO:0031520	plasma membrane of cell tip	(comment: combined localization and membrane fraction)
PMID:10087262	GO:0032178	medial membrane band	(comment: combined localization and membrane fraction)
PMID:10087262	FYPO:0001084	increased cell wall alpha-glucan level [has_severity] high	(comment: more than threefold over compared with wild-type cells (344%))
PMID:10087262	FYPO:0007294	pear-shaped vegetative cell with actin localized to rounded end [has_penetrance] 12	(comment: translocation of actin from one end to the other) (also Figure 7)
PMID:10087262	FYPO:0002060	viable vegetative cell population	Synthetic lethality was not observed between mok1- 664 and 􏰌pck1, consistent with our previous result showing that pck2􏰇 plays the major role (Toda et al., 1993)
PMID:10087262	FYPO:0003213	explosive cytokinetic cell separation resulting in vegetative cell lysis [has_penetrance] 12	The other was observed as pairs of divided cells associated side-by-side (12%), the cell wall of which appeared fragile and often lysed upon division.
PMID:10087262	GO:0016020	membrane	These results suggested that Mok1 is an stable integral membrane protein, which is consistent with the presence of several transmembrane domains (Fig. 2 a).
PMID:10087262	FYPO:0001188	sensitive to Calcofluor White [has_severity] high	data not shown
PMID:10087262	FYPO:0007293	lysed spherical vegetative cell	mok1-664􏰌pck2 was synthetically lethal at 30􏰊C, a temperature at which either single mutant could grew (Fig. 10b)
PMID:10087262	FYPO:0002061	inviable vegetative cell population	mok1-664􏰌pck2 was synthetically lethal at 30􏰊C, a temperature at which either single mutant could grew (Fig. 10b)
PMID:10091325	GO:0004371	glycerone kinase activity	(comment: activated_by CHEBI:29108 | activated_by CHEBI:18420 | inhibited_by CHEBI:16761)
PMID:10207075	FYPO:0003606	decreased duration of meiotic prophase I	In contrast to the point mutation, the rec8::ura4 strain showed no shortening of prophase in three independent time courses (data not shown). Shortening of the prophase in the point mutation strain may indicate a role of Rec8p in meiosis regulation. Alternative explanations, like shortening of prophase by an additional mutation, were not excluded.
PMID:10226032	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC19F8.07 [part_of] positive regulation of transcription initiation by RNA polymerase II	(comment: Csk1 activated both the monomeric and the Mcs2-bound forms of Mcs6)
PMID:10226032	GO:0043539	protein serine/threonine kinase activator activity [has_input] PomBase:SPBC19F8.07 [part_of] positive regulation of transcription initiation by RNA polymerase II	(comment: mcs6 requires mcs2 for CTD kinase activity but not cyclin-dependent kinase activating kinase activity. mcs2 does not cycle throughout the cell cycle.)
PMID:10226032	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC11B10.09 [part_of] positive regulation of G2/M transition of mitotic cell cycle	Surprisingly, Csk1 also activated Cdc2 in complexes with either Cdc13 or Cig2 cyclins.
PMID:10233152	GO:0005737	cytoplasm	Immunofluorescence microscopy revealed that Pyp1 was localized in the cytoplasm (Figure 3A). Nuclear exclusion of Pyp1 was unaffected by osmotic stress (Figure 3A).
PMID:10233152	GO:0006611	protein export from nucleus	Immunolocalization studies revealed that nuclear accumulation of Spc1 induced by osmotic stress was substantially increased and sustained in crm1–809 cells relative to wild type (Figure 5, A and B). At the 10-min time point, the Spc1 nuclear signal in crm1–809 cells was consistently more intense than observed in wild-type cells. At the 30-min time point after the initial exposure to stress, Spc1 was excluded from the nucleus of wild type, whereas in the crm1–809 cells the intensity of the nuclear Spc1 signal was greater than the cytoplasmic signal (Figure 5A)
PMID:10233152	GO:0005049	nuclear export signal receptor activity [part_of] protein export from nucleus [has_input] PomBase:SPAC24B11.06c	Immunolocalization studies revealed that nuclear accumulation of Spc1 induced by osmotic stress was substantially increased and sustained in crm1–809 cells relative to wild type (Figure 5, A and B). At the 10-min time point, the Spc1 nuclear signal in crm1–809 cells was consistently more intense than observed in wild-type cells. At the 30-min time point after the initial exposure to stress, Spc1 was excluded from the nucleus of wild type, whereas in the crm1–809 cells the intensity of the nuclear Spc1 signal was greater than the cytoplasmic signal (Figure 5A)
PMID:10233152	GO:0005737	cytoplasm [exists_during] cellular response to osmotic stress	Pyp2 was only very faintly detected in unstressed cells (Figure 3B), because expression of pyp2 mRNA is very low in the absence of stress (Shiozaki and Russell, 1996; Wilkinson et al., 1996). After osmotic stress, Pyp2 was readily detected as a cytoplasmic protein that appeared to be excluded from the nucleus (Figure 3B).
PMID:10364209	MOD:00046	O-phospho-L-serine	(Fig. 1B)
PMID:10364209	MOD:00046	O-phospho-L-serine	(Fig. 1B)
PMID:10364209	FYPO:0001357	normal vegetative cell population growth	DNS
PMID:10364209	FYPO:0001357	normal vegetative cell population growth	DNS
PMID:10364209	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAP8A3.08 [assayed_using] PomBase:SPCC645.05c	The same level of Myo2p co-immunoprecipitated with mutant Cdc4p as with wild-type Cdc4p (Fig. 5A).
PMID:10366596	FYPO:0004086	abnormal meiotic centromere clustering	(comment: in zygotic nucleus)
PMID:10373519	FYPO:0000256	mutator [has_severity] high	(Table 2)
PMID:10373519	FYPO:0000256	mutator [has_severity] medium	(Table 2)
PMID:10373519	GO:0006298	mismatch repair	The biochemical properties of Uve1p-mediated mismatch cleavage and the spontaneous mutator phenotype displayed by uve1 null mutants suggest that Uve1p is involved in MMR in vivo. indicates that, in addition to its UV photoproduct cleavage activity, it is a diverse mismatch endo- nuclease with broad substrate specificity.
PMID:10381387	GO:0071957	old mitotic spindle pole body [exists_during] mitotic anaphase B	(comment: it doesn't say old, but it is...)
PMID:10381387	GO:0071957	old mitotic spindle pole body [exists_during] mitotic anaphase B	(comment: it doesn't say old, but it is...)
PMID:10388806	FYPO:0001430	abnormal mitotic cell cycle arrest with unreplicated DNA	(comment: CHECK cdc18delta::p[nmt*.cdc18+-LEU2])
PMID:10388806	FYPO:0001428	normal negative regulation of mitotic DNA replication initiation	(comment: CHECK cdc18delta::p[nmt*.cdc18+-LEU2])
PMID:10388806	FYPO:0002083	inviable swollen elongated cell with enlarged nucleus [has_penetrance] high	(comment: Val: moved down from FYPO:0001429, its a fully penetrant inviable phenotype (anucleate))
PMID:10392445	FYPO:0000474	abolished meiosis	(comment: conditions under which pat1-114 alone induces meiosis & sporulation)
PMID:10398679	GO:0038066	p38MAPK cascade	(comment: CHECK is response to heat/response to denatured protein)
PMID:10398680	FYPO:0003788	nuclear envelope protrusion present during mitosis	(Fig. 1a)
PMID:10398680	FYPO:0004308	abnormal CENP-A containing chromatin organization	(Fig. 6D): Mis12 is thus required for maintaining the inner centromere structure.
PMID:10398680	FYPO:0006190	long mitotic spindle during anaphase A	(Figure 1A,B) (comment: All of these required passage through G1 - i.e. second mitosis)
PMID:10398680	FYPO:0006715	large and small daughter nuclei	(Figure 1A,B) (comment: All of these required passage through G1 - i.e. second mitosis)
PMID:10398680	FYPO:0003241	unequal mitotic sister chromatid segregation	(Figure 1F,7B) (comment: All of these required passage through G1 - i.e. second mitosis)
PMID:10398680	FYPO:0006190	long mitotic spindle during anaphase A	(Figure 2)
PMID:10398680	FYPO:0007304	short bipolar mitotic spindle during anaphase	(Figure 3)
PMID:10398680	FYPO:0006174	abolished mitotic spindle elongation during anaphase B	(Figure 3)
PMID:10398680	FYPO:0007914	mitotic sister chromatid separation during metaphase	(Figure 3) (comment: before phase 3 extension)
PMID:10398680	FYPO:0001042	inviable after spore germination, single or double cell division	(Figure 4)
PMID:10398680	FYPO:0002901	normal protein localization to kinetochore during vegetative growth [assayed_protein] PomBase:SPBC409.04c	(Figure 6) Conversely, the mis6-302 strain integrated with the Mis12-HA gene was used.
PMID:10398680	FYPO:0002901	normal protein localization to kinetochore during vegetative growth [assayed_protein] PomBase:SPAC1687.20c	(Figure 6) Hence, mis6-HA could interact with the centromere in the absence of functional Mis12.
PMID:10398680	FYPO:0002061	inviable vegetative cell population	(Figure 8a)
PMID:10398680	FYPO:0002060	viable vegetative cell population	(Figure 8a)
PMID:10398680	FYPO:0002061	inviable vegetative cell population	(Figure 8a)
PMID:10398680	GO:0000939	inner kinetochore	These results showed that Mis12 was localized at centromeres throughout the cell cycle
PMID:10398680	FYPO:0007914	mitotic sister chromatid separation during metaphase	suggesting that sister centromeres were separated in the metaphase-arrested cells.
PMID:10428959	GO:0005515	protein binding	(Figure 1,2)
PMID:10428959	GO:0005515	protein binding	(Figure 1,2)
PMID:10428959	MOD:00696	phosphorylated residue [added_during] cellular response to oxidative stress	(Figure 2C) (comemnt: vw: not by sty1)
PMID:10428959	GO:0010971	positive regulation of G2/M transition of mitotic cell cycle	(Figure 3)
PMID:10428959	GO:0010971	positive regulation of G2/M transition of mitotic cell cycle	(Figure 3)
PMID:10428959	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high [has_severity] high	(Figure 3) (comment: vw severity 23.4 micron)
PMID:10428959	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high [has_severity] high	(Figure 3) (comment: vw: severity 20.2 micron)
PMID:10428959	FYPO:0001214	sensitive to potassium chloride	(Figure 3b)
PMID:10428959	FYPO:0004481	abolished cell population growth at high temperature	(Figure 3b)
PMID:10428959	FYPO:0004062	increased duration of protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPAC24B11.06c	(Figure 5)
PMID:10428959	FYPO:0001266	normal protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPAC24B11.06c	(Figure 5)
PMID:10428959	FYPO:0004055	decreased protein localization to nucleus during cellular response to salt stress [assayed_protein] PomBase:SPAC24B11.06c	(Figure 6)
PMID:10428959	FYPO:0001885	decreased protein phosphorylation during salt stress [assayed_protein] PomBase:SPBC29B5.01	(Figure 6B)
PMID:10428959	FYPO:0007794	RNA absent from cell during cellular response to oxidative stress [assayed_transcript] PomBase:SPBC3F6.03	(Figure 7)
PMID:10428959	FYPO:0007793	delayed onset of increase in RNA level during cellular response to oxidative stress [assayed_transcript] PomBase:SPCC757.07c	(Figure 7)
PMID:10428959	FYPO:0001789	normal protein localization to nucleus during cellular response to oxidative stress [assayed_protein] PomBase:SPAC1783.07c	(Figure 7)
PMID:10428959	GO:0038066	p38MAPK cascade	(Table 2)
PMID:10428959	GO:0031139	positive regulation of conjugation with cellular fusion	(Table 2)
PMID:10428959	FYPO:0001280	decreased RNA level during cellular response to oxidative stress [assayed_transcript] PomBase:SPBC215.05 [has_penetrance] complete	(comment: vw: sty1-atf1 pathway)
PMID:10428959	FYPO:0001280	decreased RNA level during cellular response to oxidative stress [assayed_transcript] PomBase:SPAC19D5.01 [has_penetrance] complete	(comment: vw: sty1-atf1 pathway)
PMID:10428959	FYPO:0002060	viable vegetative cell population	DNS
PMID:10430583	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] high	(comment: same as rad51delta alone)
PMID:10430583	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] high	(comment: same as rad51delta alone)
PMID:10459013	GO:0044732	mitotic spindle pole body	(comment: present throughout mitotic cell cycle)
PMID:10462529	FYPO:0006037	decreased cytosolic half-mer polysome level	(Fig. 1)
PMID:10462529	FYPO:0006036	increased cytosolic monomeric ribosome level	(Fig. 1)
PMID:10462529	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:10462529	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:10462529	GO:0002183	cytoplasmic translational initiation	(Fig. 2)
PMID:10462529	FYPO:0001490	inviable elongated vegetative cell	(Fig. 2)
PMID:10462529	FYPO:0002085	normal vegetative cell growth	(Fig. 3)
PMID:10462529	FYPO:0006038	normal cytoplasmic translational initiation	(Fig. 3)
PMID:10462529	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:10462529	FYPO:0003503	normal vegetative cell length	(Fig. 5)
PMID:10462529	FYPO:0001497	inviable elongated cell with mitotic cell cycle arrest in interphase [has_severity] high [has_penetrance] high	(Fig. 5)
PMID:10462529	FYPO:0002085	normal vegetative cell growth	(Fig. 5)
PMID:10462529	FYPO:0003503	normal vegetative cell length	(Fig. 5)
PMID:10462529	FYPO:0003125	decreased cytoplasmic translational initiation [assayed_using] PomBase:SPBC582.03	(Fig. 6)
PMID:10462529	FYPO:0007317	decreased cytoplasmic translation [assayed_using] PomBase:SPAC24H6.05	(Fig. 6)
PMID:10462529	FYPO:0001122	elongated vegetative cell	(Fig. 6)
PMID:10462529	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(Fig. 7)
PMID:10462529	FYPO:0000951	inviable small vegetative cell	(Fig. 7)
PMID:10462529	FYPO:0006038	normal cytoplasmic translational initiation	(Figure 4a)
PMID:10462529	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPAC24H6.05	(comment: CHECK extension, of cdc25) Figure 7b
PMID:10473641	FYPO:0004539	short interphase microtubules present in increased numbers	(comment: CHECK broken)
PMID:10521402	FYPO:0006763	abolished meiotic cell cycle DNA replication checkpoint [has_penetrance] 60	(Fig. 1A) rad1 is required for meiotic DNA replication checkpoint
PMID:10521402	FYPO:0006764	normal activation of meiotic cell cycle DNA replication checkpoint [has_penetrance] high	(Fig. 1B)
PMID:10521402	FYPO:0006764	normal activation of meiotic cell cycle DNA replication checkpoint [has_penetrance] high	(Fig. 1B)
PMID:10521402	FYPO:0006763	abolished meiotic cell cycle DNA replication checkpoint [has_penetrance] 60	(Fig. 1B) (comment: CHECK double cds1delta chk1 delta has same phenotype as single cds1delta/cds1 delta)
PMID:10521402	FYPO:0006763	abolished meiotic cell cycle DNA replication checkpoint	(Fig. 1B) cds1 is required for meiotic DNA replication checkpoint
PMID:10521402	FYPO:0006763	abolished meiotic cell cycle DNA replication checkpoint [has_penetrance] high	(Fig. 2A, 2B)
PMID:10521402	FYPO:0006763	abolished meiotic cell cycle DNA replication checkpoint [has_penetrance] high	(Fig. 2A, 2B)
PMID:10521402	FYPO:0001733	abnormal mitotic spindle pole body separation	(Fig. 3B)
PMID:10521402	FYPO:0000734	abnormal meiotic spindle	(Fig. 3B)
PMID:10521402	FYPO:0004929	fragmented nucleus during meiotic cell cycle	(Fig. 3B)
PMID:10521402	FYPO:0000925	unequal meiotic chromosome segregation [has_penetrance] high	(Fig. 3B) data not shown
PMID:10521402	FYPO:0000925	unequal meiotic chromosome segregation [has_penetrance] high	(Fig. 3B) data not shown
PMID:10521402	GO:0072441	response to meiotic DNA replication checkpoint signaling	(Fig. 4)
PMID:10521402	MOD:00048	O4'-phospho-L-tyrosine [present_during] response to meiotic DNA replication checkpoint signaling	(Fig. 4) (comment: CHECK present during meiotic DNA replication checkpoint arrest)
PMID:10521402	FYPO:0006768	increased protein degradation in absence of meiotic DNA replication checkpoint arrest [assayed_using] PomBase:SPBC582.03	(Fig. 5A) (comment: see Fig4A for control)
PMID:10521402	FYPO:0006768	increased protein degradation in absence of meiotic DNA replication checkpoint arrest [assayed_using] PomBase:SPBC582.03	(Fig. 5A) (comment: see Fig4A for control)
PMID:10521402	FYPO:0006766	decreased protein phosphorylation in absence of meiotic DNA replication checkpoint arrest [assayed_using] PomBase:SPBC11B10.09	(Fig. 5A) (comment: see control in Fig4A)
PMID:10521402	FYPO:0006766	decreased protein phosphorylation in absence of meiotic DNA replication checkpoint arrest [assayed_using] PomBase:SPBC11B10.09	(Fig. 5A) (comment: see control in Fig4A)
PMID:10521402	FYPO:0006767	increased cyclin-dependent protein kinase activity in absence of meiotic DNA replication checkpoint arrest [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 5B) (comment: see Fig4B for control)
PMID:10521402	FYPO:0005385	abnormal cell cycle arrest in meiotic metaphase I [has_penetrance] >50	(Fig. 6A, 6D) meiotic cells unable to inhibit CDK1 activity in response to activation of the meiotic DNA replication checkpoint, arrest at metaphase of Meiosis I and do not undergo nuclear division
PMID:10521402	FYPO:0004319	increased cyclin-dependent protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 6C)
PMID:10521402	FYPO:0006764	normal activation of meiotic cell cycle DNA replication checkpoint [has_penetrance] >80	Data not shown prophase arrest with horsetail nuclear morphology see fig3A for pat1ts control
PMID:10521402	FYPO:0006764	normal activation of meiotic cell cycle DNA replication checkpoint [has_penetrance] >80	Data not shown prophase arrest with horsetail nuclear morphology see fig3A for pat1ts control
PMID:10521402	FYPO:0006763	abolished meiotic cell cycle DNA replication checkpoint [has_penetrance] 60	Data not shown when rad1 is deleted checkpoint is not activated and cells attempt meiotic nuclear divisions see also Fig1, 2, 3B
PMID:10521402	FYPO:0006763	abolished meiotic cell cycle DNA replication checkpoint [has_penetrance] high	Data not shown. kinetics same as pat1ts rad1delta diploid
PMID:10521402	FYPO:0006763	abolished meiotic cell cycle DNA replication checkpoint [has_penetrance] high	Data not shown. kinetics same as pat1ts rad1delta diploid
PMID:10521402	FYPO:0006763	abolished meiotic cell cycle DNA replication checkpoint [has_penetrance] high	Data not shown. kinetics same as pat1ts rad1delta diploid
PMID:10523629	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC24H6.05 [assayed_using] PomBase:SPAC8E11.02c [has_severity] medium	(Fig. 2a)
PMID:10523629	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC24H6.05 [assayed_using] PomBase:SPAC8E11.02c	(Fig. 2a)
PMID:10523629	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 35	(Fig. 3C)
PMID:10523629	FYPO:0001128	decreased septation index [has_penetrance] 35	(Fig. 4)
PMID:10523629	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 4)
PMID:10523629	FYPO:0005672	decreased protein localization to nucleus during mitosis [assayed_using] PomBase:SPAC24H6.05	(Fig. 5C)
PMID:10523629	FYPO:0004828	normal protein localization to nucleus during mitosis [assayed_using] PomBase:SPAC24H6.05	(Fig. 5G)
PMID:10523629	FYPO:0003192	abolished protein localization to nucleus during mitosis [assayed_using] PomBase:SPAC24H6.05	(Fig. 5J)
PMID:10523629	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10523629	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10523629	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10523629	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10523629	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10523629	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10523629	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10523629	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10523629	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10523629	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10523629	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10523629	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10523629	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10523629	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC18B5.11c	(Figure 1a)
PMID:10526233	FYPO:0003166	monoseptate vegetative cell with binucleate and anucleate compartments	(comment: (it basically the same as cut except the nucleus is not bisected))
PMID:10526233	FYPO:0003166	monoseptate vegetative cell with binucleate and anucleate compartments	(comment: (it basically the same as cut except the nucleus is not bisected))
PMID:10545452	FYPO:0003710	swollen pear-shaped vegetative cell	(Figure 1, 0) hr
PMID:10545452	FYPO:0003931	inviable aseptate vegetative cell	(Figure 1, 4) hr
PMID:10545452	FYPO:0001006	inviable elongated multinucleate vegetative cell with central constriction	(Figure 1, 8) hr
PMID:10545452	FYPO:0001368	normal actomyosin contractile ring assembly	(comment: i.e next round of replication)
PMID:10545452	FYPO:0004629	normal mitotic DNA replication	(comment: i.e next round of replication)
PMID:10545452	FYPO:0003308	normal protein localization to mitotic spindle pole body during interphase [assayed_protein] PomBase:SPBC21.06c	At the drc1-191 arrest point all binucleate cells were found to have Cdc7p staining localized at one SPB. Merged images of chromosomal staining with DAPI and Cdc7p staining with HA antibodies is shown in Figure 4. The drc1-191 mutant, therefore, arrests at a point in the cell cycle where the septum-promoting Cdc7p is located on one SPB.
PMID:10545452	FYPO:0004691	inviable swollen spherical vegetative cell	Germinated drc1::ura4 spores were capable of polarity establishment (shown with arrows in Figure 6C), but appeared to be incapable of polarity maintenance, causing them to become spherical and highly enlarged (Figure 6C).
PMID:10545452	FYPO:0008044	swollen elongated multinucleate aseptate vegetative cell with more than four nuclei [has_severity] high	Interestingly, unlike the drc1-191 mutant, drc1::ura4 underwent multiple nuclear division cycles causing arrested cells to accumulate up to 32 nuclei.
PMID:10545452	FYPO:0001028	abnormal cell cycle arrest in mitotic interphase [has_penetrance] 80	Microtubule staining confirmed that the drc1-191 cells were arrested in interphase since cells blocked predominantly either with interphase arrays of microtubules or with a postanaphase array of microtubules (Figure 3A, 4 hr).
PMID:10545452	FYPO:0002060	viable vegetative cell population	The drc1-191 mutation was found to be recessive, since cells of the genotype drc1Δ/drc1- 191 resembled wild-type cells and were capable of colony formation under conditions in which the drc1-191 mutant was unable to form colonies (data not shown).
PMID:10545452	FYPO:0002061	inviable vegetative cell population	The drc1-191 mutation was found to be recessive, since cells of the genotype drc1Δ/drc1- 191 resembled wild-type cells and were capable of colony formation under conditions in which the drc1-191 mutant was unable to form colonies (data not shown).
PMID:10545452	FYPO:0002061	inviable vegetative cell population	The drc1-191 myo2-E1 double mutant was unable to form colonies at 24􏰌, a temperature at which both parental strains were capable of colony formation (data not shown).
PMID:10545452	FYPO:0002061	inviable vegetative cell population	The drc1-191 myo2-E1 double mutant was unable to form colonies at 24􏰌, a temperature at which both parental strains were capable of colony formation (data not shown).
PMID:10545452	FYPO:0001234	slow vegetative cell population growth	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly a
PMID:10545452	FYPO:0001234	slow vegetative cell population growth	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly a
PMID:10545452	FYPO:0001495	viable elongated multinucleate vegetative cell	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly and showed cytokinesis defects at 24􏰌, a temperature at which rng2-D5 and cdc4-8 single mutants grew healthily and resembled wild-type cells in morphology (Figure 7).
PMID:10545452	FYPO:0007541	viable branched, swollen, elongated, multinucleate, multiseptate vegetative cell	The drc1-191 rng2-D5 and drc1-191 cdc4-8 double mutants grew extremely poorly and showed cytokinesis defects at 24􏰌, a temperature at which rng2-D5 and cdc4-8 single mutants grew healthily and resembled wild-type cells in morphology (Figure 7). In both double mutant combinations (drc1-191 cdc4-8 and drc1-191 rng2- D5) highly elongated cells with multiple nuclei were seen frequently.
PMID:10545452	FYPO:0002066	inviable elongated aseptate cell [has_penetrance] 80	Upon prolonged incubation at the restrictive temperature (Figure 2, 8 hr), cells assumed a variety of shapes and 􏰍20% of cells were found to contain four nuclei with actomyosin rings, whereas the rest of the cells (80%) still contained only two interphase nuclei and detectable
PMID:10545452	FYPO:0004684	inviable elongated binucleate aseptate cell [has_penetrance] 80	Upon prolonged incubation at the restrictive temperature (Figure 2, 8 hr), cells assumed a variety of shapes and 􏰍20% of cells were found to contain four nuclei with actomyosin rings, whereas the rest of the cells (80%) still contained only two interphase nuclei and detectable
PMID:10545452	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell [has_penetrance] 80	Upon prolonged incubation at the restrictive temperature (Figure 2, 8 hr), cells assumed a variety of shapes and 􏰍20% of cells were found to contain four nuclei with actomyosin rings, whereas the rest of the cells (80%) still contained only two interphase nuclei and detectable
PMID:10545452	FYPO:0006630	inviable elongated tetranucleate aseptate vegetative cell [has_penetrance] 20	Upon prolonged incubation at the restrictive temperature (Figure 2, 8 hr), cells assumed a variety of shapes and 􏰍20% of cells were found to contain four nuclei with actomyosin rings, whereas the rest of the cells (80%) still contained only two interphase nuclei and detectable
PMID:10545452	FYPO:0000272	abolished septum assembly	capable of germination and establishing polarized growth, but were incapable of performing cytokinesis and did not maintain polarity (Figure 6B).
PMID:10545452	FYPO:0000579	normal spore germination	capable of germination and establishing polarized growth, but were incapable of performing cytokinesis and did not maintain polarity (Figure 6B).
PMID:10545452	FYPO:0000026	abnormal vegetative cell polarity	capable of germination and establishing polarized growth, but were incapable of performing cytokinesis and did not maintain polarity (Figure 6B).
PMID:10547441	FYPO:0003889	decreased cell wall thickness at old end during vegetative growth	(comment: CHECK this should be decreased thickness at old end during veg growth)
PMID:10567589	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] low	(Fig. 2d)
PMID:10567589	FYPO:0006692	cut with septum between unequally sized nuclei [has_penetrance] low	(Fig. 2d)
PMID:10567589	FYPO:0001929	normal cell cycle regulation during cellular response to hydroxyurea	(Fig. 3c)
PMID:10567589	FYPO:0001122	elongated vegetative cell	The profile of pmt3􏰗 cells showed a decrease of the number of cells with 2C DNA content and an increase in the number of cells with a DNA content greater or less than 2C DNA content (at times 􏰔2 and 0 h in Fig. 3C)
PMID:10567589	FYPO:0003241	unequal mitotic sister chromatid segregation	The profile of pmt3􏰗 cells showed a decrease of the number of cells with 2C DNA content and an increase in the number of cells with a DNA content greater or less than 2C DNA content (at times 􏰔2 and 0 h in Fig. 3C)
PMID:10574765	FYPO:0001395	normal activation of monopolar cell growth [has_penetrance] 98	(Figure 2a) (comment: Boundary of non growing cell end maintained)
PMID:10574765	FYPO:0001395	normal activation of monopolar cell growth [has_penetrance] 98	(Figure 2b) (comment: Boundary of non growing cell end maintained)
PMID:10574765	FYPO:0001395	normal activation of monopolar cell growth [has_penetrance] 68	(Figure 2c) (comment: Boundary of the non growing cell end not maintained)
PMID:10574765	FYPO:0001397	monopolar actin cortical patch localization to old end [has_penetrance] 70	(Figure 3) (comment: F actin is absent from non growing end)
PMID:10574765	FYPO:0001294	normal actin cortical patch localization [has_penetrance] 70	(Figure 3) (comment: normal at non-growing end)
PMID:10574765	FYPO:0001294	normal actin cortical patch localization [has_penetrance] 70	(Figure 3) (comment: normal at non-growing end)
PMID:10574765	FYPO:0005466	protein mislocalized to non-growing cell tip [has_penetrance] 99 [assayed_using] PomBase:SPAC22H10.07	(Figure 4) (comment: Ral3/cor-CGFP fusion is expressed from pMral3/cor-C)
PMID:10574765	FYPO:0005466	protein mislocalized to non-growing cell tip [has_penetrance] 96 [assayed_using] PomBase:SPAC22H10.07	(Figure 4) (comment: Ral3/cor-CGFP fusion is expressed from pMral3/cor-C)
PMID:10574765	FYPO:0003316	normal protein localization to growing cell tip [has_penetrance] 70 [assayed_using] PomBase:SPAC22H10.07	(Figure 4) (comment: Ral3/cor-CGFP fusion is expressed from pMral3/cor-C)
PMID:10574765	FYPO:0002125	abnormal protein localization to plasma membrane during vegetative growth [assayed_protein] PomBase:SPAC11E3.08c	"(comment: vw: jacky suggested ""protein localisation to the lateral plasma membrane"" but will keep as parent Figures 1, S1 and S2. Cor-C GFP is probably episomal but it is not clear)"
PMID:10581266	FYPO:0003439	branched septum	(Fig. 4)
PMID:10581266	FYPO:0002177	viable vegetative cell with normal cell morphology	(Fig. 6)
PMID:10581266	FYPO:0002729	DNA content increased	(Fig. 6)
PMID:10581266	FYPO:0002025	inviable elongated multinucleate vegetative cell with abnormal septum morphology	(Fig. 6)
PMID:10581266	FYPO:0001493	inviable elongated multinucleate vegetative cell	(Fig. 9)
PMID:10581266	FYPO:0002061	inviable vegetative cell population	(Fig. 9) (comment: high overexpression is lethal)
PMID:10588638	FYPO:0004372	decreased response to mitotic G2 DNA damage checkpoint signaling	(comment: inferred from Chk1 phosphorylation phenotypes)
PMID:10588653	FYPO:0002061	inviable vegetative cell population	(DNS) In all tetrads, the viable colonies were Arp21 Ura2, indicating that arp21 is an essential gene
PMID:10588653	FYPO:0002061	inviable vegetative cell population	(Fig 3)
PMID:10588653	FYPO:0002060	viable vegetative cell population	(Fig 3)
PMID:10588653	FYPO:0002060	viable vegetative cell population	(Fig 3) (comment: CHECK synthetic rescue of cdc3)
PMID:10588653	GO:0005885	Arp2/3 protein complex	(Fig 6)
PMID:10588653	GO:0005885	Arp2/3 protein complex	(Fig 6)
PMID:10588653	GO:0005885	Arp2/3 protein complex	(Fig 6)
PMID:10588653	GO:0005885	Arp2/3 protein complex	(Fig 6)
PMID:10588653	GO:0005885	Arp2/3 protein complex	(Fig 6)
PMID:10588653	GO:0005524	ATP binding	(Fig. 8A) After UV irradiation, we found that both wild-type Arp2p and Arp3p were labeled by 8-azido-[a-32P]ATP, indicating that these actin-related proteins bind ATP as predicted
PMID:10588653	GO:0005524	ATP binding	(Fig. 8A) After UV irradiation, we found that both wild-type Arp2p and Arp3p were labeled by 8-azido-[a-32P]ATP, indicating that these actin-related proteins bind ATP as predicted
PMID:10588653	FYPO:0000650	increased septation index	(Figure 1)
PMID:10588653	FYPO:0001406	increased septum thickness [has_penetrance] high	(Figure 1) after 8 hours, medial region of the cells continued to accumulate excess cell wall material
PMID:10588653	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth [has_penetrance] high	(Figure 1C)
PMID:10588653	GO:0031097	medial cortex [exists_during] mitotic M phase	(Figure 4)
PMID:10588653	GO:0051285	cell cortex of cell tip [exists_during] mitotic M phase	(Figure 4)
PMID:10588653	GO:0030479	actin cortical patch	(Figure 4)
PMID:10588653	FYPO:0007453	decreased protein level in Arp2/3 complex [assayed_using] PomBase:SPAC11H11.06	(Figure 6)
PMID:10588653	FYPO:0007453	decreased protein level in Arp2/3 complex [assayed_using] PomBase:SPBC1778.08c	(Figure 6D)
PMID:10588653	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC11H11.06 [assayed_using] PomBase:SPBC1778.08c	(Figure 8) The most striking difference between wild-type Arp2p and Arp2-E316K was the failure to coimmunoprecipitate labeled Arp3p with Arp2-E316K
PMID:10588653	FYPO:0007454	decreased ATP binding [assayed_using] PomBase:SPAC11H11.06	(Figure 8A). Arp2-E316K mutant protein had a reduced affinity for ATP compared with wild type Arp2p
PMID:10588653	FYPO:0007454	decreased ATP binding [assayed_using] PomBase:SPAC11H11.06	(Figure 8A). T12A protein was also labeled by the ATP analogue, but to a much lesser degree than wild-type Arp2p
PMID:10588653	FYPO:0001324	decreased protein level during vegetative growth	(Figure 8B & C) These results clearly establish that the mutant Arp2-E316K protein turns over more rapidly than wild-type Arp2 protein
PMID:10588653	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] high	DNS
PMID:10588653	FYPO:0001367	normal cytokinesis	DNS
PMID:10588653	FYPO:0001357	normal vegetative cell population growth	DNS
PMID:10588653	FYPO:0006116	abolished protein localization to actin cortical patch	In arp2-1 mutant cells grown at the restrictive temperature, the protein was not detected in patches. Rather, it appeared to be diffusely distributed throughout the cytoplasm (Figure 4C).
PMID:10588653	FYPO:0001324	decreased protein level during vegetative growth	suggesting that the mutant protein is likely less stable than the wild-type Arp2 protein (Figure 6B), a hypothesis confirmed below (see Figure 8C).
PMID:10591634	GO:0004708	MAP kinase kinase activity [has_input] PomBase:SPBC119.08	(comment: IPI and IMP evidence)
PMID:10593886	GO:0004674	protein serine/threonine kinase activity	(comment: CHECK only in vitro data evidence)
PMID:10620770	GO:0004478	methionine adenosyltransferase activity	Figure 2 (B) Specific activities of SAMS from crude extracts (black columns) and relative intensities of the mRNA bands given in A (white columns). The activity was measured as described in Material and Methods.
PMID:10620770	FYPO:0002061	inviable vegetative cell population	No correctly integrated transformants were obtained, suggesting that the disruption is lethal. This was veri®ed by transforming the diploid hx ade6-M210 ura4-D18/h+ ade6-M216 ura4-D18 strain with the construct mentioned above, proper integration of the fragment was con®rmed by Southern blot analysis and the diploids were sporulated. From four different transformants, altogether 96 tetrads were dissected on three different media (MMA+ura+ade+SAM; YEA+ura+ade; and YEA+ura+ade+SAM). In 85 tetrads two spores grew to colonies and in 11 tetrads only one spore or none developed to a colony.
PMID:10620770	FYPO:0002705	sensitive to methionine [has_severity] high	Overexpression of the sam1 gene causes methionine sensitive growth
PMID:10641037	FYPO:0002060	viable vegetative cell population	(Figure 2)
PMID:10641037	FYPO:0007912	normal mitochondrial distribution	(Figure 3b)
PMID:10641037	FYPO:0007915	normal endoplasmic reticulum localization	Because the same distribution pattern was observed when nmt-GFP-13g6 was expressedin the klp3 null allele (Figure 3B), we conclude that ER distribution is not affected by the disruption of klp3 in Fission yeast.
PMID:10641037	FYPO:0002060	viable vegetative cell population	DNS
PMID:10651902	FYPO:0002720	sensitive to beta-glucanase [has_severity] high	(Fig. 6)
PMID:10651902	FYPO:0000647	vegetative cell lysis [has_penetrance] low	(Fig. 6)
PMID:10651902	GO:0005515	protein binding	(comment: Rho1 GTP bound form) (comment: pck2 HR1 domain)
PMID:10651902	GO:0035591	signaling adaptor activity [has_input] PomBase:SPBC12D12.04c	(comment: Rho1 appears to have a dual role in stabilizing and localizing Pck proteins)
PMID:10683155	GO:0000785	chromatin	(comment: constant level throughout cell cycle)
PMID:10683155	FYPO:0000229	cut	(comment: cut if exposed to radiation during S phase, but not if exposed during G2)
PMID:10698951	FYPO:0002061	inviable vegetative cell population	(comment: temperature restrictive for cdc27-P11 alone)
PMID:10698951	FYPO:0002060	viable vegetative cell population	(comment: temperature restrictive for cdc27-P11 alone)
PMID:10712506	FYPO:0006689	increased insertion/deletion frequency [has_severity] low	from materials and methods
PMID:10712506	FYPO:0001719	sensitive to lithium	from materials and methods
PMID:10712506	FYPO:0006689	increased insertion/deletion frequency [has_severity] high	from materials and methods
PMID:10712506	FYPO:0006689	increased insertion/deletion frequency [has_severity] high	from materials and methods
PMID:10718196	FYPO:0000337	abnormal mitosis	DNS
PMID:10725227	FYPO:0001219	increased protein level during cellular response to nitrogen starvation [assayed_using] PomBase:SPAPB2B4.03	(Fig. 10A)
PMID:10725227	FYPO:0000303	decreased conjugation frequency [assayed_using] PomBase:SPAPB2B4.03	(Fig. 10B)
PMID:10725227	FYPO:0000446	cell cycle arrest at mitotic G2/M phase transition [has_penetrance] high	(Fig. 1B)
PMID:10725227	FYPO:0000446	cell cycle arrest at mitotic G2/M phase transition [has_penetrance] high	(Fig. 1B) (comment: G1)
PMID:10725227	FYPO:0000445	cell cycle arrest in mitotic G1 phase [has_penetrance] low	(Fig. 1B) (comment: there is a small G1 peak which get slightly bigger but they also cells arrested in G1 by -N, when refed and shifted to the restrictive temp cannot enter S phase but this is data not shown)
PMID:10725227	FYPO:0002060	viable vegetative cell population	(Fig. 2B)
PMID:10725227	FYPO:0002060	viable vegetative cell population	(Fig. 2B)
PMID:10725227	FYPO:0002060	viable vegetative cell population	(Fig. 2B)
PMID:10725227	FYPO:0002060	viable vegetative cell population	(Fig. 2B)
PMID:10725227	FYPO:0002061	inviable vegetative cell population	(Fig. 2C)
PMID:10725227	FYPO:0002061	inviable vegetative cell population	(Fig. 2C)
PMID:10725227	FYPO:0002060	viable vegetative cell population	(Fig. 2D) (comment: the semi permissive temperature 34.5C for ded1-D5 allows it to suppress cdc19-P1)
PMID:10725227	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPAPB2B4.03 [has_severity] high	(Fig. 3A)
PMID:10725227	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPBC582.03 [has_severity] high	(Fig. 3A)
PMID:10725227	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPBC582.03 [has_severity] high	(Fig. 3B)
PMID:10725227	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPAPB2B4.03 [has_severity] high	(Fig. 3B)
PMID:10725227	GO:0005737	cytoplasm	(Fig. 4B)
PMID:10725227	FYPO:0003125	decreased cytoplasmic translational initiation [has_severity] high	(Fig. 5A) (comment: 35S)
PMID:10725227	FYPO:0007317	decreased cytoplasmic translation [has_severity] high	(Fig. 5B) (comment: 35S)
PMID:10725227	FYPO:0005993	normal cytoplasmic translation [has_severity] high	(Fig. 5B) (comment: 35S)
PMID:10725227	FYPO:0007317	decreased cytoplasmic translation [assayed_using] PomBase:SPAPB2B4.03 [has_severity] high	(Fig. 6) (comment: total protein translation not affected)
PMID:10725227	FYPO:0007317	decreased cytoplasmic translation [assayed_using] PomBase:SPBC582.03 [has_severity] high	(Fig. 6) (comment: total protein translation not affected)
PMID:10725227	FYPO:0001355	decreased vegetative cell population growth	(Fig. 7 B) (comment: over expression of cig2+ cDNAI partially suppresses the rescue of cdc21-M68 by ded1-1D5)
PMID:10725227	FYPO:0002061	inviable vegetative cell population	(Fig. 7 B) (comment: over expression of cig2+ cDNAII suppresses the rescue of cdc21-M68 by ded1-1D5)
PMID:10725227	FYPO:0002061	inviable vegetative cell population	(Fig. 7B)
PMID:10725227	FYPO:0006520	increased cytoplasmic translation [assayed_using] PomBase:SPAPB2B4.03 [has_severity] high	(Fig. 7C, D) (comment: The protein and mRNA levels are compared to cDNA-I which is also expressed from medium strength nmt1 promoter ON)
PMID:10725227	GO:1990625	negative regulation of cytoplasmic translational initiation in response to stress [has_input] PomBase:SPBC582.03 [happens_during] cellular response to nitrogen starvation	(Fig. 9)
PMID:10725227	GO:1990625	negative regulation of cytoplasmic translational initiation in response to stress [has_input] PomBase:SPAPB2B4.03 [happens_during] cellular response to nitrogen starvation	(Fig. 9)
PMID:10725227	FYPO:0002060	viable vegetative cell population	(Table 2)
PMID:10725227	FYPO:0002060	viable vegetative cell population	(Table 2)
PMID:10725227	FYPO:0002060	viable vegetative cell population	(Table 2)
PMID:10733588	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 3D) and data not shown
PMID:10733588	FYPO:0001840	increased minichromosome loss during vegetative growth	Table2
PMID:10733588	FYPO:0001840	increased minichromosome loss during vegetative growth	Table2
PMID:10748059	GO:0044750	high-affinity nickel cation transmembrane transporter activity	(comment: CHECK inhibited_by(CHEBI:48828))
PMID:10749926	FYPO:0003627	normal protein localization [assayed_using] PomBase:SPAC3A11.14c	(Fig. 6)
PMID:10749926	FYPO:0003627	normal protein localization [assayed_using] PomBase:SPBC32F12.04	(Fig. 6)
PMID:10749926	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	(Figure 1B)
PMID:10749926	FYPO:0002061	inviable vegetative cell population	(Figure 1B)
PMID:10749926	FYPO:0000228	lagging mitotic chromosomes	(Figure 4)
PMID:10749926	FYPO:0000229	cut	(Figure 4) (comment: spindle is still present, normally disassembled by cytokinesis)
PMID:10757807	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(comment: same as cdc27-P11 alone)
PMID:10757807	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(comment: same as cds1delta alone)
PMID:10757807	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(comment: same as rqh1delta alone)
PMID:10766248	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication [has_severity] medium	((comment: severity correlates positively with overexpression level)
PMID:10766248	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication [has_severity] medium	(comment: cdc18+ low level overexpression)
PMID:10766248	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication [has_severity] medium	(comment: severity correlates positively with overexpression level, and different isolates with same construct integrated show different Cdc18 level)
PMID:10769201	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC24B11.11c	At 25°C, sid2p-GFP spindle pole body staining was normal, but very few sid2p-GFP rings were detectable, and those which were seen were much fainter than in a wild-type background. We also noted that the spindle pole body signal of sid2p- GFP was absent, or greatly reduced in intensity at 36°C.
PMID:10769201	FYPO:0002822	decreased protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC24B11.11c [has_severity] high	At 25°C, sid2p-GFP spindle pole body staining was normal, but very few sid2p-GFP rings were detectable, and those which were seen were much fainter than in a wild-type background. We also noted that the spindle pole body signal of sid2p- GFP was absent, or greatly reduced in intensity at 36°C.
PMID:10769201	FYPO:0002424	normal actin cortical patch localization during mitotic interphase	F-actin patches were present at the growing tips in interphase (Fig. 4C).
PMID:10769201	FYPO:0007178	abolished protein localization to medial cortex during mitosis [assayed_protein] PomBase:SPBC428.13c	However, we noted that mob1p rings were scarcely detectable in sid2-250 even at 25°C (Fig. 6C)
PMID:10769201	FYPO:0000579	normal spore germination [has_penetrance] 90	In contrast to the full deletion, where the viability of the germinating spores was high (>90%),
PMID:10769201	GO:0005816	spindle pole body [exists_during] mitotic interphase	In early mitotic cells, two dots were observed associated with the nucleus (Fig. 5A). Double staining for the mitotic spindle revealed that the dots were present at the ends, suggesting that they correspond to the spindle pole bodies (Fig. 5B). This was confirmed by co- staining for sid2p (Sparks et al., 1999), which is a known spindle pole antigen (Fig. 5C).
PMID:10769201	FYPO:0004562	binucleate aseptate vegetative cell	In liquid culture, five hours after shift to 36°C, mob1-R4 cells display defects in septum formation (Fig. 2A). Cells are frequently binucleate, without a septum, and with the nuclei in a postmitotic configuration.
PMID:10769201	FYPO:0004562	binucleate aseptate vegetative cell	Next, we examined the effect of increased expression of the mob1 gene from the full-strength nmt1 promoter in wild-type cells. Approximately 6 generations at 25°C (26 hours) after removal of thiamine from the medium (the promoter is turned on after 3-3.5 generations), cells displayed a variety of abnormalities of both septum formation and mitosis, including failure to septate (Fig. 3A; cells marked 1)
PMID:10769201	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC428.13c	No effect upon spindle pole body localisation during mitosis was observed in sid2-250 (Fig. 6C).
PMID:10769201	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC428.13c	Similar results were obtained in cdc14-118, sid1-239, and cdc11-136 mutants (not shown).
PMID:10769201	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC428.13c	Similar results were obtained in cdc14-118, sid1-239, and cdc11-136 mutants (not shown).
PMID:10769201	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC428.13c	Similar results were obtained in cdc14-118, sid1-239, and cdc11-136 mutants (not shown).
PMID:10769201	FYPO:0006919	normal protein localization to nucleus during mitotic interphase [assayed_protein] PomBase:SPCC4B3.15	Staining for mid1p showed the expected nuclear localisation in interphase (Fig. 4E, right panels)
PMID:10769201	FYPO:0007106	normal mitotic spindle morphology	Staining of microtubules indicated that interphase arrays and mitotic spindles were present in the population (Fig. 4D)
PMID:10769201	FYPO:0004328	normal protein localization during mitosis [assayed_protein] PomBase:SPBC12D12.01	The spindle pole body component sad1p was visible on all nuclei (Fig. 4F)
PMID:10769201	FYPO:0002822	decreased protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC428.13c	The spindle pole body signal was greatly reduced in intensity in cdc7-24, spg1-B8, and sid4-SA1 mutants at 36°C.
PMID:10769201	FYPO:0002822	decreased protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC428.13c	The spindle pole body signal was greatly reduced in intensity in cdc7-24, spg1-B8, and sid4-SA1 mutants at 36°C.
PMID:10769201	FYPO:0002822	decreased protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC428.13c	The spindle pole body signal was greatly reduced in intensity in cdc7-24, spg1-B8, and sid4-SA1 mutants at 36°C.
PMID:10769201	FYPO:0004328	normal protein localization during mitosis [assayed_protein] PomBase:SPCC4B3.15	and ring formation in mitotic cells (Fig. 4E, left panels).
PMID:10769201	FYPO:0002150	inviable spore population	five independent diploids examined all showed reduced spore viability. In most tetrads, only one or zero spores could germinate.
PMID:10769201	FYPO:0001252	multinucleate multiseptate vegetative cell	formation of one or more septa without cell cleavage (Fig. 3A; cells marked 2),
PMID:10769201	FYPO:0007568	normal protein localization to mitotic spindle pole body during anaphase [assayed_protein] PomBase:SPBC21.06c	in anaphase cells, cdc7p was associated with the spindle pole bodies of half the nuclei (Fig. 4G), as described previously (Sohrmann et al., 1998).
PMID:10769201	FYPO:0007028	normal protein localization to medial cortex septin ring during vegetative growth [assayed_protein] PomBase:SPAC20G8.05c	the medial ring component cdc15p, which is essential for septation, also formed a ring in the absence of mob1p (Fig. 4H).
PMID:10769212	GO:0110085	mitotic actomyosin contractile ring	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:10769212	GO:0071341	medial cortical node [exists_during] mitotic M phase	(comment: early mitosis; independent of F-actin (assayed using Latrunculin A))
PMID:10769212	FYPO:0002061	inviable vegetative cell population	(comment: inviable at 34 or 37 degrees)
PMID:10769212	FYPO:0002061	inviable vegetative cell population	(comment: inviable at 37 degrees; some growth at 34 degrees)
PMID:10769212	FYPO:0002061	inviable vegetative cell population	(comment: inviable at 37 degrees; some growth at 34 degrees)
PMID:10769212	FYPO:0003389	viable elongated vegetative cell with swollen medial region	(comment: temperature restrictive for cdc4-8 alone)
PMID:10769212	FYPO:0002060	viable vegetative cell population	(comment: temperature restrictive for cdc4-8 alone)
PMID:10769212	FYPO:0004652	normal actomyosin contractile ring morphology	(comment: temperature restrictive for cdc4-8 alone)
PMID:10769212	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPCC645.05c	(comment: temperature restrictive for cdc4-8 alone)
PMID:10770926	GO:0003697	single-stranded DNA binding	(comment: CHECK activated by ATP)
PMID:10770926	GO:0003697	single-stranded DNA binding	(comment: CHECK activated by ATP)
PMID:10770926	GO:0003697	single-stranded DNA binding	(comment: CHECK activated by ATP)
PMID:10775265	FYPO:0002002	multiseptate vegetative cell, septa grouped [has_penetrance] complete	(Fig. 3c)
PMID:10775265	FYPO:0002066	inviable elongated aseptate cell [has_penetrance] complete	(Fig. 3d)
PMID:10775265	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC24C6.07	(Figure 4; Table I)
PMID:10775265	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC9G1.09	(Figure 4; Table I)
PMID:10775265	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC9G1.09	(Figure 4; Table I)
PMID:10775265	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC9G1.09	(Figure 4; Table I)
PMID:10775265	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC9G1.09	(Figure 4; Table I)
PMID:10775265	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC9G1.09	(Figure 4; Table I)
PMID:10775265	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC9G1.09	(Figure 4; Table I)
PMID:10775265	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC24C6.07	(Figure 4; Table I)
PMID:10775265	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC24C6.07	(Figure 4; Table I)
PMID:10775265	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC24C6.07	(Figure 4; Table I)
PMID:10775265	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC24C6.07	(Figure 4; Table I)
PMID:10775265	GO:0071958	new mitotic spindle pole body [exists_during] mitotic telophase	(comment: I inferred new because it's asymmetric and we know sin is new)
PMID:10775265	GO:0071958	new mitotic spindle pole body [exists_during] mitotic telophase	(comment: I inferred new because it's asymmetric and we know sin is new)
PMID:10775265	GO:0071958	new mitotic spindle pole body [exists_during] mitotic anaphase	(comment: I inferred new because it's asymmetric and we know sin is new)
PMID:10775265	FYPO:0001493	inviable elongated multinucleate vegetative cell	(comment: dns)
PMID:10775265	FYPO:0003501	inviable aseptate mononucleate vegetative cell, normal cell length	After shift to restrictive temperature, cdc16-116 cells display two phenotypes termed type I and type II cells (Minet et al., 1979; Cerutti and Simanis, 1999). Type I cells have two nuclei and make multiple septa. Type II cells have a single nucleus and a septa. It has been proposed that the type II cells immediately septate again after division because they inherit the SPB that contains active Spg1p (Cerutti and Simanis, 1999). In support of this hypothesis, Sid1p was present at the SPB in type II cells (Figure 3A; see arrow).
PMID:10775265	FYPO:0005055	binucleate multiseptate cell, septa grouped	After shift to restrictive temperature, cdc16-116 cells display two phenotypes termed type I and type II cells (Minet et al., 1979; Cerutti and Simanis, 1999). Type I cells have two nuclei and make multiple septa. Type II cells have a single nucleus and a septa. It has been proposed that the type II cells immediately septate again after division because they inherit the SPB that contains active Spg1p (Cerutti and Simanis, 1999). In support of this hypothesis, Sid1p was present at the SPB in type II cells (Figure 3A; see arrow).
PMID:10775265	FYPO:0007567	premature protein localization to mitotic spindle pole body during metaphase [assayed_using] PomBase:SPAC9G1.09	Afterashifttorestrictivetemperaturefor50min to inactivate Cdc2p, cells could now be observed that were septating without undergoing anaphase (Figure 7E and F, see arrows). At this point, 96% (68/71) of cells displaying Sid1p signal at the SPB were septating without having undergone anaphase (Figure 7E and F, see arrows
PMID:10775265	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC21.06c	Cdc7p cannot localize to the SPB(s) in cdc11 (Figure 4; Table I)
PMID:10775265	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC9G1.09	GFP±Sid1p signal was not observed at SPBs in these cells although faint nuclear signal was observed (Figure 7A). This suggests that some aspect of completion of mitosis is required in order for Sid1p to localize.
PMID:10779336	FYPO:0002061	inviable vegetative cell population	(Fig. 8)
PMID:10779336	FYPO:0001387	loss of viability at high temperature	(Figure 1A)
PMID:10779336	FYPO:0001490	inviable elongated vegetative cell	(Figure 1A) (comment:increased size?)
PMID:10779336	FYPO:0000158	DNA content increased during vegetative growth	(Figure 1B)
PMID:10779336	FYPO:0000141	abnormal mitotic sister chromatid segregation	(Figure 2)
PMID:10779336	FYPO:0003165	cut with abnormal chromosome segregation	(Figure 2B)
PMID:10779336	FYPO:0000141	abnormal mitotic sister chromatid segregation	(Figure 2B)
PMID:10779336	FYPO:0002060	viable vegetative cell population	(Figure 2B)
PMID:10779336	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	(Figure 2B)
PMID:10779336	FYPO:0000268	sensitive to UV during vegetative growth	(Figure 3A)
PMID:10779336	FYPO:0002553	abnormal double-strand break processing	(Figure 3B)
PMID:10779336	FYPO:0000089	sensitive to methyl methanesulfonate	(Figure 3B)
PMID:10779336	FYPO:0000089	sensitive to methyl methanesulfonate	(Figure 3B)
PMID:10779336	FYPO:0000095	sensitive to bleomycin	(Figure 3B)
PMID:10779336	FYPO:0001689	normal growth on 4-nitroquinoline N-oxide	(Figure 3B)
PMID:10779336	FYPO:0002092	abnormal meiotic sister chromatid cohesion	(Figure 4C)
PMID:10779336	FYPO:0001128	decreased septation index	(comment: CHECK 5.6%)
PMID:10792724	GO:0004185	serine-type carboxypeptidase activity	(comment: CHECK residue=S200)
PMID:10799520	FYPO:0007646	septated mononucleate vegetative cell with mislocalized nucleus and anucleate compartment [has_penetrance] 75	(Figure 2E) These results show that Byr4 is required to prevent septation in G1 cells.
PMID:10799520	FYPO:0001222	binucleate vegetative cell	(comment: CHECK combine, other binucleates should unde new term)
PMID:10799520	FYPO:0000619	abnormal cell cycle arrest in mitotic anaphase [has_penetrance] >90	(comment: CHECK is this the right term?)
PMID:10799520	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC1565.06c [has_penetrance] 7	A corresponding decrease in the fraction of cells with Spg1 localized to SPBs occurred and reached 7% at 16 h (Fig. 3)
PMID:10799520	FYPO:0002049	elongated multinucleate aseptate vegetative cell [has_penetrance] high	As expected, most sid3-106 mutant cells (71%) contained four or more nuclei showing that there was insufficient Spg1 function in these cells for septation.
PMID:10799520	GO:0044732	mitotic spindle pole body [exists_during] mitotic anaphase A	Cdc7-HA was not localized to SPBs during interphase (Fig. 1C, 1)
PMID:10799520	GO:0044732	mitotic spindle pole body [exists_during] mitotic metaphase	Cdc7-HA was not localized to SPBs during interphase (Fig. 1C, 1),, localized to both SPBs in metaphase and early anaphase cells (Fig. 1C, 2 and 3), and localized to one SPB in late mitotic cells (Fig. 1C, 4 - 6) (8).
PMID:10799520	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC222.10c	Examination of these cells following 12 h of growth in thiamine-containing medium also showed that most cells (59%) contained Byr4 at all SPBs (Table II). In contrast to sid3-106 mutants, though, the amount of Byr4 localized to SPBs in cells depleted of Spg1 using the conditional promoter was greatly reduced (data not shown)
PMID:10799520	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC222.10c	Examination of these cells following 12 h of growth in thiamine-containing medium also showed that most cells (59%) contained Byr4 at all SPBs (Table II). In contrast to sid3-106 mutants, though, the amount of Byr4 localized to SPBs in cells depleted of Spg1 using the conditional promoter was greatly reduced (data not shown)
PMID:10799520	GO:0044732	mitotic spindle pole body [exists_during] mitotic anaphase B	Later in anaphase, Byr4 colocalized with one SPB (Fig. 1B, 4). Byr4 colocalized with one or both SPBs in binucleate cells with septa (Fig. 1B, 5 and 6). In the vast majority of cells, Byr4 localized to SPBs that did not contain Cdc7 (Fig. 1C, 1, 4, and 5).
PMID:10799520	GO:0044732	mitotic spindle pole body [exists_during] mitotic interphase	Spg1-HAH localized to SPBs throughout the cell cycle (Fig. 1B, second column) (8). Byr4 colocalized with Spg1-HAH during interphase (Fig. 1B, 1), but was absent from SPBs in metaphase (Fig. 1B, 2) and early anaphase
PMID:10799520	GO:0031030	negative regulation of septation initiation signaling [happens_during] mitotic interphase	This analysis of microtubule structures confirmed that mononucleate cells with Cdc7 localized to SPBs were in interphase and suggested that Byr4 was required to prevent septation during interphase.
PMID:10799520	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC222.10c	Western analysis showed that the reduction in Byr4 localization to SPBs in cells depleted of Spg1 was not due to reduced Byr4 protein amounts (data not shown).
PMID:10799520	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC222.10c	Western analysis showed that this decrease was not due to reduced Byr4 amounts
PMID:10805744	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC32C12.02	(comment: not shown it is ser/thr kinase activity)
PMID:10805744	FYPO:0000708	decreased mating efficiency [has_severity] high	(comment: same as cdc2delta alone)
PMID:10805785	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC244.01c	(Fig. 1c)
PMID:10805785	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC244.01c	(Fig. 1c)
PMID:10805785	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC244.01c	(Fig. 1c)
PMID:10805785	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC244.01c	(Fig. 1c)
PMID:10805785	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC244.01c	(Fig. 1c)
PMID:10805785	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC244.01c	(Fig. 1c)
PMID:10805785	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC244.01c	(Fig. 1c)
PMID:10805785	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC244.01c	(Fig. 1c)
PMID:10805785	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC222.10c	(Fig. 2)
PMID:10837231	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	After shifting to the restrictive temperature, mob1-1 cells failed to perform cytokinesis, became multinucleate, and did not form septa(Figure 2a-b).
PMID:10837231	FYPO:0003702	normal microtubule cytoskeleton morphology during vegetative growth	Examination of microtubules showed that mob1-1 cells form normal mitotic spindles (Figure 2f,g), and interphase arrays of microtubules. Thus, unlike S. cerevisiae mob1 mutants, S. pombe mob1 mutants do not have defects in mitotic exit, but are specifically defective in cytokinesis
PMID:10837231	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC428.13c	GFP-Mob1p localization to the SPB was unaffected in sid1, sid2, spg1 and cdc14 mutants (Figure 4a and data not shown)
PMID:10837231	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC428.13c	GFP-Mob1p localization to the SPB was unaffected in sid1, sid2, spg1 and cdc14 mutants (Figure 4a and data not shown)
PMID:10837231	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_protein] PomBase:SPBC428.13c	In all of the sid mutants, sid1, sid2, spg1, sid4 cdc7,cdc11 and cdc14, GFP-Mob1p could not localize to themedial region (Figure 4a-c and data not shown)
PMID:10837231	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_protein] PomBase:SPBC428.13c	In all of the sid mutants, sid1, sid2, spg1, sid4 cdc7,cdc11 and cdc14, GFP-Mob1p could not localize to themedial region (Figure 4a-c and data not shown)
PMID:10837231	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_protein] PomBase:SPBC428.13c	In all of the sid mutants, sid1, sid2, spg1, sid4 cdc7,cdc11 and cdc14, GFP-Mob1p could not localize to themedial region (Figure 4a-c and data not shown) (vw cdc15-140 in Figure legend must be a typo)
PMID:10837231	FYPO:0001382	decreased protein kinase activity	Kinase activity was associated with 13Myc-Mob1p prepared from wild-type cells, but Mob1p-associated kinase activity was reduced in sid2-250 cells (Figure 1c).
PMID:10837231	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC428.13c [has_severity] high	SPB was unaffected in sid1, sid2, spg1 and cdc14 mutants (Figure 4a and data not shown), but was severely affected in sid4, cdc7 and cdc11 mutants.
PMID:10837231	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC428.13c [has_severity] high	SPB was unaffected in sid1, sid2, spg1 and cdc14 mutants (Figure 4a and data not shown), but was severely affected in sid4, cdc7 and cdc11 mutants.
PMID:10837231	FYPO:0001294	normal actin cortical patch localization	Staining for the myosin light chain Cdc4p and actin revealed mob1-1 cells formed normal actomyosin rings and medially placed patches (Figure 2c-e).
PMID:10837231	FYPO:0001368	normal actomyosin contractile ring assembly	Staining for the myosin light chain Cdc4p and actin revealed mob1-1 cells formed normal actomyosin rings and medially placed patches (Figure 2c-e).
PMID:10837231	GO:0044732	mitotic spindle pole body	The nuclear-associated spotlike localization of Mob1p suggested that it was a component of the SPB. To confirm SPB localization, we fixed and stained cells expressing GFP-Mob1p with an antitubulin antibody. GFP-Mob1p was localized at the ends of the mitotic spindle in cells undergoing mitosis, consistent with its localization to the SPB (Figure 3m).
PMID:10837231	GO:0032153	cell division site [exists_during] mitotic anaphase	These results are consistent with Mob1p localizing to the cell division site at, or just before, the initiation of septum formation, and then leaving the division site before cell separation. T
PMID:10837231	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC21.06c	These results support the model that Mob1p, like Sid2p, functions downstream in the sid pathway. Consistent with this hypothesis, we found that Cdc7p localizes normally to the SPB in a mob1-1 temperature-sensitive mutant (Figure 4f). I
PMID:10837231	FYPO:0002061	inviable vegetative cell population	To examine the function of Mob1p in vivo, we deleted the mob1 gene (see Supplementary material) and found that it was essential for growth.
PMID:10837231	GO:0034973	Sid2-Mob1 complex	We tested for an interaction between Mob1p and Sid2p using the yeast two-hybrid system. Sid2p and Mob1p specifically interacted with each other but not with control proteins (Figure 1a)
PMID:10837231	GO:0034973	Sid2-Mob1 complex	We tested for an interaction between Mob1p and Sid2p using the yeast two-hybrid system. Sid2p and Mob1p specifically interacted with each other but not with control proteins (Figure 1a) Western blotting with anti-Myc antibodies detected Sid2p-13Myc as two bands that co-immunoprecipitated with GFP-Mob1p (Figure 1b).
PMID:10837231	GO:0004674	protein serine/threonine kinase activity	suggesting that Mob1-associated kinase activity is probably due to Sid2p.
PMID:10850973	GO:0008441	3'(2'),5'-bisphosphate nucleotidase activity	(comment: CHECK activated_by(CHEBI:18420)| activated_by(CHEBI:29103)| inhibited_by(CHEBI:48607)| inhibited_by(CHEBI:26710))
PMID:10852821	FYPO:0000161	abnormal actomyosin contractile ring assembly	(Fig. 3B)
PMID:10852821	FYPO:0000161	abnormal actomyosin contractile ring assembly	(Fig. 3B)
PMID:10852821	FYPO:0002050	branched elongated multinucleate aseptate vegetative cell	(Fig. 3B)
PMID:10852821	FYPO:0002050	branched elongated multinucleate aseptate vegetative cell	(Fig. 3B)
PMID:10852821	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPCC613.04c	(Fig. 6)
PMID:10852821	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_using] PomBase:SPCC613.04c	(Fig. 6)
PMID:10852821	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPCC613.04c	(Fig. 6)
PMID:10852821	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_using] PomBase:SPCC613.04c	(Fig. 6)
PMID:10852821	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_using] PomBase:SPCC613.04c	(Fig. 6)
PMID:10852821	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_using] PomBase:SPCC613.04c	(Fig. 6)
PMID:10852821	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPCC613.04c	(Fig. 7A)
PMID:10852821	FYPO:0001880	abolished protein localization to cell division site [assayed_using] PomBase:SPCC613.04c	(Fig. 7A) (comment: depends on actin)
PMID:10852821	FYPO:0001368	normal actomyosin contractile ring assembly	(Fig. 8)
PMID:10852821	FYPO:0001368	normal actomyosin contractile ring assembly	(Fig. 8)
PMID:10852821	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPCC645.05c	(Fig. 8)
PMID:10852821	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPCC645.05c	(Fig. 8)
PMID:10852821	FYPO:0002998	abolished actomyosin contractile ring assembly, clumped medial cortical nodes [assayed_using] PomBase:SPCC645.05c	(Fig. 8) (comment: myo2 clumped in nodes instead of ring)
PMID:10852821	FYPO:0002998	abolished actomyosin contractile ring assembly, clumped medial cortical nodes [assayed_using] PomBase:SPCC645.05c	(Fig. 8) (comment: myo2 clumped in nodes instead of ring)
PMID:10852821	FYPO:0007127	abnormal actomyosin contractile ring maturation	(Fig. 9)
PMID:10852821	FYPO:0004736	abnormal actomyosin contractile ring	(Fig. 9) (comment: mainrtenance)
PMID:10864871	FYPO:0000284	large and small daughter nuclei, with unequal mitotic sister chromatid segregation	(comment: 2nd division)
PMID:10871341	FYPO:0000584	decreased sporulation frequency [has_severity] high	(Fig. 1)
PMID:10871341	FYPO:0000474	abolished meiosis	(Fig. 1)
PMID:10871341	FYPO:0002044	abolished premeiotic DNA replication	(Fig. 1)
PMID:10871341	FYPO:0002044	abolished premeiotic DNA replication	(Fig. 1)
PMID:10879493	FYPO:0000081	sensitive to high osmolarity	(comment: 2M glucose = 36% w/v = A LOT, so it is osmolarity rather than glucose itself I guess)
PMID:10879493	FYPO:0000081	sensitive to high osmolarity	(comment: 2M glucose = 36% w/v = A LOT, so it is osmolarity rather than glucose itself I guess)
PMID:10886372	FYPO:0002059	inviable cell population	(comment: don't know veg or spore)
PMID:10905343	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC26H8.07c [assayed_using] PomBase:SPBC800.05c	(comment: total alpha tubulin level reduced but not known whether from nda2 or atb2 or both)
PMID:10905343	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC26H8.07c [assayed_using] PomBase:SPBC800.05c	(comment: total alpha tubulin level reduced but not known whether from nda3 or atb2 or both)
PMID:10921876	FYPO:0000836	increased protein level [assayed_using] PomBase:SPAPB2B4.03	(Fig. 1a)
PMID:10921876	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPBC582.03 [assayed_using] PomBase:SPCC4E9.02	(Fig. 1a)
PMID:10921876	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication	(Fig. 1b)
PMID:10921876	FYPO:0004107	normal protein level during mitotic G2 phase [assayed_using] PomBase:SPBC582.03	(Fig. 3) ((comment: CHECK cdc25-22 block and release)
PMID:10921876	FYPO:0004107	normal protein level during mitotic G2 phase [assayed_using] PomBase:SPCC4E9.02	(Fig. 3) ((comment: CHECK cdc25-22 block and release)
PMID:10921876	FYPO:0004107	normal protein level during mitotic G2 phase [assayed_using] PomBase:SPCC4E9.02	(Fig. 3) (comment: CHECK cdc25-22 block and release)
PMID:10921876	FYPO:0004107	normal protein level during mitotic G2 phase [assayed_using] PomBase:SPBC582.03	(Fig. 3) (comment: CHECK cdc25-22 block and release)
PMID:10921876	FYPO:0004108	increased protein level during mitotic G1 phase [assayed_using] PomBase:SPBC582.03	(Fig. 3) (comment: cdc25-22 block and release)
PMID:10921876	FYPO:0004108	increased protein level during mitotic G1 phase [assayed_using] PomBase:SPCC4E9.02	(Fig. 3) (comment: cdc25-22 block and release)
PMID:10921876	GO:1905785	negative regulation of anaphase-promoting complex-dependent catabolic process	(comment: APC-SLP1)
PMID:10921876	GO:1905786	positive regulation of anaphase-promoting complex-dependent catabolic process [has_input] PomBase:SPCC4E9.02 [happens_during] mitotic G1 phase	(comment: APC-Ste9 dependent protein destruction/11365/) I didn't do a phenotype for this because they don't show a WT scanario. I used the ubiquitin-dependent term becasuethis is whet they were testing as we already know that this decgradation is APC/protiesome dependnet. I know its a bit of a stretch)
PMID:10921876	GO:1905786	positive regulation of anaphase-promoting complex-dependent catabolic process [has_input] PomBase:SPBC582.03 [happens_during] mitotic G1 phase	(comment: APC-Ste9 dependent protein destruction/11365/) I didn't do a phenotype for this because they don't show a WT scanario. I used the ubiquitin-dependent term becasuethis is whet they were testing as we already know that this decgradation is APC/protiesome dependnet. I know its a bit of a stretch)
PMID:10921878	FYPO:0004111	decreased protein phosphorylation during mitotic G2 phase [assayed_using] PomBase:SPAC144.13c	(comment: CHECK during mitotic G2 arrest)
PMID:10930468	FYPO:0006638	decreased protein localization to medial cortex, with protein distributed in cell cortex, during vegetative growth	(comment: CHECK diffuse cytoplsmic throughout the cell cycle)
PMID:10930468	FYPO:0004292	abnormal septum [has_penetrance] 95.5	(comment: CHECK diffuse cytoplsmic throughout the cell cycle)
PMID:10930468	FYPO:0003389	viable elongated vegetative cell with swollen medial region [has_penetrance] 40	Cells carrying pREP41Xmid1 exhibited a striking phenotype: they formed bulges near the cell center (Figure 1B). Medial bulges were exhibited in 40% of the cells 20 h after removal of thiamine (Figure 1C middle). Cells were longer than normal, suggestive of a cell cycle delay in interphase (Figure 1B)
PMID:10930468	FYPO:0007178	abolished protein localization to medial cortex during mitosis [assayed_protein] PomBase:SPCC4B3.15 [has_penetrance] high	DNES1-mid1p had a clear defect in nuclear export- in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	FYPO:0004293	mislocalized septum [has_penetrance] 20.5	DNES1-mid1p had a clear defect in nuclear export- in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	FYPO:0004293	mislocalized septum [has_penetrance] 74.6	DNES1-mid1p had a clear defect in nuclear export- in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	FYPO:0004293	mislocalized septum [has_penetrance] 53.6	DNES1-mid1p had a clear defect in nuclear export- in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	FYPO:0001920	decreased protein export from nucleus [assayed_protein] PomBase:SPCC4B3.15 [has_penetrance] high	DNES1-mid1p had a clear defect in nuclear export- in contrast to wild-type mid1p, which exits the nucleus during mitosis, it remained in the nucleus throughout the cell cycle, although some faint rings were occasionally seen (Figure 6, A-B).
PMID:10930468	FYPO:0007178	abolished protein localization to medial cortex during mitosis [assayed_protein] PomBase:SPCC4B3.15 [has_penetrance] low	DNES2-mid1p had a weaker, but demonstrable nuclear export defect: it retained some weak cortical staining and weak rings in addition to nuclear staining (Figure 6C), but
PMID:10930468	FYPO:0001920	decreased protein export from nucleus [assayed_protein] PomBase:SPCC4B3.15 [has_severity] low	DNES2-mid1p had a weaker, but demonstrable nuclear export defect: it retained some weak cortical staining and weak rings in addition to nuclear staining (Figure 6C), but
PMID:10930468	FYPO:0002070	normal nucleus location	No defects in nuclear positioning were apparent, as nuclei were positioned properly at the middle of the cell or in the bulge region (see Figure 2). Mid1p localization in these
PMID:10930468	FYPO:0001234	slow vegetative cell population growth	and the generation time of the population was increased approximately two-fold (Figure 1C top).
PMID:10930468	GO:0005049	nuclear export signal receptor activity [has_input] PomBase:SPCC4B3.15 [part_of] protein export from nucleus	inferred from Nuclear export of mid1p was sensitive to leptomycin B (LMB), a drug that blocks the nuclear export factor crm1p (see Figure 8; Nishi et al., 1994; Kudo et al.; 1999), showing that the nuclear export of mid1p is crm1 dependent.
PMID:10930468	FYPO:0002999	normal protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	localized in an identical manner to wild-type mid1p (Figure 9A) and was fully functional (Figure 7 and Table 2).
PMID:10930468	FYPO:0008074	increased protein localization to medial cortical node during interphase	no NLS*-mid1p was detectable in the nucleus when expressed under the control of mid1 promoter
PMID:10930468	FYPO:0003450	abolished protein localization to nucleus [assayed_protein] PomBase:SPCC4B3.15	noNLS*-mid1p was detectable in the nucleus when expressedunder the control of mid1 promoter
PMID:10947840	FYPO:0004194	decreased protein level during cellular response to hydroxyurea [assayed_protein] PomBase:SPBC660.14 [has_severity] high	At 36 8C in mis3-224, the level of Mik1 increased to a peak after 4h, but then strikingly decreased to a low level (E).
PMID:10947840	FYPO:0004194	decreased protein level during cellular response to hydroxyurea [assayed_protein] PomBase:SPBC660.14	At 36 8C in mis3-224, the level of Mik1 increased to a peak after 4h, but then strikingly decreased to a low level (E).
PMID:10947840	FYPO:0002061	inviable vegetative cell population	In addition to the interaction between Mis3 and Wee1, it was found that the double mutants mis3 cdc25 and mis3 cdc13 were able to form colonies at 268C, but not at 308C (Fig. 6A).
PMID:10947840	FYPO:0002061	inviable vegetative cell population	In addition to the interaction between Mis3 and Wee1, it was found that the double mutants mis3 cdc25 and mis3 cdc13 were able to form colonies at 268C, but not at 308C (Fig. 6A).
PMID:10947840	FYPO:0002061	inviable vegetative cell population	In addition to the interaction between Mis3 and Wee1, it was found that the double mutants mis3 cdc25 and mis3 cdc13 were able to form colonies at 268C, but not at 308C (Fig. 6A).
PMID:10947840	FYPO:0002061	inviable vegetative cell population	In addition to the interaction between Mis3 and Wee1, it was found that the double mutants mis3 cdc25 and mis3 cdc13 were able to form colonies at 268C, but not at 308C (Fig. 6A).
PMID:10947840	FYPO:0002061	inviable vegetative cell population	Tetrad dissection indicated that the mis3-224 dsk1 null double mutant failed to grow at any temperature.
PMID:10947840	FYPO:0002061	inviable vegetative cell population	Tetrad dissection indicated that the mis3-224 dsk1 null double mutant failed to grow at any temperature.
PMID:10947840	FYPO:0008218	abnormal mitotic S/G2 phase transition	These results showed that cells lacking functional Mis3 could not promote cell growth upon the release to complete medium and remained in the G1/S phase.
PMID:10947840	FYPO:0002060	viable vegetative cell population	We found, on the other hand, that the ts phenotype of mis3-224 was suppressed by dis2-11, a cs mutation with greatly reduced type 1 protein phosphatase (PP1) activity and the inability to exit from mitosis (Ohkura et al. 1989).
PMID:10947840	FYPO:0002060	viable vegetative cell population	We found, on the other hand, that the ts phenotype of mis3-224 was suppressed by dis2-11, a cs mutation with greatly reduced type 1 protein phosphatase (PP1) activity and the inability to exit from mitosis (Ohkura et al. 1989).
PMID:10947840	FYPO:0000088	sensitive to hydroxyurea	it was moderately sensitive at 308C (Fig. 5A, top): mutant failed to produce colonies in the presence of 8 mM HU at 30 8C, a semi-restrictive temperature.
PMID:10947840	FYPO:0004481	abolished cell population growth at high temperature	they ceased to increase in number after two divisions (Fig. 1A, open triangles). The growth arrest phenotype of mis3-224 (Fig. 1C) was distinct from that of typical cdc mutants, as its cell length increase was insigni®cant (1.3-fold) after 8h at 36 8C. mis3-224 at 36 8C was unable to increase in cell length because the levels of protein and RNA ceased to increase (B, ®lled and open triangles, respectively).
PMID:10947840	FYPO:0007136	small mononucleate vegetative cell	they ceased to increase in number after two divisions (Fig. 1A, open triangles). The growth arrest phenotype of mis3-224 (Fig. 1C) was distinct from that of typical cdc mutants, as its cell length increase was insigni®cant (1.3-fold) after 8h at 36 8C. mis3-224 at 36 8C was unable to increase in cell length because the levels of protein and RNA ceased to increase (B, ®lled and open triangles, respectively).
PMID:10950958	FYPO:0006626	increased phosphatidylinositol-4,5-bisphosphate level in plasma membrane	(comment: CHECK NOT PLASMA MEMBRANE)
PMID:10950958	FYPO:0006625	decreased phosphatidylinositol-4,5-bisphosphate level in plasma membrane	(comment: CHECK NOT PLASMA MEMBRANE) As shown in Fig. 5B, its3-1 mutant cells contained about 10% of the amount of PI(4,5)P2 found in wild-type cells, indicating that the mutation caused a significant decrease in PI(4)P5K activity of Its3.
PMID:10950958	FYPO:0002061	inviable vegetative cell population	As shown in Fig. 1A, its3-1 mutant cells could not grow at 33 °C, 36 °C, or in the YPD plate containing FK506, whereas wild-type cells grew normally.
PMID:10950958	FYPO:0000086	sensitive to tacrolimus	As shown in Fig. 1A, its3-1 mutant cells could not grow at 33 °C, 36 °C, or in the YPD plate containing FK506, whereas wild-type cells grew normally.
PMID:10950958	FYPO:0002128	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_protein] PomBase:SPAC19G12.14	As shown in Fig. 9B, the GFP-Its3-1 mutant protein (GFP-mIts3) was no longer localized to the plasma membrane and instead...
PMID:10950958	GO:0005886	plasma membrane	GFP-Its3 localized to the plasma membrane at all stages of the cell cycle (Fig. 9A).
PMID:10950958	GO:0032153	cell division site	GFP-Its3 localized to the plasma membrane at all stages of the cell cycle (Fig. 9A).
PMID:10950958	FYPO:0000650	increased septation index	In addition, its3-1 mutant had a septation index approximately twice that seen in wild-type cells at the permissive temperature.
PMID:10950958	FYPO:0000790	abnormal actin cortical patch organization	In wild-type cells, a shift from 27 to 33 °C caused a transient heat-induced disorganization of actin patches
PMID:10950958	FYPO:0000994	increased cellular phosphatidylinositol-4-phosphate level	Interestingly, the level of PI(4)P was significantly higher than that of the wild-type cells.
PMID:10950958	FYPO:0001406	increased septum thickness	Microscopic observation revealed that some mutant cells have a thick septum that was brightly stained with Calcofluor and was hardly seen in wild-type cells (Fig. 8A).
PMID:10950958	FYPO:0008042	abolished establishment or maintenance of actin cytoskeleton polarity during vegetative growth	On the other hand, in the its3-1 mutant cells, actin patches were partially polarized at 27 °C, and the polarization was completely lost upon temperature upshift or FK506 treatment (Fig. 7A).
PMID:10950958	FYPO:0008039	decreased 1-phosphatidylinositol-4-phosphate 5-kinase activity [assayed_enzyme] PomBase:SPAC19G12.14	PI(4)5K activity kinase: As shown in Fig. 1A, its3-1 mutant cells could not grow at 33 °C, 36 °C, or in the YPD plate containing FK506, whereas wild-type cells grew normally.
PMID:10950958	GO:0016308	1-phosphatidylinositol-4-phosphate 5-kinase activity [occurs_in] plasma membrane	Purified GST fusion proteins were subjected to in vitro kinase reaction as described under “Experimental Procedures.” Fig. 6 shows that mutant Its3 tagged with GST had detectable but reduced PI(4)5K activity compared with the wild-type.
PMID:10950958	FYPO:0002061	inviable vegetative cell population	Tetrad analysis of the heterozygous diploid showed two viable (UraΔ) and two inviable spores (Fig. 3D), indicating that the its3Δ gene is essential for cell growth.
PMID:10950958	FYPO:0002061	inviable vegetative cell population	􏰇ppb1 (􏰇CN in Fig. 2) mutant. As expected, no double mutant was obtained, indicating that its3 mutation and calcineurin deletion was synthetically lethal.
PMID:10950958	FYPO:0002061	inviable vegetative cell population	􏰇ppb1 (􏰇CN in Fig. 2) mutant. As expected, no double mutant was obtained, indicating that its3 mutation and calcineurin deletion was synthetically lethal.
PMID:10954610	FYPO:0003036	normal transcription during cellular response to UV [assayed_using] PomBase:SPBC649.04	(comment: evidence: transcription run-on assay)
PMID:10954610	FYPO:0003036	normal transcription during cellular response to UV [assayed_using] PomBase:SPBC649.04	(comment: evidence: transcription run-on assay)
PMID:10954610	FYPO:0003039	decreased RNA stability during cellular response to UV [assayed_using] PomBase:SPBC649.04	(comment: steady-state labeling assay; stability increases in wt but not mutant upon UV exposure)
PMID:10954610	FYPO:0003039	decreased RNA stability during cellular response to UV [assayed_using] PomBase:SPBC649.04	(comment: steady-state labeling assay; stability increases in wt but not sty1delta upon UV exposure)
PMID:10970777	FYPO:0006582	decreased bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity [assayed_enzyme] PomBase:SPCC4G3.02	(comment: decreased)
PMID:10970777	GO:0004081	bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity	(comment: there is another unknown gene with this activity)
PMID:10978278	GO:0044183	protein folding chaperone [has_input] PomBase:SPBC26H8.07c [part_of] post-chaperonin tubulin folding pathway	(comment: beta tubulin specific pathway)
PMID:11007487	FYPO:0004700	bent vegetative cell	(Fig. 1) (comment: tip1 expressed from pREP3X)
PMID:11007487	FYPO:0000224	lemon-shaped cell	(Fig. 1) (comment: tip1 expressed from pREP3X)
PMID:11007487	FYPO:0000015	branched vegetative cell	(Fig. 1) (comment: tip1 expressed from pREP3X)
PMID:11007487	FYPO:0000014	tapered cell	(Fig. 1) (comment: tip1 expressed from pREP3X. I've used this term as it is the nearest to schmoozing which is the term they use in the paper. To be honest I think tapered is better as they don't know that the cells are shmooing)
PMID:11007487	FYPO:0001018	abolished NETO	(Fig. 1B)
PMID:11007487	FYPO:0005464	abnormal maintenance of protein location at cell tip during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPCC1223.06	(Fig. 3) (comment: (methanol fixation))
PMID:11007487	FYPO:0004700	bent vegetative cell [has_penetrance] >80	(Fig. 3B)
PMID:11007487	FYPO:0005792	T-shaped cell during G0 to G2 transition [has_penetrance] 70-80 [has_severity] high	(Fig. 3C)
PMID:11007487	FYPO:0005794	bent cell during G0 to G1 transition [has_penetrance] 70-80	(Fig. 3D)
PMID:11007487	FYPO:0005796	short disorganized microtubule bundle [has_penetrance] high	(Fig. 3F) (comment: (methanol fixation))
PMID:11007487	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPCC1223.06	(Fig. 3H) (comment: methanol fixation)
PMID:11007487	FYPO:0004700	bent vegetative cell [has_penetrance] high	(Fig. 3I)
PMID:11007487	FYPO:0001366	normal actin cytoskeleton organization	(Fig. 3I) (comment: Formaldehyde fixation)
PMID:11007487	FYPO:0001400	normal interphase microtubules	(Fig. 3K) (comment: (methanol fixation))
PMID:11007487	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPCC1223.06	(Fig. 3K) (comment: methanol fixation)
PMID:11007487	GO:1905759	post-anaphase array microtubule [exists_during] mitotic M phase	(Fig. 4)
PMID:11007487	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	(Fig. 4A, 3G)
PMID:11007487	GO:1905721	mitotic spindle astral microtubule end [exists_during] mitotic anaphase	(Fig. 4F) However, tip1p was observed at the tips of the astral microtubules that emanated from the cytoplasmic face of the nuclear-located spindle pole body during anaphase and at the tips of the microtubules generated from the central region of postmitotic cells (Figures 4F).
PMID:11007487	FYPO:0005799	decreased microtubule dwell time at cell tip	(Fig. 6) (comment: (live cell imaging) GFP-tubulin expressed from nmt1 promoter on multi copy plasmid)
PMID:11007487	FYPO:0003194	increased rate of microtubule depolymerization during vegetative growth [has_penetrance] >70	(Fig. 6) (comment: (live cell imaging) GFP-tubulin expressed from nmt1 promoter on multi copy plasmid)
PMID:11007487	GO:0008017	microtubule binding	(Figure 4H) (comment: CHECK in vitro)
PMID:11007487	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPAC3C7.12	(Figure 4I)
PMID:11007487	FYPO:0004731	normal protein localization to interphase microtubule plus-end [assayed_using] PomBase:SPAC3C7.12	(Figure 4I) (comment: I'm not sure if we knew it was the plus end then, but we do now ;))
PMID:11007487	GO:1990752	microtubule end [exists_during] mitotic interphase	(Figures 4C, 4G)
PMID:11007487	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] <1	(data not shown)
PMID:11007487	GO:0030010	establishment of cell polarity	These phenotypes establish that tip1p is required to properly position the growth zones at the antipodes of the cells.
PMID:11007487	GO:0031122	cytoplasmic microtubule organization	We conclude that tip1p is required for the correct organization of the microtubule cytoskeleton and for the proper localization of the tea1p marker to the cell ends
PMID:11007487	FYPO:0001399	normal mitotic spindle	data not shown
PMID:11014802	GO:0010515	negative regulation of induction of conjugation with cellular fusion	(comment: maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.)
PMID:11014802	GO:0010515	negative regulation of induction of conjugation with cellular fusion	(comment: maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.)
PMID:11017199	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_at] AP_1_binding_site	(comment: from structure)
PMID:11018050	FYPO:0001512	branched, elongated cell [has_penetrance] high	(Fig. 2)
PMID:11018050	FYPO:0004700	bent vegetative cell [has_penetrance] 18	(Fig. 2B)
PMID:11018050	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 9	(Fig. 2D)
PMID:11018050	FYPO:0001512	branched, elongated cell [has_penetrance] high	(Fig. 2G)
PMID:11018050	FYPO:0002760	short cytoplasmic microtubules	(Fig. 3)
PMID:11018050	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 75	(Fig. 4)
PMID:11018050	GO:1990752	microtubule end [exists_during] mitotic interphase	(Fig. 5)
PMID:11018050	GO:0005881	cytoplasmic microtubule [exists_during] mitotic interphase	(Fig. 5)
PMID:11018050	GO:0051286	cell tip [exists_during] mitotic interphase	(Fig. 6)
PMID:11018050	GO:0051286	cell tip [exists_during] cell quiescence	(Fig. 6) cell tip localisation increased compared to exponentially growing cells
PMID:11018050	FYPO:0003329	abolished protein localization to cell tip during mitotic interphase [assayed_using] PomBase:SPCC1223.06	(Fig. 8c)
PMID:11018050	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(comment: forms microcolonies)
PMID:11018050	FYPO:0005809	short astral microtubules	Data not shown.
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: higher temp, restrictive for spp2-8 alone)
PMID:11027257	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(comment: higher temp, restrictive for spp2-8 alone)
PMID:11027257	FYPO:0000062	abnormal nuclear morphology during vegetative growth	(comment: higher temp, restrictive for spp2-8 alone)
PMID:11027257	FYPO:0000062	abnormal nuclear morphology during vegetative growth	(comment: higher temp, restrictive for spp2-9 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: higher temp, restrictive for spp2-9 alone)
PMID:11027257	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(comment: higher temp, restrictive for spp2-9 alone)
PMID:11027257	FYPO:0000158	DNA content increased during vegetative growth [has_penetrance] medium	(comment: mixed population)
PMID:11027257	FYPO:0000453	DNA content decreased during vegetative growth [has_penetrance] medium	(comment: mixed population)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002060	viable vegetative cell population	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-8 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002060	viable vegetative cell population	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027257	FYPO:0002061	inviable vegetative cell population	(comment: temp semi-permissive for spp2-9 alone)
PMID:11027263	FYPO:0004672	inviable elongated vegetative cell with fragmented nucleus	(comment: same as hsk1-1312 alone)
PMID:11027263	FYPO:0001355	decreased vegetative cell population growth	(comment: temp. restrictive for hsk1-1312 alone; fudged a bit because assayed at 32)
PMID:11030618	FYPO:0006602	decreased replication fork arrest at MPS1 barrier	(Fig. 2A)
PMID:11030618	FYPO:0006602	decreased replication fork arrest at MPS1 barrier	(Fig. 2A)
PMID:11030618	FYPO:0006603	decreased replication fork arrest at RTS1 barrier	(Fig. 4)
PMID:11030618	FYPO:0006603	decreased replication fork arrest at RTS1 barrier	(Fig. 4)
PMID:11030618	FYPO:0008230	normal replication fork arrest at MPS1 barrier	(Fig. 5)
PMID:11030618	FYPO:0006603	decreased replication fork arrest at RTS1 barrier	(Fig. 5)
PMID:11030618	FYPO:0001690	normal growth on camptothecin	(Fig. 6)
PMID:11030618	FYPO:0001690	normal growth on camptothecin	(Fig. 6)
PMID:11030618	FYPO:0001690	normal growth on camptothecin	(Fig. 6)
PMID:11030618	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 6)
PMID:11030618	FYPO:0001690	normal growth on camptothecin	(Fig. 6)
PMID:11030618	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 6)
PMID:11030618	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 6)
PMID:11030618	FYPO:0001690	normal growth on camptothecin	(Fig. 6)
PMID:11030618	FYPO:0001234	slow vegetative cell population growth	A similar slow growth phenotype was also observed for a Dtop1, swi3 double mutant (JZ454) when compared to a swi3 mutant strain (E157).
PMID:11030618	FYPO:0001234	slow vegetative cell population growth	A similar slow growth phenotype was also observed for a Dtop1, swi3 double mutant (JZ454) when compared to a swi3 mutant strain (E157).
PMID:11030618	FYPO:0001234	slow vegetative cell population growth	a swi1-111, Dtop1 double mutant revealed a decreased growth rate, suggesting a swi1 and top1 interaction.
PMID:11030618	FYPO:0001234	slow vegetative cell population growth	a swi1-111, Dtop1 double mutant revealed a decreased growth rate, suggesting a swi1 and top1 interaction.
PMID:11030618	GO:0011000	replication fork arrest at mating type locus	the swi1p and swi3p proteins, necessary for imprinting, were shown to pause the replication fork at the site of imprinting.
PMID:11030618	GO:0011000	replication fork arrest at mating type locus	the swi1p and swi3p proteins, necessary for imprinting, were shown to pause the replication fork at the site of imprinting.
PMID:11069657	FYPO:0000175	abnormal ascospore wall assembly	(comment: they form parts that fail to mature)
PMID:11069779	FYPO:0002061	inviable vegetative cell population	(comment: CHECK **SYNTHETIC LETHAL)
PMID:11069779	FYPO:0001524	resistance to L-thialysine	(comment: CONDITION toxic aa-analog)
PMID:11071923	FYPO:0007317	decreased cytoplasmic translation	(comment: global translation, not a specific gene)
PMID:11076964	GO:0030479	actin cortical patch	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:11080156	FYPO:0004537	mitotic spindle assembly checkpoint override	(comment: CHECK SAC- fypo/issues/2310)
PMID:11080156	FYPO:0003165	cut with abnormal chromosome segregation	(comment: after passage through G1)
PMID:11080156	FYPO:0002113	inviable curved vegetative cell [has_penetrance] 10	(comment: with cut at second division)
PMID:11080156	FYPO:0002113	inviable curved vegetative cell [has_penetrance] 10	(comment: with cut)
PMID:11084332	FYPO:0004332	delayed onset of protein degradation during mitosis [assayed_using] PomBase:SPBC14C8.01c	(comment: CHECK delayed during anaphase)
PMID:11084332	FYPO:0004108	increased protein level during mitotic G1 phase [assayed_using] PomBase:SPAC17C9.13c	(comment: CHECK during G1 arrest ) fig4C right hand panel
PMID:11084332	FYPO:0004108	increased protein level during mitotic G1 phase [assayed_using] PomBase:SPAC6F12.15c	(comment: CHECK during G1 arrest ) fig4C right hand panel
PMID:11084332	FYPO:0004332	delayed onset of protein degradation during mitosis [assayed_using] PomBase:SPBC582.03	(comment: CHECK during anaphase)
PMID:11084332	FYPO:0002082	increased protein ubiquitination during vegetative growth [has_severity] low	(comment: total protein in proteasome mutant)
PMID:11084332	FYPO:0002082	increased protein ubiquitination during vegetative growth [has_severity] low	(comment: total protein in proteasome mutant)
PMID:11084332	FYPO:0000833	normal protein level during vegetative growth	(comment: total ubiquitinated)
PMID:11084332	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC582.03	(comment: ubiquitinated)
PMID:11084332	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC582.03	(comment: ubiquitinated)
PMID:11102508	FYPO:0000324	mitotic metaphase/anaphase transition delay [has_penetrance] 5.6	(comment: WT 0.5%)
PMID:11112691	FYPO:0006821	slow vegetative cell growth [has_severity] high	(Fig. 3B). The double mutant myo52∆ cps8− was extremely sick even at the permissive temperature and formed only micro colonies consisting of severely deformed cells.
PMID:11112691	FYPO:0000032	abnormal cytokinesis during vegetative growth	(comment: Figure missing from pdf, so I could not be more precise myo51∆ cps8− cells were viable at 25°C but had marked cytokinetic defects) (Fig. 3B).
PMID:11112691	FYPO:0000024	stubby vegetative cell	At this temperature myo52∆ cells grew more slowly (Fig. 2B) and had an altered morphology, being shorter and
PMID:11112691	FYPO:0001234	slow vegetative cell population growth	At this temperature myo52∆ cells grew more slowly (Fig. 2B) and had an altered morphology, being shorter and
PMID:11112691	FYPO:0000801	abnormal actin cytoskeleton organization during vegetative growth	Loss of cell shape in myo52∆ was accompanied by the depolarisation of the actin cytoskeleton whereas no change in actin organisation could be detected in myo51∆ (Fig. 3A).
PMID:11112691	FYPO:0001370	abnormal protein localization [assayed_protein] PomBase:SPCC1281.01	Mok1 was delocalised in myo52∆ (Fig. 8C)
PMID:11112691	FYPO:0001357	normal vegetative cell population growth	Myo51 were indistinguishable from an isogenic wild-type strain (Fig. 2A,B).
PMID:11112691	GO:0031097	medial cortex [exists_during] mitotic M phase	Myo52 formed a cap at the growing tips (Fig. 5C,D).
PMID:11112691	GO:1902716	cell cortex of growing cell tip [exists_during] mitotic interphase	Myo52 formed a cap at the growing tips (Fig. 5C,D).
PMID:11112691	FYPO:0001122	elongated vegetative cell [has_severity] high	Whereas Myo51 overproduction resulted in elongated cells with wispy, misoriented septal material (Fig. 4A)
PMID:11112691	FYPO:0001512	branched, elongated cell [has_severity] high	cells overproducing Myo52 were less elongated and branched due to the failure of septa to properly cleave (Fig. 4B).
PMID:11112691	FYPO:0001234	slow vegetative cell population growth [has_severity] high	myo52∆ cells showed extremely slow growth at 36°C (Fig. 2C).
PMID:11112691	FYPO:0000650	increased septation index	septation index of 20%, twice that of wild type (Fig. 2A).
PMID:11134033	GO:0005737	cytoplasm	(Fig. 2)
PMID:11134033	FYPO:0000681	abnormal sporulation resulting in formation of two-spore ascus [has_penetrance] 16	(Figure 1C)
PMID:11134033	FYPO:0002946	abnormal cell wall	(Figure 1a)
PMID:11134033	FYPO:0000337	abnormal mitosis	(Figure 1b)
PMID:11134033	FYPO:0003302	nucleus mislocalized towards cell tip during mitotic interphase	(Figure 1b)
PMID:11134033	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 16	(Figure 1b) (I)
PMID:11134033	FYPO:0003166	monoseptate vegetative cell with binucleate and anucleate compartments [has_penetrance] 16	(Figure 1b) (I)
PMID:11134033	FYPO:0002060	viable vegetative cell population	(data not shown)
PMID:11134033	FYPO:0003125	decreased cytoplasmic translational initiation [has_penetrance] 16	indicated by decreased polysome to monosome ratio
PMID:11160827	GO:0005634	nucleus [exists_during] mitotic cell cycle phase	(comment: present throughout mitotic cell cycle)
PMID:11179424	FYPO:0006232	abolished protein phosphorylation during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC24B11.06c	(comment: residue not determined experimentally, but probably Y173)
PMID:11226171	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: same sensitivity as rhp54delta alone)
PMID:11226171	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: same sensitivity as rhp54delta alone)
PMID:11231017	FYPO:0001234	slow vegetative cell population growth	(Fig. 1)
PMID:11231017	FYPO:0000106	sensitive to hygromycin B	(Fig. 1)
PMID:11231572	GO:0110085	mitotic actomyosin contractile ring	(comment: dependent on F-actin, assayed using Latrunculin A)
PMID:11231572	GO:0030479	actin cortical patch	(comment: dependent on F-actin, assayed using Latrunculin A)
PMID:11238401	GO:0010515	negative regulation of induction of conjugation with cellular fusion	(comment: maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.)
PMID:11238401	GO:0010515	negative regulation of induction of conjugation with cellular fusion	(comment: maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.)
PMID:11242054	GO:0062072	histone H3K9me2/3 reader activity [has_input] hht1/Me(K9)	(comment: The fission yeast S. pombe has an HP1 homologue Swi6, which contains a chromo domain that is closely related to those of HP1 family members.) (Figure 4a) shows that the Swi6 chromo domain is able to bind H3 peptide methylated at Lys 9, whereas its chromo-shadow domain has no methyl-binding activity.
PMID:11242054	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	loss of association of Swi6 with centromeres should result in expression of a normally silent marker gene embedded in centromeric chromatin. Figure 4e shows that this is indeed the case. On indicator plates, wild-type strains silence the centromeric ade6+ marker, which results in red, repressed colonies13; however, in strains lacking Clr4 (D) or strains defective in Clr4 methylase activity (G341D), this ade6+ gene is clearly expressed, resulting in the formation of white colonies.
PMID:11242054	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	loss of association of Swi6 with centromeres should result in expression of a normally silent marker gene embedded in centromeric chromatin. Figure 4e shows that this is indeed the case. On indicator plates, wild-type strains silence the centromeric ade6+ marker, which results in red, repressed colonies13; however, in strains lacking Clr4 (D) or strains defective in Clr4 methylase activity (G341D), this ade6+ gene is clearly expressed, resulting in the formation of white colonies.
PMID:11242054	FYPO:0001678	abolished protein localization to chromatin [assayed_protein] PomBase:SPAC664.01c	whereas the Clr4-G341D strain shows loss of localization from the nuclear periphery and accumulation of more diffuse staining over the nucleolus (Fig. 4c).
PMID:11248251	FYPO:0008144	heme O absent from cell	In agreement with earlier results the cox10 mutant also had no heme O [4]. This was not true of the cox15 mutant which had a very low but detectable amount of heme O (Fig. 1).
PMID:11248251	FYPO:0008143	heme A absent from cell	The two exceptions were the cox10 and cox15 mutants, both of which lacked heme A. In agreement with earlier results the cox10 mutant also had no heme O [4].
PMID:11248251	FYPO:0008143	heme A absent from cell	The two exceptions were the cox10 and cox15 mutants, both of which lacked heme A. In agreement with earlier results the cox10 mutant also had no heme O [4]. This was not true of the cox15 mutant which had a very low but detectable amount of heme O (Fig. 1).
PMID:11248251	GO:0005759	mitochondrial matrix	These results further indicate that the C-terminal end of Cox15p, together with Yah1p, is located in the matrix compartment. Yah1p fused to Cox15p is therefore in the same compartment as the native protein (Fig. 5B).
PMID:11248251	FYPO:0008145	decreased level of heme O in cell [has_severity] high	This was not true of the cox15 mutant which had a very low but detectable amount of heme O (Fig. 1).
PMID:11248251	GO:0120547	heme A synthase activity [part_of] heme A biosynthetic process	We propose that the two proteins are part of a mitochondrial (prokaryotic) type monooxygenase that hydroxylates the methyl group of heme O. Accordingly, the third component of this pathway is ferredoxin (adrenodoxin) dehydrogenase encoded by ARH1 which has been localized in mitochondria of S. cerevisiae [13]. As depicted in Fig. 3, the function of Cox15p would be analogous to that of P450 in other three component monooxygenases [14].
PMID:11250892	GO:0004674	protein serine/threonine kinase activity [happens_during] mitotic M phase [part_of] positive regulation of septation initiation signaling	(Fig. 1)
PMID:11250892	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPAC23C11.16	(Fig. 7)
PMID:11250892	GO:0072686	mitotic spindle	(Figure 1C)
PMID:11250892	FYPO:0001384	abolished protein kinase activity [assayed_enzyme] PomBase:SPAC23C11.16	(Figure 3)
PMID:11252721	FYPO:0002061	inviable vegetative cell population	(comment: facs and author comment about growth)
PMID:11260263	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth	(Fig. 2B)
PMID:11260263	FYPO:0000708	decreased mating efficiency	(Fig. 2B)
PMID:11260263	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(comment: CONDITION 0.75 M)
PMID:11263963	GO:0005886	plasma membrane	(Fig. 1B)
PMID:11263963	FYPO:0002459	viable branched, elongated vegetative cell	(Fig. 3A)
PMID:11263963	FYPO:0000648	viable small vegetative cell	(Fig. 3A)
PMID:11263963	FYPO:0001492	viable elongated vegetative cell	(Fig. 3A)
PMID:11263963	FYPO:0002459	viable branched, elongated vegetative cell	(Fig. 3A)
PMID:11263963	FYPO:0001357	normal vegetative cell population growth	(Fig. 3B and D)
PMID:11263963	FYPO:0001355	decreased vegetative cell population growth	(Fig. 3B and D)
PMID:11263963	FYPO:0001357	normal vegetative cell population growth	(Fig. 3B and D)
PMID:11263963	FYPO:0000112	sensitive to sorbitol [has_severity] low	(Fig. 3D)
PMID:11263963	FYPO:0000961	normal growth on sorbitol	(Fig. 3D)
PMID:11263963	FYPO:0000961	normal growth on sorbitol	(Fig. 3D)
PMID:11263963	FYPO:0005889	sensitive to sodium chloride [has_severity] high	(Fig. 3D)
PMID:11263963	FYPO:0005889	sensitive to sodium chloride [has_severity] low	(Fig. 3D)
PMID:11263963	FYPO:0000112	sensitive to sorbitol [has_severity] low	(Fig. 3D)
PMID:11263963	FYPO:0005889	sensitive to sodium chloride [has_severity] medium	(Fig. 3D)
PMID:11263963	FYPO:0002526	sensitive to latrunculin B [has_severity] high	(Fig. 4)
PMID:11263963	FYPO:0002526	sensitive to latrunculin B [has_severity] high	(Fig. 4)
PMID:11263963	FYPO:0002526	sensitive to latrunculin B [has_severity] medium	(Fig. 4)
PMID:11263963	GO:0030546	signaling receptor activator activity [part_of] regulation of cytoskeleton organization [occurs_in] plasma membrane	As shown in Fig. 5, growth of the cells expressing human RACK1 was not seriously affected by the presence of LatB indicating human RACK1 is a functional homolog of Rkp1.
PMID:11271422	FYPO:0000118	multiseptate vegetative cell [has_penetrance] high [has_severity] high	(Fig. 1A)
PMID:11271422	FYPO:0002002	multiseptate vegetative cell, septa grouped [has_penetrance] low [has_severity] low	(Fig. 1A)
PMID:11271422	FYPO:0002049	elongated multinucleate aseptate vegetative cell [has_penetrance] high	(Fig. 1A)
PMID:11271422	FYPO:0004562	binucleate aseptate vegetative cell [has_penetrance] low	(Fig. 2A)
PMID:11271422	FYPO:0000118	multiseptate vegetative cell [has_penetrance] medium	(Fig. 2A)
PMID:11271422	FYPO:0000118	multiseptate vegetative cell [has_penetrance] high	(Fig. 2A)
PMID:11271422	FYPO:0002049	elongated multinucleate aseptate vegetative cell	(Fig. 2B)
PMID:11271422	FYPO:0004562	binucleate aseptate vegetative cell [has_penetrance] low	(Fig. 2B)
PMID:11271422	FYPO:0004562	binucleate aseptate vegetative cell [has_penetrance] low	(Fig. 2B)
PMID:11271422	FYPO:0001315	normal vegetative cell morphology	(Fig. 2B)
PMID:11271422	FYPO:0002060	viable vegetative cell population	(Fig. 3A)
PMID:11271422	FYPO:0005369	abolished cell population growth at low temperature	(Fig. 3A)
PMID:11271422	FYPO:0002060	viable vegetative cell population	(Fig. 3A)
PMID:11271422	FYPO:0002156	binucleate monoseptate cell, with angled septum [has_penetrance] low	Microscopy revealed occasional cells with an aberrant septum or with multiple nuclei Fig. 2A
PMID:11279037	FYPO:0002061	inviable vegetative cell population	(comment: CHECK taf73 does not substitute for taf5)
PMID:11294895	GO:0032153	cell division site [exists_during] mitotic M phase	(comment: localization requires F-actin -assayed using latrunculin A)
PMID:11294895	GO:0051286	cell tip [exists_during] mitotic M phase	(comment: localization requires F-actin -assayed using latrunculin A)
PMID:11294895	GO:0051286	cell tip [exists_during] mitotic interphase	(comment: localization requires F-actin -assayed using latrunculin A)
PMID:11294907	GO:0110085	mitotic actomyosin contractile ring	(comment: dependent on actin cytoskeleton (assayed using Latrunculin A))
PMID:11294907	GO:0031097	medial cortex [exists_during] mitotic cytokinesis	(comment: dependent on actin cytoskeleton (assayed using Latrunculin A))
PMID:11294907	GO:0030479	actin cortical patch [exists_during] meiotic cell cycle phase	(comment: dependent on actin cytoskeleton (assayed using Latrunculin A))
PMID:11294907	GO:0030479	actin cortical patch [exists_during] mitotic cell cycle phase	(comment: dependent on actin cytoskeleton (assayed using Latrunculin A))
PMID:11313455	GO:0003682	chromatin binding	(comment: increased during response to DNA damage by MMS or ionizing radiation; dissociates during response to HU)
PMID:11313465	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC18B5.03 [part_of] mitotic DNA replication checkpoint signaling	(comment: CHECK cellular response to hydroxyurea)
PMID:11313465	GO:0004674	protein serine/threonine kinase activity [directly_positively_regulates] PomBase:SPCC18B5.11c [part_of] mitotic DNA replication checkpoint signaling	(comment: CHECK phosphorylates Cds1)
PMID:11313465	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC216.05 [added_during] cellular response to hydroxyurea	(comment: Rad3 phosphorylates T11 in response to hydroxyurea treatment)
PMID:11331883	FYPO:0005648	sister kinetochore dissociation in meiotic metaphase I	(Fig. 2c and Table 1)
PMID:11331883	FYPO:0007661	normal protein localization to kinetochore during meiotic metaphase I [assayed_using] PomBase:SPBC29A10.14	Consistently, Rec8 localization was indistinguishable from wild-type from early meiosis and until metaphase I (Fig. 3). Rec8 first appeared in the centromeric regions of cells before conjugation (Fig. 3, G1 cells) and its distribution was further extended throughout chromatin during the horse-tail stage and until metaphase I. Therefore, Rec8 is properly localized and co-orientation still occurs in the absence of Bub1, indicating that the occurrence of equational segregation in Dbub1 cells may be due to a defect in functional fusion of sister kinetochores rather than to defective co-orientation of sister centromeres.
PMID:11331883	FYPO:0007662	abolished protein localization to kinetochore during meiotic anaphase I [assayed_using] PomBase:SPBC29A10.14	In contrast, Rec8 disappeared completely in Dbub1 anaphase I cells. Rec8 was not observed in any of the >100 late-anaphase cells examined and was obviously never detected in early MII cells
PMID:11331883	FYPO:0007663	abolished protein localization to kinetochore during meiosis II [assayed_using] PomBase:SPBC29A10.14	In contrast, Rec8 disappeared completely in Dbub1 anaphase I cells. Rec8 was not observed in any of the >100 late-anaphase cells examined and was obviously never detected in early MII cells
PMID:11331883	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 39.4	Table1
PMID:11331883	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 89	Table1 Interestingly, sister chromatids do not segregate randomly in the absence of Rec8 but rather segregate equationally10 (Table 1), implying that cohesion must be preserved between sister centromeres to give them a mitotic-like, back-to-back orientation
PMID:11331883	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 87.1	Table1 Together, these results rule out the possibility that equational segregation in the absence of Bub1 is due to loss of sister-chromatid cohesion before attachment of kinetochores to microtubules.
PMID:11331883	GO:1990813	meiotic centromeric cohesion protection in anaphase I	The most straightforward interpretation is that Bub1 is required to maintain sister-chromatid cohesion at anaphase I by preventing the removal of Rec8 from centromeric regions.
PMID:11350031	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC2G11.14	(comment: all taf1 introns affected)
PMID:11359920	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 55	(comment: CONDITION 30 degrees)
PMID:11359920	FYPO:0002097	decreased protein kinase activity during cellular response to hydroxyurea [assayed_enzyme] PomBase:SPCC18B5.11c	(comment: CONDITION 30 degrees)
PMID:11359920	FYPO:0001933	abnormal mitotic cell cycle regulation during cellular response to hydroxyurea	(comment: CONDITION 30 degrees)
PMID:11359920	FYPO:0004548	normal protein kinase activity during cellular response to hydroxyurea [assayed_enzyme] PomBase:SPCC1259.13	(comment: CONDITION 30 degrees)
PMID:11359920	FYPO:0000416	premature mitotic sister chromatid separation [has_penetrance] 9	(comment: CONDITION 30 degrees)
PMID:11359920	FYPO:0000416	premature mitotic sister chromatid separation [has_penetrance] 34	(comment: CONDITION 30 degrees)
PMID:11359920	FYPO:0001430	abnormal mitotic cell cycle arrest with unreplicated DNA	(comment: CONDITION 30 degrees)
PMID:11359920	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 37	(comment: CONDITION 30 degrees)
PMID:11359920	FYPO:0000416	premature mitotic sister chromatid separation [has_penetrance] 22	(comment: CONDITION 30 degrees)
PMID:11359920	FYPO:0000416	premature mitotic sister chromatid separation [has_penetrance] 13	(comment: CONDITION 30 degrees)
PMID:11359928	FYPO:0000021	spheroid vegetative cell [has_penetrance] high	(Fig. 2c)
PMID:11359928	FYPO:0005465	normal cell polarity [has_penetrance] high	(Fig. 2c)
PMID:11359928	FYPO:0002086	exocytic vesicles present in increased numbers [has_penetrance] high	(Fig. 3a)
PMID:11359928	FYPO:0000021	spheroid vegetative cell [has_penetrance] high	(Fig. 8)
PMID:11359928	FYPO:0000729	delayed onset of actomyosin contractile ring assembly [has_penetrance] high	(Figure 4A)
PMID:11359928	FYPO:0004097	normal actomyosin contractile ring contraction [has_penetrance] high	(Figure 4A)
PMID:11369198	GO:0000776	kinetochore [exists_during] mitotic metaphase	(Fig. 2B)
PMID:11369198	GO:0044732	mitotic spindle pole body [exists_during] mitotic anaphase	(Fig. 2B)
PMID:11369198	FYPO:0006102	interphase microtubules absent from cell [has_penetrance] high	(Figure 5b)
PMID:11369198	FYPO:0003758	mitotic spindle elongation without chromosome separation [has_penetrance] high	(Figure 5b)
PMID:11369198	FYPO:0004236	thin mitotic spindle midzone	(Figure 5b)
PMID:11369198	GO:0005881	cytoplasmic microtubule [exists_during] mitotic interphase	Movie 1A
PMID:11369198	FYPO:0002061	inviable vegetative cell population	data not shown
PMID:11384993	FYPO:0001382	decreased protein kinase activity [assayed_using] PomBase:SPAC9G1.09	(comment: a significant reduction in kinase activity, 40% of Sid1)
PMID:11384993	FYPO:0001384	abolished protein kinase activity [assayed_using] PomBase:SPAC9G1.09	(comment: barely above background for vector alone and Sid1C) (Fig. 2B)
PMID:11387218	FYPO:0002541	increased protein localization to nucleoplasm [assayed_using] PomBase:SPAC664.01c	(comment: punctate in wild type, diffuse throughout nucleus in mutant)
PMID:11387325	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPBC2F12.08c [part_of] 7-methylguanosine mRNA capping [occurs_in] chromatin	The key findings were that the S. pombe guanylyltransferase bound equally well to the CTD Ser5-PO4 peptide and the Ser2-PO4/Ser5-PO4 peptide. Slightly less than one-fifth of the input protein was retained on the beads in both cases
PMID:11387325	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPBC2F12.08c [part_of] 7-methylguanosine mRNA capping [occurs_in] chromatin	The key findings were that the S. pombe guanylyltransferase bound equally well to the CTD Ser5-PO4 peptide and the Ser2-PO4/Ser5-PO4 peptide. Slightly less than one-fifth of the input protein was retained on the beads in both cases
PMID:11387325	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPAC644.04 [part_of] 7-methylguanosine mRNA capping [occurs_in] chromatin	The novel finding was that the recombinant S. pombe RNA triphosphatase by itself bound specifically to CTD peptides phosphorylated on Ser-5 and not to the unphosphorylated peptide or the Ser2-PO4 peptide (Fig. 3B).
PMID:11387325	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC28F2.12 [assayed_protein] PomBase:SPBC2F12.08c	To gauge the role of the non-reiterated protein segment, we constructed an AD-Rpb1(1516 -1752) fusion clone and tested it in a directed two-hybrid assay paired with BD-Pce1 and BD- Pct1. We found that the Rpb1 interaction with both capping enzymes persisted when the AD fusion contained little more than the CTD repeats per se.
PMID:11387325	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC28F2.12 [assayed_protein] PomBase:SPAC644.04	To gauge the role of the non-reiterated protein segment, we constructed an AD-Rpb1(1516 -1752) fusion clone and tested it in a directed two-hybrid assay paired with BD-Pce1 and BD- Pct1. We found that the Rpb1 interaction with both capping enzymes persisted when the AD fusion contained little more than the CTD repeats per se.
PMID:11389847	FYPO:0006613	decreased termination of RNA polymerase II transcription [has_severity] high	(Fig. 2)
PMID:11389847	FYPO:0006279	normal termination of RNA polymerase II transcription	(Fig. 5A)
PMID:11389847	FYPO:0006279	normal termination of RNA polymerase II transcription	(Fig. 5A)
PMID:11389847	FYPO:0006279	normal termination of RNA polymerase II transcription	(Fig. 5A)
PMID:11389847	FYPO:0006613	decreased termination of RNA polymerase II transcription [has_severity] high	(Fig. 5A)
PMID:11405625	FYPO:0002151	inviable spore [has_penetrance] high	(comment: CHECK high penetrance = large fraction of cells)
PMID:11414703	FYPO:0002059	inviable cell population	One of the diploid clones (C1) was allowed to sporulate and ;100 of the haploids obtained were tested for resistance to G418. We found no resistants, which implicates that spSNW1 is an essential gene in S. pombe.
PMID:11432827	FYPO:0000141	abnormal mitotic sister chromatid segregation	(Figure 1A)
PMID:11432827	FYPO:0001574	abnormal bipolar mitotic spindle	(Figure 1A)
PMID:11432827	FYPO:0000131	abnormal mitotic spindle elongation	(Figure 1A)
PMID:11432827	FYPO:0004317	abnormal post-anaphase array morphology	(Figure 1A)
PMID:11432827	FYPO:0006196	short misoriented interphase microtubules	(Figure 1C)
PMID:11432827	FYPO:0000276	monopolar mitotic spindle	(Figure 1C)
PMID:11432827	FYPO:0001734	abolished mitotic spindle pole body separation	(Figure 1C)
PMID:11432827	FYPO:0002060	viable vegetative cell population	(Figure 2C)
PMID:11432827	FYPO:0001491	viable vegetative cell	(Figure 2C)
PMID:11432827	FYPO:0002061	inviable vegetative cell population	(Figure 3A) (comment: rapid loss of viability)
PMID:11432827	FYPO:0003165	cut with abnormal chromosome segregation	(Figure 3B)
PMID:11432827	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Figure 3F)
PMID:11432827	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Figure 4A)
PMID:11432827	FYPO:0003165	cut [has_penetrance] 20	(Figure 4B)
PMID:11432827	FYPO:0002061	inviable vegetative cell population	(Table 1)
PMID:11432827	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(comment: Question could be required for, or upstream spindle checkpoint, but it could cause a problem which preceds the point where it is possible to activate the checkpoint?BUT...alp14 and mad2 in same pathway and overexpression of mad2 cannot resuce defect of double/single mutant)
PMID:11432827	FYPO:0000416	premature mitotic sister chromatid separation	(comment: cut2 levels were reduced in alp14 mutant)
PMID:11432827	GO:0000940	outer kinetochore	(comment: dependent on mitotic spindle)
PMID:11448769	GO:0072686	mitotic spindle [exists_during] mitotic M phase	(comment: vw sid2 phenotype indicates that Clp1 localization is independent of SIN)
PMID:11453249	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Table 2)
PMID:11453249	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Expression of Mkh1p in wild-type cells also conferred a growth defect Ta- ble 2),
PMID:11453249	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Expression of Mkh1pin wild-type cells also conferred a growth defect Ta-ble 2), but the phenotype was not rescued by the Dpak2 mutation.
PMID:11453249	FYPO:0001122	elongated vegetative cell [has_penetrance] 16	Expression of Pak2D17±273p in wild- type cells also led to an increase in elongated cells within the population that was suppressed in Dmkh1 cells Fig. 1B), with 16% of Pak2D17±273p-expressing wild- type cells n=200) displaying an$2-fold increase in cell length
PMID:11453249	FYPO:0001122	elongated vegetative cell [has_penetrance] 4	Expression of Pak2D17±273p in wild- type cells also led to an increase in elongated cells within the population that was suppressed in Dmkh1 cells Fig. 1B), with 16% of Pak2D17±273p-expressing wild- type cells n=200) displaying an$2-fold increase in cell length versus 4% of Dmkh1cells.
PMID:11453249	FYPO:0001122	elongated vegetative cell [has_penetrance] 4	Expression of Pak2D17±273p in wild- type cells also led to an increase in elongated cells within the population that was suppressed in Dmkh1 cells Fig. 1B), with 16% of Pak2D17±273p-expressing wild- type cells n=200) displaying an$2-fold increase in cell length versus 4% of Dmkh1cells.
PMID:11453249	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Expression of Pak2D17±273p under the control of the thiamine-repressible nmt1 pro- moter, but not full length Pak2p, conferred a growth defect in wild-type cells (Fig. 1A; Table 2)
PMID:11453249	FYPO:0001357	normal vegetative cell population growth	Expression of Pak2D17±273p under the control of the thiamine-repressible nmt1 pro- moter, but not full length Pak2p, conferred a growth defect in wild-type cells but not in Dmkh1or Dspm1cells Fig. 1A; Table 2).
PMID:11453249	FYPO:0001357	normal vegetative cell population growth	Expression of Pak2D17±273p under the control of the thiamine-repressible nmt1 pro- moter, but not full length Pak2p, conferred a growth defect in wild-type cells but not in Dmkh1or Dspm1cells Fig. 1A; Table 2).
PMID:11453249	FYPO:0001357	normal vegetative cell population growth	Expression of Pak2D17±273p under the control of the thiamine-repressible nmt1 pro- moter, but not full length Pak2p, conferred a growth defect in wild-type cells but not in Dmkh1or Dspm1cells Fig. 1A; Table 2).
PMID:11453249	FYPO:0001357	normal vegetative cell population growth	Expression of Pak2D17±273p under the control of the thiamine-repressible nmt1 pro- moter, but not full length Pak2p, conferred a growth defect in wild-type cells but not in Dmkh1or Dspm1cells Fig. 1A; Table 2).
PMID:11453249	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Expression of the activated cdc42G12V allele in wild-type cells resulted in a growth defect (Fig. 2A)
PMID:11453249	FYPO:0004103	viable spherical vegetative cell	Expression of the activated cdc42G12V allele in wild-type cells resulted in a growth defect (Fig. 2A) and a round cell morphology (Fig. 2B).
PMID:11453249	FYPO:0000947	swollen spherical vegetative cell	However, the round cell morphology was not appreciably aected by the Dpak2 (Fig. 2B)
PMID:11453249	GO:1903137	regulation of cell integrity MAPK cascade	In this work, we show that Sch. pombe Cdc42p interfaces with the Mkh1p- Pek1p-Spm1p pathway via the Pak2p PAK.
PMID:11453249	GO:1903137	regulation of cell integrity MAPK cascade	In this work, we show that Sch. pombe Cdc42p interfaces with the Mkh1p- Pek1p-Spm1p pathway via the Pak2p PAK.
PMID:11453249	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	The Dspm1 mutation did not suppress the growth phenotype (Table 2)
PMID:11453249	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	The growth phenotype was partially suppressed by the Dpak2 and Dmkh1 null mu- tations (Fig. 2A; Table 2),
PMID:11453249	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	The growth phenotype was partially suppressed by the Dpak2 and Dmkh1 null mu- tations (Fig. 2A; Table 2),
PMID:11453249	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	The growth phenotype was partially suppressed by the Dpak2 and Dmkh1 null mu- tations (Fig. 2A; Table 2),
PMID:11453249	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	The growth phenotype was partially suppressed by the Dpak2 and Dmkh1 null mu- tations (Fig. 2A; Table 2),
PMID:11460168	FYPO:0000130	short spindle [has_penetrance] 25	(Fig. 1E and F)
PMID:11460168	FYPO:0009019	increased vegetative cell population binucleate index [has_severity] high	(Fig. 2B)
PMID:11460168	FYPO:0006660	loss of viability upon G0 to G1 transition [has_severity] high	(Fig. 2C)
PMID:11460168	FYPO:0009019	increased vegetative cell population binucleate index	(Fig. 2D)
PMID:11460168	PomGeneEx:0000020	protein level unchanged [in_presence_of] latrunculin B	(Fig. 3B)
PMID:11460168	PomGeneEx:0000019	protein level decreased [in_presence_of] latrunculin B	(Fig. 3B)
PMID:11460168	PomGeneEx:0000020	protein level unchanged [in_presence_of] latrunculin B	(Fig. 3B)
PMID:11460168	FYPO:0002526	sensitive to latrunculin B [has_severity] medium	(Fig. 4A)
PMID:11460168	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:11460168	PomGeneEx:0000018	protein level increased [in_presence_of] latrunculin B	(Fig. 4B)
PMID:11460168	MOD:00696	phosphorylated residue [increased_in_presence_of] latrunculin B	(Fig. 4B)
PMID:11460168	FYPO:0009019	increased vegetative cell population binucleate index	(Fig. 4D)
PMID:11460168	FYPO:0006660	loss of viability upon G0 to G1 transition	(Fig. 4E)
PMID:11460168	FYPO:0001252	multinucleate multiseptate vegetative cell [has_severity] high	(Fig. 4F)
PMID:11460168	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	Cells that lack Mad2 arrest in metaphase in the presence of Lat B (Fig. 3a)
PMID:11460168	FYPO:0004318	abolished mitotic spindle assembly checkpoint [has_penetrance] complete	Importantly, we found that synchronized Datf1 cells completely failed to arrest nuclear division in the presence of Lat B (Fig. 4d)
PMID:11460168	FYPO:0004318	abolished mitotic spindle assembly checkpoint [has_penetrance] complete	We found that a rad21-45 mutant was unable to arrest in the presence of Lat B. Fig. 2B and C
PMID:11493649	GO:0051447	negative regulation of meiotic cell cycle	(comment: CHECK negative regulation of meiotic exit)
PMID:11493649	GO:0051446	positive regulation of meiotic cell cycle	(comment: CHECK positive regulation of meiotic cell cycle exit)
PMID:11509236	FYPO:0000426	normal endocytosis	After 15 min, vacuoles were visible in all three strains, and this observation demonstrates that, as in budding yeast [8, 9], endocytosis does not require a functional type V myosin.
PMID:11509236	FYPO:0000426	normal endocytosis	After 15 min, vacuoles were visible in all three strains, and this observation demonstrates that, as in budding yeast [8, 9], endocytosis does not require a functional type V myosin.
PMID:11509236	FYPO:0002792	small vacuoles present in increased numbers during cellular hypotonic response	vacuoles in myo52Δ were smaller (0.21 ± 0.14 μm). (Figure 1)
PMID:11514435	FYPO:0005754	increased (1->3)-alpha-D-glucan level in periplasmic space [has_penetrance] high [has_severity] high	(Fig. 6)
PMID:11514435	FYPO:0005755	increased (1->3)-beta-D-glucan level in periplasmic space [has_penetrance] high [has_severity] high	(Fig. 6)
PMID:11514435	FYPO:0002627	altered level of substance in cell wall during vegetative growth	(Figure 1)
PMID:11514435	FYPO:0001084	increased cell wall alpha-glucan level [has_severity] high [has_penetrance] high	(Figure 1, 3B; Table 2)
PMID:11514435	FYPO:0004860	increased cell wall beta-glucan level [has_penetrance] high [has_severity] high	(Figure 1, 3B; Table 2)
PMID:11514435	FYPO:0001489	inviable vegetative cell	(Figure 2a)
PMID:11514435	FYPO:0002061	inviable vegetative cell population	(Figure 2a)
PMID:11514435	FYPO:0002061	inviable vegetative cell population	(Figure 2a)
PMID:11514435	GO:0016020	membrane	(Figure 4D)
PMID:11514435	GO:0005886	plasma membrane	(Figure 4D,5)
PMID:11514435	GO:0071944	cell periphery	(Figure 5)
PMID:11514435	FYPO:0005757	abolished protein localization to membrane during vegetative growth [assayed_using] PomBase:SPBC32F12.01c	(Figure 5D)
PMID:11514435	FYPO:0005757	abolished protein localization to membrane during vegetative growth [assayed_using] PomBase:SPBC32F12.01c	(Figure 5E)
PMID:11514435	FYPO:0002674	normal protein localization to plasma membrane [assayed_using] PomBase:SPBC32F12.01c	(Figure 5E) (comment: to membrane)
PMID:11514435	GO:0052714	mannosyl-inositol phosphorylceramide phospholipase activity	(Figure 7D) (comment: assayed reaction products)
PMID:11514435	FYPO:0005485	abolished inositol phosphate phosphatase activity	(Figure 7b)
PMID:11514435	FYPO:0005485	abolished inositol phosphate phosphatase activity	(Figure 7b)
PMID:11514435	GO:0052712	inositol phosphosphingolipid phospholipase activity	(Figure 7b) (comment: heterologous complementation)
PMID:11514435	GO:0046521	sphingoid catabolic process	(comment: from MF)
PMID:11514435	GO:0046513	ceramide biosynthetic process	(comment: from MF)
PMID:11514436	FYPO:0001357	normal vegetative cell population growth	(Figure 1C, lane 8
PMID:11514436	FYPO:0002061	inviable vegetative cell population	(Figure 2A).
PMID:11514436	FYPO:0006023	elongated multinucleate multiseptate vegetative cell, irregular septum position	(Figure 2b)
PMID:11514436	FYPO:0002061	inviable vegetative cell population	(Figure 3a)
PMID:11514436	FYPO:0002061	inviable vegetative cell population	(Figure 3a)
PMID:11514436	FYPO:0002061	inviable vegetative cell population	(Figure 3a)
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	(Figure 3b)
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	(Figure 3b)
PMID:11514436	FYPO:0001876	decreased asymmetric protein localization, with protein localized to both mitotic spindle pole bodies during anaphase [assayed_protein] PomBase:SPBC21.06c [has_penetrance] 10	(Figure 4a)
PMID:11514436	FYPO:0001120	pear-shaped vegetative cell	(Figure 4a)
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	(comment: SID PHENOTYPE) (Figure 2B).
PMID:11514436	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC21.06c	(comment: asymetric localization is normal)
PMID:11514436	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC21.06c	(comment: dns)
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	Table 2, par1/2 does not supress sin phenotype
PMID:11514436	FYPO:0002151	inviable spore	The fact that out of almost 200 tetrads analyzed, not a single ura spore survived confirmed that spg1 is essential for vegetative growth, and this essential function cannot be bypassed by inactivating par1 and par2 by deletion.
PMID:11553781	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC1259.13 [part_of] mitotic G2 DNA damage checkpoint signaling	(comment: vw: changed from response to chemical to part of DNA damage checkpoint signalling)
PMID:11554922	FYPO:0000188	abnormal DNA repair during vegetative growth	(comment: evidence: immunoblot using antibody that recognizes thymine dimers)
PMID:11598020	GO:0000228	nuclear chromosome [exists_during] mitotic interphase	(Fig. 4a)
PMID:11598020	GO:0005721	pericentric heterochromatin	(Fig. 4a)
PMID:11598020	GO:0005721	pericentric heterochromatin	(Fig. 4a)
PMID:11598020	GO:0000228	nuclear chromosome [exists_during] mitotic prometaphase	(Fig. 4a)
PMID:11598020	GO:0005634	nucleus	(Fig. 4a)
PMID:11600706	GO:0005515	protein binding	(Fig. 2B)
PMID:11600706	GO:0005515	protein binding	(Fig. 2B)
PMID:11600706	FYPO:0002778	decreased protein sumoylation during vegetative growth	(Figure 1C)
PMID:11600706	FYPO:0005934	abolished protein sumoylation during vegetative growth	(Figure 1C)
PMID:11600706	MOD:01149	sumoylated lysine	(Figure 3B)
PMID:11600706	GO:0061656	SUMO conjugating enzyme activity [has_input] PomBase:SPAC30D11.10 [part_of] protein sumoylation	(comment: vw: in vitro purification system)
PMID:11600706	GO:0061656	SUMO conjugating enzyme activity [part_of] protein sumoylation [has_input] PomBase:SPAC30D11.10	(comment: vw: in vitro purification system)
PMID:11600706	GO:0019948	SUMO activating enzyme activity [part_of] protein sumoylation [has_input] PomBase:SPAC30D11.10	(comment: vw: in vitro purification system)
PMID:11606752	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC14C8.07c	(comment: CHECK level of mutant cdc18deltaCDK1-5 protein)
PMID:1165770	FYPO:0006031	delayed onset of mitotic DNA replication initiation [has_penetrance] high	(Figure 3)
PMID:1165770	FYPO:0006848	decreased total RNA level during vegetative growth [has_penetrance] high	(Table 1)
PMID:1165770	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(Table 1)
PMID:1165770	FYPO:0006846	decreased total protein level during vegetative growth [has_penetrance] high	(Table 1)
PMID:1165770	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(comment: CHECK cdc9-50 is the original name for wee1-50 allele. It was changed in subsequent publications to wee1 because of its phenotype and there is now no cdc9 gene)
PMID:1165770	FYPO:0002516	premature mitotic G2/M phase transition [has_penetrance] high	Table 1, Figure 2
PMID:11676915	FYPO:0002912	inviable after spore germination, without cell division, elongated multinucleate cell	(Fig. 1a)
PMID:11676915	FYPO:0001368	normal actomyosin contractile ring assembly	(Fig. 1a)
PMID:11676915	FYPO:0004623	abolished astral microtubule anchoring at mitotic spindle pole body [has_penetrance] 85	(Fig. 1a)
PMID:11676915	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC244.01c	(Fig. 5a)
PMID:11676915	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16	(Fig. 5c)
PMID:11676915	GO:0044732	mitotic spindle pole body [exists_during] mitotic interphase	(Figure 3b)
PMID:11676915	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	(Figure 3b)
PMID:11676915	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1739.11c [assayed_using] PomBase:SPBC244.01c	(Figure 6)
PMID:11676915	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC24B11.11c	(Figure 6)
PMID:11676915	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPCC1739.11c	(Figure 6)
PMID:11676915	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC1565.06c	(Figure 6)
PMID:11676915	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC9G1.09	(Figure 6)
PMID:11676915	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC21.06c	(Figure 6)
PMID:11676915	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC222.10c	(Figure 6)
PMID:11676915	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPCC1739.11c	(Figure 6)
PMID:11676915	GO:0140378	protein complex scaffold activity [has_input] PomBase:SPAC1565.06c [part_of] septation initiation signaling [occurs_in] mitotic spindle pole body	(comment: scaffold, platform)
PMID:11676915	GO:0140378	protein complex scaffold activity [has_input] PomBase:SPAC222.10c [part_of] septation initiation signaling [occurs_in] mitotic spindle pole body	(comment: scaffold, platform)
PMID:11676915	GO:0140378	protein complex scaffold activity [has_input] PomBase:SPAC24B11.11c [part_of] septation initiation signaling [occurs_in] mitotic spindle pole body	(comment: scaffold, platform)
PMID:11676915	GO:0140378	protein complex scaffold activity [has_input] PomBase:SPBC21.06c [part_of] septation initiation signaling [occurs_in] mitotic spindle pole body [happens_during] mitotic anaphase	(comment: scaffold, platform)
PMID:11676915	FYPO:0000941	abolished protein localization to mitotic spindle pole body	data not shown
PMID:11676924	GO:0140445	chromosome, telomeric repeat region	(comment: colocalizes with this region and taz1, abnormal localization in taz1-delta, and physically associates with taz1)
PMID:11676924	GO:0000723	telomere maintenance	(comment: same_pathway)
PMID:11683390	GO:0044732	mitotic spindle pole body [exists_during] mitotic S phase	(Fig. 2A b-c, 5) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	GO:0044732	mitotic spindle pole body [exists_during] mitotic metaphase	(Fig. 2A b-c, 5) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	GO:0044732	mitotic spindle pole body [exists_during] mitotic G2 phase	(Fig. 2A b-c, 5) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	GO:0044732	mitotic spindle pole body [exists_during] mitotic prophase	(Fig. 2A b-c, 5) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	GO:0044732	mitotic spindle pole body [exists_during] mitotic interphase	(Fig. 2A b-c, 5D) (comment: pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	GO:0044732	mitotic spindle pole body [exists_during] mitotic prophase	(Fig. 2A b-c, 5D) (comment: pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	GO:0044732	mitotic spindle pole body [exists_during] mitotic metaphase	(Fig. 2A b-c, 5D) (comment: pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	GO:0005634	nucleus [exists_during] mitotic metaphase	(Fig. 2A) (comment: pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF))
PMID:11683390	GO:0005634	nucleus [exists_during] mitotic interphase	(Fig. 2A) (comment: pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF))
PMID:11683390	GO:0005634	nucleus [exists_during] mitotic anaphase	(Fig. 2A) (comment: pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF))
PMID:11683390	GO:0005634	nucleus [exists_during] mitotic prophase	(Fig. 2A) (comment: pREP5cdc13-YFP integrant grown in YE+supplements (i.e. promoter OFF))
PMID:11683390	GO:0005634	nucleus [exists_during] mitotic telophase	(Fig. 2A, 2B) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	GO:0005634	nucleus [exists_during] mitotic S phase	(Fig. 2A, 2B) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	GO:0005634	nucleus [exists_during] mitotic G2 phase	(Fig. 2A, 2B) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	GO:0005634	nucleus [exists_during] mitotic prophase	(Fig. 2A, 2B) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	GO:0005634	nucleus [exists_during] mitotic metaphase	(Fig. 2A, 2B) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	GO:0005634	nucleus [exists_during] mitotic anaphase	(Fig. 2A, 2B) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	GO:0005737	cytoplasm [exists_during] mitotic G2 phase	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	GO:0005737	cytoplasm [exists_during] mitotic telophase	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	GO:0005737	cytoplasm [exists_during] mitotic anaphase	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	GO:0005737	cytoplasm [exists_during] mitotic G1 phase	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	GO:0005737	cytoplasm [exists_during] mitotic S phase	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	GO:0005737	cytoplasm [exists_during] mitotic metaphase	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	GO:0005737	cytoplasm [exists_during] mitotic prophase	(Fig. 2A, 2B, 4C) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF)) Proportion of total of Cdc2YFP in nucleus and cytoplasm varies across cell cycle. Lowest in nucleus during late mitosis (~ 10% of total), highest in nucleus in late G2 (~30-40%) of total
PMID:11683390	GO:0072686	mitotic spindle [exists_during] mitotic prophase	(Fig. 2A, 3, 5D) (comment: pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	GO:0072686	mitotic spindle [exists_during] mitotic metaphase	(Fig. 2A, 3, 5D) (comment: pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	GO:0072686	mitotic spindle [exists_during] mitotic metaphase	(Fig. 2A, 3, 5D) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	GO:0072686	mitotic spindle [exists_during] mitotic prophase	(Fig. 2A, 3, 5D) (comment: pREP5cdc2YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	GO:0034399	nuclear periphery [exists_during] mitotic anaphase	(Fig. 2C) (comment: pREP5cdc13YFP integrant grown in YE+supplements (i.e. promoter OFF).)
PMID:11683390	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase [has_penetrance] high	(Fig. 6)
PMID:11683390	FYPO:0004332	delayed onset of protein degradation during mitosis [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 6) Cdc13YFP and Cdc2YFP remain associated with spindle, SPB. Cdc13 is not degraded by defective proteasome. Rpt1 is called Mts2 in this paper
PMID:11683390	FYPO:0004332	delayed onset of protein degradation during mitosis [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 6) Cdc13YFP and Cdc2YFP remain associated with spindle, SPB. Cdc13 is not recognised by defective APC
PMID:11683390	FYPO:0004332	delayed onset of protein degradation during mitosis [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 6) Cdc2YFP and non-degradable Cdc13YFP remain associated with spindle, SPB.Cdc13 degradation is abolished rather than delayed
PMID:11683390	FYPO:0003627	normal protein localization [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 7)
PMID:11683390	FYPO:0003627	normal protein localization [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Fig. 7)
PMID:11683390	FYPO:0004532	abnormal cell cycle arrest in mitotic M phase with abnormal spindle [has_penetrance] high	(Fig. 7)
PMID:11683390	GO:0035974	meiotic spindle pole body [exists_during] karyogamy involved in conjugation with cellular fusion	(Fig. 7) (comment: do not actually say it is associated with SPB just SPB region, i.e. telomere-SPB- centromere bouquet cluster)
PMID:11683390	GO:0005634	nucleus [exists_during] karyogamy involved in conjugation with cellular fusion	(Fig. 8)
PMID:11683390	FYPO:0000514	abolished nuclear import [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Figure 4A)
PMID:11683390	FYPO:0003189	decreased protein import into nucleus [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Figure 4A) (comment: Cdc13YFP expressed from integrated pREP45)
PMID:11683390	FYPO:0003449	abnormal cell cycle arrest at mitotic G1/S phase transition [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Figure 4A) (comment: Cdc13YFP expressed from integrated pREP45.)
PMID:11683390	FYPO:0003189	decreased protein import into nucleus [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Figure 4A) (comment: Cdc13YFP expressed from integrated pREP45.) Decreased nuclear import of cdc2YFP compared to cdc13delta cig1delta mutant
PMID:11683390	FYPO:0003449	abnormal cell cycle arrest at mitotic G1/S phase transition [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Figure 4B) (comment: Cdc13YFP expressed from integrated pREP45)
PMID:11683390	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPBC11B10.09	Data not shown. (comment: Cdc2 does not go prematurely to the SPB in a cut12 mutant (this is the stf1-1 mutant))
PMID:11683390	GO:0000776	kinetochore	cdc2 is localised at the centromeres during horse tail movement. Fig 9 shows that cdc2YFP is associated with cen1GFP
PMID:11685532	GO:0000776	kinetochore	(comment: mitotic, in meiosis it is only n the kinetochore during meitoic division(metaphase/anaphase) not during prophase)
PMID:11694585	FYPO:0004257	swollen multinucleate vegetative cell	(comment: CONDITION 27 degrees C)
PMID:11694585	FYPO:0002023	abnormal septum morphology during vegetative growth	(comment: CONDITION 27 degrees C)
PMID:11694585	FYPO:0004257	swollen multinucleate vegetative cell	(comment: CONDITION 27 degrees C)
PMID:11694585	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 30 degrees C)
PMID:11694585	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 30 degrees C)
PMID:11694585	GO:0051015	actin filament binding	(comment: assayed using purified rabbit skeletal muscle F-actin)
PMID:11694585	GO:0030479	actin cortical patch	(comment: dependent on actin cytoskeleton (assayed using Latrunculin A))
PMID:11694585	GO:0032153	cell division site	(comment: dependent on actin cytoskeleton (assayed using Latrunculin A))
PMID:11694585	FYPO:0002437	thick actin cables	(comment: temperature permissive for cdc4-8)
PMID:11694585	FYPO:0003315	actin cables absent from cell	(comment: temperature restrictive for cdc4-8)
PMID:11694585	FYPO:0002415	inviable swollen vegetative cell with abnormal cell shape [has_penetrance] high	(comment: various abnormal shapes)
PMID:11694585	FYPO:0002415	inviable swollen vegetative cell with abnormal cell shape [has_penetrance] high	(comment: various abnormal shapes)
PMID:11694585	GO:0051017	actin filament bundle assembly	in vitro bundling, detected by microscopy; Figure 2
PMID:11696322	FYPO:0000016	curved vegetative cell	(Figure 3)
PMID:11696322	FYPO:0003315	actin cables absent from cell	(Figure 3b-g)
PMID:11696322	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth	(Figure 3b-g,i)
PMID:11696322	FYPO:0000443	abnormal protein localization during vegetative growth [assayed_using] PomBase:SPCC645.05c	(Figure 3b-g,i)
PMID:11696322	FYPO:0001368	normal actomyosin contractile ring assembly	(Figure 3f,g)
PMID:11696322	FYPO:0001367	normal cytokinesis	(Figure 3f,g)
PMID:11696322	FYPO:0002401	microtubule bundles present in increased numbers	(Figure 4, table 1)
PMID:11696322	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	(Figure 5a)
PMID:11696322	GO:0031097	medial cortex [exists_during] mitotic metaphase	(Figure 5b,c)
PMID:11696322	GO:0036391	medial cortex septin ring [exists_during] mitotic anaphase	(Figure 5e)
PMID:11696322	FYPO:0003225	normal rate of microtubule polymerization during vegetative growth	(Table 1)
PMID:11696322	FYPO:0003193	normal rate of microtubule depolymerization during vegetative growth	(Table 1)
PMID:11696322	FYPO:0001234	slow vegetative cell population growth	data not shown
PMID:11719193	GO:0008821	crossover junction DNA endonuclease activity	(comment: magneisum activated_by CHEBI:18420)
PMID:11737264	FYPO:0000647	vegetative cell lysis [has_penetrance] low	(comment: population grows well, but very small cells look lysed)
PMID:11737264	FYPO:0007436	swollen elongated multiseptate vegetative cell	(comment: population is viable but sick, and the elongated multiseptate cells are probably dead)
PMID:11737264	FYPO:0000021	spheroid vegetative cell	(comment: population is viable but sick; can't tell which individual cells are viable)
PMID:11737264	FYPO:0005103	curved elongated vegetative cell	(comment: population is viable but sick; can't tell which individual cells are viable)
PMID:11737264	FYPO:0000647	vegetative cell lysis	(comment: population is viable but sick; can't tell which individual cells are viable, but very small cells look lysed)
PMID:11737264	FYPO:0000647	vegetative cell lysis [has_penetrance] low	(comment: population is viable, but very small cells look lysed)
PMID:11739743	FYPO:0006526	abnormal meiosis II [has_penetrance] 90	. Most of the spo4 cells (approximately 90%) arrested at the binu- cleate stage exhibited cytoplasmic microtubules (Fig. 3C), sug-gesting that these cells were in the interkinesis between meiosis I and meiosis II.
PMID:11739743	GO:0001216	DNA-binding transcription activator activity [has_input] PomBase:SPBC1778.04	Additionally, the transcriptional induction of spo6 coincided with that of spo4 and was regulated in a Mei4-dependent manner (29) (Fig. 4A). T
PMID:11739743	GO:0005634	nucleus [exists_during] meiotic cell cycle phase	During meiosis, Spo4-HA preferentially localized in the nucleus (Fig. 8). The Spo4 signal in the nucleus, how- ever, became less intense as cells proceeded through meiosis II.
PMID:11739743	FYPO:0002937	decreased pre-mRNA level [assayed_transcript] PomBase:SPBC21C3.18 [has_penetrance] complete	In conclusion, the transcription of spo4 is induced during mei- osis under the regulation of Mei4.
PMID:11739743	GO:0106310	protein serine kinase activity	In the presence of Spo6, both autokinase and Mcm2 kinase activities of Spo4 were markedly enhanced (Fig. 7).
PMID:11739743	GO:0043539	protein serine/threonine kinase activator activity	In the presence of Spo6, both autokinase and Mcm2 kinase activities of Spo4 were markedly enhanced (Fig. 7).
PMID:11739743	GO:0005634	nucleus [exists_during] meiotic cell cycle phase	Noticeably, Spo6, a partner of Spo4, localized in the nucleus during meiosis (50).
PMID:11739743	GO:0031431	Dbf4-dependent protein kinase complex	Spo6-FLAG was copurified with GST-Spo4 but not with unfused GST (Fig. 6B). Conversely, the immunoprecipitate obtained with anti- FLAG antibody contained GST-Spo4 (Fig. 6B). A kinase-neg- ative Spo4 (GST-Spo4K95A) was also able to associate with Spo6-FLAG. These results indicate that Spo4-FLAG and GST-Spo6 are physically associated and do not require the Spo4 kinase activity.
PMID:11739743	GO:0031431	Dbf4-dependent protein kinase complex	Spo6-FLAG was copurified with GST-Spo4 but not with unfused GST (Fig. 6B). Conversely, the immunoprecipitate obtained with anti- FLAG antibody contained GST-Spo4 (Fig. 6B). A kinase-neg- ative Spo4 (GST-Spo4K95A) was also able to associate with Spo6-FLAG. These results indicate that Spo4-FLAG and GST-Spo6 are physically associated and do not require the Spo4 kinase activity.
PMID:11739743	FYPO:0004629	normal mitotic DNA replication	The DNA content of spo4 cells roughly doubled prior to meiotic nuclear division (Fig. 3A).
PMID:11739743	FYPO:0000121	abnormal sporulation	The spo4 deletion mutant (spo4 ) was viable but displayed sporulation defects like the original spo4-B4 mu- tant (data not shown).
PMID:11739743	FYPO:0001357	normal vegetative cell population growth	The spo4 deletion mutant (spo4 ) was viable but displayed sporulation defects like the original spo4-B4 mu- tant (data not shown).
PMID:11739743	FYPO:0004095	normal protein localization during meiotic cell cycle [assayed_protein] PomBase:SPBC21C3.18	To clarify whether Spo6 determines the nuclear localization of Spo4, we observed the localization of Spo4 in the spo6 mutant. How- ever, the nuclear localization of Spo4-HA was not affected by the spo6 mutation (Fig. 8),
PMID:11739743	FYPO:0000121	abnormal sporulation	We ex- pressed these mutant genes under the control of the nmt1 promoter in a spo4 mutant. As Fig. 2C shows, none of these mutant spo4 genes complement the sporulation defect of the spo4 mutant.
PMID:11739743	FYPO:0000121	abnormal sporulation	We ex- pressed these mutant genes under the control of the nmt1 promoter in a spo4 mutant. As Fig. 2C shows, none of these mutant spo4 genes complement the sporulation defect of the spo4 mutant.
PMID:11739743	FYPO:0000121	abnormal sporulation	We ex- pressed these mutant genes under the control of the nmt1 promoter in a spo4 mutant. As Fig. 2C shows, none of these mutant spo4 genes complement the sporulation defect of the spo4 mutant.
PMID:11739743	FYPO:0000121	abnormal sporulation	We ex- pressed these mutant genes under the control of the nmt1 promoter in a spo4 mutant. As Fig. 2C shows, none of these mutant spo4 genes complement the sporulation defect of the spo4 mutant.
PMID:11739743	FYPO:0003563	normal meiosis I	We next examined the precise arrest phenotype of a ho- mozygous spo4 diploid strain during meiosis. Meiosis was induced by transferring a log-phase culture to nitrogen-free medium. spo4 cells proceeded through meiosis I with kinetics similar to those of the wild type. However, approximately 80% of spo4 cells arrested at the binucleate stage (Fig. 3B).
PMID:11739743	FYPO:0002043	normal premeiotic DNA replication	We observed a similar result with spo4 homozygous diploid cells cultured in nitrogen-free medium for the induction of meiosis (data not shown). We thus conclude that spo4 cells complete premeiotic DNA rep- lication normally.
PMID:11739743	GO:0045944	positive regulation of transcription by RNA polymerase II	spo4 has a consensus sequence (GTAAACAAACA) named FLEX (1, 29) in the 5 upstream region by which a meiosis-specific transcription fac- tor, Mei4, recognizes its targets (Fig. 1C). In fact, transcription of spo4 was completely abolished in mei4 (Fig. 4A).
PMID:11739743	GO:0001216	DNA-binding transcription activator activity [has_input] PomBase:SPBC21C3.18	spo4 has a consensus sequence (GTAAACAAACA) named FLEX (1, 29) in the 5 upstream region by which a meiosis-specific transcription fac- tor, Mei4, recognizes its targets (Fig. 1C). In fact, transcription of spo4 was completely abolished in mei4 (Fig. 4A).
PMID:11739743	FYPO:0006526	abnormal meiosis II	spo6 mutants exhibit defective phenotypes in the second meiotic division and in sporulation similar to spo4 mutants, though the phenotype of spo4 was slightly more severe than that of spo6 (50) (Fig. 3B).
PMID:11739743	PomGeneEx:0000011	RNA level increased [during] meiosis I cell cycle phase	the spo4 mRNA levels were mon- itored by Northern blot analysis. spo4 mRNA was barely de- tectable in vegetative cells, though it abruptly increased during meiosis.
PMID:11739743	PomGeneEx:0000015	RNA absent [during] mitotic cell cycle phase	the spo4 mRNA levels were mon- itored by Northern blot analysis. spo4 mRNA was barely de- tectable in vegetative cells, though it abruptly increased during meiosis.
PMID:11739790	FYPO:0002060	viable vegetative cell population	(Figure 2, Table 2)
PMID:11739790	FYPO:0004511	long curved interphase microtubules	(Figure 4B and D)
PMID:11739790	FYPO:0004511	long curved interphase microtubules	(Figure 4B and D)
PMID:11739790	FYPO:0005426	elongated C-shaped vegetative cell with long curved interphase microtubules [has_severity] high	(comment: arrested)
PMID:11739790	FYPO:0005426	elongated C-shaped vegetative cell with long curved interphase microtubules [has_severity] high	(comment: arrested)
PMID:11739790	FYPO:0005426	elongated C-shaped vegetative cell with long curved interphase microtubules [has_severity] high	(comment: arrested)
PMID:11777938	FYPO:0005322	normal anaphase-promoting complex assembly	(Figure 2)
PMID:11777938	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	(comment: CHECK NORMAL LENGTH)
PMID:11780129	FYPO:0001840	increased minichromosome loss during vegetative growth [has_penetrance] 23	(Fig. 2a, b).
PMID:11780129	FYPO:0001840	increased minichromosome loss during vegetative growth [has_penetrance] 28	(Fig. 2a, b).
PMID:11780129	FYPO:0000468	abnormal mating type switching [has_severity] low	(Fig. 3b, data not shown)
PMID:11780129	FYPO:0000228	lagging mitotic chromosomes	(Figure 2b)
PMID:11780129	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_protein] PomBase:SPAC664.01c	However, this mutation did not affect Swi6 localization at otr and KR (Fig. 1e).
PMID:11780129	GO:0005721	pericentric heterochromatin	Interestingly, we found that Psc3 is enriched at the heterochromatic locations containing Swi6, such as the silent mating-type locus and the centromeric repeats (Fig. 1b, c, wild type).
PMID:11780129	GO:0031934	mating-type region heterochromatin	Interestingly, we found that Psc3 is enriched at the heterochromatic locations containing Swi6, such as the silent mating-type locus and the centromeric repeats (Fig. 1b, c, wild type).
PMID:11780129	GO:0031934	mating-type region heterochromatin	Interestingly, we found that Psc3 is enriched at the heterochromatic locations containing Swi6, such as the silent mating-type locus and the centromeric repeats (Fig. 1b, c, wild type).
PMID:11780129	GO:0005721	pericentric heterochromatin	Interestingly, we found that Psc3 is enriched at the heterochromatic locations containing Swi6, such as the silent mating-type locus and the centromeric repeats (Fig. 1b, c, wild type).
PMID:11780129	FYPO:0000228	lagging mitotic chromosomes	Moreover, the psc3+-GFP swi6∆ cells showed increased mini-chromosome loss and exhibited a high incidence of lagging chromosome and other chromosome segregation abnormalities (Fig. 2c)
PMID:11780129	FYPO:0002842	decreased protein localization to centromere outer repeat [has_severity] high [assayed_protein] PomBase:SPAC17H9.20	Psc3 localization was strikingly disrupted in the swi6∆ strain at both loci (Fig. 1b).
PMID:11780129	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [has_severity] high [assayed_protein] PomBase:SPAC17H9.20	Psc3 localization was strikingly disrupted in the swi6∆ strain at both loci (Fig. 1b).
PMID:11780129	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [has_severity] high [assayed_protein] PomBase:SPAC17H9.20	Psc3 localization was strikingly disrupted in the swi6∆ strain at both loci (Fig. 1b).
PMID:11780129	FYPO:0002842	decreased protein localization to centromere outer repeat [has_severity] high [assayed_protein] PomBase:SPAC17H9.20	Psc3 localization was strikingly disrupted in the swi6∆ strain at both loci (Fig. 1b).
PMID:11780129	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	We consistently observed that psc3-4T and the other psc3 mutant alleles had no detectable effect on the silencing of a marker gene inserted at either centromeric (otr1R::ura4+) repeats or in the silent mating-type (Kint2::ura4+) region (see Supplementary Information).
PMID:11780129	FYPO:0002360	normal chromatin silencing at centromere	We consistently observed that psc3-4T and the other psc3 mutant alleles had no detectable effect on the silencing of a marker gene inserted at either centromeric (otr1R::ura4+) repeats or in the silent mating-type (Kint2::ura4+) region (see Supplementary Information).
PMID:11780129	FYPO:0001840	increased minichromosome loss during vegetative growth [has_penetrance] 0.6	psc3-1T also displays the lagging-chromosome phenotype and mis-segregated the mini-chromosome Ch16 (ref. 17) at a higher rate than the wild type, mimicking the swi6∆ phenotype (Fig. 2a, b).
PMID:11780129	FYPO:0001840	increased minichromosome loss during vegetative growth [has_penetrance] ~1	psc3-1T also displays the lagging-chromosome phenotype and mis-segregated the mini-chromosome Ch16 (ref. 17) at a higher rate than the wild type, mimicking the swi6∆ phenotype (Fig. 2a, b).
PMID:11780129	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] high [assayed_protein] PomBase:SPAC17H9.20	shown), and the association with otr and KR was much reduced (Fig. 1d).
PMID:11780129	FYPO:0000468	abnormal mating type switching [has_severity] high	we found that cohesin mutants (psc3-1T, psc3-2T, psc3-4T and rad21-K1) produced switching-defective colonies at a rate nearly 100-fold that of the wild type (Fig. 2a,b).
PMID:11780129	FYPO:0000468	abnormal mating type switching [has_severity] high	we found that cohesin mutants (psc3-1T, psc3-2T, psc3-4T and rad21-K1) produced switching-defective colonies at a rate nearly 100-fold that of the wild type (Fig. 2a,b).
PMID:11780129	FYPO:0000468	abnormal mating type switching [has_severity] high	we found that cohesin mutants (psc3-1T, psc3-2T, psc3-4T and rad21-K1) produced switching-defective colonies at a rate nearly 100-fold that of the wild type (Fig. 3a,b).
PMID:11780129	FYPO:0000468	abnormal mating type switching [has_severity] high	we found that cohesin mutants (psc3-1T, psc3-2T, psc3-4T and rad21-K1) produced switching-defective colonies at a rate nearly 100-fold that of the wild type (Fig. 3a,b).
PMID:11781565	FYPO:0005119	altered protein binding specificity [assayed_using] PomBase:SPAPB2B4.03 [assayed_using] PomBase:SPBC725.16	(Fig 4E)
PMID:11781565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAPB2B4.03 [has_penetrance] high	(Fig. 1B)
PMID:11781565	FYPO:0002975	decreased RNA level during cellular response to hydroxyurea [has_penetrance] high [assayed_using] PomBase:SPBC14C8.07c	(Fig. 1B)
PMID:11781565	FYPO:0001317	normal RNA level during vegetative growth [assayed_using] PomBase:SPAPB2B4.03 [has_penetrance] high	(Fig. 1B)
PMID:11781565	FYPO:0002975	decreased RNA level during cellular response to hydroxyurea [assayed_using] PomBase:SPAPB2B4.03 [has_penetrance] high	(Fig. 1B)
PMID:11781565	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC14C8.07c [has_severity] medium	(Fig. 1B)
PMID:11781565	FYPO:0002975	decreased RNA level during cellular response to hydroxyurea [assayed_using] PomBase:SPAPB2B4.03 [has_penetrance] high	(Fig. 1B)
PMID:11781565	FYPO:0004191	increased RNA level during cellular response to hydroxyurea [has_penetrance] high [assayed_using] PomBase:SPBC14C8.07c	(Fig. 1B)
PMID:11781565	FYPO:0001117	decreased RNA level during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC14C8.07c	(Fig. 1B)
PMID:11781565	FYPO:0000239	increased transcription from MCB promoter [assayed_using] PomBase:SPAPB2B4.03 [has_severity] medium	(Fig. 1C) 5 fold increase in HU compared to no HU. res1 and lacZ fusion on episomal plasmids
PMID:11781565	FYPO:0000239	increased transcription from MCB promoter [assayed_using] PomBase:SPAPB2B4.03 [has_severity] medium	(Fig. 1C) Shows 5 fold increase in presence of HU compared to no HU. res1 and lacZ fusion on episomal plasmids
PMID:11781565	FYPO:0002876	decreased transcription [assayed_using] PomBase:SPAPB2B4.03	(Fig. 1C) no increase in presence of HU compared to no HU when all MCB elements are removed. res1 and lacZ fusion on episomal plasmids
PMID:11781565	FYPO:0000780	increased transcription during vegetative growth [has_severity] medium [assayed_using] PomBase:SPBC428.18	(Fig. 2B)
PMID:11781565	FYPO:0006762	normal transcription during cellular response to hydroxyurea [assayed_using] PomBase:SPBC14C8.07c [has_severity] high	(Fig. 2B)
PMID:11781565	FYPO:0006676	decreased transcription during cellular response to hydroxyurea [assayed_using] PomBase:SPAPB2B4.03	(Fig. 2B)
PMID:11781565	FYPO:0000781	decreased transcription during vegetative growth [assayed_using] PomBase:SPAPB2B4.03	(Fig. 2B)
PMID:11781565	FYPO:0000780	increased transcription during vegetative growth [assayed_using] PomBase:SPBC14C8.07c [has_severity] high	(Fig. 2B)
PMID:11781565	FYPO:0006762	normal transcription during cellular response to hydroxyurea	(Fig. 2B)
PMID:11781565	GO:0005515	protein binding [part_of] regulation of mitotic cell cycle [part_of] transcription by RNA polymerase II	(Fig. 3A)
PMID:11781565	GO:0005515	protein binding [part_of] regulation of mitotic cell cycle [part_of] transcription by RNA polymerase II	(Fig. 3B)
PMID:11781565	GO:0005515	protein binding [part_of] regulation of mitotic cell cycle [part_of] transcription by RNA polymerase II	(Fig. 3B)
PMID:11781565	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC725.16	(Fig. 4D)
PMID:11781565	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC725.16	(Fig. 4D)
PMID:11781565	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC725.16	(Fig. 4D)
PMID:11781565	FYPO:0002061	inviable vegetative cell population	(Fig. 5) res1+ is unable to rescue the pat1-114 mutant at low levels of over expression
PMID:11781565	FYPO:0002060	viable vegetative cell population	(Fig. 5) res1-S130A can rescue the pat1-114 mutant at low levels of over expression
PMID:11781565	FYPO:0004988	abnormal RNA level oscillation during mitotic cell cycle [assayed_using] PomBase:SPBC14C8.07c	(Fig. 6)
PMID:11781565	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC428.18	(Fig. 7B) res1S130A prevents the normal down regulation of MBF dependent transcription by res1+
PMID:11781565	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC1F7.05	(Fig. 7B) res1S130A prevents the normal down regulation of MBF dependent transcription by res1+
PMID:11781565	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC14C8.07c	(Fig. 7B) res1S130A prevents the normal down regulation of MBF dependent transcription by res1+
PMID:11781565	FYPO:0000239	increased transcription from MCB promoter [assayed_using] PomBase:SPAPB2B4.03 [has_severity] high	Data not shown 20 fold increase in response to res1 oe. res1 and lacZ fusion on episomal plasmids
PMID:11781565	FYPO:0000239	increased transcription from MCB promoter [assayed_using] PomBase:SPAPB2B4.03	data not shown 8 fold increase in response to res1 oe. res1 and lacZ fusion on episomal plasmids
PMID:11792803	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC320.13c [present_during] mitotic M phase	(Fig. 6)
PMID:11792803	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC320.13c [present_during] mitotic M phase	(Fig. 6)
PMID:11792803	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC320.13c [present_during] mitotic M phase	(Fig. 6)
PMID:11792803	GO:1990023	mitotic spindle midzone [exists_during] mitotic anaphase A	(Fig. 8)
PMID:11792803	GO:0000776	kinetochore [exists_during] mitotic prophase	(Fig. 8)
PMID:11792803	GO:0000776	kinetochore [exists_during] mitotic metaphase	(Fig. 8)
PMID:11792803	FYPO:0003758	mitotic spindle elongation without chromosome separation	(Figure 2a) ( stretched chromaitn along elongating spindle at anaphase B)
PMID:11792803	FYPO:0005739	complete but unequal mitotic sister chromatid segregation with unseparated chromosomes	(Figure 2b)
PMID:11792803	FYPO:0005738	abolished histone H3-S10 phosphorylation during vegetative growth	(Figure 2b)
PMID:11792803	FYPO:0004255	inviable elongated mononucleate vegetative cell	(Figure 2b)
PMID:11792803	FYPO:0000276	monopolar mitotic spindle	(Figure 2b) chromsome detached from spindle
PMID:11818066	GO:0140311	protein sequestering activity [has_input] mei2/Phos(S438,T527) [part_of] negative regulation of cell cycle switching, mitotic to meiotic cell cycle	(comment: Rad24 sequesters phosphorylated Mei2, preventing Mei2 binding to meiRNA (sme2))
PMID:11818066	FYPO:0002060	viable vegetative cell population	(comment: does not undergo meiosis under conditions where pat1-114 single mutant does)
PMID:11818066	FYPO:0002052	normal sporulation frequency	(comment: not really sure freq is normal, because wt not shown, but text suggests it's close)
PMID:11839792	FYPO:0004719	abnormal mitotic cell cycle arrest with condensed chromosomes, septated cell [has_penetrance] 19	19% were septated, binucleated cells with condensed chromosomes. (comment: vw:2c binucleate? should this be WT knockdown?)
PMID:11839792	FYPO:0001784	excess endoplasmic reticulum membrane present [has_penetrance] 68	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	FYPO:0008140	dilated nuclear envelope lumen [has_penetrance] 56	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	FYPO:0008139	dilated endoplasmic reticulum lumen [has_penetrance] 68	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	FYPO:0008139	dilated endoplasmic reticulum lumen [has_penetrance] 50	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	FYPO:0008140	dilated nuclear envelope lumen [has_penetrance] 68	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	FYPO:0008140	dilated nuclear envelope lumen [has_penetrance] 50	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	FYPO:0001784	excess endoplasmic reticulum membrane present [has_penetrance] 50	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	FYPO:0008139	dilated endoplasmic reticulum lumen [has_penetrance] 56	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	FYPO:0001784	excess endoplasmic reticulum membrane present [has_penetrance] 56	56% of sar1-1, 68% of sec31-1, and 50% of pmm1-1 cells had accumulated ER membranes and dilated nuclear and ER lumens (Table 1).
PMID:11839792	FYPO:0003935	decreased protein localization to Golgi apparatus, with protein mislocalized to endoplasmic reticulum	In sar1-1 cells, acid phosphatase accumulated in its 72 kDa core glycosylated form (arrow) even at 25°C (Fig. 2A, lane 5), and this form increased in abundance upon incubation at 36°C (Fig. 2A, lanes 6-8), indicating a block in its secretion from the ER
PMID:11839792	FYPO:0002061	inviable vegetative cell population	None of the colonies or microcolonies was ura4-positive, providing further evidence that sec31 is an essential gene.
PMID:11839792	FYPO:0000516	normal nuclear import [assayed_using] PomBase:SPAC1783.07c	Pap1p was localized predominantly to the cytoplasm in wild-type cells (Fig. 5A) as well as in the sar1-1, sec31-1 and pmm1- 1 mutants grown at the restrictive temperature, suggesting that nuclear protein export was not adversely affected in these cells (Fig. 5C,E,G).
PMID:11839792	FYPO:0000509	normal nuclear export [assayed_using] PomBase:SPAC1783.07c	Pap1p was localized predominantly to the cytoplasm in wild-type cells (Fig. 5A) as well as in the sar1-1, sec31-1 and pmm1- 1 mutants grown at the restrictive temperature, suggesting that nuclear protein export was not adversely affected in these cells (Fig. 5C,E,G).
PMID:11839792	FYPO:0000509	normal nuclear export [assayed_using] PomBase:SPAC1783.07c	Pap1p was localized predominantly to the cytoplasm in wild-type cells (Fig. 5A) as well as in the sar1-1, sec31-1 and pmm1- 1 mutants grown at the restrictive temperature, suggesting that nuclear protein export was not adversely affected in these cells (Fig. 5C,E,G).
PMID:11839792	FYPO:0000516	normal nuclear import [assayed_using] PomBase:SPAC1783.07c	Pap1p was localized predominantly to the cytoplasm in wild-type cells (Fig. 5A) as well as in the sar1-1, sec31-1 and pmm1- 1 mutants grown at the restrictive temperature, suggesting that nuclear protein export was not adversely affected in these cells (Fig. 5C,E,G).
PMID:11839792	FYPO:0000516	normal nuclear import [assayed_using] PomBase:SPAC1783.07c	Pap1p was localized predominantly to the cytoplasm in wild-type cells (Fig. 5A) as well as in the sar1-1, sec31-1 and pmm1- 1 mutants grown at the restrictive temperature, suggesting that nuclear protein export was not adversely affected in these cells (Fig. 5C,E,G).
PMID:11839792	FYPO:0008138	normal nucleocytoplasmic transport [assayed_using] PomBase:SPAC1783.07c	Pap1p was localized predominantly to the cytoplasm in wild-type cells (Fig. 5A) as well as in the sar1-1, sec31-1 and pmm1- 1 mutants grown at the restrictive temperature, suggesting that nuclear protein export was not adversely affected in these cells (Fig. 5C,E,G).
PMID:11839792	FYPO:0003935	decreased protein localization to Golgi apparatus, with protein mislocalized to endoplasmic reticulum	The glycosylation profile of acid phosphatase in sec31-1 cells also revealed a block in secretion from the ER (Fig. 2B). In sec31-1 cells at 25°C (Fig. 2B, lane 3), a low level of the 72 kDa form of acid phosphatase (arrow) and high molecular weight smears indicated normal protein secretion. However, sec31-1 cells incubated at 36°C for 4 hours, accumulated a high level of the 72 kDa ER form of acid phosphatase (Fig. 2B, lane 4), indicating that protein secretion from the ER is inhibited
PMID:11839792	FYPO:0002061	inviable vegetative cell population	These data confirm that pmm1 is an essential gene
PMID:11839792	FYPO:0002280	inviable after spore germination, single cell division	These data confirm that pmm1 is an essential gene. Microscopic examination of the tetrad dissection plates revealed that, of 54 pmm1 null spores examined, 98% germinated. Of these, 52% formed single, rounded cells and 47% arrested as single, septated cells.
PMID:11839792	FYPO:0002061	inviable vegetative cell population	These data confirmed that sar1 is an essential gene in S. pombe, as previously reported (d’Enfert et al., 1992).
PMID:11839792	FYPO:0004719	abnormal mitotic cell cycle arrest with condensed chromosomes, septated cell [has_penetrance] 27	sar1, sec31 and pmm1 are essential genes (comment: vw:2c binucleate? should this be WT knockdown?)
PMID:11854402	GO:0000785	chromatin [exists_during] meiotic S phase	(comment: CHECK during premeiotic DNA replication)
PMID:11854402	GO:0000785	chromatin [exists_during] meiotic S phase	(comment: CHECK during premeiotic DNA replication)
PMID:11854402	GO:0000785	chromatin [exists_during] mitotic cell cycle G1 arrest in response to pheromone	(comment: CHECK during premeiotic DNA replication)
PMID:11854402	GO:0000785	chromatin [exists_during] mitotic G1 phase	(comment: CHECK during premeiotic DNA replication)
PMID:11854402	GO:0000785	chromatin [exists_during] meiotic S phase	(comment: CHECK during premeiotic DNA replication)
PMID:11854409	FYPO:0006556	inviable elongated tetranucleate triseptate vegetative cell, single septa between nuclei [has_penetrance] >40	(Fig. 1A) (comment: CHECK inviable)
PMID:11854409	FYPO:0003440	cell lysis during cytokinesis	(Fig. 2, 3)
PMID:11854409	FYPO:0006558	abolished septum disassembly	(Fig. 2, 3)
PMID:11854409	GO:0005515	protein binding	(Figure 5A)
PMID:11854409	GO:0005515	protein binding	(Figure 5B)
PMID:11854409	GO:0005515	protein binding	(Figure 5C)
PMID:11854409	GO:0005515	protein binding	(comment: UPR)
PMID:11854409	GO:0005515	protein binding	(comment: UPR)
PMID:11854409	GO:0005515	protein binding	(comment: UPR)
PMID:11856374	FYPO:0002061	inviable vegetative cell population	(comment: Loss of cia1+ led to a lethal phenotype)
PMID:11861551	GO:1990023	mitotic spindle midzone [exists_during] mitotic anaphase B	(Fig. 1)
PMID:11861551	GO:0000776	kinetochore [exists_during] mitotic metaphase	(Fig. 1a)
PMID:11861551	GO:0005634	nucleus	(Fig. 1a)
PMID:11861551	GO:1990385	meiotic spindle midzone [exists_during] meiotic anaphase II	(Fig. 3)
PMID:11861551	GO:1990385	meiotic spindle midzone [exists_during] meiotic anaphase I	(Fig. 3)
PMID:11861551	FYPO:0000131	abnormal mitotic spindle elongation	(Fig. 4)
PMID:11861551	FYPO:0004101	lagging mitotic chromosomes, with complete sister chromatid separation	(Fig. 4)
PMID:11861551	FYPO:0004101	lagging mitotic chromosomes, with complete sister chromatid separation	(Fig. 4)
PMID:11861551	FYPO:0003286	decreased mitotic chromosome condensation	(Fig. 4c)
PMID:11861551	FYPO:0008164	abnormal protein localization to kinetochore during mitotic M phase [assayed_protein] PomBase:SPCC320.13c	(Fig. 7)
PMID:11861551	FYPO:0000229	cut	(Fig. 7a)
PMID:11861551	FYPO:0002061	inviable vegetative cell population	(Fig. 7a)
PMID:11861551	GO:1990023	mitotic spindle midzone	(Figure 7)
PMID:11861551	GO:0000776	kinetochore	(Figure 7)
PMID:11861765	FYPO:0002060	viable vegetative cell population	(Fig. 1)
PMID:11861765	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 2)
PMID:11861765	FYPO:0005422	inviable elongated cell with fragmented nucleus and mitotic cell cycle arrest in interphase during cellular response to UV [has_severity] high	(Fig. 2A)
PMID:11861765	FYPO:0000095	sensitive to bleomycin [has_severity] medium	(Fig. 2B)
PMID:11861765	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 2B)
PMID:11861765	FYPO:0002578	resistance to hydroxyurea	(Fig. 2B)
PMID:11861765	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 3A)
PMID:11861765	FYPO:0002061	inviable vegetative cell population	(Fig. 3B)
PMID:11861765	FYPO:0004507	abolished centromeric DNA separation	(Fig. 3C)
PMID:11861765	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 25	(Fig. 3C)
PMID:11861765	FYPO:0003165	cut with abnormal chromosome segregation	(Fig. 3C)
PMID:11861765	FYPO:0001513	normal mitotic sister chromatid segregation	(Fig. 3C)
PMID:11861765	FYPO:0001779	abnormal centromere clustering at nuclear periphery during vegetative growth	(Fig. 3D)
PMID:11861765	FYPO:0001779	abnormal centromere clustering at nuclear periphery during vegetative growth	(Fig. 3D)
PMID:11861765	FYPO:0001861	increased minichromosome loss upon segregation during vegetative growth [has_severity] high	(Fig. 4A)
PMID:11861765	FYPO:0003241	unequal mitotic sister chromatid segregation	(Fig. 4B)
PMID:11861765	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 30	(Fig. 4B,C)
PMID:11861765	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 5	(Fig. 4B,C)
PMID:11861765	FYPO:0001234	slow vegetative cell population growth	(Fig. 4D)
PMID:11861765	FYPO:0000141	abnormal mitotic sister chromatid segregation	(Fig. 4D)
PMID:11861765	FYPO:0000925	unequal meiotic chromosome segregation	(Fig. 5A)
PMID:11861765	FYPO:0000581	decreased spore germination frequency	(Fig. 5B)
PMID:11861765	FYPO:0004056	decreased protein localization to nucleus, with protein mislocalized to cytoplasm [assayed_using] PomBase:SPAC110.02	(Fig. 7B)
PMID:11861765	FYPO:0000838	normal protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Fig. 7C)
PMID:11861765	FYPO:0002379	inviable after spore germination, without cell division, with elongated germ tube [has_penetrance] complete	(Fig. 8A)
PMID:11861765	FYPO:0002061	inviable vegetative cell population	(Fig. 8B)
PMID:11861765	FYPO:0001234	slow vegetative cell population growth	(Fig. 8B)
PMID:11861765	FYPO:0000141	abnormal mitotic sister chromatid segregation	(Fig. 8C)
PMID:11861765	FYPO:0000839	inviable elongated mononucleate aseptate cell	(Fig. 8C)
PMID:11861905	PomGeneEx:0000012	RNA level decreased [during] cellular response to glucose starvation	(Figure 1a)
PMID:11861905	PomGeneEx:0000011	RNA level increased [in_presence_of] glucose	(Figure 1a)
PMID:11861905	FYPO:0007627	decreased RNA catabolic process during glucose starvation	The 210-nt region resides downstream of the distal poly(A) site and it is not included in the mature rrg1+ mRNA, in contrast to other regulatory elements for post-transcriptional control. However, some recent studies on S.pombe have shown that RNA pol II transcription proceeds beyond the poly(A) site and that the downstream sequences located in the 3′ noncoding region are responsible for transcription termination and mRNA 3′-end formation, which are closely coupled to efficient gene expression
PMID:11870212	GO:0072686	mitotic spindle [exists_during] mitotic anaphase B	(Fig. 3B)
PMID:11870212	GO:0000776	kinetochore [exists_during] mitotic metaphase	(Fig. 3B)
PMID:11870212	GO:0000776	kinetochore [exists_during] mitotic anaphase A	(Fig. 3B)
PMID:11870212	GO:0072686	mitotic spindle [exists_during] mitotic anaphase B	(Fig. 3B)
PMID:11870212	GO:0000776	kinetochore [exists_during] mitotic metaphase	(Fig. 3B)
PMID:11870212	GO:0000776	kinetochore [exists_during] mitotic anaphase A	(Fig. 3B)
PMID:11870212	FYPO:0000141	abnormal mitotic sister chromatid segregation	(comment: movement in anap[hase A)
PMID:11882285	FYPO:0003307	increased mitotic index	(Fig. 1)
PMID:11882285	FYPO:0000639	delayed onset of septum assembly	(Fig. 1)
PMID:11882285	FYPO:0000274	increased duration of mitotic M phase	(Fig. 1)
PMID:11882285	FYPO:0004307	long mitotic spindle during metaphase [has_severity] low	(Fig. 1) (3-4um normal metaphese lenght 2-2.5 um
PMID:11882285	FYPO:0002797	decreased protein degradation [assayed_using] PomBase:SPBC14C8.01c [has_severity] high [has_penetrance] high	(Fig. 1C)
PMID:11882285	FYPO:0000091	sensitive to thiabendazole	(Fig. 2D)
PMID:11882285	FYPO:0000091	sensitive to thiabendazole	(Fig. 2D)
PMID:11882285	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] high	(Fig. 4)
PMID:11882285	FYPO:0000337	abnormal mitosis [has_penetrance] 43	(Fig. 5a)
PMID:11882285	FYPO:0005779	normal protein localization to kinetochore during mitosis [assayed_using] PomBase:SPCC1322.12c [has_penetrance] ~1-2	(Fig. 5a) (comment: ie wt like)
PMID:11882285	FYPO:0004308	abnormal CENP-A containing chromatin organization [assayed_using] regional_centromere_central_core	(Fig. S1)
PMID:11882285	FYPO:0004308	abnormal CENP-A containing chromatin organization [assayed_using] regional_centromere_central_core	(Fig. S1)
PMID:11882285	FYPO:0004308	abnormal CENP-A containing chromatin organization [assayed_using] regional_centromere_central_core	(Fig. S1)
PMID:11882285	FYPO:0001532	normal duration of mitotic S phase	(Fig. S1)
PMID:11882285	FYPO:0004308	abnormal CENP-A containing chromatin organization [assayed_using] regional_centromere_central_core	(Fig. S1)
PMID:11882285	GO:0000776	kinetochore [exists_during] mitotic prophase	(Figure 3)
PMID:11884512	FYPO:0001253	elongated multinucleate multiseptate vegetative cell, single septa between nuclei	(Fig. 3B)
PMID:11884512	FYPO:0000268	sensitive to UV during vegetative growth	(Figure 3C)
PMID:11884512	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: same as rad17 single mutant, epistatic)
PMID:11884512	GO:0016929	deSUMOylase activity [has_input] PomBase:SPBC365.06	NEM, which inhibit the Pmt3-processing activity of Ulp1, and the serine protease inhibitor PMSF, have no effect on Pmt3 deconjugating activity
PMID:11884512	GO:0070139	SUMO-specific endopeptidase activity [has_input] PomBase:SPBC365.06 [part_of] protein processing	Of the inhibitors we tested, only iodoacetamide (10 mM) and NEM (10 mM) inhibited Ulp1 activity
PMID:11884512	FYPO:0001234	slow vegetative cell population growth [has_severity] high	data not shown
PMID:11884512	FYPO:0000097	sensitive to caffeine during vegetative growth	data not shown
PMID:11884604	GO:0000785	chromatin	(comment: CHECK not (coincident_with(SO:0001789) | coincident_with(SO:0001795)))
PMID:11884604	GO:0031078	histone H3K14 deacetylase activity, hydrolytic mechanism [has_input] PomBase:SPBC8D2.04	(comment: actually inferred from combination of phenotype and sequence similarity)
PMID:11884604	GO:0031078	histone H3K14 deacetylase activity, hydrolytic mechanism [has_input] PomBase:SPAC1834.04	(comment: actually inferred from combination of phenotype and sequence similarity)
PMID:11884604	GO:0004407	histone deacetylase activity	(comment: actually inferred from combination of phenotype and sequence similarity)
PMID:11884604	GO:0031078	histone H3K14 deacetylase activity, hydrolytic mechanism [has_input] PomBase:SPBC1105.11c	(comment: actually inferred from combination of phenotype and sequence similarity)
PMID:11884604	GO:0032129	histone H3K9 deacetylase activity, hydrolytic mechanism [has_input] PomBase:SPBC1105.11c	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	GO:0031078	histone H3K14 deacetylase activity, hydrolytic mechanism [has_input] PomBase:SPAC1834.04	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	GO:0031078	histone H3K14 deacetylase activity, hydrolytic mechanism [has_input] PomBase:SPBC8D2.04	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	GO:0031078	histone H3K14 deacetylase activity, hydrolytic mechanism [has_input] PomBase:SPBC1105.11c	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	GO:0032129	histone H3K9 deacetylase activity, hydrolytic mechanism [has_input] PomBase:SPAC1834.04	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	GO:0034739	histone H4K16 deacetylase activity, hydrolytic mechanism [has_input] PomBase:SPBC1105.11c	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	GO:0034739	histone H4K16 deacetylase activity, hydrolytic mechanism [has_input] PomBase:SPBC8D2.04	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	GO:0034739	histone H4K16 deacetylase activity, hydrolytic mechanism [has_input] PomBase:SPAC1834.04	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	GO:0032129	histone H3K9 deacetylase activity, hydrolytic mechanism [has_input] PomBase:SPBC8D2.04	(comment: broad specificity;) actually inferred from combination of phenotype and sequence similarity
PMID:11884604	FYPO:0000331	decreased histone acetylation during vegetative growth [has_severity] low	(comment: not much evidence of specificity for H3 vs. H4 or position)
PMID:11886869	GO:0140209	zinc ion import into endoplasmic reticulum	(comment: storage)
PMID:11886869	FYPO:0000763	resistance to cadmium	In contrast to that, the zhf disruption was found to significantly protect cells from toxicity of Cd2+ ions, the third known substrate of CDF proteins. At the IC50 concentration for wild-type cells of 100 μM, Δzhf cells were inhibited by only 4% (±3%) (Fig. 1D).
PMID:11886869	FYPO:0000116	sensitive to zinc [has_severity] high	In the presence of elevated Zn2+ levels, however, they were severely growth-inhibited (Fig. 1, A and B).
PMID:11886869	FYPO:0001245	sensitive to cobalt	Similarly, the absence of a functional Zhf protein rendered the S. pombe cells Co2+-hypersensitive (Fig. 1C). At 1 mM Co2+ in EMM, wild-type cells showed 94% (±11%) of the optical density of untreated control cells, whereas Δzhf cells reached only 36% (±3.5%).
PMID:11886869	FYPO:0000763	resistance to cadmium [has_severity] high	To determine whether the main pathway for Cd2+ detoxification in S. pombe, the formation of phytochelatins, is required for the Δzhf-dependent protection, the zhf gene was disrupted in the Δpcs strain Sp27 (20). Toxicity assays showed that the protective effect was even more pronounced in this genetic background.
PMID:11886869	FYPO:0002588	resistance to nickel	a pronounced protective effect of the Zhf inactivation could be detected also for Ni2+
PMID:11886869	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Δzhf strain were viable and showed only a minor reduction in growth rate under control conditions without any added heavy metal salts.
PMID:11895484	FYPO:0008244	abolished protein localization to prospore wall [assayed_protein] PomBase:SPAC24C9.07c	As visualized by the goldparticles, 1,3-β-glucan was found at the inner layer ofthe spore wall in the wild-type ascospores but in meu10∆ascospores it was scattered throughout the spore wall(Fig. 7A).Thus, Meu10 is required for the accurate local-ization of 1,3-β-glucan in the spore wall
PMID:11895484	GO:0005619	ascospore wall	At meiosis II, however, Meu10-GFP appearedthroughout the cytoplasm and displayed a homogene-ous subcellular distribution (Fig. 6Aiv). As sporulationcommenced and progressed, the Meu10-GFP proteingradually moved to the peripheral region of the spores(Fig. 6Av), finally being distributed as a ring around eachof the four spores (Fig. 6Avi). Following sporulation, theGFP signal relocalized into the cytoplasm, where it wasfound as punctuated granules (Fig. 6Avii).
PMID:11895484	FYPO:0002150	inviable spore population	In this mutant, all the spores wereunviable and only faint signals from Meu10-C120∆-GFP were detected. (Fig. 8B, Cii)
PMID:11895484	FYPO:0002150	inviable spore population	Like the meu10∆ mutant, the spores from this mutantwere not viable (Fig. 8B)
PMID:11895484	FYPO:0000196	abnormal prospore formation	Like the meu10∆mutant (Fig. 3C), mature ascospores were not generatedby this mutant.
PMID:11895484	FYPO:0008244	abolished protein localization to prospore wall [assayed_protein] PomBase:SPCC1223.12c	Moreover, Meu10-N117∆-GFP signals in the abnormally shaped ascospores werenot detected (Fig. 8Ciii), indicating that this domain isessential for the spore wall localization of Meu10
PMID:11895484	FYPO:0004925	irregular ascospore wall	Moreover, the thickness of the walls of the meu10∆spores was not homogeneous. In some parts, the sporewall was approximately threefold thicker than wild-type spore walls and seemed to be composed of sparsematerial, whereas in other parts, they were abnormallythin and looked very weak. The enlarged image of anabnormal ascospore shows a scattered stripe structureacross the spore wall (Fig. 5C) that is not observed in thewall of wild-type ascospores. The abnormal spore wallseems fragile, as some of them appear to be broken,allowing the cytoplasmic material to leak out. In addi-tion, at the later time point (22 h), most of the ascosporewalls disappeared. This fragility of the ascospore walls islikely to be why the meu10∆ spore nuclei are stainingabnormally with Hoechst33342 (as seen in Fig. 4A).
PMID:11895484	FYPO:0000583	abolished sporulation	No mature ascospores were observed in the meu10∆mutant (Fig. 3C and see Fig. 4A).
PMID:11895484	FYPO:0002150	inviable spore population	No mature ascospores were observed in the meu10∆mutant (Fig. 3C and see Fig. 4A).
PMID:11895484	FYPO:0000196	abnormal prospore formation	No mature ascospores were observed in the meu10∆mutant (Fig. 3C and see Fig. 4A).
PMID:11895484	FYPO:0006976	normal RNA level during meiotic cell cycle [assayed_transcript] PomBase:SPCC1223.12c	Northern blot analysis on RNA from these cells usingmeu10 + cDNA as a probe revealed that meu10+ was tran-scribed during meiosis, even in mei4-null mutant cells(Fig. 1D).
PMID:11895484	FYPO:0002060	viable vegetative cell population	Thus,the meu10+ gene is not essential for vegetative growth.
PMID:11895484	FYPO:0002043	normal premeiotic DNA replication	We next measured the DNA content of the meu10∆ and wild-type cells after nitrogenstarvation by flow cytometry. No apparent differencewas observed (data not shown), which indicates thatMeu10 is not required for pre-meiotic DNA synthesis.No mature ascospores were observed in the meu10∆mutant (Fig. 3C and see Fig. 4A).
PMID:11895484	FYPO:0003835	normal horsetail movement	ell and nucleishapes in meu10∆ cells during the horse-tail, meiosisI and meiosis II stages were normal (data not shownand uppermost panel at 8 h in Fig. 4A)
PMID:11907273	FYPO:0000172	abnormal meiotic telomere clustering	(comment: using chromosome III)
PMID:11909965	FYPO:0000069	resistance to thiabendazole	(Fig. 2A)
PMID:11909965	FYPO:0003165	cut [has_penetrance] 45	(Fig. 2B)
PMID:11909965	FYPO:0001491	viable vegetative cell [has_penetrance] >95	(Fig. 2B)
PMID:11909965	FYPO:0001491	viable vegetative cell [has_penetrance] >95	(Fig. 2B)
PMID:11909965	FYPO:0001489	inviable vegetative cell [has_penetrance] 45	(Fig. 2B)
PMID:11909965	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Figure 2C)
PMID:11909965	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Figure 2C)
PMID:11909965	FYPO:0000168	abnormal mitotic spindle assembly checkpoint [has_penetrance] 8	(Figure 3a) (comment: CHECK DECREASED cell cycle arrest in mitotic anaphase)
PMID:11909965	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Figure 3a) (comment: CHECK cell cycle arrest in mitotic metaphase)
PMID:11909965	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Figure 3a) (comment: CHECK cell cycle arrest in mitotic metaphase)
PMID:11909965	GO:0000776	kinetochore [exists_during] mitotic metaphase	(Figure 5A)
PMID:11927555	FYPO:0000338	abnormal mitotic spindle	(Fig. 6)
PMID:11927555	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 6)
PMID:11927555	FYPO:0003738	abnormal mitotic cell cycle arrest with condensed chromosomes	(Fig. 6)
PMID:11927555	FYPO:0001489	inviable vegetative cell	(Fig. 6)
PMID:11927555	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	(Fig. 6) resulted in a synthetic arrest at metaphase of mitosis. This contrasts with the G1 cell cycle arrest of pim1-d1 single mutant cells (Krien et al., 1998).
PMID:11927555	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	(Figure 5)
PMID:11927555	GO:0044732	mitotic spindle pole body [exists_during] mitotic G2 phase	(Figure 5)
PMID:11927555	GO:0044732	mitotic spindle pole body [exists_during] mitotic G1 phase	(Figure 5)
PMID:11927555	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Figure 6)
PMID:11927555	FYPO:0000276	monopolar mitotic spindle	(Figure 6)
PMID:11927555	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Figure 6)
PMID:11927555	FYPO:0000276	monopolar mitotic spindle [has_penetrance] 100	(Figure 6) which was enhanced by the presence of the pim1-d1 mutation at 36°C to include all mitotic cells (arrowed
PMID:11927555	GO:0006998	nuclear envelope organization	(comment: suggesting the lethal synthetic interaction between ®n1D and cut11 might relate of the nuclear envelope rather than SPB anchoring during mitosis)
PMID:11927555	FYPO:0002061	inviable vegetative cell population	Double mutants between ®n1D and the temperature-sensitive allele rad21-K1 (Tatebayashi et al., 1998) were synthetically lethal at all temperatures
PMID:11927555	FYPO:0000141	abnormal mitotic sister chromatid segregation	The double ®n1Dbub1D mutants were viable, though substantially retarded in colony formation and showed extensive chromosome segregation defects (Figure 7A).
PMID:11927555	FYPO:0006821	slow vegetative cell growth	The double ®n1Dbub1D mutants were viable, though substantially retarded in colony formation and showed extensive chromosome segregation defects (Figure 7A).
PMID:11927555	FYPO:0007566	premature mitotic chromosome condensation	These data show that Fin1p- mediated compaction of the chromosomes is not functionally related to mitotic chromosome condensation and the mechanism by which it occurs remains obscure.
PMID:11927555	FYPO:0007566	premature mitotic chromosome condensation	These data show that Fin1p- mediated compaction of the chromosomes is not functionally related to mitotic chromosome condensation and the mechanism by which it occurs remains obscure.
PMID:11927555	FYPO:0007566	premature mitotic chromosome condensation	These data show that Fin1p- mediated compaction of the chromosomes is not functionally related to mitotic chromosome condensation and the mechanism by which it occurs remains obscure.
PMID:11927555	FYPO:0007566	premature mitotic chromosome condensation	These data show that Fin1p- mediated compaction of the chromosomes is not functionally related to mitotic chromosome condensation and the mechanism by which it occurs remains obscure.
PMID:11927555	FYPO:0002969	increased protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC649.05	during interphase (in. non mitotic cells)
PMID:11950879	GO:0000776	kinetochore [exists_during] mitotic prophase	(comment: vw: nda3 tubulin mutant does not assemble spindle and shows Mad2 is localized to unattached kinetochores)
PMID:11950879	FYPO:0003570	normal attachment of spindle microtubules to kinetochore	...majority of the Mad2-GFP was localized to the spindle
PMID:11950879	FYPO:0003570	normal attachment of spindle microtubules to kinetochore	...majority of the Mad2-GFP was localized to the spindle
PMID:11950879	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	...majority of the Mad2-GFP was localized to the spindle
PMID:11950884	FYPO:0001115	normal cellular response to P-factor [has_penetrance] high	(Fig. 1)
PMID:11950884	FYPO:0006573	normal protein level during cellular response to pheromone [has_penetrance] high [assayed_using] PomBase:SPBC1604.20c	(Fig. 2A)
PMID:11950884	FYPO:0006573	normal protein level during cellular response to pheromone [has_penetrance] high [assayed_using] PomBase:SPAC3C7.12	(Fig. 2A)
PMID:11950884	FYPO:0006573	normal protein level during cellular response to pheromone [has_penetrance] high [assayed_using] PomBase:SPCC1223.06	(Fig. 2A)
PMID:11950884	GO:0005881	cytoplasmic microtubule [exists_during] mitotic G2 phase	(Fig. 4F) location also exists during mating
PMID:11950884	FYPO:0007810	normal cytoplasmic microtubules during cellular response to pheromone	(Fig. 5 Table 3,4)
PMID:11950884	FYPO:0007810	normal cytoplasmic microtubules during cellular response to pheromone	(Fig. 5 Table 4)
PMID:11950884	FYPO:0007810	normal cytoplasmic microtubules during cellular response to pheromone	(Fig. 5, Table 3,4)
PMID:11950884	FYPO:0006501	premature actin fusion focus assembly [has_penetrance] high	(Fig. 6A)
PMID:11950884	FYPO:0006501	premature actin fusion focus assembly [has_penetrance] high	(Fig. 6A)
PMID:11950884	FYPO:0006501	premature actin fusion focus assembly [has_penetrance] high	(Fig. 6A)
PMID:11950884	FYPO:0007563	cell cycle arrest in mitotic G1 phase in response to pheromone without starvation	(Fig. 6B)
PMID:11950884	FYPO:0007563	cell cycle arrest in mitotic G1 phase in response to pheromone without starvation	(Fig. 6B)
PMID:11950884	FYPO:0007563	cell cycle arrest in mitotic G1 phase in response to pheromone without starvation	(Fig. 6B) All three mutants were able to detect and respond to pheromone by arresting in G1, as shown by FACS analysis (Fig. 6B)
PMID:11950884	FYPO:0000761	increased conjugation frequency	(Fig. 6C)
PMID:11950884	FYPO:0000761	increased conjugation frequency	(Fig. 6C)
PMID:11950884	FYPO:0003797	normal conjugation frequency [has_penetrance] medium	(Fig. 6C)
PMID:11950884	FYPO:0006772	dispersed actin cortical patch localization during mating	(Fig. 8D,E) pom1 has a role in the relocalisation of actin to the shmooing cell tip
PMID:11950884	GO:0005881	cytoplasmic microtubule [exists_during] mitotic G2 phase	location is abolished during mating Fig4Dc and Fig4Ec
PMID:11950927	FYPO:0000134	branched, elongated, multiseptate cell	(Fig. 3c)
PMID:11950927	FYPO:0001513	normal mitotic sister chromatid segregation	(Fig. 3c)
PMID:11950927	FYPO:0001357	normal vegetative cell population growth	(Fig. 4)
PMID:11950927	FYPO:0003165	cut with abnormal chromosome segregation	(Figure 1C)
PMID:11950927	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC962.02c	(Figure 2)
PMID:11950927	FYPO:0001234	slow vegetative cell population growth	(Figure 6A)
PMID:11950927	FYPO:0000134	branched, elongated, multiseptate cell	(Figure 6A)
PMID:11950927	FYPO:0001575	abolished vegetative cell population growth	(comment: dominent negative effect)
PMID:11950927	FYPO:0001575	abolished vegetative cell population growth	(comment: dominent negative effect)
PMID:11950927	FYPO:0001575	abolished vegetative cell population growth	(comment: dominent negative effect)
PMID:11950927	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC320.13c [assayed_using] PomBase:SPBC336.15	Pic1-765-924, which lacks the IN box, failed to bind Ark1p
PMID:11950932	FYPO:0000941	abolished protein localization to mitotic spindle pole body [has_penetrance] low [assayed_protein] PomBase:SPAC1565.06c	At 36°C, Spg1p-GFP was detected at SPBs in wild-type cells but was absent from SPBs in the cdc11 mutant strains (Figure 4B).
PMID:11950932	FYPO:0000941	abolished protein localization to mitotic spindle pole body [has_penetrance] low [assayed_protein] PomBase:SPAC1565.06c	At 36°C, Spg1p-GFP was detected at SPBs in wild-type cells but was absent from SPBs in the cdc11 mutant strains (Figure 4B).
PMID:11950932	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC1739.11c	GFP- Cdc11p(1- 630) was distributed throughout the cytoplasm (our unpublished results), but GFP-Cdc11p(631-1045) localized to SPBs (Figure 5A).
PMID:11950932	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC1739.11c	GFP- Cdc11p(1- 630) was distributed throughout the cytoplasm (our unpublished results), but GFP-Cdc11p(631-1045) localized to SPBs (Figure 5A).
PMID:11950932	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC1739.11c	However, its localization to the SPB was lost in the sid4-SA1 mutant at restrictive temperature (Figure 3).
PMID:11950932	FYPO:0007569	abnormal septation initiation network signaling	Interestingly, we found that overproduction of GFP-Cdc11p(631-1045) gener-ated a sid phenotype (Figure 5A).
PMID:11950932	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC1565.06c	Overproduction of Cdc11p(631-1045) had no effect on the localization of Sid4p-GFP but caused the loss of Cdc11p-GFP and Spg1p-GFP from SPBs (Figure 5B).
PMID:11950932	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC244.01c	Overproduction of Cdc11p(631-1045) had no effect on the localization of Sid4p-GFP but caused the loss of Cdc11p-GFP and Spg1p-GFP from SPBs (Figure 5B). This is consistent with the with the idea that Cdc11p(631-1045) saturates the SPB binding site for Cdc11p, thus eliminating the opportunity for the full-length protein to localize to the SPB.
PMID:11950932	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC1739.11c	The CAA20785 GFP fusion protein localized normally in cdc16-116, spg1-106, cdc7-24, and sid2-250 temperature-sensitive mutants...(Figure 3)
PMID:11950932	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC1739.11c	The CAA20785 GFP fusion protein localized normally in cdc16-116, spg1-106, cdc7-24, and sid2-250 temperature-sensitive mutants...(Figure 3)
PMID:11950932	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC1739.11c	The CAA20785 GFP fusion protein localized normally in cdc16-116, spg1-106, cdc7-24, and sid2-250 temperature-sensitive mutants...(Figure 3)
PMID:11950932	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC1739.11c	The CAA20785 GFP fusion protein localized normally in cdc16-116, spg1-106, cdc7-24, and sid2-250 temperature-sensitive mutants...(Figure 3)
PMID:11950932	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	The single and merged images indicate that CAA20785 colocalizes with Sid4p to SPBs throughout the cell cycle (Figure 2B).
PMID:11950932	GO:0044732	mitotic spindle pole body [exists_during] mitotic interphase	The single and merged images indicate that CAA20785 colocalizes with Sid4p to SPBs throughout the cell cycle (Figure 2B).
PMID:11952833	FYPO:0001876	decreased asymmetric protein localization, with protein localized to both mitotic spindle pole bodies during anaphase [assayed_using] PomBase:SPBC21.06c	(comment: even though cdc13 is present)
PMID:11952833	FYPO:0001876	decreased asymmetric protein localization, with protein localized to both mitotic spindle pole bodies during anaphase [assayed_using] PomBase:SPAC9G1.09	(comment: even though cdc13 is present)
PMID:11952833	FYPO:0004537	mitotic spindle assembly checkpoint override	(comment: premature SIN)
PMID:11955632	FYPO:0003655	abolished tRNA splicing	(comment: CHECK tRNA)
PMID:11967147	FYPO:0000274	increased duration of mitotic M phase	(Fig. 1A)
PMID:11967147	FYPO:0004863	long curved microtubules [has_penetrance] 20	(Fig. 1A)
PMID:11967147	FYPO:0004863	long curved microtubules [has_penetrance] 20	(Fig. 1A)
PMID:11967147	FYPO:0000274	increased duration of mitotic M phase	(Fig. 1A)
PMID:11967147	FYPO:0001840	increased minichromosome loss during vegetative growth	(Fig. 1C)
PMID:11967147	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 10-20	(Fig. 1D)
PMID:11967147	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 10-20	(Fig. 1D)
PMID:11967147	GO:0072686	mitotic spindle [exists_during] mitotic prophase [exists_during] mitotic metaphase	(Fig. 2a)
PMID:11967147	GO:0072686	mitotic spindle [exists_during] mitotic prophase [exists_during] mitotic metaphase	(Fig. 2a)
PMID:11967147	GO:0055028	cortical microtubule [exists_during] mitotic interphase	(Fig. 2b)
PMID:11967147	GO:0055028	cortical microtubule [exists_during] mitotic interphase	(Fig. 2b)
PMID:11967147	GO:1990023	mitotic spindle midzone [exists_during] mitotic anaphase	(Fig. 2d)
PMID:11967147	GO:1990023	mitotic spindle midzone [exists_during] mitotic anaphase	(Fig. 2d)
PMID:11967147	FYPO:0002061	inviable vegetative cell population	(Fig. 5A)
PMID:11967147	FYPO:0002061	inviable vegetative cell population	(Fig. 5A)
PMID:11967147	FYPO:0002061	inviable vegetative cell population	(Fig. 5A)
PMID:11967147	FYPO:0003969	mislocalized mitotic spindle	(Figure 5B)
PMID:11967147	FYPO:0000670	abnormal mitotic sister chromatid separation	(Figure 5B)
PMID:11967147	FYPO:0000670	abnormal mitotic sister chromatid separation	(Figure 5B)
PMID:11967147	FYPO:0000141	abnormal mitotic sister chromatid segregation	(Figure 5B)
PMID:11967147	FYPO:0003969	mislocalized mitotic spindle	(Figure 5B)
PMID:11967147	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Figure 5D)
PMID:11967147	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Figure 5D)
PMID:11967147	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B	(Figure 5D)
PMID:11967147	FYPO:0006171	mitotic spindle elongation during anaphase A	(Figure 5D) (comment: abolished pausing)
PMID:11967147	FYPO:0002060	viable vegetative cell population	(Figure S1)
PMID:11967147	FYPO:0001492	viable elongated vegetative cell [has_severity] medium	(Figure S1)
PMID:11967147	FYPO:0002060	viable vegetative cell population	(Figure S1)
PMID:11967147	FYPO:0002060	viable vegetative cell population	(Figure S1) (comment: CHECK 20% longer)
PMID:11967147	FYPO:0002060	viable vegetative cell population	(Figure S1) (comment: CHECK 20% longer)
PMID:11967147	FYPO:0002060	viable vegetative cell population	(Figure S1) (comment: CHECK 20% longer)
PMID:11967147	FYPO:0001840	increased minichromosome loss during vegetative growth	(comment: DNS)
PMID:11967147	FYPO:0001840	increased minichromosome loss during vegetative growth	(comment: DNs)
PMID:11972332	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC5E4.03c [assayed_protein] PomBase:SPCC16C4.18c	(Figure 1A)
PMID:12000964	FYPO:0000611	abnormal cell cycle arrest in mitotic S phase	(comment: vw: DNA checkpoint dept)
PMID:12000964	FYPO:0003438	mitotic G1/S phase transition delay following nitrogen starvation-induced G1 phase arrest	(comment: vw: I added this as an inference, because the checkpoint is never satisfied)
PMID:12000964	FYPO:0003545	increased duration of mitotic cell cycle DNA replication checkpoint	(comment: vw: I added this as an inference, because the checkpoint is never satisfied)
PMID:12000964	FYPO:0004588	abnormal mitosis following normal mitosis	(comment: vw: delayed)
PMID:12006645	FYPO:0002059	inviable cell population	(comment: tetrads only)
PMID:12007420	FYPO:0003532	increased monopolar index [has_severity] high	Fig. 1
PMID:12007420	FYPO:0003150	decreased NETO	Fig. 1B
PMID:12007420	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] high	Fig. 1C
PMID:12007420	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] high	Fig. 1C
PMID:12007420	FYPO:0001018	abolished NETO [has_penetrance] high	Fig. 1D
PMID:12007420	FYPO:0001018	abolished NETO [has_penetrance] high	Fig. 1D
PMID:12007420	FYPO:0001585	abolished protein localization to cell tip during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPAC6G10.02c	Fig. 2A
PMID:12007420	FYPO:0001375	abolished protein localization [assayed_using] PomBase:SPAC6G10.02c	Fig. 2D (comment: no tea3GFP staining cell middle in nda3 block)
PMID:12007420	FYPO:0003414	normal protein localization to septum [assayed_using] PomBase:SPAC6G10.02c	Fig. 2D (comment: tea3GFP staining cell middle after nda3 block and release)
PMID:12007420	FYPO:0002061	inviable vegetative cell population	Fig. 3B
PMID:12007420	FYPO:0002060	viable vegetative cell population	Fig. 3B
PMID:12007420	FYPO:0002060	viable vegetative cell population	Fig. 3B
PMID:12007420	FYPO:0001406	increased septum thickness	Fig. 3B
PMID:12007420	FYPO:0002452	inviable septated vegetative cell with abnormal cell morphology	Fig. 3B
PMID:12007420	FYPO:0002060	viable vegetative cell population	Fig. 3B
PMID:12007420	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC6G10.02c	Fig. 3C
PMID:12007420	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPAC2F7.03c [has_penetrance] high	Fig. 3D
PMID:12007420	FYPO:0006636	mislocalized protein distributed in cell cortex [assayed_using] PomBase:SPAC6G10.02c [has_penetrance] high	Fig. 4A
PMID:12007420	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPCC1223.06	Fig. 4B
PMID:12007420	FYPO:0006636	mislocalized protein distributed in cell cortex [assayed_using] PomBase:SPAC6G10.02c [has_penetrance] high	Fig. 4C
PMID:12007420	FYPO:0001492	viable elongated vegetative cell [has_penetrance] high	Fig. 4D (comment: tea3 does not affect polarity and the elongated cells do not branch. This is different to pom1 where cdc11-119 cells form branches)
PMID:12019258	FYPO:0005433	decreased meiotic recombination at hotspot	(comment: assayed using 160-bp palindromic sequence inserted into ade6 locus)
PMID:12023299	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC342.05	(comment: CHECK mah: residue=T215)
PMID:12023299	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(comment: mah: assayed substrate: exogenous histone H1)
PMID:12023299	GO:0000724	double-strand break repair via homologous recombination	(comment: mah: localization to DSB sites also contributes to inference)
PMID:12023299	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: mah: same as rad51delta alone)
PMID:12023299	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] high	(comment: mah: same as rad51delta alone)
PMID:12023299	FYPO:0005388	decreased number of Rad51 foci during cellular response to ionizing radiation [has_severity] high	(comment: mah: same as rad51delta alone)
PMID:12023299	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] high	(comment: mah: same as rad51delta alone)
PMID:12023299	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] high	(comment: mah: same as rad51delta alone)
PMID:12023299	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: mah: same as rad51delta alone)
PMID:12023299	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] high	(comment: mah: same as rad51delta alone)
PMID:12023299	FYPO:0005388	decreased number of Rad51 foci during cellular response to ionizing radiation [has_severity] high	(comment: mah: same as rad51delta alone)
PMID:12023299	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] medium	(comment: mah: same as rqh1delta alone)
PMID:12023299	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] medium	(comment: mah: sensitivity depends on how highly overexpressed top3+ is; more top3+ -> lower sensitivity)
PMID:12023299	FYPO:0005388	decreased number of Rad51 foci during cellular response to ionizing radiation [has_severity] medium	(comment: mah: slighly more severe than rad50delta alone)
PMID:12034771	FYPO:0005827	normal protein transport along microtubule during vegetative growth [assayed_using] PomBase:SPCC1223.06	(Fig. 2C) (comment: OUTSTANDING Q IS IT ALONG OR ON?)
PMID:12034771	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPCC1223.06 [has_severity] high	(Fig. 3C)
PMID:12034771	FYPO:0003185	normal protein localization to microtubule cytoskeleton during mitotic interphase [assayed_using] PomBase:SPCC1223.06	(Fig. 3C)
PMID:12034771	FYPO:0003185	normal protein localization to microtubule cytoskeleton during mitotic interphase [assayed_using] PomBase:SPCC1223.06	(Fig. 3C)
PMID:12034771	FYPO:0003185	normal protein localization to microtubule cytoskeleton during mitotic interphase [assayed_using] PomBase:SPCC1223.06	(Fig. 3C)
PMID:12034771	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [has_severity] low [assayed_using] PomBase:SPCC1223.06	(Fig. 3C)
PMID:12034771	FYPO:0004611	long interphase microtubules [has_penetrance] low	(Fig. 3C, 5A) (comment: CHECK STILL TO ADD curved around cell end during mitotic interphase)
PMID:12034771	FYPO:0005827	normal protein transport along microtubule during vegetative growth [assayed_using] PomBase:SPCC1223.06	(Fig. 4A)
PMID:12034771	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [has_severity] high [assayed_using] PomBase:SPCC1223.06	(Fig. 4B)
PMID:12034771	FYPO:0004731	normal protein localization to interphase microtubule plus-end [assayed_using] PomBase:SPCC1223.06	(Fig. 4B) (comment: I know that the protein is localising to the plus end but they did not say this in this paper although they do say it is on the tips of polymerizing microtubules so it could be FYPO 0004731)
PMID:12034771	FYPO:0003702	normal microtubule cytoskeleton morphology during vegetative growth	(Fig. 5A)
PMID:12034771	FYPO:0003702	normal microtubule cytoskeleton morphology during vegetative growth	(Fig. 5A)
PMID:12034771	FYPO:0004700	bent vegetative cell [has_penetrance] low	(Fig. 5B)
PMID:12034771	FYPO:0004700	bent vegetative cell [has_penetrance] medium	(Fig. 5B)
PMID:12034771	FYPO:0004700	bent vegetative cell [has_penetrance] medium	(Fig. 5B)
PMID:12034771	FYPO:0003329	abolished protein localization to cell tip during mitotic interphase [assayed_using] PomBase:SPBC1604.20c	(Fig. 6)
PMID:12034771	FYPO:0003329	abolished protein localization to cell tip during mitotic interphase [assayed_using] PomBase:SPAC3C7.12	(Fig. 6)
PMID:12034771	FYPO:0003329	abolished protein localization to cell tip during mitotic interphase [assayed_using] PomBase:SPAC2F7.03c	(Fig. 6)
PMID:12034771	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [has_penetrance] >95 [assayed_using] PomBase:SPCC1223.06 [has_severity] high	(Figure 2A)
PMID:12034771	GO:1990752	microtubule end [exists_during] mitotic interphase	(comment: used endogenous tea1 gene tagged at C term with YFP and tubulin CFP for live cell imaging of tea1 on microtubules) (Fig. 1 C)
PMID:12034771	GO:0051286	cell tip [exists_during] mitotic interphase	(comment: used endogenous tea2 gene tagged at C term with GFP) (Fig. 1A)
PMID:12034771	GO:0000935	division septum [exists_during] mitotic interphase	(comment: used endogenous tea2 gene tagged at C term with GFP) (Fig. 1A)
PMID:12050156	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC22H10.13 [has_severity] high	Both the basal and zinc-induced levels of zym1 transcripts were severely reduced in wis1Δ (Fig. 3C).
PMID:12050156	PomGeneEx:0000011	RNA level increased [in_presence_of] cadmium sulfate	Cadmium increased the proportion of longer zym1 transcripts as observed previously following the exposure to copper (Fig. 6B).
PMID:12050156	FYPO:0001533	sensitive to zinc starvation [has_severity] high	Fig. 1. Zhf is required for growth on high and low zinc
PMID:12050156	FYPO:0000116	sensitive to zinc [has_severity] high	Fig. 1. Zhf is required for growth on high and low zinc
PMID:12050156	GO:0140486	zinc ion sequestering activity [part_of] detoxification of zinc ion	Less zinc but normal cadmium was accumulated by zym1Δ, consistent with zinc sequestration by Zym1 in vivo. Zym1 was incubated with increasing concentrations of PMPS in the presence of the metallochromic indicator 4-(2)-(pyridylazo)resorcinol (35). Between 10 and 12 molar equivalents of PMPS displaced approximately four equivalents of zinc from Zym1, indicating that up to 12 cysteine residues are involved in binding four atoms of zinc (Fig.7A). All of the 12 cysteine residues appear to contribute ligands. Bridging ligands are probable, because there are insufficient cysteines to provide four independent tetravalent sites.
PMID:12050156	FYPO:0000116	sensitive to zinc [has_severity] high	Most importantly, the zhfΔ strain was hypersensitive to zinc showing impaired growth on rich medium (YE5S) compared with the equivalent control strain and was unable to grow in medium supplemented with 20 μm ZnSO4 (Fig. 1C).
PMID:12050156	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC22H10.13 [has_severity] medium	The abundance of zym1 transcripts was also reduced in cells lacking Pcr1, a bZIP transcription factor that in conjunction with Atf1 functions downstream of Sty1 (41, 42) (Fig. 3C).
PMID:12050156	FYPO:0000116	sensitive to zinc	The growth of the resulting zym1Δ showed only a small but reproducible impairment in rich medium (YE5S) supplemented with 10-100 μm zinc (Fig. 5A).
PMID:12050156	FYPO:0001533	sensitive to zinc starvation [has_severity] high	Zhf Is Required for Growth on Low Zinc
PMID:12050156	PomGeneEx:0000011	RNA level increased [in_presence_of] zinc sulfate	Zinc caused the accumulation of zym1 transcripts with up to 10 -20-fold increase 30 min after the addition of ZnSO4 (Fig. 3, A and C).
PMID:12050156	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC22H10.13 [has_severity] medium	but this pathway is not obligatory for zinc perception because zinc induction was retained in Wis1 mutants albeit at reduced magnitude.
PMID:12062100	PomGeneEx:0000011	RNA level increased [during] cellular response to hydroxyurea	(comment: longer transcript)
PMID:12062100	FYPO:0002975	decreased RNA level during cellular response to hydroxyurea [assayed_transcript] PomBase:SPBC25D12.04	(comment: longer transcript)
PMID:12062100	FYPO:0007845	increased rate of RNA catabolic process during vegetative growth [assayed_transcript] PomBase:SPBC25D12.04	(comment: longer transcript)
PMID:12065422	FYPO:0000276	monopolar mitotic spindle [has_penetrance] 76	(Figure 1A) We concluded that the severe phenotype of a ®n1.ts1 mutant is a transitory response to loss of Fin1 function. This implied that ®n1.D haploids adapted to loss of Fin1 after the ®rst division of a germinating spore.
PMID:12065422	FYPO:0000276	monopolar mitotic spindle [has_penetrance] 26	(Figure 1B)
PMID:12065422	FYPO:0000276	monopolar mitotic spindle [has_penetrance] 26	(Figure 1C)
PMID:12065422	FYPO:0000276	monopolar mitotic spindle [has_penetrance] 26	(Figure 1C)
PMID:12065422	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Figure 2A; Table II)
PMID:12065422	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	(Figure 2B and C)
PMID:12065422	FYPO:0000338	abnormal mitotic spindle [has_penetrance] ~38	(Figure 5d)
PMID:12065422	FYPO:0000338	abnormal mitotic spindle [has_penetrance] 26	(Figures 1C and 2C)
PMID:12065422	FYPO:0001124	normal vegetative cell size	(Table II)
PMID:12065422	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Table II)
PMID:12065422	FYPO:0000338	abnormal mitotic spindle [has_penetrance] 10-15	(comment: CONDITION 25 degrees) Figure 5d
PMID:12065422	FYPO:0000338	abnormal mitotic spindle [has_penetrance] 20	(comment: CONDITION 25 degrees) Figure 7
PMID:12065422	FYPO:0000338	abnormal mitotic spindle [has_penetrance] <10	(comment: CONDITION 25 degrees) Figure 7
PMID:12065422	FYPO:0001124	normal vegetative cell size	(comment: recessive, loss-of-function mutation)
PMID:12065422	FYPO:0001399	normal mitotic spindle	(comment: recessive, loss-of-function mutation)
PMID:12065422	FYPO:0002061	inviable vegetative cell population	DNS
PMID:12065422	FYPO:0002061	inviable vegetative cell population	DNS
PMID:12065422	FYPO:0002061	inviable vegetative cell population	Introduction of either ®n1.ts1 or ®n1.D to a cut12.s11 cdc25.22 mutant background abolished the growth of cdc25.22 above 30°C that had been conferred by the cut12.s11 mutation (Figure 6C).
PMID:12074602	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC649.04	(comment: binds to 54-bp element at 1186-1239)
PMID:12093738	FYPO:0000444	abnormal mitotic cell cycle arrest with replicated DNA [has_penetrance] high	(Fig. 1A)
PMID:12093738	FYPO:0000835	decreased protein level [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 1C)
PMID:12093738	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09 [has_penetrance] high	(Fig. 1C)
PMID:12093738	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC11B10.09 [has_penetrance] high	(Fig. 1C)
PMID:12093738	FYPO:0004189	increased protein level during cellular response to hydroxyurea [assayed_using] PomBase:SPBC11B10.09 [has_penetrance] high	(Fig. 1D)
PMID:12093738	FYPO:0002096	increased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPBC11B10.09 [has_penetrance] medium	(Fig. 1D) The protein cdc2 protein assayed is in complex with cig2 as there is no cdc2-cdc13 complex present
PMID:12093738	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09	(Fig. 2C) the cdc2-cig2 and cdc2-cdc13 complexe have no tyrosine 15 phosphorylation
PMID:12093738	FYPO:0002700	increased protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 2C) the cdc2-cig2 and cdc2-cdc13 complexes have increased kinase activity
PMID:12093738	FYPO:0001489	inviable vegetative cell [has_penetrance] medium	(Fig. 3) data not shown cell viability is reduced at late time points
PMID:12093738	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] medium	(Fig. 3A, D)
PMID:12093738	FYPO:0001383	normal DNA content [assayed_using] PomBase:SPAPB2B4.03	(Fig. 3B) no G1 peak is observed showing that S phase onset is not delayed
PMID:12093738	FYPO:0000836	increased protein level [assayed_using] PomBase:SPAPB2B4.03	(Fig. 3C) (comment: cig2 over expression from ~10hours after thiamine removal)
PMID:12093738	FYPO:0001974	increased number of cells with 1C DNA content [assayed_using] PomBase:SPAPB2B4.03	(Fig. 4A) cells block normally with 1C DNA content even when cig2 is over expressed
PMID:12093738	FYPO:0000836	increased protein level [assayed_using] PomBase:SPAPB2B4.03	(Fig. 4B) cig2 over expression also occurs when cells blocked with HU
PMID:12093738	FYPO:0000017	elongated cell	(Fig. 5A)
PMID:12093738	FYPO:0003449	abnormal cell cycle arrest at mitotic G1/S phase transition	(Fig. 5A)
PMID:12093738	FYPO:0004320	altered DNA level [has_penetrance] low	(Fig. 5A) small peak of less that 1C DNA content
PMID:12093738	FYPO:0000023	small cell [has_penetrance] low	(Fig. 5A) used forward scatter to measure cell size small peak of short cells
PMID:12093738	FYPO:0001052	cut, small cell [has_penetrance] high	(Fig. 5B)
PMID:12093738	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [has_penetrance] medium [assayed_using] PomBase:SPBC11B10.09	(Fig. 5C)
PMID:12093738	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] low	(comment: CHECK fypo/issues/3165) Fig5B in the absence of cig2 there is a delay in the appearance of cut cells
PMID:12093738	FYPO:0002830	delayed onset of protein phosphorylation during vegetative growth [has_penetrance] medium [assayed_using] PomBase:SPBC11B10.09	(comment: CHECK fypo/issues/3165) Fig5C
PMID:12095692	GO:0001181	RNA polymerase I general transcription initiation factor activity	3.4. The putative SpRrn11h co-fractionates with Sp-MHRrn7h and rDNA transcription initiation activity
PMID:12095692	GO:0001164	RNA polymerase I core promoter sequence-specific DNA binding	3.7. Association of SpRrn7h with rDNA core promoter sequences
PMID:12095692	GO:0001181	RNA polymerase I general transcription initiation factor activity	Neither the pol I/Rrn3p (Fig. 3, lane 3) nor the SpRrn7h complex fraction (Fig. 3, lanes 1 and 2) support accurate initiation of the S. pombe rRNA template 30 D 131, on their own. However, when both are present, accurate transcriptional initiation of the S. pombe rDNA gene promoter is reconstituted (Fig. 3, lanes 4 and 5).
PMID:12095692	GO:0001181	RNA polymerase I general transcription initiation factor activity	Neither the pol I/Rrn3p (Fig. 3, lane 3) nor the SpRrn7h complex fraction (Fig. 3, lanes 1 and 2) support accurate initiation of the S. pombe rRNA template 30 D 131, on their own. However, when both are present, accurate transcriptional initiation of the S. pombe rDNA gene promoter is reconstituted (Fig. 3, lanes 4 and 5).
PMID:12112233	FYPO:0001357	normal vegetative cell population growth	(Figure 1)
PMID:12112233	FYPO:0003027	normal poly(A)+ mRNA export from nucleus	(Figure 1)
PMID:12112233	FYPO:0002522	decreased poly(A)+ mRNA export from nucleus	(comment: actually accumulation)
PMID:12161753	GO:0006357	regulation of transcription by RNA polymerase II [happens_during] single-celled organism vegetative growth phase	We constructed deletion mutants and examined their phenotypes. Conjugation and meiotic divisions proceeded normally, but spore formation was defective (Fig. 3a). We used microarrays to identify potential targets of Atf21p and Atf31p (Fig. 3b,c). Atf21p and Atf31p were required for the expression of overlapping sets of genes, as all of the genes affected in atf31∆ mutants were also affected in atf21∆ mutants (Fig. 3b). All of the potential targets were upregu- lated in late meiosis after induction of atf21 and atf31 (Fig. 3d).
PMID:12161753	GO:0006357	regulation of transcription by RNA polymerase II [happens_during] single-celled organism vegetative growth phase	We constructed deletion mutants and examined their phenotypes. Conjugation and meiotic divisions proceeded normally, but spore formation was defective (Fig. 3a). We used microarrays to identify potential targets of Atf21p and Atf31p (Fig. 3b,c). Atf21p and Atf31p were required for the expression of overlapping sets of genes, as all of the genes affected in atf31∆ mutants were also affected in atf21∆ mutants (Fig. 3b). All of the potential targets were upregu- lated in late meiosis after induction of atf21 and atf31 (Fig. 3d).
PMID:12181326	FYPO:0006661	fragmented nucleus	data not shown
PMID:12181336	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC24B11.06c [assayed_using] PomBase:SPBC409.07c	(Fig. 3)
PMID:12181336	FYPO:0003075	normal protein kinase activity [assayed_using] PomBase:SPAC24B11.06c	(Fig. 3)
PMID:12181336	FYPO:0003075	normal protein kinase activity [assayed_using] PomBase:SPAC24B11.06c	(Fig. 3)
PMID:12181336	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC24B11.06c [assayed_using] PomBase:SPBC409.07c	(Fig. 3)
PMID:12181336	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC24B11.06c [assayed_using] PomBase:SPBC409.07c	(Fig. 3)
PMID:12181336	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC24B11.06c [assayed_using] PomBase:SPBC409.07c	(Fig. 4)
PMID:12181336	FYPO:0006549	decreased gene expression [assayed_using] PomBase:SPBC215.05	(Fig. 4)
PMID:12181336	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC24B11.06c [assayed_using] PomBase:SPBC409.07c [has_severity] high	(Fig. 4)
PMID:12181336	FYPO:0000255	increased nuclear protein level during vegetative growth [assayed_using] PomBase:SPBC409.07c	(Fig. 5)
PMID:12181336	FYPO:0000255	increased nuclear protein level during vegetative growth [assayed_using] PomBase:SPBC409.07c	(Fig. 5)
PMID:12181336	FYPO:0000255	increased nuclear protein level during vegetative growth [assayed_using] PomBase:SPBC409.07c	(Fig. 5)
PMID:12181336	GO:0005829	cytosol	(Fig. 5) Consistent with previous immunolocalization studies (Gaits et al., 1998), wild-type Wis1-GFP showed solely cytoplasmic localization and little GFP signal was seen in the nuclear region (Figure 5A).
PMID:12181336	FYPO:0000255	increased nuclear protein level during vegetative growth [assayed_using] PomBase:SPBC409.07c	(Fig. 6)
PMID:12181336	FYPO:0003627	normal protein localization [assayed_using] PomBase:SPAC24B11.06c	(Fig. 7)
PMID:12181336	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPAC24B11.06c [has_severity] low	(Fig. 7)
PMID:12181336	FYPO:0001265	increased protein phosphorylation during cellular hyperosmotic response [assayed_using] PomBase:SPAC24B11.06c	(Figure 2B)
PMID:12181336	FYPO:0001265	increased protein phosphorylation during cellular hyperosmotic response [assayed_using] PomBase:SPAC24B11.06c	(Figure 2B)
PMID:12181336	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPAC24B11.06c	(Figure 2B)
PMID:12185500	FYPO:0002060	viable vegetative cell population	(comment: CONDITION 25 degrees C)
PMID:12185500	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 25 degrees C)
PMID:12185500	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 27 degrees C)
PMID:12185500	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 27 degrees C)
PMID:12185500	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 29 degrees C)
PMID:12185500	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 29 degrees C)
PMID:12185500	FYPO:0000082	decreased cell population growth at high temperature	(comment: CONDITION restrictive temp 32)
PMID:12185500	FYPO:0000082	decreased cell population growth at high temperature	(comment: CONDITION restrictive temp 36)
PMID:12185500	FYPO:0002061	inviable vegetative cell population	(comment: condition 25 degrees C)
PMID:12185840	GO:0005739	mitochondrion	(Fig. 2C)
PMID:12185840	FYPO:0000783	protein mislocalized to cytoplasm during vegetative growth [assayed_using] PomBase:SPBC2G2.04c	(Figure 2C)
PMID:12186944	GO:0032153	cell division site	"(comment: localization requires microtubules (assayed using thiabendazole or carbendazim) but not F-actin (assayed using latrunculin A)"""
PMID:12186947	FYPO:0003012	mitosis with unreplicated DNA [has_penetrance] medium	(comment: CHECK penetrance low if cells exposed to UV)
PMID:12193640	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC664.01c	As expected, Swi6, which depends on histone modification for chromatin binding, was delocalized from the ura4+ transgenes (Fig. 3C).
PMID:12193640	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC664.01c	As expected, Swi6, which depends on histone modification for chromatin binding, was delocalized from the ura4+ transgenes (Fig. 3C).
PMID:12193640	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC664.01c	As expected, Swi6, which depends on histone modification for chromatin binding, was delocalized from the ura4+ transgenes (Fig. 3C).
PMID:12193640	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	However, three major transcripts that hybridized to the repeats were found to accumulate at high levels in each of the RNAi mutants (Fig. 1C).
PMID:12193640	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	However, three major transcripts that hybridized to the repeats were found to accumulate at high levels in each of the RNAi mutants (Fig. 1C).
PMID:12193640	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	However, three major transcripts that hybridized to the repeats were found to accumulate at high levels in each of the RNAi mutants (Fig. 1C).
PMID:12193640	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth	In contrast, levels of K9 were greatly reduced.
PMID:12193640	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth	In contrast, levels of K9 were greatly reduced.
PMID:12193640	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth	In contrast, levels of K9 were greatly reduced.
PMID:12193640	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] low	These transcripts were also found in swi6- (Fig. 1D) but at a much lower lev
PMID:12193640	FYPO:0004331	normal chromatin silencing at centromere central core	Two transgenes located centromere distal to the tRNA genes were de-repressed in ago1- , dcr1- , and rdp1- , but a transgene located within the central region remained silent. Similar results were obtained in all three mutant strains, as assayed by growth on medium lacking uracil and by Northern blots (Fig. 1, B) (21).
PMID:12193640	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	Two transgenes located centromere distal to the tRNA genes were de-repressed in ago1- , dcr1- , and rdp1- , but a transgene located within the central region remained silent. Similar results were obtained in all three mutant strains, as assayed by growth on medium lacking uracil and by Northern blots (Fig. 1, B) (21).
PMID:12193640	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	Two transgenes located centromere distal to the tRNA genes were de-repressed in ago1- , dcr1- , and rdp1- , but a transgene located within the central region remained silent. Similar results were obtained in all three mutant strains, as assayed by growth on medium lacking uracil and by Northern blots (Fig. 1, B) (21).
PMID:12193640	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	Two transgenes located centromere distal to the tRNA genes were de-repressed in ago1- , dcr1- , and rdp1- , but a transgene located within the central region remained silent. Similar results were obtained in all three mutant strains, as assayed by growth on medium lacking uracil and by Northern blots (Fig. 1, B) (21).
PMID:12193640	FYPO:0004331	normal chromatin silencing at centromere central core	Two transgenes located centromere distal to the tRNA genes were de-repressed in ago1- , dcr1- , and rdp1- , but a transgene located within the central region remained silent. Similar results were obtained in all three mutant strains, as assayed by growth on medium lacking uracil and by Northern blots (Fig. 1, B) (21).
PMID:12193640	FYPO:0004331	normal chromatin silencing at centromere central core	Two transgenes located centromere distal to the tRNA genes were de-repressed in ago1- , dcr1- , and rdp1- , but a transgene located within the central region remained silent. Similar results were obtained in all three mutant strains, as assayed by growth on medium lacking uracil and by Northern blots (Fig. 1, B) (21).
PMID:12193640	FYPO:0007337	increased histone H3-K4 methylation at centromere during vegetative growth	dcr1- , rdp1- , and ago1- cells had increased levels of K4 in the centromeric region in comparison to actin controls (Fig. 3B).
PMID:12193640	FYPO:0007337	increased histone H3-K4 methylation at centromere during vegetative growth	dcr1- , rdp1- , and ago1- cells had increased levels of K4 in the centromeric region in comparison to actin controls (Fig. 3B).
PMID:12193640	FYPO:0007337	increased histone H3-K4 methylation at centromere during vegetative growth	dcr1- , rdp1- , and ago1- cells had increased levels of K4 in the centromeric region in comparison to actin controls (Fig. 3B).
PMID:12196391	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] medium	(comment: same as either single mutant)
PMID:12196391	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] medium	(comment: same as either single mutant)
PMID:12196391	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] high	(comment: same as rad26delta alone)
PMID:12196391	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] high	(comment: same as rad3delta alone)
PMID:12196391	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] high	(comment: same as rad3delta alone)
PMID:12196391	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] high	(comment: same as rad3delta alone)
PMID:12196391	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] high	(comment: same as rad3delta alone)
PMID:12207036	FYPO:0002060	viable vegetative cell population	(Fig. 6)
PMID:12207036	FYPO:0002060	viable vegetative cell population	(Fig. 6)
PMID:12207036	FYPO:0002060	viable vegetative cell population	(Fig. 6)
PMID:12242222	FYPO:0005870	incomplete septum	(Fig. 4)
PMID:12242222	FYPO:0000647	vegetative cell lysis	(Fig. 4)
PMID:12242222	FYPO:0002946	abnormal cell wall	(Fig. 4E)
PMID:12242294	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. 1a)
PMID:12242294	FYPO:0002390	normal mitotic sister chromatid cohesion	(Fig. 1a) (comment: CHECK maintenence of)
PMID:12242294	FYPO:0004085	decreased vegetative cell growth	(Fig. 8a)
PMID:12242294	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Fig. 8a)
PMID:12242294	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Fig. 8a)
PMID:12242294	FYPO:0001355	decreased vegetative cell population growth	(Fig. 8a)
PMID:12242294	FYPO:0001355	decreased vegetative cell population growth	(Fig. 8b)
PMID:12242294	FYPO:0001355	decreased vegetative cell population growth	(Fig. 8b)
PMID:12242294	FYPO:0002061	inviable vegetative cell population	(Fig. 8d)
PMID:12242294	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 8d)
PMID:12242294	FYPO:0004307	long mitotic spindle during metaphase [has_penetrance] 12	(Figure 9)
PMID:12242294	FYPO:0002901	normal protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPAC25B8.14	data not shown
PMID:12242294	FYPO:0002151	inviable spore [has_severity] high	data not shown
PMID:12242294	FYPO:0000228	lagging mitotic chromosomes [has_severity] high	data not shown
PMID:12242294	FYPO:0002901	normal protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPBC409.04c	data not shown
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1)
PMID:12354095	FYPO:0001357	normal vegetative cell population growth	(Fig. 1)
PMID:12354095	FYPO:0001357	normal vegetative cell population growth	(Fig. 1)
PMID:12354095	FYPO:0000086	sensitive to tacrolimus [has_severity] high	(Fig. 1)
PMID:12354095	FYPO:0000086	sensitive to tacrolimus [has_severity] high	(Fig. 1)
PMID:12354095	FYPO:0000105	sensitive to cyclosporin A [has_severity] high	(Fig. 1)
PMID:12354095	FYPO:0000105	sensitive to cyclosporin A [has_severity] high	(Fig. 1)
PMID:12354095	FYPO:0006836	sensitive to magnesium chloride [has_severity] high	(Fig. 1)
PMID:12354095	FYPO:0005970	normal growth on magnesium chloride	(Fig. 1)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1)
PMID:12354095	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC21.06c	(Fig. 2B)
PMID:12354095	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC21.06c	(Fig. 2B)
PMID:12354095	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC21.06c	(Fig. 2B)
PMID:12354095	FYPO:0001315	normal vegetative cell morphology	(Fig. 2B)
PMID:12354095	FYPO:0000118	multiseptate vegetative cell	(Fig. 2B)
PMID:12354095	FYPO:0001315	normal vegetative cell morphology	(Fig. 2B)
PMID:12354095	FYPO:0001315	normal vegetative cell morphology	(Fig. 2B)
PMID:12354095	FYPO:0001315	normal vegetative cell morphology	(Fig. 2B)
PMID:12354095	FYPO:0001315	normal vegetative cell morphology	(Fig. 2B)
PMID:12354095	FYPO:0000674	normal cell population growth at high temperature	(Fig. 2C)
PMID:12354095	FYPO:0000674	normal cell population growth at high temperature	(Fig. 2C)
PMID:12354095	FYPO:0004562	binucleate aseptate vegetative cell [has_penetrance] 12	(Fig. 3A and D)
PMID:12354095	FYPO:0004562	binucleate aseptate vegetative cell [has_penetrance] 10	(Fig. 3A and D)
PMID:12354095	FYPO:0004562	binucleate aseptate vegetative cell [has_penetrance] 54	(Fig. 3B and D)
PMID:12354095	FYPO:0004562	binucleate aseptate vegetative cell [has_penetrance] 44	(Fig. 3B and D)
PMID:12354095	FYPO:0002049	elongated multinucleate aseptate vegetative cell [has_penetrance] 18	(Fig. 3B and D)
PMID:12354095	FYPO:0002049	elongated multinucleate aseptate vegetative cell [has_penetrance] 15	(Fig. 3B and D)
PMID:12354095	FYPO:0002049	elongated multinucleate aseptate vegetative cell [has_penetrance] 12	(Fig. 3C and D)
PMID:12354095	FYPO:0004562	binucleate aseptate vegetative cell [has_penetrance] 77	(Fig. 3C and D)
PMID:12354095	FYPO:0002049	elongated multinucleate aseptate vegetative cell [has_penetrance] 11	(Fig. 3C and D)
PMID:12354095	FYPO:0004562	binucleate aseptate vegetative cell [has_penetrance] 79	(Fig. 3C and D)
PMID:12354095	FYPO:0001470	normal growth on tacrolimus	(Fig. 4A)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:12354095	FYPO:0000086	sensitive to tacrolimus [has_severity] high	(Fig. 4A)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:12354095	FYPO:0000086	sensitive to tacrolimus [has_severity] high	(Fig. 4B)
PMID:12354095	FYPO:0000086	sensitive to tacrolimus [has_severity] high	(Fig. 4B)
PMID:12354095	FYPO:0000086	sensitive to tacrolimus [has_severity] high	(Fig. 4B)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4B)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4B)
PMID:12354095	FYPO:0001470	normal growth on tacrolimus	(Fig. 4B)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4B)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4B)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5A)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 5A)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 5A)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 5A)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5B)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 5B)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5B)
PMID:12354095	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 5B)
PMID:12354095	FYPO:0000650	increased septation index [has_severity] high	(Fig. 5C and D)
PMID:12354095	FYPO:0001406	increased septum thickness	(Fig. 6)
PMID:12390246	FYPO:0005349	increased spindle pole body-led chromosome movement during mitotic interphase	(Fig. 4a,b)
PMID:12390246	FYPO:0005347	pointed nucleus during mitotic interphase [has_penetrance] 5	(Fig. 6A)
PMID:12390246	FYPO:0005347	pointed nucleus during mitotic interphase [has_penetrance] 13	penetrance is mentioned in EXP accompanying fig 6A
PMID:12390246	FYPO:0005347	pointed nucleus during mitotic interphase [has_penetrance] 8	penetrance is mentioned in EXP accompanying fig 6A
PMID:12390246	FYPO:0005347	pointed nucleus during mitotic interphase [has_penetrance] 4	penetrance is mentioned in EXP accompanying fig 6A
PMID:12390246	FYPO:0005347	pointed nucleus during mitotic interphase [has_penetrance] 15	penetrance is mentioned in EXP accompanying fig 6A
PMID:12390246	FYPO:0005347	pointed nucleus during mitotic interphase [has_penetrance] 5	penetrance is mentioned in EXP accompanying fig 6A
PMID:12399381	FYPO:0006935	viable cell with normal cell morphology during nitrogen starvation [has_penetrance] complete	(Fig. 5)
PMID:12399381	FYPO:0006935	viable cell with normal cell morphology during nitrogen starvation [has_penetrance] complete	(Fig. 5)
PMID:12399381	FYPO:0006935	viable cell with normal cell morphology during nitrogen starvation [has_penetrance] complete	(Fig. 5)
PMID:12399381	GO:0034399	nuclear periphery	(Fig. 5A)
PMID:12399381	GO:0005634	nucleus	(Fig. 5A)
PMID:12399381	GO:0005737	cytoplasm	(Fig. 5A)
PMID:12399381	FYPO:0000590	normal sporulation	(Fig. 5C, D)
PMID:12399381	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(Figure 1)
PMID:12399381	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] complete	(Figure 1)
PMID:12399381	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Figure 1)
PMID:12399381	FYPO:0000446	cell cycle arrest at mitotic G2/M phase transition [has_penetrance] complete	(Figure 1) (comment: CHECK cdr phenotype)
PMID:12399381	FYPO:0007435	inviable elongated mononucleate cell during nitrogen starvation [has_penetrance] complete	(Figure 1) (comment: CHECK cdr phenotype)
PMID:12399381	FYPO:0001001	abnormal cell cycle arrest at mitotic G2/M phase transition during nitrogen starvation [has_penetrance] complete	(Figure 2C, D)
PMID:12399381	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] complete	(Figure 2a)
PMID:12399381	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Figure 2a)
PMID:12399381	FYPO:0001490	inviable elongated vegetative cell	(Figure 3)
PMID:12399381	FYPO:0007435	inviable elongated mononucleate cell during nitrogen starvation [has_penetrance] complete [has_severity] high	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	FYPO:0007435	inviable elongated mononucleate cell during nitrogen starvation [has_penetrance] complete [has_severity] high	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	FYPO:0007435	inviable elongated mononucleate cell during nitrogen starvation [has_penetrance] complete [has_severity] high	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	FYPO:0007435	inviable elongated mononucleate cell during nitrogen starvation [has_penetrance] complete [has_severity] high	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	FYPO:0007435	inviable elongated mononucleate cell during nitrogen starvation [has_penetrance] complete	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	FYPO:0007435	inviable elongated mononucleate cell during nitrogen starvation [has_penetrance] complete	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	FYPO:0007435	inviable elongated mononucleate cell during nitrogen starvation [has_penetrance] complete	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	FYPO:0007435	inviable elongated mononucleate cell during nitrogen starvation [has_penetrance] complete	(Figure 4) (comment: CHECK cdr phenotype)
PMID:12399381	FYPO:0004077	abnormal sporulation resulting in formation of ascus with single large spore [has_penetrance] 68	(Figure 5C, D)
PMID:12399381	FYPO:0001424	abolished protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPAC24H6.05	(Figure 6A)
PMID:12399381	FYPO:0004056	decreased protein localization to nucleus, with protein mislocalized to cytoplasm [has_severity] low	(Figure 6b) (comment: CHECK during x phase?)
PMID:12399381	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(Table 4)
PMID:12399381	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] low	(comment: semi wee)
PMID:12411492	FYPO:0004936	abolished DNA binding at PCB [assayed_using] PomBase:SPBC16G5.15c	(comment: same as plo1-ts35 alone)
PMID:12411492	FYPO:0004936	abolished DNA binding at PCB [assayed_using] PomBase:SPBC19G7.06	(comment: same as plo1-ts35 alone)
PMID:12411492	FYPO:0004936	abolished DNA binding at PCB [assayed_using] PomBase:SPBC4C3.12	(comment: same as plo1-ts35 alone)
PMID:12419251	FYPO:0003950	decreased protein localization to chromatin at replication origin [assayed_using] PomBase:SPCC16A11.17	(comment: CHECK actually ectopic expression, throughout cell cycle)
PMID:12419251	FYPO:0000333	mitotic G1/S phase transition delay	(comment: CHECK actually ectopic expression, throughout cell cycle)
PMID:12419251	FYPO:0004962	normal protein localization to chromatin at replication origin [assayed_using] PomBase:SPBC582.03	(comment: CHECK normal binding periodicity over cell cycle)
PMID:12419251	FYPO:0004962	normal protein localization to chromatin at replication origin [assayed_using] PomBase:SPCC16A11.17	(comment: normal binding periodicity over cell cycle)
PMID:12419251	FYPO:0004962	normal protein localization to chromatin at replication origin [assayed_using] PomBase:SPBC582.03	(comment: normal binding periodicity over cell cycle)
PMID:12426374	GO:0000776	kinetochore [exists_during] mitotic prophase	(Figure 1A and C)
PMID:12426374	GO:0000776	kinetochore [exists_during] mitotic prophase	(Figure 1A and C)
PMID:12426374	FYPO:0000141	abnormal mitotic sister chromatid segregation	(Figure 1B)
PMID:12426374	FYPO:0006179	abnormal lateral attachment of mitotic spindle microtubules to kinetochore	(Figure 1B, rows 4±6 )
PMID:12426374	FYPO:0006179	abnormal lateral attachment of mitotic spindle microtubules to kinetochore	(Figure 1B, rows 4±6)
PMID:12426374	FYPO:0006179	abnormal lateral attachment of mitotic spindle microtubules to kinetochore	(Figure 1B, rows 4±6)
PMID:12426374	FYPO:0006190	long mitotic spindle during anaphase A	(comment: vw: assayed by increased mad2 at kinetochore - checkpoint active)
PMID:12426374	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(comment: vw: assayed by increased mad2 at kinetochore - checkpoint active)
PMID:12427731	GO:0007163	establishment or maintenance of cell polarity	(comment: CHECK based just on this paper, candidate for involved_in_or_regulates qualifier)
PMID:12427731	GO:0004672	protein kinase activity	(comment: assayed using myelin basic protein; doesn't rule out tyrosine phosphorylation)
PMID:12442907	FYPO:0000636	increased cell population growth rate	(Fig. 1b) The estimated doubling time of the mutant was 110 min in a rich (YE) medium, while that of the wild-type cells was 150 min.
PMID:12442907	FYPO:0001046	premature mitosis	(Fig. 1c) The mutant produced daughter cells with an average length of 6 μm; whereas, the wild-type cells averaged 7.5 μm
PMID:12442907	FYPO:0007628	abnormal chromatin organization during mitotic G2 phase	(Figs. 3A and 3B).
PMID:12442907	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Figs. 3A and 3B). there were cells that initiated and completed the mitosis in a small portion (Table 1), which eventually led to cell proliferation until the stationary phase (Fig. 2A).
PMID:12442907	FYPO:0003306	decreased mitotic index	(Table 1)
PMID:12442907	FYPO:0001234	slow vegetative cell population growth	As shown in Fig. 2A, the rate of cell proliferation was immediately reduced after the amount of Rrg1 was increased.
PMID:12442907	FYPO:0001406	increased septum thickness	a considerable portion of the Rrg1-overproduced cells that undergo mitosis showed an abnormal accumulation of septum material (Figs. 3F, 3G, and 3H).
PMID:12442907	FYPO:0006822	viable small vegetative cell with normal cell growth rate	small daughter at g1 Fig 1c The mutant produced daughter cells with an average length of 6 μm; whereas, the wild-type cells averaged 7.5 μm
PMID:12455694	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 32 degrees) (comment: CHECK mcl1-1 semi-permissive)
PMID:12455694	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 32 degrees) (comment: CHECK mcl1-1 semi-permissive)
PMID:12479804	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	(Fig. 1A) I'm modelling this as decreased because nda3 is providing microtubule damage. Checkpoint would be expected to be o in WT in this scenario. cells failed to maintain the microtubule damage-induced checkpoint arrest and began to aberrantly form septa
PMID:12479804	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. 1A) I'm modelling this as normal becasue nda3 is providing microtubule damage. Checkpoint would be expected to be o in WT in this scenario. cells failed to maintain the microtubule damage-induced checkpoint arrest and began to aberrantly form septa
PMID:12479804	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC21.06c	(Fig. 1B)
PMID:12479804	GO:0005515	protein binding	(Fig. 4)
PMID:12479804	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16	(Fig. 5)
PMID:12479804	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 6)
PMID:12479804	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 6)
PMID:12479804	FYPO:0004106	inviable multinucleate aseptate vegetative cell	(Figure 2)
PMID:12479804	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [has_penetrance] 73 [assayed_using] PomBase:SPAC9G1.09	(Figure 2A)
PMID:12479804	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_using] PomBase:SPBC21.06c [has_penetrance] 73	(Figure 2A)
PMID:12479804	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPAC24B11.11c	(Figure 2D)
PMID:12479804	GO:0044732	mitotic spindle pole body [exists_during] mitotic anaphase A	(Figure 3A)
PMID:12479804	GO:0032153	cell division site [exists_during] mitotic anaphase A	(Figure 3A)
PMID:12479804	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPAC17G8.10c	(Figure 3E, 3F)
PMID:12479804	FYPO:0001880	abolished protein localization to cell division site [assayed_using] PomBase:SPAC17G8.10c	(Figure 3E, 3F)
PMID:12479804	FYPO:0001880	abolished protein localization to cell division site [assayed_using] PomBase:SPAC17G8.10c	(Figure 3E, 3F)
PMID:12479804	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC17G8.10c	(Figure 3E, 3F)
PMID:12479804	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC17G8.10c	(Figure 3E, 3F)
PMID:12479804	FYPO:0001880	abolished protein localization to cell division site [assayed_using] PomBase:SPAC17G8.10c	(Figure 3E, 3F)
PMID:12479804	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC17G8.10c	(Figure 3E, 3F)
PMID:12479804	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC17G8.10c	(Figure 3E, 3F)
PMID:12479804	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC17G8.10c [has_penetrance] 20	(Figure 3E, 3F)
PMID:12479804	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC17G8.10c [has_penetrance] 90	(Figure 4A)
PMID:12479804	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC17G8.10c [has_penetrance] 90	(Figure 4A) (comment: CHECK 10% (2/20) of anaphase cells displayed Dma1p-GFP SPB signal)
PMID:12479804	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC17G8.10c	(Figure 4B)
PMID:12479804	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC244.01c [assayed_using] PomBase:SPAC17G8.10c	(Figure 4C)
PMID:12479804	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC244.01c [assayed_using] PomBase:SPAC17G8.10c	(Figure 4C)
PMID:12479804	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16	(Figure 5)
PMID:12479804	FYPO:0004083	normal protein level [assayed_using] PomBase:SPAC23C11.16	(Figure 5)
PMID:12479804	GO:0032153	cell division site [exists_during] mitotic metaphase	(comment: faintly) Figure 3A, panel 2, arrowhead
PMID:12479804	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	Table1
PMID:12479804	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	Table1
PMID:12479804	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	Table1
PMID:12479804	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	Table1
PMID:12479804	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	Table1
PMID:12479804	GO:0031030	negative regulation of septation initiation signaling	The observation that Clp1p/Flp1p is required for septation in dma1μ mutants is consistent with a model where Dma1p inhibits SIN activation
PMID:12482946	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 1B)
PMID:12482946	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 1B)
PMID:12482946	FYPO:0001234	slow vegetative cell population growth	(Fig. 1C)
PMID:12482946	FYPO:0000091	sensitive to thiabendazole	(Fig. 1D)
PMID:12482946	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 16	(Fig. 2A)
PMID:12482946	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC19C7.04c	(Fig. 2B)
PMID:12482946	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC3E7.02c	(Fig. 2B)
PMID:12482946	FYPO:0000220	increased centromeric outer repeat transcript level	(Fig. 2B)
PMID:12482946	FYPO:0002834	decreased chromatin silencing at centromere	(Fig. 2B)
PMID:12526748	FYPO:0000964	normal growth on thiabendazole [has_severity] high	(Fig. 1)
PMID:12526748	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1)
PMID:12526748	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1)
PMID:12526748	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1)
PMID:12526748	FYPO:0006993	decreased chromatin silencing at centromere otr1R	(Fig. 1b)
PMID:12526748	FYPO:0007305	increased histone H4-K5 acetylation at centromere during vegetative growth [has_severity] high	(Fig. 3)
PMID:12526748	FYPO:0007305	increased histone H4-K5 acetylation at centromere during vegetative growth [has_severity] high	(Fig. 3)
PMID:12526748	FYPO:0007306	increased histone H4-K12 acetylation at centromere during vegetative growth [has_severity] high	(Fig. 3)
PMID:12526748	FYPO:0000893	increased histone H3-K9 acetylation at centromere during vegetative growth [has_severity] high	(Fig. 3)
PMID:12526748	FYPO:0007307	increased histone H3-K14 acetylation at centromere during vegetative growth [has_severity] high	(Fig. 3)
PMID:12526748	FYPO:0007306	increased histone H4-K12 acetylation at centromere during vegetative growth [has_severity] high	(Fig. 3)
PMID:12526748	FYPO:0007307	increased histone H3-K14 acetylation at centromere during vegetative growth [has_severity] high	(Fig. 3)
PMID:12526748	FYPO:0000893	increased histone H3-K9 acetylation at centromere during vegetative growth [has_severity] high	(Fig. 3)
PMID:12526748	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 28	(Figure 1C)
PMID:12526748	FYPO:0002390	normal mitotic sister chromatid cohesion [has_penetrance] 2.4	(Figure 1e)
PMID:12526748	FYPO:0002390	normal mitotic sister chromatid cohesion [has_penetrance] 1.4	(Figure 1e)
PMID:12526748	FYPO:0002390	normal mitotic sister chromatid cohesion [has_penetrance] 5	(Figure 1e)
PMID:12526748	FYPO:0005579	decreased meiotic sister chromatid cohesion at centromere [has_penetrance] 35	(Figure 1e)
PMID:12526748	FYPO:0000460	decreased mitotic centromeric sister chromatid cohesion [has_penetrance] 21	(Figure 1e)
PMID:12526748	FYPO:0003217	decreased chromatin silencing at centromere central core [has_severity] low	(Figure S1)
PMID:12526748	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(Figure S1)
PMID:12526748	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure S1)
PMID:12526748	FYPO:0003555	normal chromatin silencing at subtelomere [has_severity] low	(Figure S1)
PMID:12526748	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 18	(comment: D.N.S?)
PMID:12526748	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 19	(comment: D.N.S?)
PMID:12526748	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 13	(comment: D.N.S?)
PMID:12526748	GO:0005721	pericentric heterochromatin [coincident_with] regional_centromere	(comment: Pst1p colocalizes with the otr/imr region in a cell cycle-specific manner.)
PMID:12546793	FYPO:0004355	increased protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(Figure 1A) In a mob1-R4 byr4::ura4Δ mutant, and also in cdc16-116 grown for 5 hr at 36+C, cdc11p accumulated in the hyperphosphorylated (3) form
PMID:12546793	FYPO:0004355	increased protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(Figure 1A) In a mob1-R4 byr4::ura4Δ mutant, and also in cdc16-116 grown for 5 hr at 36+C, cdc11p accumulated in the hyperphosphorylated (3) form. Later: in mutants such as cdc16-116 or byr4::ura4Δ, in which cdc7p is present on both spindle pole bodies, the hyperphosphorylated form (3) of cdc11p is more abundant.
PMID:12546793	FYPO:0004082	normal protein phosphorylation during mitosis [has_severity] high [assayed_protein] PomBase:SPCC1739.11c	(Figure 1B) n G2-arrested cdc2-17 cells overexpressing spg1p, cdc11p was predominantly in the hyperphosphorylated form
PMID:12546793	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC21.06c	(Figure 1C, and data not shown) Immunofluorescence indicated that both byr4p and cdc7p showed a normal, asymmetric distribution during mitosis
PMID:12546793	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC222.10c	(Figure 1C, and data not shown) Immunofluorescence indicated that both byr4p and cdc7p showed a normal, asymmetric distribution during mitosis
PMID:12546793	FYPO:0004082	normal protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(Figure 1D) The hyperphosphorylated form (3) of cdc11p was observed during mitosis in both sid2-250 and sid1- 239 mutants
PMID:12546793	FYPO:0004082	normal protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(Figure 1D) The hyperphosphorylated form (3) of cdc11p was observed during mitosis in both sid2-250 and sid1- 239 mutants
PMID:12546793	FYPO:0004082	normal protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(Figure 1D) The hyperphosphorylated form (3) of cdc11p was observed during mitosis in both sid2-250 and sid1- 239 mutants
PMID:12546793	FYPO:0004357	decreased protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(Figure 1E) In contrast, in cdc7-24, the hyperphosphorylated form of cdc11p (3) was greatly reduced, and the intensity of the hypophosphorylated forms (1 and 2) increased
PMID:12546793	FYPO:0004357	decreased protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(Figure 1G) No significant hyperphosphorylation of cdc11p occurred at 36+C .
PMID:12546793	FYPO:0004357	decreased protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(Figure 1G) No significant hyperphosphorylation of cdc11p occurred at 36+C.
PMID:12546793	FYPO:0007890	normal protein localization to kinetochore during mitotic spindle assembly checkpoint signaling	(Figure 2B). Immunofluorescence showed that byr4p was also present on the SPB in the arrested cells
PMID:12546793	FYPO:0004357	decreased protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(Figure 3B). However, at 36+C, when cdc11p is no longer associated with the SPB [3, 4], most of the cdc11p was hypophosphorylated (form 1)
PMID:12546793	GO:0031028	septation initiation signaling	(comment: CHECK HYPERPHOSPHORYLATD FORM) Together, these data demonstrate, first, that mitotic cdc2p activity is not required for hyperphosphorylation of cdc11p and, second, that activation of the SIN correlates with accumulation of hyperphosphorylated cdc11p.
PMID:12546793	FYPO:0004082	normal protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(comment: CHECK HYPERPHOSPHORYLATION) (Figure 1C) In the mutant plo1-ts4, which is defective in SIN signaling but not spindle formation [10], hyperphosphorylated cdc11p was observed during mitosis, even though the cells were not septating .
PMID:12546793	FYPO:0004357	decreased protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(comment: DNS)
PMID:12546793	FYPO:0004082	normal protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(see the Supplementary) Additional experiments indicated that neither mph1p nor fin1p regulate the phosphorylation of cdc11p
PMID:12546793	FYPO:0004082	normal protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(see the Supplementary) Additional experiments indicated that neither mph1p nor fin1p regulate the phosphorylation of cdc11p
PMID:12546793	FYPO:0004082	normal protein phosphorylation during mitosis [assayed_protein] PomBase:SPCC1739.11c	(see the Supplementary) Additional experiments indicated that neither mph1p nor fin1p regulate the phosphorylation of cdc11p
PMID:12546793	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC1739.11c [part_of] septation initiation signaling [occurs_in] mitotic spindle pole body [happens_during] mitotic anaphase B	In contrast, in cdc7-24, the hyperphosphorylated form of cdc11p (3) was greatly reduced, and the intensity of the hypophosphorylated forms (1 and 2) increased (Figure 1E). A similar result was observed in cdc7-A20 (data not shown). Furthermore, no mitotic hyperphosphorylation of cdc11p was seen in spg1-B8 at the nonpermissive temperature (Figure 1E), when cdc7p does not localize to the SPB [13]. Finally, when cdc7 was expressed ectopically in G2-arrested cells, cdc11p accumulated in the hyperphosphorylated form (3) (Figure 1F).
PMID:12546793	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC21.06c [has_penetrance] 90	Less than 10% of these cells had cdc7p on the spindle pole body, consistent with previous studies [25].
PMID:12565823	FYPO:0001035	increased cell wall thickness during vegetative growth	(Fig. 4a)
PMID:12565827	GO:0031097	medial cortex [exists_during] mitotic M phase	(Fig. 2C)
PMID:12565827	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	(Fig. 2C)
PMID:12569356	FYPO:0003183	normal growth on phleomycin	(Figure 4a). In contrast, treatment of hob3D cells did not produce a hypersensitive phenotype.
PMID:12569356	FYPO:0001492	viable elongated vegetative cell [has_severity] low	Microscopic examination of hob1D cells revealed them to be slightly but not significantly elongated, relative to an isogenic hob1+ strain (Figure 2b).
PMID:12569356	FYPO:0001357	normal vegetative cell population growth [has_severity] low	On nitrogen-poor medium or on medium of high osmolarity (i.e. YE/250 mm NaCl), we observed no differences in the growth of hob1+ and hob1D cells (Figure 2c).
PMID:12569356	FYPO:0000426	normal endocytosis [has_severity] low	Thus, unlike RVS167 in budding yeast, hob1+ was dispensable for endocytosis in fission yeast.
PMID:12569356	FYPO:0002344	sensitive to phleomycin [has_severity] low	Treatment of hob1D cells with the DNA strand-breaking drug phleomycin, a bleomycin analog that is cytotoxic to yeasts (Pramanik et al., 1995), resulted in a marked hypersensitivity in hob1D cells (Figure 4a). In
PMID:12569356	FYPO:0000969	normal growth during cellular response to UV	UV irradiation resulted in the same phenotypes as those seen in the case of phleomycin: hob1D cells were more sensitive to the effects of UV irradiation than wild-type cells, while hob3D cells were as resistant to UV as were their wild-type cohorts (Figure 4b).
PMID:12569356	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	UV irradiation resulted in the same phenotypes as those seen in the case of phleomycin: hob1D cells were more sensitive to the effects of UV irradiation than wild-type cells, while hob3D cells were as resistant to UV as were their wild-type cohorts (Figure 4b).
PMID:12589755	FYPO:0000268	sensitive to UV during vegetative growth	(comment: same as crb2delta alone)
PMID:12604790	GO:1904931	MCM complex binding	(comment: assayed with other MCM subunits present)
PMID:12606573	FYPO:0000091	sensitive to thiabendazole	(Figure 3A) during spindle checkpoint
PMID:12606573	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Figure 4E)
PMID:12606573	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Figure 7A)
PMID:12606573	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Figure 7A)
PMID:12606573	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Figure 7A)
PMID:12606573	FYPO:0005042	normal protein localization to kinetochore [assayed_protein] PomBase:SPCC1322.12c	(Figure 7A)
PMID:12606573	FYPO:0007854	normal protein localization to kinetochore during meiotic anaphase I [assayed_protein] PomBase:SPCC1322.12c	(Figure 7B)
PMID:12606573	FYPO:0007854	normal protein localization to kinetochore during meiotic anaphase I [assayed_protein] PomBase:SPCC1322.12c	(Figure 7B)
PMID:12606573	FYPO:0007662	abolished protein localization to kinetochore during meiotic anaphase I [assayed_protein] PomBase:SPBC29A10.14	(Figure 7C,a)
PMID:12606573	FYPO:0007745	abnormal spindle assembly during meiosis I [has_severity] high	(comment: decreased rate of spindle phase I elongation (70 mins. vs 40 wt))
PMID:12606573	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPCC1322.12c [happens_during] mitotic M phase [part_of] positive regulation of mitotic cell cycle spindle assembly checkpoint	(comment: in vitro assay for activity, phenotype for process)
PMID:12606573	GO:0000775	chromosome, centromeric region [exists_during] meiotic anaphase I	In zygotes undergoing meiotic divisions, WT Bub1±GFPp became associated with the centromeres after meiotic prophase and remained associated until anaphase I, con®rming previous reports using ®xed cells (Bernard et al., 2001; Figure 7B, WT, f±h).
PMID:12606573	GO:0000775	chromosome, centromeric region [exists_during] meiotic metaphase I	In zygotes undergoing meiotic divisions, WT Bub1±GFPp became associated with the centromeres after meiotic prophase and remained associated until anaphase I, con®rming previous reports using ®xed cells (Bernard et al., 2001; Figure 7B, WT, f±h).
PMID:12606573	FYPO:0007745	abnormal spindle assembly during meiosis I [has_severity] high	normal rate of spindle phase I elongation. MI spindle elongation time is reduced to 40 min in rec7-146 bub1D cells (Figure 8Ad, upper panel)
PMID:12631727	GO:0005789	endoplasmic reticulum membrane	Fig. 2. Localization of Spo14 to the ER membrane.
PMID:12631727	GO:0006888	endoplasmic reticulum to Golgi vesicle-mediated transport	Overproduction of psr1(+) coding for an S. pombe Sar1 homologue suppressed both the sporulation defect of spo14-B221 and cold-sensitive growth of newly isolated spo14-6 and spo14-7 mutants. These results indicate that Spo14 is involved in early steps of the protein secretory pathway.
PMID:12631727	GO:0032120	ascospore-type prospore membrane formation	Overproduction of psr1(+) coding for an S. pombe Sar1 homologue suppressed both the sporulation defect of spo14-B221 and cold-sensitive growth of newly isolated spo14-6 and spo14-7 mutants. These results indicate that Spo14 is involved in early steps of the protein secretory pathway.
PMID:12653962	FYPO:0000673	normal septum assembly [has_penetrance] 15	(Fig. 6B)
PMID:12653962	FYPO:0005055	binucleate multiseptate cell, septa grouped [has_penetrance] 15	(Fig. 6B)
PMID:12653962	FYPO:0005055	binucleate multiseptate cell, septa grouped [has_penetrance] 15	(Fig. 6B)
PMID:12653962	FYPO:0000673	normal septum assembly [has_penetrance] 15	(Fig. 6B)
PMID:12654901	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells	(Fig. 2)
PMID:12654901	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells	(Fig. 2)
PMID:12654901	FYPO:0000223	elongated multiseptate vegetative cell [has_penetrance] 5	(Fig. 2) (comment: maximum 3 septa)
PMID:12654901	FYPO:0000223	elongated multiseptate vegetative cell [has_penetrance] ~4	(Fig. 2) (comment: maximum 3 septa)
PMID:12654901	FYPO:0004097	normal actomyosin contractile ring contraction	(Fig. 3)
PMID:12654901	FYPO:0006399	abnormal septin ring morphology	(Fig. 4, B and C)
PMID:12654901	GO:0036391	medial cortex septin ring	(Fig. 6)
PMID:12654901	GO:0032176	split septin rings	(Fig. 6)
PMID:12654901	GO:0036391	medial cortex septin ring	(Fig. 6)
PMID:12654901	GO:0032176	split septin rings	(Fig. 6)
PMID:12654901	FYPO:0007028	normal protein localization to medial cortex septin ring during vegetative growth [assayed_using] PomBase:SPAC9G1.11c	(Fig. 7)
PMID:12654901	FYPO:0007027	abolished protein localization to medial cortex, with protein mislocalized to cytoplasm, during vegetative growth [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 7a)
PMID:12654901	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells	(Fig. 7b)
PMID:12654901	FYPO:0007027	abolished protein localization to medial cortex, with protein mislocalized to cytoplasm, during vegetative growth [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 7c)
PMID:12654901	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 8)
PMID:12654901	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC4B3.15	(Fig. 8)
PMID:12654901	FYPO:0001420	normal vegetative cell population growth rate	DNS
PMID:12654901	FYPO:0000674	normal cell population growth at high temperature	DNS
PMID:12654901	FYPO:0002141	normal cell population growth at low temperature	DNS
PMID:12654901	FYPO:0001022	normal growth during cellular response to high osmolarity	DNS
PMID:12654901	FYPO:0001037	normal growth during cellular response to salt stress	DNS
PMID:12654901	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells	data not shown
PMID:12654901	FYPO:0004652	normal actomyosin contractile ring morphology	exhibited well-defined, normal actin rings
PMID:12668659	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells	(Fig. 1)
PMID:12668659	FYPO:0002060	viable vegetative cell population	(Fig. 1)
PMID:12668659	FYPO:0000339	mislocalized septum during vegetative growth	(Fig. 1)
PMID:12668659	GO:0031097	medial cortex	(Fig. 2a)
PMID:12668659	GO:0036391	medial cortex septin ring	(Fig. 2a) colocalizes with sep3
PMID:12668659	FYPO:0000912	abolished protein ubiquitination during vegetative growth [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 3)
PMID:12668659	FYPO:0000912	abolished protein ubiquitination during vegetative growth [assayed_using] PomBase:SPBC14C8.01c	(Fig. 3)
PMID:12668659	FYPO:0002635	normal protein ubiquitination during vegetative growth [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 3)
PMID:12668659	FYPO:0002635	normal protein ubiquitination during vegetative growth [assayed_using] PomBase:SPBC14C8.01c	(Fig. 3)
PMID:12668659	FYPO:0004503	increased cellular HMW ubiquitin conjugate level [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 3A, lanes 1 and 7)
PMID:12668659	FYPO:0004503	increased cellular HMW ubiquitin conjugate level [assayed_using] PomBase:SPBC14C8.01c	(Fig. 3A, lanes 1 and 7) (control)
PMID:12668659	FYPO:0004503	increased cellular HMW ubiquitin conjugate level [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 3C)
PMID:12668659	FYPO:0004503	increased cellular HMW ubiquitin conjugate level [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 3C)
PMID:12668659	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 4)
PMID:12668659	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 4)
PMID:12668659	FYPO:0007027	abolished protein localization to medial cortex, with protein mislocalized to cytoplasm, during vegetative growth [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 5)
PMID:12668659	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells	(Fig. 5)
PMID:12668659	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells	(Fig. 5)
PMID:12668659	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells	(Fig. 5)
PMID:12668659	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells	(Fig. 5)
PMID:12668659	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 5)
PMID:12668659	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 5)
PMID:12668659	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 5)
PMID:12668659	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells [has_severity] low	(Fig. 5)
PMID:12668659	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells	(Fig. 5)
PMID:12668659	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAPYUG7.03c	(Fig. 7D)
PMID:12668659	FYPO:0006821	slow vegetative cell growth	(Fig. 8)
PMID:12668659	FYPO:0000021	spheroid vegetative cell	(Fig. 8)
PMID:12668659	FYPO:0001492	viable elongated vegetative cell	(Fig. 8)
PMID:12668659	FYPO:0001234	slow vegetative cell population growth	(Fig. 8)
PMID:12668659	FYPO:0000132	abnormal septum disassembly	(Fig. 8)
PMID:12668659	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPAPYUG7.03c	unpublished observation
PMID:12668659	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPAPYUG7.03c	unpublished observation
PMID:12676088	GO:0008047	enzyme activator activity [has_input] PomBase:SPBC29A3.14c	(comment: CHECK telomerase regulator)
PMID:12697806	FYPO:0002687	normal telomere length during vegetative growth	(comment: after 100 generations)
PMID:12715160	FYPO:0001490	inviable elongated vegetative cell	(comment: salt stres)
PMID:12715160	FYPO:0000118	multiseptate vegetative cell [has_penetrance] low	(comment: salt stress)
PMID:12719471	FYPO:0003217	decreased chromatin silencing at centromere central core	(comment: CHECK abolished)
PMID:12719471	FYPO:0000732	short bipolar mitotic spindle	(comment: CHECK at anaphase?)
PMID:12719471	FYPO:0000732	short bipolar mitotic spindle	(comment: at anaphase?)
PMID:12748297	GO:0005730	nucleolus [exists_during] meiotic cell cycle phase	ChIP assay indicated that Rad21 associates with ribosomal DNA (rDNA) rather than telomere-associated sequences (see below). Moreover, fluorescence microscopy revealed that Rad21 tagged with GFP colocalizes mostly with a nucleolar protein, Gar1 (3), tagged with CFP in the horsetail nucleus (Fig. 1A). These results suggest that Rad21 is enriched in the nucleolus, rather than telomere-adjacent DNA sequences, although residual association with other chromosomal regions might also occur
PMID:12748297	FYPO:0003177	abnormal meiotic homologous chromosome biorientation [has_penetrance] 40	The rad21-K1 mutation by itself showed no meiotic defect. However, when rec8 was combined with rad21-K1, the equational segregation at meiosis I was partly disrupted with the reductional population increasing to ∼40% (Fig. 2B).
PMID:12748297	GO:0045143	homologous chromosome segregation	We conclude that Rad21 plays a role in ensuring equational segregation during meiosis I in rec8 cells.
PMID:12750522	FYPO:0002219	normal chromosome disjunction at meiosis I	(Figure 1B)
PMID:12750522	FYPO:0002219	normal chromosome disjunction at meiosis I	(Figure 1B)
PMID:12750522	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] 100	(Figure 1B)
PMID:12750522	FYPO:0000670	abnormal mitotic sister chromatid separation	(comment: CHECK ******premature sister kinetochore separation in meiosis I********) Reinforcing the foregoing results, clr4 cells frequently display precocious separation of cen2-GFP signals (Fig. 3C) and a decreased level of Rec8 at the centromeres if arrested after meiosis I (Fig. 3D).
PMID:12750522	FYPO:0005167	decreased protein localization to chromatin at centromere inner repeat [assayed_protein] PomBase:SPBC29A10.14	(comment: CHECK MEIOTIC!********************) The level of Rec8 association with pericentromeric regions is markedly reduced in these mutants, whereas Rec8 is still enriched at the central core (Fig. 3A).
PMID:12750522	FYPO:0006818	decreased protein localization to chromatin at centromere outer repeat [assayed_protein] PomBase:SPBC29A10.14	(comment: CHECK MEIOTIC!***********************) The level of Rec8 association with pericentromeric regions is markedly reduced in these mutants, whereas Rec8 is still enriched at the central core (Fig. 3A).
PMID:12750522	FYPO:0005167	decreased protein localization to chromatin at centromere inner repeat [assayed_protein] PomBase:SPBC29A10.14	(comment: CHECK MEIOTIC!MEIOTIC!***********************) The level of Rec8 association with pericentromeric regions is markedly reduced in these mutants, whereas Rec8 is still enriched at the central core (Fig. 3A).
PMID:12750522	FYPO:0006818	decreased protein localization to chromatin at centromere outer repeat [assayed_protein] PomBase:SPBC29A10.14	(comment: CHECK MEIOTIC!MEIOTIC!***********************) The level of Rec8 association with pericentromeric regions is markedly reduced in these mutants, whereas Rec8 is still enriched at the central core (Fig. 3A).
PMID:12750522	FYPO:0005079	normal protein localization to chromatin at centromere central core [assayed_protein] PomBase:SPBC29A10.14	(comment: CHECK MEIOTIC!MEIOTIC.*************) whereas Rec8 is still enriched at the central core (Fig. 3A).
PMID:12750522	FYPO:0005079	normal protein localization to chromatin at centromere central core [assayed_protein] PomBase:SPBC29A10.14	(comment: CHECK MEIOTIC!MEIOTIC.*************) whereas Rec8 is still enriched at the central core (Fig. 3A).
PMID:12750522	GO:0000793	condensed chromosome [exists_during] meiotic prophase I	At anaphase of meiosis I, Rec11 signals become faint in the nucleus
PMID:12750522	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase II	At anaphase of meiosis I, Rec11 signals become faint in the nucleus, but Psc3 persists, together with Rec8, at the clustered centromeres (Fig. 2C). The centromeric Rec8-Psc3 dots disappear at meiosis II.
PMID:12750522	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase II	At anaphase of meiosis I, Rec11 signals become faint in the nucleus, but Psc3 persists, together with Rec8, at the clustered centromeres (Fig. 2C).The centromeric Rec8-Psc3 dots disappear at meiosis II.
PMID:12750522	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] 20	At meiosis II, however, sisters fail to segregate properly, undergoing nondisjunction in 20 to 40% of cells (Fig. 3B).
PMID:12750522	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] 40	At meiosis II, however, sisters fail to segregate properly, undergoing nondisjunction in 20 to 40% of cells (Fig. 3B). The defect in meiosis II is more penetrating in clr4 cells than in swi6 cells, with a pattern approximating random segregation.
PMID:12750522	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase I	During meiotic prophase, Rec8 first appears at thecentromeres and later distributes throughout thechromosome (Fig. 2A) The data reveal that Rec8 associates more with centromere regions than with chromosome arms (20)
PMID:12750522	FYPO:0000678	unequal homologous chromosome segregation [has_penetrance] 20	Experiments in which cen3 were marked with GFP on both homologs revealed that >20% of rec11Δ cells exhibit homolog nondisjunction, in which both homolog pairs move to the same pole at meiosis I (Fig. 1C).
PMID:12750522	FYPO:0002093	decreased meiotic sister chromatid cohesion [has_severity] high	However, rec11Δ cells often contain three or four cut3-GFP dots (Fig. 1A), representing dissociation in these regions, as observed in rec11Δ cells.
PMID:12750522	FYPO:0000488	normal meiotic recombination	In contrast to the dramatic reduction of meiotic recombination in rec11 cells, wild-type levels of recombination occur in psc3-2T cells (fig. S2D).
PMID:12750522	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase I	In contrast, Psc3 associates exclusively with the centromere, showing a centromere-enrichment ratio 4 times higher than Rec8 and 20 times higher than Rec11 (Fig. 2B).
PMID:12750522	FYPO:0001355	decreased vegetative cell population growth	In contrast, the Rec8-Rec11 pair sustains mitotic growth better than Rec8-Psc3 (Fig. 1D; fig. S4A), underscoring the meiosis specificity of kinetochore regulation by Rec8-Psc3.
PMID:12750522	FYPO:0006426	normal attachment of spindle microtubules to kinetochore during meiosis I	In swi6 and clr4 cells marked on one pair of sister chromatids with cen1-GFP, sister chromatid pairs move together to the same nucleus during meiosis I, indicating that monopolar attachment is intact in these mutants (Fig. 3B).
PMID:12750522	FYPO:0006426	normal attachment of spindle microtubules to kinetochore during meiosis I	In swi6 and clr4 cells marked on one pair of sister chromatids with cen1-GFP, sister chromatid pairs move together to the same nucleus during meiosis I, indicating that monopolar attachment is intact in these mutants (Fig. 3B).
PMID:12750522	FYPO:0005509	abnormal meiotic sister chromatid segregation	Indeed, psc3-2T cells show defects in sister chromatid segregation during meiosis (fig. S2E). To
PMID:12750522	FYPO:0006521	abnormal mitotic sister chromatid cohesion	Mitotic cells carrying a temperature-sensitive allele of psc3 (psc3-2T) (18) displayed extensive separation of cut3-GFP dots (Fig. S2B)
PMID:12750522	FYPO:0002219	normal chromosome disjunction at meiosis I	Moreover, homologous chromosomes undergo faithful disjunction at meiosis I in these mutants (Fig. 3C) (17).
PMID:12750522	FYPO:0002219	normal chromosome disjunction at meiosis I	Moreover, homologous chromosomes undergo faithful disjunction at meiosis I in these mutants (Fig. 3C) (17).
PMID:12750522	FYPO:0000485	decreased meiotic recombination [has_severity] high	Moreover, the overexpression of psc3 leads to partial recovery of the arm cohesion defect of rec11 , but the recombination defect remains unimproved (fig. S3).
PMID:12750522	FYPO:0002093	decreased meiotic sister chromatid cohesion [has_severity] medium	Moreover, the overexpression of psc3 leads to partial recovery of the arm cohesion defect of rec11 , but the recombination defect remains unimproved (fig. S3).
PMID:12750522	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 20	Nonrandom segregation of homologs in rec11Δ cells (different from rec12 cells) can be explained by residual levels of recombination (15) and presumably, residual cohesion as well. rec11Δ cells undergo faithful disjunction during meiosis II (fig. S2C), indicating that centromeric cohesion persists through meiosis I.
PMID:12750522	FYPO:0003178	normal meiotic sister chromatid segregation	The control rec8 overexpressing (o.p.) psc3 rec11 cells undergo proper meiotic chromosome segregation, both reductional (meiosis I) and equational (meiosis II).
PMID:12750522	FYPO:0002219	normal chromosome disjunction at meiosis I	The control rec8 overexpressing (o.p.) psc3 rec11 cells undergo proper meiotic chromosome segregation, both reductional (meiosis I) and equational (meiosis II).
PMID:12750522	GO:0051754	meiotic sister chromatid cohesion, centromeric	Thus, Psc3 plays a crucial role in kinetochore regulation at both meiotic divisions, and this function of Psc3 cannot be replaced by overexpression of Rec11.
PMID:12750522	GO:0071962	mitotic sister chromatid cohesion, centromeric	Thus, Psc3 plays a crucial role in kinetochore regulation at both meiotic divisions, and this function of Psc3cannot be replaced by overexpression of Rec11.
PMID:12750522	FYPO:0004159	abnormal homologous chromosome segregation	expression of the Rec8-Rec11 pair sustains viability of rad21 psc3 cells (Fig. 1D), thus allowing meiotic induction in the complete absence of Psc3). However, rec8 o.p. psc3 rec11 o.p. cellsshow defective sister chromatid movement atboth meiotic divisions (Fig. 1D).
PMID:12750522	FYPO:0003182	sister chromatid nondisjunction at meiosis II	expression of the Rec8-Rec11 pair sustains viability of rad21 psc3 cells (Fig. 1D), thus allowing meiotic induction in the complete absence of Psc3However, rec8 o.p. psc3 rec11 o.p. cellsshow defective sister chromatid movement atboth meiotic divisions (Fig. 1D).
PMID:12750522	FYPO:0003613	normal meiotic sister chromatid cohesion during meiotic prophase I	whereas arm cohesion of psc3-2T cells is completely intact during meiotic prophase (fig. S2C).
PMID:12759375	FYPO:0000737	abnormal meiotic spindle assembly	(comment: CHECK meiosis II)
PMID:12764130	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC1604.14c	(Fig. 1) GST tea1 directly phosphorylated by Shk1 in vitro Fig2A GST-tea1 is phosphorylated in vivo in a Shk1 dependent manner
PMID:12764130	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC1223.06	(Fig. 1B,C) demonstrates in vitro kinase activity. 2A in vivo
PMID:12764130	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC1223.06	(Fig. 2B) shk1 K415R mutant is expressed from a weak allele of nmt1 promoter ON but does not say whether it is expressed at wild type levels. pREP4XGST-tea1 is a multi copy plasmid promoter ON
PMID:12764130	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	(Fig. 3A) tea1 delta is a temperature dependent suppressor of loss of skb15
PMID:12764130	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] low	(Fig. 3B) Cells shown a normal tea1 delta morphology
PMID:12764130	FYPO:0003413	inviable branched, elongated, multiseptate vegetative cell [has_penetrance] high	(Fig. 3B) ii
PMID:12764130	FYPO:0005853	aggregated filamentous actin in cytoplasm [has_penetrance] high	(Fig. 4B)
PMID:12764130	FYPO:0002437	thick actin cables [has_severity] high [has_penetrance] 1	(Fig. 4B)
PMID:12764130	FYPO:0001019	monopolar actin cortical patch localization during vegetative growth [has_penetrance] high	(Fig. 4C, D) Cells shown a normal tea1 delta actin morphology
PMID:12764130	FYPO:0004859	increased cell wall polysaccharide level [has_severity] high [has_penetrance] >40	(Fig. 4E)
PMID:12764130	FYPO:0004859	increased cell wall polysaccharide level [has_penetrance] 5	(Fig. 4F) Cells have a similar defect to a tea1 delta cell wall defect
PMID:12764130	FYPO:0000733	long mitotic spindle [has_penetrance] high	(Fig. 5B)
PMID:12764130	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 70	(Fig. 5C, D)
PMID:12764130	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 5	(Fig. 5D)
PMID:12764130	FYPO:0000118	multiseptate vegetative cell [has_penetrance] 40	(Fig. 6B, C)
PMID:12764130	FYPO:0005855	inviable after spore germination, single cell division, multiseptate cell [has_penetrance] >20	(Fig. 6D)
PMID:12764130	FYPO:0001018	abolished NETO [has_penetrance] high	(Fig. 7A)
PMID:12764130	FYPO:0003314	activation of monopolar cell growth at new end [has_penetrance] 95	(Fig. 7B, C) (comment: Penetrance refers to the penetrance of the NTR old-new end growth pattern)
PMID:12764130	FYPO:0004085	decreased vegetative cell growth [has_penetrance] high	(Fig. 8) (comment: CHECK pREP3X tea1 is a multi copy plasmid and is over expressed from the nmt1 promoter)
PMID:12764130	FYPO:0001399	normal mitotic spindle [has_penetrance] high	Data not shown
PMID:12764130	FYPO:0000118	multiseptate vegetative cell [has_penetrance] high	Data not shown. (comment: CHECK pREP3X tea1 is a multi copy plasmid and is over expressed from the nmt1 promoter)
PMID:12773390	FYPO:0002060	viable vegetative cell population	(Fig. 1a)
PMID:12773390	FYPO:0002061	inviable vegetative cell population	(Fig. 1a)
PMID:12773390	FYPO:0002060	viable vegetative cell population	(Fig. 1a)
PMID:12773390	GO:0000785	chromatin [exists_during] mitotic interphase	(Fig. 2)
PMID:12773390	GO:0005654	nucleoplasm [exists_during] mitotic M phase	(Fig. 2)
PMID:12773390	FYPO:0000964	normal growth on thiabendazole	(Fig. 3a)
PMID:12773390	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 3a)
PMID:12773390	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 3a)
PMID:12773390	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 3a)
PMID:12773390	FYPO:0000964	normal growth on thiabendazole	(Fig. 3a)
PMID:12773390	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 3a)
PMID:12773390	FYPO:0003241	unequal mitotic sister chromatid segregation [has_severity] high [has_penetrance] 48	(Fig. 3b) ((comment: WT 11%)
PMID:12773390	FYPO:0003241	unequal mitotic sister chromatid segregation [has_severity] high [has_penetrance] 52	(Fig. 3b) (comment: WT 11%)
PMID:12773390	FYPO:0001269	abolished protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPBC409.04c	(Fig. 4a)
PMID:12773390	FYPO:0002901	normal protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPBC409.04c	(Fig. 4a)
PMID:12773390	FYPO:0002061	inviable vegetative cell population	(Fig. 6a)
PMID:12773390	FYPO:0002060	viable vegetative cell population	(Fig. 6a)
PMID:12773390	FYPO:0000113	sensitive to staurosporine	(Figure 1E)
PMID:12773390	FYPO:0000113	sensitive to staurosporine	(Figure 1E)
PMID:12773390	FYPO:0000113	sensitive to staurosporine	(Figure 1E)
PMID:12773390	FYPO:0000113	sensitive to staurosporine	(Figure 1E)
PMID:12773390	GO:0005515	protein binding	(Figure 1F)
PMID:12773390	GO:0005515	protein binding	(Figure 1F)
PMID:12773390	FYPO:0002060	viable vegetative cell population	(Figure 1a)
PMID:12773390	FYPO:0002061	inviable vegetative cell population	(Figure 1a)
PMID:12773390	FYPO:0002061	inviable vegetative cell population	(Figure 1a)
PMID:12773390	FYPO:0002106	viable stubby vegetative cell	(Figure 1b) (comment: is described as a pear, but is cylindrical short and wide....)
PMID:12773390	GO:1905561	positive regulation of kinetochore assembly [has_input] PomBase:SPBC409.04c	(Figure 4A and B)
PMID:12773390	GO:1905560	negative regulation of kinetochore assembly	(Figure 4A and B)
PMID:12773390	GO:0000785	chromatin	(Figure 5B)
PMID:12773390	MOD:00047	O-phospho-L-threonine	(Figure 7A and B)
PMID:12773390	MOD:00046	O-phospho-L-serine	(Figure 7A and B)
PMID:12773390	MOD:00046	O-phospho-L-serine	(Figure 7A and B)
PMID:12773392	GO:0004407	histone deacetylase activity	Af®nity-puri®ed Clr6-HA and control wild-type fractions were incubated with [3H]acetyllabelled histones. Quantitation of released [3H]acetyl groups revealed that the Clr6-HA fraction possesses deacetylase activity and that this activity is sensitive to trichostatin A (TSA), a speci®c inhibitor of HDACs (Figure 1C).
PMID:12773392	FYPO:0005308	increased histone H4-K8 acetylation during vegetative growth	Cells carrying Dalp13 were speci®cally defective in the removal of acetyl groups present on H3 Lys9 and Lys14, as well as H4 Lys5 and Lys8.
PMID:12773392	FYPO:0005310	increased histone H3-K14 acetylation during vegetative growth	Cells carrying Dalp13 were speci®cally defective in the removal of acetyl groups present on H3 Lys9 and Lys14, as well as H4 Lys5 and Lys8.
PMID:12773392	FYPO:0000892	increased histone H3-K9 acetylation during vegetative growth	Cells carrying Dalp13 were speci®cally defective in the removal of acetyl groups present on H3 Lys9 and Lys14, as well as H4 Lys5 and Lys8.
PMID:12773392	FYPO:0005309	increased histone H4-K5 acetylation during vegetative growth	Cells carrying Dalp13 were speci®cally defective in the removal of acetyl groups present on H3 Lys9 and Lys14, as well as H4 Lys5 and Lys8.
PMID:12773392	GO:0032221	Rpd3S complex	Identi®cation of Clr6-associated proteins, (Figure 1B) /Alp13, Prw1 and Pst2 are stably associated with Clr6 in vivo (Figure 3A)
PMID:12773392	GO:0032221	Rpd3S complex	Identi®cation of Clr6-associated proteins, (Figure 1B)/ Alp13, Prw1 and Pst2 are stably associated with Clr6 in vivo (Figure 3A)
PMID:12773392	GO:0032221	Rpd3S complex	Identi®cation of Clr6-associated proteins, (Figure 1B)/Alp13, Prw1 and Pst2 are stably associated with Clr6 in vivo (Figure 3A)
PMID:12773392	GO:0032221	Rpd3S complex	Identi®cation of Clr6-associated proteins, (Figure 1B)/Alp13, Prw1 and Pst2 are stably associated with Clr6 in vivo (Figure 3A)
PMID:12773392	FYPO:0007631	increased histone H4-K12 acetylation during vegetative growth	Interestingly, we noticed that Dprw1 causes an increase in the acetylation of H4 Lys5 and Lys12, a pattern of acetylation known to be associated with newly synthesized histones (Sobel et al., 1995).
PMID:12773392	FYPO:0005309	increased histone H4-K5 acetylation during vegetative growth	Interestingly, we noticed that Dprw1 causes an increase in the acetylation of H4 Lys5 and Lys12, a pattern of acetylation known to be associated with newly synthesized histones (Sobel et al., 1995).
PMID:12773392	FYPO:0005310	increased histone H3-K14 acetylation during vegetative growth	Moreover, Dprw1 cells showed an increase in acetylation of H3 Lys9 and Lys14.
PMID:12773392	FYPO:0000892	increased histone H3-K9 acetylation during vegetative growth	Moreover, Dprw1 cells showed an increase in acetylation of H3 Lys9 and Lys14.
PMID:12773392	GO:0005634	nucleus	Our analyses showed that all four proteins were localized predominantly in the nucleus on chromatin but excluded from the nucleolus (Figure 4A and B).
PMID:12773392	GO:0005634	nucleus	Our analyses showed that all four proteins were localized predominantly in the nucleus on chromatin but excluded from the nucleolus (Figure 4A and B).
PMID:12773392	GO:0005634	nucleus	Our analyses showed that all four proteins were localized predominantly in the nucleus on chromatin but excluded from the nucleolus (Figure 4A and B).
PMID:12773392	GO:0005634	nucleus	Our analyses showed that all four proteins were localized predominantly in the nucleus on chromatin but excluded from the nucleolus (Figure 4A and B).
PMID:12773392	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] high	Our analysis revealed that mutant strains display defects in the segregation, resolution and/or condensation of chromosomes during mitosis (Figure 6A), and mis-segregated the mini-chromosome Ch16 (a 530 kb derivative of chromosome 3; Niwa et al., 1986) at a signi®cantly higher rate than wild-type cells (Figure 6C).
PMID:12773392	FYPO:0005046	abnormal mitotic sister chromatid segregation with lagging chromosomes, complete sister chromatid separation, and decreased rate of mitotic spindle elongation [has_severity] medium	Our analysis revealed that mutant strains display defects in the segregation, resolution and/or condensation of chromosomes during mitosis (Figure 6A), and mis-segregated the mini-chromosome Ch16 (a 530 kb derivative of chromosome 3; Niwa et al., 1986) at a signi®cantly higher rate than wild-type cells (Figure 6C).
PMID:12773392	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] high	Our analysis revealed that mutant strains display defects in the segregation, resolution and/or condensation of chromosomes during mitosis (Figure 6A), and mis-segregated the mini-chromosome Ch16 (a 530 kb derivative of chromosome 3; Niwa et al., 1986) at a signi®cantly higher rate than wild-type cells (Figure 6C).
PMID:12773392	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] high	Our analysis revealed that mutant strains display defects in the segregation, resolution and/or condensation of chromosomes during mitosis (Figure 6A), and mis-segregated the mini-chromosome Ch16 (a 530 kb derivative of chromosome 3; Niwa et al., 1986) at a signi®cantly higher rate than wild-type cells (Figure 6C).
PMID:12773392	FYPO:0007631	increased histone H4-K12 acetylation during vegetative growth	The Dpst2 cells showed a signi®cant increase in acetylation of most lysine residues on H3 and H4 tails, except H4 Lys8.
PMID:12773392	FYPO:0000892	increased histone H3-K9 acetylation during vegetative growth	The Dpst2 cells showed a signi®cant increase in acetylation of most lysine residues on H3 and H4 tails, except H4 Lys8.
PMID:12773392	FYPO:0005310	increased histone H3-K14 acetylation during vegetative growth	The Dpst2 cells showed a signi®cant increase in acetylation of most lysine residues on H3 and H4 tails, except H4 Lys8.
PMID:12773392	FYPO:0007632	increased histone H4-K16 acetylation during vegetative growth	The Dpst2 cells showed a signi®cant increase in acetylation of most lysine residues on H3 and H4 tails, except H4 Lys8.
PMID:12773392	FYPO:0002363	increased histone H3 acetylation during vegetative growth	The results presented in Figure 5E demonstrate that mutant strains show a signi®cant increase in histone acetylation levels compared with the wild-type control. Mutation in clr6 results in elevated acetylation levels at all residues tested on the histone H3 and H4 tails.
PMID:12773392	FYPO:0002365	increased histone H4 acetylation during vegetative growth	The results presented in Figure 5E demonstrate that mutant strains show a signi®cant increase in histone acetylation levels compared with the wild-type control. Mutation in clr6 results in elevated acetylation levels at all residues tested on the histone H3 and H4 tails.
PMID:12773392	GO:0140937	histone H4K12 deacetylase activity, hydrolytic mechanism	These data suggest that Clr6 and its associated factors are involved in the deacetylation of histones in vivo.
PMID:12773392	GO:0032129	histone H3K9 deacetylase activity, hydrolytic mechanism	These data suggest that Clr6 and its associated factors are involved in the deacetylation of histones in vivo.
PMID:12773392	GO:0034739	histone H4K16 deacetylase activity, hydrolytic mechanism	These data suggest that Clr6 and its associated factors are involved in the deacetylation of histones in vivo.
PMID:12773392	GO:0031078	histone H3K14 deacetylase activity, hydrolytic mechanism	These data suggest that Clr6 and its associated factors are involved in the deacetylation of histones in vivo.
PMID:12773392	FYPO:0008183	decreased histone H3-S10 phosphorylation during vegetative growth	We found that H3 Ser10 phosphorylation levels were considerably reduced in alp13, pst2 and clr6 mutant cells, except at 2±3 foci near the nuclear periphery, presumably representing heterochromatic loci (Figure 7)
PMID:12773392	FYPO:0008183	decreased histone H3-S10 phosphorylation during vegetative growth	We found that H3 Ser10 phosphorylation levels were considerably reduced in alp13, pst2 and clr6 mutant cells, except at 2±3 foci near the nuclear periphery, presumably representing heterochromatic loci (Figure 7)
PMID:12773392	FYPO:0000082	decreased cell population growth at high temperature	and irreversible temperature-sensitive (Ts±) growth defects (Figure 5B±D).
PMID:12773392	FYPO:0000082	decreased cell population growth at high temperature	and irreversible temperature-sensitive (Ts±) growth defects (Figure 5B±D).
PMID:12773392	FYPO:0000082	decreased cell population growth at high temperature	and irreversible temperature-sensitive (Ts±) growth defects (Figure 5B±D).
PMID:12773392	FYPO:0000082	decreased cell population growth at high temperature	and irreversible temperature-sensitive (Ts±) growth defects (Figure 5B±D).
PMID:12773392	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0000095	sensitive to bleomycin [has_severity] high	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0000095	sensitive to bleomycin [has_severity] high	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0000095	sensitive to bleomycin [has_severity] high	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0000095	sensitive to bleomycin [has_severity] medium	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773392	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	sensitivity to DNA-damaging agents [such as UV, methyl methane- sulfonate (MMS) and bleomycin] (Figure 5B±D)
PMID:12773576	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(Figure 6A, 6B)
PMID:12773576	FYPO:0005310	increased histone H3-K14 acetylation during vegetative growth	(Figure 6C)
PMID:12773576	FYPO:0001859	increased minichromosome loss	(Figure 6C)
PMID:12773576	FYPO:0004238	increased histone H3-K4 acetylation during vegetative growth	(Figure 6C)
PMID:12773576	FYPO:0000892	increased histone H3-K9 acetylation during vegetative growth	(Figure 6C)
PMID:12773576	FYPO:0006990	increased spatial extent of heterochromatin assembly at protein coding gene [assayed_region] mating_type_region	(comment: CHECK increased spatial extent of heterochromatin assembly) (comment: JUST)
PMID:12773576	FYPO:0006990	increased spatial extent of heterochromatin assembly at protein coding gene [assayed_region] mating_type_region	(comment: CHECK increased spatial extent of heterochromatin assembly) (comment: JUST, not at prpote4in coding gene!)
PMID:12773576	FYPO:0006991	normal spatial extent of heterochromatin assembly at protein coding gene [assayed_region] mating_type_region	(comment: CHECK normal spatial extent of heterochromatin assembly (comment: JUST)
PMID:12773576	FYPO:0004948	increased spatial extent of centromeric heterochromatin assembly [assayed_region] mating_type_region	(comment: outer repeats)
PMID:12789340	FYPO:0007450	decreased maintenance of protein location in cell cortex of cell tip [assayed_using] PomBase:SPCC1223.06	(comment: inferred from combination of FYPO:0005798 and FYPO:0005828)
PMID:12791993	FYPO:0003126	post-anaphase array absent from cell	(Fig. 1A)
PMID:12791993	FYPO:0006004	normal interphase microtubule organization	(Fig. 1A)
PMID:12791993	FYPO:0005689	inviable binucleate aseptate cell with mitotic cell cycle arrest before cell separation	(Fig. 1B) (comment: cell cycle arrest with post anaphase microtubule array)
PMID:12791993	FYPO:0003838	abolished actomyosin contractile ring contraction	(Fig. 1B, C) Cells arrest with a stable actinomyosin ring and fail to undergo cytokinesis
PMID:12791993	FYPO:0001400	normal interphase microtubules	(Fig. 2 E,F)
PMID:12791993	FYPO:0003126	post-anaphase array absent from cell	(Fig. 2 E,F)
PMID:12791993	FYPO:0002026	actomyosin contractile ring displaced from midpoint [has_penetrance] 30-40	(Fig. 3A)
PMID:12791993	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC1F5.04c	(Fig. 3C)
PMID:12791993	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC926.03	(Fig. 3C)
PMID:12791993	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPCC645.05c	(Fig. 3C)
PMID:12791993	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAP8A3.08	(Fig. 3C)
PMID:12791993	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPCC4B3.15	(Fig. 3E)
PMID:12791993	FYPO:0002557	decreased protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC4B3.15 [has_severity] high	(Fig. 3E)
PMID:12791993	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPCC4B3.15	(Fig. 3E,F)
PMID:12791993	FYPO:0006005	normal actomyosin contractile ring localization	(Fig. 4C) (displacemetn is supressed by inhibiting membrane trafficking
PMID:12791993	FYPO:0002026	actomyosin contractile ring displaced from midpoint	(Fig. 4D)
PMID:12791993	FYPO:0003245	telophase nuclear clustering	(Fig. 4D, E, F)
PMID:12791993	FYPO:0003303	mislocalized post-anaphase array	(Fig. 4D, E, F)
PMID:12791993	FYPO:0006004	normal interphase microtubule organization	data not shown
PMID:12791993	FYPO:0003126	post-anaphase array absent from cell	data not shown
PMID:12791993	FYPO:0003126	post-anaphase array absent from cell	data not shown
PMID:12791993	FYPO:0006004	normal interphase microtubule organization	data not shown
PMID:12796476	FYPO:0001493	inviable elongated multinucleate vegetative cell	(Figure 1D) arrested after 􏰖24 h (Fig. 1 E)
PMID:12796476	FYPO:0001008	actomyosin contractile ring absent [has_penetrance] high	(Figure 1D) but lacked both actin contractile rings and polarized actin patches (Fig. 1 D)
PMID:12796476	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth	(Figure 1D) but lacked both actin contractile rings and polarized actin patches (Fig. 1 D)
PMID:12796476	FYPO:0002437	thick actin cables	(Figure 1D) impressive enrichment of actin filaments in aberrant thick cables and aster-like accumulations
PMID:12796476	FYPO:0005853	aggregated filamentous actin in cytoplasm	(Figure 1D) impressive enrichment of actin filaments in aberrant thick cables and aster-like accumulations
PMID:12796476	FYPO:0003210	mislocalized, misoriented septum	(comment: CHECK abnormal (partial, broad, and misoriented) septa) (Fig. 1 G)
PMID:12796476	GO:0051016	barbed-end actin filament capping	(comment: MF?)
PMID:12796476	GO:0098772	molecular function regulator activity [has_input] PomBase:SPAC1F5.04c	(comment: actin binding inhibitor pointed end)
PMID:12796476	GO:0051015	actin filament binding	(comment: barbed end actin capping)
PMID:12796476	FYPO:0001357	normal vegetative cell population growth	(comment: control, functional fragment)
PMID:12796476	FYPO:0002061	inviable vegetative cell population	Thus, Cdc12(FH1FH2)p can replace the essential functions of Cdc12p in vivo when Cdc12p is nonfunctional, but is toxic when overexpressed in the presence of functional Cdc12p.
PMID:12796476	GO:0030041	actin filament polymerization	fission yeast Cdc12 (FH1FH2)p purified from bacteria (Fig. 1 B) stimulated actin polymerization, as detailed below (see Fig. 4). This is consistent with Cdc12(FH1FH2)p and MmCPcapping the barbed (fast depolymerizing) ends of the filaments with high affinity (Kd + 0.1 􏰂M), allowing dissociation only from the slowly depolymerizing (Pollard, 1986) pointed ends (Caldwell et al., 1989)
PMID:12805221	MOD:00046	O-phospho-L-serine	(comment: CHECK referred to in PMID:33137119)
PMID:12808043	GO:0000228	nuclear chromosome [exists_during] meiosis I	(comment: dependent on sme2 expression)
PMID:12810074	GO:0005737	cytoplasm	Comparison of mitochondria staining with GFP-Ung1 showed no detectable co-localization of Ung1 and mitochondria (Fig. 1B, right). Thus, these cellular localization studies indicate that fission yeast Ung1 is more similar to the nuclear form of human UNG as they both localized predominantly in the nucleus
PMID:12815070	FYPO:0005717	normal protein kinase activity during mitosis [assayed_substrate] PomBase:SPAC23C11.16	(Fig. 2A)
PMID:12815070	FYPO:0005717	normal protein kinase activity during mitosis [assayed_substrate] PomBase:SPAC23C11.16	(Fig. 2A)
PMID:12815070	FYPO:0005717	normal protein kinase activity during mitosis [assayed_substrate] PomBase:SPAC23C11.16	(Fig. 2A)
PMID:12815070	FYPO:0005717	normal protein kinase activity during mitosis [assayed_substrate] PomBase:SPAC23C11.16	(Fig. 2B)
PMID:12815070	FYPO:0002061	inviable vegetative cell population	(Fig. 9A) cdc25.22 and cdc25.22 plo1.ts19 cells, on the other hand, could not form colonies on this medium at this temperature, but cdc25.22 cut12.s11 cells could
PMID:12815070	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05	(Figs. 1A,4C)
PMID:12815070	FYPO:0002061	inviable vegetative cell population	Both plo1.ts2 and plo1.ts19 conferred temperature sensitivity for growth on minimal medium
PMID:12815070	FYPO:0002061	inviable vegetative cell population	Both plo1.ts2 and plo1.ts19 conferred temperature sensitivity for growth on minimal medium
PMID:12815070	FYPO:0007184	increased protein kinase activity during mitosis [assayed_using] PomBase:SPAC23C11.16	Kinase assays of these mitotic samples indicated that the cut12.s11 mutation promoted a 1.6 (±0.18; n = 5) in-crease in Plo1-specific activity during mitosis(Fig. 2D).
PMID:12815070	FYPO:0007183	increased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16	Plo1-associated kinase activity of extracts from arrested cdc2.33 cut12.s11 cells was 2.4-fold(±0.35;n=6)higher than that of the control cdc2.33 cut12+ cells (Fig. 4D). This established that cut12.s11 increased Plo1 activity ininterphase.
PMID:12815070	FYPO:0002823	abolished protein localization to mitotic spindle pole body during interphase [assayed_using] PomBase:SPAC23C11.16	Plo1.K65R, the “kinase dead” mutant protein,only associated with mitotic but not with interphase SPBs(data not shown).
PMID:12815070	FYPO:0001122	elongated vegetative cell [has_severity] variable severity	The extended and more random size of plo1.ts2 cells at division suggested that this may be the case. Despite the fact that these cells are able to enter mitosis,the appear to be doing so in a less efficient, or more random manner (Fig. 8B).
PMID:12815070	FYPO:0002061	inviable vegetative cell population	This established that mutating plo1 in a way that did not affect cell viability compromised the ability of cut12.s11 to suppress cdc25.22. Fig 9A. cdc25.22 and cdc25.22 plo1.ts19 cells, on the other hand, could not form colonies on this medium at this temperature, but cdc25.22 cut12.s11 cells could
PMID:12815070	GO:0030295	protein kinase activator activity [has_input] PomBase:SPAC23C11.16	This suggested that the inability to promote mitotic Plo1-associated kinase activity in cut12.1 cells was not a simple consequence of an inability to assemble a bipolar spindle,or an inability to commit to mitosis.Rather,the data indicate that Cut12 function was required for full activationof Plo1-associated kinase activity during mitotic commitment. Alspp Fig. 6B
PMID:12815070	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	Unlike classic “cut” mutants (Hirano et al. 1986), septation did not always follow on from the mitoticarrest.
PMID:12815070	FYPO:0001382	decreased protein kinase activity [assayed_using] PomBase:SPAC23C11.16	We concluded that the Plo1-dependent kinase activity of both plo1.ts2 and plo1.ts19 was greatly reduced.
PMID:12815070	FYPO:0001382	decreased protein kinase activity [assayed_using] PomBase:SPAC23C11.16	We concluded that the Plo1-dependent kinase activity of both plo1.ts2 and plo1.ts19 was greatly reduced.
PMID:12815070	FYPO:0004083	normal protein level [assayed_using] PomBase:SPAC23C11.16	Western blot analysis showed that Plo1 levels in plo1.ts2cellswerenotradicallydifferentfromwild-type
PMID:12815070	FYPO:0000405	normal mitotic G2/M phase transition [has_penetrance] 11	Whereas cells in which the expression of the constitutively active mutant remained repressed arrested cell cycle progression in interphase, 11% of those in which it had been expressed entered mitosis.This degree of suppression is very similar to the level of suppression of cdc25.22 arising from the presence of the cut12.s11 mutation (Fig. 9B) and established that activation of Plo1 is sufficient to suppress the deficiency in Cdc25 function in cdc25.22 cells.
PMID:12815070	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	Whereas single plo1.ts2 and plo1.ts19 mutant and double cut12.s11 cdc25.22 mutant cells all entered mitosis (Fig. 9B,C), the single cdc25.22 mutant and both double cdc25.22 plo1.ts and triple cut12.s11 cdc25.22 plo1.ts mutants did not.
PMID:12815070	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	Whereas single plo1.ts2 and plo1.ts19 mutant and double cut12.s11 cdc25.22 mutant cells all entered mitosis (Fig. 9B,C), the single cdc25.22 mutant and both double cdc25.22 plo1.ts and triple cut12.s11 cdc25.22 plo1.ts mutants did not.
PMID:12815070	FYPO:0002061	inviable vegetative cell population	ability to form colonies o nrich medium at 36°C was indistinguishable from that of wild-typec ells
PMID:12815070	FYPO:0002060	viable vegetative cell population	ability to form colonies o nrich medium at 36°C was indistinguishable from that of wild-typec ells
PMID:12815070	FYPO:0001984	protein absent from cell during vegetative growth [assayed_using] PomBase:SPAC23C11.16	full-length protein appeared to be largely absent from plo1.ts19 on either minimal or rich medium at either 25°C or 36°C (Fig. 7B)
PMID:12815070	FYPO:0001984	protein absent from cell during vegetative growth [assayed_using] PomBase:SPAC23C11.16	full-length protein appeared to be largely absent from plo1.ts19 on either minimal or rich medium at either 25°C or 36°C (Fig. 7B)
PMID:12815070	FYPO:0001683	abolished mitotic spindle assembly	plo1.ts2 strains entered mitosis but did not form spindles
PMID:12815070	FYPO:0000276	monopolar mitotic spindle	plo1.ts2 strains entered mitosis but did not form spindles
PMID:12815070	FYPO:0002061	inviable vegetative cell population	triple cut12.s11 cdc25.22 plo1.ts19 cells were unable to grow (Fig. 9A).
PMID:12840005	FYPO:0003084	abolished replication fork arrest at mating-type locus	(comment: assayed using RTS1 mut2 or mut8 on plasmid)
PMID:12840005	FYPO:0005356	abolished site-specific DNA replication termination at RTS1 barrier	(comment: assayed using RTS1 mut2 or mut8 on plasmid)
PMID:12840005	FYPO:0003084	abolished replication fork arrest at mating-type locus	(comment: assayed using RTS1 mut2 or mut8 on plasmid)
PMID:12840005	FYPO:0003085	decreased replication fork arrest at mating-type locus [has_severity] medium	(comment: assayed using RTS1 mut2 or mut8 on plasmid)
PMID:12840005	FYPO:0005357	decreased site-specific DNA replication termination at RTS1 barrier [has_severity] high	(comment: assayed using RTS1 mut2 or mut8 on plasmid)
PMID:12840005	FYPO:0005356	abolished site-specific DNA replication termination at RTS1 barrier	(comment: assayed using RTS1 mut2 or mut8 on plasmid)
PMID:12857865	GO:0061496	half bridge of mitotic spindle pole body	(Fig. 2,3)
PMID:12857865	FYPO:0003738	abnormal mitotic cell cycle arrest with condensed chromosomes	(Fig. 4)
PMID:12857865	FYPO:0002061	inviable vegetative cell population	(Fig. 4)
PMID:12857865	FYPO:0000276	monopolar mitotic spindle	(Fig. 4)
PMID:12857865	FYPO:0003165	cut with abnormal chromosome segregation	(Figure 6A)
PMID:12857865	FYPO:0002061	inviable vegetative cell population	(Figure 6A)
PMID:12857865	FYPO:0000608	abnormal cell cycle arrest in mitotic M phase	(Figure 7)
PMID:12857865	FYPO:0005023	inviable elongated septated mononucleate vegetative cell	(Figure 7) (this protrusion is opposite side of nucleus to the SPB)
PMID:12857865	FYPO:0003788	nuclear envelope protrusion present during mitosis	(Figure 7) (this protrusion is opposite side of nucleus to the SPB)
PMID:12857865	FYPO:0002061	inviable vegetative cell population	data not shown
PMID:12857865	FYPO:0002061	inviable vegetative cell population	data not shown
PMID:12861005	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(comment: same as rad51d alone)
PMID:12861005	FYPO:0005402	increased telomeric 3' overhang length during vegetative growth	(comment: same as taz1d alone)
PMID:12861005	FYPO:0005402	increased telomeric 3' overhang length during vegetative growth	(comment: same as taz1d alone)
PMID:12861005	FYPO:0005402	increased telomeric 3' overhang length during vegetative growth	(comment: same as taz1d alone)
PMID:12861005	FYPO:0005402	increased telomeric 3' overhang length during vegetative growth	(comment: same as taz1d alone)
PMID:12861005	FYPO:0005402	increased telomeric 3' overhang length during vegetative growth	(comment: same as taz1d alone)
PMID:12861005	FYPO:0005402	increased telomeric 3' overhang length during vegetative growth	(comment: same as taz1d alone)
PMID:12861005	FYPO:0005402	increased telomeric 3' overhang length during vegetative growth	(comment: same as taz1d alone)
PMID:12867036	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	ChIP analysis showed that the level of Swi6 associated with Kint2::ura4+ was reduced 47-fold in sir2Δ compared to wild-type cells (Figure 3B).
PMID:12867036	FYPO:0007633	increased histone H3-K14 acetylation at silent mating-type cassette during vegetative growth	Compared to wild-type cells, in sir2Δ cells, acetylation of K9 was increased by 16-, 11-, and 7-fold at the ura4+ reporter inserted in the mating locus (Kint2::ura4+), the inner (imr1R::ura4+), and the outer centromeric repeats (otr1R::ura4+), respectively (Figure 3A).
PMID:12867036	FYPO:0004690	increased histone H3-K9 acetylation at silent mating-type cassette during vegetative growth	Compared to wild-type cells, in sir2Δ cells, acetylation of K9 was increased by 16-, 11-, and 7-fold at the ura4+ reporter inserted in the mating locus (Kint2::ura4+), the inner (imr1R::ura4+), and the outer centromeric repeats (otr1R::ura4+), respectively (Figure 3A).
PMID:12867036	FYPO:0006681	increased histone H3-K9 acetylation at centromere inner repeat during vegetative growth	Compared to wild-type cells, in sir2Δ cells, acetylation of K9 was increased by 16-, 11-, and 7-fold at the ura4+ reporter inserted in the mating locus (Kint2::ura4+), the inner (imr1R::ura4+), and the outer centromeric repeats (otr1R::ura4+), respectively (Figure 3A).
PMID:12867036	FYPO:0006814	increased histone H3-K9 acetylation at centromere outer repeat during vegetative growth [has_severity] low	Compared to wild-type cells, in sir2Δ cells, acetylation of K9 was increased by 16-, 11-, and 7-fold at the ura4+ reporter inserted in the mating locus (Kint2::ura4+), the inner (imr1R::ura4+), and the outer centromeric repeats (otr1R::ura4+), respectively (Figure 3A).
PMID:12867036	FYPO:0006815	increased histone H3-K14 acetylation at centromere inner repeat during vegetative growth	Compared to wild-type cells, in sir2Δ cells, acetylation of K9 was increased by 16-, 11-, and 7-fold at the ura4+ reporter inserted in the mating locus (Kint2::ura4+), the inner (imr1R::ura4+), and the outer centromeric repeats (otr1R::ura4+), respectively (Figure 3A).
PMID:12867036	FYPO:0008200	decreased histone H3-K9 methylation at centromere inner repeat during vegetative growth [has_severity] medium	Consistent with its weaker effect on silencing of otr1R::ura4+, deletion of sir2+ had only a weak effect on methylation of this ura4+ reporter (Figure 3B).
PMID:12867036	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] low	Consistent with its weaker effect on silencing of otr1R::ura4+, deletion of sir2+ had only a weak effect on methylation of this ura4+ reporter (Figure 3B).
PMID:12867036	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	Deletion of sir2+ caused derepression of ura4+ at both loci (Figure 2D). However, this effect was much stronger at the imr repeats than at the otr repeats. While sir2Δ cells carrying imr1R::ura4+ did not form colonies on FOA-containing plates, mutant cells carrying otr1R::ura4+ showed appreciable growth on FOA plates (Figure 2D). These results indicated that Sir2 was required for silencing at the S. pombe centromeric DNA regions.
PMID:12867036	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	Deletion of sir2+ caused derepression of ura4+ at both loci (Figure 2D). However, this effect was much stronger at the imr repeats than at the otr repeats. While sir2Δ cells carrying imr1R::ura4+ did not form colonies on FOA-containing plates, mutant cells carrying otr1R::ura4+ showed appreciable growth on FOA plates (Figure 2D). These results indicated that Sir2 was required for silencing at the S. pombe centromeric DNA regions.
PMID:12867036	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	Histone H3-K9 methylation levels at Kint2::ura4+ and imr1R::ura4+ were strongly reduced in sir2Δ compared to sir2+ cells (32- and 13-fold, respectively) (Figure 3B).
PMID:12867036	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	In contrast, sir2Δ L(BglII)::ade6+ cells formed white colonies, indicating loss of silencing of the reporter gene (Figure 2C).
PMID:12867036	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPAC664.01c	Moreover, the level of Swi6 associated with imr1R::ura4+ and otr1R::ura4+ reporters was reduced 8- and 3-fold, respectively, in sir2Δ compared to wild-type cells (Figure 3B).
PMID:12867036	FYPO:0005167	decreased protein localization to chromatin at centromere inner repeat [assayed_protein] PomBase:SPAC664.01c	Moreover, the level of Swi6 associated with imr1R::ura4+ and otr1R::ura4+ reporters was reduced 8- and 3-fold, respectively, in sir2Δ compared to wild-type cells (Figure 3B).
PMID:12867036	FYPO:0006670	meiotic cell cycle entry in haploid cell	We combined the sir2Δ mutant with REIIΔ and found that the sir2Δ REIIΔ double mutant had a strong haploid meiosis phenotype (Figure 2E).
PMID:12867036	FYPO:0000470	decreased mating type switching	We observed a strong reduction in staining of sir2Δ compared to sir2+ cells, which indicated a reduced rate of switching to the opposite mating type in sir2Δ cells (Figure 2E, column 1).
PMID:12867036	GO:0046970	histone H4K16 deacetylase activity, NAD-dependent	spSir2 efficiently deacetylated an H4 peptide with acetyl-lysine at position 16 (AcK16) and an H3 peptide with acetyl-lysine at position 9 (AcK9), compared to H4 peptides with acetyl-lysine at positions 5 (AcK5), 8 (AcK8), and 12 (AcK12) (Figure 1B).
PMID:12867036	GO:0046969	histone H3K9 deacetylase activity, NAD-dependent	spSir2 efficiently deacetylated an H4 peptide with acetyl-lysine at position 16 (AcK16) and an H3 peptide with acetyl-lysine at position 9 (AcK9), compared to H4 peptides with acetyl-lysine at positions 5 (AcK5), 8 (AcK8), and 12 (AcK12) (Figure 1B).
PMID:12868054	FYPO:0000369	vacuoles absent	(Fig. 2b)
PMID:12868054	FYPO:0004483	abnormal vacuole fusion during cellular hypotonic response	(Fig. 3)
PMID:12868054	FYPO:0000583	abolished sporulation	(Fig. 5)
PMID:12868054	FYPO:0005547	decreased protein targeting to vacuole, with protein secreted	(Fig. 6)
PMID:12868054	FYPO:0007286	normal protein localization to late endosome membrane	(Fig. 7) (comment: CHECK prevacuolar compartment membrane)
PMID:12868054	FYPO:0000096	sensitive to cadmium	(Fig. 7a)
PMID:12868054	FYPO:0003656	sensitive to vanadate	(comment: 4 mM)
PMID:12868054	FYPO:0000076	resistance to nystatin	(comment: at 5 μg/ml)
PMID:12868054	FYPO:0002061	inviable vegetative cell population	While both wild-type and vps33Δ cells grew at 26 ◦ C, vps33􏰗 cells exhibited a temperature-sensitive growth at 37 ◦C (Figure 2A).
PMID:12868054	FYPO:0001234	slow vegetative cell population growth [has_severity] high	n liquid YES medium at 27 ◦ C, the cells had a doubling time of ∼8 h, in contrast to 2 h 30 min for wild-type cells.
PMID:12868054	FYPO:0000098	sensitive to calcium [has_severity] high	strong sensitivity to 100 mM CaCl2 (Figure 4A)
PMID:12871901	FYPO:0000611	abnormal cell cycle arrest in mitotic S phase	(comment: CHECK permissive for cdc25-22; restrictive for cdt2-M1)
PMID:12893961	FYPO:0001234	slow vegetative cell population growth	(Fig. 3)
PMID:12893961	FYPO:0002060	viable vegetative cell population	(Fig. 3)
PMID:12893961	FYPO:0002060	viable vegetative cell population	(Fig. 4)
PMID:12893961	FYPO:0002061	inviable vegetative cell population	(Fig. 4)
PMID:12893961	FYPO:0002061	inviable vegetative cell population	(Fig. 4)
PMID:12893961	FYPO:0002060	viable vegetative cell population	(Fig. 4)
PMID:12893961	FYPO:0004009	decreased rRNA transcription	(Fig. 5)
PMID:12894167	GO:0008093	cytoskeletal anchor activity [part_of] protein localization to microtubule	"""These results indicate that Mal3 is required for the proper association of Tea2 with microtubules and suggest that Mal3 stabilizes the kinesin-microtubule interaction"""
PMID:12894167	FYPO:0005464	abnormal maintenance of protein location at cell tip during vegetative growth [assayed_using] PomBase:SPBC1604.20c	(comment: LOCALIZES OK, IS NOT RETAINED)
PMID:12925774	GO:0000785	chromatin [exists_during] mitotic S phase [coincident_with] origin_of_replication	(comment: during mitotic DNA replication initiation)
PMID:12951601	FYPO:0006346	bipolar mitotic spindle with decreased, irregular thickness	(Fig. 1a) (comment: CHECK thinner discontinuous spindles fypo/issues/3208)
PMID:12951601	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint [has_penetrance] 18	(Fig. 1c) cells 1 and 3 Furthermore, multiple Mad2 dots, which have never been seen in wild type cells
PMID:12951601	FYPO:0002061	inviable vegetative cell population	(Fig. 1d)
PMID:12951601	FYPO:0002061	inviable vegetative cell population	(Fig. 1d)
PMID:12951601	FYPO:0002061	inviable vegetative cell population	(Fig. 1d)
PMID:12951601	FYPO:0002061	inviable vegetative cell population	(Fig. 1d)
PMID:12951601	FYPO:0003165	cut with abnormal chromosome segregation	(Fig. 1e)
PMID:12966087	GO:0000724	double-strand break repair via homologous recombination	(comment: CHECK epistasis with Rhp51)
PMID:12966087	GO:0000724	double-strand break repair via homologous recombination	(comment: CHECK epistasis with Rhp51)
PMID:12972434	GO:2000765	regulation of cytoplasmic translation	(comment: pyruvate kinase, thiazole biosynthetic enzyme, and ribosomal protein L25-A)
PMID:12972434	FYPO:0007317	decreased cytoplasmic translation [assayed_using] PomBase:SPBC106.18	These data indicate that the decrease in ribosomal protein L25-A observed in cpc2::ura4 cells is probably due to a defect in recruitment of its mRNA to polyribosomes. The decreased amounts of both sam1 and thi2 RNAs are sufficient to account for the lowered protein abundance of each in cpc2::ura4 cells. In contrast, the decline in the level of ribosomal protein Rpl25 in cpc2::ura4 cells is not likely to be caused by an inability to accumulate its mRNA transcript.
PMID:12972434	FYPO:0007317	decreased cytoplasmic translation [assayed_using] PomBase:SPBC4F6.04	These data indicate that the decrease in ribosomal protein L25-A observed in cpc2::ura4 cells is probably due to a defect in recruitment of its mRNA to polyribosomes. The decreased amounts of both sam1 and thi2 RNAs are sufficient to account for the lowered protein abundance of each in cpc2::ura4 cells. In contrast, the decline in the level of ribosomal protein Rpl25 in cpc2::ura4 cells is not likely to be caused by an inability to accumulate its mRNA transcript.
PMID:12972571	GO:0000785	chromatin [exists_during] mitotic anaphase	(comment: CHECK ADD? late anaphase)
PMID:12972571	GO:0000785	chromatin [exists_during] G1/S transition of mitotic cell cycle	(comment: CHECK ADD? late anaphase)
PMID:12972571	GO:0000785	chromatin [exists_during] single-celled organism vegetative growth phase	(comment: mcm4ts-td phenotype indicates that Cdc23 chromatin localization is independent of Mcm4)
PMID:1314171	GO:0015385	sodium:proton antiporter activity	(comment: CHECK inhibited by CCCP)
PMID:1316996	FYPO:0002060	viable vegetative cell population	(comment: CHECK cdc2-A21 suppresses mitotic catastrophe at high temperature)
PMID:1316996	FYPO:0000839	inviable elongated mononucleate aseptate cell	(comment: CHECK crosses with this mutant generate a high level of diploids.)
PMID:1316996	FYPO:0004922	inviable elongated mononucleate aseptate cell with cell cycle arrest at mitotic G2/M phase transition	(comment: G2 arrest shown by FACS analysis)
PMID:1316996	FYPO:0000839	inviable elongated mononucleate aseptate cell	(comment: G2 arrest shown by FACS analysis)
PMID:1316996	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(comment: HI used as substrate)
PMID:1316996	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(comment: HI used as substrate)
PMID:1316996	FYPO:0001382	decreased protein kinase activity	(comment: Hi used as substrate)
PMID:1316996	FYPO:0001382	decreased protein kinase activity	(comment: Hi used as substrate)
PMID:1316996	FYPO:0002060	viable vegetative cell population	(comment: cdc2-E8 suppresses mitotic catastrophe at high temperature)
PMID:1316996	FYPO:0002060	viable vegetative cell population	(comment: cdc2-E9 suppresses mitotic catastrophe at high temperature)
PMID:1316996	FYPO:0000839	inviable elongated mononucleate aseptate cell	(comment: cells inviable at all temperatures in presence of wee1+)
PMID:1324908	FYPO:0000663	decreased catalytic activity	(comment: CHECK GO:0008444 CDP-DG synthase and GO:0003882 PS synthase)
PMID:1324908	GO:0003882	CDP-diacylglycerol-serine O-phosphatidyltransferase activity	(comment: CHECK regulated by inositol)
PMID:1324908	GO:0008444	CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity	(comment: CHECK regulated by inositol)
PMID:1332977	MOD:00046	O-phospho-L-serine	(comment: 3 sites in N-terminus (1-75) and 7 in C-terminus (1221-1485), but positions not determined)
PMID:1332977	GO:0003918	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity	phosphorylated and dephosphorylated forms both active; no PR col 17 because no evidence that dephosphorylated form is physiologically relevant (dephosphorylated in vitro)
PMID:1372994	GO:0004713	protein tyrosine kinase activity [directly_negatively_regulates] PomBase:SPBC11B10.09 [part_of] negative regulation of G2/M transition of mitotic cell cycle	(comment: val: I used this to link to process term even though it isn't shown directly in this paper)
PMID:1396704	GO:0008553	P-type proton-exporting transporter activity [happens_during] cellular response to glucose stimulus	(comment: CHECK activated_by(CHEBI:17234))
PMID:1427071	FYPO:0003165	cut [has_penetrance] low	(comment: CHECK hydroxyurea absent)
PMID:14519123	FYPO:0000037	growth auxotrophic for cysteine	(Fig. 3)
PMID:14519123	FYPO:0001712	coenzyme Q10 absent from cell	(Fig. 3)
PMID:14519123	FYPO:0000087	sensitive to hydrogen peroxide	(Fig. 4)
PMID:14519123	FYPO:0003270	growth auxotrophic for glutathione	(Fig. 4)
PMID:14519123	FYPO:0000103	sensitive to copper	(Fig. 4)
PMID:14528010	GO:0008821	crossover junction DNA endonuclease activity	( comment: is not a resolvase - makes symmetric cuts on opposed strands across the junction but does not convert products to linear DNA molecules)
PMID:14528010	GO:1990238	double-stranded DNA endonuclease activity	(comment: specific for dsDNA at ds/ssDNA junction)
PMID:14532136	GO:0007129	homologous chromosome pairing at meiosis	(comment: there is good evidence for this, but not bullet proof)
PMID:14585996	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC23B6.03c [present_during] cellular response to hydroxyurea	(comment: CHECK in presence of hydroxyurea)
PMID:14585996	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC216.05 [present_during] cellular response to hydroxyurea	(comment: CHECK in presence of hydroxyurea)
PMID:14585996	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c	(comment: CHECK residue S604)
PMID:14585996	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c	(comment: CHECK residue S604)
PMID:14585996	GO:0000785	chromatin	phenotype indicates that mrc1/Phos:S604 has higher affinity for chromatin than Unphos:S604
PMID:14599746	GO:0070914	UV-damage excision repair	(comment: inferred from increased mutation rate upon UV exposure in mutant)
PMID:14599746	GO:0006284	base-excision repair	(comment: rationale: increased transversion frequency indicates that 8-oxoG persists more in mutant, but normal indel frequency suggests not NER)
PMID:14602073	GO:0005634	nucleus [exists_during] mitotic interphase	(comment: before late interphase)
PMID:14602073	GO:0110085	mitotic actomyosin contractile ring	(comment: dependent on F-actin (assayed using Latruncilin A))
PMID:14602073	GO:0110085	mitotic actomyosin contractile ring	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0110085	mitotic actomyosin contractile ring	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0110085	mitotic actomyosin contractile ring	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0110085	mitotic actomyosin contractile ring	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0110085	mitotic actomyosin contractile ring	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0110085	mitotic actomyosin contractile ring	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0110085	mitotic actomyosin contractile ring	(comment: independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0071341	medial cortical node [exists_during] mitotic interphase	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0071341	medial cortical node [exists_during] mitotic interphase	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0071341	medial cortical node [exists_during] mitotic interphase	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0030479	actin cortical patch [exists_during] mitotic interphase	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0005737	cytoplasm [exists_during] mitotic interphase	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0005737	cytoplasm [exists_during] mitotic interphase	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0071341	medial cortical node [exists_during] mitotic interphase	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0071341	medial cortical node [exists_during] mitotic interphase	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0005737	cytoplasm [exists_during] mitotic interphase	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14602073	GO:0005737	cytoplasm [exists_during] mitotic interphase	(comment: late interphase; independent of F-actin (assayed using Latrunculin A))
PMID:14612233	GO:0004382	GDP phosphatase activity	(comment: CHECK activated_by(CHEBI:29108)| activated_by(CHEBI:29035))
PMID:14633985	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Fig. 1)
PMID:14633985	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Fig. 1)
PMID:14633985	FYPO:0005947	normal growth on potassium chloride	(Fig. 1)
PMID:14633985	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] medium	(Fig. 1)
PMID:14633985	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Fig. 1c)
PMID:14633985	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Fig. 1c)
PMID:14633985	FYPO:0004052	RNA absent from cell during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC19D5.01	(Fig. 1c)
PMID:14633985	FYPO:0000271	sensitive to salt stress [has_severity] high	(Fig. 1c)
PMID:14633985	FYPO:0004052	RNA absent from cell during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC29B5.01	(Figure 4E)
PMID:14633985	GO:0005737	cytoplasm	(Figure 6A) Csx1±GFP was detected in the cytoplasm and appeared to be excluded from the nucleus. This pattern of Csx1±GFP localization was unaffected by oxidative stress.
PMID:14633985	FYPO:0003038	abnormal RNA stability [assayed_using] PomBase:SPAC21E11.03c	(Figure 6B) decreased stability in response to oxidative stress
PMID:14633985	FYPO:0003038	abnormal RNA stability [assayed_using] PomBase:SPAC21E11.03c	(Figure 6B) decreased stability in response to oxidative stress
PMID:14633985	FYPO:0003038	abnormal RNA stability [assayed_using] PomBase:SPBC29B5.01	(Figure 6B). decreased stability in response to oxidative stress
PMID:14633985	GO:0003729	mRNA binding [has_input] PomBase:SPBC29B5.01 [part_of] 3'-UTR-mediated mRNA stabilization [happens_during] cellular response to oxidative stress	(Figure 7A)
PMID:14633985	GO:0004707	MAP kinase activity [has_input] PomBase:SPAC17A2.09c [happens_during] cellular response to oxidative stress	(comment: from genetics and Sty1 consensus. Later papers say Activated Sty1 also phosphorylates Csx1)
PMID:14633985	FYPO:0001281	normal protein phosphorylation during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC24B11.06c	As shown in Figure 2C, H2O2 induced robust phosphorylation of Spc1 in csx1D cells..... Csx1 is not necessary for Spc1 activation.
PMID:14633985	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [has_severity] high [assayed_using] PomBase:SPAC21E11.03c	The H2O2-induced increase in expression of pcr1+ mRNA, which encodes a binding partner of Atf1, was similarly eliminated in csx1D cells (Figure 4A
PMID:14633985	FYPO:0002061	inviable vegetative cell population	The csx1D single mutant was less sensitive to H2O2 than the spc1D mutant, whereas the csx1D spc1D double mutant was more sensitive than the spc1D strain. These ®ndings were consistent with the idea that Csx1 and Spc1 have independent functions in oxidative stress tolerance.
PMID:14633985	FYPO:0001101	decreased protein level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC29B5.01 [has_severity] high	This decrease correlated with a large drop in the amount of Atf1 protein (Figure 4C).
PMID:14633985	FYPO:0003038	abnormal RNA stability [assayed_using] PomBase:SPBC29B5.01	decreased stability in response to oxidative stress (Figure 6B)
PMID:14633985	FYPO:0001486	normal RNA level during cellular response to salt stress [assayed_using] PomBase:SPBC29B5.01	mRNA expression levels of two other transcription factor genes involved in oxidative stress, pap1+ and prr1+, were unaffected by the csx1D mutation (Figure 4A).
PMID:14633985	FYPO:0001246	normal RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC1783.07c	mRNA expression levels of two other transcription factor genes involved in oxidative stress, pap1+ and prr1+, were unaffected by the csx1D mutation (Figure 4A).
PMID:14633985	FYPO:0001246	normal RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC8C9.14	mRNA expression levels of two other transcription factor genes involved in oxidative stress, pap1+ and prr1+, were unaffected by the csx1D mutation (Figure 4A).
PMID:14633985	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC29B5.01 [has_severity] high	the large increase in atf1+ mRNA that is induced by H2O2 in wild-type cells was abolished in csx1D cells.
PMID:14654689	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] low	(comment: same as rad11-D223Y alone)
PMID:14654689	FYPO:0002239	shortened telomeres during vegetative growth	(comment: same as rad11-D223Y alone)
PMID:14654689	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] medium	(comment: same as rad50delta alone)
PMID:14663827	FYPO:0001394	activation of monopolar cell growth at either end [has_penetrance] medium	(Figure 1) (comment: about 30% from old end)
PMID:14663827	FYPO:0001394	activation of monopolar cell growth at either end [has_penetrance] high	(Figure 1) (comment: about 60% from old end)
PMID:14663827	FYPO:0001394	activation of monopolar cell growth at either end [has_penetrance] high	(Figure 1) (comment: about 60% from old end)
PMID:14663827	FYPO:0008131	normal growth site selection after cell division	(Figure 1) Tea3 cells resumed growth from their old end after division, indicating that the cell inheriting a growing end had no difficulty in reidentifying it as the appropriate site for growth after division (Figure 1).
PMID:14663827	FYPO:0001394	activation of monopolar cell growth at either end [has_penetrance] low	(Figure 1) about 14% from new end In contrast, 14% of tea1 cells and 30% of pom1 cells failed to resume growth from a previously growing end (Figure 1).
PMID:14663827	FYPO:0001394	activation of monopolar cell growth at either end [has_penetrance] medium	(Figure 1) about 30% from new end. In contrast, 14% of tea1 cells and 30% of pom1 cells failed to resume growth from a previously growing end (Figure 1).
PMID:14663827	FYPO:0003150	decreased NETO	(Figure 2)
PMID:14663827	FYPO:0000190	abnormal actin cortical patch localization during vegetative growth [has_penetrance] 37	(Figure 3)
PMID:14663827	FYPO:0000190	abnormal actin cortical patch localization during vegetative growth [has_penetrance] 60	(Figure 3)
PMID:14663827	FYPO:0000190	abnormal actin cortical patch localization during vegetative growth [has_penetrance] 60	(Figure 3)
PMID:14663827	FYPO:0000190	abnormal actin cortical patch localization during vegetative growth [has_penetrance] 36	(Figure 3)
PMID:14663827	FYPO:0000190	abnormal actin cortical patch localization during vegetative growth [has_penetrance] 78	(Figure 3)
PMID:14663827	FYPO:0003150	decreased NETO [has_severity] high	(Figure 3)
PMID:14663827	FYPO:0000190	abnormal actin cortical patch localization during vegetative growth [has_penetrance] 15	(Figure 3)
PMID:14663827	FYPO:0003150	decreased NETO [has_severity] medium	(Figure 3) Our tea1 result differs from that of Rupes et al. (1999), who found that tea1 cells did not switch to bipolar growth after a LatA pulse. This may be due to differences in scoring or temperature between the experiments.
PMID:14663827	FYPO:0005880	long interphase microtubules curved around cell end [has_penetrance] 24	(Figure 4)
PMID:14663827	FYPO:0005880	long interphase microtubules curved around cell end [has_penetrance] 37	(Figure 4)
PMID:14663827	FYPO:0005880	long interphase microtubules curved around cell end [has_penetrance] 37	(Figure 4)
PMID:14663827	FYPO:0005880	long interphase microtubules curved around cell end [has_penetrance] 24	(Figure 4)
PMID:14663827	FYPO:0005880	long interphase microtubules curved around cell end [has_penetrance] 5	(Figure 4)
PMID:14663827	FYPO:0005880	long interphase microtubules curved around cell end [has_penetrance] 15	(Figure 4) shows that tea1 cells at high temperatures displayed microtubules bending round the cell ends in accordance with previously published results (Mata and Nurse, 1997).
PMID:14663827	FYPO:0007379	T-shaped vegetative cell [has_penetrance] 33	(Figure 5)
PMID:14663827	FYPO:0007379	T-shaped vegetative cell [has_penetrance] 11	(Figure 5)
PMID:14663827	FYPO:0000013	T-shaped vegetative cell [has_penetrance] 9	(Figure 5)
PMID:14663827	FYPO:0007379	T-shaped vegetative cell [has_penetrance] 11	(Figure 5)
PMID:14663827	FYPO:0007379	T-shaped vegetative cell [has_penetrance] 20	(Figure 5)
PMID:14663827	FYPO:0007379	T-shaped vegetative cell [has_penetrance] 33	(Figure 5)
PMID:14663827	FYPO:0007379	T-shaped vegetative cell [has_penetrance] 33	(Figure 5)
PMID:14704433	FYPO:0002834	decreased chromatin silencing at centromere	A tas3 deletion strain carrying the ura4+ reporter gene inserted at innermost (imr) or outermost (otr) centromeric repeats of chromosome 1 (imr1R::ura4+ and otr1R::ura4+, respectively) displayed a loss of silencing of both reporter genes (Fig. 2D) to an extent similar to that of the deletion of sir2, chp1, or ago1 (Fig. 2D)
PMID:14704433	FYPO:0002834	decreased chromatin silencing at centromere	A tas3 deletion strain carrying the ura4+ reporter gene inserted at innermost (imr) or outermost (otr) centromeric repeats of chromosome 1 (imr1R::ura4+ and otr1R::ura4+, respectively) displayed a loss of silencing of both reporter genes (Fig. 2D) to an extent similar to that of the deletion of sir2, chp1, or ago1 (Fig. 2D)
PMID:14704433	FYPO:0002834	decreased chromatin silencing at centromere	A tas3 deletion strain carrying the ura4+ reporter gene inserted at innermost (imr) or outermost (otr) centromeric repeats of chromosome 1 (imr1R::ura4+ and otr1R::ura4+, respectively) displayed a loss of silencing of both reporter genes (Fig. 2D) to an extent similar to that of the deletion of sir2, chp1, or ago1 (Fig. 2D)
PMID:14704433	FYPO:0002834	decreased chromatin silencing at centromere	A tas3 deletion strain carrying the ura4+ reporter gene inserted at innermost (imr) or outermost (otr) centromeric repeats of chromosome 1 (imr1R::ura4+ and otr1R::ura4+, respectively) displayed a loss of silencing of both reporter genes (Fig. 2D) to an extent similar to that of the deletion of sir2, chp1, or ago1 (Fig. 2D)
PMID:14704433	FYPO:0003744	abolished protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	Deletion of tas3+ abolished the association of Chp1-Flag with otr1::ura4+, as well as with native cen sequences (Fig. 4C).
PMID:14704433	FYPO:0002566	abolished histone H3-K9 methylation during vegetative growth	Further, chromatin immunoprecipitation (ChIP) showed that Tas3 was required for H3-K9 methylation and Swi6 localization of a ura4+ reporter gene inserted at each of the above loci (Fig. 2E).
PMID:14704433	FYPO:0003744	abolished protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC83.03c [assayed_region] dg_repeat	Furthermore, deletion of ago1+, dcr1+, or rdp1+ abolished the association of Chp1-Flag and Tas3-TAP with otr1::ura4+, as well as with centromeric repeat sequences (Fig. 4, A and B).
PMID:14704433	FYPO:0003744	abolished protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC83.03c [assayed_region] dg_repeat	Furthermore, deletion of ago1+, dcr1+, or rdp1+ abolished the association of Chp1-Flag and Tas3-TAP with otr1::ura4+, as well as with centromeric repeat sequences (Fig. 4, A and B).
PMID:14704433	FYPO:0003744	abolished protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC83.03c [assayed_region] dg_repeat	Furthermore, deletion of ago1+, dcr1+, or rdp1+ abolished the association of Chp1-Flag and Tas3-TAP with otr1::ura4+, as well as with centromeric repeat sequences (Fig. 4, A and B).
PMID:14730319	GO:0005721	pericentric heterochromatin [exists_during] meiotic metaphase I	(Fig. 2 and 3d)
PMID:14730319	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] 50	(Fig. 2a)
PMID:14730319	FYPO:0002219	normal chromosome disjunction at meiosis I	(Fig. 2a)
PMID:14730319	FYPO:0005648	sister kinetochore dissociation in meiotic metaphase I	(Fig. 2c)
PMID:14730319	FYPO:0007650	abolished protein localization to pericentric heterochromatin during meiotic prophase I [assayed_using] PomBase:SPBC29A10.14	(Fig. 2c)
PMID:14730319	FYPO:0007649	abolished protein localization to pericentric heterochromatin during meiosis II [assayed_using] PomBase:SPBC29A10.14	(Fig. 2c)
PMID:14730319	FYPO:0002060	viable vegetative cell population	(Fig. 4a)
PMID:14730319	FYPO:0000091	sensitive to thiabendazole	(Fig. 4a)
PMID:14730319	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 1.1	(Fig. 4c)
PMID:14730319	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 19	(Fig. 4c)
PMID:14730319	FYPO:0004159	abnormal homologous chromosome segregation [has_penetrance] 15	(Fig. 4c)
PMID:14730319	FYPO:0007651	abolished protein localization to pericentric heterochromatin during mitosis [assayed_using] PomBase:SPAC15A10.15	(Fig. 4d)
PMID:14730319	GO:0005721	pericentric heterochromatin [exists_during] mitotic metaphase	(Fig. 4d,e)
PMID:14739927	GO:0005515	protein binding	(comment: CHECK interaction increases during cellular response to UV)
PMID:14739927	GO:0005515	protein binding	(comment: CHECK proteins dissociate during cellular response to UV)
PMID:14742702	FYPO:0003186	abolished protein localization to mitotic spindle [assayed_using] PomBase:SPAC890.02c	(Fig. 8C)
PMID:14742702	FYPO:0000274	increased duration of mitotic M phase	(Figure 1A)
PMID:14742702	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Figure 1A) inferred from increased duration of mitosis
PMID:14742702	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B	(Figure 1B)
PMID:14742702	FYPO:0006173	abolished mitotic spindle elongation during prophase	(Figure 1B)
PMID:14742702	FYPO:0006048	unstable mitotic spindle	(Figure 1C rows 2 and 3) (comment: chromosome missegregation in the cell of row 3, and see Supplementary Figure S1 for quantification of spindle intensity)
PMID:14742702	FYPO:0000141	abnormal mitotic sister chromatid segregation	(Figure 1C)
PMID:14742702	FYPO:0000177	abnormal mitotic spindle assembly	(Figure 1C)
PMID:14742702	GO:0005881	cytoplasmic microtubule [exists_during] mitotic interphase	(Figure 1D)
PMID:14742702	GO:1990498	mitotic spindle microtubule [exists_during] mitotic M phase	(Figure 1D)
PMID:14742702	GO:1990498	mitotic spindle microtubule [exists_during] mitotic M phase	(Figure 1D)
PMID:14742702	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	(Figure 2A)
PMID:14742702	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	(Figure 2A)
PMID:14742702	GO:0000940	outer kinetochore [exists_during] mitotic M phase	(Figure 2D)
PMID:14742702	FYPO:0003186	abolished protein localization to mitotic spindle [assayed_using] PomBase:SPCC895.07	(Figure 3B)
PMID:14742702	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPCC895.07	(Figure 3B)
PMID:14742702	FYPO:0005441	abolished protein localization to microtubule during mitotic interphase [assayed_using] PomBase:SPCC895.07	(Figure 3B)
PMID:14742702	FYPO:0003186	abolished protein localization to mitotic spindle [assayed_using] PomBase:SPAC890.02c	(Figure 3B)
PMID:14742702	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_using] PomBase:SPAC890.02c	(Figure 4A)
PMID:14742702	FYPO:0002966	normal protein localization to mitotic spindle [assayed_using] PomBase:SPCC736.14	(Figure 4D)
PMID:14742702	FYPO:0005842	normal protein localization to interphase microtubule [assayed_using] PomBase:SPCC736.14	(Figure 4D)
PMID:14742702	FYPO:0002966	normal protein localization to mitotic spindle [assayed_using] PomBase:SPAC890.02c	(Figure 4E)
PMID:14742702	FYPO:0002966	normal protein localization to mitotic spindle [assayed_using] PomBase:SPBC2F12.13	(Figure 4F)
PMID:14742702	GO:0070850	TACC/TOG complex	(Figure 5A, lane 4)
PMID:14742702	GO:0070850	TACC/TOG complex	(Figure 5A, lane 4)
PMID:14742702	GO:0005515	protein binding	(Figure 6A)
PMID:14742702	GO:0005515	protein binding	(Figure 6A)
PMID:14742702	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC895.07 [assayed_using] PomBase:SPAC890.02c	(Figure 6B)
PMID:14742702	FYPO:0001355	decreased vegetative cell population growth	(Figure 8E)
PMID:14742702	FYPO:0002400	single microtubule bundle during mitotic interphase	(Figure 8E)
PMID:14742702	FYPO:0006195	decreased number of elongated microtubule bundles curved around cell end	(Figure 8E)
PMID:14742702	FYPO:0001978	bent mitotic spindle	(Figure 8E)
PMID:14742702	FYPO:0001733	abnormal mitotic spindle pole body separation	(Figure 8E)
PMID:14742702	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_using] PomBase:SPAC890.02c	On temperature shift down to 20°C, Alp7-YFP localized only to the SPB (Figure 2B). This also indicates that Alp7 does not require a microtubule cytoskeleton to localize to the SPB.
PMID:14766746	FYPO:0004384	normal single-stranded DNA binding	(comment: filter binding assay)
PMID:14766746	FYPO:0004386	abolished single-stranded DNA binding	(comment: filter binding assay)
PMID:14766746	FYPO:0004385	decreased single-stranded DNA binding [has_severity] medium	(comment: filter binding assay)
PMID:14766746	FYPO:0004385	decreased single-stranded DNA binding [has_severity] low	(comment: filter binding assay)
PMID:14972679	FYPO:0000583	abolished sporulation [has_penetrance] 10	(Figure 1B)
PMID:14972679	FYPO:0000583	abolished sporulation [has_penetrance] 90	(Figure 1B)
PMID:14972679	FYPO:0000583	abolished sporulation [has_penetrance] 20	(Figure 1B)
PMID:14972679	FYPO:0005509	abnormal meiotic sister chromatid segregation	(Figures 1A and 2)
PMID:14972679	FYPO:0004159	abnormal homologous chromosome segregation	(Figures 1A and 2)
PMID:14972679	FYPO:0004394	lagging chromosomes during meiosis II [has_penetrance] 30	(Figures 1A and 2)
PMID:14972679	FYPO:0004393	lagging chromosomes during meiosis I [has_penetrance] 35	(Figures 1A and 2)
PMID:14972679	GO:0005634	nucleus [exists_during] meiotic metaphase I	By metaphase I, 100% of cells (n 􏰆 100) contained a strong nuclear signal. Sgo1-GFP was concentrated in distinct foci in about half of these metaphase I cells (Figure 3A-2).
PMID:14972679	FYPO:0006423	decreased meiotic sister chromatid cohesion at centromere during meiosis I [assayed_using] PomBase:SPBC29A10.14	Furthermore, no Rec8-specific fluorescence at all could be detected in 10% of the mutant binucleates. In contrast, the distribution of Rec8- GFP fluorescence in Δsgo2 mutant binucleates was indistinguishable from wild-type.
PMID:15004232	FYPO:0004766	abolished cytoplasmic interphase microtubule nucleation	(Figure 5F)
PMID:15031652	FYPO:0001071	normal transport	(comment: *************normal glycerol export)
PMID:15031652	FYPO:0001164	normal growth on glucose carbon source	Deletion of the S. pombe spac977.17 gene did not cause any observable growth defect on glucose or glycerol as a sole carbon source (not shown).
PMID:15031652	FYPO:0001021	normal growth during cellular response to osmotic stress	Surprisingly, the S. pombe spac977.17 2 mutants survived both the hyper- and hypo-osmotic shocks in a similar way as the wild-type cells.
PMID:15031652	FYPO:0001409	normal growth on glycerol carbon source	The patterns and kinetics of glycerol release in the mutant were similar to those in the wild type (Figure 3A) suggesting that the export process is independent of the S. pombe spac977.17 gene.
PMID:15040954	GO:0120542	ethanol dehydrogenase (NAD+) activity	(comment: CHECK qualifier=major)
PMID:15042280	FYPO:0002060	viable vegetative cell population	A null mutant was obtained with the haploid strain; there- fore, this ORF was found to be dispensable for normal growth of S. pombe. (figure 2B)
PMID:15042280	FYPO:0008421	abolished lactoylglutathione lyase activity	Growth of S. pombe. Since GLO1 is the only gene responsible for glyox- alase I activity in S. cerevisiae, no glyoxalase I activity is detected in the ∆glo1 mutant of this yeast (Inoue and Kimura 1996, 1999). In the case of the fission yeast, gly- oxalase I activity in a null mutant of this ORF was also not detected (Table 1).
PMID:15042280	FYPO:0003408	sensitive to methylglyoxal [has_severity] high	The effect of the absence of ORF SPBC12C2.12c in S. pombe with respect to methylglyoxal sensitivity was determined in a spot assay (Fig. 2B). The mutant defective in this ORF was hypersensitive to methylglyoxal.
PMID:15042280	GO:0004462	lactoylglutathione lyase activity	To address whether ORF SPBC12C2.12c corresponds to the structural gene for glyoxalase I in S. pombe, it was expressed in the ∆glo1 mutant of S. cerevisiae. As shown in Table 1, glyoxalase I activity was detected in S. cerevisiae strain YGL1 (∆glo1) carrying the plasmid pG-1+glo1+, and tolerance to meth- ylglyoxal in this transformant was restored (Fig. 2B). Thus, SPBC12C2.12c, found in the S. pombe genome, is the structural gene for glyoxalase I (glo1+).
PMID:15047861	FYPO:0000086	sensitive to tacrolimus [has_severity] high	(Fig. 1)
PMID:15047861	FYPO:0000086	sensitive to tacrolimus [has_severity] high	(Fig. 1)
PMID:15047861	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Fig. 1)
PMID:15047861	FYPO:0002061	inviable vegetative cell population	(Fig. 1)
PMID:15047861	FYPO:0002060	viable vegetative cell population	(Fig. 1)
PMID:15047861	FYPO:0002061	inviable vegetative cell population	(Fig. 1)
PMID:15047861	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Fig. 1)
PMID:15047861	FYPO:0002061	inviable vegetative cell population	(Fig. 1)
PMID:15047861	FYPO:0000650	increased septation index	(Fig. 6)
PMID:15047861	FYPO:0002061	inviable vegetative cell population	(Fig. 8c)
PMID:15047861	FYPO:0003279	excess Golgi cisternae present	(Figure 3B, a-c)
PMID:15047861	FYPO:0000349	abnormal Golgi morphology	(Figure 3B, a-c) accumulation of presumptive post-Golgi secretory vesicles and abnormal Golgi-like structures were also characteristic of the ypt3-i5 mutants that we reported previously (Cheng et al., 2002).
PMID:15047861	FYPO:0002060	viable vegetative cell population	(comment: DNS)
PMID:15047861	FYPO:0000426	normal endocytosis	When the cells were labeled with FM4-64 for 60 min, the Δapm1 cells were highly fragmented compared with wild-type cells, consistent with the findings obtained by (Figure 7B)
PMID:15047861	FYPO:0002258	small vacuoles present in increased numbers	When the cells were labeled with FM4-64 for 60 min, the Δapm1 cells were highly fragmented compared with wild-type cells, consistent with the findings obtained by (Figure 7B)
PMID:15052323	GO:0036374	glutathione gamma-glutamate hydrolase [part_of] glutathione catabolic process	(comment: From IMP evidence & a proxy assay for hydrolase function)
PMID:15062095	FYPO:0000901	abnormal microtubule dynamics during vegetative growth	(comment: the variant caused abnormal microtubule behavior in cell-end regions, which is likely to be the cause of the previously reported shape abnormalities)
PMID:15068790	FYPO:0003302	nucleus mislocalized towards cell tip during mitotic interphase [has_penetrance] 10	(Fig. 1)
PMID:15068790	FYPO:0002818	microtubule bundles present in decreased numbers [has_penetrance] 10	(Fig. 1)
PMID:15068790	FYPO:0007983	microtubule bundles detached from the nuclear envelope	(Fig. 1)
PMID:15068790	FYPO:0007982	single microtubule bundle with aster-like microtubules [has_penetrance] 60	(Fig. 1)
PMID:15068790	FYPO:0003302	nucleus mislocalized towards cell tip during mitotic interphase [has_penetrance] 30	(Fig. 1)
PMID:15068790	FYPO:0001126	abnormal cell shape [has_penetrance] complete	(Fig. 1)
PMID:15068790	FYPO:0000339	mislocalized septum during vegetative growth	(Fig. 1)
PMID:15068790	FYPO:0007114	normal microtubule bundle	(Fig. 1)
PMID:15068790	FYPO:0001126	abnormal cell shape [has_penetrance] low	(Fig. 1)
PMID:15068790	FYPO:0007984	abolished eMTOC disassembly [has_penetrance] 30	(Fig. 2)
PMID:15068790	FYPO:0007984	abolished eMTOC disassembly [has_penetrance] 61	(Fig. 2)
PMID:15068790	FYPO:0003337	increased protein localization to septum [assayed_protein] PomBase:SPBC365.15	(Fig. 2)
PMID:15068790	FYPO:0007985	early eMTOC assembly	(Fig. 2)
PMID:15068790	FYPO:0005441	abolished protein localization to microtubule during mitotic interphase [assayed_protein] PomBase:SPBC365.15	(Fig. 6)
PMID:15068790	FYPO:0005441	abolished protein localization to microtubule during mitotic interphase [assayed_protein] PomBase:SPBC365.15	(Fig. 6)
PMID:15068790	FYPO:0002818	microtubule bundles present in decreased numbers	(Fig. 7)
PMID:15068790	FYPO:0006220	abolished protein localization to septum [assayed_protein] PomBase:SPBC365.15	(Fig. 7)
PMID:15068790	FYPO:0003302	nucleus mislocalized towards cell tip during mitotic interphase [has_penetrance] 70	(Fig. 7)
PMID:15068790	FYPO:0004624	abolished eMTOC assembly [has_penetrance] complete	(Fig. 7)
PMID:15107426	FYPO:0003360	abolished superoxide dismutase activity [assayed_enzyme] PomBase:SPAC821.10c	An S. pombe strain bearing the disrupted pccs allele displayed a deficiency in SOD1 activity (Fig. 4A).
PMID:15107426	FYPO:0003360	abolished superoxide dismutase activity [assayed_enzyme] PomBase:SPAC821.10c	Cell lysates from this strain was analyzed for SOD1 activity. As shown in Fig. 4, C and D, sod1 mutant cells were defective in SOD1 activity in the absence or presence of copper.
PMID:15107426	FYPO:0000096	sensitive to cadmium	Deletion of the pccs gene dramat- ically lowered resistance to cadmium (Fig. 8B). CdCl2 concen- trations as low as 0.6 M inhibited growth of the pccs mu- tant by 40%. The pccs single mutant was 10-fold more sensitive to cadmium compared with the wild-type strain, which showed 40% growth inhibition in the presence of 6 M CdCl2.
PMID:15107426	GO:0016532	superoxide dismutase copper chaperone activity [has_input] PomBase:SPAC821.10c	Taken together, these results demonstrate that the full-length S. pombe Pccs and Pccs domains I-III polypeptides can substitute for CCS1 in delivering copper to SOD1 in S. cerevisiae ccs1 cells.
PMID:15107426	GO:1990880	cellular detoxification of copper ion	Taken together, these results show that the Pccs protein through its domain IV plays a critical role in cell survival under conditions of copper toxicity.
PMID:15107426	FYPO:0000096	sensitive to cadmium	The zym1 single mutant strain exhibited 40% growth inhibition in the presence of 0.75 M CdCl2.
PMID:15107426	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC821.10c	Western blot analysis (Fig. 4B) of the same lysates shown in Fig. 4A revealed that the absence of SOD1 activity in the pccs mutant strain was not due to lack of SOD1 expres- sion.
PMID:15121844	FYPO:0002134	decreased protein-RNA interaction	(comment: three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site)
PMID:15121844	FYPO:0002357	normal protein-RNA interaction	(comment: three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site)
PMID:15121844	FYPO:0002134	decreased protein-RNA interaction	(comment: three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site)
PMID:15121844	FYPO:0002134	decreased protein-RNA interaction	(comment: three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site)
PMID:15121844	FYPO:0002134	decreased protein-RNA interaction	(comment: three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site)
PMID:15132994	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	(Fig. 1c)
PMID:15132994	GO:0072686	mitotic spindle [exists_during] mitotic anaphase B	(Fig. 1c)
PMID:15132994	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(comment: CHECK is this the correct term?)
PMID:15132994	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_using] PomBase:SPAC19E9.02	(comment: Fin1 binds Byr4. (A) Fin1 failed to associate with SPBs when the SIN was either inactive or hyperactive.)
PMID:15132994	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_using] PomBase:SPAC19E9.02	Fin1 binds Byr4. (A) Fin1 failed to associate withSPBs when the SIN was either inactive or hyperactive. Fin1 failed to bind to the SPB when byr4+ was deleted (Table 1).
PMID:15132994	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_using] PomBase:SPAC19E9.02	Fin1 failed to bind to the SPB when byr4+ was deleted (Table 1).
PMID:15132994	GO:0035591	signaling adaptor activity [has_input] PomBase:SPAC19E9.02 [part_of] septation initiation signaling	We draw two conclusions from these data; first, association of Fin1 with the SPB requires activation of the SIN; second, recruitment of Fin1 to the SPB requires the SIN inhibitor Byr4, with which it interacts.
PMID:15147872	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] >30	(Fig. 1A,B)
PMID:15147872	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 8	(Fig. 1A,B)
PMID:15147872	FYPO:0005721	curved mitotic spindle during anaphase B [has_penetrance] >30	(Fig. 1C, 2)
PMID:15147872	FYPO:0005722	mitotic spindle collapse during anaphase B elongation [has_penetrance] >30	(Fig. 2)
PMID:15147872	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Fig. 3A)
PMID:15147872	FYPO:0003779	abnormal nuclear envelope morphology during mitosis [has_penetrance] 90	(Fig. 4) abnormally segregating nuclear membrane #2863 PENDING
PMID:15147872	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 9	(Table 1)
PMID:15147872	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 5	(Table 1)
PMID:15147872	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 16	(Table 1)
PMID:15155581	FYPO:0002099	normal protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC664.07c	(Fig. 1)
PMID:15155581	FYPO:0002099	normal protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC664.07c	(Fig. 1)
PMID:15155581	FYPO:0002471	abolished protein phosphorylation during cellular response to ionizing radiation [assayed_using] PomBase:SPAC664.07c	(Fig. 1)
PMID:15155581	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC664.07c	(Fig. 1)
PMID:15155581	FYPO:0003131	normal protein phosphorylation during cellular response to ionizing radiation [assayed_using] PomBase:SPAC664.07c	(Fig. 1)
PMID:15155581	FYPO:0003131	normal protein phosphorylation during cellular response to ionizing radiation [assayed_using] PomBase:SPAC664.07c	(Fig. 1)
PMID:15155581	FYPO:0002099	normal protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC664.07c	(Fig. 1)
PMID:15155581	FYPO:0002471	abolished protein phosphorylation during cellular response to ionizing radiation [assayed_using] PomBase:SPAC664.07c	(Fig. 1)
PMID:15155581	FYPO:0002099	normal protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC664.07c	(Fig. 1)
PMID:15155581	FYPO:0002471	abolished protein phosphorylation during cellular response to ionizing radiation [assayed_using] PomBase:SPAC664.07c	(Fig. 1)
PMID:15155581	FYPO:0002471	abolished protein phosphorylation during cellular response to ionizing radiation [assayed_using] PomBase:SPAC664.07c	(Fig. 1)
PMID:15155581	FYPO:0003131	normal protein phosphorylation during cellular response to ionizing radiation [assayed_using] PomBase:SPAC664.07c	(Fig. 2)
PMID:15155581	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC664.07c	(Fig. 2)
PMID:15155581	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC664.07c	(Fig. 2)
PMID:15155581	FYPO:0002471	abolished protein phosphorylation during cellular response to ionizing radiation [assayed_using] PomBase:SPAC664.07c	(Fig. 2)
PMID:15155581	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC664.07c	(Fig. 2)
PMID:15155581	FYPO:0003489	abnormal mitotic cell cycle regulation during cellular response to ionizing radiation	(Fig. 3)
PMID:15155581	FYPO:0002471	abolished protein phosphorylation during cellular response to ionizing radiation [assayed_using] PomBase:SPCC1259.13	(Fig. 3)
PMID:15155581	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(Fig. 3)
PMID:15155581	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(Fig. 3)
PMID:15155581	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 3)
PMID:15155581	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 3)
PMID:15155581	FYPO:0002471	abolished protein phosphorylation during cellular response to ionizing radiation [assayed_using] PomBase:SPCC1259.13	(Fig. 3)
PMID:15155581	FYPO:0004548	normal protein kinase activity during cellular response to hydroxyurea [assayed_enzyme] PomBase:SPCC18B5.11c	(Fig. 3)
PMID:15155581	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(Fig. 3)
PMID:15155581	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 3)
PMID:15155581	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 3)
PMID:15155581	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 3)
PMID:15155581	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 3)
PMID:15155581	FYPO:0003489	abnormal mitotic cell cycle regulation during cellular response to ionizing radiation	(Fig. 3)
PMID:15155581	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(Fig. 3) (comment: same as either single mutant)
PMID:15155581	FYPO:0002096	increased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC664.07c	(Fig. 4)
PMID:15155581	FYPO:0002096	increased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC664.07c	(Fig. 4)
PMID:15155581	FYPO:0004464	decreased protein phosphorylation during cellular response to camptothecin [assayed_using] PomBase:SPAC664.07c	(Fig. 4)
PMID:15155581	FYPO:0002096	increased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC664.07c	(Fig. 4)
PMID:15155581	FYPO:0004464	decreased protein phosphorylation during cellular response to camptothecin [assayed_using] PomBase:SPAC664.07c	(Fig. 4)
PMID:15155581	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC23C4.18c [assayed_using] PomBase:SPAC664.07c	(Fig. 5)
PMID:15155581	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC23C4.18c [assayed_using] PomBase:SPAC664.07c	(Fig. 5)
PMID:15155581	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC23C4.18c [assayed_using] PomBase:SPAC664.07c	(Fig. 5)
PMID:15155581	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC23C4.18c [assayed_using] PomBase:SPAC664.07c	(Fig. 5)
PMID:15155581	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC23C4.18c [assayed_using] PomBase:SPAC664.07c	(Fig. 5)
PMID:15155581	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC23C4.18c [assayed_using] PomBase:SPAC664.07c	(Fig. 5)
PMID:15155581	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC664.07c	(comment: basal phosphorylation on T412 & S423)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004397	normal protein export from nucleus during vegetative growth	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004121	normal protein import into nucleus during vegetative growth	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15161942	FYPO:0004418	cut cell with decreased poly(A)+ mRNA export from nucleus	(comment: a reminder why we compounded these phenotypes: nuclear accumulation of poly(A)+ RNA was observed only in cells with the cut phenotype in ptr11-1. No nuclear accumulation was observed in cells without the cut phenotype indicating a possible relationship between the cut phenotype and the nuclear accumulation of poly(A)+ RNA in this mutant.)
PMID:15173168	FYPO:0002096	increased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:15173168	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:15173168	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:15173168	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:15173168	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:15173168	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:15173168	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:15173168	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:15173168	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:15173168	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:15173168	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:15173168	GO:0035591	signaling adaptor activity [has_input] PomBase:SPAC9E9.08	(comment: inferred from phenotypes of mrc1delta, rad3delta, Cds1-Rad26 fusion, other cds1 alleles, and combinations thereof)
PMID:15173383	FYPO:0002061	inviable vegetative cell population	(comment: TEV protease present; Cdc6 truncated)
PMID:15173383	FYPO:0000444	abnormal mitotic cell cycle arrest with replicated DNA	(comment: TEV protease present; Cdc6 truncated)
PMID:15175657	FYPO:0002060	viable vegetative cell population	data not shown
PMID:15177031	GO:1904511	cytoplasmic microtubule plus-end [exists_during] mitotic interphase	(Fig. 1) (comment: live imaging of Tip1YFP and CFP tubulin)
PMID:15177031	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] low	(Fig. 2) (comment: CHECK same phenotype as tea2delta and tip1delta single mutants)
PMID:15177031	FYPO:0002760	short cytoplasmic microtubules	(Fig. 2) (comment: CHECK same phenotype as tea2delta and tip1delta single mutants)
PMID:15177031	FYPO:0004700	bent vegetative cell [has_penetrance] high	(Fig. 2) (comment: CHECK same phenotype as tea2delta and tip1delta single mutants)
PMID:15177031	FYPO:0002060	viable vegetative cell population	(Fig. 2) (comment: CHECK same phenotype as tea2delta and tip1delta single mutants)
PMID:15177031	FYPO:0005817	abolished protein localization to microtubule plus-end during mitotic interphase [assayed_using] PomBase:SPAC3C7.12	(Fig. 4A, B)
PMID:15177031	FYPO:0003329	abolished protein localization to cell tip during mitotic interphase [assayed_using] PomBase:SPAC3C7.12	(Fig. 4A, B)
PMID:15177031	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC3C7.12	(Fig. 4C)
PMID:15177031	FYPO:0005817	abolished protein localization to microtubule plus-end during mitotic interphase [assayed_using] PomBase:SPAC3C7.12	(Fig. 4C) Tip1YFP is expressed from endogenous tip1 gene tagged with YFP
PMID:15177031	FYPO:0005494	decreased protein transport along microtubule during vegetative growth [assayed_using] PomBase:SPAC3C7.12	(Fig. 4E-H)
PMID:15177031	FYPO:0003329	abolished protein localization to cell tip during mitotic interphase [assayed_using] PomBase:SPAC3C7.12	(Fig. 4E-H) Tip1YFP is expressed from endogenous tip1 gene tagged with YFP
PMID:15177031	FYPO:0005833	decreased protein transport along microtubule to cell tip during vegetative growth [assayed_using] PomBase:SPAC3C7.12	(Fig. 4I)
PMID:15177031	FYPO:0005814	abolished protein localization to microtubule plus-end [assayed_using] PomBase:SPBC1604.20c	(Fig. 5A,B) (comment: Endogenous tea2 tagged with GFP)
PMID:15177031	FYPO:0000933	decreased protein localization to microtubule cytoskeleton during vegetative growth [assayed_using] PomBase:SPBC1604.20c	(Fig. 5A,B) (comment: Endogenous tea2 tagged with GFP)
PMID:15177031	FYPO:0003329	abolished protein localization to cell tip during mitotic interphase [assayed_using] PomBase:SPBC1604.20c	(Fig. 5A,B) (comment: Endogenous tea2 tagged with GFP)
PMID:15177031	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC1604.20c	(Fig. 5C)
PMID:15177031	FYPO:0003482	increased punctate cytoplasmic protein localization [assayed_using] PomBase:SPBC1604.20c	(Fig. 5E,F) (comment: CHECK tea2-GFP is mildly overexpressed from the repressed integrated nmt1 promoter)
PMID:15177031	FYPO:0002760	short cytoplasmic microtubules	(Fig. 5E,F) (comment: CHECK tea2-GFP is mildly overexpressed from the repressed integrated nmt1 promoter)
PMID:15177031	FYPO:0003185	normal protein localization to microtubule cytoskeleton during mitotic interphase [assayed_using] PomBase:SPAC18G6.15	(Fig. 6A,B) (comment: CHECK GFPmal3 is mildly overexpressed from the repressed nmt1 promoter)
PMID:15177031	FYPO:0005828	normal protein transport along microtubule to cell tip during vegetative growth [assayed_using] PomBase:SPAC18G6.15	(Fig. 6C,D) (comment: CHECK GFPmal3 is mildly overexpressed from the repressed nmt1 promoter)
PMID:15177031	FYPO:0005814	abolished protein localization to microtubule plus-end [assayed_using] PomBase:SPBC1604.20c	(Fig. 6E)
PMID:15177031	FYPO:0005827	normal protein transport along microtubule during vegetative growth [assayed_using] PomBase:SPBC1604.20c	(Fig. 6E)
PMID:15177031	GO:1904511	cytoplasmic microtubule plus-end [exists_during] mitotic interphase	(comment: co-localises with tip1)
PMID:15177031	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	(comment: colocalises with tip1)
PMID:15177031	GO:0099117	protein transport along microtubule to cell tip	(comment: plus end directed)
PMID:15177031	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC1604.20c [assayed_using] PomBase:SPAC3C7.12	data not shown
PMID:15177031	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC1604.20c [assayed_using] PomBase:SPAC3C7.12	data not shown
PMID:15184401	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC645.05c	(Fig. 1C)
PMID:15184401	FYPO:0002998	abolished actomyosin contractile ring assembly, clumped medial cortical nodes [assayed_using] PomBase:SPCC645.05c	(Fig. 1C)
PMID:15184401	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC645.05c	(Fig. 1C)
PMID:15184401	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC645.05c	(Fig. 1C)
PMID:15184401	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC645.05c	(Fig. 1C)
PMID:15184401	FYPO:0002874	premature protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC645.05c	(Fig. 1C,3)
PMID:15184401	FYPO:0001122	elongated vegetative cell	(Fig. 1E)
PMID:15184401	FYPO:0001122	elongated vegetative cell	(Fig. 1E)
PMID:15184401	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC645.05c	(Fig. 4D)
PMID:15184401	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC645.05c	(Fig. 4D)
PMID:15184401	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPCC645.05c	(Fig. 4F)
PMID:15184401	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPCC645.05c	(Fig. 4F)
PMID:15184401	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPCC645.05c	(Fig. 4F)
PMID:15184401	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPCC645.05c	(Fig. 4F)
PMID:15184401	FYPO:0007133	normal protein localization to medial cortical node during mitotic interphase [assayed_using] PomBase:SPCC645.05c	(Fig. 6B) (comment: CHECK G2)
PMID:15184401	FYPO:0007177	abolished protein localization to medial cortex during mitotic interphase [assayed_using] PomBase:SPCC645.05c	(Fig. 6C) (comment: CHECK G2)
PMID:15184401	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC4B3.15 [assayed_using] PomBase:SPCC645.05c	(Fig. 6F)
PMID:15184401	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC4B3.15 [assayed_using] PomBase:SPCC645.05c	(Fig. 6F)
PMID:15184401	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC4B3.15 [assayed_using] PomBase:SPCC645.05c	(Fig. 6F)
PMID:15184401	FYPO:0007177	abolished protein localization to medial cortex during mitotic interphase [assayed_using] PomBase:SPCC645.05c	(G2) Fig. 6B
PMID:15184402	GO:0051286	cell tip [exists_during] mitotic M phase	During mitosis, tea1p persists at the cell tips, whereas for3p and bud6p leave the cell tip and accumulate more at the cell division plane.
PMID:15184402	GO:1904511	cytoplasmic microtubule plus-end [exists_during] mitotic interphase	During mitosis, tea1p persists at the cell tips, whereas for3p and bud6p leave the cell tip and accumulate more at the cell division plane.
PMID:15189449	FYPO:0004481	abolished cell population growth at high temperature	(C) Vps5p and Vps17p are essential for growth under the high temperature or high osmotic stress.
PMID:15189449	FYPO:0004481	abolished cell population growth at high temperature	(C) Vps5p and Vps17p are essential for growth under the high temperature or high osmotic stress.
PMID:15189449	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(C) Vps5p and Vps17p are essential for growth under the high temperature or high osmotic stress.
PMID:15189449	FYPO:0001214	sensitive to potassium chloride	(C) Vps5p and Vps17p are essential for growth under the high temperature or high osmotic stress.
PMID:15189983	FYPO:0000245	loss of viability in stationary phase [has_severity] high	(Fig. 6)
PMID:15189983	FYPO:0000245	loss of viability in stationary phase	(Fig. 6)
PMID:15189983	FYPO:0000245	loss of viability in stationary phase [has_severity] high	(Fig. 6)
PMID:15189983	FYPO:0001310	normal viability in stationary phase [has_severity] low	(Fig. 6)
PMID:15189983	FYPO:0000245	loss of viability in stationary phase [has_severity] low	(Fig. 6)
PMID:15189983	FYPO:0003032	decreased RNA level during glucose starvation [assayed_transcript] PomBase:SPAC8C9.03	(Fig. 7)
PMID:15189983	FYPO:0003032	decreased RNA level during glucose starvation [assayed_transcript] PomBase:SPBC106.10	(Fig. 7)
PMID:15189983	FYPO:0005279	increased level of glucose-repressed gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC8C9.03	(Fig. 7)
PMID:15189983	FYPO:0005279	increased level of glucose-repressed gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC106.10	(Fig. 7)
PMID:15189983	PomGeneEx:0000011	RNA level increased [during] cellular response to glucose starvation	(Fig. 7) (lanes 1 and 2), we observed that both cgs1Δ and pka1Δ are transcriptionally induced by glucose starvation.
PMID:15189983	PomGeneEx:0000011	RNA level increased [during] cellular response to glucose starvation	(Fig. 7) (lanes 1 and 2), we observed that both cgs1Δ and pka1Δ are transcriptionally induced by glucose starvation.
PMID:15189983	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 1)
PMID:15189983	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 1)
PMID:15189983	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 1)
PMID:15189983	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	(Figure 1)
PMID:15189983	FYPO:0001490	inviable elongated vegetative cell	(Figure 2)
PMID:15189983	FYPO:0001490	inviable elongated vegetative cell	(Figure 2)
PMID:15189983	FYPO:0001490	inviable elongated vegetative cell	(Figure 2)
PMID:15189983	FYPO:0003032	decreased RNA level during glucose starvation [assayed_transcript] PomBase:SPBC1198.14c	(Table 3)
PMID:15189983	FYPO:0003032	decreased RNA level during glucose starvation [assayed_transcript] PomBase:SPBC1198.14c	(Table 3)
PMID:15189983	FYPO:0000708	decreased mating efficiency [has_severity] high	For cgs1-1 mutant cells, pregrowth on YEA medium results in a nearly 100- fold loss of mating efficiency, as expected. More surprisingly, we found that pregrowth of the cgs1-1 strain on PM medium reduces the mating efficiency defect to only fourfold (Table 2).
PMID:15189983	FYPO:0000708	decreased mating efficiency [has_severity] low	For cgs1-1 mutant cells, pregrowth on YEA medium results in a nearly 100- fold loss of mating efficiency, as expected. More surprisingly, we found that pregrowth of the cgs1-1 strain on PM medium reduces the mating efficiency defect to only fourfold (Table 2).
PMID:15189983	FYPO:0001214	sensitive to potassium chloride	git2􏰇 strains themselves were severely defective for growth on YEA medium containing 1 M KCl (Fig. 1).
PMID:15189983	FYPO:0000112	sensitive to sorbitol [has_severity] high	he FWP190 (git2􏰇) cells can grow in the presence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenylate cyclase appears to confer a salt-sensitive, but not an osmotically sensitive, growth defect.
PMID:15189983	FYPO:0000961	normal growth on sorbitol	he FWP190 (git2􏰇) cells can grow in the presence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenylate cyclase appears to confer a salt-sensitive, but not an osmotically sensitive, growth defect.
PMID:15189983	FYPO:0000112	sensitive to sorbitol [has_severity] high	he FWP190 (git2􏰇) cells can grow in the presence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenylate cyclase appears to confer a salt-sensitive, but not an osmotically sensitive, growth defect.
PMID:15189983	FYPO:0000961	normal growth on sorbitol	he FWP190 (git2􏰇) cells can grow in the presence of 2 M sorbitol, which is lethal to JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29) cells. Therefore, the loss of adenylate cyclase appears to confer a salt-sensitive, but not an osmotically sensitive, growth defect.
PMID:15189983	FYPO:0002199	inviable vegetative cell with normal cell morphology	unlike JSP12 (git2􏰇 spc1-12) and JSP29 (git2􏰇 wis1-29), cells that elongate and die, cells of the parental strain FWP190 (git2􏰇) appear to simply arrest growth (Fig. 2)
PMID:15194812	FYPO:0003800	normal chromatin binding at replication origin [assayed_using] PomBase:SPAC17D4.02	(comment: Cdc45 reappears quickly after shift from restrictive to permissive temperature)
PMID:15218150	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 1B)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 1B)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 1B)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 1B)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] low	(Fig. 1B)
PMID:15218150	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Fig. 1B)
PMID:15218150	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Fig. 1B)
PMID:15218150	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Fig. 1B)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 1B)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 1B)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 1B)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1B)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1B)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 1B)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 1B)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1B)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 1B)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1B)
PMID:15218150	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 1B)
PMID:15218150	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 1B)
PMID:15218150	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 1B)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 1B)
PMID:15218150	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 1B)
PMID:15218150	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 1B)
PMID:15218150	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 1B)
PMID:15218150	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 1B)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 1B)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 1B)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 1B)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 1B)
PMID:15218150	FYPO:0008212	abolished histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 1C)
PMID:15218150	FYPO:0008212	abolished histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 1C)
PMID:15218150	FYPO:0008212	abolished histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 1C)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 1C)
PMID:15218150	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 1C)
PMID:15218150	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 1C)
PMID:15218150	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 1C)
PMID:15218150	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 1C)
PMID:15218150	FYPO:0008212	abolished histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 1C)
PMID:15218150	FYPO:0008212	abolished histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 1C)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 1C)
PMID:15218150	FYPO:0008212	abolished histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 1C)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 1C)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 1C)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 1C)
PMID:15218150	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 1C)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 1C)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 1C)
PMID:15218150	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 1C)
PMID:15218150	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Fig. 1C)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 1C)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 1C)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 1C)
PMID:15218150	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 1C)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 1C)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 1C)
PMID:15218150	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 1C)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 1C)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 1C)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 1C)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 2A)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 2A)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 2A)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] low	(Fig. 2A)
PMID:15218150	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 2A)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2A)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2B)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2B)
PMID:15218150	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 2B)
PMID:15218150	FYPO:0008212	abolished histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 2B)
PMID:15218150	FYPO:0008212	abolished histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 2B)
PMID:15218150	FYPO:0008212	abolished histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 2B)
PMID:15218150	FYPO:0008212	abolished histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 2B)
PMID:15218150	FYPO:0008212	abolished histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 2B)
PMID:15218150	FYPO:0008212	abolished histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 2B)
PMID:15218150	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2B)
PMID:15218150	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2B)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2B)
PMID:15218150	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2B)
PMID:15218150	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2B)
PMID:15218150	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2B)
PMID:15218150	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 2B)
PMID:15218150	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 2B)
PMID:15218150	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2B)
PMID:15218150	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC29B5.01	(Fig. 4B)
PMID:15218150	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC21E11.03c	(Fig. 4B)
PMID:15219990	GO:0051537	2 iron, 2 sulfur cluster binding	(comment: spectra looks the same as Adx)
PMID:15226405	FYPO:0004602	normal linear element morphology	(comment: frequency of different stages of LE development is different though, but morphology is normal)
PMID:15226405	FYPO:0004602	normal linear element morphology	(comment: frequency of different stages of LE development is different though, but morphology is normal)
PMID:15249580	GO:0016314	phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity	(Fig. 1c)
PMID:15249580	FYPO:0002788	small vacuoles during vegetative growth [has_penetrance] 70	(comment: mishapen)
PMID:15249580	GO:0016308	1-phosphatidylinositol-4-phosphate 5-kinase activity [part_of] phosphatidylinositol phosphate biosynthetic process	(comment: vw fixed from GO:0052812 to GO:0016308 based on e-mail from Pgaudet) The data are consistent with a model in which its3p, like its mammalian homologue, can convert PI(3)P to PI(3,4)P2 and PI(3,4,5)P3.
PMID:15249580	GO:0052811	1-phosphatidylinositol-3-phosphate 4-kinase activity [part_of] phosphatidylinositol phosphate biosynthetic process	The data are consistent with a model in which its3p, like its mammalian homologue, can convert PI(3)P to PI(3,4)P2 and PI(3,4,5)P3.
PMID:15278909	GO:0005634	nucleus [exists_during] meiotic S phase	(comment: CHECK during premeiotic DNA replication)
PMID:15292231	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] complete [has_severity] high	(Fig. 1)
PMID:15292231	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium [has_penetrance] medium	(Fig. 1) An atf1 deletion strain carrying the ade6+ reporter gene inserted at the mat3-M locus displayed a loss of silencing of the reporter gene (Fig. 1A).
PMID:15292231	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] low [has_severity] low	(Fig. 1) Similar to atf1 mutants, Δpcr1 showed reduced silencing, but the effect was weaker than that of Δatf1 or Δatf1Δpcr1 (Fig. 1B).
PMID:15292231	FYPO:0006994	increased chromatin silencing at centromere otr1L [has_severity] medium	(Fig. 1A) In contrast, the atf1 deletion resulted in increased transcriptional repression at both centromeres and telomeres (Fig. 1A).
PMID:15292231	FYPO:0004542	increased chromatin silencing at subtelomere [has_severity] medium	(Fig. 1A) In contrast, the atf1 deletion resulted in increased transcriptional repression at both centromeres and telomeres (Fig. 1A).
PMID:15292231	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [assayed_transcript] PomBase:SPCC1322.13 [has_severity] medium [has_penetrance] medium	(Fig. 1B)
PMID:15292231	FYPO:0008174	increased histone H4-K16 acetylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2B)
PMID:15292231	FYPO:0008174	increased histone H4-K16 acetylation at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 2B)
PMID:15292231	FYPO:0005063	increased histone H3-K4 methylation at mating type locus during vegetative growth [has_severity] high	(Fig. 2B)
PMID:15292231	FYPO:0004690	increased histone H3-K9 acetylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 2B)
PMID:15292231	FYPO:0007633	increased histone H3-K14 acetylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 2B)
PMID:15292231	FYPO:0008172	increased histone H4-K5 acetylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2B)
PMID:15292231	FYPO:0006752	increased histone H4-K16 acetylation at subtelomeric heterochromatin during vegetative growth [has_severity] high	(Fig. 2B)
PMID:15292231	FYPO:0008173	increased histone H4-K8 acetylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2B)
PMID:15292231	FYPO:0008172	increased histone H4-K5 acetylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2B)
PMID:15292231	FYPO:0007633	increased histone H3-K14 acetylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 2B)
PMID:15292231	FYPO:0004690	increased histone H3-K9 acetylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 2B)
PMID:15292231	FYPO:0008173	increased histone H4-K8 acetylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2B)
PMID:15292231	FYPO:0005063	increased histone H3-K4 methylation at mating type locus during vegetative growth [has_severity] high	(Fig. 2B) Furthermore, ChIP analysis showed that the absence of atf1 and pcr1 resulted in a considerable increase in histone H3/H4 acetylation and euchromatic-specific H3 Lys-4 methylation of the selected region
PMID:15292231	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBC1711.02 [has_severity] low	(Fig. 2C)
PMID:15292231	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBC1711.02 [has_severity] low	(Fig. 2C)
PMID:15292231	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBC1711.02 [has_severity] high	(Fig. 2C)
PMID:15292231	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] medium [has_severity] medium	(Fig. 3)
PMID:15292231	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] low [has_severity] low	(Fig. 3)
PMID:15292231	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] low [has_severity] low	(Fig. 3)
PMID:15292231	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] low [has_severity] low	(Fig. 3) Moreover, the ade6-off to ade6-on conversion in Δsty1 and Δwis1 mutants was significantly reduced relative to wild-type cells, indicating that sty1 and wis1 deletions enhanced stabilization of the epigenetic inheritance of the silent states (Fig. 3B).
PMID:15292231	FYPO:0008172	increased histone H4-K5 acetylation at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 6B)
PMID:15292231	FYPO:0005063	increased histone H3-K4 methylation at mating type locus during vegetative growth [has_severity] low	(Fig. 6B)
PMID:15292231	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 6B)
PMID:15292231	FYPO:0004690	increased histone H3-K9 acetylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 6B)
PMID:15292231	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC1322.13	(comment: ATF/CREB-binding)
PMID:15292231	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC1322.13	(comment: ATF/CREB-binding)
PMID:15292231	GO:0030466	silent mating-type cassette heterochromatin formation	(comment: RNAi-independent mechanism)
PMID:15292231	GO:0030466	silent mating-type cassette heterochromatin formation	(comment: RNAi-independent mechanism)
PMID:15292231	GO:0030466	silent mating-type cassette heterochromatin formation	(comment: RNAi-independent mechanism)
PMID:15292231	GO:0090055	positive regulation of silent mating-type cassette heterochromatin formation	The results presented above suggest that the kinase activity of Wis1 and Sty1/Spc1 is required for proper control of hetero chromatin assembly by Atf1 and Pcr1.
PMID:15292231	GO:0090055	positive regulation of silent mating-type cassette heterochromatin formation	The results presented above suggest that the kinase activity of Wis1 and Sty1/Spc1 is required for proper control of hetero chromatin assembly by Atf1 and Pcr1.
PMID:15297457	GO:0031573	mitotic intra-S DNA damage checkpoint signaling	(comment: CHECK would it be better/safer to annotate to parent generic intra-S checkpoint term?)
PMID:15314153	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: CONDITION 25 degrees)
PMID:15314153	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 30 degrees)
PMID:15316017	GO:0052658	inositol-1,4,5-trisphosphate 5-phosphatase activity	(comment: CHECK activated_by(CHEBI:18420)| inhibited_by(CHEBI:29108))
PMID:15329725	FYPO:0002102	normal mitotic DNA damage checkpoint during cellular response to UV	(Fig. 1d and Fig. 1h)
PMID:15329725	FYPO:0005428	delayed onset of UV-damage excision repair	(Fig. 1f)
PMID:15329725	FYPO:0005429	decreased UV-damage excision repair during mitotic G2 phase	(Fig. 1h)
PMID:1533272	FYPO:0000839	inviable elongated mononucleate aseptate cell [has_severity] high [has_penetrance] complete	(Fig. 2) (comment: CHECK Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid.)
PMID:1533272	FYPO:0000446	cell cycle arrest at mitotic G2/M phase transition [has_penetrance] high	(Fig. 3) (comment: CHECK Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid.)
PMID:1533272	FYPO:0001384	abolished protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 4) (comment: CHECK Histone H1 used as substrate. Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid.)
PMID:1533272	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 5) (comment: Cdc2-DL2 over expressed from an integrated pREP1 (pMNS21) plasmid. Phosphorylation on threonine, but position(s) not determined.)
PMID:1533272	FYPO:0005711	decreased cyclin B1-CDK1 complex level [assayed_using] PomBase:SPBC582.03 [assayed_using] PomBase:SPBC11B10.09	(Fig. 7) (comment: HECK Cdc2-DL2 over expressed from an integrated pREP1/pMNS21 plasmid). (comment: Binds to cdc13 but this is reduced compared to binding of cdc2+ to cdc13)
PMID:1533272	FYPO:0001491	viable vegetative cell	(comment: CHECK cdc13 expressed from own promoter on multi copy plasmid pUR18)
PMID:15340008	FYPO:0003438	mitotic G1/S phase transition delay following nitrogen starvation-induced G1 phase arrest [has_severity] medium	(Fig. 1)
PMID:15340008	FYPO:0008162	increased activation of S-phase DNA damage checkpoint	(Fig. 1,3,4)
PMID:15340008	FYPO:0003306	decreased mitotic index	(Fig. 1C)
PMID:15340008	FYPO:0000029	abnormal chromosome segregation [has_penetrance] low	(Fig. 1D, Fig. 2)
PMID:15340008	FYPO:0001761	normal mitotic G1/S phase transition	(Fig. 2)
PMID:15340008	FYPO:0001513	normal mitotic sister chromatid segregation	(Fig. 2)
PMID:15340008	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] low	(Fig. 3)
PMID:15340008	FYPO:0001513	normal mitotic sister chromatid segregation	(Fig. 3)
PMID:15340008	FYPO:0001513	normal mitotic sister chromatid segregation	(Fig. 3)
PMID:15340008	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] low	(Fig. 3)
PMID:15340008	FYPO:0003503	normal vegetative cell length [has_penetrance] high [has_severity] high	(Fig. 3A)
PMID:15340008	FYPO:0001122	elongated vegetative cell [has_penetrance] high [has_severity] high	(Fig. 3A)
PMID:15340008	FYPO:0003503	normal vegetative cell length [has_penetrance] high [has_severity] high	(Fig. 3A)
PMID:15340008	FYPO:0001122	elongated vegetative cell [has_penetrance] high [has_severity] high	(Fig. 3A)
PMID:15340008	FYPO:0004355	increased protein phosphorylation during mitosis [has_severity] medium [assayed_protein] PomBase:SPCC1259.13	(Fig. 4C)
PMID:15340008	FYPO:0002150	inviable spore population	(Fig. 5A)
PMID:15340008	FYPO:0002150	inviable spore population	(Fig. 5A)
PMID:15340008	FYPO:0002150	inviable spore population	(Fig. 5B)
PMID:15340008	FYPO:0002150	inviable spore population	(Fig. 5B)
PMID:15340008	FYPO:0003612	viable spore population	(Fig. 5C)
PMID:15340008	FYPO:0003612	viable spore population	(Fig. 5D)
PMID:15340008	FYPO:0000361	abnormal nucleolar morphology [has_penetrance] medium	(Fig. 7)
PMID:15359282	FYPO:0002778	decreased protein sumoylation during vegetative growth [assayed_protein] PomBase:SPAC30D11.10 [has_severity] medium	(Fig. 3)
PMID:15359282	FYPO:0002775	decreased level of sumoylated protein in cell [has_severity] high	(Fig. 3A)
PMID:15359282	FYPO:0002775	decreased level of sumoylated protein in cell [has_severity] medium	(Fig. 3A)
PMID:15359282	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 4A)
PMID:15359282	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. 4A)
PMID:15359282	FYPO:0001840	increased minichromosome loss during vegetative growth [has_severity] medium	(Fig. 4B)
PMID:15359282	FYPO:0001840	increased minichromosome loss during vegetative growth [has_severity] high	(Fig. 4B)
PMID:15359282	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] medium	(Fig. 4C)
PMID:15359282	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	(Fig. 4C)
PMID:15359282	FYPO:0003217	decreased chromatin silencing at centromere central core [has_severity] low	(Fig. 4C)
PMID:15359282	FYPO:0003217	decreased chromatin silencing at centromere central core [has_severity] low	(Fig. 4C)
PMID:15359282	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] medium	(Fig. 4C)
PMID:15359282	FYPO:0002150	inviable spore population	(Fig. 6A)
PMID:15359282	FYPO:0002150	inviable spore population	(Fig. 6A)
PMID:15359282	FYPO:0002150	inviable spore population	(Fig. 6A)
PMID:15359282	FYPO:0002150	inviable spore population	(Fig. 6A)
PMID:15359282	FYPO:0000278	decreased cell population growth following spore germination [has_severity] high	(Fig. 6A)
PMID:15359282	FYPO:0000278	decreased cell population growth following spore germination [has_severity] high	(Fig. 6A)
PMID:15359282	FYPO:0000278	decreased cell population growth following spore germination [has_severity] high	(Fig. 6A)
PMID:15359282	FYPO:0000278	decreased cell population growth following spore germination [has_severity] high	(Fig. 6A)
PMID:15359282	FYPO:0002687	normal telomere length during vegetative growth	(Fig. 6B)
PMID:15359282	FYPO:0002687	normal telomere length during vegetative growth	(Fig. 6B)
PMID:15359282	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. 6B)
PMID:15359282	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] low	(Fig. 6B)
PMID:15359282	FYPO:0002687	normal telomere length during vegetative growth	(Fig. 6B)
PMID:15359282	GO:0005634	nucleus	(Figure 2)
PMID:15359282	GO:0019948	SUMO activating enzyme activity [has_input] PomBase:SPAC30D11.13 [part_of] protein sumoylation	(Figure 3) (comment: CHECK E1, activating)
PMID:15359282	GO:0061656	SUMO conjugating enzyme activity [has_input] PomBase:SPAC30D11.13 [part_of] protein sumoylation	(Figure 3) (comment: CHECK E2)
PMID:15359282	GO:0061665	SUMO ligase activity [has_input] PomBase:SPAC30D11.13 [part_of] protein sumoylation	(Figure 3) (comment: CHECK E3)
PMID:15367656	FYPO:0003165	cut [has_penetrance] 10	(comment: no hydroxyurea)
PMID:15369671	FYPO:0002902	decreased protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPCC970.12	(Fig. 4)
PMID:15369671	FYPO:0003786	abolished protein localization to centromere central core during vegetative growth [assayed_using] PomBase:SPBC1105.17	(Fig. 4)
PMID:15369671	FYPO:0002902	decreased protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPCC1672.10	(Fig. 4)
PMID:15369671	GO:0000785	chromatin	In sharp contrast, GFP-tagged Mis16 was enriched in the whole nuclear chromatin region throughout the cell cycle (Figure 3C).
PMID:15371542	FYPO:0001840	increased minichromosome loss during vegetative growth	(Fig. 1)
PMID:15371542	FYPO:0000091	sensitive to thiabendazole	(Fig. 1)
PMID:15371542	FYPO:0000964	normal growth on thiabendazole	(Fig. 1a)
PMID:15371542	FYPO:0001839	normal minichromosome loss	(Fig. 1a)
PMID:15372076	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC16C6.10	(Figure 1)
PMID:15372076	FYPO:0005918	decreased protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPAC18G6.02c	(Figure 1)
PMID:15372076	FYPO:0005918	decreased protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPAC664.01c	(Figure 1)
PMID:15372076	GO:0005721	pericentric heterochromatin	(Figure 1)
PMID:15372076	GO:0005721	pericentric heterochromatin	(Figure 1)
PMID:15372076	GO:0031934	mating-type region heterochromatin	(Figure 1)
PMID:15372076	GO:0140720	subtelomeric heterochromatin	(Figure 1)
PMID:15372076	GO:0005721	pericentric heterochromatin	(Figure 1)
PMID:15372076	GO:0140720	subtelomeric heterochromatin	(Figure 1)
PMID:15372076	GO:0140720	subtelomeric heterochromatin	(Figure 1)
PMID:15372076	GO:0031934	mating-type region heterochromatin	(Figure 1)
PMID:15372076	GO:0031934	mating-type region heterochromatin	(Figure 1)
PMID:15372076	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC18G6.02c	(Figure 1)
PMID:15372076	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Figure 1)
PMID:15372076	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC16C6.10	(Figure 1)
PMID:15372076	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC664.01c	(Figure 1)
PMID:15372076	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	(Figure 1)
PMID:15372076	FYPO:0005918	decreased protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPBC16C6.10	(Figure 1)
PMID:15372076	GO:0030466	silent mating-type cassette heterochromatin formation	H3-K9 methylation at the three heterochromatic regions (CEN-dg223,MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A), suggesting that Rik1 has a critical role in H3-K9 methylation at the native heterochromatic regions.
PMID:15372076	GO:0031508	pericentric heterochromatin formation	H3-K9 methylation at the three heterochromatic regions (CEN-dg223,MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A), suggesting that Rik1 has a critical role in H3-K9 methylation at the native heterochromatic regions.
PMID:15372076	GO:0031509	subtelomeric heterochromatin formation	H3-K9 methylation at the three heterochromatic regions (CEN-dg223,MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A), suggesting that Rik1 has a critical role in H3-K9 methylation at the native heterochromatic regions.
PMID:15372076	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC16C6.10	In contrast, the centromeric localization of Swi6 or Chp2-13myc was specifically decreased in the Dchp1 cells (Figures 2B and C, Dchp1)
PMID:15372076	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC664.01c	In contrast, the centromeric localization of Swi6 or Chp2-13myc was specifically decreased in the Dchp1 cells (Figures 2B and C, Dchp1)
PMID:15372076	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPBC16C6.10	Interestingly, Swi6 was required for the localization of Chp2 to the mating-type region or telomeres but not to the centromeres (Figure 2B, Dswi6).
PMID:15372076	FYPO:0005072	normal protein localization to centromeric chromatin [assayed_protein] PomBase:SPBC16C6.10	Interestingly, Swi6 was required for the localization of Chp2 to the mating-type region or telomeres but not to the centromeres (Figure 2B, Dswi6).
PMID:15372076	FYPO:0005396	abolished protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPBC16C6.10	Interestingly, Swi6 was required for the localization of Chp2 to the mating-type region or telomeres but not to the centromeres (Figure 2B, Dswi6).
PMID:15372076	FYPO:0003097	abolished histone H3-K9 methylation at centromere outer repeat during vegetative growth	Interestingly, we found that swi6þ deletion caused a loss of the H3-K9 methylation at CEN (dg223) in the Dchp1 background (Figure 5D, Dchp1Dswi6), suggesting that Swi6 is required for the maintenance of centromeric H3- K9 methylation in the Dchp1 strain.
PMID:15372076	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth	Interestingly, we found that, although deletion of either swi6 þ or chp2 þ did not affect the H3-K9 methylation at MAT (K-R) and TEL (E12) in the Dchp1 background, the methylation level in these regions was severely decreased in the triple-mutant strain (Figure 5D, Dchp1Dchp2Dswi6). Again, these results demonstrate that Swi6 and Chp2 are required for the maintenance of H3-K9 methylation at the three heterochromatic regions, and also indicate that Swi6 and Chp2 have overlapping functions in the maintenance of H3-K9 methylation.
PMID:15372076	FYPO:0003235	normal histone H3-K9 methylation at centromere outer repeat during vegetative growth	Intriguingly, we found that, even in the Dchp1 cells, histone H3 in native centromeric heterochromatin (CEN-dg223 locus) remained methylated at lysine 9 (Figure 4B, Dchp1).
PMID:15372076	FYPO:0003235	normal histone H3-K9 methylation at centromere outer repeat during vegetative growth	Intriguingly, we found that, even in the Dchp1 cells, histone H3 in native centromeric heterochromatin (CEN-dg223 locus) remained methylated at lysine 9 (Figure 4B, Dchp1).
PMID:15372076	GO:0030466	silent mating-type cassette heterochromatin formation	The present data also demonstrate that Chp1 function is required not only for the centromeres but also for the mating-type region and telomeres.
PMID:15372076	GO:0031509	subtelomeric heterochromatin formation	The present data also demonstrate that Chp1 function is required not only for the centromeres but also for the mating-type region and telomeres.
PMID:15372076	GO:0031508	pericentric heterochromatin formation	Therefore, Chp1 protein was also involved in the production or processing of centromeric RNA transcripts, which might be linked to heterochromatin establishment.
PMID:15372076	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] high	We found that H3-K9 methylation at the three heterochromatic regions (CEN- dg223, MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A)
PMID:15372076	FYPO:0003572	decreased histone H3-K9 methylation at subtelomeric heterochromatin during vegetative growth [has_severity] high	We found that H3-K9 methylation at the three heterochromatic regions (CEN- dg223, MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A)
PMID:15372076	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	We found that H3-K9 methylation at the three heterochromatic regions (CEN- dg223, MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A)
PMID:15372076	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] high	We found that H3-K9 methylation at the three heterochromatic regions (CEN- dg223, MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A)
PMID:15372076	FYPO:0003572	decreased histone H3-K9 methylation at subtelomeric heterochromatin during vegetative growth [has_severity] high	We found that H3-K9 methylation at the three heterochromatic regions (CEN- dg223, MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A)
PMID:15372076	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	We found that H3-K9 methylation at the three heterochromatic regions (CEN- dg223, MAT-K-R, or TEL-E12) was reduced to a level comparable to that in Dclr4 (Figure 6A)
PMID:15372076	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC18G6.02c	We found that the association of Chp1-13myc with the three heterochromatic regions (CEN, MAT, and TEL) was not affected in the absence of swi6 þ or chp2 þ (Figure 2A).
PMID:15372076	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPAC18G6.02c	We found that the association of Chp1-13myc with the three heterochromatic regions (CEN, MAT, and TEL) was not affected in the absence of swi6 þ or chp2 þ (Figure 2A).
PMID:15372076	FYPO:0005072	normal protein localization to centromeric chromatin [assayed_protein] PomBase:SPAC18G6.02c	We found that the association of Chp1-13myc with the three heterochromatic regions (CEN, MAT, and TEL) was not affected in the absence of swi6 þ or chp2 þ (Figure 2A).
PMID:15372076	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC18G6.02c	We found that the association of Chp1-13myc with the three heterochromatic regions (CEN, MAT, and TEL) was not affected in the absence of swi6 þ or chp2 þ (Figure 2A).
PMID:15372076	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPAC18G6.02c	We found that the association of Chp1-13myc with the three heterochromatic regions (CEN, MAT, and TEL) was not affected in the absence of swi6 þ or chp2 þ (Figure 2A).
PMID:15372076	FYPO:0005072	normal protein localization to centromeric chromatin [assayed_protein] PomBase:SPAC18G6.02c	We found that the association of Chp1-13myc with the three heterochromatic regions (CEN, MAT, and TEL) was not affected in the absence of swi6 þ or chp2 þ (Figure 2A).
PMID:15372076	FYPO:0003235	normal histone H3-K9 methylation at centromere outer repeat during vegetative growth	n Dswi6 or Dchp2 cells, the three heterochromatic regions were enriched in K9-methylated H3 at the same level as in wild-type cells (Figure 5B).
PMID:15372076	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth	nexpectedly, the centromeric H3-K9 methylation was also severely decreased in the Dchp1Dchp2 strain (Figure 5D, Dchp1Dchp2).
PMID:15385632	FYPO:0001972	abnormal cell separation after cytokinesis resulting in septated cell	(Fig. 5)
PMID:15385632	FYPO:0001972	abnormal cell separation after cytokinesis resulting in septated cell [has_severity] low	(Fig. 5)
PMID:15385632	FYPO:0006062	ectopic septin ring assembly during vegetative growth	(Fig. 6)
PMID:15385632	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC16A3.01 [assayed_using] PomBase:SPAC9G1.11c	(Figure 1H, Table 1)
PMID:15385632	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC16A3.01	(Figure 1I)
PMID:15385632	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC9G1.11c [assayed_using] PomBase:SPAC4F10.11	(Figure 1J) Based on the lower recovery of coimmunoprecipitated proteins, this Spn1p-Spn4p complex appears to be less stable than in the presence of Spn2p or Spn3p.
PMID:15385632	GO:0005515	protein binding	(Figure 2, D and E)
PMID:15385632	GO:0005515	protein binding	(Figure 2A Figure 2B and C)
PMID:15385632	GO:0005515	protein binding	(Figure 2A)
PMID:15385632	GO:0005515	protein binding	(Figure 2A)
PMID:15385632	GO:0005515	protein binding	(Figure 2A)
PMID:15385632	GO:0005515	protein binding	(Figure 2A, Figure 2, D and E)
PMID:15385632	GO:0005515	protein binding	(Figure 2A, Figure 2, D and E)
PMID:15385632	FYPO:0006060	abolished protein localization to septin ring [assayed_using] PomBase:SPAC4F10.11	(Figure 5)
PMID:15385632	FYPO:0006060	abolished protein localization to septin ring [assayed_using] PomBase:SPAC821.06	(Figure 5)
PMID:15385632	FYPO:0006060	abolished protein localization to septin ring [assayed_using] PomBase:SPBC16A3.01	(Figure 5)
PMID:15385632	FYPO:0006060	abolished protein localization to septin ring [assayed_using] PomBase:SPBC16A3.01	(Figure 5)
PMID:15385632	FYPO:0006060	abolished protein localization to septin ring [assayed_using] PomBase:SPAC821.06	(Figure 5)
PMID:15385632	FYPO:0006060	abolished protein localization to septin ring [assayed_using] PomBase:SPAC9G1.11c	(Figure 5C)
PMID:15385632	FYPO:0003334	normal protein localization to septin ring [assayed_using] PomBase:SPAC9G1.11c	(Figure 6A, D, and E)
PMID:15385632	FYPO:0003334	normal protein localization to septin ring [assayed_using] PomBase:SPAC4F10.11	(Figure 6A, D, and E)
PMID:15385632	FYPO:0006062	ectopic septin ring assembly during vegetative growth	(Figure 6A, D, and E)
PMID:15385632	FYPO:0003334	normal protein localization to septin ring [assayed_using] PomBase:SPBC16A3.01	(Figure 6A, D, and E)
PMID:15385632	FYPO:0003334	normal protein localization to septin ring [assayed_using] PomBase:SPAC4F10.11	(Figure 6A, D, and E)
PMID:15385632	FYPO:0003334	normal protein localization to septin ring [assayed_using] PomBase:SPAC9G1.11c	(Figure 6A, D, and E)
PMID:15385632	FYPO:0006062	ectopic septin ring assembly during vegetative growth	(Figure 6A, D, and E)
PMID:15385632	FYPO:0003334	normal protein localization to septin ring [assayed_using] PomBase:SPAC821.06	(Figure 6A, D, and E)
PMID:15385632	GO:0000921	septin ring assembly	Combining this observation with our biochemical data, we conclude that a subcomplex of Spn1p-Spn4p is sufficient for formation of ectopic structures and localizing to the medial cortex, but at least one other septin is required for assembly of a ring structure.
PMID:15385632	GO:0000921	septin ring assembly	Combining this observation with our biochemical data, we conclude that a subcomplex of Spn1p-Spn4p is sufficient for formation of ectopic structures and localizing to the medial cortex, but at least one other septin is required for assembly of a ring structure.
PMID:15385632	GO:0031106	septin ring organization	In this case, Spn3p-GFP was recruited to the medial region before mitosis as before (Figure 8A) and it was now assembled into highly organized ring structures that were easily visualized as split rings once septa had formed (Figure 8, B and C). Virtually no diffuse disk structures were observed (Figure 8, B-D). We conclude from this experiment that Mid2p is solely responsible directly or indirectly for regulating septin ring coalesence in S. pombe.
PMID:15385632	FYPO:0006063	septin ring assembly during mitotic interphase	erexpression was the relative persistence of septin rings and the inhibition of mitotic progression, as determined by monitoring the formation of binucleates (Figure 8A). This result is consistent with our previous results, indicating that prolonged expression of Mid2p stabilizes septin ring structures and influences cell cycle progression (Tasto et al., 2003). erexpression was the relative persistence of septin rings and the inhibition of mitotic progression, as determined by monitoring the formation of binucleates (Figure 8A). This result is consistent with our previous results, indicating that prolonged expression of Mid2p stabilizes septin ring structures and influences cell cycle progression (Tasto et al., 2003).
PMID:1538784	GO:0044732	mitotic spindle pole body	(comment: CHECK throughout_cell_cycle)
PMID:15470240	FYPO:0002903	viable pear-shaped vegetative cell	(Fig. 2)
PMID:15470240	FYPO:0004256	viable lemon-shaped cell	(Fig. 2)
PMID:15470240	FYPO:0002903	viable pear-shaped vegetative cell	(Fig. 2)
PMID:15471884	GO:0070337	3'-flap-structured DNA binding	(comment: lower affinity than for Y-form DNA)
PMID:15475954	GO:0005721	pericentric heterochromatin	(Fig. 1)
PMID:15475954	GO:0031934	mating-type region heterochromatin	(Fig. 1)
PMID:15475954	GO:0140720	subtelomeric heterochromatin	(Fig. 1)
PMID:15475954	GO:0140720	subtelomeric heterochromatin	(Fig. 1)
PMID:15475954	GO:0005721	pericentric heterochromatin	(Fig. 1)
PMID:15475954	GO:0005721	pericentric heterochromatin	(Fig. 1)
PMID:15475954	GO:0140720	subtelomeric heterochromatin	(Fig. 1)
PMID:15475954	GO:0031934	mating-type region heterochromatin	(Fig. 1)
PMID:15475954	GO:0031934	mating-type region heterochromatin	(Fig. 1)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2B)
PMID:15475954	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 2B)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2B)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2B)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 2B)
PMID:15475954	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 2B)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] low	(Fig. 2B)
PMID:15475954	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Fig. 2B)
PMID:15475954	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 2B)
PMID:15475954	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 2B)
PMID:15475954	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 2B)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 2B)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 2B)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 2B)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 2B)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] low	(Fig. 2B)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 2B)
PMID:15475954	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 2B)
PMID:15475954	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Fig. 2B)
PMID:15475954	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 2B)
PMID:15475954	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 2B)
PMID:15475954	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 2B)
PMID:15475954	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Fig. 2B)
PMID:15475954	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 2B)
PMID:15475954	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 2B)
PMID:15475954	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Fig. 2B)
PMID:15475954	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 2B)
PMID:15475954	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 2B)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2B)
PMID:15475954	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 2B)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 2C)
PMID:15475954	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2C)
PMID:15475954	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2C)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2C)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2C)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2C)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2C)
PMID:15475954	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2C)
PMID:15475954	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2C)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2C)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2C)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2C)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 2C)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2C)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2C)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2C)
PMID:15475954	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2C)
PMID:15475954	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2C)
PMID:15475954	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 2C)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2C)
PMID:15475954	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Fig. 2C)
PMID:15475954	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 2C)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 2C)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 2C)
PMID:15475954	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 2C)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 2C)
PMID:15475954	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 2C)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 2C)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 2C)
PMID:15475954	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 2C)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC18G6.02c [has_severity] medium	(Fig. 3)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC83.03c [has_severity] medium	(Fig. 3)
PMID:15475954	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC83.03c	(Fig. 4)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC18G6.02c [has_severity] low	(Fig. 4)
PMID:15475954	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	(Fig. 4)
PMID:15475954	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPBC83.03c	(Fig. 4)
PMID:15475954	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 5B)
PMID:15475954	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 5B)
PMID:15475954	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 5D)
PMID:15475954	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 5D)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 6A)
PMID:15475954	FYPO:0008212	abolished histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 6A)
PMID:15475954	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 6A)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC18G6.02c [has_severity] medium	(Fig. 6B)
PMID:15475954	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	(Fig. 6B)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC18G6.02c [has_severity] high	(Fig. 6B)
PMID:15475954	FYPO:0008236	normal siRNA loading onto RITS complex	(Fig. 7A)
PMID:15475954	FYPO:0008236	normal siRNA loading onto RITS complex	(Fig. 7A)
PMID:15475954	FYPO:0008011	abolished siRNA loading onto RITS complex	(Fig. 7A)
PMID:15475954	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPAC18G6.02c [has_severity] high	(Fig. 7B)
PMID:15475954	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 7B)
PMID:15475954	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. 7B)
PMID:15475954	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC18G6.02c [has_severity] high	(Fig. 7B)
PMID:15475954	FYPO:0008011	abolished siRNA loading onto RITS complex	(Fig. 7C)
PMID:15475954	FYPO:0008011	abolished siRNA loading onto RITS complex	(Fig. 7C)
PMID:15475954	GO:0030466	silent mating-type cassette heterochromatin formation	These results indicate that RITS and Atf1-Pcr1 participate in distinct and parallel pathways to nucleate heterochromatin at the mat locus.
PMID:15475954	GO:0030466	silent mating-type cassette heterochromatin formation	These results indicate that RITS and Atf1-Pcr1 participate in distinct and parallel pathways to nucleate heterochromatin at the mat locus.
PMID:15475954	GO:0030466	silent mating-type cassette heterochromatin formation	These results indicate that RITS and Atf1-Pcr1 participate in distinct and parallel pathways to nucleate heterochromatin at the mat locus.
PMID:15485922	FYPO:0005402	increased telomeric 3' overhang length during vegetative growth	(comment: same as taz1delta alone)
PMID:15485922	FYPO:0005402	increased telomeric 3' overhang length during vegetative growth	(comment: same as taz1delta alone)
PMID:15504913	GO:0016460	myosin II complex	(Fig. 1)
PMID:15504913	GO:0016460	myosin II complex	(Fig. 1)
PMID:15504913	GO:0033275	actin-myosin filament sliding	(Fig. 3)
PMID:15504913	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC645.05c [assayed_protein] PomBase:SPCC613.04c	(Fig. 3B, 3C)
PMID:15504913	FYPO:0000161	abnormal actomyosin contractile ring assembly	(Fig. 4A)
PMID:15504913	FYPO:0000418	decreased cytokinesis	(Fig. 4A)
PMID:15504913	FYPO:0001252	multinucleate multiseptate vegetative cell	(Fig. 4A)
PMID:15504913	FYPO:0000418	decreased cytokinesis	(Fig. 4B)
PMID:15504913	FYPO:0000161	abnormal actomyosin contractile ring assembly	(Fig. 4B)
PMID:15504913	FYPO:0001252	multinucleate multiseptate vegetative cell	(Fig. 4B)
PMID:15504913	FYPO:0000418	decreased cytokinesis	(Fig. 4C)
PMID:15504913	FYPO:0001252	multinucleate multiseptate vegetative cell	(Fig. 4C)
PMID:15504913	FYPO:0000161	abnormal actomyosin contractile ring assembly	(Fig. 4C)
PMID:15504913	FYPO:0001357	normal vegetative cell population growth	(Fig. 6B)
PMID:15504913	FYPO:0000304	sensitive to stress during vegetative growth [has_severity] high	(Fig. 6B)
PMID:15504913	FYPO:0001357	normal vegetative cell population growth	(Fig. 6B)
PMID:15504913	FYPO:0001367	normal cytokinesis	(Fig. 6C)
PMID:15504913	FYPO:0008207	normal microfilament motor activity	(Table 1)
PMID:15504913	FYPO:0007603	decreased microfilament motor activity [has_severity] high	(Table 1)
PMID:15504913	FYPO:0007603	decreased microfilament motor activity [has_severity] high	(Table 1)
PMID:15504913	FYPO:0006025	abolished actin filament binding [assayed_protein] PomBase:SPCC645.05c	(Table 1)
PMID:15504913	FYPO:0007603	decreased microfilament motor activity [has_severity] high	(Table 1)
PMID:15504913	FYPO:0007603	decreased microfilament motor activity [has_severity] high	(Table 1)
PMID:15504913	FYPO:0007603	decreased microfilament motor activity [has_severity] high	(Table 1)
PMID:15504913	FYPO:0008207	normal microfilament motor activity	(Table 1)
PMID:15504913	FYPO:0008207	normal microfilament motor activity	(Table 1)
PMID:15504913	FYPO:0008207	normal microfilament motor activity	(Table 1)
PMID:15504913	FYPO:0008207	normal microfilament motor activity	(Table 1)
PMID:15504913	FYPO:0007603	decreased microfilament motor activity [has_severity] low	(Table 1)
PMID:15504913	FYPO:0007603	decreased microfilament motor activity [has_severity] low	(Table 1)
PMID:15504913	FYPO:0006025	abolished actin filament binding [assayed_protein] PomBase:SPCC645.05c	(Table 1)
PMID:15504913	FYPO:0008207	normal microfilament motor activity	(Table 1)
PMID:15504913	GO:0110085	mitotic actomyosin contractile ring	Rng3p-GFP3 and Rng3p-YFP3 concentrated in contractile rings from anaphase B through constriction (Fig. 5).
PMID:15504913	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic anaphase B	Rng3p-GFP3 and Rng3p-YFP3 concentrated in contractile rings from anaphase B through constriction (Fig. 5).
PMID:15504913	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic telophase	Rng3p-GFP3 and Rng3p-YFP3 concentrated in contractile rings from anaphase B through constriction (Fig. 5).
PMID:15509783	FYPO:0000091	sensitive to thiabendazole [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPAC23H3.08c	(Fig. 7B)
PMID:15509783	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPAC23H3.08c	(Fig. 7B)
PMID:15509783	FYPO:0000229	cut	(Fig. 7D)
PMID:15509783	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 7D)
PMID:15509783	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Figure 1B)
PMID:15509783	FYPO:0000229	cut	(Figure 1B)
PMID:15509783	GO:0000776	kinetochore [exists_during] mitotic metaphase	(Figure 2A)
PMID:15509783	FYPO:0008164	abnormal protein localization to kinetochore during mitotic M phase [assayed_protein] PomBase:SPCC1322.12c	(comment: checkpoint)
PMID:15509783	FYPO:0000786	increased plasmid loss [has_penetrance] 3.5	Table2
PMID:15509783	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 2.4	Table2
PMID:15509783	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 17.5	Table2
PMID:15509783	FYPO:0000786	increased plasmid loss [has_penetrance] 0.1	Table2
PMID:15509783	FYPO:0000786	increased plasmid loss [has_penetrance] 0.2	Table2
PMID:15509865	FYPO:0000927	abolished horsetail movement	(Fig. 2A)
PMID:15509865	FYPO:0000927	abolished horsetail movement	(Fig. 2A)
PMID:15509865	FYPO:0005383	normal duration of meiosis I	(Fig. 2B,C)
PMID:15509865	GO:0005515	protein binding	(Fig. 3B)
PMID:15509865	GO:0005515	protein binding	(Fig. 3B)
PMID:15509865	GO:0005515	protein binding	(Fig. 3C)
PMID:15509865	FYPO:0004731	normal protein localization to interphase microtubule plus-end	(Fig. 6A-C), (comment: CHECK during meiotic prophase, shmooing)
PMID:15509865	FYPO:0005814	abolished protein localization to microtubule plus-end	(Fig. 6B,C) (comment: in meiotic cells, shmooing cells)
PMID:15509865	FYPO:0005814	abolished protein localization to microtubule plus-end	(Fig. 6B,C). (comment: in meiotic cells, shmooing cells)
PMID:15509865	FYPO:0004764	normal protein localization to meiotic spindle pole body during meiosis I	(Fig. 6B,C). (comment: in meiotic cells, shmooing cells)
PMID:15509865	FYPO:0004764	normal protein localization to meiotic spindle pole body during meiosis I	(Fig. 6B,C). in meiotic cells, shmooing cells
PMID:15509865	FYPO:0003179	decreased intragenic meiotic recombination	(Table 2).leu1 and his2 loc, reduced 12 fold
PMID:15509865	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 20	(Table 3)
PMID:15509865	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 20	(Table 3)
PMID:15509865	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 20	(Table 3)
PMID:15509865	FYPO:0003025	decreased homologous chromosome pairing [has_penetrance] 42	(Table 3) assayed using pairing of his2 loci
PMID:15509865	FYPO:0006128	normal duration of meiosis II	(comment: CHECK DURATION) Fig. 2B,C
PMID:15509865	FYPO:0006130	abolished protein localization to microtubule during meiosis	(comment: CHECK meiosis)
PMID:15509865	FYPO:0004093	normal meiotic telomere clustering	data not shown
PMID:15509865	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores	data not shown , phenocopies ssm4 & dhc1
PMID:15509865	FYPO:0000927	abolished horsetail movement	data not shown , phenocopies ssm4 &dhc1
PMID:15525536	GO:0072479	response to mitotic cell cycle spindle assembly checkpoint signaling	(comment: only required when there are problems , possibly involved in repair of monoorientation)
PMID:15537393	FYPO:0001355	decreased vegetative cell population growth	(Figure 2d)
PMID:15537393	FYPO:0002061	inviable vegetative cell population	(Figure 2d)
PMID:15537393	FYPO:0008114	sensitive to amiloride [has_severity] low	(Figure 2e)
PMID:15537393	FYPO:0004078	normal growth on cyclosporin A [has_severity] low	(Figure 2e)
PMID:15537393	FYPO:0008115	increased cell population growth on sorbitol carbon source [has_severity] low	(Figure 2e)
PMID:15537393	FYPO:0000098	sensitive to calcium [has_severity] high	(Figure 2e)
PMID:15537393	FYPO:0000094	sensitive to benomyl [has_severity] low	(Figure 2e)
PMID:15537393	FYPO:0000223	elongated multiseptate vegetative cell [has_penetrance] 11	(Figure 2f)
PMID:15537393	FYPO:0002196	abnormal vegetative cell shape	(Figure 2f)
PMID:15537393	FYPO:0001489	inviable vegetative cell [has_penetrance] 5	(Figure 2f)
PMID:15537393	FYPO:0001327	increased protein level during vegetative growth	(Figure 2g)
PMID:15537393	FYPO:0000647	vegetative cell lysis	(Figure 3b)
PMID:15537393	FYPO:0002050	branched elongated multinucleate aseptate vegetative cell	(Figure 3b)
PMID:15537393	FYPO:0001190	sensitive to cell wall-degrading enzymes	(Figure 3c)
PMID:15537393	FYPO:0001190	sensitive to cell wall-degrading enzymes	(Figure 3c)
PMID:15537393	FYPO:0001082	decreased cell wall beta-glucan level	(Figure 3d)
PMID:15537393	FYPO:0001082	decreased cell wall beta-glucan level	(Figure 3d)
PMID:15537537	FYPO:0000470	decreased mating type switching [has_penetrance] low	(Fig. 1A)
PMID:15537537	FYPO:0000470	decreased mating type switching [has_penetrance] high	(Fig. 1A)
PMID:15537537	FYPO:0000470	decreased mating type switching [has_penetrance] low	(Fig. 1A)
PMID:15537537	FYPO:0000470	decreased mating type switching [has_penetrance] high	(Fig. 1A)
PMID:15537537	GO:0005634	nucleus	(Fig. 2B)
PMID:15537537	GO:0031934	mating-type region heterochromatin	(Fig. 2F)
PMID:15537537	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Fig. 2G)
PMID:15537537	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] low	(Fig. 2G)
PMID:15537537	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 2G)
PMID:15537537	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Fig. 2G)
PMID:15537537	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC1142.03c	(Fig. 2G)
PMID:15537537	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC1142.03c	(Fig. 2G)
PMID:15537537	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC1142.03c	(Fig. 2G)
PMID:15537537	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC1142.03c	(Fig. 2G)
PMID:15537537	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPBC409.03	(Fig. 5)
PMID:15537537	FYPO:0008070	normal histone H3-K9 methylation at centromere during vegetative growth	(Fig. S1)
PMID:15537537	FYPO:0005865	normal histone H3-K9 methylation at silent mating-type cassette during vegetative growth	(Fig. S1)
PMID:15537537	FYPO:0002360	normal chromatin silencing at centromere	(Fig. S1)
PMID:15537537	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. S1)
PMID:15537537	GO:0031934	mating-type region heterochromatin	Swi5 localization pattern closely resembled that of Swi2. Fig. 5
PMID:15546915	FYPO:0007949	increased (1->3)-beta-D-glucan level	(1-3 beta D) As shown in Fig. 6C, there was an increase in the amount of β-glucan in cells that overexpressed rgf3+ compared with wild-type cells (16% and 10%, respectively)
PMID:15546915	FYPO:0002159	decreased 1,3-beta-D-glucan synthase activity	(Fig. 1A)
PMID:15546915	FYPO:0000647	vegetative cell lysis	(Fig. 1A)
PMID:15546915	FYPO:0002150	inviable spore population	(Fig. 3A)
PMID:15546915	FYPO:0001253	elongated multinucleate multiseptate vegetative cell, single septa between nuclei	(Fig. 6A) + DAPI staining revealed that, in most multiseptate cells, each compartment contained one nucleus, indicative of a defect in cell separation after septum assembly (not shown)
PMID:15546915	FYPO:0001968	increased 1,3-beta-D-glucan synthase activity	(Fig. 6B)....an increase in enzymatic activity was detected in cells overexpressing rgf3+ compared with the activity observed in the wild-type strain
PMID:15546915	FYPO:0001123	elongated spore	(Figure 3B) indicates a bypass of cytokinesis checkpoint
PMID:15546915	FYPO:0000951	inviable small vegetative cell	(Figure 3C) (comment: CHECK shrunken cell)
PMID:15546915	FYPO:0000951	inviable small vegetative cell	(Figure 3C) (comment: CHECK shrunken cell)
PMID:15546915	FYPO:0002061	inviable vegetative cell population	(Figure 4)
PMID:15546915	FYPO:0004892	normal growth on echinocandin	(Figure 4) GI Rho1 OEX rescues echinocandin sensitivity
PMID:15546915	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPAC1F7.04 [occurs_in] cell division site	(Figure 5) These results indicate that Rgf3p acts as a specific Rho1p activator in S. pombe.
PMID:15546915	PomGeneEx:0000011	RNA level increased [during] mitotic telophase	(comment: CHECK replace with cytokinetic phase)
PMID:15546915	FYPO:0007949	increased (1->3)-beta-D-glucan level	As shown in Fig. 6C, there was an increase in the amount of β-glucan in cells that overexpressed rgf3+ compared with wild-type cells (16% and 10%, respectively)
PMID:15548596	FYPO:0002134	decreased protein-RNA interaction	(comment: three-hybrid assay involving Uaf2, Prp2, and an RNA fragment containing the heterologous beta-globin 3′ splice site)
PMID:15550243	FYPO:0008179	decreased histone H4-K20 monomethylation during vegetative growth [has_severity] high	(Fig. 1)
PMID:15550243	FYPO:0004217	abolished histone H4-K20 dimethylation during vegetative growth	(Fig. 1)
PMID:15550243	FYPO:0004126	abolished histone H3-K4 trimethylation during vegetative growth	(Fig. 1)
PMID:15550243	FYPO:0004224	decreased histone H4-K20 trimethylation during vegetative growth [has_severity] high	(Fig. 1)
PMID:15550243	FYPO:0004218	abolished histone H4-K20 trimethylation during vegetative growth	(Fig. 1) Expression of exogenous wt HA- tagged Set9 but not Set9Y220A was able to rescue H4- K20 methylation in set9Δ cells (Figure 1E).
PMID:15550243	GO:0140943	histone H4K20 trimethyltransferase activity [has_input] PomBase:SPAC1834.03c [part_of] mitotic G2 DNA damage checkpoint signaling	(Fig. 1, 3 and 4)
PMID:15550243	GO:0140943	histone H4K20 trimethyltransferase activity [has_input] PomBase:SPBC8D2.03c [part_of] mitotic G2 DNA damage checkpoint signaling	(Fig. 1, 3 and 4)
PMID:15550243	GO:0140943	histone H4K20 trimethyltransferase activity [has_input] PomBase:SPBC1105.12 [part_of] mitotic G2 DNA damage checkpoint signaling	(Fig. 1, 3 and 4)
PMID:15550243	FYPO:0004217	abolished histone H4-K20 dimethylation during vegetative growth	(Fig. 1, Figure 1D) shows that the modification is specifically Set9 dependent, as loss of Set9 but not Set1, Set2, Set6, or Clr4 resulted in essentially undetectable mono-, di-, and trimethylated H4-K20.
PMID:15550243	FYPO:0004218	abolished histone H4-K20 trimethylation during vegetative growth	(Fig. 1, Figure 1D) shows that the modification is specifically Set9 dependent, as loss of Set9 but not Set1, Set2, Set6, or Clr4 resulted in essentially undetectable mono-, di-, and trimethylated H4-K20.
PMID:15550243	GO:0042393	histone binding	(Fig. 1A)
PMID:15550243	FYPO:0000265	sensitive to DNA damage [has_severity] medium	(Fig. 3)
PMID:15550243	FYPO:0000265	sensitive to DNA damage [has_severity] medium	(Fig. 3)
PMID:15550243	FYPO:0000265	sensitive to DNA damage [has_severity] medium	(Fig. 3)
PMID:15550243	FYPO:0000265	sensitive to DNA damage [has_severity] medium	(Fig. 3)
PMID:15550243	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3)
PMID:15550243	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3)
PMID:15550243	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3)
PMID:15550243	FYPO:0002897	decreased protein phosphorylation during cellular response to DNA damage [assayed_protein] PomBase:SPCC1259.13 [has_severity] medium	(Fig. 4C)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] medium	(Fig. 4D)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] low	(Fig. 4D)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] low	(Fig. 4D)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] medium	(Fig. 4D)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] medium	(Fig. 4D)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] medium	(Fig. 4D)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] medium	(Fig. 4D)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] medium	(Fig. 4D)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] medium	(Fig. 4D)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] high	(Fig. 4D)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] high	(Fig. 4D)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] high	(Fig. 4D)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] high	(Fig. 4D)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] low	(Fig. 4D)
PMID:15550243	FYPO:0002898	abolished protein phosphorylation during cellular response to DNA damage [assayed_protein] PomBase:SPBC342.05	(Fig. 5)
PMID:15550243	FYPO:0004372	decreased response to mitotic G2 DNA damage checkpoint signaling [has_severity] high	(Fig. 5)
PMID:15550243	FYPO:0007272	decreased protein localization to nucleoplasm during cellular response to DNA damage [assayed_protein] PomBase:SPBC342.05	(Fig. 5) Crb2 phosphorylation is markedly compromised in the absence of Set9, even at low IR doses (Figure 5A).
PMID:15550243	FYPO:0004372	decreased response to mitotic G2 DNA damage checkpoint signaling [has_severity] high	(Fig. 5) Further, the double mutant displays a checkpoint defect equivalent to that of the crb2Δ mutant (Figure 5C).
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] low	(Fig. 5B)
PMID:15550243	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] high	(Fig. 5B) Clearly, this is not the case, as the sensitivity of the double crb2T215A-set9Δ mutant is much greater than either single mutant alone and equal to deletion of crb2+ (Figure 5B).
PMID:15550243	GO:0140999	histone H3K4 trimethyltransferase activity [has_input] PomBase:SPBC1105.11c	(Figure 1)
PMID:15550243	GO:0140999	histone H3K4 trimethyltransferase activity [has_input] PomBase:SPAC1834.04	(Figure 1)
PMID:15550243	GO:0140999	histone H3K4 trimethyltransferase activity [has_input] PomBase:SPBC8D2.04	(Figure 1)
PMID:15550243	FYPO:0000964	normal growth on thiabendazole	Neither loss of Set9 protein, its catalytic activity, nor its H4-K20 substrate rendered cells hypersensitive to TBZ over a range of concentrations (10-30 μg/ml) or temperatures (18°C-36°C) (Figure 2D
PMID:15550243	FYPO:0000085	sensitive to camptothecin [has_severity] high	resulted in cells hyper-sensitive to DNA damage induced by ultraviolent (UV) light, ionizing radiation (IR), and the topoisomerase I poison camptothecin (CPT) (Figure 3A).
PMID:15550243	FYPO:0004372	decreased response to mitotic G2 DNA damage checkpoint signaling [has_severity] medium	set9 cells arrested similar to wt but reentered mitosis markedly faster. Unlike wt, 20%-30% of set9 cells exhibited an abberant or “cut-like” mitotic phenotype. Fig. 4
PMID:15572668	FYPO:0004780	decreased protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	(Fig. 2D)
PMID:15572668	FYPO:0008198	decreased protein localization to plasma membrane during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	(Fig. 2D)
PMID:15572668	FYPO:0002779	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	(Fig. 4A)
PMID:15572668	FYPO:0006326	decreased protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15 [has_severity] medium	(Fig. 4A)
PMID:15572668	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	(Fig. 4A)
PMID:15572668	FYPO:0001514	decreased protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	(Fig. 4A)
PMID:15572668	FYPO:0007133	normal protein localization to medial cortical node during mitotic interphase [assayed_protein] PomBase:SPCC4B3.15	(Fig. 4A)
PMID:15572668	FYPO:0006326	decreased protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15 [has_severity] high	(Fig. 4A)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 99 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 80 [has_severity] medium	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 29 [has_severity] medium	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 49 [has_severity] medium	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 47 [has_severity] medium	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 33 [has_severity] medium	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 50 [has_severity] medium	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 27 [has_severity] medium	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 62 [has_severity] medium	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 98 [has_severity] high	(Table 2)
PMID:15572668	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] high [has_severity] high	(Table 2)
PMID:15572668	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	Cter-GFP mutated in the helix (Helix* Cter-GFP) was concentrated in the nucleus, even during mitosis (arrow in Fig. 2C)
PMID:15572668	FYPO:0002718	abnormal protein localization to septum [assayed_protein] PomBase:SPCC4B3.15	Cter-GFP was then observed in the region of septum formation (Fig. 1B, 16 to 52 min), where it was probably associated with the ingressing plasma membrane of the cleavage furrow. [...] An association with the cell tips and septum region was never observed for wild-type mid1p and may either result from the truncation of mid1p or from the higher concentration of this construct.
PMID:15572668	FYPO:0001584	abnormal protein localization to cell tip during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	Finally, Cter-GFP remained more concentrated at the new tip compared to the old tip in short cells after sister cell separation. [...] An association with the cell tips and septum region was never observed for wild-type mid1p and may either result from the truncation of mid1p or from the higher concentration of this construct.
PMID:15572668	FYPO:0006552	increased protein localization to cytoplasm [assayed_protein] PomBase:SPCC4B3.15	When mutations in the helix were combined with mutations in the NLS (Helix* NLS* Cter-GFP), Cter-GFP was found in the cytoplasm. Fig. 2C
PMID:15601865	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC644.12 [assayed_protein] PomBase:SPAC29A4.08c	(Fig. 3)
PMID:15601865	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC29A4.08c [assayed_protein] PomBase:SPAC29A4.08c	As expected from the two-hybrid results, neither the U-box (His6-Prp19p 1-58) nor the C terminus containing the WD40 repeats (His6-Prp19p 165-503) was able to tetramerize (data not shown).
PMID:15601865	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC29A4.08c [assayed_protein] PomBase:SPAC29A4.08c	As expected from the two-hybrid results, neither the U-box (His6-Prp19p 1-58) nor the C terminus containing the WD40 repeats (His6-Prp19p 165-503) was able to tetramerize (data not shown).
PMID:15601865	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC29A4.08c [assayed_protein] PomBase:SPAC29A4.08c	As expected from the two-hybrid results, neither the U-box (His6-Prp19p 1-58) nor the C terminus containing the WD40 repeats (His6-Prp19p 165-503) was able to tetramerize (data not shown).
PMID:15607976	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	(Fig. 2A)
PMID:15607976	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	(Fig. 2A)
PMID:15607976	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	(Fig. 2B)
PMID:15607976	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	(Fig. 2B)
PMID:15607976	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	(Fig. 2B)
PMID:15607976	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] high [assayed_protein] PomBase:SPBC83.03c	(Fig. 2C and D)
PMID:15607976	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] high [assayed_protein] PomBase:SPBC83.03c	(Fig. 2C and D)
PMID:15607976	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC83.03c [assayed_protein] PomBase:SPAC6F12.09	(Fig. 3C)
PMID:15607976	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC83.03c [assayed_protein] PomBase:SPAC6F12.09	(Fig. 3C)
PMID:15607976	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC1739.03 [assayed_protein] PomBase:SPBC83.03c	(Fig. 3C)
PMID:15607976	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC18G6.02c [assayed_protein] PomBase:SPCC1739.03	(Fig. 3C)
PMID:15607976	FYPO:0008011	abolished siRNA loading onto RITS complex	(Fig. 3D)
PMID:15607976	FYPO:0008011	abolished siRNA loading onto RITS complex	(Fig. 3D)
PMID:15607976	FYPO:0008011	abolished siRNA loading onto RITS complex	(Fig. 3D)
PMID:15607976	FYPO:0008011	abolished siRNA loading onto RITS complex	(Fig. 3D)
PMID:15607976	FYPO:0008010	decreased RNA-dependent RNA polymerase [has_severity] high [assayed_enzyme] PomBase:SPAC6F12.09	(Fig. 6C and E)
PMID:15607976	FYPO:0008010	decreased RNA-dependent RNA polymerase [has_severity] high [assayed_enzyme] PomBase:SPAC6F12.09	(Fig. 6E)
PMID:15607976	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	(Fig. 6F)
PMID:15607976	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	(Fig. 6F)
PMID:15607976	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	(Fig. 6F)
PMID:15607976	FYPO:0008235	abolished nuclear RNA-directed RNA polymerase complex assembly	(Table 1)
PMID:15607976	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC18G6.02c [assayed_protein] PomBase:SPCC1739.03	(Table 1)
PMID:15607976	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC18G6.02c [assayed_protein] PomBase:SPCC1739.03	(Table 1)
PMID:15607976	FYPO:0008235	abolished nuclear RNA-directed RNA polymerase complex assembly	(Table 1)
PMID:15607976	FYPO:0008235	abolished nuclear RNA-directed RNA polymerase complex assembly	(Table 1)
PMID:15607976	GO:0003968	RNA-directed RNA polymerase activity [part_of] siRNA-mediated pericentric heterochromatin formation	The deletion analysis then indicates that the RNA synthesis activity observed in our experiments is intrinsic to Rdp1. Finally, loss of enzymatic activity for the above Rdp1 truncations correlated with the loss of centromeric silencing (Figure 6F). We also examined the activity of an Rdp1 active site point mutation and found that it lacked activity in vitro and silencing function in vivo (T. Sugiyama et al., submitted). Together these results suggest that activity of Rdp1 is required for RNAi-mediated transcriptional gene silencing.
PMID:15611161	FYPO:0001357	normal vegetative cell population growth	(Table 2). Cells containing pka1-T36E (SP870c) or pka1-T356D (SP870d) alleles have a doubling time similar to wild-type cells (SP870a).
PMID:15611161	FYPO:0001357	normal vegetative cell population growth	(Table 2). Cells containing pka1-T36E (SP870c) or pka1-T356D (SP870d) alleles have a doubling time similar to wild-type cells (SP870a).
PMID:15611161	FYPO:0001234	slow vegetative cell population growth	(Table 2). In contrast, the doubling time of cells containing the pka1-T356A allele (SP870b; doubling time similar to that of cells containing a loss-of function pka1 5.1 hr) is more
PMID:15611161	FYPO:0000280	sterile	As shown in Figure 3, ksg1.12 cells fail to conjugate but undergo meiosis in response to nitrogen starvation.
PMID:15611161	FYPO:0001829	normal growth on gluconate carbon source	As shown in Figure 5A, both ksg1.12 cells and the pka1 mutant, git6-261 utilize gluconate as well as wild-type cells.
PMID:15611161	FYPO:0001829	normal growth on gluconate carbon source	As shown in Figure 5A, both ksg1.12 cells and the pka1 mutant, git6-261 utilize gluconate as well as wild-type cells.
PMID:15611161	FYPO:0006660	loss of viability upon G0 to G1 transition [has_severity] low	At daily intervals, the viability of cells from each culture was determined by plating a portion of each onto fresh medium.
PMID:15611161	FYPO:0001004	viable upon G0 to G1 transition [has_penetrance] complete	At daily intervals, the viability of cells from each culture was determined by plating a portion of each onto fresh medium. In contrast, continuing survivability of both ksg1.12 and cgs1::ura4 ksg1.12 was excellent in all three media tested (Figure 5E).
PMID:15611161	FYPO:0001004	viable upon G0 to G1 transition [has_penetrance] complete	At daily intervals, the viability of cells from each culture was determined by plating a portion of each onto fresh medium. In contrast, continuing survivability of both ksg1.12 and cgs1::ura4 ksg1.12 was excellent in all three media tested (Figure 5E).
PMID:15611161	FYPO:0006660	loss of viability upon G0 to G1 transition [has_severity] high	At daily intervals, the viability of cells from each culture was determined by plating a portion of each onto fresh medium. the long-term survivability of cgs1::ura4 cells decreases as cells remain at G0 to an extent that depends on the composition of the medium
PMID:15611161	FYPO:0000581	decreased spore germination frequency [has_severity] high	However in minimal defined medium (EMM) differences between the strains becomes apparent. Compared with wild-type spores, germination of spores containing either pka1.261 or pka1-T356A alleles is reduced by 50%.
PMID:15611161	FYPO:0000581	decreased spore germination frequency [has_severity] high	However in minimal defined medium (EMM) differences between the strains becomes apparent. Compared with wild-type spores, germination of spores containing either pka1.261 or pka1-T356A alleles is reduced by 50%.
PMID:15611161	FYPO:0004993	normal spore germination frequency	In complete, rich medium (YEA), spore germination is high (between 85 and 95%) in wild-type cells, pka1 cells, and all three pka1-Thr-356 substituted alleles
PMID:15611161	FYPO:0000579	normal spore germination	In complete, rich medium (YEA), spore germination is high (between 85 and 95%) in wild-type cells, pka1 cells, and all three pka1-Thr-356 substituted alleles
PMID:15611161	FYPO:0000579	normal spore germination	In complete, rich medium (YEA), spore germination is high (between 85 and 95%) in wild-type cells, pka1 cells, and all three pka1-Thr-356 substituted alleles
PMID:15611161	FYPO:0006141	abolished cell population growth on gluconate carbon source	In contrast, cgs1::ura4 cells fail to grow on gluconate.
PMID:15611161	FYPO:0003503	normal vegetative cell length	Loss of ksg1 reverses the elon-gated cgs1-phenotype (Figure 5D)
PMID:15611161	FYPO:0003503	normal vegetative cell length	Loss of ksg1 reverses the elon-gated cgs1-phenotype (Figure 5D)
PMID:15611161	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPCC576.15c	Phosphorylation of Pka1-Thr-356 is required for its invivo activation and is dependent on Ksg1:
PMID:15611161	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC106.10	Phosphorylation of Pka1-Thr-356 is required for its invivo activation and is dependent on Ksg1: (Figure 6A and data not shown).
PMID:15611161	FYPO:0001829	normal growth on gluconate carbon source [has_severity] high	Significantly, loss of ksg1 reverses this phenotype and cgs1::ura4 ksg1.12 cells grow well on gluconate.
PMID:15611161	FYPO:0001829	normal growth on gluconate carbon source [has_severity] high	Significantly, loss of ksg1 reverses this phenotype and cgs1::ura4 ksg1.12 cells grow well on gluconate.
PMID:15611161	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC106.10	The band shift is dependent on Ksg1 because it is not observed when Pka1 is immunoprecipitated from ksg1.12 cells (Figure 6A; compare lane 7 with lanes 2 and 3
PMID:15611161	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC106.10	The upper band was also not detected when extract was prepared from cells containing pka1-T36E pka1-T356D, or pka1-T356A alleles (Figure 6A lanes 4–6)
PMID:15611161	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC106.10	The upper band was also not detected when extract was prepared from cells containing pka1-T36E pka1-T356D, or pka1-T356A alleles (Figure 6A lanes 4–6)
PMID:15611161	FYPO:0004481	abolished cell population growth at high temperature [has_severity] high	This analysis revealed previously undescribed phenotypes. cells fail to form colonies when incubated at 35 . The cells do not die at the high temperature, but return to growth when the culture is shifted to 25 (Figure 2A).
PMID:15611161	FYPO:0001234	slow vegetative cell population growth	Twenty-five degrees is only a semipermissive temperature for ksg1.12 ...At 25 , ksg1.12 cells grow more slowly than wild-developtype cells (doubling times of 4.5 and 3.0 hr, respec-
PMID:15611161	FYPO:0000711	decreased cell cycle arrest in mitotic G1 phase in response to nitrogen starvation	We found that ksg1 is required for efficient G1 arrest induced by nitrogen starvation (Figure 3B).
PMID:15611161	FYPO:0000113	sensitive to staurosporine [has_severity] high	ksg1.12 cells are more sensitive to staurosporine than cells containing mutations in either pck1 or pck2 alone (Figure 4)
PMID:15611161	FYPO:0001864	mating without glucose starvation	pka1-T356A allele caused cells to conjugate and sporulate in a density-dependent manner on rich medium.
PMID:15611161	FYPO:0000581	decreased spore germination frequency [has_severity] high	spores derived from cells containing mutations that mimic constitutive phosphorylation of T356 (pka1- T356E and pka1-T356D) have rates of spore germina-6E and pka1-T356D) have rates of spore germina-tion similar to spores derived from wild-type cells.
PMID:15615784	FYPO:0003000	abolished actin filament polymerization	(comment: CHECK assayed in vitro)
PMID:15615784	FYPO:0003000	abolished actin filament polymerization	(comment: CHECK assayed in vitro)
PMID:15615784	GO:0007163	establishment or maintenance of cell polarity	(comment: CHECK based just on this paper, candidate for involved_in_or_regulates qualifier)
PMID:15615784	GO:0007163	establishment or maintenance of cell polarity	(comment: CHECK based just on this paper, candidate for involved_in_or_regulates qualifier)
PMID:15615848	GO:0140720	subtelomeric heterochromatin	(Fig. 1A)
PMID:15615848	GO:0005721	pericentric heterochromatin	(Fig. 1A) (comment: CenH)
PMID:15615848	GO:0031934	mating-type region heterochromatin	(Fig. 1A) (comment: CenH)
PMID:15615848	FYPO:0003074	abolished protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC6F12.09	(Fig. 1B)
PMID:15615848	FYPO:0003074	abolished protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC6F12.09	(Fig. 1B)
PMID:15615848	FYPO:0003074	abolished protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC6F12.09	(Fig. 1B)
PMID:15615848	FYPO:0003074	abolished protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC6F12.09	(Fig. 1B)
PMID:15615848	FYPO:0003074	abolished protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC6F12.09	(Fig. 1B)
PMID:15615848	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPAC6F12.09	(Fig. 1B)
PMID:15615848	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC6F12.09	(Fig. 2B) Immunoblotting assay showed that the protein level of the Rdp1 mutant (Rdp1D903A) is comparable to that of wild-type Rdp1, suggesting that the D903A mutation does not affect the stability of the mutant protein
PMID:15615848	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	(Fig. 2C). (otr1R::ura4+) (Fig. 2B) Immunoblotting assay showed that the protein level of the Rdp1 mutant (Rdp1D903A) is comparable to that of wild-type Rdp1, suggesting that the D903A mutation does not affect the stability of the mutant protein
PMID:15615848	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPAC664.01c	(Fig. 2D). cells localization of both methylated H3-K9 and Swi6 at centromeric otr1R::ura4+ was severely affected in rdp1D903A cells (Fig. 2D).
PMID:15615848	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth	(Fig. 2D). cells localization of both methylated H3-K9 and Swi6 at centromeric otr1R::ura4+ was severely affected in rdp1D903A cells (Fig. 2D).
PMID:15615848	FYPO:0008009	abnormal interphase mitotic telomere clustering during vegetative growth	(Fig. 3C and D) In contrast, a noticeably larger fraction of rdp1D903A cells exhibited an increased number of Swi6 foci, and most of these Swi6 foci still colocalized with Taz1, suggesting a declustering of telomeres even though the localization of telomeres to the nuclear periphery was unaffected
PMID:15615848	FYPO:0008011	abolished siRNA loading onto RITS complex	(Fig. 4B). We found that, whereas siRNAs could be readily detected in the affinity-purified fraction of RITS from wild-type cells, there were no detectable RITS- associated siRNAs present in rdp1D903A, rdp1Δ, or dcr1Δ cells
PMID:15615848	FYPO:0008011	abolished siRNA loading onto RITS complex	(Fig. 4B). We found that, whereas siRNAs could be readily detected in the affinity-purified fraction of RITS from wild-type cells, there were no detectable RITS- associated siRNAs present in rdp1D903A, rdp1Δ, or dcr1Δ cells
PMID:15615848	FYPO:0008011	abolished siRNA loading onto RITS complex	(Fig. 4B). We found that, whereas siRNAs could be readily detected in the affinity-purified fraction of RITS from wild-type cells, there were no detectable RITS- associated siRNAs present in rdp1D903A, rdp1Δ, or dcr1Δ cells
PMID:15615848	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPBC83.03c	(Fig. 5A) Although all three components of RITS (Ago1, Chp1, and Tas3) are found to be dramatically enriched at otr1R::ura4+ and centromeric repeats in wild-type cells, these proteins completely fail to localize to these centromeric loci in rdp1D903A cells
PMID:15615848	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPAC18G6.02c	(Fig. 5A) Although all three components of RITS (Ago1, Chp1, and Tas3) are found to be dramatically enriched at otr1R::ura4+ and centromeric repeats in wild-type cells, these proteins completely fail to localize to these centromeric loci in rdp1D903A cells
PMID:15615848	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC736.11	(Fig. 5A) Although all three components of RITS (Ago1, Chp1, and Tas3) are found to be dramatically enriched at otr1R::ura4+ and centromeric repeats in wild-type cells, these proteins completely fail to localize to these centromeric loci in rdp1D903A cells
PMID:15615848	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 20	. We found that rdp1 mutants have a significantly higher percentage (∼20%) of cells with lagging chromosomes during late anaphase than in the wild-type strain (􏰆1%) (Fig. 3B)
PMID:15615848	FYPO:0008010	decreased RNA-dependent RNA polymerase	In contrast, a noticeably larger fraction of rdp1D903A cells exhibited an increased number of Swi6 foci, and most of these Swi6 foci still colocalized with Taz1, suggesting a declustering of telomeres even though the localization of telomeres to the nuclear periphery was unaffected (Fig. 3 C and D)
PMID:15615848	FYPO:0004974	normal telomere localization during mitotic interphase	In contrast, a noticeably larger fraction of rdp1D903A cells exhibited an increased number of Swi6 foci, and most of these Swi6 foci still colocalized with Taz1, suggesting a declustering of telomeres even though the localization of telomeres to the nuclear periphery was unaffected (Fig. 3 C and D)
PMID:15615848	GO:0003968	RNA-directed RNA polymerase activity [part_of] siRNA-mediated pericentric heterochromatin formation	Therefore, we conclude from these analyses that the RdRP activity of Rdp1 is essential for the generation of RITS-associated siRNAs. plus centrromeric chromatin assays
PMID:15615848	FYPO:0000091	sensitive to thiabendazole [has_severity] high	hypersensitive to TBZ, indicating that chromosome segregation is not robust in these mutant cells (Fig. 3A).
PMID:15616156	GO:0005654	nucleoplasm	(Figure 2A)
PMID:15616156	FYPO:0000096	sensitive to cadmium [has_severity] high	(Figure 2I).
PMID:15616156	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	At 38 C, however, the growth rate of both JY741/tfg3::ura4 and JY741/tfg3D was significantly reduced than JY741, and only small-sized colonies were detected after prolonged incubation, indicating that tfg3+ was essential for cell growth at elevated temperatures.
PMID:15616156	FYPO:0001214	sensitive to potassium chloride [has_severity] high	When S.pombe cells that lacked Tfg3 were streaked on a plate that contained 0.9 M KCl, they did not grow. In contrast, tfg3+ cells were able to grow (Figure 2G).
PMID:15616156	GO:0005674	transcription factor TFIIF complex	e, we found that more Tfg3-H formed complexes with GST-Tfg3 (Figure 1D), confirming our hypothesis that Tfg3 forms dimers or multimers. Our observations indicated that Tfg3 is a component of TFIIF in S.pombe as it is in S.cerevisiae.
PMID:15616156	FYPO:0002060	viable vegetative cell population	our spores from each tetrad grew (Figure 2B) and each tetrad contained two Ura+ and two Ura− spores (data not shown), indicating that tfg3+ was nonessential for cell growth under the conditions employed.
PMID:15625190	GO:0003729	mRNA binding [occurs_at] exonic_splice_enhancer	(comment: three-hybrid assay; also binds exogenous ESEs)
PMID:15632064	FYPO:0007326	decreased mitochondrial tRNA 3'-end processing	(Fig. 1) The data suggest that the mutants are not deficient in termination efficiency.
PMID:15632064	FYPO:0007008	normal termination of RNA polymerase III transcription	(Fig. 1) The data suggest that the mutants are not deficient in termination efficiency.
PMID:15632064	FYPO:0007326	decreased mitochondrial tRNA 3'-end processing	(Fig. 1) The data suggest that the mutants are not deficient in termination efficiency.
PMID:15632064	GO:0005666	RNA polymerase III complex	(Figure 3) Mutated Rpc11p subunits associate with Pol III and impair its RNA 3' cleavage activity.
PMID:15632064	GO:0000049	tRNA binding [part_of] tRNA 3'-end processing	(comment: trna chaperone)
PMID:15643072	FYPO:0001250	decreased origin firing efficiency	(comment: assayed in strain with cdc10-129 to synchronize)
PMID:15647375	FYPO:0002303	inviable mononucleate monoseptate vegetative cell with anucleate compartment	(Fig. 4)
PMID:15647375	FYPO:0000229	cut	(Fig. 4)
PMID:15647375	FYPO:0000252	increased spontaneous diploidization	(Fig. 4)
PMID:15654094	GO:0042138	meiotic DNA double-strand break formation	(comment: assayed using 160-bp palindromic sequence inserted into ade6 locus)
PMID:15654094	GO:0007131	reciprocal meiotic recombination	(comment: assayed using 160-bp palindromic sequence inserted into ade6 locus)
PMID:15654094	GO:0042138	meiotic DNA double-strand break formation	(comment: assayed using 160-bp palindromic sequence inserted into ade6 locus)
PMID:15654094	GO:0042138	meiotic DNA double-strand break formation	(comment: assayed using 160-bp palindromic sequence inserted into ade6 locus)
PMID:15665379	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC1604.20c [assayed_using] PomBase:SPAC18G6.15	(Fig. 2)
PMID:15665379	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC1604.20c [assayed_using] PomBase:SPAC18G6.15	(Fig. 2)
PMID:15665379	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC1604.20c [assayed_using] PomBase:SPAC18G6.15	(Fig. 2)
PMID:15665379	FYPO:0001944	abolished microtubule binding [assayed_using] PomBase:SPBC1604.20c [assayed_using] PomBase:SPAC18G6.15	(Fig. 3b)
PMID:15671491	FYPO:0003932	normal nuclear 5'-3' exonucleolytic mRNA catabolic process	(comment: assayed using reporter based on S. cerevisiae MFA2)
PMID:15671491	FYPO:0003933	decreased nuclear 5'-3' exonucleolytic mRNA catabolic process	(comment: assayed using reporter based on S. cerevisiae MFA2)
PMID:15671491	FYPO:0003933	decreased nuclear 5'-3' exonucleolytic mRNA catabolic process	(comment: assayed using reporter based on S. cerevisiae MFA2)
PMID:15671491	FYPO:0003934	abolished nuclear mRNA catabolic process	(comment: assayed using reporter based on S. cerevisiae MFA2)
PMID:15671491	FYPO:0003932	normal nuclear 5'-3' exonucleolytic mRNA catabolic process	(comment: assayed using reporter based on S. cerevisiae MFA2)
PMID:15689489	FYPO:0000339	mislocalized septum during vegetative growth [has_severity] low	(Fig. 1)
PMID:15689489	FYPO:0003840	sensitive to carbendazim	(Fig. 1)
PMID:15689489	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Fig. 1)
PMID:15689489	FYPO:0004700	bent vegetative cell [has_severity] low	(Fig. 1)
PMID:15689489	FYPO:0005558	abnormal microtubule bundle	(Fig. 2)
PMID:15689489	FYPO:0002401	microtubule bundles present in increased numbers	(Fig. 2)
PMID:15689489	FYPO:0003302	nucleus mislocalized towards cell tip during mitotic interphase	(Fig. 5)
PMID:15689489	FYPO:0005722	mitotic spindle collapse during anaphase B elongation	(Fig. 6)
PMID:15689489	FYPO:0007981	abnormal interpolar microtubule length distribution during anaphase B	(Fig. 6)
PMID:15689489	FYPO:0004395	short bipolar mitotic spindle during metaphase	(Fig. 6)
PMID:15689489	FYPO:0007304	short bipolar mitotic spindle during anaphase	(Fig. 6)
PMID:15689489	GO:0005827	polar microtubule [exists_during] mitotic anaphase B	(comment: In metaphase the difference kinds of microtubules cannot be distinguished, but they can be distinguished during anaphase B)
PMID:15710398	FYPO:0000492	decreased mitochondrial genome maintenance	(Fig. 4B)
PMID:15710398	FYPO:0000492	decreased mitochondrial genome maintenance	(Fig. 4B)
PMID:15710398	FYPO:0000492	decreased mitochondrial genome maintenance	(Fig. 4B), Loss of the GTPase function of Msp1p is thus sufficient to affect the maintenance of the mitochondrial genome and the viability of S. pombe cells.
PMID:15710398	GO:0008053	mitochondrial fusion	(comment: MEMBRANE)
PMID:15710398	FYPO:0002061	inviable vegetative cell population	(comment: while cells that expressed cytosolic Msp1pDMIS or CAT died.)
PMID:15710398	FYPO:0002061	inviable vegetative cell population	(comment: while cells that expressed cytosolic Msp1pDMIS or CAT died.)
PMID:15710398	FYPO:0002061	inviable vegetative cell population	(comment: while cells that expressed cytosolic Msp1pDMIS or CAT died.)
PMID:15710398	FYPO:0002061	inviable vegetative cell population	GTPase (Msp1pK276A) and coiledcoil deleted (Msp1pD25-D50) mutants did not support the function of Msp1p as they failed to complement the msp1+ gene deletion.
PMID:15710398	FYPO:0000895	mitochondrial aggregation [has_penetrance] 85	In Msp1p overexpressing cells, more than 85% of the cells had an aggregated filamentous mitochondrial network.
PMID:15710398	FYPO:0008108	normal mitochondrial inheritance	In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur
PMID:15710398	FYPO:0008108	normal mitochondrial inheritance	In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur
PMID:15710398	FYPO:0002060	viable vegetative cell population	In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur.
PMID:15710398	FYPO:0002060	viable vegetative cell population	In the Dmsp1Ddnm1 strain, mtDNA depletion (Fig. 5F) and lethality (not shown) did not occur.
PMID:15710398	FYPO:0003896	normal mitochondrial morphology	In the doubledisrupted Dmsp1Ddnm1 strain, the mitochondria formed elongated tubules which resembled those seen in wild-type cells ...... (Fig. 5E).
PMID:15710398	FYPO:0003896	normal mitochondrial morphology	In the doubledisrupted Dmsp1Ddnm1 strain, the mitochondria formed elongated tubules which resembled those seen in wild-type cells ...... (Fig. 5E).
PMID:15710398	FYPO:0003810	small fragmented mitochondria present in increased numbers	On the contrary, even slight overexpression of Msp1pK276A, Msp1pD50 or Msp1pD25 induced mitochondrial fragmentation; in about 60% of the cells the mitochondria appeared as small more or less clustered individual dots.
PMID:15710398	FYPO:0003810	small fragmented mitochondria present in increased numbers	On the contrary, even slight overexpression of Msp1pK276A, Msp1pD50 or Msp1pD25 induced mitochondrial fragmentation; in about 60% of the cells the mitochondria appeared as small more or less clustered individual dots.
PMID:15710398	FYPO:0003810	small fragmented mitochondria present in increased numbers	On the contrary, even slight overexpression of Msp1pK276A, Msp1pD50 or Msp1pD25 induced mitochondrial fragmentation; in about 60% of the cells the mitochondria appeared as small more or less clustered individual dots.
PMID:15710398	FYPO:0000636	increased cell population growth rate	Time-course measurements of the doubling times of these cultures showed that at day 5 the growth rate of strains expressing Msp1pK276A, Msp1pD50 and Msp1pD25 was greatly increased... (Fig. 4A).
PMID:15710398	FYPO:0000636	increased cell population growth rate	Time-course measurements of the doubling times of these cultures showed that at day 5 the growth rate of strains expressing Msp1pK276A, Msp1pD50 and Msp1pD25 was greatly increased... (Fig. 4A).
PMID:15710398	FYPO:0000636	increased cell population growth rate	Time-course measurements of the doubling times of these cultures showed that at day 5 the growth rate of strains expressing Msp1pK276A, Msp1pD50 and Msp1pD25 was greatly increased... (Fig. 4A).
PMID:15710398	FYPO:0003810	small fragmented mitochondria present in increased numbers	fragmented: By 27 h, when repression was almost complete, the mitochondrial network fragmented into clusters of small rounded mitochondria. This phenotype is reminiscent of the mitochondrial morphology defect observed in S. cerevisiae deleted for MGM1 [18].
PMID:15710398	FYPO:0003807	net-like mitochondrial morphology	the mitochondrial network appeared as highly interconnected tubules forming net-like structures (Fig. 5A).
PMID:15710398	FYPO:0003896	normal mitochondrial morphology	while cells that expressed cytosolic Msp1pDMIS or CAT died.
PMID:15716270	FYPO:0003699	snoRNA guided rRNA pseudouridine synthesis abolished at specific site	(comment: 18S rRNA position 1204)
PMID:15716270	FYPO:0003699	snoRNA guided rRNA pseudouridine synthesis abolished at specific site	(comment: 18S rRNA position 1307)
PMID:15716270	FYPO:0003699	snoRNA guided rRNA pseudouridine synthesis abolished at specific site	(comment: 18S rRNA positions 208, 2341)
PMID:15716270	FYPO:0003699	snoRNA guided rRNA pseudouridine synthesis abolished at specific site	(comment: 25S rRNA position 1074)
PMID:15716270	FYPO:0003699	snoRNA guided rRNA pseudouridine synthesis abolished at specific site	(comment: 25S rRNA position 1084)
PMID:15716270	FYPO:0003699	snoRNA guided rRNA pseudouridine synthesis abolished at specific site	(comment: 25S rRNA position 1723)
PMID:15716270	FYPO:0003699	snoRNA guided rRNA pseudouridine synthesis abolished at specific site	(comment: 25S rRNA position 3017)
PMID:15716270	FYPO:0003699	snoRNA guided rRNA pseudouridine synthesis abolished at specific site	(comment: 25S rRNA position 3069)
PMID:15716270	FYPO:0003699	snoRNA guided rRNA pseudouridine synthesis abolished at specific site	(comment: 25S rRNA positions 2216, 2220, 2351)
PMID:15716270	FYPO:0003699	snoRNA guided rRNA pseudouridine synthesis abolished at specific site	(comment: 25S rRNA positions 2298, 2401)
PMID:15728720	FYPO:0000209	abnormal attachment of spindle microtubules to kinetochore during meiosis I	(comment: CHECK increased centromere spindle pole body detachment during meiotic prophase fission-yeast-phenotype/2055/)
PMID:15731009	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth [has_penetrance] complete	(comment: CHECK same as orb3-167 alone)
PMID:15731009	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth [has_penetrance] complete	(comment: CHECK same as orb3-167 alone)
PMID:15731009	GO:0004672	protein kinase activity	(comment: assayed using casein; doesn't quite rule out tyrosine phosphorylation)
PMID:15731009	GO:0007163	establishment or maintenance of cell polarity	(comment: based just on this paper, candidate for involved_in_or_regulates qualifier)
PMID:15731009	GO:0030950	establishment or maintenance of actin cytoskeleton polarity	(comment: based just on this paper, candidate for involved_in_or_regulates qualifier)
PMID:15731009	GO:0110085	mitotic actomyosin contractile ring	(comment: dependent on F-actin (asayed using Latrunculin A); independent of microtubules (assayed using MBC))
PMID:15731009	GO:0030479	actin cortical patch	(comment: dependent on F-actin (asayed using Latrunculin A); independent of microtubules (assayed using MBC))
PMID:15743828	FYPO:0001508	abolished protein localization to chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	Consistent with this result, immunolocalization of 3xHA- chp11-409 with anti-HA antibody revealed that the truncated protein was diffusely localized throughout the chromatin and nucleolus (Fig. 3D).
PMID:15743828	FYPO:0000141	abnormal mitotic sister chromatid segregation	Importantly, cells lacking only the Chp1 chromodomain (ΔCDchp1-6xmyc) behaved similar to the chp1 null strain, with elevated transcription of the centromeric marker gene (Fig. 2C) and numerous mitotic chromosome segregation defects (Fig. 2D)
PMID:15743828	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] high	Importantly, cells lacking only the Chp1 chromodomain (ΔCDchp1-6xmyc) behaved similar to the chp1 null strain, with elevated transcription of the centromeric marker gene (Fig. 2C) and numerous mitotic chromosome segregation defects (Fig. 2D)
PMID:15743828	FYPO:0001509	normal protein localization to chromatin during vegetative growth [has_penetrance] high	In contrast, cells lacking the RRM domain of Chp1 (ΔRRMchp1-6xmyc) exhibited no loss of Chp1 function.
PMID:15743828	FYPO:0004742	normal chromatin silencing at centromere outer repeat [has_penetrance] high	In contrast, cells lacking the RRM domain of Chp1 (ΔRRMchp1-6xmyc) exhibited no loss of Chp1 function.
PMID:15743828	FYPO:0001508	abolished protein localization to chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	In contrast, ΔCDchp1-6xmyc exhibited a diffuse faint spotty staining pattern throughout the nucleoplasm and was not associated with chromatin (Fig. 2E). Thus, the chromodomain, but not the RRM, is essential for Chp1 localization to all sites of heterochromatin and for normal Chp1 function at centromeric sequences.
PMID:15743828	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	Nonetheless, deletion of chp1+ or ago1+ only slightly alleviated silencing (20, 38), as revealed by the presence of pink colonies compared with the red, fully repressed colonies (Fig. 8A).
PMID:15743828	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	Nonetheless, deletion of chp1+ or ago1+ only slightly alleviated silencing (20, 38), as revealed by the presence of pink colonies compared with the red, fully repressed colonies (Fig. 8A).
PMID:15743828	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPAC18G6.02c	Surprisingly, however, other foci of Chp1-6xmyc and Tas3- 13xmyc persisted in ago1Δ cells. Similar results were obtained in cells from which Dicer was deleted (Fig. 5A and B, right panels).
PMID:15743828	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPBC83.03c	Surprisingly, however, other foci of Chp1-6xmyc and Tas3- 13xmyc persisted in ago1Δ cells. Similar results were obtained in cells from which Dicer was deleted (Fig. 5A and B, right panels).
PMID:15743828	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPBC83.03c	Surprisingly, however, other foci of Chp1-6xmyc and Tas3- 13xmyc persisted in ago1Δ cells. Similar results were obtained in cells from which Dicer was deleted (Fig. 5A and B, right panels).
PMID:15743828	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPAC18G6.02c	Surprisingly, however, other foci of Chp1-6xmyc and Tas3- 13xmyc persisted in ago1Δ cells. Similar results were obtained in cells from which Dicer was deleted (Fig. 5A and B, right panels).
PMID:15743828	FYPO:0001984	protein absent from cell during vegetative growth [assayed_protein] PomBase:SPBC83.03c	Tas3-13xmyc protein was essentially lost in chp1Δ cells, whereas it was present at normal levels in the ago1Δ cells (Fig. 6B). To address whether loss of Tas3-13xmyc protein in chp1Δ cells was due to suppression of tas3-13xmyc+ transcription, we performed quantitative RT-PCR using RNA prepared from wild-type, chp1Δ, and ago1Δ backgrounds. Deletion of chp1+ had no effect on tas3-13xmyc+ transcript levels (Fig. 6C); therefore, the loss of Tas3 protein in chp1 null cells is a posttranscriptional effect.
PMID:15743828	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] high	These cells exhibited high levels of chromosome segregation defects (Fig. 3C) and defects in centromeric silencing (Fig. 3B).
PMID:15743828	FYPO:0000141	abnormal mitotic sister chromatid segregation	These cells exhibited high levels of chromosome segregation defects (Fig. 3C) and defects in centromeric silencing (Fig. 3B).
PMID:15743828	GO:0140720	subtelomeric heterochromatin	Thus, Tas3-13xmyc and Chp1-6xmyc colocalize to the mat2/3 locus, to telomeres, and to centromeres and possibly associate with all sites of heterochromatin.
PMID:15743828	GO:0031934	mating-type region heterochromatin	Thus, Tas3-13xmyc and Chp1-6xmyc colocalize to the mat2/3 locus, to telomeres, and to centromeres and possibly associate with all sites of heterochromatin.
PMID:15743828	GO:0005721	pericentric heterochromatin	Thus, Tas3-13xmyc and Chp1-6xmyc colocalize to the mat2/3 locus, to telomeres, and to centromeres and possibly associate with all sites of heterochromatin.
PMID:15743828	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	We also assessed the localization of Chp1-6xmyc and Tas3- 13xmyc in cells lacking tas3 and chp1, respectively (Fig. 6A). In cells with tas3 deleted, Chp1 was delocalized, with a cloud of small foci of staining that mainly accumulated over the nucleolus (Fig. 6A)
PMID:15743828	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC83.03c	in ago1 cells there is a loss of centromere-associated Chp1 and Tas3, as revealed by loss of costaining of Chp1-6xmyc (Fig. 5A) and Tas3-13xmyc (Fig. 5B)
PMID:15743828	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	in ago1 cells there is a loss of centromere-associated Chp1 and Tas3, as revealed by loss of costaining of Chp1-6xmyc (Fig. 5A) and Tas3-13xmyc (Fig. 5B)
PMID:15743909	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores	(comment: CHECK homozygous cross)
PMID:15743909	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores	(comment: CHECK homozygous cross)
PMID:15743909	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores	(comment: CHECK homozygous cross)
PMID:15743909	GO:0030479	actin cortical patch [exists_during] mitotic cell cycle phase	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:15743909	GO:0030479	actin cortical patch [exists_during] meiotic cell cycle phase	(comment: dependent on F-actin (assayed using Latrunculin A))
PMID:15772152	FYPO:0000899	normal microtubule cytoskeleton organization during vegetative growth	(comment: normal length)
PMID:15772152	FYPO:0004724	long nuclear microtubules protruding through nuclear envelope during interphase	Consistent with this, we observed that the nuclear envelope formed thin protrusions that grew and shrank (Figure 4, G and H, Supplementary Movie 8). Such intranuclear MTs and nuclear envelope distortions were notobserved in wild-type cells. Several criteria confirmed that these cells with intranuclear MTs were in interphase and not in mitosis
PMID:15797383	GO:0032936	SREBP-SCAP complex	(Fig. 1)
PMID:15797383	GO:0032936	SREBP-SCAP complex	(Fig. 1)
PMID:15797383	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPBC19C2.09	(Fig. 2 lane 11-12)
PMID:15797383	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC19C2.09	(Fig. 2)
PMID:15797383	GO:0032933	SREBP signaling pathway	(Fig. 2,3,4)
PMID:15797383	GO:0032933	SREBP signaling pathway	(Fig. 2,5)
PMID:15797925	FYPO:0004121	normal protein import into nucleus during vegetative growth	(comment: assayed using NLS-LacI-GFP construct)
PMID:15797925	GO:0034399	nuclear periphery	punctate, similar to nuclear pore components (comment: localization not dependent on microtubules)
PMID:15800064	GO:0005515	protein binding	(Fig. 1C)
PMID:15800064	GO:0044732	mitotic spindle pole body [exists_during] mitotic metaphase	(Fig. 2A,2C,2D)
PMID:15800064	GO:0044732	mitotic spindle pole body [exists_during] mitotic prophase	(Fig. 2A,2C,2D)
PMID:15800064	GO:0005881	cytoplasmic microtubule [exists_during] mitotic interphase	(Fig. 2A,2D)
PMID:15800064	GO:0000923	equatorial microtubule organizing center [exists_during] mitotic anaphase B	(Fig. 2A,2D)
PMID:15800064	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPBC902.06	(Fig. 5A)
PMID:15800064	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPBC902.06	(Fig. 5A)
PMID:15800064	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC902.06	(Fig. 5B)
PMID:15800064	FYPO:0003171	binucleate monoseptate cell with mitotic cell cycle arrest before cell separation	(Fig. 6B)
PMID:15800064	FYPO:0002026	actomyosin contractile ring displaced from midpoint	(Fig. 6C)
PMID:15800064	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPBC428.20c	(Figure 3) (comment: CHECK fypo/issues/2830)
PMID:15800064	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPBC365.15	(Figure 3) (comment: CHECK fypo/issues/2830)
PMID:15800064	FYPO:0005688	normal astral microtubules	(Figure 3A)
PMID:15800064	FYPO:0004611	long interphase microtubules	(Figure 3A)
PMID:15800064	FYPO:0005686	microtubule bundles present in decreased numbers during mitotic interphase [has_penetrance] 83	(Figure 3A)
PMID:15800064	FYPO:0004700	bent vegetative cell [has_penetrance] 38	(Figure 3A)
PMID:15800064	FYPO:0004624	abolished eMTOC assembly	(Figure 3A,3C)
PMID:15800064	FYPO:0003126	post-anaphase array absent from cell	(Figure 3A,3C)
PMID:15800064	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC417.07c	(Figure 3B) (comment: CHECK fypo/issues/2830)
PMID:15800064	FYPO:0004766	abolished cytoplasmic interphase microtubule nucleation	(Figure 4)
PMID:15809031	GO:0008093	cytoskeletal anchor activity [has_input] PomBase:SPCC895.05 [has_input] PomBase:SPCC1223.06 [part_of] establishment of bipolar cell polarity	(comment: inferred from direct physical interactions between tea4,tea1 and tea4,for3, plus tea4delta phenotype)
PMID:15827087	FYPO:0000021	spheroid vegetative cell	(Fig. 1)
PMID:15827087	FYPO:0000224	lemon-shaped cell	(Fig. 1) (comment: They describe cells as swollen in their middle region)
PMID:15827087	FYPO:0001120	pear-shaped vegetative cell	(Fig. 1) (comment: They describe cells as swollen in their middle region)
PMID:15827087	FYPO:0000015	branched vegetative cell	(Fig. 1) (comment: permissive temperature is 25°C)
PMID:15827087	FYPO:0002297	dispersed actin cortical patch localization during mitotic interphase [has_penetrance] 91	(Fig. 1, Table 2)
PMID:15827087	FYPO:0000899	normal microtubule cytoskeleton organization during vegetative growth [has_penetrance] medium	(Fig. 1B) (comment: This distribution is only seen in cells with a rod shaped appearance)
PMID:15827087	FYPO:0002297	dispersed actin cortical patch localization during mitotic interphase [has_penetrance] 56	(Fig. 1C, Table 2)
PMID:15827087	FYPO:0003150	decreased NETO	(Fig. 2A) and data not shown
PMID:15827087	FYPO:0001019	monopolar actin cortical patch localization during vegetative growth [has_penetrance] 62	(Fig. 2A) and data not shown
PMID:15827087	FYPO:0001019	monopolar actin cortical patch localization during vegetative growth [has_penetrance] 78	(Fig. 2A, 2B)
PMID:15827087	FYPO:0003150	decreased NETO	(Fig. 2A, 2B)
PMID:15827087	FYPO:0003314	activation of monopolar cell growth at new end [has_penetrance] 27	(Fig. 2D)
PMID:15827087	FYPO:0003150	decreased NETO [has_penetrance] high	(Fig. 3A, 2B) Deletion of the talin domain suppresses the premature activation of bipolar growth in a cdc10 mutant in latA
PMID:15827087	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC688.11	(Fig. 4B)
PMID:15827087	GO:0031097	medial cortex [exists_during] mitotic M phase	(Fig. 4B)
PMID:15827087	FYPO:0005503	abnormally monopolar protein localization to cell tip [assayed_using] PomBase:SPAC688.11	(Fig. 4C)
PMID:15827087	GO:0035840	old growing cell tip [exists_during] mitotic interphase	(Fig. 4D)
PMID:15827087	FYPO:0003028	normal actin cortical patch localization during mitosis [has_penetrance] 19	(Table 2)
PMID:15827087	FYPO:0001019	monopolar actin cortical patch localization during vegetative growth [has_penetrance] 9	Table 2 (comment: This distribution is only seen in cells with a rod shaped appearance)
PMID:15827087	FYPO:0001019	monopolar actin cortical patch localization during vegetative growth [has_penetrance] 36	Table 2 (comment: This distribution is only seen in cells with a rod shaped appearance)
PMID:15827087	FYPO:0002424	normal actin cortical patch localization during mitotic interphase [has_penetrance] 8	Table 2 (comment: This distribution is only seen in cells with a rod shaped appearance)
PMID:15827087	GO:0035841	new growing cell tip [exists_during] mitotic G2 phase	data for cdc25-22 block not shown but see also Fig4A
PMID:15827087	FYPO:0002058	viable cell population	data not shown
PMID:15827087	FYPO:0000426	normal endocytosis	data not shown
PMID:15827087	FYPO:0002058	viable cell population	data not shown
PMID:15827087	FYPO:0001387	loss of viability at high temperature [has_severity] high	data not shown (comment: Non permissive temperature is 32°C and above)
PMID:15827087	FYPO:0001355	decreased vegetative cell population growth	data not shown, (comment: permissive temperature 25°C)
PMID:15827087	FYPO:0005503	abnormally monopolar protein localization to cell tip [assayed_using] PomBase:SPAC688.11	data not shown, same as Fig 4C
PMID:15837798	FYPO:0005686	microtubule bundles present in decreased numbers during mitotic interphase	The average number of MT bundles in mto2Δ cells (n = 1.3 ± 0.7 SD; Fig. 3 E) was significantly lower than in wild-type cells (3.6 ± 0.9)
PMID:15837798	FYPO:0004700	bent vegetative cell	mto2 deletion strain, which yielded viable but slightly bent cells (Fig. 3 A)
PMID:15837798	FYPO:0005441	abolished protein localization to microtubule during mitotic interphase [assayed_protein] PomBase:SPBC365.15	mto2 deletion strain, which yielded viable but slightly bent cells (Fig. 3 A)
PMID:15857958	FYPO:0000061	multinucleate vegetative cell [has_penetrance] 5	(Fig. 2)
PMID:15857958	FYPO:0004087	increased number of cells with astral spindle microtubules	(Fig. 2)
PMID:15857958	FYPO:0000252	increased spontaneous diploidization [has_severity] low	(Fig. 2)
PMID:15857958	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. 2,3) (comment: cdc13 signal)
PMID:15857958	FYPO:0000729	delayed onset of actomyosin contractile ring assembly	(Fig. 3)
PMID:15857958	FYPO:0000729	delayed onset of actomyosin contractile ring assembly	(Fig. 3)
PMID:15857958	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 3)
PMID:15857958	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 3)
PMID:15857958	FYPO:0004213	abnormal attachment of mitotic spindle microtubules to kinetochore [has_severity] low	(Fig. 3) mad2 signal.
PMID:15857958	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	(Fig. 4)
PMID:15857958	GO:0071341	medial cortical node [exists_during] mitotic M phase	(Fig. 4)
PMID:15857958	FYPO:0002060	viable vegetative cell population	(Fig. 5)
PMID:15857958	FYPO:0000417	abolished cytokinesis [has_penetrance] 25	(Fig. 5)
PMID:15857958	FYPO:0000417	abolished cytokinesis [has_penetrance] 15	(Fig. 5)
PMID:15857958	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 45	(Fig. 5)
PMID:15857958	FYPO:0002061	inviable vegetative cell population	(Fig. 5)
PMID:15857958	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 45	(Fig. 5)
PMID:15857958	FYPO:0002061	inviable vegetative cell population	(Fig. 5)
PMID:15857958	FYPO:0000417	abolished cytokinesis [has_penetrance] 20	(Fig. 5)
PMID:15857958	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 20	(Fig. 5)
PMID:15857958	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 20	(Fig. 5)
PMID:15857958	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 5	(Fig. 5)
PMID:15857958	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 5	(Fig. 5)
PMID:15857958	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 10	(Fig. 5)
PMID:15857958	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 10	(Fig. 5)
PMID:15857958	FYPO:0001355	decreased vegetative cell population growth	(Fig. 5)
PMID:15857958	FYPO:0002060	viable vegetative cell population	(Fig. 5)
PMID:15857958	FYPO:0002060	viable vegetative cell population	(Fig. 5)
PMID:15857958	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 25	(Fig. 5)
PMID:15857958	FYPO:0000417	abolished cytokinesis [has_penetrance] 20	(Fig. 5)
PMID:15857958	FYPO:0000061	multinucleate vegetative cell [has_penetrance] 30	(Fig. 6)
PMID:15857958	FYPO:0000061	multinucleate vegetative cell [has_penetrance] 60	(Fig. 6)
PMID:15857958	FYPO:0002061	inviable vegetative cell population	(Fig. 7)
PMID:15857958	FYPO:0002061	inviable vegetative cell population	(Fig. 7)
PMID:15857958	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPBC1778.10c	(Fig. 7)
PMID:15857958	FYPO:0000061	multinucleate vegetative cell [has_penetrance] 20	(Fig. 7)
PMID:15857958	FYPO:0002560	abnormal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPCC4B3.15 [has_penetrance] 34	(Fig. 7)
PMID:15857958	FYPO:0002560	abnormal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPAP8A3.08	(Fig. 7)
PMID:15857958	FYPO:0002061	inviable vegetative cell population	(Fig. 7)
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell	See Table 2 multi copy pwis4 does not suppress cdc25-22 wee1-50 mcs4-13
PMID:1588914	FYPO:0002061	inviable vegetative cell population	Table 2 pwis1 does not suppress wee1-50 cdc25-22 mcs6-13
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell	Table 2 pwis1 does not suppress wee1-50 cdc25-22 mcs6-13
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell	Table 2 pwis4 does not suppress wee1-50 cdc25-22 mcs6-13
PMID:1588914	FYPO:0002061	inviable vegetative cell population	Table 2 pwis4 does not suppress wee1-50 cdc25-22 mcs6-13
PMID:1588914	FYPO:0001491	viable vegetative cell [has_penetrance] high	Table 2 the wis1 gene on a multi copy plasmid pwis1 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	FYPO:0001492	viable elongated vegetative cell	Table 3 cells are 30-50% longer than wild type
PMID:1588914	FYPO:0002176	viable vegetative cell with normal cell size	Table 3 pwis4 surpresses the elongated cell phenotype of win1-1
PMID:1588914	FYPO:0002176	viable vegetative cell with normal cell size	data not shown
PMID:1588914	FYPO:0002061	inviable vegetative cell population	multicopy pwis1 does not suppress cdc13-117 ts phenotype
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	multicopy pwis1 does not suppress cdc13-117 ts phenotype
PMID:1588914	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	multicopy pwis1 does not suppress cdc2-1w phenotype
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	multicopy pwis1 does not suppress cdc2-33 ts phenotype
PMID:1588914	FYPO:0002061	inviable vegetative cell population	multicopy pwis1 does not suppress cdc2-33 ts phenotype
PMID:1588914	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	multicopy pwis1 does not suppress cdc2-3w phenotype
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	multicopy pwis1 does not suppress cdc25-22 ts phenotype showing that wis1 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	FYPO:0002061	inviable vegetative cell population	multicopy pwis1 does not suppress cdc25-22 ts phenotype showing that wis1 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high	multicopy pwis1 does not suppress cdr1-34 phenotype
PMID:1588914	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high	multicopy pwis1 does not suppress cdr2-69 phenotype
PMID:1588914	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	multicopy pwis1 does not suppress wee1-50 ts phenotype
PMID:1588914	FYPO:0002061	inviable vegetative cell population	multicopy pwis2 does not suppress cdc13-117 ts phenotype
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	multicopy pwis2 does not suppress cdc13-117 ts phenotype
PMID:1588914	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	multicopy pwis2 does not suppress cdc2-1w phenotype
PMID:1588914	FYPO:0002061	inviable vegetative cell population	multicopy pwis2 does not suppress cdc2-33 ts phenotype
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	multicopy pwis2 does not suppress cdc2-33 ts phenotype
PMID:1588914	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	multicopy pwis2 does not suppress cdc2-3w phenotype
PMID:1588914	FYPO:0002061	inviable vegetative cell population	multicopy pwis2 does not suppress cdc25-22 ts phenotype showing that wis2 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	multicopy pwis2 does not suppress cdc25-22 ts phenotype showing that wis2 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high	multicopy pwis2 does not suppress cdr1-34 phenotype
PMID:1588914	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high	multicopy pwis2 does not suppress cdr2-69 phenotype
PMID:1588914	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	multicopy pwis2 does not suppress wee1-50 ts phenotype
PMID:1588914	FYPO:0002061	inviable vegetative cell population	multicopy pwis3 does not suppress cdc13-117 ts phenotype
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	multicopy pwis3 does not suppress cdc13-117 ts phenotype
PMID:1588914	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	multicopy pwis3 does not suppress cdc2-1w phenotype
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	multicopy pwis3 does not suppress cdc2-33 ts phenotype
PMID:1588914	FYPO:0002061	inviable vegetative cell population	multicopy pwis3 does not suppress cdc2-33 ts phenotype
PMID:1588914	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	multicopy pwis3 does not suppress cdc2-3w phenotype
PMID:1588914	FYPO:0002061	inviable vegetative cell population	multicopy pwis3 does not suppress cdc25-22 ts phenotype showing that spo12 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	multicopy pwis3 does not suppress cdc25-22 ts phenotype showing that spo12 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high	multicopy pwis3 does not suppress cdr1-34 phenotype
PMID:1588914	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high	multicopy pwis3 does not suppress cdr2-69 phenotype
PMID:1588914	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	multicopy pwis3 does not suppress wee1-50 ts phenotype
PMID:1588914	FYPO:0002061	inviable vegetative cell population	multicopy pwis4 does not suppress cdc13-117 ts phenotype
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	multicopy pwis4 does not suppress cdc13-117 ts phenotype
PMID:1588914	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	multicopy pwis4 does not suppress cdc2-1w phenotype
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	multicopy pwis4 does not suppress cdc2-33 ts phenotype
PMID:1588914	FYPO:0002061	inviable vegetative cell population	multicopy pwis4 does not suppress cdc2-33 ts phenotype
PMID:1588914	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	multicopy pwis4 does not suppress cdc2-3w phenotype
PMID:1588914	FYPO:0002061	inviable vegetative cell population	multicopy pwis4 does not suppress cdc25-22 ts phenotype showing that wis4 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	multicopy pwis4 does not suppress cdc25-22 ts phenotype showing that wis4 does not act by by directly reversing cdc25-22 loss of function
PMID:1588914	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high	multicopy pwis4 does not suppress cdr1-34 phenotype
PMID:1588914	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high	multicopy pwis4 does not suppress cdr2-69 phenotype
PMID:1588914	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	multicopy pwis4 does not suppress wee1-50 ts phenotype
PMID:1588914	FYPO:0002060	viable vegetative cell population	see Table 2
PMID:1588914	FYPO:0001491	viable vegetative cell [has_penetrance] high	see Table 2
PMID:1588914	FYPO:0001491	viable vegetative cell [has_penetrance] medium	see Table 2
PMID:1588914	FYPO:0002060	viable vegetative cell population	see Table 2
PMID:1588914	FYPO:0001491	viable vegetative cell [has_penetrance] low	see Table 2
PMID:1588914	FYPO:0002060	viable vegetative cell population	see Table 2
PMID:1588914	FYPO:0002060	viable vegetative cell population	see Table 2
PMID:1588914	FYPO:0002060	viable vegetative cell population	see Table 2
PMID:1588914	FYPO:0001491	viable vegetative cell [has_penetrance] medium	see Table 2
PMID:1588914	FYPO:0001491	viable vegetative cell [has_penetrance] low	see Table 2
PMID:1588914	FYPO:0002061	inviable vegetative cell population	see Table 2 multi copy pwis4 does not suppress cdc25-22 wee1-50 mcs4-13
PMID:1588914	FYPO:0001491	viable vegetative cell [has_penetrance] low	the spo12 gene on a multi copy plasmid pwis3 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	FYPO:0002060	viable vegetative cell population	the spo12 gene on a multi copy plasmid pwis3 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	FYPO:0002060	viable vegetative cell population	the wis1 gene on a multi copy plasmid pwis1 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	FYPO:0001491	viable vegetative cell [has_penetrance] medium	the wis2 gene on a multi copy plasmid pwis2 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	FYPO:0002060	viable vegetative cell population	the wis2 gene on a multi copy plasmid pwis2 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	FYPO:0002060	viable vegetative cell population	the wis4 gene on a multi copy plasmid pwis4 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:1588914	FYPO:0001491	viable vegetative cell [has_penetrance] low	the wis4 gene on a multi copy plasmid pwis4 can suppress the lethal phenotype of wee1-50 cdc25-22 win1-1
PMID:15908586	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(Figure 1)
PMID:15908586	FYPO:0004542	increased chromatin silencing at subtelomere	(Figure 1)
PMID:15908586	FYPO:0004331	normal chromatin silencing at centromere central core	(Figure 1)
PMID:15908586	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Figure 1)
PMID:15908586	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 15	(Figure 2)
PMID:15908586	FYPO:0002620	normal growth on trichostatin A	(Figure 2)
PMID:15908586	FYPO:0002620	normal growth on trichostatin A	(Figure 2)
PMID:15908586	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 25	(Figure 2)
PMID:15908586	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 9	(Figure 2)
PMID:15908586	FYPO:0001355	decreased vegetative cell population growth	(Figure 2)
PMID:15908586	FYPO:0000284	large and small daughter nuclei, with unequal mitotic sister chromatid segregation [has_penetrance] 2.1	(Figure 2) Further examination of the IF samples revealed that hrp1D single and hrp1D hrp3D double mutants cells showed elevated numbers of asymmetric segregation (large and small nuclei) in late anaphase cells
PMID:15908586	FYPO:0003937	increased cell population growth	(Figure 2) In cultures without TSA, the hrp1D cells grew slightly faster than wt cells as reported previously (48).
PMID:15908586	FYPO:0002546	sensitive to trichostatin A [has_severity] high	(Figure 2A) However, growth of the double mutant cells was completely inhibited by TSA.
PMID:15908586	FYPO:0002061	inviable vegetative cell population	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	FYPO:0002061	inviable vegetative cell population	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	FYPO:0001357	normal vegetative cell population growth	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	FYPO:0001357	normal vegetative cell population growth	(Figure 2A) In contrast, both of the single mutants were hypersensitive to this concentration of TBZ, showing a 5- to 25-fold growth reduction compared with wt
PMID:15908586	FYPO:0007314	increased histone H4-K12 acetylation at centromere central core during vegetative growth	(Figure 3)
PMID:15908586	FYPO:0007313	increased histone H4-K8 acetylation at centromere central core during vegetative growth	(Figure 3)
PMID:15908586	FYPO:0008062	increased chromatin binding at centromere central core	(Figure 3) There was a 4- fold reduction of Cnp1 at cnt2 in hrp1D cells
PMID:15908586	FYPO:0004984	decreased chromatin binding at centromere central core [assayed_protein] PomBase:SPBC1105.17	(Figure 3) There was a 4- fold reduction of Cnp1 at cnt2 in hrp1D cells
PMID:15908586	FYPO:0001355	decreased vegetative cell population growth	The mis6-302 hrp1D double mutant had a reduced growth at 30 C as compared with the mis6-302 and hrp1D single mutants (Figure 3C).
PMID:15908586	FYPO:0001355	decreased vegetative cell population growth	The mis6-302 hrp1D double mutant had a reduced growth at 30 C as compared with the mis6-302 and hrp1D single mutants (Figure 3C).
PMID:15908586	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] regional_centromere_outer_repeat_transcript	dhIII transcripts were detectable in hrp1D dcr1D and dcr1D cells, but not in the wild-type and hrp1D cells (Figure 4E). The dhIII transcripts were more abundant in hrp1D dcr1D cells than in dcr1D cells consistent with the reduced silencing observed at dg-dh in hrp1D (Figure 1E). If transcripts read through in hrp1D from dh-dg into the central core region, then they should be readily detectable in the intervening imrIII region. However, imrIII transcripts were not observed in hrp1D cells. From these results, we concluded that the hrp1D mutant does not cause read through of dg-dh transcripts into the central core region. Hrp1 is present at the centromere in a cell
PMID:15915339	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: more sensitive than either single mutant)
PMID:15915339	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(comment: more sensitive than either single mutant)
PMID:15915339	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(comment: more sensitive than either single mutant)
PMID:15915339	FYPO:0000095	sensitive to bleomycin [has_severity] high	(comment: more sensitive than either single mutant)
PMID:15920625	GO:0036374	glutathione gamma-glutamate hydrolase [part_of] glutathione catabolic process	(comment: Proxy assay for hydrolase function used and IMP evidence for catalytic activity)
PMID:15925945	GO:0010856	adenylate cyclase activator activity [has_input] PomBase:SPBC19C7.03	(comment: assayed using AlF4- to mimic GTP-bound Gpa2)
PMID:15933715	FYPO:0001493	inviable elongated multinucleate vegetative cell	(Figure 1A and B)
PMID:15933715	FYPO:0000842	sensitive to ethanol during vegetative growth	(Figure 1A and B)
PMID:15933715	GO:0071957	old mitotic spindle pole body [exists_during] mitotic metaphase	(comment: missing annotation, we dont have that cdc7 is on old SPB in metaphase) Cdc7p-GFP appeared at both SPBs at the initiation of mitosis and only at one SPB as cells progressed through anaphase until the completion of cell division.
PMID:15933715	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPAC1006.08	Etd1p-GFP failed to localise to the medial ring at the restrictive temperature. Instead, these mutant cells accumulated Etd1-GFP in a broad band at the plasma membrane overlying the site of cytokinesis (Figure 6A, upper panel
PMID:15933715	GO:0106006	cytoskeletal protein-membrane anchor activity [has_input] PomBase:SPAC1006.08 [part_of] mitotic actomyosin contractile ring assembly [occurs_in] medial cortex [happens_during] mitotic M phase	Etd1p-GFP, demonstrating that Etd1p interacts physically with Cdc15p. Similarly, Cdc15p was detected in anti-GFP immune complexes (data not shown). Thus, Etd1p may localise to the actomyosin ring by association with Cdc15p. (comment: the anchor is using 2022 knowledge)
PMID:15933715	FYPO:0003838	abolished actomyosin contractile ring contraction	However, in etd1-1 mutant cells, the medial ring marked with Cdc15p-GFP seems to fail constriction. To bette
PMID:15933715	GO:0031097	medial cortex [exists_during] mitotic anaphase	In early anaphase, Etd1p-GFP became concentrated in the medial region of the cell cortex as a broad band (Figure 2A, cell 2)
PMID:15933715	GO:0031097	medial cortex [exists_during] mitotic metaphase	In early anaphase, Etd1p-GFP became concentrated in the medial region of the cell cortex as a broad band (Figure 2A, cell 2)
PMID:15933715	GO:0000935	division septum [exists_during] mitotic anaphase B	In early anaphase, Etd1p-GFP became concentrated in the medial region of the cell cortex as a broad band (Figure 2A, cell 2)
PMID:15933715	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	In interphase cells, Etd1p-GFP was located at the cell cortex and was more concentrated at the cell tips (Figure 2A, cell 1).
PMID:15933715	FYPO:0002816	inviable after spore germination, without cell division, multinucleate cell with elongated germ tube	Spores deleted for etd1 (etd1D) germinated and accumulated multiple nuclei without septation, an identical phenotype to that of etd1-1 mutant cells under restrictive conditions (Figure 1C).
PMID:15933715	MOD:01148	ubiquitinylated lysine	These results indicate that Etd1p is polyubiquitinated and degraded through the ubiquitin-dependent 26S-proteasome pathway.
PMID:15933715	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	Under derepressed conditions ( thiamine), Etd1p overproduction generated elongated and multinucleate cells in both etd1-1 mutant and wild-type backgrounds (Figure 1D and data not shown). Thus, the phenotypic defect caused by an excess of Etd1p was identical to that produced by a deficiency of this protein, suggesting that Etd1p functions in a stoichiometric protein complex.
PMID:15933715	FYPO:0006220	abolished protein localization to septum [assayed_protein] PomBase:SPAC1006.08	We therefore analysed the localisation of Etd1p-GFP in cdc8-110 mutant cells and found that, at the restrictive temperature of 361C, Etd1p never formed a ring (Figure 3B upper panels).
PMID:15933715	FYPO:0001880	abolished protein localization to cell division site [assayed_protein] PomBase:SPAC1006.08	We therefore analysed the localisation of Etd1p-GFP in cdc8-110 mutant cells and found that, at the restrictive temperature of 361C, Etd1p never formed a ring (Figure 3B upper panels).
PMID:15933715	GO:0031028	septation initiation signaling	suggesting that Etd1p is somehow necessary to maintain Spg1p activity during anaphase until the completion of cytokinesis
PMID:15936270	FYPO:0007380	elongated T-shaped vegetative cell	(Figure 2B)
PMID:15936270	FYPO:0001018	abolished NETO	(comment: Δwsh3 cells were found to grow exclusively in a monopolar fashion.)
PMID:15936270	FYPO:0000013	T-shaped vegetative cell [has_penetrance] 30	(penetrance from 6B) highly bent or branched morphology (Figure 2a)
PMID:15936270	FYPO:0007379	T-shaped vegetative cell [has_penetrance] 20	(penetrance from 6B) nWe found that high osmolarity stress by 0.6 M KCl also promotes appearance of T-shaped cells in the Δtea1 strain, to the levels comparable to the Δwsh3 mutant (Figure 6B).
PMID:15936270	FYPO:0001019	monopolar actin cortical patch localization during vegetative growth	Actin patches, which are localized to the growing tips of fission yeast cells [38], were detected mostly in one tip of the Δwsh3 cell (Figure 2C).
PMID:15936270	FYPO:0007379	T-shaped vegetative cell	Cell polarity defects with bent and branched morphology were observed after shifting the Δspc1 mutant from 25oC to 36oC (Figure 6C).
PMID:15936270	FYPO:0001357	normal vegetative cell population growth	DNS
PMID:15936270	FYPO:0007398	normal stress-activated MAPK cascade	DNS
PMID:15936270	FYPO:0005503	abnormally monopolar protein localization to cell tip [assayed_using] PomBase:SPCC1223.06 [has_severity] high	In contrast, most of Δwsh3 cells showed highly concentrated Tea1-GFP signals at one end, while the other end contained significantly less Tea1-GFP dots (Figure 5A, right panel)
PMID:15936270	FYPO:0002104	viable vegetative cell with normal cell shape	On the other hand, oxidative stress by hydrogen peroxide, which also induces Spc1 activation [34], did not significantly affect Δwsh3 cells (data not shown).
PMID:15936270	FYPO:0003209	abolished protein localization to cell tip, with protein mislocalized to cytoplasm [assayed_using] PomBase:SPBC1706.01	The specific localization of Wsh3-GFP was lost in the Δtea1 mutant and the Wsh3-GFP signal was diffused throughout the cytoplasm (Figure 4A)
PMID:15936270	FYPO:0004700	bent vegetative cell [has_penetrance] 65	We also found that, even under the optimal growth condition, the Δspc1 mutation exacerbates the morphology defects of the Δtea1 mutant; the Δtea1 Δspc1 double mutant grown at 30oC in rich YES medium contain large fractions of significantly bent and branched cells (Figure 6D).
PMID:15936270	FYPO:0007379	T-shaped vegetative cell [has_penetrance] 3	We also found that, even under the optimal growth condition, the Δspc1 mutation exacerbates the morphology defects of the Δtea1 mutant; the Δtea1 Δspc1 double mutant grown at 30oC in rich YES medium contain large fractions of significantly bent and branched cells (Figure 6D).
PMID:15936270	FYPO:0003209	abolished protein localization to cell tip, with protein mislocalized to cytoplasm [assayed_using] PomBase:SPCC1223.06	Wsh3-GFP was abrogated by a mutation in β- tubulin, nda3-KM311 [39] even at its permissive temperature, 30oC (Figure 3B, left).
PMID:15936270	FYPO:0007379	T-shaped vegetative cell [has_penetrance] 20	highly bent or branched morphology (Figure 2a) (penetrance from Figure 6B)
PMID:15936270	FYPO:0007379	T-shaped vegetative cell [has_penetrance] 20	highly bent or branched morphology (Figure 2a) (penetrance from Figure 6B)
PMID:15936270	FYPO:0003209	abolished protein localization to cell tip, with protein mislocalized to cytoplasm [assayed_using] PomBase:SPAC2F7.03c	Δwsh3 cells, the cell-end localization of Pom1 was lost and Pom1-GFP often accumulated in vesicle-like structures in the cytoplasm (Figure 5D)
PMID:15937127	GO:0061608	nuclear import signal receptor activity [has_input] PomBase:SPAC1783.07c [part_of] protein import into nucleus	(Fig. 2)
PMID:15937127	GO:0061608	nuclear import signal receptor activity [part_of] protein import into nucleus	(Fig. 2)
PMID:15937127	GO:0006606	protein import into nucleus	(Fig. 2)
PMID:15937127	GO:0006606	protein import into nucleus	(Fig. 2)
PMID:15937127	FYPO:0003302	nucleus mislocalized towards cell tip during mitotic interphase [has_penetrance] 10.4	(Fig. 3 B-2) (comment: 1.1% WT)
PMID:15937127	FYPO:0006339	mononucleate vegetative cell with mislocalized nucleus [has_penetrance] 2.1	(Fig. 3 B-2) (comment: never seen in WT)
PMID:15937127	FYPO:0001355	decreased vegetative cell population growth	(Fig. 3)
PMID:15937127	FYPO:0002060	viable vegetative cell population	(Fig. 3)
PMID:15937127	FYPO:0003165	cut with abnormal chromosome segregation	(Fig. 3C)
PMID:15937127	GO:0061608	nuclear import signal receptor activity [has_input] PomBase:SPAC1783.07c [part_of] protein import into nucleus	(Figure 2)
PMID:15937127	GO:0034399	nuclear periphery	(Figure 3F-3)
PMID:15937127	GO:0005634	nucleus	(Figure 3F-3)
PMID:15937127	GO:0034399	nuclear periphery	(Figure 3F-3)
PMID:15937127	GO:0005634	nucleus	(Figure 3F-3)
PMID:15937127	FYPO:0000726	sensitive to oxidative stress [has_severity] high	(Figure 4D)
PMID:15937127	FYPO:0004339	decreased protein localization to nucleus during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC1783.07c	(Figure 4D)
PMID:15937127	FYPO:0000726	sensitive to oxidative stress [has_severity] medium	(Figure 4D)
PMID:15937127	FYPO:0004835	abolished protein localization to nucleus during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC1783.07c	(Figure 4D)
PMID:15937127	FYPO:0000839	inviable elongated mononucleate aseptate cell [has_severity] medium	(Figure 5B)
PMID:15937127	FYPO:0000839	inviable elongated mononucleate aseptate cell [has_severity] medium	(Figure 5B)
PMID:15937127	FYPO:0006338	nucleus mislocalized towards cell tip during mitotic telophase	(comment: DNA at the tips, telophase delay)
PMID:15941470	FYPO:0002061	inviable vegetative cell population	(comment: Tev protease present; Cdc23 truncated)
PMID:15941470	FYPO:0002060	viable vegetative cell population	(comment: Tev protease present; Cdc23 truncated)
PMID:15941470	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPAC6B12.10c	(comment: Tev protease present; Cdc23 truncated; Cdc23 C-terminal fragment not retained in nucleus)
PMID:15941470	FYPO:0000838	normal protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPBC725.13c	(comment: Tev protease present; Cdc23 truncated; Cdc23 C-terminal fragment not retained in nucleus)
PMID:15941470	FYPO:0001430	abnormal mitotic cell cycle arrest with unreplicated DNA	(comment: Tev protease present; Cdc23 truncated; N starvation/recovery synchronizes cells)
PMID:15941470	FYPO:0000611	abnormal cell cycle arrest in mitotic S phase	(comment: Tev protease present; Cdc23 truncated; cells not synchronized)
PMID:15947136	FYPO:0001355	decreased vegetative cell population growth	(Fig. S4)
PMID:15957215	GO:0006265	DNA topological change	(comment: from the catenated plasmid experiment and failure to separate sisters)
PMID:15992541	FYPO:0004609	spindle pole bodies present in increased numbers during meiosis [has_penetrance] 10	(comment: CHECK promoter repressed)
PMID:15992541	FYPO:0004609	spindle pole bodies present in increased numbers during meiosis [has_penetrance] 25	(comment: thiamine absent; expression level lower than with endogenous promoter but higher than when repressed)
PMID:16055437	GO:0140309	unfolded protein holdase activity [part_of] cellular response to unfolded protein	(Figure 1a)
PMID:16079916	FYPO:0007632	increased histone H4-K16 acetylation during vegetative growth	(comment: assayed in intergenic regions)
PMID:16079916	FYPO:0007631	increased histone H4-K12 acetylation during vegetative growth	(comment: assayed in intergenic regions)
PMID:16079916	FYPO:0005309	increased histone H4-K5 acetylation during vegetative growth	(comment: assayed in intergenic regions)
PMID:16079916	FYPO:0005310	increased histone H3-K14 acetylation during vegetative growth	(comment: assayed in intergenic regions)
PMID:16079916	FYPO:0000892	increased histone H3-K9 acetylation during vegetative growth	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0007632	increased histone H4-K16 acetylation during vegetative growth	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0005310	increased histone H3-K14 acetylation during vegetative growth	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0005310	increased histone H3-K14 acetylation during vegetative growth	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0000892	increased histone H3-K9 acetylation during vegetative growth	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0007632	increased histone H4-K16 acetylation during vegetative growth	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0007631	increased histone H4-K12 acetylation during vegetative growth	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0000892	increased histone H3-K9 acetylation during vegetative growth	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0005309	increased histone H4-K5 acetylation during vegetative growth	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0005309	increased histone H4-K5 acetylation during vegetative growth	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0005310	increased histone H3-K14 acetylation during vegetative growth	(comment: protein-coding genes and intergenic regions)
PMID:16079916	FYPO:0007631	increased histone H4-K12 acetylation during vegetative growth	(comment: protein-coding genes and intergenic regions)
PMID:16079916	GO:0031509	subtelomeric heterochromatin formation	Sir2 and Clr3 act cooperatively upon histone H3 at K9/K14 throughout the genome, including all the silent regions (rDNA, centromeres, mat2/3 and telomeres).
PMID:16085489	GO:0044878	mitotic cytokinesis checkpoint signaling	(comment: clp1 cytoplasmic localization not maintained during cytokinetic stress. cdc7 localization to SPB not maintained during cytokinetic stress)
PMID:16087707	GO:0000147	actin cortical patch assembly	(comment: also from synthetic lethality with myo1, timing of localization to patches, and vrp1 mutant phenotype)
PMID:16087707	GO:0000147	actin cortical patch assembly	(comment: also from timing of localization to patches)
PMID:16087707	GO:0000147	actin cortical patch assembly	(comment: also from timing of localization to patches)
PMID:16087707	GO:0000147	actin cortical patch assembly	(comment: also from timing of localization to patches)
PMID:16087707	GO:0030479	actin cortical patch	(comment: dependent on F-actin, assayed using Latrunculin A)
PMID:16087707	GO:0030479	actin cortical patch	(comment: dependent on F-actin, assayed using Latrunculin A)
PMID:16087707	GO:0030479	actin cortical patch	(comment: dependent on F-actin, assayed using Latrunculin A)
PMID:16087707	GO:0071933	Arp2/3 complex binding	(comment: specific Arp2/3 complex subunit(s) not identified; authors use Myo1 tail as representative of whole protein)
PMID:16087707	GO:0071933	Arp2/3 complex binding	(comment: specific Arp2/3 complex subunit(s) not identified; authors use Myo1 tail as representative of whole protein)
PMID:16087749	GO:0140673	transcription elongation-coupled chromatin remodeling	. No unmodifiedPol II could be detected in these immunoprecipitates, althoughunmodified Pol II could be readily detected in the input extracts. These data demonstrate that SpSet2 is associated withthe elongating form of Pol II in S. pombe.
PMID:16087749	FYPO:0002919	abolished histone H3-K36 methylation during vegetative growth	As shown in Fig. 4A, deletion of set2+ resulted in a complete abolishment of K36 methylation (mono-, di-, and trimethylation), but not K4 methylation or H3 K9 acetylation, in bulk histones
PMID:16087749	GO:0140955	histone H3K36 trimethyltransferase activity [has_input] PomBase:SPAC1834.04 [part_of] transcription elongation-coupled chromatin remodeling	As shown in Fig. Fig. 2D,3D, SpSet2 was able to methylate an H3 peptide of residues 27 to 45, but not that of an H3 N-terminal peptide (residues 1 to 20). These data demonstrate that SpSet2 is a robust nucleosome-selective HMT specific for K36 methylation.
PMID:16087749	GO:0140955	histone H3K36 trimethyltransferase activity [has_input] PomBase:SPBC1105.11c [part_of] transcription elongation-coupled chromatin remodeling	As shown in Fig. Fig. 2D,3D, SpSet2 was able to methylate an H3 peptide of residues 27 to 45, but not that of an H3 N-terminal peptide (residues 1 to 20). These data demonstrate that SpSet2 is a robust nucleosome-selective HMT specific for K36 methylation.
PMID:16087749	GO:0140955	histone H3K36 trimethyltransferase activity [has_input] PomBase:SPBC8D2.04 [part_of] transcription elongation-coupled chromatin remodeling	As shown in Fig. Fig. 2D,3D, SpSet2 was able to methylate an H3 peptide of residues 27 to 45, but not that of an H3 N-terminal peptide (residues 1 to 20). These data demonstrate that SpSet2 is a robust nucleosome-selective HMT specific for K36 methylation.
PMID:16087749	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPAC29B12.02c [part_of] transcription elongation-coupled chromatin remodeling	As shown in Fig. Fig. 2D,3D, SpSet2 was able to methylate an H3 peptide of residues 27 to 45, but not that of an H3 N-terminal peptide (residues 1 to 20). These data demonstrate that SpSet2 is a robust nucleosome-selective HMT specific for K36 methylation.
PMID:16087749	GO:0140954	histone H3K36 dimethyltransferase activity [has_input] PomBase:SPAC1834.04 [part_of] transcription elongation-coupled chromatin remodeling	The results revealed that histone H3 was the only histone methylated (Fig. 3B).
PMID:16087749	GO:0140954	histone H3K36 dimethyltransferase activity [has_input] PomBase:SPBC1105.11c [part_of] transcription elongation-coupled chromatin remodeling	The results revealed that histone H3 was the only histone methylated (Fig. 3B).
PMID:16087749	GO:0140954	histone H3K36 dimethyltransferase activity [has_input] PomBase:SPBC8D2.04 [part_of] transcription elongation-coupled chromatin remodeling	The results revealed that histone H3 was the only histone methylated (Fig. 3B).
PMID:16087749	FYPO:0002060	viable vegetative cell population	set2Δ cells grew normally on rich YEA medium, they showed a strong growth defect in synthetic medium (EMM), which is nutrient depleted compared to YEA (Fig. 4B).
PMID:16087749	FYPO:0001355	decreased vegetative cell population growth	set2Δ cells grew normally on rich YEA medium, they showed a strong growth defect in synthetic medium (EMM), which is nutrient depleted compared to YEA (Fig. 4B).
PMID:16096637	GO:0043539	protein serine/threonine kinase activator activity [has_input] PomBase:SPBC17F3.02	(comment: Pmo25 formed a complex with Nak1 and was required for both the localization and kinase activity of Nak1).
PMID:16096637	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	(comment: both SPBs in early mitosis)
PMID:16096637	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC1834.06c	In sharp contrast, on a cdc7-24 or sid1-239 mutant background, no Pmo25 was detected at the mitotic SPB(s) (Figure 8B and C).
PMID:16096637	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC1834.06c	In sharp contrast, on a cdc7-24 or sid1-239 mutant background, no Pmo25 was detected at the mitotic SPB(s) (Figure 8B and C).
PMID:16111942	GO:0035974	meiotic spindle pole body [exists_during] meiotic prophase I	(Fig. 1A) appeared at the SPB upon conjugation of haploid cells, persisted until the onset of meiosis I, and disappeared thereafter
PMID:16111942	FYPO:0000590	normal sporulation	(Supp. Figure. S1D)
PMID:16111942	GO:0030989	dynein-driven meiotic oscillatory nuclear movement	(comment: various exp, and ectoptic mitotic expression)
PMID:16111942	GO:0032118	horsetail-astral microtubule organization	(comment: various exp, and ectoptic mitotic expression)
PMID:16111942	FYPO:0004796	normal azygotic meiosis	Interestingly, however, azygotic asci arising from diploid hrs1D cells did not show an apparent defect in spore formation (Figure S1D
PMID:16120966	GO:0003899	DNA-directed RNA polymerase activity	(comment: can incorporate NTPs or dNTPs; changed from primase activity because not tested with unprimed template)
PMID:16120966	GO:0003887	DNA-directed DNA polymerase activity	(comment: distributive; substrate preference: small gaps with a 5′-phosphate group)
PMID:16127433	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2A)
PMID:16127433	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	(Fig. 2A)
PMID:16127433	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [has_severity] high [assayed_protein] PomBase:SPAC664.01c	(Fig. 2B)
PMID:16127433	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAC664.01c	(Fig. 2B)
PMID:16127433	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] high [assayed_protein] PomBase:SPAC664.01c	(Fig. 2B)
PMID:16127433	FYPO:0004137	decreased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth [has_severity] high	(Fig. 2B)
PMID:16127433	FYPO:0002355	decreased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 2B)
PMID:16127433	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 2B)
PMID:16127433	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 17	(Fig. 3A)
PMID:16127433	FYPO:0001861	increased minichromosome loss upon segregation during vegetative growth	(Fig. 3B)
PMID:16127433	FYPO:0000468	abnormal mating type switching	(Fig. 3C)
PMID:16127433	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	(Fig. 4A)
PMID:16127433	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 4A)
PMID:16127433	FYPO:0004745	abolished histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 4B)
PMID:16127433	FYPO:0008208	abolished protein neddylation during vegetative growth [assayed_protein] PomBase:SPAC3A11.08	(Fig. 4B)
PMID:16127433	FYPO:0005850	abolished protein localization to heterochromatin at centromere outer repeat [assayed_protein] PomBase:SPAC664.01c	(Fig. 4B)
PMID:16127433	FYPO:0002331	increased histone H3-K4 dimethylation at centromere outer repeat during vegetative growth	(Fig. 4B)
PMID:16127433	FYPO:0004745	abolished histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 4B)
PMID:16127433	FYPO:0005850	abolished protein localization to heterochromatin at centromere outer repeat [assayed_protein] PomBase:SPAC664.01c	(Fig. 4B)
PMID:16127433	FYPO:0002331	increased histone H3-K4 dimethylation at centromere outer repeat during vegetative growth	(Fig. 4B)
PMID:16127433	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [has_severity] high [assayed_protein] PomBase:SPBC428.08c	(Fig. 5A)
PMID:16127433	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] high [assayed_protein] PomBase:SPBC428.08c	(Fig. 5A)
PMID:16127433	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC664.01c	(Fig. 5C)
PMID:16127433	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC428.08c	(Fig. 5C)
PMID:16127433	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_protein] PomBase:SPCC11E10.08	(Fig. 5D)
PMID:16127433	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. S3)
PMID:16127433	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	(Fig. S3)
PMID:16127433	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. S3)
PMID:16127433	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Fig. S3)
PMID:16127433	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S3)
PMID:16127433	FYPO:0001357	normal vegetative cell population growth	(Fig. S3)
PMID:16127433	FYPO:0001357	normal vegetative cell population growth	(Fig. S3)
PMID:16127433	FYPO:0001357	normal vegetative cell population growth	(Fig. S3)
PMID:16138082	FYPO:0008060	normal mono ubiquitin binding	From these results, we conclude that the F330A mutation significantly reduces the affinity of the Mud1 UBA domain for K48-linked polyUb chains without significantly affecting monoUb binding.
PMID:16138082	FYPO:0008059	decreased K48-linked polyubiquitin binding	From these results, we conclude that the F330A mutation significantly reduces the affinity of the Mud1 UBA domain for K48-linked polyUb chains without significantly affecting monoUb binding.
PMID:16141239	FYPO:0000422	decreased endocytosis during vegetative growth	(Fig. 5A,B)
PMID:16141239	FYPO:0000426	normal endocytosis	(Fig. 5A,B)
PMID:16141239	FYPO:0000422	decreased endocytosis during vegetative growth	(Fig. 5A,B)
PMID:16141239	FYPO:0006341	abolished equatorial endocytosis during mitosis	(comment: endocytosis restricted to cell end)
PMID:16141239	FYPO:0000034	abnormal endocytosis during vegetative growth	(comment: endocytosis restricted to cell end)
PMID:16141239	FYPO:0006341	abolished equatorial endocytosis during mitosis	(comment: endocytosis restricted to cell end)
PMID:16141239	FYPO:0006341	abolished equatorial endocytosis during mitosis	(comment: endocytosis restricted to cell end)
PMID:16157682	FYPO:0000468	abnormal mating type switching	(Fig. 1C)
PMID:16157682	FYPO:0000468	abnormal mating type switching	(Fig. 1C)
PMID:16157682	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	(Fig. 2A)
PMID:16157682	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	(Fig. 2A)
PMID:16157682	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. 2B)
PMID:16157682	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. 2B)
PMID:16157682	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2C)
PMID:16157682	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 2C)
PMID:16157682	FYPO:0004909	loss of punctate nuclear protein localization, with protein distributed in nucleus [assayed_protein] PomBase:SPAC664.01c [has_penetrance] complete	(Fig. 5)
PMID:16157682	FYPO:0004909	loss of punctate nuclear protein localization, with protein distributed in nucleus [assayed_protein] PomBase:SPAC664.01c [has_penetrance] complete	(Fig. 5)
PMID:16157682	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	(Fig. 7)
PMID:16157682	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 7)
PMID:16157682	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 7)
PMID:16157682	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 7)
PMID:16157682	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	(Fig. 7)
PMID:16157682	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	(Fig. 7)
PMID:16157682	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	(Fig. 7)
PMID:16157682	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	(Fig. 7)
PMID:16157682	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	(Fig. 7)
PMID:16157682	FYPO:0002355	decreased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 8B)
PMID:16157682	FYPO:0002355	decreased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 8B)
PMID:16157682	FYPO:0006112	abolished histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth	(Fig. 8B)
PMID:16157682	FYPO:0005063	increased histone H3-K4 methylation at mating type locus during vegetative growth	(Fig. 8C)
PMID:16157682	FYPO:0005063	increased histone H3-K4 methylation at mating type locus during vegetative growth	(Fig. 8C)
PMID:16157682	FYPO:0005063	increased histone H3-K4 methylation at mating type locus during vegetative growth	(Fig. 8C)
PMID:16157682	FYPO:0001840	increased minichromosome loss during vegetative growth [has_severity] high	Table 2 and Fig. 4
PMID:16157682	FYPO:0001840	increased minichromosome loss during vegetative growth [has_severity] high	Table 2 and Fig. 4
PMID:16169489	FYPO:0000581	decreased spore germination frequency	(comment: 27% of spores produce viable colonies)
PMID:16169489	FYPO:0002059	inviable cell population	(comment: knocked out in diploid. Can't tell if it vegetative or spore?)
PMID:16169489	FYPO:0002059	inviable cell population	(comment: knocked out in diploid. Can't tell if it vegetative or spore?)
PMID:1617727	GO:0045292	mRNA cis splicing, via spliceosome	(comment: CHECK splicing of artificial construct with wt or mutated splice sites assayed in mutants)
PMID:16199877	FYPO:0002061	inviable vegetative cell population	(Fig. 1A)
PMID:16199877	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] complete	(Fig. 1B)
PMID:16199877	FYPO:0001234	slow vegetative cell population growth	(Fig. 1D)
PMID:16199877	FYPO:0001234	slow vegetative cell population growth	(Fig. 1D)
PMID:16199877	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] complete	(Fig. 1E)
PMID:16199877	FYPO:0002061	inviable vegetative cell population	(Fig. 3A)
PMID:16199877	FYPO:0001490	inviable elongated vegetative cell	(Fig. 3B)
PMID:16199877	FYPO:0000229	cut	(Fig. 3B)
PMID:16199877	FYPO:0001494	inviable elongated multiseptate vegetative cell	(Fig. 3B)
PMID:16199877	FYPO:0004412	abolished protein localization to mitotic spindle midzone during anaphase [assayed_using] PomBase:SPBC336.15	(Fig. 3C)
PMID:16199877	GO:0072686	mitotic spindle [exists_during] mitotic anaphase	(Fig. 3C)
PMID:16199877	GO:0000776	kinetochore [exists_during] mitotic metaphase	(Fig. 3C)
PMID:16199877	GO:0072686	mitotic spindle [exists_during] mitotic anaphase	(Fig. 3C)
PMID:16199877	GO:0000776	kinetochore [exists_during] mitotic metaphase	(Fig. 3C)
PMID:16199877	FYPO:0008164	abnormal protein localization to kinetochore during mitotic M phase	(Fig. 3C)
PMID:16199877	FYPO:0000316	inviable after spore germination	(Fig. 4)
PMID:16199877	FYPO:0008164	abnormal protein localization to kinetochore during mitotic M phase [assayed_protein] PomBase:SPCC962.02c [has_penetrance] 76	(Fig. 5D,E)
PMID:16199877	FYPO:0000316	inviable after spore germination	(Fig. S1A)
PMID:16199877	FYPO:0000141	abnormal mitotic sister chromatid segregation	(Fig. S1B)
PMID:16199877	FYPO:0006640	abnormal protein localization to mitotic spindle pole body during anaphase B [assayed_using] PomBase:SPCC962.02c	(Fig. S1C)
PMID:16199877	FYPO:0007401	abnormal protein localization to kinetochore during mitotic anaphase [assayed_using] PomBase:SPCC962.02c	(Fig. S1C)
PMID:16199877	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 65	(Figure 4B)
PMID:16199877	FYPO:0000229	cut	(Figure 4B)
PMID:16199877	FYPO:0000228	lagging mitotic chromosomes	(Figure 4B)
PMID:16199877	FYPO:0000284	large and small daughter nuclei, with unequal mitotic sister chromatid segregation	(Figure 4B)
PMID:16199877	FYPO:0000268	sensitive to UV during vegetative growth	DNS
PMID:16199877	FYPO:0000266	sensitive to DNA damaging agents	DNS
PMID:16199877	FYPO:0000091	sensitive to thiabendazole	DNS
PMID:16199877	FYPO:0000229	cut	DNS
PMID:16246721	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPBC800.03	(comment: [ vw specifically to REIII/ CAS, nucleation site]) In double mutant cells lacking Pcr1 and Swi6, the localization of Clr3 was almost completely abolished from REIII (Figure 3).
PMID:16246721	GO:0030466	silent mating-type cassette heterochromatin formation	(comment: [NUCLEATION/SPREADING]) Subsequently, Clr3 spreads across the entire mat2/3 interval that is dependent upon its own HDAC activity, Swi6 and Sir2 proteins, and possibly other factors, such as Chp2, involved in heterochromatin assembly. These results suggest that Clr3 operates in a pathway parallel to RNAi to nucleate heterochromatin at the mat locus.
PMID:16246721	GO:0030466	silent mating-type cassette heterochromatin formation	(comment: [NUCLEATION] Same pathway as clr3)
PMID:16246721	GO:0030466	silent mating-type cassette heterochromatin formation	(comment: [NUCLEATION])
PMID:16246721	GO:0030466	silent mating-type cassette heterochromatin formation	(comment: [SPREADING] ) Subsequently, Clr3 spreads across the entire mat2/3 interval that is dependent upon its own HDAC activity, Swi6 and Sir2 proteins, and possibly other factors, such as Chp2, involved in heterochromatin assembly.
PMID:16246721	GO:0030466	silent mating-type cassette heterochromatin formation	(comment: [SPREADING] ) Subsequently, Clr3 spreads across the entire mat2/3 interval that is dependent upon its own HDAC activity, Swi6 and Sir2 proteins, and possibly other factors, such as Chp2, involved in heterochromatin assembly.
PMID:16246721	GO:0030466	silent mating-type cassette heterochromatin formation	(comment: [SPREADING]) Subsequently, Clr3 spreads across the entire mat2/3 interval that is dependent upon its own HDAC activity, Swi6 and Sir2 proteins, and possibly other factors, such as Chp2, involved in heterochromatin assembly.
PMID:16246721	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth	..... However, in clr3D cells, H3K9me3 was significantly reduced, while there was a substantial increase in H3K9me1. Furthermore, H3K9me2 levels were slightly elevated (Figure 5A).
PMID:16246721	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth	.....Interestingly, identical modification patterns were also observed in a swi6 mutant, consistent with Swi6 involvement in Clr3 spreading (Figure 5A).
PMID:16246721	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPBC800.03 [part_of] silent mating-type cassette heterochromatin formation	At the mat locus, Clr3 is recruited at a specific site through a mechanism involving ATF/CREB family proteins
PMID:16246721	FYPO:0007891	decreased spatial extent of mating-type region heterochromatin assembly	ChIP analysis revealed that the Clr3 mutant protein was mainly restricted to the nucleation site adjacent to the mat3 locus and the spreading of Clr3 across the mat2/3 region was severely affected (Figure 2A).
PMID:16246721	FYPO:0008158	increased histone H3-S10 phosphorylation at the silent mating-type locus during vegetative growth	Furthermore, the levels of H3S10 phosphorylation (H3S10ph), another modification mark associated with active chromatin as well as mitotic chromosomes (Nowak and Corces, 2004), were also increased at the mat locus (Figure 6A).
PMID:16246721	FYPO:0007891	decreased spatial extent of mating-type region heterochromatin assembly	In the absence of Swi6, Clr3 localization was confined to a small region near the mat3 locus (Figure 2A), which is distinct from the cenH element responsible for RNAi-mediated targeting of heterochromatin to this region.
PMID:16246721	FYPO:0008159	abolished histone H3-S10 phosphorylation at the silent mating-type locus during vegetative growth	Our analyses revealed that a temperature-sensitive mutation in the survivin homolog Cut17/ Bir1 (cut17-275), which is known to bind centromeric repeats and is required for proper localization of fission yeast aurora kinase Ark1 (Morishita et al., 2001), almost completely abolished H3S10ph at the mat locus in clr3D cells (Figure 6C).
PMID:16246721	GO:0031934	mating-type region heterochromatin	Our results revealed that Clr3 is indeed enriched throughout the 20 kb heterochromatic domain surrounded by the IR-R and IR-L boundary elements but is absent at the surrounding euchromatic regions (Figure 2A).
PMID:16246721	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPBC428.08c	Remarkably, loss of Swi6 and Chp2 but not Chp1 completely abolished the localization of Clr3 at Kint2::ura4+ (Figure 1)
PMID:16246721	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPBC800.03	Remarkably, loss of Swi6 and Chp2 but not Chp1 completely abolished the localization of Clr3 at Kint2::ura4+ (Figure 1)
PMID:16246721	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPBC800.03	Remarkably, loss of Swi6 and Chp2 but not Chp1 completely abolished the localization of Clr3 at Kint2::ura4+ (Figure 1)
PMID:16246721	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPBC800.03	Remarkably, loss of Swi6 and Chp2 but not Chp1 completely abolished the localization of Clr3 at Kint2::ura4+ (Figure 1)
PMID:16246721	FYPO:0003097	abolished histone H3-K9 methylation at centromere outer repeat during vegetative growth	Remarkably, whereas clr3D or dcr1D single mutant strains still maintained H3K9 methylation, H3K9me at centromeric repeats was almost completely abolished in clr3Ddcr1D double mutant cells (Figure 4C).
PMID:16246721	FYPO:0008158	increased histone H3-S10 phosphorylation at the silent mating-type locus during vegetative growth [has_severity] low	Similar changes were observed in the swi6 mutant; however, the effect on H3S10ph was weaker than in the clr3 mutant (Figure 6A).
PMID:16246721	FYPO:0007891	decreased spatial extent of mating-type region heterochromatin assembly [has_severity] high	Surprisingly, except for a small but reproducible enrichment of Clr3 at the nucleation site, Clr3 was virtually absent from the entire mat2/3 region in a sir2D strain (Figure 2A).
PMID:16246721	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC800.03	These data, together with results showing defects in Swi6 localization at the mat locus in clr3-735 cells (see below; Figure S2)
PMID:16246721	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	We next explored whether loss of Clr3 affects Swi6 binding at the mat locus. Deletion of clr3 resulted in severely reduced Swi6 levels at Kint2::ura4+ even though Swi6 expression was not affected (Figure 5C; Figure S3).
PMID:16246721	GO:0031508	pericentric heterochromatin formation	We show that Cir3, a fission yeast homolog of mammalian class |I HDACs, acts in a distinct pathway parallel to RNAi-directed heterochromatin nucleation to recruit Cl4 and mediate H3K9 methylation at the silent mating-type region and centromeres.
PMID:16246721	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth	Whereas H3K9me levels at Kint2:: ura4+ were not affected in clr3D, dcr1D, or atf1D single mutants compared to wild-type, H3K9me was completely abolished in a clr3D dcr1D double mutant strain (Figure 4A).
PMID:16246721	FYPO:0007633	increased histone H3-K14 acetylation at silent mating-type cassette during vegetative growth	deletion of clr3 resulted in an increase in acetylation at H3K14 (H3K14ac) (Figure 6A), a mark of active chromatin that is absent at heterochromatic loci.
PMID:16246721	FYPO:0008157	abnormal histone deacetylation at the silent mating-type locus during vegetative growth	mutant cells are defective in histone deacetylation and silencing at the mat2/3 locus (see Figure S1
PMID:16251348	GO:0005730	nucleolus	(Fig. 2c)
PMID:16251348	GO:0006364	rRNA processing	(Fig. 3B)
PMID:16252005	GO:0006511	ubiquitin-dependent protein catabolic process	(comment: CHECK -regulation - can also infer from GO:0030674)
PMID:16252005	FYPO:0000085	sensitive to camptothecin [has_severity] high	(comment: same as cdt2delta alone)
PMID:16252005	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(comment: same as cdt2delta alone)
PMID:16252005	FYPO:0000085	sensitive to camptothecin [has_severity] low	(comment: same as csn1delta alone)
PMID:16252005	FYPO:0000085	sensitive to camptothecin [has_severity] high	(comment: same as ddb1delta alone)
PMID:16252005	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(comment: same as ddb1delta alone)
PMID:16252005	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(comment: same as pcu4delta alone)
PMID:16252005	FYPO:0000085	sensitive to camptothecin [has_severity] high	(comment: same as pcu4delta alone_
PMID:16262791	GO:0043539	protein serine/threonine kinase activator activity [part_of] positive regulation of TORC1 signaling	detectable in mutants that increase bound GTP:GDP ratio, implying that protein-protein interaction is GTP-dependent
PMID:16272747	FYPO:0008141	decreased RNA level during meiosis II [assayed_transcript] PomBase:SPBC26H8.02c	As shown in Fig. 2A, accumulation of sec9 mRNA was completely abolished in the mei4Δ mutant. Furthermore, ectopic overexpression of mei4+ was found to induce sec9+ mRNA in vegetative cells (Fig. 2C). sec9+ has a consensus recognition sequence for Mei4, GTAAAYA (Horie et al., 1998) in the 5' upstream region. We conclude that transcription of sec9+ during meiosis is strictly regulated by Mei4.
PMID:16272747	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC26H8.02c [happens_during] meiosis II cell cycle phase	As shown in Fig. 2A, accumulation of sec9 mRNA was completely abolished in the mei4Δ mutant. Furthermore, ectopic overexpression of mei4+ was found to induce sec9+ mRNA in vegetative cells (Fig. 2C). sec9+ has a consensus recognition sequence for Mei4, GTAAAYA (Horie et al., 1998) in the 5' upstream region. We conclude that transcription of sec9+ during meiosis is strictly regulated by Mei4.
PMID:16272747	FYPO:0002061	inviable vegetative cell population	In addition to causing a defect in ascospore formation, the sec9-10 mutation compromised vegetative growth. As shown in Fig. 3B, the sec9-10 mutant grew well at 25°C but was unable to form colonies at 37°C.
PMID:16272747	FYPO:0000622	abnormal cell cycle arrest in mitotic telophase	In marked contrast, sec9-10 cells exhibited a rather uniform arrest morphology at the restrictive temperature (Fig. 3C). At 12 hr after the shift to 34°C, approximately 43% of the sec9-10 cells had a single septum, and 4% exhibited multiple septa (Table II).
PMID:16272747	FYPO:0001253	elongated multinucleate multiseptate vegetative cell, single septa between nuclei [has_penetrance] 4	In marked contrast, sec9-10 cells exhibited a rather uniform arrest morphology at the restrictive temperature (Fig. 3C). At 12 hr after the shift to 34°C, approximately 43% of the sec9-10 cells had a single septum, and 4% exhibited multiple septa (Table II).
PMID:16272747	FYPO:0001914	abnormal prospore membrane formation	In wild type cells, most haploid nuclei produced by meiotic second divisions were encapsulated by the FSM (Fig. 4A). In sec9-10 mutant cells, FSMs initiated normally at both poles of the meiosis II spindles (Fig. 4A), but extension of the FSMs was soon blocked, resulting in anucleated small prespores (Fig. 4B). These results indicated that the FSM initiated normally, but its subsequent development was abnormal.
PMID:16272747	PomGeneEx:0000011	RNA level increased [during] meiotic prophase II	The level of sec9 mRNA began to increase about 6 hr after induction and peaked at about 9 hr, when cells were in early meiosis II (Fig. 2A, 2B).
PMID:16272747	FYPO:0001234	slow vegetative cell population growth	Therefore, sec9+ is essential for vegetative cell growth and spore germination.
PMID:16272747	FYPO:0001234	slow vegetative cell population growth	Therefore, sec9+ is essential for vegetative cell growth and spore germination.
PMID:16272747	FYPO:0002061	inviable vegetative cell population	Therefore, sec9+ is essential for vegetative cell growth and spore germination.
PMID:16291723	FYPO:0001234	slow vegetative cell population growth	(Fig. 1A)
PMID:16291723	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] 95	(Fig. 1A) All cells lysed while undergoing division and the daughter cells remained attached to one another.
PMID:16291723	FYPO:0001366	normal actin cytoskeleton organization	(Fig. 1A) All cells lysed while undergoing division and the daughter cells remained attached to one another.
PMID:16291723	GO:0005783	endoplasmic reticulum	(Fig. 3B). Gyp10 localized to structures reminiscent of the endoplasmic reticulum (Broughton et al., 1997) when expressed from the low strength nmt81 promoter
PMID:16291723	FYPO:0002060	viable vegetative cell population	(Fig. 3C)
PMID:16291723	FYPO:0005869	inviable stubby multiseptate vegetative cell [has_penetrance] low	(Fig. 3C)
PMID:16291723	FYPO:0002200	inviable stubby septated vegetative cell	(Fig. 3C)
PMID:16291723	FYPO:0002061	inviable vegetative cell population	(Fig. 3C)
PMID:16291723	FYPO:0001234	slow vegetative cell population growth	(Fig. 3C).
PMID:16291723	FYPO:0000118	multiseptate vegetative cell [has_penetrance] low	(Fig. 3C).
PMID:16291723	FYPO:0001367	normal cytokinesis	(Fig. 6)
PMID:16291723	FYPO:0002442	normal protein localization to cell division site [assayed_protein] PomBase:SPCC645.07	(Figure 5C)
PMID:16291723	FYPO:0001880	abolished protein localization to cell division site [assayed_protein] PomBase:SPCC645.06c	(Figure 5C)
PMID:16291723	FYPO:0002442	normal protein localization to cell division site [assayed_protein] PomBase:SPCC645.06c	(Figure 5C) Interestingly, overexpression of gpt10+ (Fig. 5G), but not rho1+ (data not shown) restored the localization of Rgf3 in lad1-1 cells at 36°C.
PMID:16291723	FYPO:0002061	inviable vegetative cell population	(comment: CHECK `SYNTHETIC LETHAL)
PMID:16291723	FYPO:0003369	sensitive to sodium fluoride	(comment: CONDITION 50 mM)
PMID:16291723	FYPO:0002060	viable vegetative cell population	(comment: rgf3+ is essential)
PMID:16291723	FYPO:0002061	inviable vegetative cell population	(comment: rgf3+ is essential)
PMID:16291723	GO:0031097	medial cortex	.By contrast, Rgf3p-GFP was not detected at cell ends, only at the medial region of the cell (Fig. 4D). Furthermore, Rgf3p rings constricted (Fig. 4D, inset). These differences in pattern are illustrated in Fig. 4E
PMID:16291723	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC645.06c	Ace2p, we examined whether Rgf3p levels were altered in cells lacking or overproducing Ace2p. Overproduction of Ace2p led to increased Rgf3p levels whereas Rgf3p was less abundant in cells lacking Ace2p (Fig. 7B). However, Rgf3p-Myc13 was clearly detectable in the absence of Ace2p suggesting that other factors cooperate with Ace2p to regulate rgf3+ expression.
PMID:16291723	GO:0000935	division septum	Both proteins localized to the division site(Fig. 4B,D). Rgf1p-GFP formed rings (Fig. 4B) late in mitosis as only cells containing segregated DNA masses contained them (data not shown and Fig. 7A)
PMID:16291723	GO:0016192	vesicle-mediated transport	Consistent with a role in vesicular trafficking, gyp10 showed a strong negative genetic interaction with cells lacking the exocyst subunit, Exo70p (Wang et al., 2002) (Fig. 3C).
PMID:16291723	GO:0051286	cell tip	Rgf1p-GFP was also detected at cell ends (Fig. 4B).
PMID:16291723	GO:0140279	regulation of mitotic division septum assembly	Rgf3p appears necessary to stimulate Rho1p-mediated activation of a glucan synthase crucial after septation for proper new cell-end formation.
PMID:16291723	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC645.06c	To determine whether Rgf3p production was controlled by Ace2p, we examined whether Rgf3p levels were altered in cells lacking or overproducing Ace2p. Overproduction of Ace2p led to increased Rgf3p levels whereas Rgf3p was less abundant in cells lacking Ace2p (Fig. 7B
PMID:16291723	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC645.06c	To determine whether Rgf3p production was controlled by Ace2p, we examined whether Rgf3p levels were altered in cells lacking or overproducing Ace2p. Overproduction of Ace2p led to increased Rgf3p levels whereas Rgf3p was less abundant in cells lacking Ace2p (Fig. 7B
PMID:16291723	FYPO:0002442	normal protein localization to cell division site [assayed_protein] PomBase:SPAC1F7.04	asked whether Rho1p was able to localize correctly to the medial region of the cell in the lad1-1 strain that we had shown lacks medially placed Rgf3p (Fig. 5C). We found that it did (Fig. 6B).
PMID:16291723	FYPO:0000132	abnormal septum disassembly	with lysis (these are not chained cells) (Fig. 2C).....cells septum degradation appeared to initiate at a single position around the cell circumference and the entire cell wall disappeared from this area
PMID:16317005	GO:0051063	CDP reductase activity [part_of] dCDP biosynthetic process	(comment: CHECK activated_by CHEBI:15422 | inhibited_by CHEBI:16284)
PMID:16317005	GO:0051063	CDP reductase activity [part_of] dCDP biosynthetic process	(comment: CHECK activated_by CHEBI:15422 | inhibited_by CHEBI:16284)
PMID:16317047	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAPYUG7.03c	(Fig. 1B)
PMID:16317047	FYPO:0001327	increased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAPYUG7.03c	(Fig. 1D)
PMID:16317047	FYPO:0001327	increased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAPYUG7.03c	(Fig. 1E)
PMID:16317047	FYPO:0001327	increased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAPYUG7.03c	(Fig. 1F)
PMID:16317047	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAPYUG7.03c	(Fig. 1G)
PMID:16317047	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAPYUG7.03c	(Fig. 1G)
PMID:16317047	FYPO:0005115	elongated vegetative cell with central constriction	(Fig. 2A)
PMID:16317047	FYPO:0001584	abnormal protein localization to cell tip during vegetative growth [assayed_protein] PomBase:SPAPYUG7.03c	(Fig. 2B)
PMID:16317047	FYPO:0007028	normal protein localization to medial cortex septin ring during vegetative growth [assayed_protein] PomBase:SPAPYUG7.03c	(Fig. 2B)
PMID:16317047	FYPO:0001584	abnormal protein localization to cell tip during vegetative growth [assayed_protein] PomBase:SPBC16A3.01	(Fig. 2C)
PMID:16317047	FYPO:0006399	abnormal septin ring morphology	(Fig. 2D)
PMID:16317047	FYPO:0003334	normal protein localization to septin ring [assayed_protein] PomBase:SPBC16A3.01	(Fig. 3A)
PMID:16317047	FYPO:0003334	normal protein localization to septin ring [assayed_protein] PomBase:SPBC16A3.01	(Fig. 3A)
PMID:16317047	FYPO:0003334	normal protein localization to septin ring [assayed_protein] PomBase:SPBC16A3.01	(Fig. 3A)
PMID:16317047	FYPO:0003334	normal protein localization to septin ring [assayed_protein] PomBase:SPBC16A3.01	(Fig. 3A)
PMID:16317047	FYPO:0000118	multiseptate vegetative cell [has_severity] low [has_penetrance] 25	(Fig. 3B, 3C)
PMID:16317047	FYPO:0000118	multiseptate vegetative cell [has_penetrance] 25 [has_severity] medium	(Fig. 3B, 3C)
PMID:16317047	FYPO:0003500	viable branched, elongated, multiseptate vegetative cell [has_severity] medium [has_penetrance] 55	(Fig. 3B, 3C)
PMID:16317047	FYPO:0003500	viable branched, elongated, multiseptate vegetative cell [has_severity] medium [has_penetrance] 55	(Fig. 3B, 3C)
PMID:16317047	FYPO:0003500	viable branched, elongated, multiseptate vegetative cell [has_penetrance] 90 [has_severity] high	(Fig. 3B, 3C)
PMID:16317047	FYPO:0000118	multiseptate vegetative cell [has_penetrance] 40	(Fig. 3C)
PMID:16317047	FYPO:0000650	increased septation index [has_severity] high	(Fig. 3C)
PMID:16317047	FYPO:0000650	increased septation index [has_severity] high	(Fig. 3C)
PMID:16317047	FYPO:0000650	increased septation index [has_severity] high	(Fig. 3C)
PMID:16317047	FYPO:0000650	increased septation index [has_severity] high	(Fig. 3C)
PMID:16317047	FYPO:0000650	increased septation index [has_severity] high	(Fig. 3C)
PMID:16317047	FYPO:0000650	increased septation index [has_severity] medium	(Fig. 3C)
PMID:16317047	FYPO:0000118	multiseptate vegetative cell [has_penetrance] 10	(Fig. 3C)
PMID:16317047	FYPO:0000118	multiseptate vegetative cell [has_penetrance] 40	(Fig. 3C)
PMID:16317047	FYPO:0006399	abnormal septin ring morphology	(Fig. 3D)
PMID:16317047	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC6G10.12c [has_severity] high	(Fig. 4B)
PMID:16317047	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC6G10.12c [has_severity] high	(Fig. 4C)
PMID:16317047	MOD:00696	phosphorylated residue	(Fig. 4E)
PMID:16317047	MOD:01148	ubiquitinylated lysine	(Fig. 4F)
PMID:16317047	FYPO:0001327	increased protein level during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPAC6G10.12c	(Fig. 5C)
PMID:16317047	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC6G10.12c [has_severity] low	(Fig. 5C)
PMID:16317047	PomGeneEx:0000018	protein level increased [during] mitotic anaphase	Ace2p-Myc13 was periodically produced through the cell cycle (Fig. 4A). It began to accumulate during anaphase as determined by the coincidence of binucleate formation, and it peaked in abundance concomitantly with the peak of septation.
PMID:16325576	GO:0005515	protein binding	(Fig. 5A)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 60	(Fig. S1)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 15-20	(Fig. S1)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 15-20	(Fig. S1)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 15-20	(Fig. S1)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] >75	(Fig. S1)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 80	(Fig. S1)
PMID:16325576	FYPO:0000488	normal meiotic recombination	(Fig. S2)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] high	(Figure 1)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] high	(Figure 1)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] high	(Figure 1)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] high	(Figure 1)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] high	(Figure 1)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 95	(Figure 2C)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] complete	(Figure 2C)
PMID:16325576	FYPO:0004159	abnormal homologous chromosome segregation	(Figure 2C)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] complete	(Figure 2C, 3b)
PMID:16325576	FYPO:0005648	sister kinetochore dissociation in meiotic metaphase I	(Figure 2D) Although deletion of moa1+ thus causes a centromere-specific defect, recombination appears to promote reductional segregation in moa1D cells because the defect in monopolar attachment is lessened in diploid recombination-proficient meiosis compared to haploid meiosis or diploid
PMID:16325576	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores	(Figure 2a)
PMID:16325576	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores	(Figure 2a)
PMID:16325576	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 20	(Figure 2b)
PMID:16325576	FYPO:0007234	normal protein localization to centromere central core [assayed_protein] PomBase:SPAC15E1.07c	(Figure 5C) However, the ChIP assay demonstrated intact localization of Moa1 in rec8D meiotic cells (Figure 5C). Instead, we discovered that Moa1 localization was abolished in cells lacking CENP-C (Cnp3) (Figure 5C)
PMID:16325576	FYPO:0007234	normal protein localization to centromere central core [assayed_protein] PomBase:SPAC15E1.07c	(Figure 5C) However, the ChIP assay demonstrated intact localization of Moa1 in rec8D meiotic cells (Figure 5C). Instead, we discovered that Moa1 localization was abolished in cells lacking CENP-C (Cnp3) (Figure 5C)
PMID:16325576	FYPO:0004212	decreased protein localization to kinetochore during meiosis I	(comment: VW, I am not sure that I captured this correctly?) A ChIP assay revealed that the association of Rec8(TEV) with chromatin is partly, but not entirely, impaired only at the centromeric central core region when cen-TEV protease is coexpressed (Figure 7C), suggesting that Rec8(TEV) is cleaved in a region-specific manner. We reasoned that, even if central core Rec8 is cleaved by cen-TEV protease, newly produced or free Rec8 complexes can be reloaded, resulting in the observed association of low levels of Rec8 at the central core. Nevertheless, such ‘‘turnover’’ of cohesin complexes would eventually abolish cohesion because newly associated cohesins do not reestablish cohesion after DNA replication.
PMID:16325576	PomGeneEx:0000018	protein level increased [during] meiotic prophase I	(comment: induced)
PMID:16325576	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_protein] PomBase:SPBC29A10.14	Surprisingly, moa1D cells displayed slightly stronger signals of Rec8-GFP at the cluster of centromeres (Figure 6A, GFP dots in the nucleus). Subsequent ChIP assays revealed that the association of Rec8 to chromatin increased nearly 2-fold in moa1D cells, particularly at the centromeric central core region (Figure 6B).
PMID:16325576	FYPO:0004314	normal protein localization to CENP-A containing chromatin [assayed_protein] PomBase:SPBC29A10.14	This hypothesis makes the key prediction that the increase of Rec8 at the centromeric central core would depend on DNA replication. To test this possibility, we blocked DNA replication by adding HU to the synchronized meiotic culture and examined by ChIP the localization pattern of Rec8 (Figure 6C). Levels of central core-associated Rec8 were the same before (+HU) or after DNA replication (-HU) in wild-type cells. Remarkably, HU treatment abolished the increase of central core Rec8 in moa1D cells, and the pattern became similar to that in moa1+ cells (Figure 6C, +HU).
PMID:16325576	FYPO:0003178	normal meiotic sister chromatid segregation [has_penetrance] complete	Whereas monopolar attachment is obviously impaired in moa1D rec12D meiosis I, the protection of centromere cohesion also appears defective since almost all sister chromatids eventually separate.
PMID:16325576	FYPO:0004393	lagging chromosomes during meiosis I	Whereas monopolar attachment is obviously impaired in moa1D rec12D meiosis I, the protection of centromere cohesion also appears defective since almost all sister chromatids eventually separate.
PMID:16360688	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] ~10	(Figure 1a)
PMID:16360688	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 25	(Figure 1a)
PMID:16360688	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] ~10	(Figure 1a)
PMID:16360688	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] ~5	(Figure 1a)
PMID:16360688	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] 40	(Figure 1a)
PMID:16360688	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] ~10	(Figure 1a)
PMID:16360688	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] ~22	(Figure 1b)
PMID:16360688	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] ~22	(Figure 1c)
PMID:16360688	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] ~22	(Figure 1c)
PMID:16360688	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] 10	(Figure 1c)
PMID:16360688	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] ~42	(Figure 1c)
PMID:16360688	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] ~37	(Figure 1c)
PMID:16360688	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] ~27	(Figure 1c)
PMID:16360688	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] 10	(Figure 1c) Interestingly, no additive effect was seen in the bub11-179 sgo2D double mutant, indicating that Sgo2 and the kinase domain of Bub1 act in the same pathway (Figure 3A).
PMID:16360688	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] ~25	(Figure 1c) a high frequency of sister-chromatid nondisjunction during MII (Figure 1C), consistent with Sgo1’s being largely nonfunctional in this mutant background.
PMID:16360688	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] ~22	(Figure 3a) Interestingly, no additive effect was seen in the bub11-179 sgo2D double mutant, indicating that Sgo2 and the kinase domain of Bub1 act in the same pathway (Figure 3A).
PMID:16360688	FYPO:0007661	normal protein localization to kinetochore during meiotic metaphase I [assayed_protein] PomBase:SPBP35G2.03c	, Sgo1 is seen as nuclear staining with punctate dots of fluorescence along the spindle (Figure 1D and [2, 9]). This localization is abolished in a bub1D background but preserved in the truncated mutants (Figure 1D), although the signal intensity was variable; in bub11-585, Sgo1 staining was as strong as in the wild-type, but it was weaker in bub11-179 and bub11-826 backgrounds. We conclude that the N terminus of Bub1 is sufficient to promote correct Sgo1 localization and function during MI.
PMID:16360688	FYPO:0007661	normal protein localization to kinetochore during meiotic metaphase I [assayed_protein] PomBase:SPBP35G2.03c	, Sgo1 is seen as nuclear staining with punctate dots of fluorescence along the spindle (Figure 1D and [2, 9]). This localization is abolished in a bub1D background but preserved in the truncated mutants (Figure 1D), although the signal intensity was variable; in bub11-585, Sgo1 staining was as strong as in the wild-type, but it was weaker in bub11-179 and bub11-826 backgrounds. We conclude that the N terminus of Bub1 is sufficient to promote correct Sgo1 localization and function during MI.
PMID:16360688	FYPO:0007688	abolished protein localization to kinetochore during meiotic metaphase I [assayed_protein] PomBase:SPBP35G2.03c	, Sgo1 is seen as nuclear staining with punctate dots of fluorescence along the spindle (Figure 1D and [2, 9]). This localization is abolished in a bub1D background but preserved in the truncated mutants (Figure 1D), although the signal intensity was variable; in bub11-585, Sgo1 staining was as strong as in the wild-type, but it was weaker in bub11-179 and bub11-826 backgrounds. We conclude that the N terminus of Bub1 is sufficient to promote correct Sgo1 localization and function during MI.
PMID:16360688	FYPO:0007661	normal protein localization to kinetochore during meiotic metaphase I [assayed_protein] PomBase:SPBP35G2.03c	, Sgo1 is seen as nuclear staining with punctate dots of fluorescence along the spindle (Figure 1D and [2, 9]). This localization is abolished in a bub1D background but preserved in the truncated mutants (Figure 1D), although the signal intensity was variable; in bub11-585, Sgo1 staining was as strong as in the wild-type, but it was weaker in bub11-179 and bub11-826 backgrounds. We conclude that the N terminus of Bub1 is sufficient to promote correct Sgo1 localization and function during MI.
PMID:16360688	FYPO:0006315	abolished homologous chromosome segregation	As reported previously [13], expression of Rec8RDRD in wild-type cells prevented homolog segregation (no bi-nucleate cells), but homolog segregation was restored to a certain extent by the deletion of rec11 (approximately 40% binucleated cells).
PMID:16360688	FYPO:0004214	normal protein localization to kinetochore during meiosis I [assayed_protein] PomBase:SPCC1322.12c	However, we found that Bub1K762M was properly localized in metaphase I cells and that the amount of protein at centromeres was close to wild-type levels (Figure S1).
PMID:16360688	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] 10	Interestingly, no additive effect was seen in the bub11-179 sgo2D double mutant, indicating that Sgo2 and the kinase domain of Bub1 act in the same pathway (Figure 3A).
PMID:16360688	FYPO:0007688	abolished protein localization to kinetochore during meiotic metaphase I [assayed_protein] PomBase:SPBP35G2.03c	Similarly, we found that Sgo1 was mislocalized in a different allele (Figure 1D, K762M [6])
PMID:16360688	FYPO:0004159	abnormal homologous chromosome segregation [has_penetrance] 60	but homolog segregation was restored to a certain extent by the deletion of rec11 (approximately 40% binucleated cells).
PMID:16394105	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 18	(Fig. 3)
PMID:16394105	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 60	(Fig. 3)
PMID:16394105	FYPO:0005684	increased duration of mitotic prometaphase	(Fig. 4)
PMID:16394105	FYPO:0005706	increased duration of mitotic anaphase B	(Fig. 4)
PMID:16394105	FYPO:0005683	increased duration of mitotic prophase	(Fig. 4)
PMID:16394105	FYPO:0005684	increased duration of mitotic prometaphase	(Fig. 4)
PMID:16394105	FYPO:0005683	increased duration of mitotic prophase	(Fig. 4)
PMID:16394105	FYPO:0005706	increased duration of mitotic anaphase B	(Fig. 4)
PMID:16394105	FYPO:0002061	inviable vegetative cell population	(Fig. 5d)
PMID:16394105	FYPO:0002060	viable vegetative cell population	(Fig. 5e)
PMID:16394105	FYPO:0001357	normal vegetative cell population growth	(Fig. 7a)
PMID:16394105	FYPO:0001357	normal vegetative cell population growth	(Fig. 7a)
PMID:16394105	FYPO:0001234	slow vegetative cell population growth	(Fig. 7b)
PMID:16394105	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Figure 1B)
PMID:16394105	FYPO:0003003	increased protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPCC1322.12c [has_penetrance] 60	(Figure 1B)
PMID:16394105	FYPO:0003003	increased protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPCC1322.12c [has_penetrance] 8	(Figure 1B)
PMID:16394105	FYPO:0003003	increased protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPCC1322.12c [has_penetrance] 4	(Figure 1B)
PMID:16394105	FYPO:0003003	increased protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPCC1322.12c [has_penetrance] 6.2	(Figure 1B)
PMID:16394105	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] >70	(Figure 6B, C)
PMID:16394105	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 7	(Figure 6B, C)
PMID:16394105	FYPO:0003841	decreased protein localization to mitotic spindle midzone [assayed_using] PomBase:SPAC18G6.15	(Figure 8A, B)
PMID:16394105	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC18G6.15	(Figure 8C)
PMID:16394105	FYPO:0002966	normal protein localization to mitotic spindle [assayed_using] PomBase:SPAC18G6.15	(Figure 8D)
PMID:16394105	FYPO:0002966	normal protein localization to mitotic spindle [assayed_using] PomBase:SPAC18G6.15	(Figure 8D)
PMID:16394105	FYPO:0002966	normal protein localization to mitotic spindle [assayed_using] PomBase:SPAC18G6.15	(Figure 8D)
PMID:16394105	FYPO:0005691	decreased spindle pole body-led chromosome movement during mitotic interphase	(Figure 9)
PMID:16394105	FYPO:0000899	normal microtubule cytoskeleton organization during vegetative growth	(comment: morphology)
PMID:16394105	FYPO:0003003	increased protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPCC1322.12c [has_penetrance] 9	Supplemental data
PMID:16394105	FYPO:0002060	viable vegetative cell population	Table 4
PMID:16394105	FYPO:0002060	viable vegetative cell population	Table 4
PMID:16394105	FYPO:0002060	viable vegetative cell population	Table 4
PMID:16394105	FYPO:0002061	inviable vegetative cell population	Table 4
PMID:16394105	FYPO:0002061	inviable vegetative cell population	Table 4
PMID:16394105	FYPO:0005703	decreased rate of microtubule polymerization during vegetative growth	both the growth and shrinkage rates were decreased down to 33 and 60%, respectively
PMID:16394105	FYPO:0000903	decreased rate of microtubule depolymerization during vegetative growth	both the growth and shrinkage rates were decreased down to 33 and 60%, respectively
PMID:16407242	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC428.18	(comment: higher protein level than in absence of HU, in both wild type and mutant)
PMID:16407242	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPAC29B12.03	(comment: higher protein level than in absence of HU, in both wild type and mutant)
PMID:16407242	FYPO:0004189	increased protein level during cellular response to hydroxyurea [assayed_using] PomBase:SPBC428.18	(comment: higher protein level than in absence of HU, in both wild type and mutant)
PMID:16407242	FYPO:0004189	increased protein level during cellular response to hydroxyurea [assayed_using] PomBase:SPAC29B12.03	(comment: higher protein level than in absence of HU, in both wild type and mutant)
PMID:16421249	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Figure 2A The resulting strain, rgf1+, showed a slow growth pattern at 28°C
PMID:16421249	FYPO:0001234	slow vegetative cell population growth [has_severity] low	(Figure 2A The resulting strain, rgf1+, showed a slow growth pattern at 28°C
PMID:16421249	FYPO:0001491	viable vegetative cell [has_penetrance] 55	(Figure 2A)
PMID:16421249	FYPO:0000647	vegetative cell lysis [has_penetrance] 30-45	(Figure 2B) regardless of the growth temperature 30 -35% of the cells were lysed
PMID:16421249	FYPO:0000647	vegetative cell lysis [has_penetrance] 30-35	(Figure 2B) regardless of the growth temperature 30 -35% of the cells were lysed
PMID:16421249	FYPO:0000647	vegetative cell lysis [has_penetrance] 30-35	(Figure 2B) regardless of the growth temperature 30 -35% of the cells were lysed
PMID:16421249	FYPO:0000647	vegetative cell lysis [has_penetrance] 30-35	(Figure 2B) regardless of the growth temperature 30 -35% of the cells were lysed
PMID:16421249	FYPO:0001491	viable vegetative cell [has_penetrance] >90	(Figure 2B) regardless of the growth temperature 30 -35% of the cells were lysed
PMID:16421249	FYPO:0001366	normal actin cytoskeleton organization	(Figure 3A) (comment: at cell division site)
PMID:16421249	FYPO:0001397	monopolar actin cortical patch localization to old end	(Figure 3A) As shown in Figure 3A, the rgf1 mutants showed a defect in actin organization in that they organized actin patches mostly at one end of the cell only
PMID:16421249	FYPO:0003535	decreased bipolar index	(Figure 3B) 55% of cdc10-129 cells displayed bipolar growth, whereas only 4% of cdc10-129 rgf1+ cells were bipolar
PMID:16421249	FYPO:0000079	sensitive to caspofungin	(Figure 4A) the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1+
PMID:16421249	FYPO:0000079	sensitive to caspofungin	(Figure 4A) the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1+
PMID:16421249	FYPO:0000079	sensitive to caspofungin	(Figure 4A) the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1+
PMID:16421249	FYPO:0005152	resistance to caspofungin	(Figure 4A) the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1+
PMID:16421249	FYPO:0000079	sensitive to caspofungin	(Figure 4A) the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1+
PMID:16421249	FYPO:0000079	sensitive to caspofungin	(Figure 4A) the Csp hypersensitivity of the rgf1delta mutant was suppressed by rho1delta in .... None of the other genes was able to suppress the hypersensitivity of rgf1+
PMID:16421249	FYPO:0007436	swollen elongated multiseptate vegetative cell	(Figure 4c) Lack of Rga1p produces small colonies and the cells show a swollen, multiseptated or branched shape; a phenotype similar to that seen in cells in which Rho1p is excessively activated
PMID:16421249	FYPO:0001968	increased 1,3-beta-D-glucan synthase activity	(Figure 6B) GS activity increased during rgf1+ overexpression. This activity was fourfold higher than that observed in the wild-type strain
PMID:16421249	FYPO:0001357	normal vegetative cell population growth	(Figure 7A)
PMID:16421249	FYPO:0001357	normal vegetative cell population growth	(Figure 7A)
PMID:16421249	FYPO:0001357	normal vegetative cell population growth	(Figure 7A)
PMID:16421249	FYPO:0001357	normal vegetative cell population growth	(Figure 7A) only a moderate expression of bgs4+ restored growth of an rgf1+ mutant in the presence of the antifungal agent
PMID:16421249	FYPO:0001357	normal vegetative cell population growth	(Figure 7C)
PMID:16421249	GO:1902716	cell cortex of growing cell tip [exists_during] mitotic interphase	(Figure 8A)
PMID:16421249	GO:0000935	division septum [exists_during] mitotic M phase	(Figure 8A)
PMID:16421249	GO:0140472	cell cortex of non-growing cell tip	(Figure 8A)
PMID:16421249	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	(Figure 8A)
PMID:16421249	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC1F7.04	(comment: decreased gtp-bound gtpase, inactive)
PMID:16421249	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC1F7.04	(comment: increased gtp-bound gtpase, active)
PMID:16421249	GO:0090334	regulation of cell wall (1->3)-beta-D-glucan biosynthetic process	(comment: positive regulation)
PMID:16421249	GO:0030866	cortical actin cytoskeleton organization	(comment: positive regulation)
PMID:16421249	GO:0051523	cell growth mode switching, monopolar to bipolar	(comment: positive regulation)
PMID:16421249	GO:0090334	regulation of cell wall (1->3)-beta-D-glucan biosynthetic process	(comment: positive regulation)
PMID:16421249	FYPO:0002380	viable spheroid vegetative cell [has_severity] low	(comment: rescue of multiseptate, swollen)
PMID:16421249	FYPO:0002060	viable vegetative cell population	DNS
PMID:16421249	FYPO:0001234	slow vegetative cell population growth [has_severity] low	rga1+ cells were severely impaired for growth, whereas rgf1+rga1+ exhibited a better growth pattern and resembled rgf1+ cells. (Figure 4)
PMID:16421249	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPAC1F7.04 [part_of] regulation of cell wall (1->3)-beta-D-glucan biosynthetic process	this being consistent with the idea that rgf1+ could act in the same pathway as rho1+ (Figure 4A). Figure 5. The amount of active Rho1p increased considerably in the strain overexpressing Rgf1p compared with the wild-type strain. Moreover, only a minor amount of GTP-Rho1p was detected in the strain lacking Rgf1p.
PMID:16428309	FYPO:0002689	sensitive to cumene hydroperoxide [has_severity] low	(Fig. 1)
PMID:16428309	FYPO:0000108	sensitive to menadione [has_severity] high	(Fig. 1)
PMID:16428309	FYPO:0002691	normal growth on menadione	(Fig. 1)
PMID:16428309	FYPO:0000108	sensitive to menadione [has_severity] medium	(Fig. 1)
PMID:16428309	FYPO:0002691	normal growth on menadione	(Fig. 1)
PMID:16428309	FYPO:0000108	sensitive to menadione [has_severity] low	(Fig. 1)
PMID:16428309	FYPO:0002691	normal growth on menadione	(Fig. 1)
PMID:16428309	FYPO:0008287	sensitive to 1-chloro-2,4-dinitrobenzene [has_severity] high	(Fig. 1)
PMID:16428309	FYPO:0008287	sensitive to 1-chloro-2,4-dinitrobenzene [has_severity] low	(Fig. 1)
PMID:16428309	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] medium	(Fig. 1)
PMID:16428309	FYPO:0000962	normal growth on hydrogen peroxide	(Fig. 1)
PMID:16428309	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Fig. 1)
PMID:16428309	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] medium	(Fig. 1)
PMID:16428309	FYPO:0002690	normal growth on cumene hydroperoxide	(Fig. 1)
PMID:16428309	FYPO:0008287	sensitive to 1-chloro-2,4-dinitrobenzene [has_severity] medium	(Fig. 2)
PMID:16428309	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] low	(Fig. 2)
PMID:16428309	FYPO:0008287	sensitive to 1-chloro-2,4-dinitrobenzene [has_severity] medium	(Fig. 2)
PMID:16428309	FYPO:0002689	sensitive to cumene hydroperoxide [has_severity] high	(Fig. 2)
PMID:16428309	FYPO:0002689	sensitive to cumene hydroperoxide [has_severity] high	(Fig. 2)
PMID:16428309	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Fig. 2)
PMID:16428309	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Fig. 2)
PMID:16428309	FYPO:0000108	sensitive to menadione [has_severity] high	(Fig. 2)
PMID:16428309	FYPO:0000108	sensitive to menadione [has_severity] medium	(Fig. 2)
PMID:16428435	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC32H8.10	(Fig. 2)
PMID:16428435	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC32H8.10 [assayed_substrate] PomBase:SPAC23C4.19 [has_severity] high	(Fig. 2B)
PMID:16428435	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC32H8.10 [has_severity] high	(Fig. 2C and D)
PMID:16428435	FYPO:0008170	decreased cyclin-dependent protein kinase activity [assayed_protein] PomBase:SPAC23C4.19 [has_severity] high	(Fig. 2D)
PMID:16428435	FYPO:0008170	decreased cyclin-dependent protein kinase activity [assayed_protein] PomBase:SPAC23C4.19 [has_severity] medium	(Fig. 2D)
PMID:16428435	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC32H8.10	(Fig. 3)
PMID:16428435	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC32H8.10 [assayed_substrate] PomBase:SPAC23C4.19 [has_severity] high	(Fig. 3B and C)
PMID:16428435	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4)
PMID:16428435	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4)
PMID:16428435	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 4)
PMID:16428435	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 4)
PMID:16428435	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 4)
PMID:16428435	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4)
PMID:16428435	FYPO:0005369	abolished cell population growth at low temperature	(Fig. 4)
PMID:16428435	FYPO:0005369	abolished cell population growth at low temperature	(Fig. 4)
PMID:16428435	FYPO:0005369	abolished cell population growth at low temperature	(Fig. 4)
PMID:16428435	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 4)
PMID:16428435	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 4)
PMID:16428435	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 4)
PMID:16428435	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	(Fig. 4)
PMID:16428435	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 4)
PMID:16428435	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 4)
PMID:16428435	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 4)
PMID:16428435	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4)
PMID:16428435	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4)
PMID:16428435	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 4)
PMID:16428435	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 4)
PMID:16428435	FYPO:0002061	inviable vegetative cell population	Tetrad analysis revealed a 2:2 segregation of viability, and all viable progeny were G418 sensitive, indicating that cdk9 + is essential (data not shown).
PMID:16428435	FYPO:0002150	inviable spore population	Thus, the carboxyl terminus of Cdk9 [...] is required for cell viability. Table 2
PMID:16453724	FYPO:0003758	mitotic spindle elongation without chromosome separation	(comment: CHECK ABOLISHED SEPARATION)
PMID:16453724	FYPO:0003758	mitotic spindle elongation without chromosome separation	(comment: CHECK ABOLISHED SEPARATION)
PMID:16453724	FYPO:0000608	abnormal cell cycle arrest in mitotic M phase	(comment: with re-replication)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0000674	normal cell population growth at high temperature	(Table 1)
PMID:16453733	FYPO:0000674	normal cell population growth at high temperature	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0000674	normal cell population growth at high temperature	(Table 1)
PMID:16453733	FYPO:0000674	normal cell population growth at high temperature	(Table 1)
PMID:16453733	FYPO:0000674	normal cell population growth at high temperature	(Table 1)
PMID:16453733	FYPO:0000674	normal cell population growth at high temperature	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:16453733	FYPO:0001357	normal vegetative cell population growth	(Table 1)
PMID:1645660	GO:0016791	phosphatase activity	(comment: CHECK inhibited_by zinc(2+) activated_by magnesium(2+))
PMID:16467379	GO:0031097	medial cortex	(comment: localization dependent on F-actin (assayed using Latrunculin A))
PMID:16481403	GO:0036449	microtubule minus-end [exists_during] mitotic interphase	(Fig. 1)
PMID:16481403	FYPO:0006195	decreased number of elongated microtubule bundles curved around cell end	(Fig. 1D) (comment: actually 2 bundles)
PMID:16481403	GO:0008017	microtubule binding	(Fig. 1c)
PMID:16481403	GO:0000923	equatorial microtubule organizing center [exists_during] mitotic telophase	(Figure 5B)
PMID:16481403	GO:0051415	microtubule nucleation by interphase microtubule organizing center	(comment: emtoc)
PMID:16481403	FYPO:0006397	cytoplasmic microtubules detached from nuclear envelope	(comment: from both ends)
PMID:16481403	FYPO:0005558	abnormal microtubule bundle	(comment: from both ends)
PMID:16489217	GO:0010515	negative regulation of induction of conjugation with cellular fusion	(comment: maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.)
PMID:16537923	FYPO:0001357	normal vegetative cell population growth	(comment: CHECK aerobic conditions)
PMID:16537923	FYPO:0003251	decreased transcription from SRE promoter [assayed_using] PomBase:SPAC1687.16c	(comment: genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed)
PMID:16537923	FYPO:0003251	decreased transcription from SRE promoter [assayed_using] PomBase:SPAC222.11	(comment: genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed)
PMID:16537923	FYPO:0003251	decreased transcription from SRE promoter [assayed_using] PomBase:SPAC17A2.05	(comment: genes specified in extensions assayed in low-throughput Northern blots; additional genes assayed in high-throughput microarrays not listed)
PMID:16541024	GO:0000159	protein phosphatase type 2A complex	(Fig. 1)
PMID:16541024	GO:0000159	protein phosphatase type 2A complex	(Fig. 1)
PMID:16541024	GO:0000159	protein phosphatase type 2A complex	(Fig. 2)
PMID:16541024	FYPO:0000678	unequal homologous chromosome segregation [has_penetrance] ~20	(Fig. 2a)
PMID:16541024	FYPO:0002219	normal chromosome disjunction at meiosis I	(Fig. 2a)
PMID:16541024	FYPO:0002219	normal chromosome disjunction at meiosis I	(Fig. 2a)
PMID:16541024	FYPO:0002219	normal chromosome disjunction at meiosis I	(Fig. 2a)
PMID:16541024	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPCC188.02	(Fig. 2b)
PMID:16541024	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] ~50	(Fig. 2b)
PMID:16541024	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] ~50	(Fig. 2b)
PMID:16541024	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] ~18	(Fig. 2b)
PMID:16541024	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] ~18	(Fig. 2b)
PMID:16541024	FYPO:0000460	decreased mitotic centromeric sister chromatid cohesion [has_penetrance] 80-90	(Fig. 2b)
PMID:16541024	FYPO:0000460	decreased mitotic centromeric sister chromatid cohesion [has_penetrance] 80-90	(Fig. 2b)
PMID:16541024	FYPO:0000460	decreased mitotic centromeric sister chromatid cohesion [has_penetrance] 80-90	(Fig. 2b)
PMID:16541024	FYPO:0007661	normal protein localization to kinetochore during meiotic metaphase I [assayed_using] PomBase:SPBP35G2.03c	(Fig. 4)
PMID:16541024	FYPO:0007688	abolished protein localization to kinetochore during meiotic metaphase I [assayed_using] PomBase:SPBP35G2.03c	(Fig. 4)
PMID:16541024	FYPO:0007661	normal protein localization to kinetochore during meiotic metaphase I [assayed_using] PomBase:SPBP35G2.03c	(Fig. 4)
PMID:16541024	GO:0000775	chromosome, centromeric region [exists_during] meiotic anaphase I	(Fig. 4b)
PMID:16541024	GO:0000775	chromosome, centromeric region [exists_during] meiotic anaphase I	(Fig. 4b)
PMID:16541024	GO:0000775	chromosome, centromeric region [exists_during] meiotic anaphase I	(Fig. 4b)
PMID:16541024	GO:0000775	chromosome, centromeric region [exists_during] meiotic anaphase I	(Fig. 4b)
PMID:16541024	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPBC16H5.07c [has_input] PomBase:SPCC188.02 [has_input] PomBase:SPAP8A3.09c [part_of] meiotic centromeric cohesion protection in anaphase I [occurs_in] inner kinetochore [happens_during] meiotic anaphase I	(comment: Notably, we detected only a single combination of PP2A subunits associated with SpSgo1, namely SpPaa1A-SpPar1B′-SpPpa2C)
PMID:16541024	GO:0004722	protein serine/threonine phosphatase activity [has_input] PomBase:SPBC29A10.14 [part_of] meiotic centromeric cohesion protection in anaphase I [happens_during] meiotic anaphase I	(comment: this is an inference, but almost certainly true based on the genetics)
PMID:16541024	FYPO:0003176	normal meiotic chromosome segregation [has_penetrance] high	Supplementary Fig. S2a
PMID:16541024	FYPO:0003176	normal meiotic chromosome segregation	Supplementary Fig. S2a
PMID:16541024	FYPO:0003176	normal meiotic chromosome segregation	Supplementary Fig. S2a
PMID:16541024	FYPO:0003176	normal meiotic chromosome segregation [has_penetrance] medium	Supplementary Fig. S2a
PMID:16541024	FYPO:0003176	normal meiotic chromosome segregation	Supplementary Fig. S2a
PMID:16541025	GO:0005515	protein binding [part_of] meiotic centromeric cohesion protection in anaphase I [occurs_in] condensed chromosome, centromeric region [happens_during] meiotic anaphase I	(Fig. 5a)
PMID:16541025	GO:0005515	protein binding [part_of] meiotic centromeric cohesion protection in anaphase I [occurs_in] condensed chromosome, centromeric region [happens_during] meiotic anaphase I	(Fig. 5a)
PMID:16541025	GO:0000939	inner kinetochore [exists_during] meiosis I cell cycle phase	(Fig. 5b) (comment: CHECK however, it colocalizes with Sgo1 at centromeres during meiosis I)
PMID:16541025	FYPO:0004763	abolished protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPCC188.02	(Fig. 5b).
PMID:16541025	FYPO:0003182	sister chromatid nondisjunction at meiosis II	(Supplementary Fig. 7)
PMID:16541025	FYPO:0003182	sister chromatid nondisjunction at meiosis II	(Supplementary Fig. 7)
PMID:16541025	FYPO:0005648	sister kinetochore dissociation in meiotic metaphase I	(Supplementary Fig. 7).
PMID:16541025	FYPO:0005648	sister kinetochore dissociation in meiotic metaphase I	(Supplementary Fig. 7)...both of these mutant cell types showed precocious centromeric dissociation after meiosis I, and random chromosome segregation following meiosis II
PMID:16541025	FYPO:0004214	normal protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPBP35G2.03c	(comment: dns)
PMID:16541025	FYPO:0004763	abolished protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPBC29A10.14	We found that, like sgo1D cells, par1D cells mostly lost centromeric Rec8 localization at this stage (Fig. 5d)
PMID:1655416	MOD:00047	O-phospho-L-threonine [present_during] mitotic S phase	(Figure 10C)
PMID:1655416	MOD:00048	O4'-phospho-L-tyrosine [present_during] mitotic S phase	(Figure 10C)
PMID:1655416	GO:0005515	protein binding	(comment: CHECK ADD MODIFIED FORMS)
PMID:1655416	FYPO:0000333	mitotic G1/S phase transition delay	(comment: is delayed but the delay is reduced compared to the single mutant)
PMID:1655416	FYPO:0002176	viable vegetative cell with normal cell size [has_penetrance] complete	(comment: length)
PMID:1655416	FYPO:0000333	mitotic G1/S phase transition delay	(comment: transient)
PMID:1657594	GO:0004862	cAMP-dependent protein kinase inhibitor activity [has_input] PomBase:SPBC106.10	(Fig. 6)
PMID:1657594	GO:0030552	cAMP binding	(Fig. 6)
PMID:16585273	FYPO:0000927	abolished horsetail movement	(Fig. 4E)
PMID:16611237	FYPO:0001837	increased duration of protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC582.03	(comment: indicates a G2 delay)
PMID:16618806	FYPO:0006440	abolished protein kinase activity during cellular response to hydroxyurea [assayed_enzyme] PomBase:SPCC18B5.11c	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	FYPO:0006440	abolished protein kinase activity during cellular response to hydroxyurea [assayed_enzyme] PomBase:SPCC18B5.11c	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	FYPO:0006440	abolished protein kinase activity during cellular response to hydroxyurea [assayed_enzyme] PomBase:SPCC18B5.11c	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	FYPO:0006440	abolished protein kinase activity during cellular response to hydroxyurea [assayed_enzyme] PomBase:SPCC18B5.11c	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	FYPO:0006440	abolished protein kinase activity during cellular response to hydroxyurea [assayed_enzyme] PomBase:SPCC18B5.11c	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	FYPO:0002097	decreased protein kinase activity during cellular response to hydroxyurea [assayed_enzyme] PomBase:SPCC18B5.11c	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	FYPO:0002700	increased protein kinase activity [assayed_enzyme] PomBase:SPCC18B5.11c	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	FYPO:0002700	increased protein kinase activity [assayed_enzyme] PomBase:SPCC18B5.11c	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	FYPO:0002700	increased protein kinase activity [assayed_enzyme] PomBase:SPCC18B5.11c	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	FYPO:0002700	increased protein kinase activity [assayed_enzyme] PomBase:SPCC18B5.11c	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	FYPO:0006440	abolished protein kinase activity during cellular response to hydroxyurea [assayed_enzyme] PomBase:SPCC18B5.11c	(comment: CHECK assayed substrate myelin basic protein)
PMID:16618806	FYPO:0001384	abolished protein kinase activity [assayed_enzyme] PomBase:SPCC18B5.11c [assayed_substrate] PomBase:SPCC18B5.11c	(comment: CHECK effect of mutation in substrate Cds1 molecule)
PMID:16618806	FYPO:0003020	abolished protein autophosphorylation during vegetative growth [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK effect of mutation in substrate Cds1 molecule)
PMID:16618806	FYPO:0006440	abolished protein kinase activity during cellular response to hydroxyurea [assayed_enzyme] PomBase:SPCC18B5.11c [assayed_substrate] PomBase:SPCC18B5.11c	(comment: CHECK effect of mutation in substrate Cds1 molecule)
PMID:16618806	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC18B5.11c	(comment: CHECK has output PR:000037300)
PMID:16618806	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [has_severity] low [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:16618806	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:16618806	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [has_severity] low [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:16618806	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [has_severity] medium [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:16618806	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [has_severity] high [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:16618806	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [has_severity] low [assayed_using] PomBase:SPCC18B5.11c	(comment: CHECK residue T11)
PMID:16618806	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC18B5.11c [assayed_using] PomBase:SPCC18B5.11c	(comment: abolished dimerization in kinase-dead cds1-D312E)
PMID:16618806	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(comment: cells otherwise haploid)
PMID:16618806	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(comment: cells otherwise haploid)
PMID:16618806	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(comment: cells otherwise haploid)
PMID:16618806	FYPO:0003077	increased protein autophosphorylation during vegetative growth [assayed_using] PomBase:SPCC18B5.11c	(comment: induced dimerization increases Cds1 autophosphorylation without prior phosphorylation on T11)
PMID:16624923	GO:0106006	cytoskeletal protein-membrane anchor activity [has_input] PomBase:SPAC1093.06c [part_of] horsetail-astral microtubule organization [occurs_at] medial membrane band	(comment: CHECK membrane anchor)
PMID:16624923	FYPO:0007168	abolished microtubule attachment to cell cortex	cortical location/microtubules did not show a lateral interaction with the cell corte/Ninety-two percent of microtubules in num1D cells underwent catastrophe Figure 3.—Nuclear behavior in wild-type and num1D zygotes. Chromosomal DNA in zygotes (JY450 or JV627) was stained with Hoechst 33342 and monitored. The numbers on the left indicate time in minutes. Microtubules were visualized simultaneously by GFP-tagged a-tubulin. Stained DNA is shown in red, and GFP fluorescence in green. Bar, 5 mm. within 2 min of contacting the cell cortex (n 1⁄4 59). In contrast, 80% of microtubules that interacted with the cell cortex laterally in wild-type cells remained at the cell ends for .2 min (n 1⁄4 15).
PMID:16682348	FYPO:0005386	decreased protein localization to chromatin at chromosome arms [assayed_using] PomBase:SPAC10F6.09c	(comment: CHECK add background G1 arrested cells)
PMID:16682348	FYPO:0005386	decreased protein localization to chromatin at chromosome arms [assayed_using] PomBase:SPCC338.17c	(comment: CHECK- add background? G1 arrested cells)
PMID:16682348	FYPO:0001514	decreased protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPAC31A2.05c	Reminiscent to this, we found that the localization of Mis4 was disrupted in ssl3-29 cells at the restrictive temperature and that Mis4 overexpression suppressed the thermosensitive growth defect of ssl3-29 cells (Figure 2).
PMID:16687577	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAP8A3.08	(Fig. 1)
PMID:16687577	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAP8A3.08	(Fig. 1)
PMID:16687577	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAP8A3.08	(Fig. 1)
PMID:16687577	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC926.03	(Fig. 2)
PMID:16687577	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC11C11.04c [has_penetrance] 85	(Fig. 2)
PMID:16687577	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic metaphase	(Fig. 3)
PMID:16687577	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC1F5.04c [has_penetrance] 78	(Fig. 3)
PMID:16687577	FYPO:0002026	actomyosin contractile ring displaced from midpoint	(Fig. 4)
PMID:16687577	FYPO:0001009	abolished actomyosin contractile ring assembly [has_penetrance] 73	(Fig. 4)
PMID:16687577	FYPO:0002998	abolished actomyosin contractile ring assembly, clumped medial cortical nodes [has_penetrance] complete	(Fig. 4)
PMID:16687577	FYPO:0001009	abolished actomyosin contractile ring assembly [has_penetrance] 50	(Fig. 5)
PMID:16687577	FYPO:0001368	normal actomyosin contractile ring assembly [has_penetrance] 50	(Fig. 5)
PMID:16687577	FYPO:0001009	abolished actomyosin contractile ring assembly [has_penetrance] complete	(Fig. 5) (comment: during ectopic SIN activation)
PMID:16687577	FYPO:0001009	abolished actomyosin contractile ring assembly [has_penetrance] 98.5	(Figure 5, D and E)
PMID:16687577	FYPO:0001009	abolished actomyosin contractile ring assembly [has_penetrance] 58	(Figure 5, D and E)
PMID:16687577	FYPO:0002967	normal protein localization to mitotic spindle pole body [has_penetrance] 98.5	(Figure 6) (comment: asymetric during cytokinesis delay)
PMID:16687577	FYPO:0004357	decreased protein phosphorylation during mitosis [assayed_using] PomBase:SPAC20G8.05c	(Figure 7)
PMID:16687577	GO:1903475	mitotic actomyosin contractile ring assembly	(comment: different pathway)
PMID:16687577	GO:1903475	mitotic actomyosin contractile ring assembly	(comment: different pathway)
PMID:16738311	FYPO:0002928	normal poly(A) tail length	(comment: CHECK centromere outer repeat transcripts)
PMID:16738311	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 26 °C)
PMID:16738311	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 26 °C)
PMID:16738311	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: CONDITION 32 °C)
PMID:16738311	FYPO:0001355	decreased vegetative cell population growth	(comment: CONDITION 32 °C)
PMID:16738311	FYPO:0001355	decreased vegetative cell population growth	(comment: CONDITION 32 °C)
PMID:16738311	FYPO:0001355	decreased vegetative cell population growth	(comment: CONDITION 32 °C)
PMID:16738311	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: CONDITION 32 °C)
PMID:16738311	FYPO:0001355	decreased vegetative cell population growth	(comment: CONDITION 32 °C)
PMID:16738311	FYPO:0001357	normal vegetative cell population growth	(comment: CONDITION 32 °C)
PMID:16738311	FYPO:0001355	decreased vegetative cell population growth	(comment: CONDITION 32 °C;) better than without cid12delta
PMID:16738311	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: CONDITION 32 °C;) same as without cid12delta
PMID:16738311	FYPO:0001355	decreased vegetative cell population growth	(comment: CONDITION 32 °C;) very slightly worse than without cid12delta
PMID:16762840	FYPO:0006373	increased histone H3-K9 dimethylation at heterochromatin island during vegetative growth	A similar increase in H3K9me2 levels was also observed in swi6 mutant cells defective in Epe1 recruitment to meiotic genes (Figure 6E).
PMID:16762840	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC622.16c [assayed_protein] PomBase:SPAC664.01c	ChIP analysis showed that mutant protein is recruited to heterochromatic loci (Figure 6B), consistent with data showing that Y307A mutation has no effect on Epe1 interaction with Swi6 in vitro (Figure 3D)
PMID:16762840	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPBC28F2.12 [has_severity] high	Deletion of clr3 results in a dramatic increase in Pol II occupancy at cenH element within silent mat domain.
PMID:16762840	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] low	However, abundant transcripts corresponding to centromeric repeats and cenH are detectable in RNAi- defective Dago1 cells. We found that the levels of transcripts in Depe1Dago1 double mutant cells were significantly reduced (Figures 5A and 5B), indicating that Epe1 facilitates transcription of the heterochromatic repeats.
PMID:16762840	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] low	However, abundant transcripts corresponding to centromeric repeats and cenH are detectable in RNAi- defective Dago1 cells. We found that the levels of transcripts in Depe1Dago1 double mutant cells were significantly reduced (Figures 5A and 5B), indicating that Epe1 facilitates transcription of the heterochromatic repeats.
PMID:16762840	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	However, abundant transcripts corresponding to centromeric repeats and cenH are detectable in RNAi- defective Dago1 cells. We found that the levels of transcripts in Depe1Dago1 double mutant cells were significantly reduced (Figures 5A and 5B), indicating that Epe1 facilitates transcription of the heterochromatic repeats.
PMID:16762840	FYPO:0001132	abolished protein localization to heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC622.16c	In swi6 mutant background, Epe1-GFP was no longer localized to discrete spots at the nuclear periphery (Figure 3A).
PMID:16762840	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	Indeed, in a situation wherein heterochromatin has been completely abolished, such as in a Dclr4 background, loss of Epe1 had no detectable effect on transcript levels (Figure 5D).
PMID:16762840	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	Indeed, in a situation wherein heterochromatin has been completely abolished, such as in a Dclr4 background, loss of Epe1 had no detectable effect on transcript levels (Figure 5D).
PMID:16762840	FYPO:0000862	normal histone H3-K9 dimethylation at centromere during vegetative growth	Indeed, we found that loss of H3K9me2 in cells overexpressing Epe1 is dependent upon Swi6 (Figure 6D).
PMID:16762840	GO:0000792	heterochromatin	Localization of Epe1-GFP revealed two to three discrete foci at the nuclear periphery (Figure S1 available in the Supplemental Data with this article online), in a pattern that is similar to those of proteins associated with heterochromatin such as Swi6 (Ekwall et al., 1995).
PMID:16762840	FYPO:0005396	abolished protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPCC622.16c	Moreover, ChIP analysis revealed that mutation in Swi6 or an H3K9-specific methyltransferase Clr4 abolished Epe1 localization at centromeres, telomeres, and the mat locus, concurrent with loss of Swi6 at these loci (Figure 3B)
PMID:16762840	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPCC622.16c	Moreover, ChIP analysis revealed that mutation in Swi6 or an H3K9-specific methyltransferase Clr4 abolished Epe1 localization at centromeres, telomeres, and the mat locus, concurrent with loss of Swi6 at these loci (Figure 3B)
PMID:16762840	FYPO:0003074	abolished protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC622.16c	Moreover, ChIP analysis revealed that mutation in Swi6 or an H3K9-specific methyltransferase Clr4 abolished Epe1 localization at centromeres, telomeres, and the mat locus, concurrent with loss of Swi6 at these loci (Figure 3B)
PMID:16762840	GO:1990342	heterochromatin island [coincident_with] PomBase:SPBC32H8.11	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	GO:1990342	heterochromatin island [coincident_with] PomBase:SPAC27D7.13c	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	GO:1990342	heterochromatin island [coincident_with] PomBase:SPAC3H8.10	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	GO:1990342	heterochromatin island [coincident_with] PomBase:SPBC24C6.09c	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	GO:1990342	heterochromatin island [coincident_with] PomBase:SPCC18B5.01c	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	GO:1990342	heterochromatin island [coincident_with] PomBase:SPAC13A11.03	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	GO:1990342	heterochromatin island [coincident_with] PomBase:SPCC330.05c	Moreover, Epe1 was detected at certain meiotic genes, some of which are coated with heterochromatic markers (Figure 2A; [Cam et al., 2005]).
PMID:16762840	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] low	Our analysis revealed that Epe1 is required for the increase in transcription of repeats in Dclr3 background, as suggested by the dramatic reduction in transcript levels in Depe1 Dclr3 double mutant compared to Dclr3 single mutant (Figures 5A and 5B).
PMID:16762840	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] low	Our analysis revealed that Epe1 is required for the increase in transcription of repeats in Dclr3 background, as suggested by the dramatic reduction in transcript levels in Depe1 Dclr3 double mutant compared to Dclr3 single mutant (Figures 5A and 5B).
PMID:16762840	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	Our analysis revealed that Epe1 is required for the increase in transcription of repeats in Dclr3 background, as suggested by the dramatic reduction in transcript levels in Depe1 Dclr3 double mutant compared to Dclr3 single mutant (Figures 5A and 5B).
PMID:16762840	FYPO:0008154	normal protein localization to centromeric heterochromatin [assayed_protein] PomBase:SPBC28F2.12	Remarkably, loss of Epe1 resulted in a diminished access of Pol II to cenH in Dclr3 cells, as indicated by substantial reduction in Pol II levels in Depe1 Dclr3 double mutant as compared to Dclr3 single mutant (Figure 5E).
PMID:16762840	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth	Remarkably, loss of Epe1 resulted in a diminished access of Pol II to cenH in Dclr3 cells, as indicated by substantial reduction in Pol II levels in Depe1 Dclr3 double mutant as compared to Dclr3 single mutant (Figure 5E). These results suggest that Epe1 has an important role in promoting access of transcriptional machinery to heterochromatic sequences, thereby facilitating transcription of repeat elements. Therefore, the balance of activities between Clr3 and Epe1, both of which are recruited by Swi6, seems critical in determining the transcriptional state of repeat elements.
PMID:16762840	FYPO:0002335	normal chromatin silencing	The Y307 mutation abolished the ability of Epe1 to destabilize heterochromatic silencing (Figure 6A).
PMID:16762840	FYPO:0006373	increased histone H3-K9 dimethylation at heterochromatin island during vegetative growth	We also tested the effect of Epe1 on heterochromatic markers at meiotic genes. Interestingly, loss of Epe1 resulted in considerable increase in H3K9me2 and H3K9me3 levels, concomitant with moderate increase in Swi6 binding at the ssm4 gene (Figures 6E and 6F).
PMID:16762840	FYPO:0002335	normal chromatin silencing	We found that loss of Epe1 restores Swi6 localization and silencing in Dago1 and Dclr3 mutants to levels comparable to wild-type cells (Figure 5C and Figure S3)
PMID:16762840	FYPO:0002335	normal chromatin silencing	We found that loss of Epe1 restores Swi6 localization and silencing in Dago1 and Dclr3 mutants to levels comparable to wild-type cells (Figure 5C and Figure S3)
PMID:16762840	FYPO:0007953	increased spatial extent of heterochromatin assembly [assayed_region] boundary_element	We next investigated the possible involvement of Epe1 in boundary function of the IRC elements. Remarkably, deletion of epe1 resulted in spreading of Swi6 and H3K9me into euchromatic regions surrounding cen1 (Figure 7D).
PMID:16762840	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPCC622.16c	a glutathione S-transferase (GST) pull-down assay showed that in vitro-translated Epe1 directly binds to GST-Swi6, but not GST alone (Figure 3D). This interaction is not affected by a mutation in JmjC domain of Epe1 (Y307A) that impairs Epe1 function. Based on these analyses, Swi6-mediated recruitment of Epe1 might involve direct interaction between these factors. ChIP analysis revealed that mutations in swi6 or clr4 resulted in loss of Epe1 from mcp5, mcp7, mei4, and ssm4, and from the LC region (Figures 4A and 4B), suggesting Swi6 facilitated recruitment of Epe1 to these loci.
PMID:16762840	GO:0031934	mating-type region heterochromatin	heterochromatic loci, including centromeres, telomeres, and the mat locus (Figure 2A).
PMID:16762840	GO:0005721	pericentric heterochromatin	heterochromatic loci, including centromeres, telomeres, and the mat locus (Figure 2A).
PMID:16762840	GO:0140720	subtelomeric heterochromatin	heterochromatic loci, including centromeres, telomeres, and the mat locus (Figure 2A).
PMID:16775007	GO:0044732	mitotic spindle pole body	(Fig. 1A)
PMID:16775007	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC244.01c [assayed_using] PomBase:SPAC4H3.11c	(Fig. 2A)
PMID:16775007	GO:0005515	protein binding	(Fig. 2A)
PMID:16775007	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell [has_penetrance] 6	(Fig. 5D)
PMID:16775007	GO:0005515	protein binding	(Figure 4C)
PMID:16775007	FYPO:0002061	inviable vegetative cell population	(Figure 5, A and B)
PMID:16775007	FYPO:0002061	inviable vegetative cell population	(Figure 7A)
PMID:16787941	GO:0035974	meiotic spindle pole body [exists_during] meiosis I cell cycle phase	(Fig. 1A)
PMID:16787941	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Fig. 1A)
PMID:16787941	GO:0035974	meiotic spindle pole body [exists_during] meiosis I cell cycle phase	(Fig. 1B)
PMID:16787941	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Fig. 1B)
PMID:16787941	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Fig. 1C)
PMID:16787941	GO:0035974	meiotic spindle pole body [exists_during] meiosis I cell cycle phase	(Fig. 1C)
PMID:16787941	GO:0035974	meiotic spindle pole body [exists_during] meiosis I cell cycle phase	(Fig. 1D)
PMID:16787941	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Fig. 1E)
PMID:16787941	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Fig. 1F)
PMID:16787941	GO:0035974	meiotic spindle pole body [exists_during] meiosis I cell cycle phase	(Fig. 1G)
PMID:16787941	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Fig. 1G)
PMID:16787941	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Fig. 1H)
PMID:16787941	GO:0035974	meiotic spindle pole body [exists_during] meiosis I cell cycle phase	(Fig. 1H)
PMID:16787941	FYPO:0000586	abolished ascospore wall assembly [has_penetrance] 90	(Fig. 2C)
PMID:16787941	FYPO:0000586	abolished ascospore wall assembly [has_penetrance] 30	(Fig. 2C)
PMID:16787941	FYPO:0000586	abolished ascospore wall assembly [has_penetrance] 80	(Fig. 2C)
PMID:16787941	FYPO:0000586	abolished ascospore wall assembly [has_penetrance] 60	(Fig. 2C)
PMID:16787941	FYPO:0000586	abolished ascospore wall assembly [has_penetrance] 95	(Fig. 2C)
PMID:16787941	FYPO:0000586	abolished ascospore wall assembly [has_penetrance] 30	(Fig. 2C)
PMID:16787941	FYPO:0002708	abolished prospore formation	(Fig. 3, Fig. 6)
PMID:16787941	FYPO:0000478	normal meiosis	(Fig. 3B, 3C, Fig. 4, Fig. 5)
PMID:16787941	FYPO:0007246	abolished protein localization to meiotic spindle pole body during anaphase II [assayed_protein] PomBase:SPBC21.06c	(Fig. 7A)
PMID:16787941	FYPO:0007246	abolished protein localization to meiotic spindle pole body during anaphase II [assayed_protein] PomBase:SPAC9G1.09	(Fig. 7A)
PMID:16787941	FYPO:0008402	septum assembly during meiosis I	(Fig. 8)
PMID:16787941	FYPO:0000478	normal meiosis	(Fig. 8B)
PMID:16787941	FYPO:0000478	normal meiosis	(Fig. 8B)
PMID:16822282	FYPO:0002143	decreased cellular reactive oxygen species level in stationary phase	(Fig. 3A)
PMID:16822282	FYPO:0002143	decreased cellular reactive oxygen species level in stationary phase	(Fig. 3A)
PMID:16822282	FYPO:0001309	increased viability in stationary phase	(Fig. 3A)
PMID:16822282	FYPO:0001310	normal viability in stationary phase	(Fig. 3A)
PMID:16822282	FYPO:0002143	decreased cellular reactive oxygen species level in stationary phase	(Fig. 3A)
PMID:16822282	FYPO:0001309	increased viability in stationary phase	(Fig. 3A)
PMID:16822282	FYPO:0001310	normal viability in stationary phase	(Fig. 3A)
PMID:16822282	FYPO:0004129	increased cysteine-type peptidase activity	(comment: caspase)
PMID:16822282	FYPO:0004129	increased cysteine-type peptidase activity	(comment: caspase)
PMID:16822282	FYPO:0004129	increased cysteine-type peptidase activity [has_severity] high	(comment: caspase)
PMID:16823445	GO:0140311	protein sequestering activity [has_input] PomBase:SPCC736.12c [occurs_in] Mei2 nuclear dot complex [happens_during] single-celled organism vegetative growth phase [part_of] positive regulation of nuclear mRNA surveillance of meiosis-specific transcripts	We propose that Mei2 turns off the DSR-Mmi1 system by sequestering Mmi1 to the dot and thereby secures stable expression of meiosis-specific transcripts (Abstract).
PMID:16824200	GO:1990023	mitotic spindle midzone [exists_during] mitotic anaphase B	(comment: requires intact mitotic spindle, as shown by cold-depolymerizing microtubules and nda3 mad2 double mutant phenotype)
PMID:16857197	FYPO:0002521	decreased frequency of conjugation with h- cells [has_severity] high	(comment: CHECK might be abolished. Sometimes you see diploidization.)
PMID:16914721	FYPO:0003917	decreased nonsense-mediated decay	(comment: assayed using ade6-M26)
PMID:16914721	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC29B5.01	(comment: microarray data shows 111 genes affected)
PMID:16914721	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC21E11.03c	(comment: microarray data shows 111 genes affected)
PMID:16914721	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC32F12.03c	(comment: microarray data shows 111 genes affected)
PMID:16914721	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPCC757.07c	(comment: microarray data shows 111 genes affected)
PMID:16914721	GO:0000184	nuclear-transcribed mRNA catabolic process, nonsense-mediated decay	These findings showed that Upf1 is required for degradation of the ade6-M26 mRNA in S. pombe.
PMID:16916637	PomGeneEx:0000014	RNA present [during] mitotic G1 phase	Analysis of nrm1+ transcript abundance in temperature-sensitive cdc25-22 cells arrested in G2/M and, subsequently, released into the cell cycle revealed that nrm1+, like the well-established G1-specific targetscdc18+ and ste9+, is a G1-specific transcript (Figure 6D).
PMID:16916637	GO:0003714	transcription corepressor activity [happens_during] mitotic M phase [has_input] PomBase:SPBC336.12c [part_of] negative regulation of transcription by RNA polymerase II	elevated levels of these MBF-dependent transcripts throughout the cell cycle (cdc22+, Figure 6F; cdc18+ and ste9+, data not shown). We conclude that SpNrm1 is essential for repression of MBF-regulated genes outside of the G1 phase and that both Res2 and the SpNrm1 are required for periodic expression of G1-specific transcripts. I
PMID:16916637	GO:0003714	transcription corepressor activity [happens_during] mitotic S phase [has_input] PomBase:SPBC336.12c [part_of] negative regulation of transcription by RNA polymerase II	nrm1D mutants exhibited elevated levels of these MBF-dependent transcripts throughout the cell cycle (cdc22+ , Figure 6F; cdc18+ and ste9+, data not shown). We conclude that SpNrm1 is essential for repression of MBF-regulated genes outside of the G1 phase and that both Res2 and the SpNrm1 are required for periodic expression of G1-specific transcripts. I
PMID:16916637	GO:0003714	transcription corepressor activity [happens_during] mitotic G2 phase [has_input] PomBase:SPBC336.12c [part_of] negative regulation of transcription by RNA polymerase II	nrm1D mutants exhibited elevated levels of these MBF-dependent transcripts throughout the cell cycle (cdc22+, Figure 6F; cdc18+ and ste9+, data not shown). We conclude that SpNrm1 is essential for repression of MBF-regulated genes outside of the G1 phase and that both Res2 and the SpNrm1 are required for periodic expression of G1-specific transcripts. I
PMID:16920624	FYPO:0000964	normal growth on thiabendazole	(Fig. 6)
PMID:16920624	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPCC736.14	(Figure 1B)
PMID:16920624	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPCC736.14	(Figure 1B)
PMID:16920624	MOD:00046	O-phospho-L-serine [added_during] mitotic M phase [removed_during] mitotic anaphase [added_by] PomBase:SPBC11B10.09	(Figure 1C)
PMID:16920624	FYPO:0002141	normal cell population growth at low temperature	(Figure 2A)
PMID:16920624	FYPO:0002141	normal cell population growth at low temperature	(Figure 2A)
PMID:16920624	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Figure 2B)
PMID:16920624	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Figure 2B)
PMID:16920624	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Figure 2B)
PMID:16920624	FYPO:0000964	normal growth on thiabendazole	(Figure 2B) The sensitivities of Dis1N3A and Dis1C3A were similar to that of the wild-type.
PMID:16920624	FYPO:0000964	normal growth on thiabendazole	(Figure 2B) The sensitivities of Dis1N3A and Dis1C3A were similar to that of the wild-type.
PMID:16920624	FYPO:0001839	normal minichromosome loss	(Figure 2C) .... whereas Dis1N3A and Dis1C3A had loss rates that were comparable to those of the wild-type Dis1 integrant.
PMID:16920624	FYPO:0001839	normal minichromosome loss	(Figure 2C) .... whereas Dis1N3A and Dis1C3A had loss rates that were comparable to those of the wild-type Dis1 integrant.
PMID:16920624	FYPO:0001861	increased minichromosome loss upon segregation during vegetative growth [has_penetrance] low	(Figure 2C) The loss rate in Dis16E was lower than Dis16A and slightly higher than that in the wild-type. (The Dis16E mutant appears to mimic at least partially the Cdc2-phosphorylated form of Dis1)
PMID:16920624	FYPO:0001861	increased minichromosome loss upon segregation during vegetative growth [has_penetrance] high	(Figure 2C) The loss rate of CN2 minichromosome in Dis16A was much higher than that of the wild-type integrant...
PMID:16920624	FYPO:0001357	normal vegetative cell population growth	(Figure 2D) However, the double mutant mis12 Dis16E could form colonies at 33ΔC.
PMID:16920624	FYPO:0002061	inviable vegetative cell population	(Figure 2D) The double mutant mis12 Dis16A failed to produce colonies at 33
PMID:16920624	FYPO:0001355	decreased vegetative cell population growth	(Figure 2D) whereas mis12 Dis1N3A and mis12 Dis1C3A showed weak inhibition of colony formation
PMID:16920624	FYPO:0001355	decreased vegetative cell population growth	(Figure 2D) whereas mis12 Dis1N3A and mis12 Dis1C3A showed weak inhibition of colony formation
PMID:16920624	GO:0000776	kinetochore [exists_during] mitotic metaphase	(comment: CHECK PHOSPHORYLATED.) Fig3A The Dis1WT-GFP signals are seen as the kinetochore dots in metaphase. AND 4b
PMID:16920624	GO:0072686	mitotic spindle [exists_during] mitotic anaphase	(comment: CHECK UNPHOSPHORYLATED.) In anaphase, Dis1WT-GFP signals abruptly increased along the spindle and at the SPBs despite being absent from the central zone.
PMID:16920624	FYPO:0007244	decreased protein localization to kinetochore during mitotic metaphase [has_penetrance] 99.2 [assayed_using] PomBase:SPCC736.14	(comment: CHECK protein localized to spindle (also a child of mislocalized protein))
PMID:16920624	GO:0044732	mitotic spindle pole body [exists_during] mitotic anaphase	Because Dis1WT, Dis16A, and Dis16E all associated with anaphase SPBs, this association was independent of modification of the molecule on the Cdc2 phosphorylation sites.
PMID:16920624	FYPO:0001978	bent mitotic spindle [has_penetrance] 43	Curiously, bent spindles were observed in late anaphase of 53 of 121 Dis16A cells in movies, whereas only 18 of 104 Dis1WT and ten of 127 Dis16E cells examined showed the bent spindle (Figure S1D).
PMID:16920624	FYPO:0002061	inviable vegetative cell population	In contrast, the Dis16E mutant, which shows the synthetic lethality with Dmtc1, diminished signals along the metaphase spindle. Thus, there is a correlation between the affinity for microtubules of the mutant versions of Dis1 and these mutants’ ability to rescue the Dmtc1 defect.
PMID:16920624	FYPO:0004310	normal duration of mitotic M phase	Measurements of the durations of phase 1 (prophase to metaphase), 2 (metaphase to anaphase), and 3 (anaphase B) on each of the 30 movies of Dis1WT, Dis16A, and Dis16E strains indicated that the timing of mitosis did not seem to be affected by any mutations because measured differences were within the boundaries of experimental error (Figure S1C)
PMID:16920624	FYPO:0004310	normal duration of mitotic M phase	Measurements of the durations of phase 1 (prophase to metaphase), 2 (metaphase to anaphase), and 3 (anaphase B) on each of the 30 movies of Dis1WT, Dis16A, and Dis16E strains indicated that the timing of mitosis did not seem to be affected by any mutations because measured differences were within the boundaries of experimental error (Figure S1C)
PMID:16920624	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPCC736.14 [happens_during] mitotic metaphase [part_of] mitotic spindle assembly	These results established that phosphorylation of Dis1 by Cdc2 is required for the high-fidelity segregation of a minichromosome. (comment: (A little bit of curator licence here))
PMID:16921379	GO:0001671	ATPase activator activity [has_input] PomBase:SPAC644.14c	(comment: in complex with Sfr1)
PMID:16921379	GO:0001671	ATPase activator activity [has_input] PomBase:SPAC644.14c	(comment: in complex with Swi5)
PMID:16921379	GO:0005515	protein binding	(comment: sfr1 protein is not stable without swi5. swi5 alone does not bind rad51)
PMID:16921379	GO:0005515	protein binding	(comment: sfr1 protein is not stable without swi5. swi5 alone does not bind rad51.)
PMID:16931764	FYPO:0003822	decreased ribonuclease activity [assayed_enzyme] PomBase:SPCC736.11	(Fig. 1C)
PMID:16931764	FYPO:0003822	decreased ribonuclease activity [assayed_enzyme] PomBase:SPCC736.11	(Fig. 1C)
PMID:16931764	FYPO:0003822	decreased ribonuclease activity [assayed_enzyme] PomBase:SPCC736.11	(Fig. 1C)
PMID:16931764	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat	(Fig. 1D)
PMID:16931764	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dg_repeat	(Fig. 1D)
PMID:16931764	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat	(Fig. 1D)
PMID:16931764	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dg_repeat	(Fig. 1D)
PMID:16931764	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat	(Fig. 1D)
PMID:16931764	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dg_repeat	(Fig. 1D)
PMID:16931764	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat	(Fig. 1D)
PMID:16931764	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dg_repeat	(Fig. 1D)
PMID:16931764	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	(Fig. 1E)
PMID:16931764	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	(Fig. 1E)
PMID:16931764	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_region] dh_repeat [has_severity] medium [assayed_protein] PomBase:SPAC6F12.09	(Fig. 2A)
PMID:16931764	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_region] dg_repeat [has_severity] low [assayed_protein] PomBase:SPAC6F12.09	(Fig. 2A)
PMID:16931764	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_region] dh_repeat [has_severity] medium [assayed_protein] PomBase:SPAC6F12.09	(Fig. 2A)
PMID:16931764	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_region] dg_repeat [has_severity] low [assayed_protein] PomBase:SPAC6F12.09	(Fig. 2A)
PMID:16931764	FYPO:0004237	increased protein localization to heterochromatin at centromere outer repeat region [assayed_region] dh_repeat [has_severity] low [assayed_protein] PomBase:SPCC736.11	(Fig. 2B)
PMID:16931764	FYPO:0004237	increased protein localization to heterochromatin at centromere outer repeat region [assayed_region] dg_repeat [has_severity] medium [assayed_protein] PomBase:SPCC736.11	(Fig. 2B)
PMID:16931764	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 2C)
PMID:16931764	FYPO:0002331	increased histone H3-K4 dimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 2C)
PMID:16931764	FYPO:0002331	increased histone H3-K4 dimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 2C)
PMID:16931764	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 2C)
PMID:16931764	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	(Fig. 3C)
PMID:16931764	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	(Fig. 3C)
PMID:16931764	GO:0070551	endoribonuclease activity, cleaving siRNA-paired mRNA [part_of] siRNA-mediated heterochromatin formation	"Thus, Ago1 from fission yeast has ""slicing"" activity and can direct site-specific cleavage of RNA substrates via siRNA."
PMID:16963626	GO:0016602	CCAAT-binding factor complex	(Fig. 6b)
PMID:16963626	GO:0045944	positive regulation of transcription by RNA polymerase II [happens_during] response to iron ion	Consistently, mutations in the php3Δ - and php5Δ -encoded CCAAT-binding proteins were phenocopies of php2􏰂
PMID:16963626	GO:0045944	positive regulation of transcription by RNA polymerase II [happens_during] response to iron ion	Consistently, mutations in the php3Δ - and php5Δ -encoded CCAAT-binding proteins were phenocopies of php2􏰂
PMID:16963626	GO:0016602	CCAAT-binding factor complex	using the cross-linking agent EGS, we found that the Php4 protein associates with the Php2/Php3/Php5 complex
PMID:1699136	GO:0071958	new mitotic spindle pole body [exists_during] mitotic prophase	(Figure 1c)
PMID:1699136	GO:0071957	old mitotic spindle pole body [exists_during] mitotic prophase	(Figure 1c) and Double staining using a combination of cdc13- and tubulin- specific antibodies showed that the dots corresponded exactly to the positions of the mitotic spindle poles (Fig. 3a, b)
PMID:1699136	GO:0071957	old mitotic spindle pole body [exists_during] mitotic prophase	(Figure 1c) and Double staining using a combination of cdc13- and tubulin- specific antibodies showed that the dots corresponded exactly to the positions of the mitotic spindle poles (Fig. 3a, b)
PMID:1699136	GO:0005654	nucleoplasm [exists_during] mitotic prophase	(Figure 2)
PMID:17004072	FYPO:0001861	increased minichromosome loss upon segregation during vegetative growth	(Figure 2a)
PMID:17004072	FYPO:0001861	increased minichromosome loss upon segregation during vegetative growth	(Figure 2a)
PMID:17004072	FYPO:0002060	viable vegetative cell population	(Figure 5b)
PMID:17004072	FYPO:0002061	inviable vegetative cell population	(Table 2)
PMID:17005570	GO:0005515	protein binding	(Fig. 1)
PMID:17005570	GO:0005515	protein binding	(Fig. 1)
PMID:17005570	GO:0005515	protein binding	(Fig. 1)
PMID:17005570	GO:0005515	protein binding	(Fig. 1)
PMID:17005570	GO:0005515	protein binding	(Fig. 1)
PMID:17005570	GO:0005515	protein binding	(Fig. 1)
PMID:17005570	GO:0005515	protein binding	(Fig. 1)
PMID:17005570	GO:0005515	protein binding	(Fig. 1F)
PMID:17005570	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPAC14C4.02c	(Fig. 1b)
PMID:17005570	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPAC14C4.02c	(Fig. 1b)
PMID:17005570	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPAC14C4.02c	(Fig. 1c)
PMID:17005570	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPAC14C4.02c	(Fig. 1c) lane 9
PMID:17005570	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPAC14C4.02c	(Fig. 1d)
PMID:17005570	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPCC5E4.06	(Fig. 1f)
PMID:17005570	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPCC5E4.06	(Fig. 1f)
PMID:17005570	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPAC14C4.02c	(Fig. 3)
PMID:17005570	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPCC645.04	(Fig. 3)
PMID:17005570	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPAC14C4.02c	(Fig. 3)
PMID:17005570	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPAC14C4.02c	(Fig. 3)
PMID:17005570	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPCC645.04	(Fig. 3)
PMID:17005570	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPCC645.04	(Fig. 3)
PMID:17005570	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC14C4.02c [assayed_using] PomBase:SPCC645.04	(Fig. 5A)
PMID:17005570	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC14C4.02c [assayed_using] PomBase:SPCC645.04	(Fig. 5C)
PMID:17005570	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC14C4.02c [assayed_using] PomBase:SPBC651.10	(Fig. 6A, lane 9)
PMID:17005570	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC14C4.02c [assayed_using] PomBase:SPBC651.10	(Fig. 6B, lane 3)
PMID:17005570	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC14C4.02c [assayed_using] PomBase:SPBC651.10	(Fig. 6B, lane 9)
PMID:17005570	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC14C4.02c [assayed_using] PomBase:SPAC11E3.08c	(Fig. 7A)
PMID:17005570	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC14C4.02c [assayed_using] PomBase:SPAC11E3.08c	(Fig. 7A)
PMID:1703321	FYPO:0000776	normal protein phosphorylation during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Figure 4)
PMID:1703321	FYPO:0000776	normal protein phosphorylation during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Figure 4D)
PMID:1703321	FYPO:0000776	normal protein phosphorylation during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Figure 4D)
PMID:1703321	FYPO:0000776	normal protein phosphorylation during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Figure 4D)
PMID:1703321	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(comment: CHECK Also think this is previously annotated)
PMID:1703321	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(comment: CHECK I'm sure this has already been annotated. But previous annotations didn't come up, should they?)
PMID:1703321	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(comment: cdc2-F15 gene is expressed from episomal pIRT2)
PMID:1703321	FYPO:0002060	viable vegetative cell population	(comment: cdc2-F15 gene is expressed from episomal pIRT2)
PMID:1703321	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(comment: cdc25 over expressed from the constitutive ADH promoter. Data not shown)
PMID:1703321	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	cdc2-F15 (comment: gene is expressed from episomal pIRT2)
PMID:1703321	FYPO:0002060	viable vegetative cell population	cdc2-F15 (comment: gene is expressed from episomal pIRT2)
PMID:1703321	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	data not shown
PMID:1703321	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	data not shown
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic interphase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	18 proteins were localized at the centromere throughout the mitotic cell cycle (Table 2; group 1)
PMID:17035632	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPCC1235.07	In addition, their centromere localization depended on Mis6: Cnl2 and Fta7 proteins lost their centromere localization in a mis6-302 temperature-sensitive mutant at the restricted temperature of 36°C (Figure 1E)
PMID:17035632	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAC23H4.11c	In addition, their centromere localization depended on Mis6: Cnl2 and Fta7 proteins lost their centromere localization in a mis6-302 temperature-sensitive mutant at the restricted temperature of 36°C (Figure 1E)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	In contrast, four proteins (Dam1, Dad2, Ask1, and Spc34) were localized at the centromere only at the M phase (Table 2; group 2).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	In contrast, four proteins (Dam1, Dad2, Ask1, and Spc34) were localized at the centromere only at the M phase (Table 2; group 2).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	In contrast, four proteins (Dam1, Dad2, Ask1, and Spc34) were localized at the centromere only at the M phase (Table 2; group 2).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] mitotic M phase	In contrast, four proteins (Dam1, Dad2, Ask1, and Spc34) were localized at the centromere only at the M phase (Table 2; group 2).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase I	Proteins of the Mis6-like group remained at the centromere throughout meiosis (Figure 2B), whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	Sgo1 protein signal intensity increased in two steps (52 and 20 min before the metaphase-anaphase transition of meiosis I) in a way similar to the NMS (Ndc80- Mis12-Spc7) complex proteins (Figure 7B).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic prophase I	Sgo1 protein signal intensity increased in two steps (52 and 20 min before the metaphase-anaphase transition of meiosis I) in a way similar to the NMS (Ndc80- Mis12-Spc7) complex proteins (Figure 7B).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	The DASH complex proteins (Dam1, Spc34, Dad2, and Ask1) were not detected during meiotic prophase. They reappeared at the centromere shortly before metaphase of meiosis I (Figure 4)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	The DASH complex proteins (Dam1, Spc34, Dad2, and Ask1) were not detected during meiotic prophase. They reappeared at the centromere shortly before metaphase of meiosis I (Figure 4)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	The DASH complex proteins (Dam1, Spc34, Dad2, and Ask1) were not detected during meiotic prophase. They reappeared at the centromere shortly before metaphase of meiosis I (Figure 4)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	The DASH complex proteins (Dam1, Spc34, Dad2, and Ask1) were not detected during meiotic prophase. They reappeared at the centromere shortly before metaphase of meiosis I (Figure 4)
PMID:17035632	GO:0042729	DASH complex [exists_during] mitotic M phase	These 4 proteins share homology with the S. cerevisiae DASH complex, DAM1, DAD2, ASK1, and SPC34 (Miranda et al., 2005), and the observation that their centromere localization is limited to the M phase has been previously reported in S. pombe (Liu et al., 2005). Thus, we assigned these four proteins to the DASH complex (Table 2)
PMID:17035632	GO:0042729	DASH complex [exists_during] mitotic M phase	These 4 proteins share homology with the S. cerevisiae DASH complex, DAM1, DAD2, ASK1, and SPC34 (Miranda et al., 2005), and the observation that their centromere localization is limited to the M phase has been previously reported in S. pombe (Liu et al., 2005). Thus, we assigned these four proteins to the DASH complex (Table 2)
PMID:17035632	GO:0042729	DASH complex [exists_during] mitotic M phase	These 4 proteins share homology with the S. cerevisiae DASH complex, DAM1, DAD2, ASK1, and SPC34 (Miranda et al., 2005), and the observation that their centromere localization is limited to the M phase has been previously reported in S. pombe (Liu et al., 2005). Thus, we assigned these four proteins to the DASH complex (Table 2)
PMID:17035632	GO:0042729	DASH complex [exists_during] mitotic M phase	These 4 proteins share homology with the S. cerevisiae DASH complex, DAM1, DAD2, ASK1, and SPC34 (Miranda et al., 2005), and the observation that their centromere localization is limited to the M phase has been previously reported in S. pombe (Liu et al., 2005). Thus, we assigned these four proteins to the DASH complex (Table 2)
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17035632	GO:0000779	condensed chromosome, centromeric region [exists_during] meiotic metaphase I	whereas those of the NMS group disappeared from the centromere or their presence was significantly reduced, during meiotic prophase (Figure 3).
PMID:17036054	FYPO:0005720	normal mitotic metaphase chromosome recapture [has_penetrance] 20	(Fig. 1b)
PMID:17036054	FYPO:0005720	normal mitotic metaphase chromosome recapture	(Fig. 1b)
PMID:17036054	FYPO:0005720	normal mitotic metaphase chromosome recapture [has_penetrance] 20	(Fig. 1b)
PMID:17036054	FYPO:0005720	normal mitotic metaphase chromosome recapture [has_penetrance] 20	(Fig. 1b)
PMID:17036054	FYPO:0006041	decreased rate of mitotic metaphase chromosome recapture [has_penetrance] 30	(Fig. 1b)
PMID:17036054	FYPO:0001733	abnormal mitotic spindle pole body separation [has_penetrance] 30	(Figure 1a)
PMID:17036054	FYPO:0005411	increased number of unattached kinetochores [has_penetrance] 80	(Figure 1a)
PMID:17036054	FYPO:0001733	abnormal mitotic spindle pole body separation [has_penetrance] 20	(Figure 1a)
PMID:17036054	FYPO:0001733	abnormal mitotic spindle pole body separation [has_penetrance] 20	(Figure 1a)
PMID:17036054	FYPO:0001733	abnormal mitotic spindle pole body separation [has_penetrance] 20	(Figure 1a)
PMID:17036054	FYPO:0005411	increased number of unattached kinetochores [has_penetrance] 90	(Figure 1a)
PMID:17036054	FYPO:0005411	increased number of unattached kinetochores [has_penetrance] 80	(Figure 1a)
PMID:17036054	FYPO:0005411	increased number of unattached kinetochores [has_penetrance] 80	(Figure 1a)
PMID:17036054	FYPO:0002004	microtubules absent from cell [has_penetrance] 81	(comment: CHECK Supplement)
PMID:17038309	GO:0097680	double-strand break repair via classical nonhomologous end joining	(comment: CHECK i) xlf1 deletion is epistatic with lig4 deletion ii) IR sensitivity during spore state and inability to ligate linearised plasmids during vegetative state)
PMID:17038309	GO:0003677	DNA binding	(comment: binds both circular and linear DNA fragments)
PMID:17039252	FYPO:0000255	increased nuclear protein level during vegetative growth [assayed_using] PomBase:SPBC428.18	(comment: especially during S and G2 phases)
PMID:17039252	FYPO:0000255	increased nuclear protein level during vegetative growth [assayed_using] PomBase:SPBC428.18	(comment: especially during S and G2 phases)
PMID:17039252	FYPO:0000255	increased nuclear protein level during vegetative growth [assayed_using] PomBase:SPBC428.18	(comment: especially during S and G2 phases)
PMID:17039252	FYPO:0000255	increased nuclear protein level during vegetative growth [assayed_using] PomBase:SPBC428.18	(comment: especially during S and G2 phases)
PMID:17043360	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1B)
PMID:17043360	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1B)
PMID:17043360	FYPO:0000012	mitotic G2/M phase transition delay	(Fig. 1C)
PMID:17043360	FYPO:0000650	increased septation index	(Fig. 2)
PMID:17043360	FYPO:0006642	decreased protein localization to nucleus during mitotic interphase [assayed_protein] PomBase:SPAC24H6.05	(Fig. 4A)
PMID:17043360	FYPO:0001038	increased protein phosphorylation during vegetative growth [has_severity] high [assayed_protein] PomBase:SPBC11B10.09	(Fig. 4C)
PMID:17046992	FYPO:0002060	viable vegetative cell population	(Comment: cells stop growing at high temperature, but remain viable and resume growth and division when returned to standard temperature
PMID:17046992	FYPO:0004481	abolished cell population growth at high temperature	(Comment: cells stop growing at high temperature, but remain viable and resume growth and division when returned to standard temperature)
PMID:17046992	GO:1900087	positive regulation of G1/S transition of mitotic cell cycle	(comment: TORC1 senses nutrients and pushes cells into the next cell cycle. Removing TORC1 activity, you get a buildup of rum1 and srw1 which inhibit G1/S)
PMID:17085965	GO:1902929	plasma membrane of growing cell tip	localization depends on microtubule cytoskeleton, as determined by treatment with carbendazim (methyl 2-benzimidazolecarbamate; MBC), and on actin cytoskeleton, as determined by treatment with latrunculin B or cytochalasin D
PMID:17112379	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: CONDITION 25 degrees)
PMID:17112379	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: CONDITION 25 degrees)
PMID:17112379	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: CONDITION 25 degrees)
PMID:17112379	FYPO:0001974	increased number of cells with 1C DNA content	(comment: CONDITION 30 degrees)
PMID:17112379	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 30 degrees)
PMID:17121544	FYPO:0002061	inviable vegetative cell population	(Figure 1B)
PMID:17121544	FYPO:0002061	inviable vegetative cell population	(Figure 1B)
PMID:17121544	FYPO:0002085	normal vegetative cell growth [has_severity] high	(comment: CONDITION at 30 degrees)
PMID:17121544	FYPO:0004085	decreased vegetative cell growth [has_severity] high	(comment: CONDITION at 30 degrees) Tor1 becomes necessary for cell growth when Tor2 function is compromised.
PMID:17121544	FYPO:0000951	inviable small vegetative cell [has_penetrance] high [has_severity] high	(mimic nitrogen starvation response, When starved for nitrogen, on the other hand, the cells divide twice and then arrest at G1) At 4 h and 8 h after the shift to36 °C, the average cell length was reduced to 6.4 μm and6.2 μm, respectively, which were ∼50% decreases com-pared to wild-type cells (13.0 μm and 12.9 μm). Similar tsresults were obtained for tor2 -19. It is of note that, in contrast to the reduced length, the cell width remained constant in these mutant cells.
PMID:17121544	FYPO:0000951	inviable small vegetative cell [has_penetrance] high [has_severity] high	(mimic nitrogen starvation response, When starved for nitrogen, on the other hand, the cells divide twice and then arrest at G1) At 4 h and 8 h after the shift to36 °C, the average cell length was reduced to 6.4 μm and6.2 μm, respectively, which were ∼50% decreases com-pared to wild-type cells (13.0 μm and 12.9 μm). Similar tsresults were obtained for tor2 -19. It is of note that, in contrast to the reduced length, the cell width remained constant in these mutant cells.
PMID:17121544	FYPO:0005097	abnormal cell cycle arrest in mitotic G1 phase	(mimic nitrogen starvation response, When starved for nitrogen, on the other hand, the cells divide twice and then arrest at G1) At 4 h and 8 h after the shift to36 °C, the average cell length was reduced to 6.4 μm and6.2 μm, respectively, which were ∼50% decreases com-pared to wild-type cells (13.0 μm and 12.9 μm). Similar tsresults were obtained for tor2 -19. It is of note that, in contrast to the reduced length, the cell width remained constant in these mutant cells.
PMID:17121544	FYPO:0005097	abnormal cell cycle arrest in mitotic G1 phase	(mimic nitrogen starvation response, When starved for nitrogen, on the other hand, the cells divide twice and then arrest at G1) At 4 h and 8 h after the shift to36 °C, the average cell length was reduced to 6.4 μm and6.2 μm, respectively, which were ∼50% decreases com-pared to wild-type cells (13.0 μm and 12.9 μm). Similar tsresults were obtained for tor2 -19. It is of note that, in contrast to the reduced length, the cell width remained constant in these mutant cells.
PMID:17121544	FYPO:0003031	mating without nitrogen starvation [has_penetrance] 70	70% of ts the tor2 -13 cells committed sexual development to ts form zygotes and spores (Fig. 3B,C)
PMID:17121544	FYPO:0002578	resistance to hydroxyurea	As expected, these double mutants behaved the same as tor1∆rhb1+o/e cells, in which growth was restored under stress conditions (the fourth row).
PMID:17121544	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	tor1∆tor2 -19 showed only the 2C peak, and no 1C peak appeared at 36 °C
PMID:17130122	FYPO:0003669	exon skipping	(comment: assayed using artificial reporter construct ura4 containing two introns and one exon from nda3)
PMID:17130122	FYPO:0003669	exon skipping	(comment: assayed using artificial reporter construct ura4 containing two introns and one exon from nda3)
PMID:17130122	FYPO:0003669	exon skipping	(comment: assayed using artificial reporter construct ura4 containing two introns and one exon from nda3)
PMID:17130122	FYPO:0003669	exon skipping	(comment: assayed using artificial reporter construct ura4 containing two introns and one exon from nda3)
PMID:17178839	FYPO:0002060	viable vegetative cell population	(Fig. 1A)
PMID:17178839	FYPO:0002060	viable vegetative cell population	(Fig. 1A)
PMID:17178839	FYPO:0002060	viable vegetative cell population	(Fig. 1A)
PMID:17178839	FYPO:0002061	inviable vegetative cell population	(Fig. 1B)
PMID:17178839	FYPO:0002061	inviable vegetative cell population	(Fig. 1B)
PMID:17178839	FYPO:0002058	viable cell population	(Fig. 1B)
PMID:17178839	FYPO:0002060	viable vegetative cell population	(Fig. 1B)
PMID:17178839	FYPO:0002061	inviable vegetative cell population	(Fig. 1B)
PMID:17178839	FYPO:0003165	cut with abnormal chromosome segregation	(Fig. 1c,d)
PMID:17178839	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] 14	(Fig. 2 a,b)
PMID:17178839	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] >45	(Fig. 2 a,b)
PMID:17178839	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] >25	(Fig. 2 a,b)
PMID:17178839	FYPO:0002060	viable vegetative cell population	(Fig. 3A)
PMID:17178839	FYPO:0002061	inviable vegetative cell population	(Fig. 3B)
PMID:17178839	FYPO:0002060	viable vegetative cell population	(Fig. 3C)
PMID:17178839	FYPO:0005435	inviable after spore germination with elongated germ tube and fragmented nucleus	(Fig. 3c)
PMID:17178839	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 4A)
PMID:17178839	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 4A)
PMID:17178839	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 4A)
PMID:17178839	FYPO:0000095	sensitive to bleomycin [has_severity] medium	(Fig. 4A)
PMID:17178839	FYPO:0000950	elongated aseptate vegetative cell [has_penetrance] high	(Fig. 4B)
PMID:17178839	FYPO:0001705	normal mitotic DNA damage checkpoint [has_penetrance] high	(Fig. 4B)
PMID:17178839	FYPO:0005436	abolished double-strand break repair [has_penetrance] high	(Fig. 4C)
PMID:17178839	FYPO:0005437	normal number of Rad52 foci during cellular response to bleomycin	(Fig. 4D)
PMID:17178839	FYPO:0000671	abnormal rDNA separation	(comment: CHECK not sure if this is correct....)
PMID:17178839	FYPO:0000671	abnormal rDNA separation	(comment: CHECK not sure if this is correct....)
PMID:17192844	FYPO:0000488	normal meiotic recombination	The wild-type cross yielded 81 ± 7.5% viable spores, the pnu1Δ cross 82 ± 3%. As far as tested, no change of meiosis and recombination was detected in mutants abolishing the function of the Pnu1 (End1) nuclease.
PMID:17211518	FYPO:0002800	normal protein degradation during vegetative growth	(comment: proteasomal)
PMID:17213188	FYPO:0002926	abolished poly(A) RNA binding	(comment: binding by Pab2)
PMID:17222800	FYPO:0003720	snoRNA guided rRNA 2'-O-methylation abolished at specific site	(comment: CHECK 25S rRNA positions 2304, 2497)
PMID:17276356	FYPO:0002321	decreased cellular ergosterol level	...contained a reduced amount of ergosterol and elevated amounts of the ergosterol biosynthetic intermediates 24-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7-dienol, consistent with defects at the Erg11 and Erg5 enzymatic steps (Figure 1B).
PMID:17276356	PomGeneEx:0000011	RNA level increased [during] cellular response to hypoxia	Expression of dap1+ mRNA was induced in the absence of oxygen in a Sre1-dependent manner (Figure 1A)
PMID:17276356	FYPO:0002321	decreased cellular ergosterol level	However, similar to dap1D, yeast carrying the HA-dap1 Y138F plasmid accumulated 24-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7- dienol, reflecting defects in Erg11 and Erg5 (Figure 3B). These data indicate that dap1 Y138F is a loss-of-function mutation and that Dap1 function requires bound heme.
PMID:17276356	GO:0008047	enzyme activator activity [has_input] PomBase:SPAC13A11.02c	These data demonstrate that Dap1 is required in vivo for the activity of Erg11 and Erg5, the entire complement of cytochrome P450 enzymes in fission yeast.
PMID:17276356	GO:0008047	enzyme activator activity [has_input] PomBase:SPAC19A8.04	These data demonstrate that Dap1 is required in vivo for the activity of Erg11 and Erg5, the entire complement of cytochrome P450 enzymes in fission yeast.
PMID:17276356	GO:0020037	heme binding [has_input] PomBase:SPAC19A8.04	These data demonstrate that Dap1 is required in vivo for the activity of Erg11 and Erg5, the entire complement of cytochrome P450 enzymes in fission yeast.
PMID:17276356	FYPO:0002060	viable vegetative cell population	dap1D cells were viable under normal growth conditions but .....
PMID:17276356	FYPO:0008296	increased cellular 24-methylene lanosterol level	elevated amounts of the ergosterol biosynthetic intermediates 2. upon loss of Dap1, cells accumulated 24-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7-dienol, substrates for Erg11 and Erg5. 4-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7-dienol, Figure 1B. Ergosta-5,7-dienol is not a normal pathway intermediate, but forms when Erg5 is inhibited (Figure S1)
PMID:17276356	FYPO:0008298	increased ergosta-5,7-dienol level	elevated amounts of the ergosterol biosynthetic intermediates 2. upon loss of Dap1, cells accumulated 24-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7-dienol, substrates for Erg11 and Erg5. 4-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7-dienol, Figure 1B. Ergosta-5,7-dienol is not a normal pathway intermediate, but forms when Erg5 is inhibited (Figure S1)
PMID:17276356	FYPO:0008297	increased cellular ergosta-5,7,24(28)-trienol level	elevated amounts of the ergosterol biosynthetic intermediates 2. upon loss of Dap1, cells accumulated 24-methylene lanosterol, ergosta5,7,24(28)-trienol, and ergosta-5,7-dienol, substrates for Erg11 and Erg5. 4-methylene lanosterol, ergosta-5,7,24(28)-trienol, and ergosta-5,7-dienol, Figure 1B. Ergosta-5,7-dienol is not a normal pathway intermediate, but forms when Erg5 is inhibited (Figure S1)
PMID:17276356	FYPO:0009071	sensitive to itraconazole	sensitive to the inhibitors of sterol synthesis itraconazole and CoCl2 (Figure 1D).
PMID:17289569	FYPO:0005918	decreased protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPBC800.03	(Figure 4B)
PMID:17289569	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPCC188.07	(Figure 4B) However, defect in RNAi pathway had no impact on Ccq1 localization
PMID:17289569	FYPO:0005396	abolished protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPBC800.03	(Figure 4B) We found that Clr3 localization at telomere ends was completely abolished in cells defective in both Taz1 and RNAi pathways.
PMID:17289569	FYPO:0005918	decreased protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPBC800.03	(Figure 4B) clr3 at telomeres were reduced to the same extent in mutant strains disrupted for either Ccq1 or Taz1
PMID:17289569	FYPO:0005918	decreased protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPBC800.03	(Figure 4B) clr3 at telomeres were reduced to the same extent in mutant strains disrupted for either Ccq1 or Taz1
PMID:17289569	FYPO:0005918	decreased protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPCC188.07	(Figure 4B) while the levels of Ccq1 at telomeres, relative to those in wild-type cells, were unchanged in clr3D cells but decreased in taz1D
PMID:17289569	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPCC188.07	(Figure 4B) while the levels of Ccq1 at telomeres, relative to those in wild-type cells, were unchanged in clr3D cells but decreased in taz1D
PMID:17289569	FYPO:0005918	decreased protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPBP35G2.10	(Figure 4C), Levels of Clr3 and Mit1 were dramatically reduced at subtelomeres in swi6 mutant strains
PMID:17289569	FYPO:0000966	increased histone H3-K14 acetylation at centromere outer repeat during vegetative growth	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	FYPO:0003011	increased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPBC28F2.12	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	FYPO:0000966	increased histone H3-K14 acetylation at centromere outer repeat during vegetative growth	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	FYPO:0000966	increased histone H3-K14 acetylation at centromere outer repeat during vegetative growth	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	FYPO:0000966	increased histone H3-K14 acetylation at centromere outer repeat during vegetative growth	(Figure 5B) we found increases in H3K14ac levels and greater Pol II occupancy at the reporter embedded within pericentromeric heterochromatin in....strains lacking SHREC components
PMID:17289569	FYPO:0002836	increased centromeric outer repeat transcript-derived siRNA level	(Figure 5E). Enhanced transcriptional-machinery occupancy at heterochromatic repeats in SHREC defective cells,..should result in elevated repeat transcripts ...corresponding increase in siRNA production.
PMID:17289569	FYPO:0002836	increased centromeric outer repeat transcript-derived siRNA level	(Figure 5E). Enhanced transcriptional-machinery occupancy at heterochromatic repeats in SHREC defective cells,..should result in elevated repeat transcripts ...corresponding increase in siRNA production.
PMID:17289569	FYPO:0002836	increased centromeric outer repeat transcript-derived siRNA level	(Figure 5E). Enhanced transcriptional-machinery occupancy at heterochromatic repeats in SHREC defective cells,..should result in elevated repeat transcripts ...corresponding increase in siRNA production.
PMID:17289569	FYPO:0002836	increased centromeric outer repeat transcript-derived siRNA level	(Figure 5E). Enhanced transcriptional-machinery occupancy at heterochromatic repeats in SHREC defective cells,..should result in elevated repeat transcripts ...corresponding increase in siRNA production.
PMID:17289569	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Figure 6A) both clr3D232N and mit1K587A mutant alleles alleviated silencing of a marker gene inserted at pericentromeric repeats
PMID:17289569	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Figure 6A) both clr3D232N and mit1K587A mutant alleles alleviated silencing of a marker gene inserted at pericentromeric repeats
PMID:17289569	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	(Figure 6B)
PMID:17289569	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	(Figure 6B)
PMID:17289569	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Figure 6B)
PMID:17289569	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Figure 6B)
PMID:17289569	FYPO:0003704	decreased histone deacetylase activity	(Figure 6D)
PMID:17289569	FYPO:0001168	decreased ATPase activity	(Figure 6D)
PMID:17289569	FYPO:0000853	abnormal nucleosome positioning	(Figure 6E)
PMID:17289569	GO:0000183	rDNA heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0000183	rDNA heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0030466	silent mating-type cassette heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0031509	subtelomeric heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0031509	subtelomeric heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0031508	pericentric heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0031508	pericentric heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0031508	pericentric heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0000183	rDNA heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0030466	silent mating-type cassette heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0031509	subtelomeric heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0031508	pericentric heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0031509	subtelomeric heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0030466	silent mating-type cassette heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0030466	silent mating-type cassette heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0000183	rDNA heterochromatin formation	(comment: by TGS)
PMID:17289569	GO:0060090	molecular adaptor activity [has_input] PomBase:SPBC800.03	(comment: part of TGS)
PMID:17289569	GO:0060090	molecular adaptor activity [has_input] PomBase:SPBC800.03	(comment: part of TGS)
PMID:17289569	FYPO:0007278	normal protein localization to euchromatin [assayed_using] PomBase:SPBP35G2.10	In contrast to heterochromatic loci, SHREC recruitment to euchromatic sites was unaffected in the absence of Swi6, as shown by Clr3 and Mit1 localization at a locus encoding a noncoding RNA and an intergenic region (Figure 4D).
PMID:17289569	FYPO:0007278	normal protein localization to euchromatin [assayed_using] PomBase:SPBC800.03	In contrast to heterochromatic loci, SHREC recruitment to euchromatic sites was unaffected in the absence of Swi6, as shown by Clr3 and Mit1 localization at a locus encoding a noncoding RNA and an intergenic region (Figure 4D).
PMID:17289569	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_using] PomBase:SPCC736.11	The role of SHREC in transcriptional silencing could be decoupled from the cis-PTGS function of the RNAi machinery since impaired SHREC had no effect on the localization of RITS Agol subunit at heterochromatin (Figure 5D).
PMID:17289569	FYPO:0003216	decreased chromatin silencing at rDNA [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0003216	decreased chromatin silencing at rDNA [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0003216	decreased chromatin silencing at rDNA [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] low	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17289569	FYPO:0003216	decreased chromatin silencing at rDNA [has_severity] high	pericentromeric repeats, the silent mat locus, telomeres, and rDNA loci were derepressed in strains lacking any individual core component of SHREC (Figure 5A).
PMID:17304215	GO:0005634	nucleus	(Figure 1A) In normally growing cells, Swi5-EGFP localized to the nucleus and exhibited diffuse nuclear staining with a few distinct foci
PMID:17304215	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPBC409.03	(Figure 1B) The absence of Swi2 or Sfr1 did not affect the cellular expression level of the Swi5-EGFP protein .
PMID:17304215	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPBC409.03	(Figure 1B) The absence of Swi2 or Sfr1 did not affect the cellular expression level of the Swi5-EGFP protein .
PMID:17304215	GO:0005634	nucleus	(Figure 2A)
PMID:17304215	FYPO:0008168	abolished nuclear foci [assayed_using] PomBase:SPBC409.03	On the other hand, the nuclei of sfr1D cells contained Swi5-EGFP foci
PMID:17304223	FYPO:0005165	abnormal spatio-temporal regulation of replication fork localization	(comment: CHECK foci disappear in HU; without HU foci appear but with abnormal dynamics)
PMID:17304223	FYPO:0005165	abnormal spatio-temporal regulation of replication fork localization	(comment: CHECK foci disappear in HU; without HU foci appear but with abnormal dynamics)
PMID:17307401	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(comment: same as mus81delta alone)
PMID:17307401	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(comment: same as mus81delta alone)
PMID:17307401	FYPO:0000085	sensitive to camptothecin [has_severity] high	(comment: same as mus81delta alone)
PMID:17307401	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(comment: same as mus81delta alone)
PMID:17307401	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: worse than either single mutant)
PMID:17307401	FYPO:0000085	sensitive to camptothecin [has_severity] high	(comment: worse than either single mutant)
PMID:17307401	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(comment: worse than either single mutant)
PMID:17307401	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: worse than either single mutant)
PMID:17307401	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: worse than either single mutant)
PMID:17307401	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(comment: worse than either single mutant)
PMID:17307401	FYPO:0000085	sensitive to camptothecin [has_severity] high	(comment: worse than either single mutant)
PMID:17307401	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(comment: worse than either single mutant)
PMID:17310250	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] high	(Fig. 1C)
PMID:17310250	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] high	(Fig. 1C)
PMID:17310250	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] high	(Fig. 1C)
PMID:17310250	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 1C)
PMID:17310250	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 1C)
PMID:17310250	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 1D)
PMID:17310250	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_region] dg_repeat [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 1D)
PMID:17310250	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_region] dg_repeat [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 1D)
PMID:17310250	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 1D)
PMID:17310250	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	(Fig. 2C)
PMID:17310250	GO:0005737	cytoplasm	(Fig. 3A)
PMID:17310250	GO:0005634	nucleus	(Fig. 3A)
PMID:17310250	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] high	(Fig. 5B)
PMID:17310250	FYPO:0006992	normal chromatin silencing at centromere otr1R	(Fig. 5B)
PMID:17310250	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] medium	(Fig. 5B)
PMID:17310250	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] medium	(Fig. 5B)
PMID:17310250	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level	(Fig. 5C)
PMID:17310250	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level	(Fig. 5C)
PMID:17310250	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_region] dg_repeat [assayed_protein] PomBase:SPCC736.11 [has_severity] medium	(Fig. 6A)
PMID:17310250	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_region] dg_repeat [assayed_protein] PomBase:SPAC18G6.02c	(Fig. 6A)
PMID:17310250	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_region] dg_repeat [assayed_protein] PomBase:SPAC18G6.02c	(Fig. 6A)
PMID:17310250	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_region] dg_repeat [assayed_protein] PomBase:SPAC18G6.02c [has_severity] high	(Fig. 6A)
PMID:17310250	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_region] dg_repeat [has_severity] medium [assayed_protein] PomBase:SPAC18G6.02c	(Fig. 6A)
PMID:17310250	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 6A)
PMID:17310250	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 6A)
PMID:17310250	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 6A)
PMID:17310250	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] low	(Fig. 6A)
PMID:17310250	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_region] dg_repeat [assayed_protein] PomBase:SPCC736.11	(Fig. 6A)
PMID:17310250	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_region] dg_repeat [assayed_protein] PomBase:SPCC736.11 [has_severity] medium	(Fig. 6A)
PMID:17310250	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_region] dg_repeat [assayed_protein] PomBase:SPCC736.11 [has_severity] medium	(Fig. 6A)
PMID:17310250	GO:0060698	endoribonuclease inhibitor activity [has_input] PomBase:SPCC736.11	Nonetheless Arb1, by itself and/or together with Arb2, is a direct inhibitor of the slicer activity of fission yeast Ago1. Fig. 4D
PMID:17310250	GO:0070551	endoribonuclease activity, cleaving siRNA-paired mRNA [part_of] siRNA processing	These results indicate that the slicer activity of Ago1 is required for the in vivo conversion of double-stranded siRNA to single-stranded siRNA
PMID:17317928	FYPO:0002700	increased protein kinase activity	(comment: assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25)
PMID:17317928	FYPO:0003075	normal protein kinase activity	(comment: assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25)
PMID:17317928	FYPO:0001382	decreased protein kinase activity	(comment: assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25)
PMID:17317928	FYPO:0002700	increased protein kinase activity	(comment: assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25)
PMID:17317928	FYPO:0002700	increased protein kinase activity	(comment: assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25)
PMID:17317928	FYPO:0001382	decreased protein kinase activity	(comment: assayed substrate: myelin basic protein; assayed enzyme is, or is bound to, Pmo25)
PMID:17339332	GO:0006357	regulation of transcription by RNA polymerase II	(comment: same pathway)
PMID:17352737	FYPO:0004439	long curved mitotic spindle during anaphase	(comment: CHECK anaphase, elongating beyond cell end resulting in long curved spindle, requested)
PMID:17363370	GO:0033503	HULC complex	(Fig. 1C)
PMID:17363370	GO:0033503	HULC complex	(Fig. 1C)
PMID:17363370	GO:0033503	HULC complex	(Fig. 1C)
PMID:17363370	GO:0033503	HULC complex	(Fig. 1C)
PMID:17363370	FYPO:0001122	elongated vegetative cell [has_penetrance] high	(Fig. 1D)
PMID:17363370	FYPO:0001122	elongated vegetative cell [has_penetrance] high	(Fig. 1D)
PMID:17363370	FYPO:0001122	elongated vegetative cell [has_penetrance] high	(Fig. 1D)
PMID:17363370	FYPO:0001122	elongated vegetative cell [has_penetrance] high	(Fig. 1D)
PMID:17363370	FYPO:0001122	elongated vegetative cell [has_penetrance] high	(Fig. 1D)
PMID:17363370	FYPO:0002360	normal chromatin silencing at centromere	(Fig. 4A,B)
PMID:17363370	FYPO:0005072	normal protein localization to centromeric chromatin [assayed_protein] PomBase:SPAC664.01c	(Fig. 4A,B)
PMID:17363370	FYPO:0002360	normal chromatin silencing at centromere	(Fig. 4A,B)
PMID:17363370	FYPO:0005072	normal protein localization to centromeric chromatin [assayed_protein] PomBase:SPAC664.01c	(Fig. 4A,B)
PMID:17363370	FYPO:0002360	normal chromatin silencing at centromere	(Fig. 4A,B)
PMID:17363370	FYPO:0005072	normal protein localization to centromeric chromatin [assayed_protein] PomBase:SPAC664.01c	(Fig. 4A,B)
PMID:17363370	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_protein] PomBase:SPBC28F2.12	(Fig. 5D)
PMID:17363370	FYPO:0004237	increased protein localization to heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPBC28F2.12	(Fig. 5D)
PMID:17363370	FYPO:0002922	abolished histone H2B-K119 ubiquitination during vegetative growth	(Figure 2b)
PMID:17363370	FYPO:0002922	abolished histone H2B-K119 ubiquitination during vegetative growth	(Figure 2b)
PMID:17363370	FYPO:0002922	abolished histone H2B-K119 ubiquitination during vegetative growth	(Figure 2b)
PMID:17363370	FYPO:0002922	abolished histone H2B-K119 ubiquitination during vegetative growth	(Figure 2b)
PMID:17363370	FYPO:0002922	abolished histone H2B-K119 ubiquitination during vegetative growth	(Figure 2b)
PMID:17363370	FYPO:0006299	increased chromatin silencing at centromere outer repeat	(Figure 2d) Δrhp6 resulted in enhanced silencing of the otr1::ura4+, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	FYPO:0006299	increased chromatin silencing at centromere outer repeat	(Figure 2d) Δrhp6 resulted in enhanced silencing of the otr1::ura4+, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	FYPO:0006299	increased chromatin silencing at centromere outer repeat	(Figure 2d) Δrhp6 resulted in enhanced silencing of the otr1::ura4+, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	FYPO:0006299	increased chromatin silencing at centromere outer repeat	(Figure 2d) Δrhp6 resulted in enhanced silencing of the otr1::ura4+, as shown by reduced growth on medium lacking uracil (Fig. 2D)
PMID:17363370	FYPO:0007843	normal nucleosome positioning at centromere	(supplemental Fig. 2)
PMID:17363370	GO:0140850	histone H2B C-terminal K residue ubiquitin ligase activity [has_input] PomBase:SPCC622.09	HULC revealed that slower migrating band representing ubH2B was missing in cells lacking either Bre1 homologs (i.e. Rfp1 or Rfp2) or Shf1. These analyses suggest that components of HULC are required for ubiquitination of H2B.
PMID:17363370	GO:0140850	histone H2B C-terminal K residue ubiquitin ligase activity [has_input] PomBase:SPCC622.09	HULC revealed that slower migrating band representing ubH2B was missing in cells lacking either Bre1 homologs (i.e. Rfp1 or Rfp2) or Shf1. These analyses suggest that components of HULC are required for ubiquitination of H2B.
PMID:17363370	FYPO:0007844	increased histone H3-K9 monomethylation at centromere during vegetative growth	Interestingly, levels of trimethylated H3K9 (H3K9me3) were significantly reduced, although the levels of monomethylated H3K9 (H3K9me1) were increased at the dg repeat element and otr1::ura4+ (Fig. 3B).
PMID:17363370	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC664.01c	Interestingly, levels of trimethylated H3K9 (H3K9me3) were significantly reduced, although the levels of monomethylated H3K9 (H3K9me1) were increased at the dg repeat element and otr1::ura4+ (Fig. 3B).
PMID:17363370	FYPO:0005071	increased chromatin silencing at centromere	Interestingly, the H2B-K119R mutation significantly enhanced silencing of the otr1::ura4+ (Fig. 5A)
PMID:17363370	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	Overexpression of Rhp6 abrogates silencing of the otr1::ura4+ reporter, resulting in the loss of cell viability on medium supplemented with FOA (Fig. 3A)
PMID:17369611	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] low	However, H3-K56R, rtt109Δ, and the H3-K56R/rtt109Δ mutant cells formed colonies of variable pink indicating a slight decrease in silencing at centromeres (Fig. 4A). This might indicate a cross-talk of H3 Lys-56-Ac with the establishment or the maintenance of other activating or repressing histone modifications required for proper centromeric heterochromatin formation.
PMID:17371846	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2A)
PMID:17371846	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 2A)
PMID:17371846	FYPO:0001387	loss of viability at high temperature [has_severity] medium	(Fig. 2C)
PMID:17371846	FYPO:0001387	loss of viability at high temperature [has_severity] high	(Fig. 2C)
PMID:17371846	FYPO:0001387	loss of viability at high temperature [has_severity] high	(Fig. 2C)
PMID:17371846	FYPO:0000674	normal cell population growth at high temperature	(Fig. 2C)
PMID:17371846	FYPO:0001357	normal vegetative cell population growth	(Fig. 2C)
PMID:17371846	FYPO:0001357	normal vegetative cell population growth	(Fig. 2C)
PMID:17371846	FYPO:0001357	normal vegetative cell population growth	(Fig. 2C)
PMID:17371846	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] low	(Fig. 4B)
PMID:17371846	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] medium	(Fig. 4B)
PMID:17371846	FYPO:0005225	increased histone H3-K4 dimethylation during vegetative growth	(Fig. 4C)
PMID:17371846	FYPO:0006361	increased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth	(Fig. 5)
PMID:17371846	GO:0005721	pericentric heterochromatin	In addition, SAPHIRE occupies the junctions between the central region of the centromeres and the dg/dh repeats
PMID:17371846	GO:0005721	pericentric heterochromatin	In addition, SAPHIRE occupies the junctions between the central region of the centromeres and the dg/dh repeats
PMID:17371846	GO:0005721	pericentric heterochromatin	In addition, SAPHIRE occupies the junctions between the central region of the centromeres and the dg/dh repeats
PMID:17371846	GO:0005721	pericentric heterochromatin	In addition, SAPHIRE occupies the junctions between the central region of the centromeres and the dg/dh repeats
PMID:17371846	GO:0000785	chromatin	In general, we found SAPHIRE distributed widely throughout the genome and dispersed at genes over all three chromosome arms.
PMID:17371846	GO:0000785	chromatin	In general, we found SAPHIRE distributed widely throughout the genome and dispersed at genes over all three chromosome arms.
PMID:17371846	GO:0000785	chromatin	In general, we found SAPHIRE distributed widely throughout the genome and dispersed at genes over all three chromosome arms.
PMID:17371846	GO:0000785	chromatin	In general, we found SAPHIRE distributed widely throughout the genome and dispersed at genes over all three chromosome arms.
PMID:17371846	FYPO:0002150	inviable spore population	We found that saf140, saf60, and saf50 are essential genes, as viability segregated 2:2 in four-spore tetrads
PMID:17371846	FYPO:0002150	inviable spore population	We found that saf140, saf60, and saf50 are essential genes, as viability segregated 2:2 in four-spore tetrads
PMID:17371846	FYPO:0002150	inviable spore population	We found that saf140, saf60, and saf50 are essential genes, as viability segregated 2:2 in four-spore tetrads
PMID:17371846	GO:0140720	subtelomeric heterochromatin	in peaks in the subtelomeric regions of chromosomes 1 and 2
PMID:17371846	GO:0140720	subtelomeric heterochromatin	in peaks in the subtelomeric regions of chromosomes 1 and 2
PMID:17371846	GO:0140720	subtelomeric heterochromatin	in peaks in the subtelomeric regions of chromosomes 1 and 2
PMID:17371846	GO:0140720	subtelomeric heterochromatin	in peaks in the subtelomeric regions of chromosomes 1 and 2
PMID:17371846	GO:0031934	mating-type region heterochromatin	we observed SAPHIRE in the region of the silent mating (MAT) locus
PMID:17371846	GO:0031934	mating-type region heterochromatin	we observed SAPHIRE in the region of the silent mating (MAT) locus
PMID:17371846	GO:0031934	mating-type region heterochromatin	we observed SAPHIRE in the region of the silent mating (MAT) locus
PMID:17371846	GO:0031934	mating-type region heterochromatin	we observed SAPHIRE in the region of the silent mating (MAT) locus
PMID:17412958	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3A)
PMID:17412958	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 3A)
PMID:17412958	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 3A)
PMID:17412958	FYPO:0000123	large vacuoles during vegetative growth	(Fig. 3B)
PMID:17412958	FYPO:0001315	normal vegetative cell morphology	(Fig. 3B)
PMID:17412958	FYPO:0000647	vegetative cell lysis	(Fig. 3B)
PMID:17412958	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	(Fig. 3C)
PMID:17412958	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 3C)
PMID:17412958	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	(Fig. 3C)
PMID:17412958	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	(Fig. 3C)
PMID:17412958	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 3C)
PMID:17412958	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	(Fig. 3C)
PMID:17412958	FYPO:0003210	mislocalized, misoriented septum	(Fig. 3D)
PMID:17412958	FYPO:0003210	mislocalized, misoriented septum	(Fig. 3D)
PMID:17412958	FYPO:0006213	normal septum morphology	(Fig. 3D)
PMID:17412958	FYPO:0003210	mislocalized, misoriented septum	(Fig. 3D)
PMID:17434129	FYPO:0007508	increased histone H3-K9 trimethylation at subtelomeric heterochromatin during vegetative growth	(comment: TEL2L only)
PMID:17434129	FYPO:0003010	increased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_using] PomBase:SPBC28F2.12	(comment: TEL2L only)
PMID:17434129	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_using] PomBase:SPAC664.01c	(comment: TEL2L only)
PMID:17434129	GO:0006338	chromatin remodeling	(comment: also from localization and phenotypes)
PMID:17434129	GO:0006338	chromatin remodeling	(comment: also from localization and phenotypes)
PMID:17434129	FYPO:0002061	inviable vegetative cell population	data not shown
PMID:17434129	FYPO:0002061	inviable vegetative cell population	data not shown
PMID:17440621	GO:0140683	histone H3K9me/H3K9me2 demethylase activity [part_of] facultative heterochromatin formation	(comment: they only show that this is part of a complex that demethylates H3K9 so there is a chance it is not active?)
PMID:17442892	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(comment: inferred from the fact growth is impaired in the double mutant spc7-23/mad2 OR spc7-23/mph1 are growth impaired, so assumption is that spindle checkpoint is active in mutant)
PMID:17450151	FYPO:0004137	decreased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0006361	increased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0000887	increased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0002355	decreased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0003557	increased antisense RNA level	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0006987	increased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0005523	increased reverse centromeric outer repeat transcript level	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0005315	increased chromatin silencing at centromere central core	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0003547	increased DNA damage during vegetative growth	(comment: bulk antisense transcripts)
PMID:17450151	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC1783.05	(comment: sense strand)
PMID:17450151	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC6B1.07	(comment: sense strand)
PMID:17452352	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC1105.12	(Fig. 5c)
PMID:17452352	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1834.04	(Fig. 5c)
PMID:17452352	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC8D2.04	(Fig. 5c)
PMID:17452352	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC1105.11c	(Fig. 5c)
PMID:17452352	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1834.03c	(Fig. 5c)
PMID:17452352	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC8D2.03c	(Fig. 5c)
PMID:17452352	FYPO:0006412	decreased level of histone gene mRNA during mitotic S phase [assayed_using] PomBase:SPAC1834.03c	(Fig. 6)
PMID:17452352	FYPO:0006412	decreased level of histone gene mRNA during mitotic S phase [assayed_using] PomBase:SPBC1105.12	(Fig. 6)
PMID:17452352	FYPO:0006412	decreased level of histone gene mRNA during mitotic S phase [assayed_using] PomBase:SPBC1105.11c	(Fig. 6)
PMID:17452352	FYPO:0006412	decreased level of histone gene mRNA during mitotic S phase [assayed_using] PomBase:SPAC1834.04	(Fig. 6)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPBC8D2.03c	(Figure 5a)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPBC8D2.04	(Figure 5a)
PMID:17452352	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC8D2.03c	(Figure 5d)
PMID:17452352	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC1105.12	(Figure 5d)
PMID:17452352	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC1105.11c	(Figure 5d)
PMID:17452352	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1834.03c	(Figure 5d)
PMID:17452352	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1834.04	(Figure 5d)
PMID:17452352	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC8D2.04	(Figure 5d)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPAC1834.03c	(Figure 7)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPBC1105.11c	(Figure 7)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPBC8D2.04	(Figure 7)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPAC1834.04	(Figure 7)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPBC1105.12	(Figure 7)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPBC8D2.03c	(Figure 7)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPAC1834.03c	(Figure 7)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPBC1105.11c	(Figure 7)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPBC8D2.04	(Figure 7)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPAC1834.04	(Figure 7)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPBC1105.12	(Figure 7)
PMID:17452352	FYPO:0006414	increased level of histone gene mRNA during mitotic interphase [assayed_using] PomBase:SPBC8D2.03c	(Figure 7)
PMID:17452352	GO:0045944	positive regulation of transcription by RNA polymerase II	(comment: CHECK bet this is a term Val hates :p)
PMID:17452352	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1834.03c [part_of] positive regulation of transcription by RNA polymerase II [happens_during] mitotic S phase	"(comment: chromatin binding shown, and regulation of transcription shown. no evidence for dna binding BUT later paper by akayama and Toda state that "" Ams2 directly binds a consensus ""AACCCT-box"" that exists in the 5' franking regions of these histone genes."" and says that ams2 is sole responsible TF + cites this paper)"
PMID:17452352	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1834.04 [part_of] positive regulation of transcription by RNA polymerase II [happens_during] mitotic S phase	"(comment: chromatin binding shown, and regulation of transcription shown. no evidence for dna binding BUT later paper by akayama and Toda state that "" Ams2 directly binds a consensus ""AACCCT-box"" that exists in the 5' franking regions of these histone genes."" and says that ams2 is sole responsible TF + cites this paper)"
PMID:17452625	GO:1904530	negative regulation of actin filament binding	(comment: regulates binding by myosin; assayed in vitro using rabbit actin and unspecified myosin motor domain)
PMID:17486116	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(comment: CHECK assayed using bub1)
PMID:17510629	FYPO:0007656	increased nucleosome occupancy at transcription start site	Hence, from these results it was evident that Hrp1, Hrp3 and Nap1 occupancy in vivo generally correlated with increased nucleosome densities in the corresponding mutants, and that this effect was most pronounced in promoter regions.
PMID:17510629	FYPO:0007656	increased nucleosome occupancy at transcription start site	Hence, from these results it was evident that Hrp1, Hrp3 and Nap1 occupancy in vivo generally correlated with increased nucleosome densities in the corresponding mutants, and that this effect was most pronounced in promoter regions.
PMID:17510629	FYPO:0007656	increased nucleosome occupancy at transcription start site	Hence, from these results it was evident that Hrp1, Hrp3 and Nap1 occupancy in vivo generally correlated with increased nucleosome densities in the corresponding mutants, and that this effect was most pronounced in promoter regions.
PMID:17512405	FYPO:0002834	decreased chromatin silencing at centromere	(Figure 2,4)
PMID:17512405	FYPO:0002834	decreased chromatin silencing at centromere	(Figure 2,4)
PMID:17512405	FYPO:0002834	decreased chromatin silencing at centromere	(Figure 2,4)
PMID:17512405	GO:0031499	TRAMP complex	Cid14 copurified with two proteins that are homologs of Mtr4 and Air1 (Figures 4A and 4B). Thus, like Trf4 in S. cerevisiae, Cid14 is found in a complex together with Air1 and Mtr4, which we refer to as spTRAMP (S. pombe TRAMP).
PMID:17512405	GO:0031499	TRAMP complex	Cid14 copurified with two proteins that are homologs of Mtr4 and Air1 (Figures 4A and 4B). Thus, like Trf4 in S. cerevisiae, Cid14 is found in a complex together with Air1 and Mtr4, which we refer to as spTRAMP (S. pombe TRAMP).
PMID:17512405	GO:0031499	TRAMP complex	Cid14 copurified with two proteins that are homologs of Mtr4 and Air1 (Figures 4A and 4B). Thus, like Trf4 in S. cerevisiae, Cid14 is found in a complex together with Air1 and Mtr4, which we refer to as spTRAMP (S. pombe TRAMP).
PMID:17512405	FYPO:0004982	increased centromeric transcript level [has_severity] low	Consistent with a role for the exosome in degrading heterochromatic ura4+ transcripts, we observed elevated ura4+ transcript levels in rrp6D compared to wild-type cells (Figures 4C-4E).
PMID:17512405	FYPO:0006995	normal chromatin silencing at centromere inner repeat	Finally, deletion of the other four members of the fission yeast Cid14/Trf4/5 poly(A) polymerase family did not affect silencing of an imr1R::ura4+ reporter gene (Figure 2H).
PMID:17512405	FYPO:0006995	normal chromatin silencing at centromere inner repeat	Finally, deletion of the other four members of the fission yeast Cid14/Trf4/5 poly(A) polymerase family did not affect silencing of an imr1R::ura4+ reporter gene (Figure 2H).
PMID:17512405	FYPO:0006995	normal chromatin silencing at centromere inner repeat	Finally, deletion of the other four members of the fission yeast Cid14/Trf4/5 poly(A) polymerase family did not affect silencing of an imr1R::ura4+ reporter gene (Figure 2H).
PMID:17512405	FYPO:0006995	normal chromatin silencing at centromere inner repeat	Finally, deletion of the other four members of the fission yeast Cid14/Trf4/5 poly(A) polymerase family did not affect silencing of an imr1R::ura4+ reporter gene (Figure 2H).
PMID:17512405	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC28F2.12	Furthermore, consistent with a CTGS model for silencing of mat3M::ura4+, none of the tested mutants affected RNApII occupancy at this locus (Figure 3C).
PMID:17512405	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	However, we observed loss of silencing of mat3M:::ura4+ in cells carrying a hypomorphic allele of mtr4+ (mtr4-1, Figures 4F and 4H), suggesting the involvement of a TRAMP-like complex.
PMID:17512405	FYPO:0008056	abolished poly(A)-specific ribonuclease activity [assayed_enzyme] PomBase:SPAC12G12.13c	Importantly, Cid14 activity was completely abolished in Cid14DADA (Figure 5B)
PMID:17512405	FYPO:0003231	decreased histone H3-K9 methylation at heterochromatin domain during vegetative growth [has_severity] low	In addition, while H3K9 methylation was lost in clr4D cells, only a slight reduction in H3K9 methylation was observed in cid14D cells (Figures 3A and 3B)
PMID:17512405	GO:1990817	poly(A) RNA polymerase activity	In order to directly determine whether Cid14 is a bona fide poly(A) polymerase, we assayed recombinant wild-type or mutant Cid14 (GST-Cid14wt or GST-Cid14DADA, respectively; Figure 5A) for polyadenylation activity in vitro and found that wild-type Cid14 was able to extend a synthetic oligo(A)15 RNA but not an oligo(dA)15 DNA substrate (Figures 5B, 5C, and 5E).
PMID:17512405	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] high	Like cid14D, Cid14 active site mutations had dramatically reduced centromeric siRNA levels (Figure 6D)
PMID:17512405	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	Loss of imr1R::ura4+ and mat3M::ura4+ silencing in cid14D cells could be rescued by overexpressing Cid14wt (pRep- Cid14) but not by Cid14DADA (pRep-Cid14DADA) (Figure 5F).
PMID:17512405	GO:0035197	siRNA binding	Quantification of the signals revealed that Ago1 contained about 3-fold more antisense than sense ura4+ siRNAs. etc....(Figure 1)
PMID:17512405	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPAC18G6.02c	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was significantly reduced at several heterochromatic loci, including mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Figures 3A and 3B).
PMID:17512405	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPAC664.01c	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was significantly reduced at several heterochromatic loci, including mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Figures 3A and 3B).
PMID:17512405	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_protein] PomBase:SPAC18G6.02c	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was significantly reduced at several heterochromatic loci, including mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Figures 3A and 3B).
PMID:17512405	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_protein] PomBase:SPAC664.01c	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was significantly reduced at several heterochromatic loci, including mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Figures 3A and 3B).
PMID:17512405	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was significantly reduced at several heterochromatic loci, including mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Figures 3A and 3B).
PMID:17512405	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC18G6.02c	Surprisingly, in cid14D cells, neither Chp1 nor Swi6 binding was significantly reduced at several heterochromatic loci, including mat3M::ura4+, imr1R::ura4+, the subtelomeric tlh1+ gene, and cen-dg and cen-dh repeats, as assayed by chromatin immunoprecipitation experiments (ChIP) (Figures 3A and 3B).
PMID:17512405	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	We found that deletion of cid14+ resulted in a complete loss of ura4+ silencing at all the tested loci as assayed by growth on 5-FOA-containing medium (Figures 2A-2C).
PMID:17512405	FYPO:0007335	abolished chromatin silencing at centromere inner repeat	We found that deletion of cid14+ resulted in a complete loss of ura4+ silencing at all the tested loci as assayed by growth on 5-FOA-containing medium (Figures 2A-2C).
PMID:17512405	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	We found that deletion of cid14+ resulted in a complete loss of ura4+ silencing at all the tested loci as assayed by growth on 5-FOA-containing medium (Figures 2A-2C).
PMID:17512405	FYPO:0002335	normal chromatin silencing	We found that the deletion of air1+ had no effect on heterochromatic gene silencing (Figure S2
PMID:17512405	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] high	While we were not able to detect any centromeric siRNAs in cid12D cells, centromeric siRNAs were about 22-fold reduced in cid14D compared to wild-type cells (Figure 6B). and However, centromeric siRNAs from cid14D were barely detectable on total RNA northern blots (Figure 6A).
PMID:17512405	FYPO:0004573	increased telomeric transcript level [has_severity] high [assayed_transcript] PomBase:SPAC212.11	we observed 7-fold and a 25-fold increases in tlh1+ transcript levels in rrp6D and dis3-54 cells, respectively, and 33- and 100- fold increases in cid14D and clr4D cells, respectively (Figures 4G and S3)
PMID:17512405	FYPO:0004573	increased telomeric transcript level [has_severity] high [assayed_transcript] PomBase:SPAC212.11	we observed 7-fold and a 25-fold increases in tlh1+ transcript levels in rrp6D and dis3-54 cells, respectively, and 33- and 100- fold increases in cid14D and clr4D cells, respectively (Figures 4G and S3)
PMID:17512405	FYPO:0004604	decreased chromatin silencing at subtelomere	we observed 7-fold and a 25-fold increases in tlh1+ transcript levels in rrp6D and dis3-54 cells, respectively, and 33- and 100- fold increases in cid14D and clr4D cells, respectively (Figures 4G and S3)
PMID:17512405	FYPO:0004573	increased telomeric transcript level [has_severity] low [assayed_transcript] PomBase:SPAC212.11	we observed 7-fold and a 25-fold increases in tlh1+ transcript levels in rrp6D and dis3-54 cells, respectively, and 33- and 100- fold increases in cid14D and clr4D cells, respectively (Figures 4G and S3)
PMID:17512405	FYPO:0004573	increased telomeric transcript level [assayed_transcript] PomBase:SPAC212.11 [has_severity] low	we observed a 3-fold increase in tlh1+ RNA levels in dcr1D cells and a 10-fold increase in mtr4-1 cells (Figures 4F and 4H), indicating that both RNAi and TRAMP contribute to the full silencing of this subtelomeric gene.
PMID:17512405	FYPO:0004573	increased telomeric transcript level [assayed_transcript] PomBase:SPAC212.11 [has_severity] low	we observed a 3-fold increase in tlh1+ RNA levels in dcr1D cells and a 10-fold increase in mtr4-1 cells (Figures 4F and 4H), indicating that both RNAi and TRAMP contribute to the full silencing of this subtelomeric gene.
PMID:17531813	FYPO:0001974	increased number of cells with 1C DNA content [has_severity] high	(Fig. 1B)
PMID:17531813	FYPO:0001974	increased number of cells with 1C DNA content [has_severity] high	(Fig. 1B)
PMID:17531813	FYPO:0001974	increased number of cells with 1C DNA content [has_severity] high	(Fig. 1C)
PMID:17531813	FYPO:0001490	inviable elongated vegetative cell [has_severity] high	(Fig. 1C)
PMID:17531813	FYPO:0004359	abolished mitotic cell cycle DNA replication checkpoint [has_severity] high	(Fig. 1C)
PMID:17531813	FYPO:0001974	increased number of cells with 1C DNA content [has_severity] high	(Fig. 1C)
PMID:17531813	FYPO:0000950	elongated aseptate vegetative cell [has_severity] high	(Fig. 1C) (comment: vw data not shown, but assume are elongated)
PMID:17531813	GO:0000785	chromatin [exists_during] mitotic S phase	(Fig. 2A)
PMID:17531813	GO:0000785	chromatin [exists_during] mitotic S phase	(Fig. 2A) (comment: CHECK during mitotic DNA replication checkpoint)
PMID:17531813	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC14C8.07c [assayed_using] PomBase:SPAC9E9.08	(Fig. 4A)
PMID:17531813	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC14C8.07c [assayed_using] PomBase:SPAC9E9.08 [has_severity] high	(Fig. 4A)
PMID:17531813	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC216.05 [assayed_using] PomBase:SPBC14C8.07c	(Fig. 4A)
PMID:17531813	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC216.05 [assayed_using] PomBase:SPBC14C8.07c	(Fig. 4A)
PMID:17531813	FYPO:0001678	abolished protein localization to chromatin [assayed_using] PomBase:SPBC216.05	(Fig. 4D) In the absence of rad26, cdc18 is unable to stabilise rad3 on chromatin
PMID:17531813	FYPO:0006291	increased protein level during mitotic G2 phase [assayed_using] PomBase:SPBC14C8.07c [has_penetrance] high	(Fig. 5A) cdc18 disappears at the end of S-phase in cig2+ strain and accumulates in the absence of cig2
PMID:17531813	FYPO:0006290	normal protein phosphorylation during mitotic S phase during cellular response to hydroxyurea [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Fig. 5B)
PMID:17531813	FYPO:0001430	abnormal mitotic cell cycle arrest with unreplicated DNA [has_penetrance] high	(Fig. 5B)
PMID:17531813	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 32	(Fig. 6B)
PMID:17531813	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09	(Fig. 6B)
PMID:17531813	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPBC14C8.07c [has_penetrance] high	(Fig. 6B)
PMID:17531813	FYPO:0004083	normal protein level [assayed_using] PomBase:SPBC216.05	(Figure 2B) In the cytosol rad3 is present in absence of cdc18
PMID:17531813	FYPO:0002577	decreased chromatin binding [assayed_using] PomBase:SPBC216.05 [has_severity] high	(Figure 2B) rad3 is not present in the chromatin fraction in the absence of cdc18
PMID:17531813	FYPO:0002679	decreased protein phosphorylation [has_severity] high [assayed_using] PomBase:SPCC18B5.11c	(Figure 2C) cds1 is no longer phosphorylated because rad3 is absent in absence of cdc18
PMID:17531813	FYPO:0003075	normal protein kinase activity [has_severity] high [assayed_enzyme] PomBase:SPBC11B10.09	(Figure 2D)
PMID:17531813	FYPO:0005107	normal regulation of mitotic DNA replication initiation [has_severity] high	(Figure 3) Replication Structures Are Not Lost When Cdc18 Is Depleted)
PMID:17531813	FYPO:0006291	increased protein level during mitotic G2 phase [assayed_using] PomBase:SPAPB2B4.03	The same experiment was repeated, but HU was added at the time of release, allowing cells to progress through mitosis and stall after initiation of DNA replication. In that case, Cdc2 tyrosine 15 phosphorylation reappeared after 100 min and increased further with time. Cig2 remained present at a high level, indicating that the Cdc2-Cig2 complex was inhibited (Figure 5B)
PMID:17531816	FYPO:0003098	abnormal heterochromatin assembly at centromere outer repeat during vegetative growth	(comment: de novo)
PMID:17531816	FYPO:0004744	normal heterochromatin maintenance involved in chromatin silencing at centromere outer repeat	(comment: de novo)
PMID:17531816	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(dg repeat) Centromeric transcripts were only marginally elevated in tas3WG cells, in marked contrast to the 10- to 20-fold accumulation of transcripts in tas3-, dcr1-, or ago1-null cells (Figure 2B).
PMID:17531816	FYPO:0005930	normal chromatin binding at centromere outer repeat [assayed_protein] PomBase:SPAC18G6.02c	......as were Chp1 and the mutant Tas3WG protein (Figure 2C).
PMID:17531816	FYPO:0005930	normal chromatin binding at centromere outer repeat [assayed_protein] PomBase:SPBC83.03c	......as were Chp1 and the mutant Tas3WG protein (Figure 2C).
PMID:17531816	FYPO:0005930	normal chromatin binding at centromere outer repeat [assayed_protein] PomBase:SPCC736.11	Chromatin immunoprecipitation (ChIP) analyses showed that Ago1 was indeed localized at centromeres in the tas3WG mutant, a
PMID:17531816	FYPO:0001513	normal mitotic sister chromatid segregation	Consistent with these findings, tas3WG mutant cells showed no defects in chromosome segregation (Table S2).
PMID:17531816	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	F276A-ago1 (Figure S3B) caused a slight defect in silencing of the dg cen::ura4+ reporter (Figure S3C).
PMID:17531816	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	Further, centromeric siRNAs were similarly abundant in tas3WG and tas3+ cells (Figure 2D).
PMID:17531816	GO:0031508	pericentric heterochromatin formation	The reestablishmentof centromeric heterochromatin was then monitored after reintroduction of clr4+. Addition of clr4+to tas3+ cells allowed efficient establishment of heterochromatinand silencing of the cen::ura4+ transgene atdg (Figure 3A). In marked contrast, on reintroduction ofclr4+, cells expressing tas3WG failed to silence the cen::ura4+ reporter
PMID:17531816	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPAC18G6.02c	We have previously demonstrated that Tas3 binds directly to Chp1 (Petrie et al., 2005). In addition, Tas3 binds to Ago1 and this interaction is independent of Chp1 (Figure 1A). Thus, Tas3 forms a bridge linking the Chp1 chromodomain protein to Ago1.
PMID:17531816	FYPO:0006076	siRNA absent from cell	centromeric siRNAs were present in the F276Aago1 and tas3WG single mutants but were undetectable in the double mutant (Figure 2F).
PMID:17531816	FYPO:0003241	unequal mitotic sister chromatid segregation	centromeric siRNAs were present in the F276Aago1 and tas3WG single mutants but were undetectable in the double mutant (Figure 2F).
PMID:17531816	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	the double mutant (tas3WG, F276Aago1) displayed markedly elevated levels of total centromeric transcripts (Figure 2E), similar to an ago1 null.
PMID:17538026	FYPO:0002023	abnormal septum morphology during vegetative growth [has_penetrance] 10	(Fig. 1, 2)
PMID:17538026	FYPO:0002023	abnormal septum morphology during vegetative growth [has_penetrance] 50-60	(Fig. 1, 2)
PMID:17538026	FYPO:0004506	abnormal nucleolar chromatin organization resulting in peripheral chromatin distribution	(Fig. 1B)
PMID:17538026	FYPO:0004506	abnormal nucleolar chromatin organization resulting in peripheral chromatin distribution	(Fig. 1B)
PMID:17538026	FYPO:0002060	viable vegetative cell population	(Fig. 1a)
PMID:17538026	FYPO:0002060	viable vegetative cell population	(Fig. 1a)
PMID:17538026	FYPO:0002061	inviable vegetative cell population	(Fig. 1a)
PMID:17538026	FYPO:0002060	viable vegetative cell population	(Fig. 1a)
PMID:17538026	GO:0005730	nucleolus	(Fig. 3a)
PMID:17538026	FYPO:0003688	abolished protein localization to nucleolus [assayed_using] PomBase:SPBC25D12.02c	(Fig. 4)
PMID:17538026	FYPO:0003688	abolished protein localization to nucleolus [assayed_using] PomBase:SPBC25D12.02c	(Fig. 4)
PMID:17538026	FYPO:0003688	abolished protein localization to nucleolus [assayed_using] PomBase:SPBC4C3.05c	(Fig. 4)
PMID:17538026	FYPO:0005714	premature protein localization to nucleolus [assayed_using] PomBase:SPAC1782.09c	(Fig. 6B)
PMID:17538026	FYPO:0005714	premature protein localization to nucleolus [assayed_using] PomBase:SPAC1782.09c	(Fig. 6B)
PMID:17538026	GO:0005730	nucleolus	(Figure 3, B and D)
PMID:17538026	GO:0072686	mitotic spindle [exists_during] mitotic anaphase B	(Figure 3, B and D)
PMID:17538026	FYPO:0002061	inviable vegetative cell population	(Table 2)
PMID:17538026	FYPO:0002061	inviable vegetative cell population	(Table 2)
PMID:17556368	FYPO:0001573	increased RNA level during cellular response to rapamycin [assayed_using] PomBase:SPAC1039.09	(comment: CHECK get double mutant phenotypes)
PMID:17556368	FYPO:0001573	increased RNA level during cellular response to rapamycin [assayed_using] PomBase:SPBC29B5.02c	(comment: CHECK get double mutant phenotypes)
PMID:17556368	FYPO:0001573	increased RNA level during cellular response to rapamycin [assayed_using] PomBase:SPAP7G5.06	(comment: CHECK get double mutant phenotypes)
PMID:17556368	FYPO:0001573	increased RNA level during cellular response to rapamycin [assayed_using] PomBase:SPAC869.10c	(comment: CHECK get double mutant phenotypes)
PMID:17561805	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(comment: tested through observing no delay when checkpoint is inactivated)
PMID:17579515	FYPO:0000619	abnormal cell cycle arrest in mitotic anaphase	(APC) activation occurred and chromosome cohesion was lost (Figure 1A and 1B).
PMID:17579515	FYPO:0004536	abnormal response to mitotic cell cycle spindle assembly checkpoint signaling	(APC) activation occurred and chromosome cohesion was lost (Figure 1A and 1B).
PMID:17579515	FYPO:0000276	monopolar mitotic spindle [has_penetrance] 50	(Fig. 4G)
PMID:17579515	FYPO:0002061	inviable vegetative cell population	(Fig. S1)
PMID:17579515	FYPO:0000276	monopolar mitotic spindle [has_penetrance] 7	(Figure 1).
PMID:17579515	FYPO:0003787	long mitotic spindle microtubules protruding beyond spindle pole body	(Figure 2C)
PMID:17579515	FYPO:0001734	abolished mitotic spindle pole body separation	(Figure 3A and 3B, and Video S3)
PMID:17579515	FYPO:0001513	normal mitotic sister chromatid segregation [has_penetrance] 10	(Figure 6C)
PMID:17579515	FYPO:0001513	normal mitotic sister chromatid segregation [has_penetrance] 30	(Figure 6C)
PMID:17579515	FYPO:0004396	normal mitotic spindle elongation	(Figure S4)
PMID:17579515	FYPO:0005380	normal mitotic spindle pole body duplication	(Figure S4; Figure 3A,B; Video S3)
PMID:17596513	GO:0004311	geranylgeranyl diphosphate synthase activity [part_of] farnesyl diphosphate biosynthetic process, mevalonate pathway	(comment: E. coli ispA mutant used as assay system)
PMID:17596513	GO:0004311	geranylgeranyl diphosphate synthase activity [part_of] farnesyl diphosphate biosynthetic process, mevalonate pathway	(comment: E. coli ispA mutant used as assay system)
PMID:17596513	GO:0004337	(2E,6E)-farnesyl diphosphate synthase activity [part_of] farnesyl diphosphate biosynthetic process, mevalonate pathway	(comment: E. coli ispA mutant used as assay system)
PMID:17614284	FYPO:0001357	normal vegetative cell population growth	(Fig. 2A)
PMID:17614284	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 2A)
PMID:17614284	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	(Fig. 2A)
PMID:17614284	FYPO:0003217	decreased chromatin silencing at centromere central core [has_severity] low	(Fig. 2B)
PMID:17614284	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] medium	(Fig. 2B)
PMID:17614284	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] low	(Fig. 2B)
PMID:17614284	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 2C)
PMID:17614284	FYPO:0008265	normal chromatin silencing at rDNA	(Fig. 2C)
PMID:17614284	FYPO:0003555	normal chromatin silencing at subtelomere	(Fig. 2C)
PMID:17614284	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 10	(Fig. 3A, B)
PMID:17614284	FYPO:0005372	increased circular minichromosome loss during vegetative growth [has_penetrance] 56	(Fig. 3C)
PMID:17614284	FYPO:0005371	increased linear minichromosome loss during vegetative growth [has_penetrance] 1	(Fig. 3C)
PMID:17614284	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 3D)
PMID:17614284	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 4C)
PMID:17614284	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 4C)
PMID:17614284	FYPO:0002150	inviable spore population	(Fig. S3)
PMID:17614284	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. S6A)
PMID:17614284	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. S6B)
PMID:17614284	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(Fig. S6C)
PMID:17614284	FYPO:0000084	sensitive to 6-azauracil [has_severity] low	(Fig. S6D)
PMID:17614284	FYPO:0000084	sensitive to 6-azauracil [has_severity] low	(Fig. S6D)
PMID:17614284	FYPO:0000084	sensitive to 6-azauracil [has_severity] medium	(Fig. S6D)
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC965.07c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC19G12.09	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB1A11.03	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1739.08c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC22F8.05	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPJ4664.02	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC9E9.04	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1834.10c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC750.07c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC212.08c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC212.06c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC29A4.06c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1002.17c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1002.19	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC212.11	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1F8.03c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC19B12.09	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC22F8.12c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC22F8.08	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC637.10c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1921.06c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC365.20c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC557.03c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC338.12	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB2B2.01	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC12B10.10	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC17C9.02c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC9E9.03	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC144.14	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAP8A3.04c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC3E7.02c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC11H11.05c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1683.09c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1F7.07c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1F7.08	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC27B12.03c	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1782.01	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.01	Table S1
PMID:17614284	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC6F6.08c	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC8E11.10	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC694.03	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC3B9.10	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1B3.16c	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC146.08c	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC29B12.04	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP23A10.03c	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP22H7.08	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC5D6.05	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC622.19	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC965.14c	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC644.05c	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1709.06	Table S1
PMID:17614284	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC926.05c	Table S1
PMID:17632059	FYPO:0000590	normal sporulation [has_penetrance] ~95	(Fig. 1B)
PMID:17632059	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] ~25	(Fig. 1B)
PMID:17632059	FYPO:0000590	normal sporulation [has_penetrance] ~75	(Fig. 1B)
PMID:17632059	FYPO:0000590	normal sporulation [has_penetrance] ~18	(Fig. 1B)
PMID:17632059	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] ~82	(Fig. 1B)
PMID:17632059	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] ~82	(Fig. 1B)
PMID:17632059	FYPO:0000590	normal sporulation [has_penetrance] ~42	(Fig. 1B)
PMID:17632059	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] ~58	(Fig. 1B)
PMID:17632059	FYPO:0000590	normal sporulation [has_penetrance] ~18	(Fig. 1B)
PMID:17632059	FYPO:0000590	normal sporulation [has_penetrance] ~55	(Fig. 1b)
PMID:17632059	FYPO:0000590	normal sporulation [has_penetrance] ~39	(Fig. 1b)
PMID:17632059	FYPO:0004077	abnormal sporulation resulting in formation of ascus with single large spore	(Fig. 1b)
PMID:17632059	FYPO:0000681	abnormal sporulation resulting in formation of two-spore ascus	(Fig. 1c)
PMID:17632059	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] ~61	(Fig. 1c)
PMID:17632059	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] ~45	(Fig. 1c)
PMID:17632059	FYPO:0000485	decreased meiotic recombination	(Fig. 1c)
PMID:17632059	FYPO:0000485	decreased meiotic recombination	(Fig. 1c)
PMID:17632059	FYPO:0000485	decreased meiotic recombination	(Fig. 1c)
PMID:17632059	FYPO:0000681	abnormal sporulation resulting in formation of two-spore ascus	(Fig. 1e) (comment: twice their share of DNA and SPBs.)
PMID:17632059	FYPO:0006383	abnormal sporulation resulting in formation of ascus containing non-uniform spores and unencapsulated DNA	(Fig. 1f)
PMID:17632059	FYPO:0006363	monopolar spindle during meiosis I [has_penetrance] ~19	(Fig. 3)
PMID:17632059	FYPO:0006363	monopolar spindle during meiosis I	(Fig. 3)
PMID:17632059	FYPO:0006394	abnormal meiotic spindle localization [has_penetrance] ~2	(Fig. 3)
PMID:17632059	FYPO:0005652	abnormal spindle morphology during meiosis I [has_penetrance] 37	(Fig. 3)
PMID:17632059	FYPO:0006390	multiple meiotic spindles [has_penetrance] ~4	(Fig. 3) (comment: V-shaped patterns indicating multiple spindles)
PMID:17632059	FYPO:0003614	meiotic spindle absent from cell during meiosis II [has_penetrance] ~13	(Fig. 3D)
PMID:17632059	FYPO:0006391	meiotic spindle absent from cell during meiosis [has_penetrance] ~13	(Fig. 3D) (I)
PMID:17632059	FYPO:0000927	abolished horsetail movement	(Fig. S3)
PMID:17632059	FYPO:0003835	normal horsetail movement	(Fig. S3)
PMID:17632059	FYPO:0003835	normal horsetail movement	(Fig. S3)
PMID:17632059	FYPO:0002890	abnormal horsetail nucleus morphology	(Fig. S3)
PMID:17632059	FYPO:0000927	abolished horsetail movement	(Fig. S3)
PMID:17632059	FYPO:0000927	abolished horsetail movement	(Fig. S3)
PMID:17632059	FYPO:0002890	abnormal horsetail nucleus morphology	(Fig. S3)
PMID:17632059	FYPO:0006364	spindle microtubules detached from spindle pole body during meiosis I [has_penetrance] 13	(Fig. s4e, movie S2)
PMID:17632059	FYPO:0006365	meiotic spindle pole body detached from nucleus	(comment: CHECK Matching synonym SPB detached from nucleuss fix syn)
PMID:17632059	FYPO:0006389	normal meiotic spindle pole body oscillation during prophase I	In taz1Dlig4D zygotes, SPBs move normally during the horsetail stage even though they are rarely associated with chromatin. However, as the horsetail stage ends and meiosis I begins, the Pcp1-GFP signals appear brighter than in WT cells and are markedly disorganized (Figure 2B; 75 min
PMID:17632059	FYPO:0000737	abnormal meiotic spindle assembly [has_penetrance] 37	Table S3
PMID:17632059	FYPO:0000734	abnormal meiotic spindle [has_penetrance] 50	Table S3
PMID:17632059	FYPO:0000737	abnormal meiotic spindle assembly [has_penetrance] 46	Table S3
PMID:17632059	FYPO:0000737	abnormal meiotic spindle assembly [has_penetrance] 57	Table S3
PMID:17632059	FYPO:0000737	abnormal meiotic spindle assembly [has_penetrance] 75	Table S3
PMID:17677001	FYPO:0003217	decreased chromatin silencing at centromere central core	(Figure 2A)
PMID:17677001	FYPO:0003217	decreased chromatin silencing at centromere central core	(Figure 2A)
PMID:17677001	FYPO:0003217	decreased chromatin silencing at centromere central core	(Figure 2A)
PMID:17677001	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPAC1834.04	(Figure 2B)
PMID:17677001	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC1105.11c	(Figure 2B)
PMID:17677001	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC8D2.04	(Figure 2B)
PMID:17677001	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPAC1834.04	(Figure 2B)
PMID:17677001	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC1105.11c	(Figure 2B)
PMID:17677001	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC8D2.04	(Figure 2B)
PMID:17677001	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPAC1834.04	(Figure 2B)
PMID:17677001	FYPO:0004313	decreased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC1105.17	(Figure 2B)
PMID:17677001	FYPO:0004313	decreased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC1105.17	(Figure 2B)
PMID:17677001	FYPO:0004313	decreased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC1105.17	(Figure 2B)
PMID:17677001	FYPO:0004313	decreased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC1105.17	(Figure 2B)
PMID:17677001	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPAC1834.04	(Figure 2B)
PMID:17677001	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC1105.11c	(Figure 2B)
PMID:17677001	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC8D2.04	(Figure 2B)
PMID:17677001	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC1105.11c	(Figure 2B)
PMID:17677001	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC8D2.04	(Figure 2B)
PMID:17677001	FYPO:0004331	normal chromatin silencing at centromere central core	(Figure 3A) EXP says increased, but is normal compared to WT (i.e ura4 insertion derepresses)
PMID:17677001	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC1105.17	(Figure 3B)
PMID:17677001	FYPO:0003410	increased spatial extent of CENP-A containing chromatin assembly [assayed_using] PomBase:SPBC1105.17	(Figure 3C) spreading is still within the central domain, to the flanking tRNAs
PMID:17677001	FYPO:0007234	normal protein localization to centromere central core [assayed_using] PomBase:SPAC1834.04	(Figure 4B)
PMID:17677001	FYPO:0007234	normal protein localization to centromere central core [assayed_using] PomBase:SPBC1105.17	(Figure 4C)
PMID:17677001	GO:0061638	CENP-A containing chromatin	(Figure S1)
PMID:17677001	FYPO:0000228	lagging mitotic chromosomes [assayed_using] PomBase:SPBC1105.17	(Figure S8)
PMID:17690116	FYPO:0004474	normal mitotic cell cycle DNA replication checkpoint [has_penetrance] high	(Fig. 1B) At 25°C the permissive temperature rad3ts the checkpoint is active and cells expressing the mutant form of pREP4X cdc18 from the screen elongate
PMID:17690116	FYPO:0004359	abolished mitotic cell cycle DNA replication checkpoint [has_penetrance] high	(Fig. 1B) At 36°C the restrictive temperature for rad3ts the checkpoint is inactive and cells expressing the mutant form of pREP4X cdc18 from the screen do not elongate and are able to form colonies
PMID:17690116	FYPO:0001383	normal DNA content [has_penetrance] high	(Fig. 1C) rad3ts cells over expressing the mutated pREP4X-cdc18 construct do not rereplicate at 25°C or 36°C (the permissive and non permissive temperatures for rad3ts). This is in contrast to Control cells expressing cdc18+ from pREP3X promoter at 32°C (Fig1D , Table 2) which don't activate the mitotic DNA checkpoint and undergo DNA re-replicatiom
PMID:17690116	FYPO:0001383	normal DNA content [has_penetrance] high	(Fig. 1C) rad3ts cells over expressing the mutated pREP4X-cdc18 construct do not rereplicate at 25°C or 36°C (the permissive and non permissive temperatures for rad3ts). This is in contrast to Control cells expressing cdc18+ from pREP3X promoter at 32°C (Fig1D , Table 2) which don't activate the mitotic DNA checkpoint and undergo DNA re-replicatiom
PMID:17690116	FYPO:0001221	normal nucleus:cytoplasm ratio [has_penetrance] high	(Fig. 2 A,C) (comment: cells arrested due to active rad3)
PMID:17690116	FYPO:0001122	elongated vegetative cell [has_penetrance] high [has_severity] high	(Fig. 2A) (cdc18T6A expression at 25°C causes cell elongation due to activation of the mitotic DNA replication checkpoint -permissive temperature for rad3ts)
PMID:17690116	FYPO:0002176	viable vegetative cell with normal cell size [has_penetrance] high	(Fig. 2A) (comment: non permissive temperature for rad3ts )
PMID:17690116	FYPO:0001221	normal nucleus:cytoplasm ratio [has_penetrance] high	(Fig. 2A,C)
PMID:17690116	FYPO:0001383	normal DNA content [has_penetrance] high	(Fig. 2B) (comment: cells arrested due to activation of the rad3 checkpoint gene do not rereplicate)
PMID:17690116	FYPO:0007510	cell cycle arrest at mitotic G2/M phase transition in absence of mitotic DNA replication checkpoint [has_penetrance] high	(Fig. 2D) (comment: different to when pREP3X cdc18+ is over expressed in G2 block which show replicate intermediates and cells undergo re replication)
PMID:17690116	FYPO:0000836	increased protein level [has_penetrance] high [assayed_using] PomBase:SPBC14C8.07c [has_severity] medium	(Fig. 3) (comment: CHECK This is the mutant form of pREP4X cdc18 from the screen)
PMID:17690116	FYPO:0000836	increased protein level [has_penetrance] high [assayed_using] PomBase:SPBC14C8.07c [has_severity] high	(Fig. 3) cdc18 expressed from pREP3X is at a high level. They argue that higher levels cdc18 lead to rereplication and lower levels lead to a rad3 dependent block but no rereplication
PMID:17690116	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC14C8.07c [has_severity] low	(Fig. 3) lack of re replication with moderate increase in cdc18 protein level
PMID:17690116	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC14C8.07c [has_severity] medium	(Fig. 3) lack of re replication with moderate increase in cdc18 protein level
PMID:17690116	FYPO:0007511	normal mitosis following cell cycle arrest in response to mitotic DNA replication checkpoint [has_penetrance] high	(Fig. 4A)
PMID:17690116	FYPO:0002177	viable vegetative cell with normal cell morphology [has_penetrance] high	(Fig. 4C) (comment: At 25°C rad3 is active but checkpoint cannot be activated in absence of crb2)
PMID:17690116	FYPO:0002177	viable vegetative cell with normal cell morphology [has_penetrance] high	(Fig. 4C) (comment: At 25°C rad3 is active but checkpoint cannot be activated in absence of rad1)
PMID:17690116	FYPO:0002177	viable vegetative cell with normal cell morphology [has_penetrance] high	(Fig. 4C) (comment: At 25°C rad3 is active but checkpoint cannot be activated in absence of rad17)
PMID:17690116	FYPO:0002177	viable vegetative cell with normal cell morphology [has_penetrance] high	(Fig. 4C) (comment: At 25°C rad3 is active but checkpoint cannot be activated in absence of rad26)
PMID:17690116	FYPO:0002177	viable vegetative cell with normal cell morphology [has_penetrance] high	(Fig. 4C) (comment: At 25°C rad3 is active but checkpoint cannot be activated in absence of rad9)
PMID:17690116	FYPO:0002177	viable vegetative cell with normal cell morphology [has_penetrance] high	(Fig. 4C) (comment: At the permissive temperature 25*C rad3 is active but checkpoint cannot be activated in absence of chk1)
PMID:17690116	FYPO:0001122	elongated vegetative cell [has_penetrance] high	(Fig. 4C) (comment: at 25°C rad3ts is active and the checkpoint is activated in absence of cds1)
PMID:17690116	FYPO:0001122	elongated vegetative cell [has_penetrance] high	(Fig. 4C) (comment: at the permissive temperature rad3ts is active and the checkpoint is activated in absence of mrc1)
PMID:17690116	FYPO:0002176	viable vegetative cell with normal cell size	(Fig. 4C) At 25°C rad3 is active but checkpoint cannot be activated in absence of hus1
PMID:17690116	FYPO:0001532	normal duration of mitotic S phase [has_penetrance] high	(Fig. 5A)
PMID:17690116	FYPO:0000411	normal mitotic cell cycle [has_penetrance] high	(Fig. 5B)
PMID:17690116	FYPO:0006291	increased protein level during mitotic G2 phase [has_penetrance] high	(Fig. 5C)
PMID:17690116	FYPO:0006114	increased protein level during mitotic S phase [has_penetrance] high	(Fig. 5C)
PMID:17690116	FYPO:0007512	abnormal chromosome III morphology [has_penetrance] high	(Fig. 6A, B)
PMID:17690116	FYPO:0007512	abnormal chromosome III morphology [has_penetrance] high	(Fig. 6A,B)
PMID:17690116	FYPO:0007512	abnormal chromosome III morphology [has_penetrance] high [has_severity] high	(Fig. 6C) shows Chromosome III smear is present throughout the cell cycle
PMID:17690116	FYPO:0006494	decreased rDNA copy number during vegetative growth	(Fig. 7A, B, C) after crossing out of cdc18TA6 chromosome size is stabilised and a single band is seen on PFGE which varies in size. If strains with larger Chr III are culture for <30 generations Chromosome III gradually reduces in size
PMID:17690116	FYPO:0007513	increased rDNA copy number during vegetative growth	(Fig. 8A, B)
PMID:17690116	FYPO:0000361	abnormal nucleolar morphology [has_penetrance] high	(Fig. 9A)
PMID:17690116	FYPO:0001122	elongated vegetative cell [has_severity] medium	(Fig. 9B, C) rad52D reduces amount inappropriate recombination at DNA repeats leading to a reduction in cell elongation during checkpoint activation
PMID:17690116	FYPO:0001122	elongated vegetative cell [has_severity] low	(Fig. 9B, C) reb1D reduces amount inappropriate recombination at DNA repeats leading to a reduction in cell elongation during checkpoint activation
PMID:17690116	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC14C8.07c [has_severity] medium	(comment: The western blot in Fig 3 actually shows the TAP tagged version but they use the two strains interchangeable so don't actually show data for this strain CCL9)
PMID:17868468	GO:0006264	mitochondrial DNA replication	(comment: deleted existing genome maintence term, and annotated this instead, all things considered...)
PMID:17881496	FYPO:0001779	abnormal centromere clustering at nuclear periphery during vegetative growth [has_penetrance] 9.1	(Fig. 1A)
PMID:17881496	FYPO:0003302	nucleus mislocalized towards cell tip during mitotic interphase	(Fig. 1B)
PMID:17881496	GO:1990942	mitotic metaphase chromosome recapture	(Fig. 3A)
PMID:17881496	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	(Figure 3A)
PMID:17881496	FYPO:0005719	abolished mitotic metaphase chromosome recapture	(Figure 3A)
PMID:17881496	FYPO:0005719	abolished mitotic metaphase chromosome recapture	(comment: CHECK ABOLISHED Figure 3B)
PMID:17881729	GO:0004707	MAP kinase activity [has_input] PomBase:SPBC29B5.01 [part_of] positive regulation of cell wall organization or biogenesis	(comment: the evidence isn't great)
PMID:17933563	GO:0042973	glucan endo-1,3-beta-D-glucosidase activity	(Figure 1a)
PMID:17936710	GO:0000706	meiotic DNA double-strand break processing	(comment: inferred from combination of phenotype plus GO:0000014 MF)
PMID:17937917	GO:0043531	ADP binding	(comment: site A)
PMID:17937917	GO:0016208	AMP binding	(comment: site B)
PMID:17937917	GO:0005524	ATP binding	(comment:site B)
PMID:18030666	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(comment: spatial extent ******)The assay is Ura4 expression as a reporter gene for whether heterochromatin is spreading beyond the normal boundry, which it isn't here and so the toxic analogue results in growth attenuation. But sensitivity to FOA isn't the phenotype of interest, that's just the tool
PMID:18030666	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	"(comment: spatial extent ********)"" These results suggested that the 5-FOA-resistant phenotype of the original mutants was indeed due to ura4 repression, presumably as a result of heterochromatin assembly occurring outside the inverted repeat region."""
PMID:18030666	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(comment: spatial extent)
PMID:18030666	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(comment: spatial extent)
PMID:18030666	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(comment: spatial extent)
PMID:18030666	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(comment: spatial extent)
PMID:18030666	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(comment: spatial extent)
PMID:18030666	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(comment: spatial extent)
PMID:18030666	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(comment: spatial extent)
PMID:18030666	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	"(comment: spatial extent. )"" These results suggested that the 5-FOA-resistant phenotype of the original mutants was indeed due to ura4 repression, presumably as a result of heterochromatin assembly occurring outside the inverted repeat region."""
PMID:18030666	FYPO:0007477	abnormal epigenetic heterochromatin inheritance	epigenetic variegation both 5-FOA-resistant and -sensitive colonies were found
PMID:18042546	FYPO:0002137	decreased RNA catabolic process during vegetative growth [assayed_using] PomBase:SPCC1494.03 [has_severity] high	(comment: time course after transcription shutoff, so actually measuring degradation)
PMID:18042546	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC19G12.15c	all microarray (Table 1); arz1 also northern (Fig 1)
PMID:18042546	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC8C9.16c	all microarray (Table 1); arz1 also northern (Fig 1)
PMID:18042546	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC1289.13c	all microarray (Table 1); arz1 also northern (Fig 1)
PMID:18042546	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC30D11.07	all microarray (Table 1); arz1 also northern (Fig 1)
PMID:18042546	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC31A2.12	all microarray (Table 1); arz1 also northern (Fig 1)
PMID:18042546	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC17D11.01	all microarray (Table 1); arz1 also northern (Fig 1)
PMID:18042546	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC343.06c	all microarray (Table 1); arz1 also northern (Fig 1)
PMID:18042546	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC20F10.03	all microarray (Table 1); arz1 also northern (Fig 1)
PMID:18042546	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC4D7.10c	all microarray (Table 1); arz1 also northern (Fig 1)
PMID:18042546	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC365.09c	all microarray (Table 1); arz1 also northern (Fig 1)
PMID:18042546	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC7D4.12c	all microarray (Table 1); arz1 also northern (Fig 1)
PMID:18042546	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPCC1494.03	all microarray (Table 1); arz1 also northern (Fig 1)
PMID:18057023	FYPO:0001496	viable elongated multiseptate vegetative cell [has_severity] low	(Fig. 1A)
PMID:18057023	FYPO:0001315	normal vegetative cell morphology	(Fig. 1A)
PMID:18057023	FYPO:0001315	normal vegetative cell morphology	(Fig. 1A)
PMID:18057023	FYPO:0007584	multiseptate vegetative cell with normal cell length [has_severity] medium	(Fig. 1A)
PMID:18057023	FYPO:0007584	multiseptate vegetative cell with normal cell length [has_severity] high	(Fig. 1A)
PMID:18057023	FYPO:0001496	viable elongated multiseptate vegetative cell [has_severity] medium	(Fig. 1A)
PMID:18057023	FYPO:0001496	viable elongated multiseptate vegetative cell [has_severity] medium	(Fig. 1A)
PMID:18057023	FYPO:0001496	viable elongated multiseptate vegetative cell [has_severity] low	(Fig. 1A)
PMID:18057023	FYPO:0001496	viable elongated multiseptate vegetative cell [has_severity] high	(Fig. 1A)
PMID:18057023	FYPO:0001496	viable elongated multiseptate vegetative cell [has_severity] high	(Fig. 1A)
PMID:18057023	FYPO:0001315	normal vegetative cell morphology	(Fig. 1B)
PMID:18057023	FYPO:0003161	RNA absent from cell during vegetative growth [assayed_transcript] PomBase:SPAC20G8.05c	(Fig. 1B)
PMID:18057023	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC20G8.05c [has_severity] low	(Fig. 1B)
PMID:18057023	FYPO:0003161	RNA absent from cell during vegetative growth [assayed_transcript] PomBase:SPAC3F10.15c	(Fig. 1B)
PMID:18057023	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC3F10.15c [has_severity] medium	(Fig. 1B)
PMID:18057023	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC3F10.15c [has_severity] medium	(Fig. 1B)
PMID:18057023	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC20G8.05c	(Fig. 1B)
PMID:18057023	FYPO:0001315	normal vegetative cell morphology	(Fig. 1B)
PMID:18057023	FYPO:0001315	normal vegetative cell morphology	(Fig. 1B)
PMID:18057023	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC23C11.16 [assayed_protein] PomBase:SPBC19G7.06	(Fig. 2B)
PMID:18057023	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC23C11.16 [assayed_protein] PomBase:SPBC19G7.06	(Fig. 2B)
PMID:18057023	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC23C11.16 [assayed_protein] PomBase:SPBC19G7.06	(Fig. 2B)
PMID:18057023	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	(Fig. 3)
PMID:18057023	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_region] PomBase:SPAC23C11.16 [assayed_protein] PomBase:SPBC16G5.15c	(Fig. 7A)
PMID:18057023	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_region] PomBase:SPBC16G5.15c [assayed_protein] PomBase:SPBC16G5.15c	(Fig. 7A)
PMID:18057023	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_region] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPBC16G5.15c	(Fig. 7A)
PMID:18057023	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_region] PomBase:SPAC23C11.16 [assayed_protein] PomBase:SPBC16G5.15c	(Fig. 7A)
PMID:18057023	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_region] PomBase:SPBC16G5.15c [assayed_protein] PomBase:SPBC16G5.15c	(Fig. 7A)
PMID:18057023	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_region] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPBC16G5.15c	(Fig. 7A)
PMID:18057023	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_region] PomBase:SPAC23C11.16 [assayed_protein] PomBase:SPBC16G5.15c	(Fig. 7A)
PMID:18057023	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_region] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPBC16G5.15c	(Fig. 7A)
PMID:18057023	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_region] PomBase:SPBC16G5.15c [assayed_protein] PomBase:SPBC16G5.15c	(Fig. 7A)
PMID:18057023	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_region] PomBase:SPAC23C11.16 [assayed_protein] PomBase:SPBC16G5.15c	(Fig. 7A)
PMID:18057023	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_region] PomBase:SPBC16G5.15c [assayed_protein] PomBase:SPBC16G5.15c	(Fig. 7A)
PMID:18057023	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_region] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPBC16G5.15c	(Fig. 7A)
PMID:18057023	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [happens_during] G2/M transition of mitotic cell cycle [has_input] PomBase:SPAC23C11.16	(Fig. 8A)
PMID:18057023	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [happens_during] G2/M transition of mitotic cell cycle [has_input] PomBase:SPAC20G8.05c	(Fig. 8A)
PMID:18057023	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [happens_during] G2/M transition of mitotic cell cycle [has_input] PomBase:SPBC16G5.15c	(Fig. 8A)
PMID:18057023	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [happens_during] mitotic G1 phase [has_input] PomBase:SPAC20G8.05c	(Fig. 8B)
PMID:18057023	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [happens_during] mitotic G1 phase [has_input] PomBase:SPBC16G5.15c	(Fig. 8B)
PMID:18057023	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [happens_during] mitotic G1 phase [has_input] PomBase:SPAC1F7.05	(Fig. 8B)
PMID:18059460	GO:0008574	plus-end-directed microtubule motor activity	speckles in Fig. 4A
PMID:18060866	GO:0051285	cell cortex of cell tip	(comment: localization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim))
PMID:18061564	GO:0005515	protein binding [occurs_at] mitotic spindle midzone	(Figure 6)
PMID:18061564	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAPB1A10.09 [assayed_using] PomBase:SPAC3G9.12	(Figure 6F)
PMID:18061564	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAPB1A10.09 [assayed_using] PomBase:SPAC3G9.12	(Figure 6F)
PMID:18079700	FYPO:0005894	normal protein localization to chromatin during mitotic G1 phase [assayed_using] PomBase:SPCC338.17c	(Figure 3A)
PMID:18079700	FYPO:0005896	decreased protein localization to chromatin during mitotic G1 phase [assayed_using] PomBase:SPCC338.17c [has_severity] low	(Figure 3A) (comment: but not S phase)
PMID:18079700	FYPO:0005897	increased protein localization to chromatin during mitotic G1 phase [has_severity] low [assayed_using] PomBase:SPCC338.17c	(Figure 3A, 3B)
PMID:18079700	FYPO:0005897	increased protein localization to chromatin during mitotic G1 phase [assayed_using] PomBase:SPCC338.17c	(Figure 3B)
PMID:18079700	FYPO:0005894	normal protein localization to chromatin during mitotic G1 phase [assayed_using] PomBase:SPCC338.17c	(Figure 3B)
PMID:18079700	FYPO:0005898	increased protein localization to centromeric chromatin during mitotic G1 phase [has_severity] low [assayed_using] PomBase:SPBC29A10.14	(Figure 3C, 3E)
PMID:18079700	FYPO:0005898	increased protein localization to centromeric chromatin during mitotic G1 phase [has_severity] low [assayed_using] PomBase:SPBC29A10.14	(Figure 3C, 3E)
PMID:18079700	FYPO:0005898	increased protein localization to centromeric chromatin during mitotic G1 phase [has_severity] low [assayed_using] PomBase:SPBC29A10.14	(Figure 3C, 3E)
PMID:18079700	FYPO:0005072	normal protein localization to centromeric chromatin [assayed_using] PomBase:SPCC338.17c	(Figure 3C, 3E) (comment: CHECK during G1)
PMID:18079700	FYPO:0000450	decreased protein localization to centromere during vegetative growth	(comment: CHECK Rad21)
PMID:18079700	GO:0007064	mitotic sister chromatid cohesion	(comment: maintenence)
PMID:18079700	FYPO:0002060	viable vegetative cell population	Supplementary Figure S2
PMID:18093330	FYPO:0001982	decreased rate of DNA replication during vegetative growth	(Fig. 1)
PMID:18093330	FYPO:0007068	increased origin firing efficiency in subtelomeric heterochromatin	(Fig. 8)
PMID:18093330	FYPO:0007068	increased origin firing efficiency in subtelomeric heterochromatin	(Fig. 8)
PMID:18157152	MOD:00427	methylated residue	(comment: CHECK this is a protein modification so should be changed once we can do RNA mods)
PMID:18160711	FYPO:0002702	circularized chromosome	(comment: CHECK region between NdeI and XhoI sites deleted)
PMID:18160711	FYPO:0002702	circularized chromosome	(comment: CHECK region between NsiI sites deleted)
PMID:18160711	FYPO:0002702	circularized chromosome	(comment: CHECK truncated at PacI site)
PMID:18165685	GO:0051015	actin filament binding	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18165685	GO:0051015	actin filament binding	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18165685	GO:0051015	actin filament binding	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18165685	GO:0051015	actin filament binding	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18165685	GO:0051015	actin filament binding	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18165685	GO:0051015	actin filament binding	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18165685	GO:0051015	actin filament binding	(comment: assayed using assembled Arp2/3 complex, so perhaps some subunits should have contributes_to (but most subunits, maybe all, make contact with actin in the model in http://jcb.rupress.org/content/180/5/887))
PMID:18184749	GO:1990753	equatorial cell cortex [exists_during] mitotic M phase	(Figure 1A, right panel). Figure 1C
PMID:18184749	GO:0005801	cis-Golgi network [exists_during] mitotic interphase	(Figure 1A, right panel). Figure 1C
PMID:18184749	GO:0070971	endoplasmic reticulum exit site [exists_during] mitotic M phase	(Figure 1A, right panel). Figure 1C
PMID:18184749	GO:0000138	Golgi trans cisterna [exists_during] mitotic interphase	(Figure 1B, left panel)
PMID:18184749	GO:0000137	Golgi cis cisterna [exists_during] mitotic interphase	(Figure 1B, left panel)
PMID:18184749	GO:0000138	Golgi trans cisterna [exists_during] mitotic M phase	(Figure 1B, left panel)
PMID:18184749	GO:0032541	cortical endoplasmic reticulum	(Supp. Fig. 1A)
PMID:18184749	GO:0042175	nuclear outer membrane-endoplasmic reticulum membrane network	(Supp. Fig. 1A)
PMID:18184749	GO:0042175	nuclear outer membrane-endoplasmic reticulum membrane network	(Supp. Fig. 1A)
PMID:18184749	GO:0032541	cortical endoplasmic reticulum	(Supp. Fig. 1A)
PMID:18184749	FYPO:0002872	abnormal endoplasmic reticulum localization	(comment: CHECK abnormal ER polarization (ectopic))
PMID:18184749	FYPO:0002872	abnormal endoplasmic reticulum localization	(comment: CHECK abnormal ER polarization) We observed a striking reduction in the number of cells exhibiting clear polarization of the tER in cdc15-140 cells already at the permissive temperature of 24°C (Figure 5A, bottom panel)
PMID:18184749	FYPO:0002872	abnormal endoplasmic reticulum localization	(comment: to cell division site) We confirmed that the actomyosin ring structure was important for polarization of the early secretory compartments by examiningthe spatial distribution of the tER and Golgi compartmentsin cells with compromised function of the myosin lightchainCdc4p
PMID:18203864	FYPO:0001547	increased RNA level during cellular response to zinc ion starvation [assayed_transcript] PomBase:SPBC1348.06c [has_severity] high	(Fig. 2B)
PMID:18203864	FYPO:0001547	increased RNA level during cellular response to zinc ion starvation [assayed_transcript] PomBase:SPBC16D10.06 [has_severity] medium	(Fig. 2B)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPAPB1E7.07	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPAC9E9.03	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPAC13A11.02c	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPAC26F1.14c	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPCC1235.02	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPAC23E2.01	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPAC140.01	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPCC645.03c	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPAC20G8.04c	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPAC24C9.06c	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPBP23A10.16	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPCC330.12c	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPCC757.07c	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPAC24B11.13	(Fig. 2)
PMID:18223116	FYPO:0002014	increased RNA level during cellular response to iron ion starvation [assayed_using] PomBase:SPAC10F6.01c	(Fig. 2)
PMID:18223116	GO:0003714	transcription corepressor activity [has_input] PomBase:SPBC725.11c [has_input] PomBase:SPAC23C11.08 [has_input] PomBase:SPBC3B8.02 [happens_during] cellular response to iron ion starvation [part_of] negative regulation of transcription by RNA polymerase II [occurs_in] nucleus	(Fig. 6) (comment: it doesn't bind dna according to later studies)
PMID:18256284	GO:0061673	mitotic spindle astral microtubule [exists_during] mitotic anaphase	(Figure 1A)
PMID:18256284	GO:0061673	mitotic spindle astral microtubule [exists_during] mitotic metaphase	(Figure 1A)
PMID:18256284	GO:1990941	mitotic spindle kinetochore microtubule [exists_during] mitotic metaphase	(Figure 1B) (comment: plus end)
PMID:18256284	GO:1990537	mitotic spindle polar microtubule [exists_during] mitotic anaphase	(Figure 1B) (comment: plus end)
PMID:18256284	GO:1990537	mitotic spindle polar microtubule [exists_during] mitotic metaphase	(Figure 1B) (comment: plus end)
PMID:18256284	GO:1990941	mitotic spindle kinetochore microtubule [exists_during] mitotic anaphase	(Figure 1B) (comment: plus end)
PMID:18256290	FYPO:0000650	increased septation index [has_severity] medium	(comment: increased more than pxl1delta alone)
PMID:18256290	FYPO:0000650	increased septation index [has_severity] medium	(comment: increased more than pxl1delta alone)
PMID:18256290	FYPO:0000650	increased septation index [has_severity] medium	(comment: increased more than pxl1delta alone)
PMID:18256290	FYPO:0000650	increased septation index [has_severity] medium	(comment: increased more than pxl1delta alone)
PMID:18256290	FYPO:0000650	increased septation index [has_severity] medium	(comment: increased more than pxl1delta alone)
PMID:18256290	FYPO:0000650	increased septation index [has_severity] medium	(comment: less levere than pxl1 null)
PMID:18256290	FYPO:0000650	increased septation index [has_severity] medium	(comment: less levere than pxl1 null)
PMID:18256290	GO:0110085	mitotic actomyosin contractile ring	(comment: localization dependent on filamentous actin (GO:0031941); tested using latrunculin A)
PMID:18262494	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 40-70	(Fig. 1B)
PMID:18262494	FYPO:0001919	fragmented nucleus during vegetative growth	(comment: CHECK after chromosome segregation)
PMID:18262494	FYPO:0000030	abnormal mitotic chromosome congression	(comment: CHECK with extreme sister chromtid oscillations)
PMID:18272786	GO:0110085	mitotic actomyosin contractile ring	(comment: dependent on F-actin, assayed using Latrunculin A)
PMID:18272791	GO:0005829	cytosol [exists_during] cellular response to osmotic stress	Therefore, we can conclude that Cdc25 protein is exported from the nucleus under stress conditions in a Srk1-dependent manner
PMID:18276645	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC17G6.02c	(comment: CHECK normal oxygen level)
PMID:18276645	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC17G6.02c	(comment: CHECK normal oxygen level)
PMID:18303049	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition [has_severity] high	(Fig. 1)
PMID:18303049	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 2C)
PMID:18303049	FYPO:0000151	abnormal meiotic chromosome segregation [has_penetrance] high	(Fig. 3A)
PMID:18303049	FYPO:0007664	mononucleate monoseptate vegetative cell with anucleate compartment [has_penetrance] 11	(Fig. 3B)
PMID:18303049	FYPO:0007664	mononucleate monoseptate vegetative cell with anucleate compartment [has_penetrance] complete	(Fig. 3B)
PMID:18303049	FYPO:0001315	normal vegetative cell morphology	(Fig. 3C)
PMID:18303049	FYPO:0001315	normal vegetative cell morphology	(Fig. 3C)
PMID:18303049	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition [has_severity] low	(Fig. 3D)
PMID:18303049	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition [has_severity] low	(Fig. 3D)
PMID:18303049	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC9G1.09	(Fig. 5)
PMID:18303049	FYPO:0004635	increased protein localization to mitotic spindle [assayed_protein] PomBase:SPBC582.03	(Fig. 6B)
PMID:18303049	FYPO:0007743	premature septum assembly during mitotic interphase	(Fig. 6C)
PMID:18303049	FYPO:0000252	increased spontaneous diploidization	(Table 1)
PMID:18303049	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC21.06c [has_severity] medium	(Table 2)
PMID:18303049	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC23C11.16 [has_severity] high	(Table 2)
PMID:18303049	FYPO:0002874	premature protein localization to medial cortex during vegetative growth [assayed_protein] PomBase:SPBC428.13c	(Table 2)
PMID:18303049	FYPO:0002874	premature protein localization to medial cortex during vegetative growth [assayed_protein] PomBase:SPBC19G7.05c	(Table 2)
PMID:18303049	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC21.06c [has_severity] medium	(Table 2)
PMID:18303049	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC23C11.16 [has_severity] medium	(Table 2)
PMID:18303049	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC23C11.16 [has_severity] medium	(Table 2)
PMID:18303049	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC21.06c [has_severity] high	(Table 2)
PMID:18328707	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPBC28E12.03	(Fig. 1)
PMID:18328707	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC28E12.03 [assayed_using] PomBase:SPAC2F7.03c	(Fig. 1)
PMID:18328707	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC28E12.03 [assayed_using] PomBase:SPAC2F7.03c	(Fig. 1)
PMID:18328707	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC28E12.03 [assayed_using] PomBase:SPAC2F7.03c	(Fig. 1)
PMID:18328707	MOD:01455	O-phosphorylated residue	(Fig. 1D)
PMID:18328707	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPBC28E12.03	(Fig. 1D)
PMID:18328707	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPBC28E12.03	(Fig. 1D)
PMID:18328707	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPBC28E12.03	(Fig. 1D) (comment: pom1 is catalytically active but not localized to cell ends)
PMID:18328707	FYPO:0005466	protein mislocalized to non-growing cell tip [assayed_using] PomBase:SPBC28E12.03	(Fig. 1SE) to cell cortex of (new non growing) cell tip from medial cortex
PMID:18328707	FYPO:0003527	protein mislocalized to cell tip [assayed_using] PomBase:SPBC28E12.03	(Fig. 1SE) to cell cortex of (new) cell tip from medial cortex
PMID:18328707	FYPO:0003527	protein mislocalized to cell tip [assayed_using] PomBase:SPBC28E12.03	(Fig. 1SE) to cell cortex of (new) cell tip from medial cortex
PMID:18328707	FYPO:0006638	decreased protein localization to medial cortex, with protein distributed in cell cortex, during vegetative growth [assayed_using] PomBase:SPBC28E12.03 [has_penetrance] 47	(Fig. 2C)
PMID:18328707	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC2F7.03c	(Fig. S1D)
PMID:18328707	GO:0005096	GTPase activator activity [has_input] PomBase:SPAC110.03	(Figure 3A)
PMID:18328707	GO:0005515	protein binding	(Figure 3B)
PMID:18328707	FYPO:0000024	stubby vegetative cell	(Figure 4E)
PMID:18328707	GO:1903067	negative regulation of protein localization to cell tip [has_input] PomBase:SPBC28E12.03 [part_of] activation of bipolar cell growth	(comment: *****OLD*****waiting for GO)
PMID:18328707	GO:1902716	cell cortex of growing cell tip [exists_during] mitotic interphase	(comment: CHECK GTP bound active form)
PMID:18328707	FYPO:0000836	increased protein level [assayed_using] PomBase:SPAC110.03	(comment: CHECK GTP bound)
PMID:18328707	FYPO:0000836	increased protein level [assayed_using] PomBase:SPAC110.03 [assayed_using] cdc42/GTP+	(comment: CHECK GTP bound) fig 3C
PMID:18328707	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03 [assayed_using] cdc42/GTP+	(comment: CHECK GTP-bound) Figure 4E
PMID:18328707	FYPO:0002424	normal actin cortical patch localization during mitotic interphase [assayed_using] PomBase:SPAC110.03 [assayed_using] cdc42/GTP+	(comment: CHECK GTP-bound) Figure 4E, polarization localization to both cell ends
PMID:18328707	FYPO:0000930	abolished protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPAC110.03 [assayed_using] cdc42/GTP+	(comment: CHECK active GTP bound form)
PMID:18328707	GO:0031097	medial cortex [exists_during] mitotic G2 phase	(comment: old end)
PMID:18331722	GO:1990949	metaphase/anaphase transition of meiosis I	First, we have shown that a true APC/C substrate regulates the activity of the APC/C. Cells might precisely control protein levels of each or a subset of APC/C substrate to fine-tune the APC/C itself....Mes1 transcripts and protein levels peak in late MI (Izawa et al., 2005; Mata et al., 2002) when Mes1 sequesters the Fizzy family of proteins to inhibit APC/C, in turn slowing down cyclin B proteolysis (‘‘APC/C inhibited’’ in Figure 4G). At the same time, Mes1 is inhibited through ubiquitylation by APC/C to allow partial APC/C activation required for anaphase I onset.
PMID:18337696	FYPO:0003118	normal cellular reactive oxygen species level during vegetative growth	(comment: at time 0. they don't look at nitrogen starvation for very long, only 60 mins)
PMID:18344406	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(comment: CHECK significantly sensitive to HU. less than that of wild-type cells but higher than that of checkpoint mutant rad3Δ cells) (Fig. 1B).
PMID:18344406	FYPO:0000963	normal growth on hydroxyurea	(comment: CHECK significantly sensitive to HU.)
PMID:18344406	FYPO:0007142	loss of viability following cellular response to ionizing radiation [has_severity] high	(comment: If this signal is not generated, cells mutant go through the cell cycle with damage and eventually die.)
PMID:18344406	FYPO:0002060	viable vegetative cell population	Both mutant strains were viable and able to grow at 32°C.
PMID:18344406	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Both mutant strains were viable and able to grow at 32°C. However, like the hst4Δ strain, the histone H3 K56R mutant strains had slight growth defects compared to the strain containing a single copy of the H3 histone (Fig. 7B, first panel).
PMID:18344406	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	H184Y mutation were as sensitive to MMS as the hst4Δ strains were, indicating that Hst4 enzymatic activity was important for cells to be resistant to MMS.
PMID:18344406	FYPO:0002061	inviable vegetative cell population	However, every single repair mutant that we tested was synthetically sick in combination with hst4Δ when cells were grown on medium containing MMS (Fig. 3).
PMID:18344406	FYPO:0002061	inviable vegetative cell population	However, every single repair mutant that we tested was synthetically sick in combination with hst4Δ when cells were grown on medium containing MMS (Fig. 3).
PMID:18344406	FYPO:0002061	inviable vegetative cell population	However, every single repair mutant that we tested was synthetically sick in combination with hst4Δ when cells were grown on medium containing MMS (Fig. 3).
PMID:18344406	FYPO:0002061	inviable vegetative cell population	However, every single repair mutant that we tested was synthetically sick in combination with hst4Δ when cells were grown on medium containing MMS (Fig. 3).
PMID:18344406	FYPO:0002061	inviable vegetative cell population	However, every single repair mutant that we tested was synthetically sick in combination with hst4Δ when cells were grown on medium containing MMS (Fig. 3).
PMID:18344406	FYPO:0008162	increased activation of S-phase DNA damage checkpoint	In cells lacking Hst4, Chk1 was phosphorylated even in the absence of MMS exposure, and this phosphorylation did not significantly increase upon exposure to MMS (Fig. 2B).
PMID:18344406	FYPO:0000871	increased histone H3-K9 methylation during vegetative growth	In the absence of Sir2, we observed elevated levels of histone H3 K9 and histone H4 K16, which was consistent with previous reports (17, 48).
PMID:18344406	FYPO:0007632	increased histone H4-K16 acetylation during vegetative growth	In the absence of Sir2, we observed elevated levels of histone H3 K9 and histone H4 K16, which was consistent with previous reports (17, 48).
PMID:18344406	FYPO:0000085	sensitive to camptothecin [has_severity] high	Interestingly, hst4Δ cells were sensitive to MMS and CPT (Fig. 1A)
PMID:18344406	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	Interestingly, hst4Δ cells were sensitive to MMS and CPT (Fig. 1A)
PMID:18344406	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	Interestingly, similar to the hst4Δ mutant, both K56R and K56Q mutants were sensitive to MMS and CPT.
PMID:18344406	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	Interestingly, similar to the hst4Δ mutant, both K56R and K56Q mutants were sensitive to MMS and CPT. However, the histone H3 K56Q mutant, which mimics the constitutively acetylated state, was less sensitive to MMS and CPT than the K56R mutant, which mimics the constitutively deacetylated state.
PMID:18344406	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] 5	Like hst4Δ cells, both histone H3 mutant cells were very elongated, and a percentage of these cells exhibited abnormal DAPI staining (Fig. 7A).
PMID:18344406	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	Like hst4Δ cells, both histone H3 mutant cells were very elongated, and a percentage of these cells exhibited abnormal DAPI staining (Fig. 7A).
PMID:18344406	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] 10	Like hst4Δ cells, both histone H3 mutant cells were very elongated, and a percentage of these cells exhibited abnormal DAPI staining (Fig. 7A).
PMID:18344406	FYPO:0004928	fragmented DNA during vegetative growth	Our fluorescence microscopic analysis also clearly indicated that a significant percentage of the hst4Δ cells in culture had fragmented DNA (see Fig. S1 in the supplemental material).
PMID:18344406	FYPO:0002151	inviable spore	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002151	inviable spore	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002060	viable vegetative cell population	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002060	viable vegetative cell population	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002060	viable vegetative cell population	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002060	viable vegetative cell population	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002151	inviable spore	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002151	inviable spore	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0002151	inviable spore	Tetrad analysis demonstrating synthetic lethality of representatives of the DNA damage checkpoint mutant crb2Δ and rad3Δ are shown in Fig. 2A
PMID:18344406	FYPO:0003223	normal histone H3-K9 acetylation during vegetative growth	The hst4 mutant did not show significant changes in the acetylation levels of histone H3 K9 or K14 and histone H4 K16 compared to the wild-type control (Fig. 4A).
PMID:18344406	FYPO:0008160	normal histone H3-K56 acetylation during vegetative growth	The hst4Δ mutant did not show significant changes in the acetylation levels of histone H3 K9 or K14 and histone H4 K16 compared to the wild-type control (Fig. 4A).
PMID:18344406	FYPO:0008161	normal histone H4-K16 acetylation during vegetative growth	The hst4Δ mutant did not show significant changes in the acetylation levels of histone H3 K9 or K14 and histone H4 K16 compared to the wild-type control (Fig. 4A).
PMID:18344406	GO:0140765	histone H3K56 deacetylase activity, NAD-dependent [happens_during] mitotic S phase [part_of] DNA repair-dependent chromatin remodeling	These results (Fig. 4C) showed that the acetylation of H3 K56 is cell cycle regulated and occurred during the S phase of the cell cycle.
PMID:18344406	GO:0140861	DNA repair-dependent chromatin remodeling	These results collectively suggest that alterations in K56 acetylation are dependent upon the presence of Hst4 in the cell, and more importantly, they suggest that the levels of Hst4 are regulated in response to cell cycle progression and DNA damage.
PMID:18344406	FYPO:0000502	abnormally arrested mitotic cell cycle progression	Wild-type cells showed a peak of septation approximately 80 min after release, whereas the hst4Δ cells showed a delayed peak of septation at 120 min (see Fig. S2 in the supplemental material).
PMID:18344406	FYPO:0001925	normal cellular response to gamma radiation	hst4Δ cells behaved as wild-type cells did and were able to survive exposure to gamma irradiation (Fig. 1C).
PMID:18345014	GO:0033553	rDNA heterochromatin	(Fig. 1)
PMID:18345014	GO:0140720	subtelomeric heterochromatin	(Fig. 1)
PMID:18345014	GO:0005721	pericentric heterochromatin	(Fig. 1)
PMID:18345014	GO:0005721	pericentric heterochromatin	(Fig. 1)
PMID:18345014	GO:0005721	pericentric heterochromatin	(Fig. 1)
PMID:18345014	GO:0005721	pericentric heterochromatin	(Fig. 1)
PMID:18345014	GO:0031934	mating-type region heterochromatin	(Fig. 1)
PMID:18345014	GO:0031934	mating-type region heterochromatin	(Fig. 1)
PMID:18345014	GO:0031934	mating-type region heterochromatin	(Fig. 1)
PMID:18345014	GO:0031934	mating-type region heterochromatin	(Fig. 1)
PMID:18345014	GO:0033553	rDNA heterochromatin	(Fig. 1)
PMID:18345014	GO:0140720	subtelomeric heterochromatin	(Fig. 1)
PMID:18345014	GO:0005721	pericentric heterochromatin	(Fig. 1)
PMID:18345014	GO:0031934	mating-type region heterochromatin	(Fig. 1)
PMID:18345014	GO:0140720	subtelomeric heterochromatin	(Fig. 1)
PMID:18345014	GO:0140720	subtelomeric heterochromatin	(Fig. 1)
PMID:18345014	GO:0140720	subtelomeric heterochromatin	(Fig. 1)
PMID:18345014	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC11E10.08	(Fig. 2A)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC613.12c	(Fig. 2A)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC970.07c	(Fig. 2A)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC428.08c	(Fig. 2A)
PMID:18345014	FYPO:0004237	increased protein localization to heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC11E10.08 [has_severity] medium	(Fig. 2B and D)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPBC428.08c	(Fig. 2B)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC613.12c	(Fig. 2B)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC970.07c	(Fig. 2B)
PMID:18345014	FYPO:0002836	increased centromeric outer repeat transcript-derived siRNA level	(Fig. 2C)
PMID:18345014	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	(Fig. 2C)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC11E10.08 [has_severity] medium	(Fig. 2D)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC11E10.08 [has_severity] high	(Fig. 2D)
PMID:18345014	FYPO:0004237	increased protein localization to heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC11E10.08 [has_severity] high	(Fig. 2D)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC11E10.08 [has_severity] high	(Fig. 2D)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC11E10.08 [has_severity] medium	(Fig. 2D)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC11E10.08 [has_severity] medium	(Fig. 2D)
PMID:18345014	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(Fig. 2E)
PMID:18345014	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC18G6.02c [assayed_protein] PomBase:SPBC428.08c	(Fig. 3B)
PMID:18345014	FYPO:0008195	decreased histone H3-K9Me binding	(Fig. 4C)
PMID:18345014	FYPO:0008195	decreased histone H3-K9Me binding	(Fig. 4C)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC11E10.08	(Fig. 5A)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC613.12c	(Fig. 5A)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC970.07c	(Fig. 5A)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPBC428.08c	(Fig. 5A)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC613.12c	(Fig. 5B)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC970.07c	(Fig. 5B)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC428.08c	(Fig. 5B)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC11E10.08	(Fig. 5B)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC613.12c	(Fig. 5C)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC970.07c	(Fig. 5C)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPBC428.08c	(Fig. 5C)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC970.07c	(Fig. 5D)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC613.12c	(Fig. 5D)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC428.08c	(Fig. 5D)
PMID:18345014	FYPO:0002355	decreased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth	(Fig. 6A)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Fig. 6A)
PMID:18345014	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(Fig. 6B)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC11E10.08	(Fig. S5)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC11E10.08	(Fig. S5)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC11E10.08	(Fig. S5)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC11E10.08	(Fig. S5)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC11E10.08	(Fig. S5)
PMID:18345014	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC11E10.08	(Fig. S5)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC11E10.08	(Fig. S5)
PMID:18345014	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC11E10.08	(Fig. S5)
PMID:18345014	GO:0141194	siRNA-mediated heterochromatin formation	Our analyses suggest that Rik1 is a crucial factor involved in RNAi- mediated targeting of ClrC to heterochromatic repeat elements.
PMID:18345014	GO:0062072	histone H3K9me2/3 reader activity [part_of] constitutive heterochromatin formation [has_input] hht3/Me(K9)	The results presented here show that binding of Clr4 to H3K9me via its chromodomain is crucial for the spreading of heterochromatic structures.
PMID:18345014	GO:0062072	histone H3K9me2/3 reader activity [part_of] constitutive heterochromatin formation [has_input] hht1/Me(K9)	The results presented here show that binding of Clr4 to H3K9me via its chromodomain is crucial for the spreading of heterochromatic structures.
PMID:18345014	GO:0062072	histone H3K9me2/3 reader activity [part_of] constitutive heterochromatin formation [has_input] hht2/Me(K9)	The results presented here show that binding of Clr4 to H3K9me via its chromodomain is crucial for the spreading of heterochromatic structures.
PMID:18378696	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: same as either single mutant)
PMID:18378696	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(comment: same as either single mutant)
PMID:18378696	FYPO:0000095	sensitive to bleomycin [has_severity] medium	(comment: same as either single mutant)
PMID:18378696	FYPO:0000095	sensitive to bleomycin [has_severity] medium	(comment: same as nbs1delta alone)
PMID:18378696	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(comment: same as nbs1delta alone)
PMID:18378696	FYPO:0000088	sensitive to hydroxyurea	(comment: same as nbs1delta alone)
PMID:18378696	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: same as nbs1delta alone)
PMID:18378696	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] high	(comment: same as rad51delta alone)
PMID:18388861	FYPO:0003082	normal genetic imprinting at mating-type locus	(Fig. 5)
PMID:18388861	FYPO:0003082	normal genetic imprinting at mating-type locus	(Fig. 5)
PMID:18388861	FYPO:0003082	normal genetic imprinting at mating-type locus	(Fig. 5)
PMID:18388861	FYPO:0000278	decreased cell population growth following spore germination	(Table 1)
PMID:18388861	FYPO:0003612	viable spore population	(Table 1)
PMID:18388861	FYPO:0003612	viable spore population	(Table 1)
PMID:18388861	FYPO:0003612	viable spore population	(Table 1)
PMID:18388861	FYPO:0003612	viable spore population	(Table 1)
PMID:18388861	FYPO:0003612	viable spore population	(Table 1)
PMID:18388861	FYPO:0000316	inviable after spore germination	(Table 1)
PMID:18388861	FYPO:0000316	inviable after spore germination	(Table 1)
PMID:18388861	FYPO:0000316	inviable after spore germination	(Table 1)
PMID:18388861	FYPO:0000316	inviable after spore germination	(Table 1)
PMID:18388861	FYPO:0000316	inviable after spore germination	(Table 1)
PMID:18388861	FYPO:0000470	decreased mating type switching	(Table 1)
PMID:18388861	FYPO:0000316	inviable after spore germination	(Table 1)
PMID:18388861	FYPO:0000316	inviable after spore germination	(Table 1)
PMID:18388861	FYPO:0003612	viable spore population	(Table 1)
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0003612	viable spore population	As expected, mat1-Msmt-0 and mat1-PD17 strains, which do not exhibit SSBs, are fully viable regardless of the mutant status.
PMID:18388861	FYPO:0000316	inviable after spore germination [has_penetrance] complete	However, the h90 rhp57D swi5D double mutant is not viable (Figure 2C). Table 1
PMID:18388861	FYPO:0000316	inviable after spore germination [has_penetrance] complete	However, the h90 rhp57D swi5D double mutant is not viable (Figure 2C). Table 1
PMID:18388861	GO:0007533	mating type switching	Interestingly, upon re-streaking, the h 90 rhp57D cells progressively produced colonies defective in MT switching, indicating that Rhp57 participates in efficient MT switching.
PMID:18388861	FYPO:0000470	decreased mating type switching [has_penetrance] low	None of the single helicase and essential topoisomerase 3 (in rqh1D background) mutant strains exhibit MT switching and/or viability defect, except for the pfh1 mutant where a mild MT switching defect was observed (Table I, data not shown).
PMID:18388861	FYPO:0002430	inviable after spore germination, multiple cell divisions [has_penetrance] high	Table 1, Fig. 3A and B
PMID:18388861	FYPO:0003612	viable spore population	Table 1, Fig. 3A, C and D
PMID:18388861	FYPO:0002430	inviable after spore germination, multiple cell divisions [has_penetrance] complete	Table 1. Fig. 2A. Further observation of the germinating spores showed that the mutated h90 cells elongated and eventually divided, but never formed visible colonies (data not shown).
PMID:18388861	FYPO:0000470	decreased mating type switching	Table 1. Fig. 3C and D
PMID:18388861	FYPO:0000316	inviable after spore germination	Table 1. Fig. 3C and D
PMID:18388861	FYPO:0000316	inviable after spore germination	Table 1. Fig. 3C and D
PMID:18388861	FYPO:0000470	decreased mating type switching	Table 1. Fig. 3C and D
PMID:18388861	FYPO:0002430	inviable after spore germination, multiple cell divisions [has_penetrance] complete	Table 1. Further observation of the germinating spores showed that the mutated h90 cells elongated and eventually divided, but never formed visible colonies (data not shown).
PMID:18388861	FYPO:0002430	inviable after spore germination, multiple cell divisions [has_penetrance] complete	Table 1. Further observation of the germinating spores showed that the mutated h90 cells elongated and eventually divided, but never formed visible colonies. Table 1
PMID:18388861	FYPO:0000472	normal mating type switching	The h90 exo1D mutant is viable and does not exhibit MT switching defects. Fig. 2B. Table 1
PMID:18388861	FYPO:0003612	viable spore population	The h90 exo1D mutant is viable. Fig. 2B. Table 1
PMID:18388861	FYPO:0000470	decreased mating type switching [has_penetrance] low	The h90 rhp57D strain produces colonies with a mild defect in MT switching. Fig. 2C. Table 1
PMID:18388861	FYPO:0000470	decreased mating type switching [has_penetrance] high	h90 swi5D mutant produces healthy colonies but MT switching is drastically reduced. Fig. 2C. Table 1
PMID:18388861	FYPO:0003612	viable spore population	rhp22AD, rhp51D and rhp54D mutants do not form colonies in the wild-type h90 strain, as already shown for rhp22AD, although they are viable in mat1-Msmt-0 and mat1-PD17 backgrounds.
PMID:18388861	FYPO:0003612	viable spore population	rhp22AD, rhp51D and rhp54D mutants do not form colonies in the wild-type h90 strain, as already shown for rhp22AD, although they are viable in mat1-Msmt-0 and mat1-PD17 backgrounds.
PMID:18388861	FYPO:0003612	viable spore population	rhp22AD, rhp51D and rhp54D mutants do not form colonies in the wild-type h90 strain, as already shown for rhp22AD, although they are viable in mat1-Msmt-0 and mat1-PD17 backgrounds.
PMID:18388861	FYPO:0003612	viable spore population	rhp22AD, rhp51D and rhp54D mutants do not form colonies in the wild-type h90 strain, as already shown for rhp22AD, although they are viable in mat1-Msmt-0 and mat1-PD17 backgrounds.
PMID:18388861	FYPO:0003612	viable spore population	rhp22AD, rhp51D and rhp54D mutants do not form colonies in the wild-type h90 strain, as already shown for rhp22AD, although they are viable in mat1-Msmt-0 and mat1-PD17 backgrounds.
PMID:18388861	FYPO:0003612	viable spore population	rhp22AD, rhp51D and rhp54D mutants do not form colonies in the wild-type h90 strain, as already shown for rhp22AD, although they are viable in mat1-Msmt-0 and mat1-PD17 backgrounds. Fig. 2A
PMID:18388861	FYPO:0000278	decreased cell population growth following spore germination [has_severity] high	the double h90 rad50D exo1D mutant is not viable, but can eventually form micro-colonies (Figure 2B, left panel). Table 1
PMID:18388861	FYPO:0000278	decreased cell population growth following spore germination [has_severity] high	the double h90 rad50D exo1D mutant is not viable, but can eventually form micro-colonies (Figure 2B, left panel). Table 1
PMID:18388861	FYPO:0000278	decreased cell population growth following spore germination	the h90 rad50D or h90 mre11D (data not shown) mutant forms small colonies. However, these colonies contain many dead cells and few spores.
PMID:18388861	FYPO:0000278	decreased cell population growth following spore germination	the h90 rad50D or h90 mre11D (data not shown) mutant forms small colonies. However, these colonies contain many dead cells and few spores. Table 1.
PMID:18391219	GO:0002143	tRNA wobble position uridine thiolation	"(comment: provides the sulfur....seems ok based on the def ""The process in which a uridine residue at position 34 in the anticodon of a tRNA is post-transcriptionally thiolated at the C2 position. **This process involves transfer of a sulfur from cysteine to position C2 by several steps)"
PMID:18397994	PomGeneEx:0000011	RNA level increased [during] meiosis I cell cycle phase	(Fig. 2A)
PMID:18397994	PomGeneEx:0000018	protein level increased [during] meiosis I cell cycle phase	(Fig. 2B)
PMID:18397994	FYPO:0000346	small spores	(Fig. 3A)
PMID:18397994	FYPO:0000478	normal meiosis	(Fig. 3B)
PMID:18397994	FYPO:0004953	abnormal prospore membrane [has_penetrance] 40	(Fig. 4)
PMID:18397994	GO:0032120	ascospore-type prospore membrane formation	(Fig. 5)
PMID:18397994	FYPO:0002708	abolished prospore formation	(Fig. 6A)
PMID:18397994	FYPO:0000346	small spores	(Fig. 6A)
PMID:18397994	FYPO:0002708	abolished prospore formation	(Fig. 6A)
PMID:18397994	FYPO:0002708	abolished prospore formation	(Fig. 6A)
PMID:18397994	FYPO:0002708	abolished prospore formation	(Fig. 6A)
PMID:18397994	GO:0005628	prospore membrane	(Fig. 7)
PMID:18397994	FYPO:0002708	abolished prospore formation	(Fig. 8)
PMID:18397994	FYPO:0002708	abolished prospore formation	(Fig. 8)
PMID:18397994	FYPO:0002708	abolished prospore formation	(Fig. 8A)
PMID:18397994	FYPO:0002708	abolished prospore formation	(Fig. 8A)
PMID:18397994	FYPO:0000943	normal spore morphology	(Fig. 9)
PMID:18397994	FYPO:0000943	normal spore morphology	(Fig. 9)
PMID:18397994	GO:0035974	meiotic spindle pole body [exists_during] meiotic metaphase II	We found that Slk1 was also localized to the SPB during metaphase II and anaphase II. Fig. 7
PMID:18397994	GO:0035974	meiotic spindle pole body [exists_during] meiotic anaphase II	We found that Slk1 was also localized to the SPB during metaphase II and anaphase II. Fig. 7
PMID:18399988	GO:0004324	ferredoxin-NADP+ reductase activity [has_input] PomBase:SPAC22E12.10c	(comment: they show transfer to a heterologous cytochrome p450 enzyme, but pombe doesn't have any mitochondrial ones.)
PMID:18411246	GO:0035974	meiotic spindle pole body [exists_during] meiotic prometaphase I	(Fig. 2A)
PMID:18411246	GO:0005628	prospore membrane [exists_during] meiotic anaphase II	(Fig. 2B)
PMID:18411246	FYPO:0004443	decreased protein localization to prospore membrane during meiosis II [assayed_using] PomBase:SPCC417.06c	(Fig. 3A)
PMID:18411246	FYPO:0006317	decreased protein localization to meiotic spindle pole body during meiosis II [assayed_using] PomBase:SPCC417.06c	(Fig. 3A)
PMID:18411246	FYPO:0001914	abnormal prospore membrane formation	(Fig. 5B)
PMID:18411246	FYPO:0004952	incomplete prospore membrane closure	enclosure arrow in Figs 4Ci,ii)
PMID:18414064	FYPO:0001052	cut, small cell [has_penetrance] 23	(comment: penetrance at 4 hours)
PMID:18414064	FYPO:0001052	cut, small cell [has_penetrance] 86	(comment: penetrance at 4 hours)
PMID:18414064	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 7	(comment: penetrance at 4 hours; increases upon longer time at restrictive temp)
PMID:18414064	FYPO:0001387	loss of viability at high temperature	(comment: same with or without TBZ)
PMID:18414064	FYPO:0001387	loss of viability at high temperature	(comment: same with or without TBZ)
PMID:18416603	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPAC644.14c [part_of] homologous recombination	Based on these results, we propose a model for the early step of the strand exchange reaction involving Rhp51 and the two mediators. Rad22 recruits Rhp51 to RPA-coated ssDNA.
PMID:18459978	GO:0045899	positive regulation of RNA polymerase II transcription preinitiation complex assembly	Quantification of the results shown in Fig. 4A is illustrated in Fig. 4B. Taken together, these experiments reveal that PC4 stimulates the rate of preinitiation complex formation.
PMID:1849107	FYPO:0000044	abnormal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0000044	abnormal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0000044	abnormal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0000044	abnormal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0000044	abnormal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0000044	abnormal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0000044	abnormal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0000044	abnormal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0000044	abnormal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001865	normal negative regulation of transcription by glucose [assayed_using] PomBase:SPBC1198.14c	(comment: also assayed using lacZ under fbp1 promoter)
PMID:1849107	FYPO:0001660	decreased cellular cAMP level	(comment: git2-1 is effectively null, even though it isn't a complete deletion of the coding sequence)
PMID:1849107	FYPO:0001869	abolished adenylyl cyclase activity	(comment: git2-1 is effectively null, even though it isn't a complete deletion of the coding sequence)
PMID:1849107	FYPO:0000781	decreased transcription during vegetative growth [assayed_using] PomBase:SPBC1198.14c	(comment: glycerol = derepressing for glucose repression) (comment: also assayed using lacZ under fbp1 promoter and maltose carbon source, also derepressing)
PMID:18493607	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(comment: CHECK same as sir2+ overexpression alone)
PMID:18493607	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(comment: CHECK slighly more severe than sir2+ overexpression alone)
PMID:18493607	GO:0005634	nucleus [exists_during] mitotic cell cycle phase	(comment: present throughout mitotic cell cycle)
PMID:18495844	GO:0000132	establishment of mitotic spindle orientation [happens_during] mitotic G2 phase	(Fig. 1B and 2B,C) normal MTs required to establish early orientation of mitotic spindle by aligning SPBs with long axis of cell
PMID:18495844	FYPO:0007388	misoriented mitotic spindle [has_penetrance] high [has_severity] high	(Fig. 1B)
PMID:18495844	GO:0000132	establishment of mitotic spindle orientation [happens_during] mitotic G2 phase	(Fig. 1B) normal interphase MTs required to establish early orientation of mitotic spindle by aligning SPBs with long axis of cell
PMID:18495844	FYPO:0005691	decreased spindle pole body-led chromosome movement during mitotic interphase	(Fig. 2A-C) This oscillatory movement was not perturbed by Latrunculin A treatment, but was lost in cells treated with MBC or in mto1Δ cells, and was reduced in tip1Δ cells
PMID:18495844	FYPO:0005691	decreased spindle pole body-led chromosome movement during mitotic interphase	(Fig. 2B)
PMID:18495844	FYPO:0007412	normal mitotic spindle orientation [has_penetrance] high	(Fig. 3B)
PMID:18495844	FYPO:0007390	increased variability of angle of spindle pole body-led chromosome movement during mitotic interphase [has_penetrance] high	(Fig. 3B)
PMID:18495844	FYPO:0007388	misoriented mitotic spindle [has_penetrance] high	(Fig. 3B, C)
PMID:18495844	FYPO:0007388	misoriented mitotic spindle [has_penetrance] high	(Fig. 3B, C) As expected, the range of SPB trajectory angles was much wider than in wild-type cells (Fig. 2C, Fig. 3B,C
PMID:18504300	GO:0034399	nuclear periphery [exists_during] mitotic G1 phase	(Fig. 5)
PMID:18504300	GO:0034399	nuclear periphery [exists_during] cell quiescence	(Fig. 5)
PMID:18504300	GO:0034515	proteasome storage granule [exists_during] cell quiescence	(Fig. 5)
PMID:18504300	GO:0034515	proteasome storage granule [exists_during] mitotic G1 phase	(Fig. 5)
PMID:18514516	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] medium	(comment:same as either single mutant)
PMID:18514516	FYPO:0002485	decreased intergenic meiotic recombination [has_severity] medium	(comment:same as either single mutant)
PMID:18514516	FYPO:0002485	decreased intergenic meiotic recombination [has_severity] medium	(comment:same as either single mutant)
PMID:18514516	FYPO:0002485	decreased intergenic meiotic recombination [has_severity] medium	(comment:same as either single mutant)
PMID:18514516	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] medium	(comment:same as either single mutant)
PMID:18562692	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. 1)
PMID:18562692	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 1)
PMID:18562692	FYPO:0007388	misoriented mitotic spindle	(Fig. 2)
PMID:18562692	FYPO:0007388	misoriented mitotic spindle	(Fig. 2)
PMID:18562692	FYPO:0002022	normal actin cortical patch morphology	(Fig. 3)
PMID:18562692	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 4)
PMID:18562692	FYPO:0005722	mitotic spindle collapse during anaphase B elongation [has_penetrance] 45	(Fig. 5A)
PMID:18562692	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. 5A)
PMID:18562692	FYPO:0006643	mitotic spindle collapse without elongation during metaphase [has_penetrance] 45	(Fig. 5A)
PMID:18562692	FYPO:0006643	mitotic spindle collapse without elongation during metaphase [has_penetrance] 35	(Fig. 5B)
PMID:18562692	FYPO:0001778	abnormal centromere localization	(Fig. 5B)
PMID:18562692	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 6C)
PMID:18562692	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 6C)
PMID:18562692	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 6C)
PMID:18562692	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 6C)
PMID:18562692	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 6C)
PMID:18562692	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 6C)
PMID:18562692	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. 6C)
PMID:18562692	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. 6C)
PMID:18562692	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. 6C)
PMID:18562692	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 6C)
PMID:18562692	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 6C)
PMID:18562692	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Table 1)
PMID:18562696	GO:0035974	meiotic spindle pole body [exists_during] meiosis I cell cycle phase	(Fig. 2)
PMID:18562696	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Fig. 2)
PMID:18562696	PomGeneEx:0000022	protein absent [during] single-celled organism vegetative growth phase	(Fig. 2A)
PMID:18562696	FYPO:0004632	decreased protein level during meiosis II [assayed_protein] PomBase:SPBC244.01c	(Fig. 3A)
PMID:18562696	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 95	(Fig. 3C)
PMID:18562696	FYPO:0006317	decreased protein localization to meiotic spindle pole body during meiosis II [assayed_protein] PomBase:SPCC417.06c	(Fig. 3D and E)
PMID:18562696	FYPO:0006317	decreased protein localization to meiotic spindle pole body during meiosis II [assayed_protein] PomBase:SPCC417.06c	(Fig. 3F)
PMID:18562696	FYPO:0006317	decreased protein localization to meiotic spindle pole body during meiosis II [assayed_protein] PomBase:SPCC417.06c	(Fig. 3F)
PMID:18562696	FYPO:0006317	decreased protein localization to meiotic spindle pole body during meiosis II [assayed_protein] PomBase:SPCC417.06c	(Fig. 3G)
PMID:18562696	FYPO:0006317	decreased protein localization to meiotic spindle pole body during meiosis II [assayed_protein] PomBase:SPCC417.06c	(Fig. 3G)
PMID:18562696	FYPO:0000346	small spores	(Fig. 4A and B)
PMID:18562696	FYPO:0000346	small spores	(Fig. 4A)
PMID:18562696	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 80	(Fig. 4C)
PMID:18562696	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 80	(Fig. 4C)
PMID:18562696	GO:1903023	regulation of ascospore-type prospore membrane formation	(Fig. 4C, 4F, 5A,B, 5E)
PMID:18562696	FYPO:0000581	decreased spore germination frequency	(Fig. 4D)
PMID:18562696	FYPO:0000581	decreased spore germination frequency	(Fig. 4D)
PMID:18562696	FYPO:0004484	abolished protein localization to prospore membrane [assayed_protein] PomBase:SPCC417.06c	(Fig. 4F)
PMID:18562696	FYPO:0006055	normal protein localization to meiotic spindle pole body during meiosis II [assayed_protein] PomBase:SPCC417.06c	(Fig. 4F)
PMID:18562696	FYPO:0006777	prospore membrane formation excluding nucleus	(Fig. 4H)
PMID:18562696	FYPO:0003139	abnormal sporulation resulting in formation of ascus containing anucleate spores [has_penetrance] 51	(Fig. 5A and B)
PMID:18562696	FYPO:0003845	normal protein localization to prospore membrane [assayed_protein] PomBase:SPBC1347.03	(Fig. 5C)
PMID:18562696	FYPO:0003845	normal protein localization to prospore membrane [assayed_protein] PomBase:SPCC825.03c	(Fig. 5D)
PMID:18562696	FYPO:0005737	delayed onset of prospore membrane formation	(Fig. 5E)
PMID:18562696	FYPO:0000346	small spores	(Fig. 6A)
PMID:18562696	FYPO:0000583	abolished sporulation	(Fig. 6B)
PMID:18562696	FYPO:0000583	abolished sporulation	(Fig. 6B)
PMID:18562696	FYPO:0003845	normal protein localization to prospore membrane [assayed_protein] PomBase:SPBC1347.03	(Fig. 6C)
PMID:18562696	FYPO:0003845	normal protein localization to prospore membrane [assayed_protein] PomBase:SPCC825.03c	(Fig. 6D)
PMID:18562696	FYPO:0006777	prospore membrane formation excluding nucleus	(Fig. 6E)
PMID:18562696	FYPO:0006777	prospore membrane formation excluding nucleus	(Fig. 6E)
PMID:18562696	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 80	(Fig. 7B)
PMID:18562696	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 60	(Fig. 7B)
PMID:18562696	FYPO:0006777	prospore membrane formation excluding nucleus	(Fig. 8B)
PMID:18562696	FYPO:0006777	prospore membrane formation excluding nucleus	(Fig. 8B)
PMID:18562696	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_protein] PomBase:SPAC9G1.09	(Fig. S1A)
PMID:18562696	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_protein] PomBase:SPBC428.13c	(Fig. S1A)
PMID:18562696	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_protein] PomBase:SPAC24B11.11c	(Fig. S1A)
PMID:18562696	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_protein] PomBase:SPBC21.06c	(Fig. S1A)
PMID:18562696	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_protein] PomBase:SPBC244.01c	(Fig. S1A)
PMID:18562696	FYPO:0003790	normal protein localization during meiosis [assayed_protein] PomBase:SPAC1F3.06c	(Fig. S2)
PMID:18562696	FYPO:0003790	normal protein localization during meiosis [assayed_protein] PomBase:SPBC19G7.05c	(Fig. S2)
PMID:18562696	FYPO:0000583	abolished sporulation	(Fig. S3)
PMID:18562696	FYPO:0000583	abolished sporulation	(Fig. S3)
PMID:18562696	FYPO:0000583	abolished sporulation	(Fig. S3)
PMID:18562696	FYPO:0000583	abolished sporulation	(Fig. S3)
PMID:18615848	FYPO:0002019	elongated telomeres during vegetative growth	(comment: same as swi7-H4 alone, i.e. it's dominant)
PMID:1863602	GO:0010515	negative regulation of induction of conjugation with cellular fusion	(comment: maybe not shown strongly in this paper but I'm trying to get the git genes annotated to this term because pka1 phosphorylates rst2 which excludes rst2 from the nucleus. rst2 when in the nucleus activates ste11 transcription.)
PMID:18640983	FYPO:0007061	normal Arp2/3 complex-mediated actin nucleation	(comment: CHECK in vitro)
PMID:18653539	FYPO:0006275	increased pyknosis during stationary phase	(Fig. 1D)
PMID:18653539	FYPO:0006276	increased karyorrhexis during stationary phase	(Fig. 1D, Fig. 1F)
PMID:18653539	FYPO:0003975	fragmented nuclear envelope	(Fig. 2F) (comment: CHECK during veg phase)
PMID:18653539	FYPO:0002060	viable vegetative cell population	(Figure 1A)
PMID:18653539	FYPO:0005231	loss of viability in stationary phase upon glucose starvation [has_severity] high	(Figure 1A, 8A)
PMID:18653539	FYPO:0005231	loss of viability in stationary phase upon glucose starvation [has_severity] high	(Figure 1B)
PMID:18653539	FYPO:0001673	normal nuclear morphology	(Figure 1C)
PMID:18653539	FYPO:0006289	increased cellular phytoceramide level	(Figure 2A)
PMID:18653539	FYPO:0005585	decreased cellular triglyceride level during vegetative growth	(Figure 2A)
PMID:18653539	FYPO:0004695	increased cellular diglyceride level	(Figure 2A)
PMID:18653539	FYPO:0004168	normal viability in stationary phase during glucose starvation	(Figure 8B)
PMID:18653539	FYPO:0004168	normal viability in stationary phase during glucose starvation	(Figure 8B)
PMID:18653539	FYPO:0004168	normal viability in stationary phase during glucose starvation	(Figure 8B)
PMID:18653539	FYPO:0004168	normal viability in stationary phase during glucose starvation	(Figure 8B)
PMID:18658154	FYPO:0003744	abolished protein localization to centromeric chromatin during vegetative growth	As shown in Fig. 1C, recruitment of RITS to both sites was abolished in ers1Δ cells.
PMID:18658154	FYPO:0000884	decreased histone H3-K9 trimethylation at centromere inner repeat during vegetative growth	We found that ers1Δ cells display a defect in both H3 Lys9 dimethylation and trimethylation (both normalized for nucleosome density) at the endogenous dh and dg regions of the centromeric outer repeats (Fig. 1B).
PMID:18658154	FYPO:0000878	decreased histone H3-K9 dimethylation at centromere inner repeat during vegetative growth	We found that ers1Δ cells display a defect in both H3 Lys9 dimethylation and trimethylation (both normalized for nucleosome density) at the endogenous dh and dg regions of the centromeric outer repeats (Fig. 1B).
PMID:18658154	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	We found that ers1Δ cells display a defect in both H3 Lys9 dimethylation and trimethylation (both normalized for nucleosome density) at the endogenous dh and dg regions of the centromeric outer repeats (Fig. 1B).
PMID:18658154	FYPO:0000890	decreased histone H3-K9 trimethylation at centromere outer repeat during vegetative growth	We found that ers1Δ cells display a defect in both H3 Lys9 dimethylation and trimethylation (both normalized for nucleosome density) at the endogenous dh and dg regions of the centromeric outer repeats (Fig. 1B).
PMID:18658154	FYPO:0006076	siRNA absent from cell	We observed an apparently complete defect in siRNA production (Fig. 2B).
PMID:18658154	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	ers1Δ mutant is completely defective in the silencing of ura4+ genes placed in the inner or outer repeats of cen1.
PMID:18658154	FYPO:0002567	normal centromeric outer repeat transcript level	nalysis revealed robust accumulation of the centromeric dg transcript in ers1Δ cells (Fig. 2A).
PMID:18658154	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	no defect in silencing of ura4+ reporter genes placed at mat3M or tel2R, where RNAi- dependent mechanisms act redundantly with RNAi-independent silencing mechanisms.
PMID:18658154	FYPO:0003555	normal chromatin silencing at subtelomere	no defect in silencing of ura4+ reporter genes placed at mat3M or tel2R, where RNAi- dependent mechanisms act redundantly with RNAi-independent silencing mechanisms.
PMID:18662319	GO:0034634	glutathione transmembrane transporter activity	(comment: also L-gamma-glutamyl-L-cysteine)
PMID:18667531	FYPO:0002061	inviable vegetative cell population	(comment: CHECK synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81) (Figure 2, C and D).
PMID:18667531	FYPO:0002061	inviable vegetative cell population	(comment: CHECK synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81) (Figure 2, C and D).
PMID:18667531	FYPO:0001234	slow vegetative cell population growth	(comment: CHECK synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81) (Figure 2, C and D).
PMID:18667531	FYPO:0001234	slow vegetative cell population growth	(comment: CHECK synthetic sick when combined with a deletion of the Holliday junction endonuclease Mus81) (Figure 2, C and D).
PMID:18667531	FYPO:0004329	normal mitotic rDNA separation	(comment: nulcleolus inheritance)
PMID:18667531	GO:0006281	DNA repair	On the basis of these data, we propose that the Nse1 NH-RING contributes to the DNA repair functions of the Smc5-Smc6 holocomplex.
PMID:18667531	FYPO:0000674	normal cell population growth at high temperature	The C219A mutant was not temperature sensitive (Figure 2A).
PMID:18667531	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC550.05 [assayed_protein] PomBase:SPCC645.04	The Nse1-Nse3 interaction is not perturbed by deletion of Nse1 NH-RING as tested by yeast two-hybrid assay, which is consistent with a previous report (Figure 5B and Sergeant et al., 2005).
PMID:18667531	FYPO:0001357	normal vegetative cell population growth	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensitive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensitive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	FYPO:0001357	normal vegetative cell population growth	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensitive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensitive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensitive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18667531	FYPO:0001357	normal vegetative cell population growth	The 􏰂RING, C197A, C199A, and C197A/C199A mutants were mildly temperature sensitive but grew normally at 25°C (Figure 2A and data not shown)
PMID:18676809	FYPO:0000088	sensitive to hydroxyurea	(Fig. 4a)
PMID:18676809	FYPO:0000268	sensitive to UV during vegetative growth	(Fig. 4a)
PMID:18676809	FYPO:0000268	sensitive to UV during vegetative growth	(Fig. 4a)
PMID:18676809	FYPO:0000268	sensitive to UV during vegetative growth	(Fig. 4a)
PMID:18676809	FYPO:0000085	sensitive to camptothecin	(Fig. 4a)
PMID:18676809	FYPO:0000085	sensitive to camptothecin	(Fig. 4a)
PMID:18676809	FYPO:0000085	sensitive to camptothecin	(Fig. 4a)
PMID:18676809	FYPO:0000088	sensitive to hydroxyurea	(Fig. 4a)
PMID:18676809	FYPO:0000088	sensitive to hydroxyurea	(Fig. 4a)
PMID:18676809	FYPO:0000006	abnormal mitotic DNA damage checkpoint	(Fig. 4a)
PMID:18676809	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPAC19G12.06c	"(comment: CHECK "")"
PMID:18676809	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPAC19G12.06c	"(comment: CHECK "")"
PMID:18676809	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPAC19G12.06c	"(comment: CHECK "")"
PMID:18676809	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPCC622.08c	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2-BRCT2 interaction with the peptide (Fig. 3A)
PMID:18676809	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPCC622.08c	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2-BRCT2 interaction with the peptide (Fig. 3A)
PMID:18676809	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPBC342.05	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2-BRCT2 interaction with the peptide (Fig. 3A)
PMID:18676809	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPBC342.05	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2-BRCT2 interaction with the peptide (Fig. 3A)
PMID:18676809	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPBC342.05	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2-BRCT2 interaction with the peptide (Fig. 3A)
PMID:18676809	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPCC622.08c	Consistent with their observed structural roles, charge reversal mutations Arg616Glu, Lys617Glu, and Lys619Glu all abolished Crb2-BRCT2 interaction with the peptide (Fig. 3A)
PMID:18676809	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPCC622.08c	Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C).
PMID:18676809	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPCC622.08c	Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C).
PMID:18676809	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPAC19G12.06c	Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C).
PMID:18676809	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPAC19G12.06c	Conversely, mutations disrupting dimerization did not disrupt -H2A.1 binding (Fig. 3C).
PMID:18676809	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPBC342.05	the Ser666Arg and Cys663Arg mutants ran as monomeric species in gel filtration, indicative of disruption of their dimerization
PMID:18676809	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC342.05 [assayed_protein] PomBase:SPBC342.05	the Ser666Arg and Cys663Arg mutants ran as monomeric species in gel filtration, indicative of disruption of their dimerization
PMID:18716626	FYPO:0002353	decreased chromatin silencing	(Fig. 1a)
PMID:18716626	FYPO:0000964	normal growth on thiabendazole	(Fig. 1a-d)
PMID:18716626	FYPO:0001513	normal mitotic sister chromatid segregation	(Fig. 1a-d)
PMID:18716626	FYPO:0005072	normal protein localization to centromeric chromatin [assayed_protein] PomBase:SPCC338.17c	(Fig. 1a-d)
PMID:18716626	FYPO:0007853	normal protein localization to centromere [assayed_protein] PomBase:SPAC17H9.20	(Fig. 1e, 1f) As predicted, the additional expression of Psc3-2CD (but not of 2CD alone) improved the localization of the cohesin complex to the peri-centromeric regions and also centromeric cohesion in swi6D cells
PMID:18716626	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] ~7	(Fig. 2a, 2b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
PMID:18716626	FYPO:0003182	sister chromatid nondisjunction at meiosis II	(Fig. 2a, 2b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
PMID:18716626	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] ~40	(Fig. 2a, 2b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
PMID:18716626	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] ~7	(Fig. 2a, 2b) As with sgo1D cells, swi6D cells undergo intact meiosis I but suffer a nondisjunction of sister chromatids in meiosis II
PMID:18716626	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_protein] PomBase:SPBP35G2.03c	(Fig. 2e) Sgo1 localization is impaired in swi6D cells
PMID:18716626	FYPO:0007853	normal protein localization to centromere [assayed_protein] PomBase:SPBP35G2.03c	(Fig. 2f) Sgo1-CD did indeed localize at the centromere regardless of swi6D
PMID:18716626	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBP35G2.03c [assayed_protein] PomBase:SPAC664.01c	(Fig. 3c) Accordingly, the replacement of Val 242 with Glu (VE) in Sgo1 abolished the interaction with Swi6 while preserving the interaction with Par1, a subunit of PP2A. An immunoprecipitation assay also supports the loss of the interaction of Sgo1-VE with Swi6
PMID:18716626	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBP35G2.03c [assayed_protein] PomBase:SPCC188.02	(Fig. 3c) Accordingly, the replacement of Val 242 with Glu (VE) in Sgo1 abolished the interaction with Swi6 while preserving the interaction with Par1, a subunit of PP2A. An immunoprecipitation assay also supports the loss of the interaction of Sgo1-VE with Swi6
PMID:18716626	FYPO:0007993	decreased protein localization to pericentromeric region during meiosis I	(Fig. 3c) Accordingly, the replacement of Val 242 with Glu (VE) in Sgo1 abolished the interaction with Swi6 while preserving the interaction with Par1, a subunit of PP2A. An immunoprecipitation assay also supports the loss of the interaction of Sgo1-VE with Swi6
PMID:18716626	FYPO:0007994	normal meiotic sister chromatid cohesion protection during meiotic anaphase I	(Fig. 3f and Supplementary Fig. 8). The Sgo1-VE protein, when fused with CDand thereby localized to the centromere, can perform its full functionin protecting Rec8
PMID:18716626	FYPO:0003182	sister chromatid nondisjunction at meiosis II	(Fig. 3f). The assay of chromosome segregation further revealed that sgo1-VE cells provoke nondisjunction in meiosis II, similarly to swi6D cells
PMID:18716626	FYPO:0000228	lagging mitotic chromosomes [has_severity] high [has_penetrance] 30	(Figure 1g) (comment: 30% cells?)
PMID:18716626	FYPO:0007853	normal protein localization to centromere [assayed_protein] PomBase:SPAC17H9.20	(Supplementary Fig. 2a) , but not in another heterochromatin-defective strain, clr4D, which lacks H3K9me (ref. 7)
PMID:18716626	FYPO:0007853	normal protein localization to centromere [assayed_protein] PomBase:SPAC17H9.20	(Supplementary Fig. 2a) We confirmed that Psc3-2CD, as well as 2CD, itself localizesat discrete nuclear dots in swi6D cell
PMID:18716626	FYPO:0002353	decreased chromatin silencing	(Supplementary Fig. 3a). We confirmed that the expression of Psc3-2CD does not restore transcriptional silencing in swi6D cells
PMID:18716626	FYPO:0003176	normal meiotic chromosome segregation [assayed_protein] PomBase:SPCC338.17c	(Supplementary Fig. 4). The transcriptional silencing of Swi6 is not relevant to this function, because swi6-sm1 cells have intact meiotic chromosome segregation
PMID:18716626	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPBP35G2.03c [part_of] meiotic centromeric cohesion protection in anaphase I [happens_during] meiotic anaphase I [occurs_in] chromosome, centromeric region	various: These results indicate that Swi6 is crucial in localizing Sgo1 and thereby promotes the protection of cohesin from separase during anaphase I.
PMID:18723894	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus	"RTS1 inversion background abolishes DSB formation; ""decreased"" level in rtf1-W405G is relative to wild type and above the inverted-RTS1 background level"
PMID:18723894	FYPO:0003084	abolished replication fork arrest at mating-type locus	no barrier activity with reversed polarity as in rtf1-S154L single mutant
PMID:18723894	FYPO:0003084	abolished replication fork arrest at mating-type locus	no barrier activity with reversed polarity as in rtf1-S154L single mutant
PMID:18725402	FYPO:0004337	abolished protein localization to mitochondrion [assayed_protein] PomBase:SPBC887.14c	(Fig. 2A)
PMID:18725402	FYPO:0004455	decreased protein localization to nucleus [assayed_protein] PomBase:SPBC887.14c [has_severity] high	(Fig. 2A)
PMID:18725402	FYPO:0000095	sensitive to bleomycin	(Fig. 7A)
PMID:18725402	FYPO:0000088	sensitive to hydroxyurea	(Fig. 7A)
PMID:18725402	GO:0006281	DNA repair	Based on their elongated cellular morphology, and large number of Rad22 foci, we conclude that cells depleted of nuclear Pfh1p suffer persistent DNA damage, and this damage triggers a G2 -phase arrest.
PMID:18725402	GO:0006281	DNA repair	Based on their elongated cellular morphology, and large number of Rad22 foci, we conclude that cells depleted of nuclear Pfh1p suffer persistent DNA damage, and this damage triggers a G2 -phase arrest.
PMID:18725402	FYPO:0002060	viable vegetative cell population	Importantly, combination of the pfh1-mt* allele with the pfh1-nuc allele (mt* X nuc) fully complemented the pfh1D strain at 18°C, arguing that the pfh1-mt* strain was indeed deficient in nuclear Pfh1p function (Table 2, line 12).
PMID:18725402	FYPO:0002060	viable vegetative cell population	Importantly, combination of the pfh1-mt* allele with the pfh1-nuc allele (mt* X nuc) fully complemented the pfh1D strain at 18°C, arguing that the pfh1-mt* strain was indeed deficient in nuclear Pfh1p function (Table 2, line 12).
PMID:18725402	GO:0043504	mitochondrial DNA repair	Pfh1p was also essential in mitochondria (Table 2), where its depletion resulted in rapid loss of mtDNA and very slow growth (Fig. 3 and 5).
PMID:18725402	GO:0043504	mitochondrial DNA repair	Pfh1p was also essential in mitochondria (Table 2), where its depletion resulted in rapid loss of mtDNA and very slow growth (Fig. 3 and 5).
PMID:18725402	GO:0005730	nucleolus	Since the two fusion proteins, Gar2p-mCherry and WT Pfh1p-GFP, colocalized (Fig. 2B), we conclude that nuclear Pfh1p is found throughout the nucleus but is concentrated in the nucleolus.
PMID:18725402	FYPO:0002061	inviable vegetative cell population	The pfh1-nuc allele (nuc) did not complement the pfh1D allele, indicating that the mitochondrial isoform of Pfh1p is essential (Table 2, line 4).
PMID:18725402	GO:0035861	site of double-strand break	WT Pfh1p-GFP colocalized with Rad22p- RFP in distinct nuclear foci (Fig. 2C).
PMID:18725402	GO:0035861	site of double-strand break	WT Pfh1p-GFP colocalized with Rad22p- RFP in distinct nuclear foci (Fig. 2C).
PMID:18725402	FYPO:0002061	inviable vegetative cell population	because the pfh1-mt* allele did not complement the catalytically inactive pfh1-K338A allele (mt* X cd) (Table 2, line 13), the ATPase/helicase activity of Pfh1p was essential in the nucleus.
PMID:18725402	FYPO:0002061	inviable vegetative cell population	but the pfh1-nuc allele in combination with the pfh1-K338A allele (nuc X cd) did not (Table 2, line 16). Therefore, the ATPase/helicase activity of Pfh1p was also essential in mitochondria.
PMID:18725402	FYPO:0002060	viable vegetative cell population	the pfh1-mt allele (mt) did complement pfh1D (Table 2, line 5)
PMID:18725402	FYPO:0002061	inviable vegetative cell population	when this strain was grown at 18°C, the pfh1-mt* allele did not complement pfh1D (402/ 407 His+ cells; Table 2, line 7).
PMID:18769921	FYPO:0001386	increased haploidization	(comment: during vegetative growth because non-sporulating strains used)
PMID:18769921	FYPO:0000473	increased mitotic recombination	(comment: during vegetative growth because non-sporulating strains used)
PMID:18769921	FYPO:0004437	normal mitotic recombination frequency	(comment: during vegetative growth because non-sporulating strains used)
PMID:18769921	FYPO:0001839	normal minichromosome loss	(comment: during vegetative growth because non-sporulating strains used)
PMID:18769921	FYPO:0001839	normal minichromosome loss	(comment: during vegetative growth because non-sporulating strains used)
PMID:18769921	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(comment: slightly more sensitive at low temperature than standard)
PMID:18769921	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(comment: slightly worse than sfr1delta alone)
PMID:18794373	FYPO:0007206	abolished replication fork arrest at rDNA repeats	(comment: arrest at Ter2 and Ter3 sites abolished)
PMID:18794373	FYPO:0007206	abolished replication fork arrest at rDNA repeats	(comment: arrest at Ter2 and Ter3 sites abolished)
PMID:18794373	FYPO:0007206	abolished replication fork arrest at rDNA repeats	(comment: arrest at Ter2 and Ter3 sites abolished)
PMID:18794373	FYPO:0007206	abolished replication fork arrest at rDNA repeats	(comment: arrest at Ter2 and Ter3 sites abolished)
PMID:18794373	FYPO:0007206	abolished replication fork arrest at rDNA repeats	(comment: arrest at Ter2 and Ter3 sites abolished)
PMID:18794373	FYPO:0007206	abolished replication fork arrest at rDNA repeats	(comment: arrest at Ter2 and Ter3 sites abolished)
PMID:18794373	GO:0043110	rDNA spacer replication fork barrier binding	(comment: binds at Ter3 site)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1B and C)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 1B and C)
PMID:18809570	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 1D)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 1D)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 1D)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 1E)
PMID:18809570	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC664.01c [assayed_protein] PomBase:SPAC664.01c	(Fig. 2C)
PMID:18809570	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC16C6.10 [assayed_protein] PomBase:SPBC16C6.10	(Fig. 2D)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 2E)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 2G)
PMID:18809570	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC622.16c [has_severity] high	(Fig. 4A)
PMID:18809570	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_region] dg_repeat [assayed_protein] PomBase:SPCC622.16c [has_severity] high	(Fig. 4A)
PMID:18809570	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC622.16c [has_severity] high	(Fig. 4A)
PMID:18809570	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC622.16c [has_severity] high	(Fig. 4A)
PMID:18809570	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC622.16c [has_severity] medium	(Fig. 4A)
PMID:18809570	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_region] dg_repeat [assayed_protein] PomBase:SPCC622.16c [has_severity] medium	(Fig. 4A)
PMID:18809570	FYPO:0005396	abolished protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPBC800.03	(Fig. 4D)
PMID:18809570	FYPO:0003744	abolished protein localization to centromeric chromatin during vegetative growth [assayed_region] dg_repeat [assayed_protein] PomBase:SPBC800.03	(Fig. 4D)
PMID:18809570	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_region] dg_repeat [assayed_protein] PomBase:SPBC800.03 [has_severity] high	(Fig. 4D)
PMID:18809570	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPBC800.03	(Fig. 4D)
PMID:18809570	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPBC800.03	(Fig. 4D)
PMID:18809570	FYPO:0005396	abolished protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPBC800.03	(Fig. 4D)
PMID:18809570	FYPO:0002360	normal chromatin silencing at centromere	(Fig. 5A)
PMID:18809570	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] low	(Fig. 5A)
PMID:18809570	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] low	(Fig. 5A)
PMID:18809570	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] medium	(Fig. 5A)
PMID:18809570	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	(Fig. 5A)
PMID:18809570	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	(Fig. 5A)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 5B)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 5B)
PMID:18809570	GO:0031934	mating-type region heterochromatin	(Fig. 7A)
PMID:18809570	GO:0005721	pericentric heterochromatin	(Fig. 7A)
PMID:18809570	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPBC16C6.10	(Fig. 7A)
PMID:18809570	GO:0140720	subtelomeric heterochromatin	(Fig. 7A)
PMID:18809570	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC16C6.10	(Fig. 7A)
PMID:18809570	FYPO:0001132	abolished protein localization to heterochromatin during vegetative growth [assayed_protein] PomBase:SPBC16C6.10	(Fig. 7A)
PMID:18809570	GO:0005721	pericentric heterochromatin	(Fig. 7B)
PMID:18809570	GO:0031934	mating-type region heterochromatin	(Fig. 7B)
PMID:18809570	FYPO:0001132	abolished protein localization to heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC664.01c	(Fig. 7B)
PMID:18809570	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC664.01c	(Fig. 7B)
PMID:18809570	GO:0140720	subtelomeric heterochromatin	(Fig. 7B)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 8D)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 8D)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 8D)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 8D)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 8H)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 8H)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 8H)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 8H)
PMID:18809570	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 9A)
PMID:18809570	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 9A)
PMID:18809570	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 9C)
PMID:18809570	FYPO:0008209	normal histone H3-K14 acetylation at silent mating-type cassette during vegetative growth	(Fig. 9D)
PMID:18809570	FYPO:0007633	increased histone H3-K14 acetylation at silent mating-type cassette during vegetative growth	(Fig. 9D)
PMID:18809570	GO:0031507	heterochromatin formation	Chp2’s function is not exclusively associated with the establishment step and that its continued activity is critical for the maintenance of heterochromatin. Fig. 3
PMID:18820678	FYPO:0006357	decreased chromatin remodeling during glucose starvation [assayed_region] PomBase:SPBC1198.14c	Chromatin remodelling events and RNAPII loading around the TATA box are severely impaired in an atf12 mutant, demonstrating that the progression of ncRNA initiation events mediated by Atf1 is essential to convert chromatin to an RNAPII accessible state (Fig. 4B).
PMID:18820678	FYPO:0008156	RNA absent from cell during cellular response to glucose starvation	Expression of transcript c is not restored in the atf12tup112tup122 mutant, suggesting that Atf1 is essential to induce transcript c.
PMID:18820678	FYPO:0004171	normal RNA level during glucose starvation [assayed_transcript] PomBase:SPNCRNA.4604	In the atf1- mutant, transcripts a and b are expressed normally, whereas transcripts c and d are absent (Fig. 4A).
PMID:18820678	FYPO:0008156	RNA absent from cell during cellular response to glucose starvation [assayed_transcript] PomBase:SPNCRNA.1325	In the atf1- mutant, transcripts a and b are expressed normally, whereas transcripts c and d are absent (Fig. 4A).
PMID:18820678	FYPO:0004171	normal RNA level during glucose starvation [assayed_transcript] PomBase:SPNCRNA.1326	In the atf1- mutant, transcripts a and b are expressed normally, whereas transcripts c and d are absent (Fig. 4A).
PMID:18820678	FYPO:0008156	RNA absent from cell during cellular response to glucose starvation [assayed_transcript] PomBase:SPBC1198.14c	In the atf1- mutant, transcripts a and b are expressed normally, whereas transcripts c and d are absent (Fig. 4A).
PMID:18820678	FYPO:0004171	normal RNA level during glucose starvation [assayed_transcript] PomBase:SPNCRNA.1325	In the rst22 mutant, transcripts a, b, and c are expressed normally, whereas transcript d is absent (Fig. 4A).
PMID:18820678	FYPO:0008156	RNA absent from cell during cellular response to glucose starvation [assayed_transcript] PomBase:SPBC1198.14c	In the rst22 mutant, transcripts a, b, and c are expressed normally, whereas transcript d is absent (Fig. 4A).
PMID:18820678	FYPO:0004171	normal RNA level during glucose starvation [assayed_transcript] PomBase:SPNCRNA.4604	In the rst22 mutant, transcripts a, b, and c are expressed normally, whereas transcript d is absent (Fig. 4A).
PMID:18820678	FYPO:0004171	normal RNA level during glucose starvation [assayed_transcript] PomBase:SPNCRNA.1326	In the rst22 mutant, transcripts a, b, and c are expressed normally, whereas transcript d is absent (Fig. 4A).
PMID:18820678	FYPO:0004171	normal RNA level during glucose starvation	Moreover, fbp11 derepression is recovered by deleting both tup111 and tup121, indicating that Atf1 and Rst2 are dispensable for fbp11 induction in the absence of both Tup proteins
PMID:18820678	FYPO:0004171	normal RNA level during glucose starvation	Moreover, fbp11 derepression is recovered by deleting both tup111 and tup121, indicating that Atf1 and Rst2 are dispensable for fbp11 induction in the absence of both Tup proteins
PMID:18849471	GO:0004585	ornithine carbamoyltransferase activity	(comment: major)
PMID:18854158	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC13C5.07 [assayed_using] PomBase:SPAC13C5.07	(comment: abolished interaction between wt and mutant; interaction partially restored if both copies are mutant)
PMID:18854158	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC13C5.07 [assayed_using] PomBase:SPAC13C5.07	(comment: abolished interaction between wt and mutant; interaction partially restored if both copies are mutant)
PMID:18854158	FYPO:0000085	sensitive to camptothecin	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000268	sensitive to UV during vegetative growth	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000085	sensitive to camptothecin	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000268	sensitive to UV during vegetative growth	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000085	sensitive to camptothecin	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000085	sensitive to camptothecin	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000268	sensitive to UV during vegetative growth	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000268	sensitive to UV during vegetative growth	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18854158	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: no extension because growth is decreased generally, making expressivity hard to judge)
PMID:18948543	FYPO:0003097	abolished histone H3-K9 methylation at centromere outer repeat during vegetative growth	(Fig. 3A and fig. S3).
PMID:18948543	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] high	Chromatin immunoprecipitation (ChIP) revealed that splicing mutants cwf10-1 and prp10-1 (but not prp2-1) exhibited only a modest decrease in levels of H3K9me2 associated with both centromere repeats and cen1:ura4+ (Fig. 3A and fig. S3).
PMID:18948543	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] medium	Chromatin immunoprecipitation (ChIP) revealed that splicing mutants cwf10-1 and prp10-1 (but not prp2-1) exhibited only a modest decrease in levels of H3K9me2 associated with both centromere repeats and cen1:ura4+ (Fig. 3A and fig. S3).
PMID:18948543	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] medium	Chromatin immunoprecipitation (ChIP) revealed that splicing mutants cwf10-1 and prp10-1 (but not prp2-1) exhibited only a modest decrease in levels of H3K9me2 associated with both centromere repeats and cen1:ura4+ (Fig. 3A and fig. S3).
PMID:18948543	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPAC664.01c	Chromatin immunoprecipitation (ChIP) revealed that splicing mutants cwf10-1 and prp10-1 (but not prp2-1) exhibited only a modest decrease in levels of H3K9me2 associated with both centromere repeats and cen1:ura4+ (Fig. 3A and fig. S3).
PMID:18948543	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPAC664.01c	Chromatin immunoprecipitation (ChIP) revealed that splicing mutants cwf10-1 and prp10-1 (but not prp2-1) exhibited only a modest decrease in levels of H3K9me2 associated with both centromere repeats and cen1:ura4+ (Fig. 3A and fig. S3).
PMID:18948543	FYPO:0003619	normal mRNA splicing, via spliceosome	However, at the permissive temperature of 25°C (at which centromeric silencing was alleviated), splicing efficiency was similar to that in wild-type cells (Fig. 2A).
PMID:18948543	FYPO:0003619	normal mRNA splicing, via spliceosome	However, at the permissive temperature of 25°C (at which centromeric silencing was alleviated), splicing efficiency was similar to that in wild-type cells (Fig. 2A).
PMID:18948543	FYPO:0003619	normal mRNA splicing, via spliceosome	However, at the permissive temperature of 25°C (at which centromeric silencing was alleviated), splicing efficiency was similar to that in wild-type cells (Fig. 2A).
PMID:18948543	FYPO:0003619	normal mRNA splicing, via spliceosome	However, at the permissive temperature of 25°C (at which centromeric silencing was alleviated), splicing efficiency was similar to that in wild-type cells (Fig. 2A).
PMID:18948543	FYPO:0003619	normal mRNA splicing, via spliceosome	However, at the permissive temperature of 25°C (at which centromeric silencing was alleviated), splicing efficiency was similar to that in wild-type cells (Fig. 2A).
PMID:18948543	FYPO:0003619	normal mRNA splicing, via spliceosome	However, at the permissive temperature of 25°C (at which centromeric silencing was alleviated), splicing efficiency was similar to that in wild-type cells (Fig. 2A).
PMID:18948543	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0000220	increased centromeric outer repeat transcript level	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0000220	increased centromeric outer repeat transcript level	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0000220	increased centromeric outer repeat transcript level	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0000220	increased centromeric outer repeat transcript level	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0000220	increased centromeric outer repeat transcript level	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	In contrast, mutations in prp5 (Prp46Sc/PLRG1Hs), prp8 (Prp2Sc/DHX16Hs), prp10 (Hsh155Sc/ SF3B1Hs), and prp12 (Rse1Sc/SF3B2Hs), like cwf10 and prp39, alleviated cen1:ade6+ silencing (Fig. 1B) and increased cen1:ade6+ transcript accumulation (Fig. 1C, ade6)
PMID:18948543	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level	Moreover, mutants that alleviated cen1:ade6+ silencing also displayed increased levels of noncoding centromeric otr transcripts and concomitant reductions in centromeric siRNA accumulation, with prp10-1 showing the most severe silencing defects (Fig. 1C
PMID:18948543	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] high	Moreover, mutants that alleviated cen1:ade6+ silencing also displayed increased levels of noncoding centromeric otr transcripts and concomitant reductions in centromeric siRNA accumulation, with prp10-1 showing the most severe silencing defects (Fig. 1C
PMID:18948543	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level	Moreover, mutants that alleviated cen1:ade6+ silencing also displayed increased levels of noncoding centromeric otr transcripts and concomitant reductions in centromeric siRNA accumulation, with prp10-1 showing the most severe silencing defects (Fig. 1C
PMID:18948543	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level	Moreover, mutants that alleviated cen1:ade6+ silencing also displayed increased levels of noncoding centromeric otr transcripts and concomitant reductions in centromeric siRNA accumulation, with prp10-1 showing the most severe silencing defects (Fig. 1C
PMID:18948543	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	We therefore constructed strains in which the endogenous ago1+ and hrr1+ genes were replaced by cDNAs. Even in these strains, the prp10-1 mutation alleviated silencing as in wild-type cells (Fig. 2C, white colonies).
PMID:18948543	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	We therefore constructed strains in which the endogenous ago1+ and hrr1+ genes were replaced by cDNAs. Even in these strains, the prp10-1 mutation alleviated silencing as in wild-type cells (Fig. 2C, white colonies).
PMID:18948543	FYPO:0004742	normal chromatin silencing at centromere outer repeat	we surveyed several additional ts lethal splicing mutants for silencing defects at the permissive temperature (11-14). Only particular splicing mutants affected silencing. Silencing of a centromeric cen1:ade6+ marker gene (Fig. 1A) remained intact in the presence of prp1 (Prp6Sc/Hs), prp2 (U2AFHs), prp3 (Prp3Sc/PRPF3Hs), or prp4 (PRPF4BHs) mutations
PMID:18948543	FYPO:0004742	normal chromatin silencing at centromere outer repeat	we surveyed several additional ts lethal splicing mutants for silencing defects at the permissive temperature (11-14). Only particular splicing mutants affected silencing. Silencing of a centromeric cen1:ade6+ marker gene (Fig. 1A) remained intact in the presence of prp1 (Prp6Sc/Hs), prp2 (U2AFHs), prp3 (Prp3Sc/PRPF3Hs), or prp4 (PRPF4BHs) mutations
PMID:18948543	FYPO:0004742	normal chromatin silencing at centromere outer repeat	we surveyed several additional ts lethal splicing mutants for silencing defects at the permissive temperature (11-14). Only particular splicing mutants affected silencing. Silencing of a centromeric cen1:ade6+ marker gene (Fig. 1A) remained intact in the presence of prp1 (Prp6Sc/Hs), prp2 (U2AFHs), prp3 (Prp3Sc/PRPF3Hs), or prp4 (PRPF4BHs) mutations
PMID:18948543	FYPO:0004742	normal chromatin silencing at centromere outer repeat	we surveyed several additional ts lethal splicing mutants for silencing defects at the permissive temperature (11-14). Only particular splicing mutants affected silencing. Silencing of a centromeric cen1:ade6+ marker gene (Fig. 1A) remained intact in the presence of prp1 (Prp6Sc/Hs), prp2 (U2AFHs), prp3 (Prp3Sc/PRPF3Hs), or prp4 (PRPF4BHs) mutations
PMID:18951025	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC1782.09c	(comment: one or more of mutated serine residues)
PMID:18951025	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC1782.09c	(comment: one or more of mutated serine residues)
PMID:18957202	FYPO:0004909	loss of punctate nuclear protein localization, with protein distributed in nucleus [assayed_using] PomBase:SPAC664.01c	(Figure 1A)
PMID:18957202	GO:0005634	nucleus	(Figure 2A)
PMID:18957202	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Figure 5F) the point mutation resulted in a significant loss of silencing at the centromere otr region.
PMID:18957202	GO:0033696	heterochromatin boundary formation [occurs_at] mating-type region heterochromatin	(comment: RNAI dependent)
PMID:18957202	FYPO:0001352	abnormal chromatin organization during vegetative growth [has_penetrance] 28	28% of the cells contained fragmented nuclear DNA (Figure 2D), indicating that the mutant nucleus is disorganized.
PMID:18957202	FYPO:0007345	increased euchromatin-derived RNA level	About 50% (2665 out of 5241) of the genes in the genome were downregulated in mutant cells compared to WT (Figure 6C and Table S3), consistent with the formation of ectopic heterochromatin.
PMID:18957202	FYPO:0000091	sensitive to thiabendazole [has_severity] high	As shown in Figure 2E, lid2-j, like clr8Δ, is hypersensitive to TBZ
PMID:18957202	FYPO:0004170	abolished histone H3-K9 dimethylation at centromere during vegetative growth	As shown in Figure 3B, H3K9 methylation at the centromere was completely abolished.
PMID:18957202	FYPO:0004205	decreased siRNA level [has_severity] high	As shown in Figure 5C, siRNA is barely detectable.
PMID:18957202	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_using] PomBase:SPCC736.11	As shown in Figure 5D, the association of Ago1 with the centromere is significantly reduced in lid2-j, indicating that Lid2 is required for RITS to load onto centromeres.
PMID:18957202	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_using] PomBase:SPBP19A11.06	As shown in Figure 5E, while Lid2 accumulated at centromeres in the WT, the centromere localization of Lid2 in the clr8 mutant is significantly decreased.
PMID:18957202	FYPO:0007337	increased histone H3-K4 methylation at centromere during vegetative growth	ChIP assays indicated that H3K9me2 methylation at the region was abolished, while H3K4me3 methylation was increased more than seven-fold (Figure S2)
PMID:18957202	FYPO:0004170	abolished histone H3-K9 dimethylation at centromere during vegetative growth	ChIP assays indicated that H3K9me2 methylation at the region was abolished, while H3K4me3 methylation was increased more than seven-fold (Figure S2)
PMID:18957202	GO:0003682	chromatin binding	GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A).
PMID:18957202	GO:0031934	mating-type region heterochromatin	GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A).showed enrichment of DNA from centromeres and the mating-type region, indicating Lid2 is associated with heterochromatin (Figure 2B).
PMID:18957202	GO:0005721	pericentric heterochromatin	GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A).showed enrichment of DNA from centromeres and the mating-type region, indicating Lid2 is associated with heterochromatin (Figure 2B).
PMID:18957202	GO:0005721	pericentric heterochromatin	GFP-Lid2 is resistant to detergent extraction indicating Lid2 is a chromatin-binding protein (Figure 2A).showed enrichment of DNA from centromeres and the mating-type region, indicating Lid2 is associated with heterochromatin (Figure 2B).
PMID:18957202	FYPO:0002368	decreased histone H3-K4 trimethylation during vegetative growth [has_severity] high	H3K4me3 staining was reduced to nearly undetectable levels in 82% of the cells overexpressing Lid2, suggesting that Lid2 can specifically demethylate H3K4 me3 (Figure 4B)
PMID:18957202	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_using] PomBase:SPCC613.12c	In WT cells, Myc- Clr8 associates with centromere otr regions, but not in lid2-j suggesting that Lid2 is required for Clr8 association with heterochromatin (Figure 5E).
PMID:18957202	FYPO:0007341	normal histone H3-K4 trimethylation during vegetative growth [has_severity] high	In contrast to the overexpression of Lid2 alone, which leads to a dramatic decrease in H3K4me3 (Figure 4B), reduction of H3K4me3 is minimal when Set1 or Lsd1 is also overexpressed (Figure 4C).
PMID:18957202	FYPO:0007338	increased histone H3-K4 trimethylation at centromere during vegetative growth	In contrast, H3K4me3 methylation was increased significantly (Figure 3C)
PMID:18957202	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth	Obvious reduction of H3K9 methylation was also observed in lid2-phd2 and lid2-phd3 mutants (Figure S9)
PMID:18957202	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth	Obvious reduction of H3K9 methylation was also observed in lid2-phd2 and lid2-phd3 mutants (Figure S9)
PMID:18957202	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	WT and frequently exhibited an aberrant elongated cell shape (Figure 2C)
PMID:18957202	FYPO:0000452	abnormal protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPAC664.01c	We also examined the GFP-Swi6 distribution in the mutants (Figure 7B). While the lid2-phd1 mutant is similar to the WT, the nuclei in the lid2-phd2 and lid2-phd3 mutants often contained excessive GFP- Swi6 dots, suggesting that euchromatin assembly is disrupted in the mutants (Figure 7B).
PMID:18957202	FYPO:0007341	normal histone H3-K4 trimethylation during vegetative growth [has_severity] high	We also examined the GFP-Swi6 distribution in the mutants (Figure 7B). While the lid2-phd1 mutant is similar to the WT, the nuclei in the lid2-phd2 and lid2-phd3 mutants often contained excessive GFP- Swi6 dots, suggesting that euchromatin assembly is disrupted in the mutants (Figure 7B).
PMID:18957202	FYPO:0002151	inviable spore	We deleted one copy of lid2+ by kanamycin reporter gene replacement (kan+) in a WT diploid strain (lid2+/lid2Δ::kan+) and tetrad analysis was performed after sporulation. Only two germinating spores from a tetrad were viable, confirming that lid2+ is an essential gene
PMID:18957202	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	We found that deletion of the Lid2 JmjC domain resulted in the complete loss of ura4+ silencing at both the otr and imr loci (Figure 3A and Figure 7A).
PMID:18957202	FYPO:0007335	abolished chromatin silencing at centromere inner repeat	We found that deletion of the Lid2 JmjC domain resulted in the complete loss of ura4+ silencing at both the otr and imr loci (Figure 3A and Figure 7A).
PMID:18957202	FYPO:0000825	increased RNA level during vegetative growth	We further noted the striking similarity of the genome-wide transcription profiles of the lid2-j and lsd1Δ mutants (Figure 6C), suggest
PMID:18957202	FYPO:0000452	abnormal protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPAC664.01c	We next examined Swi6 localization in the lid2-j mutant using N-terminal tagged GFP-Swi6. In WT vegetative cells, 3-4 GFP-Swi6 spots are observed. This is because the three centromeres cluster on the nuclear envelope in the vicinity of the spindle pole body whereas telomeres loosely cluster on the nuclear envelope, apart from centromeres. clr4 and clr8 mutants have a diffuse Swi6 localization due to the disruption of heterochromatin. To our surprise, we did not see the same GFP-Swi6 pattern in the lid2-j mutant as in clr8Δ. Rather, we found that 78% of the cells contain more than 5 GFP-Swi6 spots, with nearly 30% having more than 10 spots (Figure 6A). The abnormal distribution of Swi6 also can be observed in meiotic horsetail stage nuclei (Figure 6A). The aberrant Swi6 localization is not caused by defects in centromere or telomere clustering since the distribution of centromeres and telomeres, as marked by Cnp1-GFP or Taz1-GFP respectively, is unaffected in the lid2-j mutant (Figure S4). We further confirmed that telomeres cluster normally by visualizing their distribution in a lid2-j strain carrying mCherry-Swi6 and the telomere marker Taz1-GFP (Figure S4). These results suggest that heterochromatin is induced in euchromatic regions in lid2-j.
PMID:18957202	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_using] PomBase:SPBC428.08c	We then determined whether Lid2 is required for the recruitment of Clr4 to heterochromatin. We carried out a ChIP experiment using lid2-j or clr8Δ containing a N-terminal FLAG-tagged Clr4. The localization of Clr4 at centromeres is abrogated in both mutants (Figure 3E).
PMID:18957202	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_using] PomBase:SPBC428.08c	We then determined whether Lid2 is required for the recruitment of Clr4 to heterochromatin. We carried out a ChIP experiment using lid2-j or clr8Δ containing a N-terminal FLAG-tagged Clr4. The localization of Clr4 at centromeres is abrogated in both mutants (Figure 3E).
PMID:18957202	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_using] PomBase:SPAC664.01c	drastic reduction of Swi6 binding (Figure 3D).
PMID:18957202	FYPO:0000220	increased centromeric outer repeat transcript level	forward and reverse centromeric strands were detected in lid2-j and accumulated at the same level as in clr8Δ, suggesting that Lid2 is involved in the RNAi pathway.
PMID:18957202	FYPO:0007339	increased cen-dg RNA level	forward and reverse centromeric strands were detected in lid2-j and accumulated at the same level as in clr8Δ, suggesting that Lid2 is involved in the RNAi pathway.
PMID:18957202	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	mating-type region was likewise reduced (Figure 3A)
PMID:18957202	FYPO:0000874	increased histone H3-K9 dimethylation at centromere during vegetative growth	overexpressing Lid2 enhances H3K9 methylation (Figures 5G and H)
PMID:18957202	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	silencing at the imr region in lid2-phd2 and lid2-phd3 mutants was significantly impaired while lid2-phd1 showed only a slight defect (Figure 7A).
PMID:18957202	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	silencing at the imr region in lid2-phd2 and lid2-phd3 mutants was significantly impaired while lid2-phd1 showed only a slight defect (Figure 7A).
PMID:18957202	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	silencing at the imr region in lid2-phd2 and lid2-phd3 mutants was significantly impaired while lid2-phd1 showed only a slight defect (Figure 7A).
PMID:18957202	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBP19A11.06 [assayed_using] PomBase:SPCC306.04c	the point mutation had little effect on the interaction of Lid2 with its interacting partners, such as Cul4 and Set1 (Figure S3 and S8).
PMID:18957202	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBP19A11.06 [assayed_using] PomBase:SPAC3A11.08	the point mutation had little effect on the interaction of Lid2 with its interacting partners, such as Cul4 and Set1 (Figure S3 and S8).
PMID:1899284	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	(comment: also supported by complementation of S.c. deletion)
PMID:19001497	FYPO:0002112	viable curved vegetative cell [has_penetrance] high	(Fig. 1C)
PMID:19001497	FYPO:0002112	viable curved vegetative cell [has_penetrance] low	(Fig. 1C)
PMID:19001497	FYPO:0002112	viable curved vegetative cell [has_penetrance] high	(Fig. 1C)
PMID:19001497	FYPO:0002112	viable curved vegetative cell [has_penetrance] high	(Fig. 1C)
PMID:19001497	FYPO:0005697	abolished cytoplasmic interphase microtubule nucleation from spindle pole body [has_penetrance] complete	(Fig. 1D)
PMID:19001497	FYPO:0005696	abolished cytoplasmic microtubule nucleation from iMTOC [has_penetrance] complete	(Fig. 1D)
PMID:19001497	FYPO:0005694	decreased interphase microtubule nucleation [has_severity] medium	(Fig. 1D, 1E)
PMID:19001497	FYPO:0005697	abolished cytoplasmic interphase microtubule nucleation from spindle pole body [has_penetrance] complete	(Fig. 1D, 1E)
PMID:19001497	FYPO:0005696	abolished cytoplasmic microtubule nucleation from iMTOC [has_penetrance] complete	(Fig. 1D, 1E)
PMID:19001497	FYPO:0005696	abolished cytoplasmic microtubule nucleation from iMTOC [has_penetrance] complete	(Fig. 1D, 1E)
PMID:19001497	FYPO:0005697	abolished cytoplasmic interphase microtubule nucleation from spindle pole body [has_penetrance] complete	(Fig. 1D, 1E)
PMID:19001497	FYPO:0004511	long curved interphase microtubules	(Fig. 1E)
PMID:19001497	FYPO:0005696	abolished cytoplasmic microtubule nucleation from iMTOC	(Fig. 1E)
PMID:19001497	FYPO:0004511	long curved interphase microtubules	(Fig. 1E)
PMID:19001497	FYPO:0004511	long curved interphase microtubules	(Fig. 1E)
PMID:19001497	GO:0044732	mitotic spindle pole body	(Fig. 2B, 2C)
PMID:19001497	GO:0000923	equatorial microtubule organizing center	(Fig. 2B, 2C)
PMID:19001497	GO:0031021	interphase microtubule organizing center	(Fig. 2B, 2C)
PMID:19001497	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC365.15	(Fig. 2D-F)
PMID:19001497	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC365.15	(Fig. 2D-F)
PMID:19001497	FYPO:0005700	abolished protein localization to eMTOC [assayed_using] PomBase:SPBC365.15	(Fig. 2D-F)
PMID:19001497	FYPO:0005701	abolished protein localization to iMTOC [assayed_using] PomBase:SPBC365.15	(Fig. 2D-F)
PMID:19001497	FYPO:0005701	abolished protein localization to iMTOC [assayed_using] PomBase:SPBC365.15	(Fig. 2D-F)
PMID:19001497	FYPO:0005708	normal protein localization to iMTOC [assayed_using] PomBase:SPCC417.07c	(Fig. 2D-F)
PMID:19001497	FYPO:0005707	normal protein localization to eMTOC [assayed_using] PomBase:SPCC417.07c	(Fig. 2D-F)
PMID:19001497	FYPO:0005707	normal protein localization to eMTOC [assayed_using] PomBase:SPCC417.07c	(Fig. 2D-F)
PMID:19001497	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_using] PomBase:SPCC417.07c	(Fig. 2D-F)
PMID:19001497	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_using] PomBase:SPCC417.07c	(Fig. 2D-F)
PMID:19001497	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC32F12.04 [assayed_using] PomBase:SPCC417.07c	(Fig. 2a) (comment: this fig also has expression level for mutant alleles)
PMID:19001497	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC417.07c [assayed_using] PomBase:SPBC365.15	(Fig. 3)
PMID:19001497	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC417.07c [assayed_using] PomBase:SPBC365.15	(Fig. 3)
PMID:19001497	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC417.07c [assayed_using] PomBase:SPBC365.15	(Fig. 3)
PMID:19001497	FYPO:0005696	abolished cytoplasmic microtubule nucleation from iMTOC	(Fig. 4D)
PMID:19001497	FYPO:0005699	normal interphase microtubule nucleation from spindle pole body	(Fig. 4D)
PMID:19001497	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPBC365.15	(Fig. 4F)
PMID:19001497	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPBC365.15	(Fig. 4F)
PMID:19001497	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC417.07c [assayed_using] PomBase:SPBC902.06	(Fig. 4a)
PMID:19001497	FYPO:0002112	viable curved vegetative cell	(Fig. 4c)
PMID:19001497	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC417.07c [assayed_using] PomBase:SPBC32F12.04	(Fig. 4c)
PMID:19001497	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPCC417.07c	supplementary material Fig. S1)
PMID:19001497	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPCC417.07c	supplementary material Fig. S1)
PMID:19001497	FYPO:0005691	decreased spindle pole body-led chromosome movement during mitotic interphase	supplementary material Movies 2-4).
PMID:19001497	FYPO:0005691	decreased spindle pole body-led chromosome movement during mitotic interphase	supplementary material Movies 2-4).
PMID:19001497	FYPO:0005691	decreased spindle pole body-led chromosome movement during mitotic interphase	supplementary material Movies 2-4).
PMID:19001497	FYPO:0004619	cytoplasmic microtubules nucleated from eMTOC absent from cell	supplementary material Movies 2-4).
PMID:19001497	GO:0106006	cytoskeletal protein-membrane anchor activity [has_input] PomBase:SPBC32F12.04 [part_of] astral microtubule nucleation [occurs_in] extrinsic component of nuclear outer membrane [happens_during] mitotic interphase	we conclude that the function of Mto2 in MT nucleation is mediated primarily, if not exclusively, via its binding to Mto1. Moreover, the failure of Mto1-334 to immunoprecipitate the γ-TuC indicates that the Mto1-Mto2 interaction is required for an efficient association of Mto1 with the γ-TuC, as detected in cytoplasmic extracts.
PMID:19001497	GO:0106006	cytoskeletal protein-membrane anchor activity [has_input] PomBase:SPBC32F12.04 [part_of] astral microtubule nucleation [occurs_in] extrinsic component of nuclear outer membrane [happens_during] mitotic interphase	we conclude that the function of Mto2 in MT nucleation is mediated primarily, if not exclusively, via its binding to Mto1. Moreover, the failure of Mto1-334 to immunoprecipitate the γ-TuC indicates that the Mto1-Mto2 interaction is required for an efficient association of Mto1 with the γ-TuC, as detected in cytoplasmic extracts.
PMID:19023408	GO:0045027	DNA end binding	(comment: forms covalent linkage upon binding (wouldn't normally use ChIP as IDA for DNA binding MF, but the phenol extraction with or without protease adds more confidence))
PMID:19026779	FYPO:0004067	decreased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004068	decreased phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0005041	increased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004067	decreased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004068	decreased phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004067	decreased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004068	decreased phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004067	decreased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004068	decreased phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004068	decreased phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004067	decreased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004067	decreased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004068	decreased phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004067	decreased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0008061	abolished phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004069	abolished phosphorylation of RNA polymerase II C-terminal domain serine 2 residues [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004067	decreased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0005061	normal phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004067	decreased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004068	decreased phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0005041	increased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004067	decreased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004068	decreased phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0005041	increased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0005184	increased phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0005041	increased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004067	decreased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19026779	FYPO:0004068	decreased phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure 4D)
PMID:19033384	GO:0031571	mitotic G1 DNA damage checkpoint signaling	(comment: The checkpoint doesn't sense all types of dna damage eg that caused by gamma radiation or DNA adduct formation by UVA)
PMID:19033384	MOD:00046	O-phospho-L-serine [added_during] cellular response to leucine starvation	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	MOD:00046	O-phospho-L-serine [added_during] cellular response to hydrogen peroxide	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	MOD:00046	O-phospho-L-serine [added_during] cellular response to methyl methanesulfonate	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	MOD:00046	O-phospho-L-serine [added_during] cellular response to UV-C [added_during] mitotic G2 phase	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	MOD:00046	O-phospho-L-serine [added_during] cellular response to UV-C [added_during] mitotic S phase	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	MOD:00046	O-phospho-L-serine [absent_during] cellular response to gamma radiation	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	MOD:00046	O-phospho-L-serine [added_during] DNA damage response [added_during] mitotic G1 phase	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19033384	MOD:00046	O-phospho-L-serine [added_during] cellular response to UV-C [added_during] mitotic G1 phase	(comment: Use of Western blot to assay phosphorylation levels)
PMID:19037094	FYPO:0001883	normal growth on caspofungin	(Fig. 1)
PMID:19037094	FYPO:0001883	normal growth on caspofungin	(Fig. 1)
PMID:19037094	FYPO:0000079	sensitive to caspofungin [has_severity] high	(Fig. 1, Fig. 2D and Fig. 3)
PMID:19037094	FYPO:0001473	resistance to tacrolimus during salt stress	(Fig. 2A)
PMID:19037094	FYPO:0001473	resistance to tacrolimus during salt stress	(Fig. 2A)
PMID:19037094	FYPO:0001473	resistance to tacrolimus during salt stress	(Fig. 2A)
PMID:19037094	FYPO:0002720	sensitive to beta-glucanase	(Fig. 2B)
PMID:19037094	FYPO:0002720	sensitive to beta-glucanase	(Fig. 2B)
PMID:19037094	FYPO:0001214	sensitive to potassium chloride	(Fig. 2C)
PMID:19037094	FYPO:0001214	sensitive to potassium chloride	(Fig. 2C)
PMID:19037094	FYPO:0000079	sensitive to caspofungin [has_severity] medium	(Fig. 2D and Fig. 3B)
PMID:19037094	FYPO:0000079	sensitive to caspofungin [has_severity] medium	(Fig. 2D and Fig. 3B)
PMID:19037094	FYPO:0000079	sensitive to caspofungin [has_severity] medium	(Fig. 2D and Fig. 3B)
PMID:19037094	FYPO:0000079	sensitive to caspofungin	(Fig. 2D)
PMID:19037094	FYPO:0001883	normal growth on caspofungin	(Fig. 2D)
PMID:19037094	FYPO:0000079	sensitive to caspofungin	(Fig. 2D)
PMID:19037094	FYPO:0001883	normal growth on caspofungin	(Fig. 2D)
PMID:19037094	FYPO:0001883	normal growth on caspofungin	(Fig. 2D)
PMID:19037094	FYPO:0001883	normal growth on caspofungin	(Fig. 3A)
PMID:19037094	FYPO:0001883	normal growth on caspofungin	(Fig. 3A)
PMID:19037094	FYPO:0000079	sensitive to caspofungin [has_severity] high	(Fig. 3B)
PMID:19037094	FYPO:0000079	sensitive to caspofungin [has_severity] high	(Fig. 3B)
PMID:19037094	FYPO:0000079	sensitive to caspofungin [has_severity] high	(Fig. 3B)
PMID:19037094	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPBC119.08	(Fig. 4A)
PMID:19037094	FYPO:0001885	decreased protein phosphorylation during salt stress [assayed_protein] PomBase:SPBC119.08	(Fig. 4A)
PMID:19037094	FYPO:0002376	decreased protein phosphorylation during cellular response to osmotic stress [assayed_protein] PomBase:SPBC119.08	(Fig. 4B)
PMID:19037094	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPBC119.08	(Fig. 4C)
PMID:19037094	FYPO:0004154	normal protein phosphorylation during cellular response to heat [assayed_protein] PomBase:SPBC119.08	(Fig. 4D)
PMID:19037094	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPBC119.08	(Fig. 4E)
PMID:19037094	FYPO:0003214	normal protein phosphorylation during cellular response to glucose starvation [assayed_protein] PomBase:SPBC119.08	(Fig. 4F)
PMID:19037094	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPAC24B11.06c	(Fig. 5)
PMID:19037094	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPAC24B11.06c	(Fig. 5)
PMID:19037094	FYPO:0001529	decreased GTP binding [assayed_protein] PomBase:SPAC1F7.04 [has_severity] high	(Fig. 6A)
PMID:19037094	FYPO:0001529	decreased GTP binding [assayed_protein] PomBase:SPAC1F7.04 [has_severity] high	(Fig. 6A)
PMID:19037094	FYPO:0001885	decreased protein phosphorylation during salt stress [assayed_protein] PomBase:SPBC119.08	(Fig. 6C)
PMID:19037094	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08 [has_severity] high	(Fig. 6D and Fig. 7A)
PMID:19037094	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08	(Fig. 6D)
PMID:19037094	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08	(Fig. 6D)
PMID:19037094	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08	(Fig. 6D)
PMID:19037094	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08	(Fig. 6D)
PMID:19037094	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08	(Fig. 6D)
PMID:19037094	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08	(Fig. 6D)
PMID:19037094	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08	(Fig. 6D)
PMID:19037094	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08	(Fig. 6D)
PMID:19037094	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08	(Fig. 6D)
PMID:19037094	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08	(Fig. 6D)
PMID:19037094	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08	(Fig. 6D)
PMID:19037094	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08	(Fig. 6D)
PMID:19037094	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08	(Fig. 6D)
PMID:19037094	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08 [has_severity] medium	(Fig. 7A)
PMID:19037094	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08 [has_severity] low	(Fig. 7A)
PMID:19037094	FYPO:0001266	normal protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPBC119.08	(Fig. 7B)
PMID:19037094	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPBC119.08	(Fig. 7B)
PMID:19037094	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPBC119.08	(Fig. 7B)
PMID:19037094	FYPO:0004154	normal protein phosphorylation during cellular response to heat [assayed_protein] PomBase:SPBC119.08	(Fig. 7B)
PMID:19037094	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPBC119.08	(Fig. 7C)
PMID:19037094	FYPO:0004154	normal protein phosphorylation during cellular response to heat [assayed_protein] PomBase:SPBC119.08	(Fig. 7C)
PMID:19037094	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPBC119.08	(Fig. 7C)
PMID:19037094	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPBC119.08	(Fig. 7C)
PMID:19037094	FYPO:0003214	normal protein phosphorylation during cellular response to glucose starvation [assayed_protein] PomBase:SPBC119.08	(Fig. 7C)
PMID:19037094	GO:1903139	positive regulation of cell integrity MAPK cascade	Rgf1p, a Rho1p-specific GEF, is a new member of the Pmk1p MAPK pathway in fission yeast.
PMID:19037096	GO:0008574	plus-end-directed microtubule motor activity	(Figure 4, A and B, and Supplemental Movie S1)
PMID:1905818	GO:0003924	GTPase activity	(comment: changed to GTPase from signal transducer)
PMID:1905818	FYPO:0000280	sterile	(comment: haploid, either mating type)
PMID:19075108	FYPO:0006326	decreased protein localization to medial cortical node [has_severity] high [assayed_protein] PomBase:SPAC1F5.04c	(Fig. 1A)
PMID:19075108	FYPO:0006326	decreased protein localization to medial cortical node [assayed_protein] PomBase:SPAC926.03 [has_severity] high	(Fig. 1A)
PMID:19075108	FYPO:0006326	decreased protein localization to medial cortical node [has_severity] high [assayed_protein] PomBase:SPAC20G8.05c	(Fig. 1A)
PMID:19075108	FYPO:0006326	decreased protein localization to medial cortical node [assayed_protein] PomBase:SPAC20G8.05c	(Fig. 1A)
PMID:19075108	FYPO:0008204	delayed orthogonal actomyosin contractile ring assembly from randomly oriented actomyosin filaments	(Fig. 2, Fig. 3)
PMID:19075108	FYPO:0008204	delayed orthogonal actomyosin contractile ring assembly from randomly oriented actomyosin filaments	(Fig. 2, Fig. 3)
PMID:19075108	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_penetrance] 85	(Fig. 2A and C)
PMID:19075108	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_penetrance] 80	(Fig. 2A and C)
PMID:19075108	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_penetrance] 85	(Fig. 2A and C)
PMID:19075108	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_penetrance] 95	(Fig. 2A and C)
PMID:19075108	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_penetrance] 15	(Fig. 2B and C)
PMID:19075108	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_penetrance] 15	(Fig. 2B and C)
PMID:19075108	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_penetrance] 15	(Fig. 2B and C)
PMID:19075108	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_penetrance] 10	(Fig. 2B and C)
PMID:19075108	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_penetrance] 10	(Fig. 2B and C)
PMID:19075108	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_penetrance] 10	(Fig. 2B and C)
PMID:19075108	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_penetrance] 10	(Fig. 2B and C)
PMID:19075108	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_penetrance] 15	(Fig. 2B and C)
PMID:19075108	FYPO:0006005	normal actomyosin contractile ring localization	(Fig. 2B)
PMID:19075108	FYPO:0002027	angled actomyosin contractile ring [has_penetrance] 85	(Fig. 4)
PMID:19075108	FYPO:0002027	angled actomyosin contractile ring [has_penetrance] 60	(Fig. 5A, B and C)
PMID:19075108	FYPO:0007827	normal actomyosin contractile ring organization	(Fig. 5D)
PMID:19075108	FYPO:0007827	normal actomyosin contractile ring organization	(Fig. 5D)
PMID:19075108	GO:1903475	mitotic actomyosin contractile ring assembly [happens_during] mitotic prometaphase	These results furthered the notion that the function of Mid1p and cortical nodes was important for organization of normal actomyosin rings in early mitosis.
PMID:19111658	GO:0003723	RNA binding	(comment: binds centromeric transcripts)
PMID:19117951	FYPO:0002346	abnormal chromatin silencing at centromere outer repeat	(comment: CHECK BACKGROUND? mat1Msmto REIIdelta mat2::ura4)
PMID:19117951	FYPO:0000156	abnormal chromatin silencing at silent mating-type cassette	(comment: gave dark staining with iodine,switch to the opposite state at a low rate)
PMID:19117951	FYPO:0000156	abnormal chromatin silencing at silent mating-type cassette	(comment: gave dark staining with iodine,switch to the opposite state at a low rate)
PMID:19117951	FYPO:0000156	abnormal chromatin silencing at silent mating-type cassette	(comment: mat1Msmto REIIdelta mat2::ura4 gave dark staining with iodine, metastable and switch to the opposite state at a low rate)
PMID:19117951	FYPO:0001234	slow vegetative cell population growth	(comment: mat1Msmto REIIdelta mat2::ura4)
PMID:19117951	FYPO:0002355	decreased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth	(comment: mat1Msmto REIIdelta mat2::ura4)
PMID:19117951	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth	(comment: mat1Msmto REIIdelta mat2::ura4)
PMID:19117951	FYPO:0005102	decreased protein level at silent mating-type cassette [assayed_using] PomBase:SPAC664.01c	(comment: mat1Msmto REIIdelta mat2::ura4)
PMID:19117951	FYPO:0003681	decreased protein level at centromere outer repeat heterochromatin [assayed_using] PomBase:SPAC664.01c	(comment: mat1Msmto REIIdelta mat2::ura4)
PMID:19117951	FYPO:0001886	meiotic cell cycle entry and sporulation in haploid	(comment: mat1Msmto REIIdelta mat2::ura4)
PMID:19136623	FYPO:0003235	normal histone H3-K9 methylation at centromere outer repeat during vegetative growth	Both H3K9me and Swi6 were enriched on centromeric repeats (dg223) in ckb1D cells similar to wild-type or clr3D cells (Fig. 1C).
PMID:19136623	FYPO:0003235	normal histone H3-K9 methylation at centromere outer repeat during vegetative growth	Both H3K9me and Swi6 were enriched on centromeric repeats (dg223) in ckb1D cells similar to wild-type or clr3D cells (Fig. 1C).
PMID:19136623	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPAC664.01c	Conversely, mutations at the five CK2 sites located in the C-terminal region of Swi6 (Fig. 3A) (swi6-S192-274A) did not influence the mobility of Swi6 (Fig. 3B).
PMID:19136623	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] low	H3K9me on the ura4 inserted at the mating locus heterochromatin (Kint2 ::ura4) was hardly affected by deletion of either atf1 or dcr1, an essential component of the RNAi-directed pathway (Fig. 1D).
PMID:19136623	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] low	H3K9me on the ura4 inserted at the mating locus heterochromatin (Kint2 ::ura4) was hardly affected by deletion of either atf1 or dcr1, an essential component of the RNAi-directed pathway (Fig. 1D).
PMID:19136623	FYPO:0008200	decreased histone H3-K9 methylation at centromere inner repeat during vegetative growth	In contrast, levels of H3K9me and Swi6 at imr::ura4 were significantly decreased in clr3D and ckb1D cells (Fig. 1C).
PMID:19136623	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC800.03	In wild-type cells, both Clr3 and Mit1 were enriched on centromeric repeats; this localization was decreased in swi6D or chp2D cells, though substantial Mit1 was retained in swi6D cells, as reported previously (Sadaie et al. 2008).
PMID:19136623	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBP35G2.10	In wild-type cells, both Clr3 and Mit1 were enriched on centromeric repeats; this localization was decreased in swi6D or chp2D cells, though substantial Mit1 was retained in swi6D cells, as reported previously (Sadaie et al. 2008).
PMID:19136623	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC800.03	In wild-type cells, both Clr3 and Mit1 were enriched on centromeric repeats; this localization was decreased in swi6D or chp2D cells, though substantial Mit1 was retained in swi6D cells, as reported previously (Sadaie et al. 2008).
PMID:19136623	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBP35G2.10	In wild-type cells, both Clr3 and Mit1 were enriched on centromeric repeats; this localization was decreased in swi6D or chp2D cells, though substantial Mit1 was retained in swi6D cells, as reported previously (Sadaie et al. 2008).
PMID:19136623	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC800.03	In wild-type cells, both Clr3 and Mit1 were enriched on centromeric repeats; this localization was decreased in swi6D or chp2D cells, though substantial Mit1 was retained in swi6D cells, as reported previously (Sadaie et al. 2008).
PMID:19136623	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBP35G2.10 [has_severity] low	In wild-type cells, both Clr3 and Mit1 were enriched on centromeric repeats; this localization was decreased in swi6D or chp2D cells, though substantial Mit1 was retained in swi6D cells, as reported previously (Sadaie et al. 2008).
PMID:19136623	MOD:00046	O-phospho-L-serine	Mass spectrometric analysis of Swi6 prepared from wild-type and ckb1D cells showed that five potential CK2 phosphorylation sites (S18, S24, S46, S52, and S117) in the N-terminal half are really phosphorylated in vivo, and the phosphorylation of four of them (S18, S24, S46, and S117) decreased in ckb1D cells (Supplemental Fig. S5).
PMID:19136623	MOD:00046	O-phospho-L-serine	Mass spectrometric analysis of Swi6 prepared from wild-type and ckb1D cells showed that five potential CK2 phosphorylation sites (S18, S24, S46, S52, and S117) in the N-terminal half are really phosphorylated in vivo, and the phosphorylation of four of them (S18, S24, S46, and S117) decreased in ckb1D cells (Supplemental Fig. S5).
PMID:19136623	MOD:00046	O-phospho-L-serine	Mass spectrometric analysis of Swi6 prepared from wild-type and ckb1D cells showed that five potential CK2 phosphorylation sites (S18, S24, S46, S52, and S117) in the N-terminal half are really phosphorylated in vivo, and the phosphorylation of four of them (S18, S24, S46, and S117) decreased in ckb1D cells (Supplemental Fig. S5).
PMID:19136623	MOD:00046	O-phospho-L-serine	Mass spectrometric analysis of Swi6 prepared from wild-type and ckb1D cells showed that five potential CK2 phosphorylation sites (S18, S24, S46, S52, and S117) in the N-terminal half are really phosphorylated in vivo, and the phosphorylation of four of them (S18, S24, S46, and S117) decreased in ckb1D cells (Supplemental Fig. S5).
PMID:19136623	MOD:00046	O-phospho-L-serine	Mass spectrometric analysis of Swi6 prepared from wild-type and ckb1D cells showed that five potential CK2 phosphorylation sites (S18, S24, S46, S52, and S117) in the N-terminal half are really phosphorylated in vivo, and the phosphorylation of four of them (S18, S24, S46, and S117) decreased in ckb1D cells (Supplemental Fig. S5).
PMID:19136623	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPAC664.01c [has_severity] high	Mutations at the five CK2 sites located in the N-terminal half (S18-117A in Fig. 3A) resulted in an increase in mobility
PMID:19136623	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC664.01c	Similarly, CK2 efficiently phosphorylated bacteria-prepared Swi6 in a Ckb1-dependent manner, resulting in slower migrating bands in SDS- PAGE (Fig. 2C).
PMID:19136623	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBP35G2.10	Similarly, Clr3 and Mit1 localization was decreased in ckb1D and swi6-S18-117A mutants, although this decrease was less in swi6-S18-117A than in ckb1D cells.
PMID:19136623	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC800.03	Similarly, Clr3 and Mit1 localization was decreased in ckb1D and swi6-S18-117A mutants, although this decrease was less in swi6-S18-117A than in ckb1D cells.
PMID:19136623	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC800.03	Similarly, Clr3 and Mit1 localization was decreased in ckb1D and swi6-S18-117A mutants, although this decrease was less in swi6-S18-117A than in ckb1D cells.
PMID:19136623	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBP35G2.10	Similarly, Clr3 and Mit1 localization was decreased in ckb1D and swi6-S18-117A mutants, although this decrease was less in swi6-S18-117A than in ckb1D cells.
PMID:19136623	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] low	Similarly, H3K9me on Kint2::ura4 was diminished in dcr1Dckb1D but still retained in atf1Dckb1D cells (Fig. 1D). T
PMID:19136623	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [has_severity] high	Similarly, H3K9me on Kint2::ura4 was diminished in dcr1Dckb1D but still retained in atf1Dckb1D cells (Fig. 1D). T
PMID:19136623	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	The extent of the silencing defects in ckb1D cells was comparable with that caused by disruption of other heterochromatic genes, including clr4, a histone H3K9-specific histone methyltransferase; clr3, a histone deacetylase and a subunit of SHREC; and swi6, a HP1 homolog (Fig. 1B).
PMID:19136623	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	The extent of the silencing defects in ckb1D cells was comparable with that caused by disruption of other heterochromatic genes, including clr4, a histone H3K9-specific histone methyltransferase; clr3, a histone deacetylase and a subunit of SHREC; and swi6, a HP1 homolog (Fig. 1B).
PMID:19136623	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	The extent of the silencing defects in ckb1D cells was comparable with that caused by disruption of other heterochromatic genes, including clr4, a histone H3K9-specific histone methyltransferase; clr3, a histone deacetylase and a subunit of SHREC; and swi6, a HP1 homolog (Fig. 1B).
PMID:19136623	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPAC664.01c [has_severity] low	The lesser mobility change in ckb1D cells than that of Swi6-S18-117A would reflect the partial phosphorylation of Swi6 by residual activity of CK2 in ckb1D cells (Fig. 2A,C).
PMID:19136623	GO:0090055	positive regulation of silent mating-type cassette heterochromatin formation	Therefore, Clr3 and Ckb1 function similarly in Atf1/Pcr1-dependent heterochromatin formation at the mating locus.
PMID:19136623	GO:0030466	silent mating-type cassette heterochromatin formation	Therefore, Clr3 and Ckb1 function similarly in Atf1/Pcr1-dependent heterochromatin formation at the mating locus.
PMID:19136623	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	disruption of ckb1 alleviated the silencing of marker genes inserted in centromeric heterochromatin (Fig. 1A,B).
PMID:19136623	FYPO:0002834	decreased chromatin silencing at centromere [has_penetrance] high	swi6-S192-274A mutations did not affect silencing at the centromere (imr::ura4), while swi6-S18-24A and S18- 117A mutants displayed decreases in silencing (Fig. 3C).
PMID:19136623	FYPO:0002834	decreased chromatin silencing at centromere [has_penetrance] high	swi6-S192-274A mutations did not affect silencing at the centromere (imr::ura4), while swi6-S18-24A and S18- 117A mutants displayed decreases in silencing (Fig. 3C).
PMID:19136623	FYPO:0002360	normal chromatin silencing at centromere	swi6-S192-274A mutations did not affect silencing at the centromere (imr::ura4), while swi6-S18-24A and S18- 117A mutants displayed decreases in silencing (Fig. 3C).
PMID:19136623	GO:0090053	positive regulation of pericentric heterochromatin formation	this result suggests that Ckb1 is involved in the spreading of heterochromatin. (in ~GO, spreading is included in formation)
PMID:19136623	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPAC664.01c [has_severity] low	whereas mutant Swi6 harboring S18A and S24A showed a slight mobility change
PMID:19139265	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC83.18c	(Fig. 8)
PMID:19139265	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC4F6.12	(Fig. 9)
PMID:19139265	FYPO:0002061	inviable vegetative cell population	(Fig. S5)
PMID:19139265	FYPO:0002061	inviable vegetative cell population	(Fig. S5)
PMID:19150433	FYPO:0000657	increased DNA binding [assayed_using] PomBase:SPBC1A4.03c	(comment: covalent binding between topoisomerase and DNA)
PMID:19150433	FYPO:0000657	increased DNA binding [assayed_using] PomBase:SPBC1A4.03c	(comment: covalent binding between topoisomerase and DNA)
PMID:19150433	FYPO:0005919	sensitive to TOP-53 [has_severity] high	(comment: covalent binding between topoisomerase and DNA)
PMID:19150433	FYPO:0000657	increased DNA binding [assayed_using] PomBase:SPBC1703.14c	(comment: covalent binding between topoisomerase and DNA)
PMID:19150433	FYPO:0000657	increased DNA binding [assayed_using] PomBase:SPBC1A4.03c	(comment: covalent binding between topoisomerase and DNA)
PMID:19150433	FYPO:0000657	increased DNA binding [assayed_using] PomBase:SPBC1703.14c	(comment: covalent binding between topoisomerase and DNA)
PMID:19150433	FYPO:0000658	decreased DNA binding [assayed_using] PomBase:SPBC1703.14c	(comment: covalent binding between topoisomerase and DNA)
PMID:19155267	GO:0008721	D-serine ammonia-lyase activity	Table S1, Supplementary Data
PMID:19155267	GO:0030378	serine racemase activity	Table S1, Supplementary Data
PMID:19155267	GO:0003941	L-serine ammonia-lyase activity	Table S1, Supplementary Data
PMID:19158664	GO:0000785	chromatin [coincident_with] origin_of_replication [exists_during] replication fork processing	"(comment: closest we can get to ""at stalled fork"" with available terms)"
PMID:19164572	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_region] dg_repeat [assayed_region] dh_repeat [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 1B)
PMID:19164572	FYPO:0000875	increased histone H3-K9 dimethylation at centromere inner repeat during vegetative growth [has_severity] high	(Fig. 1C)
PMID:19164572	FYPO:0000884	decreased histone H3-K9 trimethylation at centromere inner repeat during vegetative growth [has_severity] high	(Fig. 1D)
PMID:19164572	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_region] dg_repeat [assayed_region] dh_repeat [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 1E)
PMID:19164572	FYPO:0000863	normal histone H3-K9 dimethylation at centromere inner repeat during vegetative growth	(Fig. 1F)
PMID:19164572	FYPO:0008203	normal histone H3-K9 trimethylation at centromere inner repeat during vegetative growth	(Fig. 1G)
PMID:19164572	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC664.01c	(Fig. 1H)
PMID:19164572	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Fig. 2A)
PMID:19164572	FYPO:0006299	increased chromatin silencing at centromere outer repeat	(Fig. 2A)
PMID:19164572	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Fig. 2A)
PMID:19164572	FYPO:0000887	increased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 2B)
PMID:19164572	FYPO:0004237	increased protein localization to heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPAC664.01c	(Fig. 2C)
PMID:19164572	FYPO:0000470	decreased mating type switching [has_penetrance] 1.5	(Fig. 3)
PMID:19164572	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 4B)
PMID:19164572	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 4B)
PMID:19164572	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	(Fig. 4B)
PMID:19164572	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 4B)
PMID:19164572	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(Fig. 4D)
PMID:19164572	FYPO:0000472	normal mating type switching	(Fig. 4E)
PMID:19164572	FYPO:0000472	normal mating type switching	(Fig. 4E)
PMID:19164572	FYPO:0000472	normal mating type switching	(Fig. 5)
PMID:19164572	FYPO:0000472	normal mating type switching	(Fig. 5)
PMID:19164572	FYPO:0000472	normal mating type switching	(Fig. 5)
PMID:19164572	FYPO:0008154	normal protein localization to centromeric heterochromatin [assayed_protein] PomBase:SPBC11B10.10c	(Fig. S2)
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC18G6.02c	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC736.11	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC23H4.12	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC428.08c	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC664.01c	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC6F12.09	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC188.13c	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1739.03	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC663.12	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC83.03c	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC800.03	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC36.05c	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBP35G2.10	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC2D10.17	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1B3.17	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC16D10.07c	Table S1
PMID:19164572	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC622.16c	Table S1
PMID:19189958	FYPO:0001357	normal vegetative cell population growth	(Figure 1)
PMID:19189958	FYPO:0002104	viable vegetative cell with normal cell shape	(Figure 1)
PMID:19189958	FYPO:0002060	viable vegetative cell population	(Figure 1) Rgf2p, a Rho1-GEF Required for Sporulation in S. pombe 1329 6A (top) shows that rgf2 expressed from plasmids, containing the rgf21 genomic promoter (pGR13) or the strongest nmt1 promoter (pGR70), fully rescued the lysis and the Csp hypersensitivity of rgf1D cells in medium containing thiamine.
PMID:19189958	FYPO:0000590	normal sporulation	(Figure 2)
PMID:19189958	FYPO:0000121	abnormal sporulation	(Figure 2)
PMID:19189958	FYPO:0000478	normal meiosis	(Figure 2A)
PMID:19189958	FYPO:0000175	abnormal ascospore wall assembly [has_penetrance] high	(Figure 2A)
PMID:19189958	FYPO:0000175	abnormal ascospore wall assembly [has_penetrance] high	(Figure 2A)
PMID:19189958	FYPO:0000175	abnormal ascospore wall assembly [has_penetrance] high	(Figure 2A)
PMID:19189958	FYPO:0004927	normal prospore membrane formation	(Figure 2A)
PMID:19189958	FYPO:0000280	sterile [has_penetrance] 99	(Figure 2b)
PMID:19189958	GO:0140748	positive regulation of regulation of ascospore wall (1->3)-beta-D-glucan biosynthetic process	"(Figure 3) ""This result indicates that Rgf2p is involved in b-glucan biosynthesis during sporulation."" figure4c These results clearly indicate that Rgf2p is involved in the regulation of b(1,3)-glucan biosynthesis."
PMID:19189958	FYPO:0007905	abnormal beta-glucan synthesis	(Figure 3A)
PMID:19189958	GO:0005632	inner layer of spore wall	(Figure 3B)
PMID:19189958	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPAC1F7.04 [part_of] regulation of ascospore wall (1->3)-beta-D-glucan biosynthetic process [occurs_in] inner layer of spore wall	(Figure 4c) (comment: positive affect)
PMID:19189958	FYPO:0002061	inviable vegetative cell population	(Figure 5B) As expected for the rgf31 shut-off, the cells died in the presence of thiamine (promoter off).
PMID:19189958	FYPO:0002061	inviable vegetative cell population	(Figure 5B) As expected for the rgf31 shut-off, the cells died in the presence of thiamine (promoter off).
PMID:19189958	FYPO:0002060	viable vegetative cell population	(Figure 5B) However, their growth was rescued in the presence of sorbitol
PMID:19189958	FYPO:0002060	viable vegetative cell population	(Figure 5B) However, their growth was rescued in the presence of sorbitol
PMID:19189958	FYPO:0002060	viable vegetative cell population	(Figure 5B) viable and phenotypically indistinguishable from the ehs2-1 mutant
PMID:19189958	FYPO:0003535	decreased bipolar index [has_severity] high	(comment: CHECK 10% of cells)
PMID:19189958	FYPO:0003535	decreased bipolar index [has_severity] low	(comment: CHECKB 47% of cells)
PMID:19189958	FYPO:0001310	normal viability in stationary phase	90% viability ? We also examined cell viability of stationary phase rgf2D and rgf21 cultures incubated for 4 days at 28°; both strains were found to be .90% viable during this period.
PMID:19189958	FYPO:0002177	viable vegetative cell with normal cell morphology	As expected, over-expression of the rgf2-PTTRD mutant in a pREP3X vector produced viable cells and no multiseptated phenotype was seen, even at very long times of derepresion in the absence of thiamine (Figure 4A).
PMID:19189958	FYPO:0001968	increased 1,3-beta-D-glucan synthase activity [has_severity] medium	GS activity was threefold higher than that observed in the wild-type strain (Figure 4C)
PMID:19189958	FYPO:0001968	increased 1,3-beta-D-glucan synthase activity [has_severity] high	GS activity was threefold higher than that observed in the wild-type strain (Figure 4C)
PMID:19189958	FYPO:0002061	inviable vegetative cell population	None of the 11 spores predicted to be rgf1This31 rgf2Tura1 was viable, strongly supporting the idea that simultaneous disruption of rgf11 and rgf21 is lethal. To eliminate the possibility that these mutations might be affecting only sporulation or germination, we also tested for synthetic lethality during vegetative growth
PMID:19189958	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPAC1F7.04 [part_of] regulation of cell wall (1->3)-beta-D-glucan biosynthetic process [happens_during] mitotic interphase	Our results indicate that Rgf1p and Rgf2p share an essential role as Rho1p activators, and they suggest that in the absence of Rgf1p, Rgf2p takes over the essential functions for Rho1p during vegetative growth.
PMID:19189958	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPAC1F7.04 [part_of] regulation of cell wall (1->3)-beta-D-glucan biosynthetic process [happens_during] mitotic interphase	Our results indicate that Rgf1p and Rgf2p share an essential role as Rho1p activators, and they suggest that in the absence of Rgf1p, Rgf2p takes over the essential functions for Rho1p during vegetative growth.
PMID:19189958	FYPO:0001357	normal vegetative cell population growth	We also examined cell viability of stationary phase rgf2D and rgf21 cultures incubated for 4 days at 28°; both strains were found to be .90% viable during this period.
PMID:19189958	FYPO:0007436	swollen elongated multiseptate vegetative cell	cells were larger than wild-type cells and displayed multiple abnormal septa.
PMID:19189958	FYPO:0007911	increased level of GTP-bound protein [assayed_protein] PomBase:SPAC1F7.04	the amount of active Rho1p increased considerably in the strain overexpressing Rgf2p as compared with the wild-type strain (Figure 4B
PMID:19202278	FYPO:0002447	abnormal protein N-linked glycosylation during vegetative growth	(comment: absent beta 1,3 gal)
PMID:19202289	FYPO:0003563	normal meiosis I	(Fig. 1A)
PMID:19202289	FYPO:0000121	abnormal sporulation	(Fig. 1A)
PMID:19202289	FYPO:0003563	normal meiosis I	(Fig. 1B)
PMID:19202289	FYPO:0003798	normal meiosis II	(Fig. 1B)
PMID:19202289	FYPO:0002061	inviable vegetative cell population	(Fig. 1B)
PMID:19202289	FYPO:0000307	inviable small spore	(Fig. 2B)
PMID:19202289	GO:0032120	ascospore-type prospore membrane formation	(Fig. 2B)
PMID:19202289	GO:0005628	prospore membrane	(Fig. 2D)
PMID:19202289	GO:0005886	plasma membrane	(Fig. 2D)
PMID:19202289	FYPO:0000590	normal sporulation	(Fig. 3A and B)
PMID:19202289	FYPO:0000590	normal sporulation	(Fig. 3A and B)
PMID:19202289	GO:0032120	ascospore-type prospore membrane formation	(Fig. 3B)
PMID:19202289	GO:0032120	ascospore-type prospore membrane formation	(Fig. 3B)
PMID:19202289	FYPO:0002060	viable vegetative cell population	(Fig. 3C)
PMID:19202289	FYPO:0002060	viable vegetative cell population	(Fig. 3C)
PMID:19202289	FYPO:0003905	normal meiotic spindle pole body morphology during meiosis II	(comment: data not shown)
PMID:19205745	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: temp semi-permissive for cdc20-M10 alone
PMID:19205745	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(comment: temp semi-permissive for cdc6-23 alone
PMID:19205745	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(comment: temp semi-permissive for cdc6-23 alone)
PMID:19205745	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: temp semi-permissive for cdc6-23 alone)
PMID:19205745	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: temp semi-permissive for cdc6-23 alone)
PMID:19205745	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: temp semi-permissive for pol1-1 alone)
PMID:19214192	GO:0140445	chromosome, telomeric repeat region [exists_during] mitotic S phase	(comment: DNA polymerases present in late S; epsilon (cdc20) earlier than alpha (pol1) or delta (cdc6))
PMID:19214192	GO:0140445	chromosome, telomeric repeat region [exists_during] mitotic S phase	(comment: DNA polymerases present in late S; epsilon (cdc20) earlier than alpha (pol1) or delta (cdc6))
PMID:19214192	GO:0140445	chromosome, telomeric repeat region [exists_during] mitotic S phase	(comment: DNA polymerases present in late S; epsilon (cdc20) earlier than alpha (pol1) or delta (cdc6))
PMID:19214192	GO:0140445	chromosome, telomeric repeat region	(comment: present at roughly constant level throughout cell cycle)
PMID:19214192	GO:0140445	chromosome, telomeric repeat region [exists_during] mitotic S phase	(comment: present in late S)
PMID:19214192	GO:0140445	chromosome, telomeric repeat region [exists_during] mitotic S phase	(comment: present in late S)
PMID:19214192	GO:0140445	chromosome, telomeric repeat region [exists_during] mitotic S phase	(comment: present in late S)
PMID:19214192	GO:0140445	chromosome, telomeric repeat region [exists_during] mitotic S phase	(comment: present in late S, as late as pols alpha & delta)
PMID:19214192	GO:0140445	chromosome, telomeric repeat region	(comment: present throughout cell cycle but at higher level in S phase)
PMID:19214192	GO:0140445	chromosome, telomeric repeat region	(comment: present throughout cell cycle but at higher level in S phase)
PMID:19214192	GO:0140445	chromosome, telomeric repeat region	(comment: present throughout cell cycle but at higher level in late S phase)
PMID:19214192	GO:0140445	chromosome, telomeric repeat region	(comment: present throughout cell cycle but at lower level in S phase)
PMID:19217404	GO:0000785	chromatin	(Fig. 4, Fig. S8)
PMID:19217404	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAPB1A10.02 [assayed_using] PomBase:SPBC1105.17	(Fig. S10)
PMID:19217404	FYPO:0003740	decreased CENP-A containing chromatin assembly	(comment: CHECK abolished,) fig1d
PMID:19217404	FYPO:0003740	decreased CENP-A containing chromatin assembly	(comment: CHECK abolished,) fig1d
PMID:19217404	FYPO:0003740	decreased CENP-A containing chromatin assembly	(comment: CHECK abolished,) fig1d
PMID:19217404	FYPO:0003740	decreased CENP-A containing chromatin assembly	(comment: CHECK abolished,) fig1d
PMID:19217404	FYPO:0003740	decreased CENP-A containing chromatin assembly	(comment: CHECK abolished,) fig1d
PMID:19217404	FYPO:0003740	decreased CENP-A containing chromatin assembly	(comment: abolished CHECK,) fig1d
PMID:19250904	GO:0140005	histone H4K20me2 reader activity	(comment: assayed using purified HeLa histone octamers)
PMID:19250904	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] high	(comment: same as either single mutant)
PMID:19250904	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: same as either single mutant)
PMID:19250904	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] high	(comment: same as either single mutant)
PMID:19250904	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: same as either single mutant)
PMID:19250904	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] high	(comment: same as either single mutant)
PMID:19250904	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: same as either single mutant)
PMID:19250904	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: same as either single mutant)
PMID:19250904	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] high	(comment: same as either single mutant)
PMID:19250904	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(comment: same as either single mutant)
PMID:19250904	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] medium	(comment: same as either single mutant)
PMID:19279143	GO:0003729	mRNA binding [has_input] PomBase:SPAP8A3.08	"""Thus, Nrd1 directly binds with Cdc4 mRNA in vivo and in vitro"""
PMID:19279143	FYPO:0002138	increased RNA catabolic process during vegetative growth [assayed_using] PomBase:SPAP8A3.08	(Fig. 4F)
PMID:19279143	FYPO:0002137	decreased RNA catabolic process during vegetative growth [assayed_using] PomBase:SPAP8A3.08	(Fig. 4F)
PMID:19279143	GO:1902413	negative regulation of mitotic cytokinesis	Notably, Pmk1, the mitogen-activated protein kinase (MAPK), which regulates cell integrity (Toda et al., 1996; Sugiura et al., 1999; Sugiura et al., 2003), directly phosphorylates Nrd1, thereby negatively regulating the activity of Nrd1 to bind to and stabilize Cdc4 mRNA. We propose that the MAPK-dependent phosphorylation of the RNA-binding protein Nrd1 may serve as a novel mechanism for the regulation of myosin mRNA and cytokinesis in fission yeast.
PMID:19328067	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_using] PomBase:SPBC28F2.12	(comment: All at eng2 CDS)
PMID:19328067	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPCC330.10	(comment: All at eng2 CDS)
PMID:19328067	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_using] PomBase:SPCC330.10	(comment: All at eng2 CDS)
PMID:19328067	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_using] PomBase:SPBC32H8.10	(comment: All at eng2 CDS)
PMID:19328067	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_using] PomBase:SPBC28F2.12	(comment: All at eng2 CDS)
PMID:19328067	GO:0140834	RNA polymerase II CTD heptapeptide repeat S2 kinase activity [has_input] PomBase:SPBC28F2.12 [part_of] positive regulation of 7-methylguanosine mRNA capping	(comment: CHECK positive regulation)
PMID:19328067	FYPO:0003836	decreased RNA polymerase II carboxy-terminal domain kinase activity [assayed_using] PomBase:SPBC32H8.10	"(comment: Mcs6 ""primes"" Rpb1 for phosphorylation by cdk9)"
PMID:19330768	FYPO:0000141	abnormal mitotic sister chromatid segregation	(comment: G1 temperature shift)
PMID:19330768	FYPO:0004588	abnormal mitosis following normal mitosis	(comment: G2 temperature shift)
PMID:19330768	FYPO:0000802	abnormal cytoskeleton organization	(comment: in arrested cells, indicating independent of cell cycle progression)
PMID:1934126	FYPO:0000681	abnormal sporulation resulting in formation of two-spore ascus	(comment: same as cdc25-22 single mutant)
PMID:1934126	FYPO:0000681	abnormal sporulation resulting in formation of two-spore ascus	(comment: same as cdc25-22 single mutant)
PMID:1934126	FYPO:0000681	abnormal sporulation resulting in formation of two-spore ascus	(comment: same as cdc25-22 single mutant)
PMID:1934126	FYPO:0000681	abnormal sporulation resulting in formation of two-spore ascus	(comment: same as cdc25-22 single mutant)
PMID:19357077	GO:0004674	protein serine/threonine kinase activity [has_input] cds1/Phos(T11) dimer [happens_during] DNA damage response	Activation of Cds1 requires the recruitment by Mrc1 and subsequent phosphorylation of threonine 11 by Rad3. Phosphorylation of threonine 11 promotes homodimerization of Cds1, which facilitates the autophosphorylation of threonine 328 in the kinase domains of the dimer partners. Phosphorylation of threonine 328 directly activates Cds1. The kinase activity of Cds1 is low during a normal cell cycle. However, it increases dramatically during a perturbed S phase.
PMID:19362535	FYPO:0003099	normal heterochromatin assembly	(comment: CHAECK ******abolished /de novo**********) Reintegration of clr4+ into cells bearing the chp1 chromodomain mutants showed a striking separation of phenotypes, with some mutants unable to re-establish centromeric heterochromatin (e.g., E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+) and others showing efficient re-establishment (e.g., F61Achp1clr4D to clr4+), as assessed by silencing of the cen::ura4+ transgene (Figure 5A).
PMID:19362535	FYPO:0003099	normal heterochromatin assembly	(comment: CHAECK ******abolished /de novo**********) Reintegration of clr4+ into cells bearing the chp1 chromodomain mutants showed a striking separation of phenotypes, with some mutants unable to re-establish centromeric heterochromatin (e.g., E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+) and others showing efficient re-establishment (e.g., F61Achp1clr4D to clr4+), as assessed by silencing of the cen::ura4+ transgene (Figure 5A).
PMID:19362535	FYPO:0003044	abnormal heterochromatin assembly [assayed_region] regional_centromere_outer_repeat_region	(comment: CHECK ******abolished /de novo**********) Reintegration of clr4+ into cells bearing the chp1 chromodomain mutants showed a striking separation of phenotypes, with some mutants unable to re-establish centromeric heterochromatin (e.g., E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+) and others showing efficient re-establishment (e.g., F61Achp1clr4D to clr4+), as assessed by silencing of the cen::ura4+ transgene (Figure 5A).
PMID:19362535	FYPO:0003044	abnormal heterochromatin assembly [assayed_region] regional_centromere_outer_repeat_region	(comment: CHECK ******abolished /de novo**********) Reintegration of clr4+ into cells bearing the chp1 chromodomain mutants showed a striking separation of phenotypes, with some mutants unable to re-establish centromeric heterochromatin (e.g., E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+) and others showing efficient re-establishment (e.g., F61Achp1clr4D to clr4+), as assessed by silencing of the cen::ura4+ transgene (Figure 5A).
PMID:19362535	FYPO:0003044	abnormal heterochromatin assembly [assayed_region] regional_centromere_outer_repeat_region	(comment: CHECK ******abolished /de novo**********) Reintegration of clr4+ into cells bearing the chp1 chromodomain mutants showed a striking separation of phenotypes, with some mutants unable to re-establish centromeric heterochromatin (e.g., E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+) and others showing efficient re-establishment (e.g., F61Achp1clr4D to clr4+), as assessed by silencing of the cen::ura4+ transgene (Figure 5A).
PMID:19362535	FYPO:0008195	decreased histone H3-K9Me binding [has_severity] medium	A second class of mutants showed a 5- to 17-fold reduction in binding affinity for H3K9me2 compared with the wild-type Chp1 chromodomain (V21A, E23V, N59A, and V24M). A
PMID:19362535	FYPO:0008195	decreased histone H3-K9Me binding [has_severity] medium	A second class of mutants showed a 5- to 17-fold reduction in binding affinity for H3K9me2 compared with the wild-type Chp1 chromodomain (V21A, E23V, N59A, and V24M). A
PMID:19362535	FYPO:0008195	decreased histone H3-K9Me binding [has_severity] medium	A second class of mutants showed a 5- to 17-fold reduction in binding affinity for H3K9me2 compared with the wild-type Chp1 chromodomain (V21A, E23V, N59A, and V24M). A
PMID:19362535	FYPO:0008195	decreased histone H3-K9Me binding [has_severity] medium	A second class of mutants showed a 5- to 17-fold reduction in binding affinity for H3K9me2 compared with the wild-type Chp1 chromodomain (V21A, E23V, N59A, and V24M). A
PMID:19362535	FYPO:0008195	decreased histone H3-K9Me binding [has_severity] high	A third class showed a more profound reduction in binding affinity: the E23V,V24M mutant reduced binding affinity 40 fold
PMID:19362535	FYPO:0000862	normal histone H3-K9 dimethylation at centromere during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	High copy expression of clr4+ in the E23Vchp1clr4D and in the V24Mchp1clr4D cells allowed efficient establishment of centromeric heterochromatin (Figure 6C). Thus, the establishment defect of chp1 mutants with reduced H3K9me-binding affinity can be compensated by an increased dosage of clr4+ .
PMID:19362535	FYPO:0000862	normal histone H3-K9 dimethylation at centromere during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	High copy expression of clr4+ in the E23Vchp1clr4D and in the V24Mchp1clr4D cells allowed efficient establishment of centromeric heterochromatin (Figure 6C). Thus, the establishment defect of chp1 mutants with reduced H3K9me-binding affinity can be compensated by an increased dosage of clr4+ .
PMID:19362535	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	High levels of centromeric transcripts also accumulated in these establishment-defective clr4+ reintroduction strains E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+, but not in the establishment-competent F61Achp1clr4D to clr4+ cells (Figure 5B; Figure S9A)
PMID:19362535	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	High levels of centromeric transcripts also accumulated in these establishment-defective clr4+ reintroduction strains E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+, but not in the establishment-competent F61Achp1clr4D to clr4+ cells (Figure 5B; Figure S9A)
PMID:19362535	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	High levels of centromeric transcripts also accumulated in these establishment-defective clr4+ reintroduction strains E23Vchp1clr4D to clr4+, V24Mchp1clr4D to clr4+, and N59Achp1clr4D to clr4+, but not in the establishment-competent F61Achp1clr4D to clr4+ cells (Figure 5B; Figure S9A)
PMID:19362535	FYPO:0004742	normal chromatin silencing at centromere outer repeat	In contrast, the F61Achp1; F276Aago1 mutant strain showed no defect in the silencing of the reporter (Figure 4D).
PMID:19362535	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	Interestingly, cells expressing most of the mutant alleles of chp1 showed no defect in heterochromatin assembly as measured in this assay (Figure 3A), with the exception of the double mutant E23V V24M and the V24R chp1 mutant, which did show silencing defects.
PMID:19362535	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	Interestingly, cells expressing most of the mutant alleles of chp1 showed no defect in heterochromatin assembly as measured in this assay (Figure 3A), with the exception of the double mutant E23V V24M and the V24R chp1 mutant, which did show silencing defects.
PMID:19362535	FYPO:0004742	normal chromatin silencing at centromere outer repeat	Interestingly, cells expressing most of the mutant alleles of chp1 showed no defect in heterochromatin assembly as measured in this assay (Figure 3A), with the exception of the double mutant E23V V24M and the V24R chp1 mutant, which did show silencing defects.
PMID:19362535	FYPO:0004742	normal chromatin silencing at centromere outer repeat	Interestingly, cells expressing most of the mutant alleles of chp1 showed no defect in heterochromatin assembly as measured in this assay (Figure 3A), with the exception of the double mutant E23V V24M and the V24R chp1 mutant, which did show silencing defects.
PMID:19362535	FYPO:0004982	increased centromeric transcript level	Interestingly, cells expressing most of the mutant alleles of chp1 showed no defect in heterochromatin assembly as measured in this assay (Figure 3A), with the exception of the double mutant E23V V24M and the V24R chp1 mutant, which did show silencing defects.
PMID:19362535	FYPO:0008196	increased histone H3-K9Me binding [has_severity] high	Introduction of an E80V mutation, corresponding to V21 of Chp1, into Swi6V82E further increased Swi6’s affinity by 2-fold (Table 1; Figure S2A).
PMID:19362535	FYPO:0005306	abnormal protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	Results for Chp1 localization were similar to those seen in maintenance strains with mutants such as E23Vchp1clr4D to clr4+ and V24Mchp1clr4D to clr4+ showing little association with centromeres, whereas F61Achp1clr4D to clr4+ was enriched at levels close to wild-type Chp1clr4D to clr4+
PMID:19362535	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c [has_severity] high	Results for Chp1 localization were similar to those seen in maintenance strains with mutants such as E23Vchp1clr4D to clr4+ and V24Mchp1clr4D to clr4+ showing little association with centromeres, whereas F61Achp1clr4D to clr4+ was enriched at levels close to wild-type Chp1clr4D to clr4+
PMID:19362535	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c [has_severity] high	Results for Chp1 localization were similar to those seen in maintenance strains with mutants such as E23Vchp1clr4D to clr4+ and V24Mchp1clr4D to clr4+ showing little association with centromeres, whereas F61Achp1clr4D to clr4+ was enriched at levels close to wild-type Chp1clr4D to clr4+
PMID:19362535	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c [has_severity] high	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c [has_severity] medium	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c [has_severity] medium	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c [has_severity] high	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c [has_severity] high	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c [has_severity] high	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c [has_severity] high	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	GO:0000779	condensed chromosome, centromeric region [coincident_with] regional_centromere_outer_repeat_region	Surprisingly, in contrast to robust association of wild-type Chp1 at the centromeric outer repeat sites, we found only very low levels of many of the mutant Chp1 proteins at centromeres under our standard ChIP conditions (Figure 4A and Figure S5A)
PMID:19362535	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	Surprisingly, when we monitored the presence of centromeric siRNAs in these clr4+ reintroduction strains, we found that even mutants that were defective for establishment of centromeric heterochromatin efficiently synthesized siRNAs derived from both the dg and dh centromeric repeats (Figure 5C)
PMID:19362535	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	Surprisingly, when we monitored the presence of centromeric siRNAs in these clr4+ reintroduction strains, we found that even mutants that were defective for establishment of centromeric heterochromatin efficiently synthesized siRNAs derived from both the dg and dh centromeric repeats (Figure 5C)
PMID:19362535	FYPO:0008196	increased histone H3-K9Me binding [has_severity] medium	The Swi6 V82E mutant bound H3K9me2 with 5-fold higher affinity than wild-type Swi6 (Table 1; Figure S2A)
PMID:19362535	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 11	The efficiency of chromosome segregation was also monitored in clr4+ reintroduction chp1 mutant cells (Table S4) and closely correlated with Chp1’s binding efficiency. Mutants with >5-fold reduction in H3K9me-binding efficiency that cannot establish centromeric heterochromatin exhibited elevated rates of chromosome missegregation.
PMID:19362535	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 5.5	The efficiency of chromosome segregation was also monitored in clr4+ reintroduction chp1 mutant cells (Table S4) and closely correlated with Chp1’s binding efficiency. Mutants with >5-fold reduction in H3K9me-binding efficiency that cannot establish centromeric heterochromatin exhibited elevated rates of chromosome missegregation.
PMID:19362535	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 15.3	The efficiency of chromosome segregation was also monitored in clr4+ reintroduction chp1 mutant cells (Table S4) and closely correlated with Chp1’s binding efficiency. Mutants with >5-fold reduction in H3K9me-binding efficiency that cannot establish centromeric heterochromatin exhibited elevated rates of chromosome missegregation.
PMID:19362535	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 8.1	The efficiency of chromosome segregation was also monitored in clr4+ reintroduction chp1 mutant cells (Table S4) and closely correlated with Chp1’s binding efficiency. Mutants with >5-fold reduction in H3K9me-binding efficiency that cannot establish centromeric heterochromatin exhibited elevated rates of chromosome missegregation.
PMID:19362535	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 4.6	The efficiency of chromosome segregation was also monitored in clr4+ reintroduction chp1 mutant cells (Table S4) and closely correlated with Chp1’s binding efficiency. Mutants with >5-fold reduction in H3K9me-binding efficiency that cannot establish centromeric heterochromatin exhibited elevated rates of chromosome missegregation.
PMID:19362535	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 8.7	The efficiency of chromosome segregation was also monitored in clr4+ reintroduction chp1 mutant cells (Table S4) and closely correlated with Chp1’s binding efficiency. Mutants with>5-fold reduction in H3K9me-binding efficiency that cannot establish centromeric heterochromatin exhibited elevated rates of chromosome missegregation.
PMID:19362535	FYPO:0008195	decreased histone H3-K9Me binding [has_severity] low	The observed affinities ranged from close to wild-type to complete loss of specific binding. The F61A mutant showed little reduction in binding affinity compared with wild-type Chp1. A
PMID:19362535	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 23	Unlike chp1 null cells, which showed 23% of mitotic cells undergoing chromosome missegregation, the chromodomain point-mutated strains, with the exception of V24Rchp1, showed few cells undergoing aberrant mitoses (Table S3).
PMID:19362535	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	We found, however, that introduction of F276Aago1 into either the E23Vchp1 or V24Mchp1 mutants resulted in loss of silencing of cen::ura4+ .
PMID:19362535	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	We found, however, that introduction of F276Aago1 into either the E23Vchp1 or V24Mchp1 mutants resulted in loss of silencing of cen::ura4+ .
PMID:19362535	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	We found, however, that introduction of F276Aago1 into either the E23Vchp1 or V24Mchp1 mutants resulted in loss of silencing of cen::ura4+ .
PMID:19362535	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	We found, however, that introduction of F276Aago1 into either the E23Vchp1 or V24Mchp1 mutants resulted in loss of silencing of cen::ura4+ .
PMID:19362535	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	While chp1D and chp1CDD cells lack centromeric siRNAs, they were present in all other mutants with the exception of V24R.
PMID:19362535	FYPO:0003431	abolished histone H3K9me binding	and the V24R mutant abolished the specificity of the chromodomain interaction for K9 methylated peptides (Kd > 500 mM).
PMID:19362535	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various mutant backgrounds (Figure 6B).
PMID:19362535	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various mutant backgrounds (Figure 6B).
PMID:19362535	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various mutant backgrounds (Figure 6B).
PMID:19362535	FYPO:0000862	normal histone H3-K9 dimethylation at centromere during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various centromeric H3K9me2 levels were low in many of the chp1 chromodomain clr4+ reintroduction strains and closely mirrored the levels of Chp1 recruitment in the various mutant backgrounds (Figure 6B).
PMID:19362535	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	loss of maintenance of heterochromatin was seen in cells expressing both Tas3WG and E23Vchp1, unlike cells expressing either single mutant
PMID:19362535	FYPO:0004742	normal chromatin silencing at centromere outer repeat	loss of maintenance of heterochromatin was seen in cells expressing both Tas3WG and E23Vchp1, unlike cells expressing either single mutant
PMID:19362535	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	loss of maintenance of heterochromatin was seen in cells expressing both Tas3WG and E23Vchp1, unlike cells expressing either single mutant
PMID:19362535	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	loss of maintenance of heterochromatin was seen in cells expressing both Tas3WG and E23Vchp1, unlike cells expressing either single mutant
PMID:19362535	GO:0062072	histone H3K9me2/3 reader activity [has_input] hht2/Me(K9)	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).
PMID:19362535	GO:0062072	histone H3K9me2/3 reader activity [has_input] hht3/Me(K9)	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).
PMID:19362535	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPAC18G6.02c [part_of] heterochromatin formation	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2). S10 of histone H3 is phosphorylated during mitosis and displaces HP1 proteins (including Swi6) from chromatin (Fischle et al., 2005; Hirota et al., 2005; Yamada et al., 2005). We investigated whether binding of Swi6 and Chp1 to H3K9me peptides was affected by S10 phosphorylation and found a strong reduction in both Chp1- and Swi6-binding affinity (Table S2; Figure S2B)
PMID:19362535	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPAC664.01c [part_of] heterochromatin formation	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2). S10 of histone H3 is phosphorylated during mitosis and displaces HP1 proteins (including Swi6) from chromatin (Fischle et al., 2005; Hirota et al., 2005; Yamada et al., 2005). We investigated whether binding of Swi6 and Chp1 to H3K9me peptides was affected by S10 phosphorylation and found a strong reduction in both Chp1- and Swi6-binding affinity (Table S2; Figure S2B)
PMID:19362535	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPAC18G6.02c [part_of] heterochromatin formation	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).S10 of histone H3 is phosphorylated during mitosis and displaces HP1 proteins (including Swi6) from chromatin (Fischle et al., 2005; Hirota et al., 2005; Yamada et al., 2005). We investigated whether binding of Swi6 and Chp1 to H3K9me peptides was affected by S10 phosphorylation and found a strong reduction in both Chp1- and Swi6-binding affinity (Table S2; Figure S2B)
PMID:19362535	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPAC664.01c [part_of] heterochromatin formation	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).S10 of histone H3 is phosphorylated during mitosis and displaces HP1 proteins (including Swi6) from chromatin (Fischle et al., 2005; Hirota et al., 2005; Yamada et al., 2005). We investigated whether binding of Swi6 and Chp1 to H3K9me peptides was affected by S10 phosphorylation and found a strong reduction in both Chp1- and Swi6-binding affinity (Table S2; Figure S2B)
PMID:19362535	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPAC18G6.02c [part_of] heterochromatin formation	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).S10 of histone H3 is phosphorylated during mitosis and displaces HP1 proteins (including Swi6) from chromatin (Fischle et al., 2005; Hirota et al., 2005; Yamada et al., 2005). We investigated whether binding of Swi6 and Chp1 to H3K9me peptides was affected by S10 phosphorylation and found a strong reduction in both Chp1- and Swi6-binding affinity (Table S2; Figure S2B)
PMID:19362535	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPAC664.01c [part_of] heterochromatin formation	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. || we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).S10 of histone H3 is phosphorylated during mitosis and displaces HP1 proteins (including Swi6) from chromatin (Fischle et al., 2005; Hirota et al., 2005; Yamada et al., 2005). We investigated whether binding of Swi6 and Chp1 to H3K9me peptides was affected by S10 phosphorylation and found a strong reduction in both Chp1- and Swi6-binding affinity (Table S2; Figure S2B)
PMID:19362535	GO:0062072	histone H3K9me2/3 reader activity [has_input] hht1/Me(K9)	the Chp1 chromodomain bound both H3K9me2 and H3K9me3 peptides with significantly higher affinity than either Clr4 or Swi6 (Table 1), and all proteins bound H3K9me3 more tightly than H3K9me2. ||we solved the crystal structure of the Chp1 chromodomain (CD) in complex with an H3K9me3 peptide (Figure 1C; Table 2).
PMID:19362535	FYPO:0008070	normal histone H3-K9 methylation at centromere during vegetative growth	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19362535	FYPO:0008070	normal histone H3-K9 methylation at centromere during vegetative growth	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19362535	FYPO:0008070	normal histone H3-K9 methylation at centromere during vegetative growth	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19362535	FYPO:0008070	normal histone H3-K9 methylation at centromere during vegetative growth	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19362535	FYPO:0008070	normal histone H3-K9 methylation at centromere during vegetative growth	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19362535	FYPO:0008070	normal histone H3-K9 methylation at centromere during vegetative growth	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19362535	FYPO:0008070	normal histone H3-K9 methylation at centromere during vegetative growth	unlike chp1 null cells, there was no significant decrease in centromeric H3K9me2 or Swi6 association in any of the chp1 mutants tested (Figures 4B and 4C; Figure S5B).
PMID:19363481	FYPO:0002150	inviable spore population	(Figure 5)
PMID:19363481	FYPO:0002150	inviable spore population	(Figure 5)
PMID:19363481	FYPO:0002150	inviable spore population	(Figure 5)
PMID:19363481	FYPO:0002150	inviable spore population	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	FYPO:0001234	slow vegetative cell population growth	(Figure 5)
PMID:19363481	GO:0005515	protein binding	(comment: CHECK SLD1)
PMID:19363481	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC30D11.13 [assayed_protein] PomBase:SPBC16H5.03c	Strikingly, a GST-Rad60 SLD2E380R construct did not detectably interact with Ubc9-TAP (Fig. 3a)
PMID:19363481	FYPO:0000088	sensitive to hydroxyurea	slow growth phenotype and heterogeneity in cell length; reflecting elevated levels of spontaneous DNA damage and “constitutive” activation of the DNA damage checkpoint in these cells (Fig. 4a and data not shown).
PMID:19363481	FYPO:0001127	abnormal cell size [has_severity] variable severity	slow growth phenotype and heterogeneity in cell length; reflecting elevated levels of spontaneous DNA damage and “constitutive” activation of the DNA damage checkpoint in these cells (Fig. 4a and data not shown).
PMID:19363481	FYPO:0001355	decreased vegetative cell population growth	slow growth phenotype and heterogeneity in cell length; reflecting elevated levels of spontaneous DNA damage and “constitutive” activation of the DNA damage checkpoint in these cells (Fig. 4a and data not shown).
PMID:19366728	FYPO:0006518	loss of viability in G0	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	loss of viability in G0	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	loss of viability in G0	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	loss of viability in G0	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	loss of viability in G0	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	loss of viability in G0	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	loss of viability in G0	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	loss of viability in G0	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	loss of viability in G0	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	loss of viability in G0	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	loss of viability in G0	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	loss of viability in G0	(comment: CHECK fragmented)
PMID:19366728	FYPO:0006518	loss of viability in G0	(comment: CHECK fragmented)
PMID:19373772	GO:0032153	cell division site [exists_during] mitotic M phase	(comment: CHECK during mitotic M phase?)
PMID:19373772	FYPO:0000251	decreased cell population growth on galactose carbon source	(comment: CONDITION non fermentable carbon source)
PMID:19373772	GO:0090149	mitochondrial membrane fission [happens_during] mitotic M phase	"(comment: happens during mitotic M phase? term will be renames ""mitochondrial membrane fission"")"
PMID:19373772	GO:0090149	mitochondrial membrane fission [happens_during] mitotic interphase	"(comment: happens during mitotic M phase? term will be renames ""mitochondrial membrane fission"")"
PMID:19394293	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure 3)
PMID:19394293	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPBC83.03c	(Figure 3) To rule out that the observed silencing defects were due to instability of the mutant Tas3 proteins, we examined the levels of wild-type and mutant Tas3 protein by western blotting and found that the mutant proteins were expressed to similar levels as the wild-type protein (Figure 3C).
PMID:19394293	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure 3) tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1
PMID:19394293	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure 3) tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1
PMID:19394293	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure 3) tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1
PMID:19394293	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure 3) tas3-TAM Mutations Cause a Dramatic Loss of ura4+ Silencing at imr1 but Only a Modest Loss at otr1
PMID:19394293	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPBC83.03c	(Figure 3C)
PMID:19394293	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPBC83.03c	(Figure 3C)
PMID:19394293	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPBC83.03c	(Figure 3C)
PMID:19394293	FYPO:0005929	decreased chromatin binding at centromere outer repeat	At the dg and dh repeats, we found a consistent 2- to 3-fold reduction in mutant Tas3 occupancy compared to wild-type (Figure 5B, compare lanes 3-6 with lane 2; and Figure 5C). Also, consistent with the otr1R::ura4+ silencing data (Figure 3B), mutant Tas3-TAM proteins associated with the ura4+ insert at otr1R less efficiently than wild-type Tas3 (Figure 5D, compare lanes 3-6 with lane 2; and Figure 5E). In
PMID:19394293	FYPO:0008072	normal spatial extent of histone H3-K9 methylation at peri-centromere during vegetative growth	Surprisingly, we found no defect in H3K9me in tas3DTAM compared to wild-type cells at native centromeric repeats (dg1, imr1, imr2-1, or imr2-2) or the ura4+ inserts (for imr1R::ura4+
PMID:19394293	FYPO:0004205	decreased siRNA level	To determine the effect of tas3-TAM mutations on cen siRNAs levels, we performed northern blot analysis on RNAs isolated from wild-type, tas3D, and tas3-TAM mutant cells. We found a dramatic reduction in the levels of both total (Figure 4C) and Ago1-purified (Figure 4D) cen siRNAs in all tas3-TAM mutants compared to wild-type.
PMID:19394293	FYPO:0004205	decreased siRNA level	To determine the effect of tas3-TAM mutations on cen siRNAs levels, we performed northern blot analysis on RNAs isolated from wild-type, tas3D, and tas3-TAM mutant cells. We found a dramatic reduction in the levels of both total (Figure 4C) and Ago1-purified (Figure 4D) cen siRNAs in all tas3-TAM mutants compared to wild-type.
PMID:19394293	FYPO:0004205	decreased siRNA level	To determine the effect of tas3-TAM mutations on cen siRNAs levels, we performed northern blot analysis on RNAs isolated from wild-type, tas3D, and tas3-TAM mutant cells. We found a dramatic reduction in the levels of both total (Figure 4C) and Ago1-purified (Figure 4D) cen siRNAs in all tas3-TAM mutants compared to wild-type.
PMID:19394293	FYPO:0004205	decreased siRNA level	To determine the effect of tas3-TAM mutations on cen siRNAs levels, we performed northern blot analysis on RNAs isolated from wild-type, tas3D, and tas3-TAM mutant cells. We found a dramatic reduction in the levels of both total (Figure 4C) and Ago1-purified (Figure 4D) cen siRNAs in all tas3-TAM mutants compared to wild-type.
PMID:19394293	FYPO:0008073	normal RITS complex assembly	We found that mutant proteins coimmunoprecipitated with Chp1 and FLAG-Ago1 with similar efficiency as the wild-type protein (Figures 4A and 4B, compare lane 1 with lanes 2-5). This result demonstrates that RITS complex formation is not affected in tas3-TAM mutants and that theCterminus of Tas3 is not involved in Chp1 or Ago1 binding (also shown in Partridge et al. [2007]).
PMID:19416828	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus	"(comment: RTS1 inversion background abolishes DSB formation; ""decreased"" level in rtf1-W405G is relative to wild type and above the inverted-RTS1 background level)"
PMID:19417105	FYPO:0001645	decreased protein-protein interaction	(Fig. 5B)
PMID:19417105	FYPO:0001645	decreased protein-protein interaction	(Fig. 5B)
PMID:19417105	FYPO:0001645	decreased protein-protein interaction	(Fig. 5B)
PMID:19417105	GO:0018444	translation release factor complex	(Figure 1)
PMID:19417105	GO:0018444	translation release factor complex	(Figure 1)
PMID:19417105	FYPO:0001355	decreased vegetative cell population growth	(Figure 5A)
PMID:19417105	FYPO:0001355	decreased vegetative cell population growth	(Figure 5A)
PMID:19417105	FYPO:0002061	inviable vegetative cell population	(Figure 5A)
PMID:19417105	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC584.04 [assayed_using] PomBase:SPAC1834.01 [has_severity] high	(Supplemental Table S1).
PMID:19417105	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC584.04 [assayed_using] PomBase:SPAC1834.01 [has_severity] high	(Supplemental Table S1).
PMID:19417105	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC584.04 [assayed_using] PomBase:SPAC1834.01 [has_severity] high	(Supplemental Table S1).
PMID:19417105	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC584.04 [assayed_using] PomBase:SPAC1834.01 [has_severity] high	(Supplemental Table S1).
PMID:19417105	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC584.04 [assayed_using] PomBase:SPAC1834.01	(Supplemental Table S1).
PMID:19417105	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC584.04 [assayed_using] PomBase:SPAC1834.01	(Supplemental Table S1).
PMID:19417105	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC584.04 [assayed_using] PomBase:SPAC1834.01 [has_severity] medium	(Supplemental Table S1).
PMID:19417105	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC584.04 [assayed_using] PomBase:SPAC1834.01 [has_severity] high	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC584.04 [assayed_using] PomBase:SPAC1834.01 [has_severity] high	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC584.04 [assayed_using] PomBase:SPAC1834.01 [has_severity] high	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC584.04 [assayed_using] PomBase:SPAC1834.01 [has_severity] high	Supplemental Table S1; Supplemental Fig. S3
PMID:19417105	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC584.04 [assayed_using] PomBase:SPAC1834.01 [has_severity] high	Supplemental Table S1; Supplemental Fig. S3
PMID:19422421	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(comment: 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:19422421	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(comment: 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:19422421	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(comment: 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:19422421	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(comment: 25 degrees, permissive for hsk1-89)
PMID:19422421	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: 25 degrees, permissive for hsk1-89)
PMID:19422421	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(comment: 25 degrees, permissive for hsk1-89)
PMID:19422421	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(comment: 25 degrees, permissive for hsk1-89)
PMID:19422421	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: 25 degrees, permissive for hsk1-89)
PMID:19422421	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: 25 degrees, permissive for hsk1-89)
PMID:19422421	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(comment: 25 degrees, permissive for hsk1-89)
PMID:19422421	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 30 degrees)
PMID:19422421	FYPO:0001357	normal vegetative cell population growth	(comment: actually 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:19422421	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC216.06c	(comment: actually 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:19422421	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC30D10.04	(comment: actually 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:19422421	GO:0000785	chromatin	(comment: increased chromatin association in presence of HU)
PMID:19427212	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 100	(Fig. 1B)
PMID:19427212	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 100	(Fig. 1B)
PMID:19427212	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 100	(Fig. 1B)
PMID:19427212	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 20	(Fig. 1B)
PMID:19427212	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 20	(Fig. 1B)
PMID:19427212	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 20	(Fig. 1B)
PMID:19427212	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 100	(Fig. 1B)
PMID:19427212	FYPO:0000784	protein mislocalized to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	(Fig. 1C)
PMID:19427212	FYPO:0002557	decreased protein localization to medial cortex during vegetative growth [assayed_protein] PomBase:SPCC4B3.15 [has_penetrance] high	(Fig. 1C)
PMID:19427212	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 80	(Fig. 2B)
PMID:19427212	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 85	(Fig. 2B)
PMID:19427212	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 90	(Fig. 2B)
PMID:19427212	FYPO:0000784	protein mislocalized to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	(Fig. 2C)
PMID:19427212	FYPO:0002557	decreased protein localization to medial cortex during vegetative growth [assayed_protein] PomBase:SPCC4B3.15 [has_penetrance] high	(Fig. 2C)
PMID:19427212	FYPO:0002557	decreased protein localization to medial cortex during vegetative growth [assayed_protein] PomBase:SPCC4B3.15 [has_penetrance] low	(Fig. 2C)
PMID:19427212	FYPO:0000784	protein mislocalized to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	(Fig. 2C)
PMID:19427212	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC57A10.02 [assayed_protein] PomBase:SPCC4B3.15	(Fig. 2D)
PMID:19427212	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC57A10.02 [assayed_protein] PomBase:SPCC4B3.15 [has_severity] high	(Fig. 2D)
PMID:19427212	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	(Fig. 3A)
PMID:19427212	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 85	(Fig. 3B)
PMID:19427212	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 85	(Fig. 3B)
PMID:19427212	FYPO:0001369	mislocalized actomyosin contractile ring [has_penetrance] 20	(Fig. 3C,D)
PMID:19427212	FYPO:0001369	mislocalized actomyosin contractile ring [has_penetrance] 60	(Fig. 3C,D)
PMID:19427212	FYPO:0001369	mislocalized actomyosin contractile ring [has_penetrance] 90	(Fig. 3C,D)
PMID:19427212	GO:1902408	mitotic cytokinesis, division site positioning	(Fig. 4)
PMID:19427212	GO:0043495	protein-membrane adaptor activity [has_input] PomBase:SPCC4B3.15 [occurs_in] medial cortex [happens_during] mitotic interphase [part_of] mitotic cytokinesis, division site positioning	We conclude that fission yeast cytokinesis uses two overlapping mechanisms to position Mid1 at the central cortex. First, Cdr2 anchors Mid1 at the medial cortex during interphase through a physical interaction.
PMID:19430462	GO:0036450	polyuridylation-dependent decapping of nuclear-transcribed mRNA	(comment: urg1, gar2, act1, adh1, pof9 and hcn1 mRNAs were shown to be direct targets by cRACE sequence analysis.)
PMID:19430466	GO:0008569	minus-end-directed microtubule motor activity [part_of] microtubule bundle formation	(Fig. 1f) (comment: ATP-dependent) Supplementary Information, Movie 1)
PMID:19430466	GO:0008017	microtubule binding	(Fig. 2c)
PMID:19430466	FYPO:0006342	decreased microtubule binding [assayed_using] PomBase:SPAC664.10	(Fig. 2d)
PMID:19430466	FYPO:0006343	abolished microtubule bundle formation [assayed_using] PomBase:SPAC664.10	(Fig. 2j)
PMID:19430466	FYPO:0006343	abolished microtubule bundle formation [assayed_using] PomBase:SPAC664.10	(Fig. 2j)
PMID:19430466	GO:0005872	minus-end kinesin complex	(comment: CHECK homodimer)
PMID:19431238	GO:0051285	cell cortex of cell tip	(comment: ocalization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim))
PMID:19431238	GO:0005938	cell cortex	(comment: ocalization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim))
PMID:1943699	FYPO:0004204	decreased mature snRNA level [assayed_using] PomBase:SPSNRNA.02	(comment: assay construct also has nt change G36C to distinguish from snu2+ transcript)
PMID:1943699	FYPO:0004204	decreased mature snRNA level [assayed_using] PomBase:SPSNRNA.02	(comment: assay construct also has nt change G36C to distinguish from snu2+ transcript)
PMID:1943699	FYPO:0003161	RNA absent from cell during vegetative growth [assayed_using] PomBase:SPSNRNA.02	(comment: assay construct also has nt change G36C to distinguish from snu2+ transcript)
PMID:1943699	FYPO:0004204	decreased mature snRNA level [assayed_using] PomBase:SPSNRNA.02	(comment: assay construct also has nt change G36C to distinguish from snu2+ transcript)
PMID:1944266	FYPO:0001759	normal protein phosphatase activity	(comment: assayed substrate: rabbit muscle phosphorylase)
PMID:19443688	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. 1)
PMID:19443688	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	(Fig. 1)
PMID:19443688	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. 1)
PMID:19443688	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. 2D)
PMID:19443688	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPBP35G2.10	(Fig. 3D)
PMID:19443688	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. 4C)
PMID:19443688	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	(Fig. 4C)
PMID:19443688	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. 4C)
PMID:19443688	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPAC31A2.05c	(Fig. S3A)
PMID:19443688	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC338.17c	(Fig. S3A)
PMID:19443688	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC622.16c	(Fig. S3B)
PMID:19443688	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. S5)
PMID:19474789	GO:0071341	medial cortical node [exists_during] mitotic G2 phase	(Fig. 1a, b)
PMID:19474789	GO:0071341	medial cortical node [exists_during] mitotic G2 phase	(Fig. 1a, b)
PMID:19474789	GO:0071341	medial cortical node [exists_during] mitotic G2 phase	(Fig. 1a, b)
PMID:19474789	GO:0071341	medial cortical node [exists_during] mitotic G2 phase	(Fig. 1c, Supplementary Fig. 2a)
PMID:19474789	FYPO:0002556	decreased protein localization to medial cortex, with protein distributed in cell cortex near non-growing end, during vegetative growth [assayed_using] PomBase:SPAC57A10.02 [has_severity] low	(Fig. 2a, S3a)
PMID:19474789	FYPO:0003919	abolished protein localization to medial cortical node [assayed_using] PomBase:SPCC18B5.03	(Fig. 2a, S3a)
PMID:19474789	FYPO:0002556	decreased protein localization to medial cortex, with protein distributed in cell cortex near non-growing end, during vegetative growth [assayed_using] PomBase:SPAC57A10.02 [has_severity] low	(Fig. 2a, S3a)
PMID:19474789	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPAC57A10.02	(Fig. 2a, S3a)
PMID:19474789	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPAC57A10.02	(Fig. 2a, S3a)
PMID:19474789	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPAC57A10.02	(Fig. 2a, S3a)
PMID:19474789	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPAC57A10.02	(Fig. 2a, S3a)
PMID:19474789	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPCC18B5.03	(Fig. 2a, S3a)
PMID:19474789	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPCC18B5.03	(Fig. 2a, S3a)
PMID:19474789	FYPO:0003919	abolished protein localization to medial cortical node [assayed_using] PomBase:SPCC4B3.15	(Fig. 2a, Supplementary Fig. 3a)
PMID:19474789	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPAC57A10.02	(Fig. 2a, Supplementary Fig. 3a)
PMID:19474789	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPAC57A10.02	(Fig. 2a, Supplementary Fig. 3a)
PMID:19474789	FYPO:0003919	abolished protein localization to medial cortical node [assayed_using] PomBase:SPAC644.06c	(Fig. 2a, Supplementary Fig. 3a)
PMID:19474789	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPAC57A10.02	(Fig. 2a, Supplementary Fig. 3a)
PMID:19474789	FYPO:0003919	abolished protein localization to medial cortical node [assayed_using] PomBase:SPBC1A4.05	(Fig. 2a, Supplementary Fig. 3a)
PMID:19474789	GO:0005634	nucleus [exists_during] mitotic G2 phase	(Fig. 2c, d, e)
PMID:19474789	GO:0071341	medial cortical node [exists_during] mitotic G2 phase	(Fig. 2c, d, e)
PMID:19474789	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	(Fig. 2c, d, e)
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 3)
PMID:19474789	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] medium	(Fig. 3)
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	(Fig. 3)
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 3)
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 3)
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 3)
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 3)
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 3)
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 3)
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high	(Fig. 3)
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 3)
PMID:19474789	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(Fig. 3)
PMID:19474789	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(Fig. 3)
PMID:19474789	FYPO:0002556	decreased protein localization to medial cortex, with protein distributed in cell cortex near non-growing end, during vegetative growth [assayed_using] PomBase:SPAC57A10.02 [has_severity] high	(Fig. 3a)
PMID:19474789	FYPO:0003919	abolished protein localization to medial cortical node [assayed_using] PomBase:SPCC18B5.03	(Fig. S6)
PMID:19474789	FYPO:0002556	decreased protein localization to medial cortex, with protein distributed in cell cortex near non-growing end, during vegetative growth [assayed_using] PomBase:SPAC57A10.02	(Figure 4d)
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Supplementary Table 1)
PMID:19474789	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09	Supplementary Fig. 10
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [assayed_using] PomBase:SPCC18B5.03 [has_penetrance] high	Supplementary Fig. 6
PMID:19474789	FYPO:0002556	decreased protein localization to medial cortex, with protein distributed in cell cortex near non-growing end, during vegetative growth [has_severity] high [assayed_using] PomBase:SPCC4B3.15	Supplementary Figure S8
PMID:19474789	FYPO:0002556	decreased protein localization to medial cortex, with protein distributed in cell cortex near non-growing end, during vegetative growth [has_severity] high [assayed_using] PomBase:SPAC644.06c	Supplementary Figure S8
PMID:19474789	FYPO:0002556	decreased protein localization to medial cortex, with protein distributed in cell cortex near non-growing end, during vegetative growth [has_severity] high [assayed_using] PomBase:SPAC144.14	Supplementary Figure S8
PMID:19474789	FYPO:0002556	decreased protein localization to medial cortex, with protein distributed in cell cortex near non-growing end, during vegetative growth [assayed_using] PomBase:SPBC1A4.05 [has_severity] high	Supplementary Figure S8
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	Supplementary Table 2
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high	Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete
PMID:19474789	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete
PMID:19474789	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	Supplementary Table 2 These experiments support the pom1 gradient model, pom1 is delocalized in tea1 delete
PMID:19474789	GO:0004674	protein serine/threonine kinase activity [directly_negatively_regulates] PomBase:SPCC18B5.03 [part_of] positive regulation of G2/M transition of mitotic cell cycle	all data These data indicate that Pom1 functions in a dose-dependent manner to delay entry into mitosis through negative regulation of the Cdr2-Cdr1-Wee1 pathway. The pom1D size phenotype is not as severe as wee11 deletion, indicating that further Wee1 regulatory mechanisms are likely to be operating. We conclude that Pom1 is a potential functional link between polarized cell growth and mitotic entry by regulating these two processes.
PMID:19474789	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC57A10.02	all data These data indicate that Pom1 functions in a dose-dependent manner to delay entry into mitosis through negative regulation of the Cdr2-Cdr1-Wee1 pathway. The pom1D size phenotype is not as severe as wee11 deletion, indicating that further Wee1 regulatory mechanisms are likely to be operating. We conclude that Pom1 is a potential functional link between polarized cell growth and mitotic entry by regulating these two processes.
PMID:19474789	GO:0031569	mitotic G2 cell size control checkpoint signaling	all data These data indicate that Pom1 functions in a dose-dependent manner to delay entry into mitosis through negative regulation of the Cdr2-Cdr1-Wee1 pathway. The pom1D size phenotype is not as severe as wee11 deletion, indicating that further Wee1 regulatory mechanisms are likely to be operating. We conclude that Pom1 is a potential functional link between polarized cell growth and mitotic entry by regulating these two processes.
PMID:19474789	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC57A10.02 [part_of] negative regulation of G2/M transition of mitotic cell cycle	all data These data indicate that Pom1 functions in a dose-dependent manner to delay entry into mitosis through negative regulation of the Cdr2-Cdr1-Wee1 pathway. The pom1D size phenotype is not as severe as wee11 deletion, indicating that further Wee1 regulatory mechanisms are likely to be operating. We conclude that Pom1 is a potential functional link between polarized cell growth and mitotic entry by regulating these two processes.
PMID:19474792	FYPO:0001355	decreased vegetative cell population growth	(Fig. 1b)
PMID:19474792	FYPO:0001355	decreased vegetative cell population growth	(Fig. 1b)
PMID:19474792	FYPO:0001355	decreased vegetative cell population growth	(Fig. 1b)
PMID:19474792	FYPO:0000405	normal mitotic G2/M phase transition [has_penetrance] 50	(Fig. 1d) ie not blocked in g2
PMID:19474792	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC57A10.02	(Fig. 1e) in vitro link from epistastis and delayed cdc2 phosphorylation
PMID:19474792	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC57A10.02 [part_of] negative regulation of G2/M transition of mitotic cell cycle	(Fig. 1e) in vitro link from epistastis and delayed cdc2 phosphorylation
PMID:19474792	MOD:01455	O-phosphorylated residue [added_by] PomBase:SPAC2F7.03c	(Fig. 1e, 1f)
PMID:19474792	FYPO:0002830	delayed onset of protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09	(Fig. 1g)
PMID:19474792	FYPO:0002556	decreased protein localization to medial cortex, with protein distributed in cell cortex near non-growing end, during vegetative growth [assayed_using] PomBase:SPAC57A10.02	(Fig. 2a) and data not shown
PMID:19474792	FYPO:0002556	decreased protein localization to medial cortex, with protein distributed in cell cortex near non-growing end, during vegetative growth [assayed_using] PomBase:SPAC57A10.02	(Fig. 2a) and data not shown
PMID:19474792	FYPO:0002556	decreased protein localization to medial cortex, with protein distributed in cell cortex near non-growing end, during vegetative growth [assayed_using] PomBase:SPAC57A10.02	(Fig. 2a) and data not shown
PMID:19474792	FYPO:0003307	increased mitotic index	(Fig. 3b).
PMID:19474792	FYPO:0003736	normal mitotic index	(Fig. 3b).
PMID:19474792	FYPO:0002516	premature mitotic G2/M phase transition	(Fig. 3b).
PMID:19474792	FYPO:0003736	normal mitotic index	(Fig. 3b).
PMID:19474792	FYPO:0003736	normal mitotic index	(Fig. 3b).
PMID:19474792	GO:0051285	cell cortex of cell tip	(Supplementary Fig. 2)
PMID:19474792	GO:0051285	cell cortex of cell tip	(Supplementary Fig. 2)
PMID:19474792	GO:0071341	medial cortical node [exists_during] mitotic interphase	(Supplementary Fig. 3)
PMID:19474792	GO:0071341	medial cortical node [exists_during] mitotic interphase	(Supplementary Fig. 3)
PMID:19474792	FYPO:0005841	normal protein transport along microtubule to cell tip cortex during vegetative growth [assayed_using] PomBase:SPAC2F7.03c	(Supplementary Fig. 4)
PMID:19474792	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Table 1)
PMID:19474792	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Table 1)
PMID:19474792	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Table 1)
PMID:19474792	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Table 1)
PMID:19474792	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(Table 1)
PMID:19474792	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Table 1)
PMID:19474792	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] low	(Table 1)
PMID:19474792	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] low	(Table 1)
PMID:19474792	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] low	(Table 1)
PMID:19474792	GO:1903067	negative regulation of protein localization to cell tip [has_input] PomBase:SPAC57A10.02	(comment: cortex)
PMID:19474792	FYPO:0001357	normal vegetative cell population growth	(comment: or is this reduced with low exressivity?)
PMID:19474792	FYPO:0001124	normal vegetative cell size [has_severity] low	Table 1
PMID:19474792	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	Table 1
PMID:19474792	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	Table 1
PMID:19474792	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	Table 1
PMID:19474792	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	Table 1
PMID:19474792	FYPO:0001124	normal vegetative cell size [has_severity] low	Table 1
PMID:19474792	FYPO:0001234	slow vegetative cell population growth	Table 1, Fig. 2d
PMID:19474792	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	Table 1, Fig. 2d
PMID:19474792	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC57A10.02	Table 1, Fig. 2d
PMID:19474792	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] medium	table1
PMID:19474792	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] low	table1
PMID:19474792	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] medium	table1
PMID:19486165	FYPO:0002061	inviable vegetative cell population	(Fig. 1A)
PMID:19486165	FYPO:0001234	slow vegetative cell population growth	(Fig. 1A)
PMID:19486165	FYPO:0000086	sensitive to tacrolimus	(Fig. 1A)
PMID:19486165	FYPO:0000110	sensitive to pravastatin	(Fig. 1C)
PMID:19486165	GO:0042175	nuclear outer membrane-endoplasmic reticulum membrane network	(Fig. 2A)
PMID:19486165	GO:0005635	nuclear envelope	(Fig. 2B)
PMID:19486165	FYPO:0000650	increased septation index	(Fig. 4B)
PMID:19486165	FYPO:0002060	viable vegetative cell population	(Fig. 5A)
PMID:19486165	FYPO:0002720	sensitive to beta-glucanase	(Fig. 5B)
PMID:19486165	FYPO:0000046	decreased cell population growth	(Fig. 5C)
PMID:19486165	FYPO:0000046	decreased cell population growth	(Fig. 5C)
PMID:19486165	FYPO:0000046	decreased cell population growth	(Fig. 5C)
PMID:19486165	FYPO:0002674	normal protein localization to plasma membrane [assayed_using] PomBase:SPAC16.01	(Fig. 6C)
PMID:19486165	FYPO:0000104	sensitive to cycloheximide [has_severity] high	(Fig. 7B)
PMID:19486165	FYPO:0000104	sensitive to cycloheximide [has_severity] high	(Fig. 7B)
PMID:19486165	FYPO:0000070	resistance to amphotericin B [has_severity] high	(Fig. 7B)
PMID:19486165	FYPO:0000070	resistance to amphotericin B [has_severity] high	(Fig. 7B)
PMID:19486165	FYPO:0000070	resistance to amphotericin B [has_severity] high	(Fig. 7B)
PMID:19486165	FYPO:0000104	sensitive to cycloheximide [has_severity] high	(Fig. 7B)
PMID:19486165	FYPO:0000046	decreased cell population growth	(Figure 4C)
PMID:19486165	FYPO:0000032	abnormal cytokinesis during vegetative growth	(Figure 4C)
PMID:19486165	FYPO:0002061	inviable vegetative cell population	(Figure 4C)
PMID:19486165	FYPO:0000110	sensitive to pravastatin	(Figure 7A)
PMID:19486165	FYPO:0002061	inviable vegetative cell population	(data not shown).
PMID:19487457	FYPO:0000772	perforated nuclear envelope [has_penetrance] 80	(Fig. 4 C and Video 3)
PMID:19487457	FYPO:0007426	abolished new mitotic spindle pole body insertion into nuclear envelope	(Figure 1 and 2) We conclude that it is the new SPB that fails to activate and insert into the nuclear envelope in cut12.1 mutants.
PMID:19487457	FYPO:0007426	abolished new mitotic spindle pole body insertion into nuclear envelope	(Figure 1 and 2) We conclude that it is the new SPB that fails to activate and insert into the nuclear envelope in cut12.1 mutants.
PMID:19487457	GO:0140480	mitotic spindle pole body insertion into the nuclear envelope	(comment: CHECK insertion)
PMID:19487457	FYPO:0007428	delayed onset of mitotic spindle microtubule nucleation from old spindle pole body	(comment: CHECK monopolar)
PMID:19487457	FYPO:0007428	delayed onset of mitotic spindle microtubule nucleation from old spindle pole body	(comment: CHECK monopolar)
PMID:19487457	FYPO:0000772	perforated nuclear envelope [has_penetrance] 50	Surprisingly, in 50% (n = 79) of the cut12.1 cells that successfully completed mitosis, an efflux of the NLS-GFP--Gal marker accompanied mitotic commitment (Fig. 7, C and D).
PMID:19487457	FYPO:0000772	perforated nuclear envelope [has_penetrance] 80	gapped membrane distortions in the nuclear envelope of cut12.1 cells at 36°C (Fig. 3, A-D). 7D
PMID:19487457	FYPO:0007427	abnormal old mitotic spindle pole body insertion into nuclear envelope, with spindle pole body in nucleoplasm	our ability to identify cells in which an active SPB had apparently lost its association with the membrane completely and fallen into the middle of the nucleus (Fig. 3 E) and the proximity of the SPB to these gaps in the membrane (Fig. 3, A-C).
PMID:19487457	FYPO:0007427	abnormal old mitotic spindle pole body insertion into nuclear envelope, with spindle pole body in nucleoplasm	our ability to identify cells in which an active SPB had apparently lost its association with the membrane completely and fallen into the middle of the nucleus (Fig. 3 E) and the proximity of the SPB to these gaps in the membrane (Fig. 3, A-C).
PMID:19487461	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(Fig. 1A) BrdU incorporation wee1-50 strain analysed at 32°C
PMID:19487461	GO:0005634	nucleus [exists_during] mitotic S phase	(Fig. 1B)
PMID:19487461	FYPO:0005933	decreased protein level during mitotic G1 phase [assayed_using] PomBase:SPAP14E8.02	(Fig. 1G) amount of tos1-GFP in nucleus is dependent on cdc10
PMID:19487461	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication	(Fig. 5A)
PMID:19487461	FYPO:0006575	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication, with otherwise normal S phase	section titled MBF-dependent gene expression...these cells undergo G1 transcription, a seemingly normal Sphase (no region specific amplifications) and can only reinitiate replication once size per genome is minimal size.
PMID:19502236	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC16E9.01c	(Fig. 1A)
PMID:19502236	FYPO:0005639	normal RNA level during cellular response to iron ion starvation [assayed_transcript] PomBase:SPCC645.03c	(Fig. 1B)
PMID:19502236	FYPO:0005639	normal RNA level during cellular response to iron ion starvation [assayed_transcript] PomBase:SPCC645.03c	(Fig. 1B)
PMID:19502236	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 1C)
PMID:19502236	GO:0005634	nucleus [exists_during] cellular response to iron ion	(Fig. 2)
PMID:19502236	GO:0005737	cytoplasm [exists_during] cellular response to iron ion starvation	(Fig. 2)
PMID:19502236	FYPO:0006100	decreased protein localization to cytoplasm, with protein mislocalized to nucleus [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 4B)
PMID:19502236	FYPO:0000840	normal RNA level [assayed_transcript] PomBase:SPCC645.03c	(Fig. 7B)
PMID:19502236	FYPO:0000840	normal RNA level [assayed_transcript] PomBase:SPCC645.03c	(Fig. 7B)
PMID:19502236	FYPO:0000840	normal RNA level [assayed_transcript] PomBase:SPCC645.03c	(Fig. 7B)
PMID:19502236	FYPO:0000840	normal RNA level [assayed_transcript] PomBase:SPCC645.03c	(Fig. 7B)
PMID:19502236	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC645.03c	(Fig. 7B)
PMID:19502236	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC645.03c	(Fig. 7B)
PMID:19502236	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC645.03c	(Fig. 7B)
PMID:19502236	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC645.03c	(Fig. 7B)
PMID:19502236	FYPO:0006100	decreased protein localization to cytoplasm, with protein mislocalized to nucleus [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 7C)
PMID:19502236	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC26H8.06 [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 9A)
PMID:19502236	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC26H8.06 [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 9A)
PMID:19502236	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC26H8.06 [assayed_protein] PomBase:SPBC16E9.01c [has_severity] high	(Fig. 9A)
PMID:19502236	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC26H8.06 [assayed_protein] PomBase:SPBC16E9.01c [has_severity] medium	(Fig. 9A)
PMID:19502236	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC26H8.06 [assayed_protein] PomBase:SPBC16E9.01c [has_severity] medium	(Fig. 9A)
PMID:19502236	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC26H8.06 [assayed_protein] PomBase:SPBC16E9.01c [has_severity] medium	(Fig. 9A)
PMID:19502236	SO:0001531	nuclear_export_signal	Nonetheless, taken together, our results are consistent with the 93-100-amino acid region of Php4 functioning as an NES in S. pombe.
PMID:19523829	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	((comment: CHECK increased localization of mad2 to kinetochore)
PMID:19543678	FYPO:0002196	abnormal vegetative cell shape [assayed_using] PomBase:SPBC1652.02	(Fig. 3)
PMID:19543678	FYPO:0000806	abnormal Golgi organization [assayed_using] PomBase:SPBC1652.02	(Fig. 3)
PMID:19543678	FYPO:0002714	protein mislocalized to Golgi apparatus [assayed_using] PomBase:SPBC1652.02	(comment: from PM ) (Fig. 3c
PMID:19546237	GO:0010971	positive regulation of G2/M transition of mitotic cell cycle	(comment: CHECK during recovery from stress)
PMID:19567474	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3A)
PMID:19567474	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3A)
PMID:19567474	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3A)
PMID:19567474	FYPO:0007197	increased mitochondrial fission [has_penetrance] high	(Fig. 4)
PMID:19567474	FYPO:0007197	increased mitochondrial fission [has_penetrance] medium	(Fig. 4)
PMID:19570908	FYPO:0001495	viable elongated multinucleate vegetative cell [has_penetrance] 20	(comment: CONDITION 25 degrees C, i.e. lower end of normal temp. range; penetrance higher at 29 degrees C)
PMID:19570908	GO:1902404	mitotic actomyosin contractile ring contraction	(comment: request and use GO:new positive regulation of (MF) microfilament motor activity instead? depends on ancestry of motor activity branch)
PMID:19571115	FYPO:0006716	large and small daughter nuclei, with unequal nuclear envelope distribution [has_penetrance] 7	(Fig. 1)
PMID:19571115	FYPO:0003975	fragmented nuclear envelope [has_penetrance] 50	(Fig. 1)
PMID:19571115	FYPO:0002060	viable vegetative cell population	(Fig. 5B)
PMID:19571115	FYPO:0000411	normal mitotic cell cycle	(Fig. 5B)
PMID:19571115	FYPO:0003975	fragmented nuclear envelope [has_penetrance] 3.2	(Fig. 5D)
PMID:19571115	FYPO:0007572	cortical endoplasmic reticulum detached from plasma membrane	(Fig. 5a)
PMID:19592249	GO:0090267	positive regulation of mitotic cell cycle spindle assembly checkpoint	(Fig. 1)
PMID:19592249	GO:1902426	deactivation of mitotic spindle assembly checkpoint	(Fig. 2)
PMID:19592249	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC19G12.01c [assayed_using] PomBase:SPCC1795.01c	(Figure 1E)
PMID:19592249	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC20F10.06 [assayed_using] PomBase:SPAC19G12.01c	(Figure 1E)
PMID:19592249	FYPO:0001837	increased duration of protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC582.03	(Figure 1a)
PMID:19592249	FYPO:0004754	abolished protein localization to mitotic spindle during mitosis [assayed_using] PomBase:SPBC582.03	(Figure 1a)
PMID:19592249	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Figure 2)
PMID:19592249	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Figure 2)
PMID:19592249	FYPO:0005726	abolished deactivation of mitotic spindle assembly checkpoint [assayed_using] PomBase:SPBC582.03	(Figure 2a) (comment: CHECK abolished)
PMID:19592249	FYPO:0000846	decreased protein degradation during vegetative growth [assayed_using] PomBase:SPBC582.03	(Figure 2a) abolished
PMID:19597328	FYPO:0001125	normal vegetative cell shape	Cell shape or interphase F-actin polarity defects were not observed (Suppl. Fig. S1) conversely to the deletion strain.
PMID:19597328	FYPO:0002442	normal protein localization to cell division site [assayed_protein] PomBase:SPBC4F6.06	During mitosis, the tip signal was detected on the most distant cell end relative to the asymmetric ring (arrow, Fig. 1B). Kin1-GFP was also detected at the division site in tea4Δ (arrowhead, Fig. 1B). We conclude that correct localization of Kin1-GFP does not require Tea4.
PMID:19597328	FYPO:0007451	normal protein localization to cell cortex of cell tip during vegetative growth [assayed_protein] PomBase:SPBC4F6.06	During mitosis, the tip signal was detected on the most distant cell end relative to the asymmetric ring (arrow, Fig. 1B). Kin1-GFP was also detected at the division site in tea4Δ (arrowhead, Fig. 1B). We conclude that correct localization of Kin1-GFP does not require Tea4.
PMID:19597328	FYPO:0003302	nucleus mislocalized towards cell tip during mitotic interphase	Hence, Kin1-K154R acts as a dominant negative mutant and its primary effect is to inhibit maintenance of the nucleus at the geometric cell centre.
PMID:19597328	FYPO:0000339	mislocalized septum during vegetative growth	In Kin1 downregulating cells, we observed that septa were orthogonal to the long cell axis but their positions seemed to be frequently eccentric (Kin1 OFF, Fig. 3A).
PMID:19597328	GO:0032153	cell division site [exists_during] mitotic anaphase B	Indeed, in mitotic cells, we detected a Kin1-GFP signal at the division site (arrowheads, Fig. 1A and C). Kin1-GFP appeared as a ring overlying the cell equator prior to nuclei separation at the onset of anaphase B (Fig. 1C).
PMID:19597328	FYPO:0000117	abnormal septum assembly	Kin1 downregulation promoted aberrant septum material synthesis in tea4Δ: a main asymmetric septal structure was observed together with aberrant septal deposits along the cortex or stretched structures that run along the main cell axis were detected (Fig. 4B)
PMID:19597328	FYPO:0000161	abnormal actomyosin contractile ring assembly	Kin1 was downregulated. Upon Kin1 repression, we observed a defect in F-actin incorporation into the CAR at mitosis compared to Kin1 ON. In 84% of anaphase cells, F-actin patches and/or cables were present outside
PMID:19597328	GO:1902716	cell cortex of growing cell tip [exists_during] mitotic G2 phase	Kin1-GFP was detected on the new cell end in early G2 as previously reported24 but also on the old end soon after growth resumption (arrow, Fig. 1C) conversely to the previous report.24
PMID:19597328	FYPO:0000118	multiseptate vegetative cell [has_penetrance] ~3	Kin1Δ cells synthesize normal septa (Fig. 2A) but exhibit a high septation index and a small percentage of multi- septate cells (Fig. 2B), indicating a cell separation defect as previously shown.22-24
PMID:19597328	FYPO:0000650	increased septation index	Kin1Δ cells synthesize normal septa (Fig. 2A) but exhibit a high septation index and a small percentage of multi- septate cells (Fig. 2B), indicating a cell separation defect as previously shown.22-24
PMID:19597328	FYPO:0006213	normal septum morphology	Kin1Δ cells synthesize normal septa (Fig. 2A) but exhibit a high septation index and a small percentage of multi- septate cells (Fig. 2B), indicating a cell separation defect as previously shown.22-24
PMID:19597328	FYPO:0000117	abnormal septum assembly [has_severity] high [has_penetrance] 60	Kin1Δ tea4Δ cells showed a severe cytokinetic phenotype (Fig. 2A), with aberrant septal material randomly deposited in a majority of cells (Fig. 2B).
PMID:19597328	FYPO:0000026	abnormal vegetative cell polarity [has_severity] high [has_penetrance] 60	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	FYPO:0000021	spheroid vegetative cell [has_severity] high	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	FYPO:0000021	spheroid vegetative cell [has_severity] high	Moreover, double mutant cells completey lose their polarity and appeared almost round. This phenotype is strickingly similar to that of kin1Δ tea1Δ (Fig. 2A and B).
PMID:19597328	GO:0140472	cell cortex of non-growing cell tip [exists_during] mitotic G2 phase	The kin1-GFP strain exhibited a wild type phenotype. In living interphase cells, Kin1-GFP signal captured either in static images (Fig. 1A) or by time-lapse video microscopy (Fig. 1C) was localized at the cell tips (arrows, Fig. 1A). The signal appeared as dynamic dots close to the plasma membrane (Suppl. movie S1). Kin1-GFP was detected on the new cell end in early G2 as previously reported24 but also on the old end soon after growth resumption (arrow, Fig. 1C) conversely to the previous report.24
PMID:19597328	FYPO:0003013	abnormal actomyosin contractile ring disassembly	Thus, Kin1 downregulation in tea4Δ uncoupled packed ring formation and constriction but also altered ring disassembly in a subset of cells.
PMID:19597328	FYPO:0003302	nucleus mislocalized towards cell tip during mitotic interphase [has_penetrance] 26	he par1Δ mutant shows a nuclear and septum (arrowhead, Fig. 6C; 25.6% of asymmetric septa versus 10.2% in wild type cells)
PMID:19597328	FYPO:0003302	nucleus mislocalized towards cell tip during mitotic interphase	of the nucleus relative to the cell ends in late G2 cells (≥10 μm) and we observed that a higher proportion of nuclei were misplaced towards the new cell end
PMID:19605557	FYPO:0007797	decreased glucan 1,3-alpha-glucosidase activity [assayed_enzyme] PomBase:SPCC825.02	(Figure 6)
PMID:19605557	FYPO:0007797	decreased glucan 1,3-alpha-glucosidase activity [assayed_enzyme] PomBase:SPCC825.02	(Figure 6)
PMID:19605557	FYPO:0007797	decreased glucan 1,3-alpha-glucosidase activity [assayed_enzyme] PomBase:SPCC825.02	(Figure 6)
PMID:19605557	FYPO:0007797	decreased glucan 1,3-alpha-glucosidase activity [assayed_enzyme] PomBase:SPCC825.02	(Figure 6)
PMID:19605557	GO:0106407	Glc2Man9GlcNAc2 oligosaccharide glucosidase activity	(comment: GII is required for efficient in vitro glucose trimming from G2M9 and G1M9)
PMID:19605557	FYPO:0007797	decreased glucan 1,3-alpha-glucosidase activity	However, GII activity is significantly reduced in the microsomal fraction of ΔGIIΔ cells (Figure 2B), suggesting that GIIΔ is involved in ER localization of GII+
PMID:19606211	SO:0001531	nuclear_export_signal	(comment: CHECK Sequence LVIAMDQLNL mentioned in the text)
PMID:19606211	SO:0001528	nuclear_localization_signal	See Fig. 1
PMID:19624755	FYPO:0000086	sensitive to tacrolimus [has_severity] high	(Fig. 2b) D-apl2 and D-apm1 cells was completely inhibited in the presence of FK506
PMID:19624755	FYPO:0000086	sensitive to tacrolimus [has_severity] high	(Fig. 2b) D-apl2 and D-apm1 cells was completely inhibited in the presence of FK506
PMID:19624755	FYPO:0000086	sensitive to tacrolimus [has_severity] low	(Fig. 2b) whereas that of Dapl4 and Daps1 cells was partially inhibited
PMID:19624755	GO:0005794	Golgi apparatus	(Fig. 4) suggesting that the four adaptin subunits of the AP-1 complex are all localized to the Golgi ⁄ endosomes.
PMID:19624755	FYPO:0007059	decreased protein localization to late endosome [has_severity] high [assayed_using] PomBase:SPCP1E11.06	(Fig. 5)
PMID:19624755	FYPO:0007059	decreased protein localization to late endosome [has_severity] high [assayed_using] PomBase:SPAP27G11.06c	(Fig. 5)
PMID:19624755	FYPO:0007588	abolished protein localization to late endosome [has_severity] high [assayed_using] PomBase:SPBC947.02	(Fig. 5)
PMID:19624755	FYPO:0007059	decreased protein localization to late endosome [assayed_using] PomBase:SPAP27G11.06c [has_severity] low	(Fig. 5)
PMID:19624755	FYPO:0007059	decreased protein localization to late endosome [has_severity] high [assayed_using] PomBase:SPAP27G11.06c	(Fig. 5)
PMID:19624755	FYPO:0007588	abolished protein localization to late endosome [has_severity] high [assayed_using] PomBase:SPBC947.02	(Fig. 5)
PMID:19624755	FYPO:0007588	abolished protein localization to late endosome [has_severity] high [assayed_using] PomBase:SPBC947.02	(Fig. 5)
PMID:19624755	FYPO:0007059	decreased protein localization to late endosome [has_severity] high [assayed_using] PomBase:SPCP1E11.06	(Fig. 5)
PMID:19624755	GO:0005768	endosome	(Fig. 6a)
PMID:19624755	GO:0005886	plasma membrane	(Fig. 6a)
PMID:19624755	FYPO:0002128	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_using] PomBase:SPAC6G9.11	(comment: localized to large endosomal structures)
PMID:19624755	FYPO:0002128	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_using] PomBase:SPAC6G9.11	(comment: localized to large endosomal structures)
PMID:19624755	FYPO:0002128	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_using] PomBase:SPAC6G9.11	(comment: localized to large endosomal structures)
PMID:19624755	FYPO:0002128	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_using] PomBase:SPAC6G9.11	(comment: localized to large endosomal structures)
PMID:19624755	FYPO:0002128	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_using] PomBase:SPAC6G9.11	(comment: localized to large endosomal structures)
PMID:19624755	FYPO:0007589	protein mislocalized to endosome [assayed_using] PomBase:SPAC22E12.09c	(comment: localized to large endosomal structures)
PMID:19624755	FYPO:0002128	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_using] PomBase:SPAC6G9.11	(comment: localized to large endosomal structures)
PMID:19624755	FYPO:0002128	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_using] PomBase:SPAC6G9.11	(comment: localized to large endosomal structures)
PMID:19624755	FYPO:0000115	sensitive to valproic acid [has_severity] high	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA compared with those of Dapl4 and Daps1 cells
PMID:19624755	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA compared with those of Dapl4 and Daps1 cells
PMID:19624755	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA compared with those of Dapl4 and Daps1 cells
PMID:19624755	FYPO:0000115	sensitive to valproic acid [has_severity] high	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA compared with those of Dapl4 and Daps1 cells
PMID:19624755	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	Dapl2 and Dapm1 cells were more sensitive when exposed to 34 °C or to 5 mM VPA compared with those of Dapl4 and Daps1 cells
PMID:19624755	GO:0005794	Golgi apparatus	n wild-type cells, most of Krp1- red fluorescent protein (RFP) colocalized with GFP- Vrg4 (Fig. 7a), indicating that Krp1 mainly localized to the Golgi apparatus
PMID:19624755	GO:0005794	Golgi apparatus	n wild-type cells, most of Krp1- red fluorescent protein (RFP) colocalized with GFP- Vrg4 (Fig. 7a), indicating that Krp1 mainly localized to the Golgi apparatus
PMID:19625445	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high [has_penetrance] high	(Fig. 1)
PMID:19625445	FYPO:0000118	multiseptate vegetative cell [has_penetrance] 12	(Fig. 1)
PMID:19625445	FYPO:0000118	multiseptate vegetative cell [has_penetrance] 3	(Fig. 1)
PMID:19625445	FYPO:0000223	elongated multiseptate vegetative cell	(Fig. 1)
PMID:19625445	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high [has_penetrance] high	(Fig. 1)
PMID:19625445	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high [has_penetrance] high	(Fig. 1) (comment: 16.5 +/- 0.78)
PMID:19625445	FYPO:0002106	viable stubby vegetative cell	(Fig. 1) (comment: IS THIS SMALL OR STUBBY? 11.6 +/- 0.45)
PMID:19625445	FYPO:0002720	sensitive to beta-glucanase [has_severity] high	(Fig. 1C)
PMID:19625445	FYPO:0002720	sensitive to beta-glucanase [has_severity] medium	(Fig. 1C)
PMID:19625445	FYPO:0002720	sensitive to beta-glucanase [has_severity] high	(Fig. 1C)
PMID:19625445	FYPO:0002720	sensitive to beta-glucanase [has_severity] high	(Fig. 1C)
PMID:19625445	FYPO:0007520	normal growth on beta-glucanase	(Fig. 1C)
PMID:19625445	FYPO:0000105	sensitive to cyclosporin A [has_severity] medium	(Fig. 1D)
PMID:19625445	FYPO:0000105	sensitive to cyclosporin A [has_severity] medium	(Fig. 1D)
PMID:19625445	FYPO:0000105	sensitive to cyclosporin A [has_severity] high	(Fig. 1D)
PMID:19625445	FYPO:0000105	sensitive to cyclosporin A [has_severity] high	(Fig. 1D)
PMID:19625445	FYPO:0002680	increased protein phosphorylation [assayed_using] PomBase:SPBC119.08 [has_severity] high	(Fig. 2A)
PMID:19625445	FYPO:0002680	increased protein phosphorylation [assayed_using] PomBase:SPBC119.08 [has_severity] medium	(Fig. 2A)
PMID:19625445	FYPO:0002680	increased protein phosphorylation [assayed_using] PomBase:SPBC119.08 [has_severity] medium	(Fig. 2A)
PMID:19625445	FYPO:0002680	increased protein phosphorylation [has_severity] low [assayed_using] PomBase:SPBC119.08	(Fig. 2A)
PMID:19625445	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPBC119.08 [has_severity] high	(Fig. 2A)
PMID:19625445	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPBC119.08 [has_severity] low	(Fig. 2A)
PMID:19625445	FYPO:0007521	resistance to tacrolimus and magnesium chloride [has_severity] high	(Fig. 2A)
PMID:19625445	FYPO:0007521	resistance to tacrolimus and magnesium chloride [has_severity] high	(Fig. 2A)
PMID:19625445	FYPO:0002680	increased protein phosphorylation [has_severity] low [assayed_using] PomBase:SPBC119.08	(Fig. 2A)
PMID:19625445	FYPO:0007521	resistance to tacrolimus and magnesium chloride [has_severity] high	(Fig. 2B)
PMID:19625445	FYPO:0007521	resistance to tacrolimus and magnesium chloride [has_severity] medium	(Fig. 2B)
PMID:19625445	FYPO:0007522	sensitive to tacrolimus and magnesium chloride [has_severity] medium	(Fig. 2B)
PMID:19625445	FYPO:0007520	normal growth on beta-glucanase	(Fig. 2B)
PMID:19625445	FYPO:0006836	sensitive to magnesium chloride [has_severity] high	(Fig. 2D)
PMID:19625445	FYPO:0006836	sensitive to magnesium chloride [has_severity] medium	(Fig. 2D)
PMID:19625445	FYPO:0007525	decreased ribosome binding	(Fig. 8)
PMID:19625445	FYPO:0002444	loss of punctate cytoplasmic protein localization	(Fig. 8)
PMID:19625445	FYPO:0002680	increased protein phosphorylation [assayed_using] PomBase:SPBC119.08	(Fig. 9A)
PMID:19625445	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPCC4F11.02	(Figure 3D)
PMID:19625445	FYPO:0002680	increased protein phosphorylation [assayed_using] PomBase:SPAC24B11.06c	(Figure 3D)
PMID:19625445	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC26F1.10c	(Figure 3D)
PMID:19625445	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC1685.01	(Figure 3D)
PMID:19625445	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC2G11.07c	(Figure 3D)
PMID:19625445	FYPO:0001885	decreased protein phosphorylation during salt stress [assayed_using] PomBase:SPBC119.08	(Figure 4A)
PMID:19625445	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [assayed_using] PomBase:SPBC119.08	(Figure 4A) (comment: IS THIS NORMAL OR EVEN HIGHER THAN WT? this is higher than wis1DD-cpc2delet so must be increased)
PMID:19625445	FYPO:0001266	normal protein phosphorylation during cellular response to salt stress [assayed_using] PomBase:SPBC119.08	(Figure 4A) (comment: IS THIS NORMAL OR EVEN HIGHER THAN WT?)
PMID:19625445	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_using] PomBase:SPCC4F11.02	(Figure 4B)
PMID:19625445	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_using] PomBase:SPAC2G11.07c	(Figure 4B)
PMID:19625445	FYPO:0003930	decreased protein level during cellular response to salt stress [assayed_using] PomBase:SPAC26F1.10c	(Figure 4B)
PMID:19625445	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_using] PomBase:SPBC1685.01	(Figure 4B)
PMID:19625445	FYPO:0003930	decreased protein level during cellular response to salt stress [assayed_using] PomBase:SPAC19D5.01	(Figure 4B)
PMID:19625445	FYPO:0003151	decreased protein level during cellular response to heat [assayed_using] PomBase:SPAC19D5.01	(Figure 4c)
PMID:19625445	FYPO:0007523	decreased protein level during cellular response to oxidative stress [assayed_using] PomBase:SPAC19D5.01	(Figure 4c)
PMID:19625445	FYPO:0003930	decreased protein level during cellular response to salt stress [assayed_using] PomBase:SPBC29B5.01 [has_penetrance] medium	(Figure 5A)
PMID:19625445	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC29B5.01	(Figure 5A)
PMID:19625445	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_using] PomBase:SPAC19D5.01	(Figure 5B)
PMID:19625445	FYPO:0001486	normal RNA level during cellular response to salt stress [assayed_using] PomBase:SPBC29B5.01	(Figure 5B)
PMID:19625445	FYPO:0001317	normal RNA level during vegetative growth [assayed_using] PomBase:SPBC29B5.01	(Figure 5B)
PMID:19625445	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_using] PomBase:SPAC26F1.10c	(Figure 5B)
PMID:19625445	FYPO:0007523	decreased protein level during cellular response to oxidative stress [assayed_using] PomBase:SPBC29B5.01	(Figure 5D)
PMID:19625445	FYPO:0003930	decreased protein level during cellular response to salt stress [assayed_using] PomBase:SPBC29B5.01	(Figure 5D)
PMID:19625445	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] low	(Figure 6a)
PMID:19625445	FYPO:0000271	sensitive to salt stress [has_severity] high	(Figure 6a)
PMID:19625445	FYPO:0000112	sensitive to sorbitol [has_severity] high	(Figure 6a)
PMID:19625445	FYPO:0000271	sensitive to salt stress [has_severity] high	(Figure 6a)
PMID:19625445	FYPO:0000112	sensitive to sorbitol [has_severity] high	(Figure 6a)
PMID:19625445	FYPO:0001037	normal growth during cellular response to salt stress	(Figure 6a)
PMID:19625445	FYPO:0000961	normal growth on sorbitol	(Figure 6a)
PMID:19625445	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] medium	(Figure 6a)
PMID:19625445	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Figure 6a)
PMID:19625445	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Figure 6a)
PMID:19625445	FYPO:0007524	delayed onset of protein import into nucleus [assayed_using] PomBase:SPAC1783.07c	(Figure 6c,d)
PMID:19625445	FYPO:0004038	delayed onset of increase in RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC3F6.03	(Figure 7)
PMID:19625445	FYPO:0004038	delayed onset of increase in RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPCC757.07c	(Figure 7)
PMID:19625445	FYPO:0004038	delayed onset of increase in RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPCC576.03c	(Figure 7)
PMID:19625445	FYPO:0003930	decreased protein level during cellular response to salt stress [assayed_using] PomBase:SPBC29B5.01 [has_penetrance] medium	(Figure 9)
PMID:19625445	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC29B5.01	(Figure 9)
PMID:19625445	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC26F1.10c	(Figure 9B)
PMID:19625445	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC19D5.01	(Figure 9B)
PMID:19627505	GO:0070867	mating projection tip membrane	(comment: localization requires F-actin -assayed using latrunculin A and membrane rafts -assayed using filipin)
PMID:19636559	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPATRNAPRO.02	data not shown, from text
PMID:19636559	FYPO:0004481	abolished cell population growth at high temperature	data not shown, from text
PMID:19636559	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPATRNAPRO.02	data not shown, from text
PMID:19640845	GO:0036088	D-serine catabolic process	(comment: taken together with TAS from PMID:40259883)
PMID:19643199	FYPO:0002788	small vacuoles during vegetative growth [has_severity] medium	(Fig. 1c)
PMID:19643199	FYPO:0006266	normal vacuole size during vegetative growth	(Fig. 1d)
PMID:19643199	FYPO:0001423	normal protein targeting to vacuole	(Fig. 1d)
PMID:19643199	FYPO:0001423	normal protein targeting to vacuole	(Fig. 1d) (comment: CHECK this term should really be trafficing)
PMID:19646873	FYPO:0003627	normal protein localization [assayed_using] PomBase:SPCC1223.06	(Fig. 2f)
PMID:19646873	FYPO:0006637	decreased protein localization to cell cortex of cell tip, with protein distributed in cortex [assayed_using] PomBase:SPAC110.03	(Fig. 2f)
PMID:19646873	FYPO:0006637	decreased protein localization to cell cortex of cell tip, with protein distributed in cortex [assayed_using] PomBase:SPCC895.05	(Fig. 2f)
PMID:19646873	FYPO:0003627	normal protein localization [assayed_using] PomBase:SPBC1706.01	(Fig. 2f)
PMID:19646873	FYPO:0006637	decreased protein localization to cell cortex of cell tip, with protein distributed in cortex [assayed_using] PomBase:SPAC110.03	(Fig. S2)
PMID:19680287	FYPO:0006428	normal mitotic sister chromatid biorientation	(Fig 3C), showed a similar fraction of mono-oriented chromosomes as wild-type cells
PMID:19680287	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1A)
PMID:19680287	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. 1A)
PMID:19680287	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1A)
PMID:19680287	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1A)
PMID:19680287	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1A)
PMID:19680287	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c	(Fig. 1B, S3)
PMID:19680287	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC20F10.06	(Fig. 1B, S3)
PMID:19680287	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPCC1795.01c	(Fig. 1B, S3)
PMID:19680287	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPCC1322.12c	(Fig. 1B, S3)
PMID:19680287	FYPO:0005684	increased duration of mitotic prometaphase	(Fig. 2A) (comment: assayed with plo1 GFP)
PMID:19680287	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 25	(Fig. 2B)
PMID:19680287	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 7	(Fig. 2B)
PMID:19680287	FYPO:0000326	abnormal mitotic sister chromatid biorientation [has_penetrance] 20	(Fig. 3B,C)
PMID:19680287	FYPO:0000030	abnormal mitotic chromosome congression [has_penetrance] 25	(Fig. 3B,C)
PMID:19680287	FYPO:0000326	abnormal mitotic sister chromatid biorientation [has_penetrance] 30	(Fig. 3B,C)
PMID:19680287	FYPO:0007399	normal protein localization to kinetochore during mitotic interphase [assayed_using] PomBase:SPAC15A10.15	(Fig. 3E)
PMID:19680287	FYPO:0007400	abolished protein localization to kinetochore during mitotic interphase [assayed_using] PomBase:SPAC15A10.15	(Fig. 3E)
PMID:19680287	FYPO:0007399	normal protein localization to kinetochore during mitotic interphase [assayed_using] PomBase:SPAC15A10.15	(Fig. 3E)
PMID:19680287	FYPO:0007244	decreased protein localization to kinetochore during mitotic metaphase [assayed_using] PomBase:SPAC15A10.15	(Fig. 3E, S9)
PMID:19680287	FYPO:0007244	decreased protein localization to kinetochore during mitotic metaphase [assayed_using] PomBase:SPAC15A10.15	(Fig. 3E, S9)
PMID:19680287	FYPO:0004396	normal mitotic spindle elongation	(Fig. S10)
PMID:19680287	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. S2A)
PMID:19680287	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. S2A)
PMID:19680287	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. S2A)
PMID:19680287	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. S2B)
PMID:19680287	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. S2B)
PMID:19680287	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. S2B)
PMID:19680287	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPCC1322.12c	(Fig. S6A,B)
PMID:19680287	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPAC23H3.08c	(Fig. S6C,D)
PMID:19680287	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPAC23H3.08c	(Fig. S6C,D)
PMID:19680287	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 27	(Fig. S7)
PMID:19680287	FYPO:0005720	normal mitotic metaphase chromosome recapture	rarely showed a delay in bi-orienting chromosomes that had been pulled towards one SPB (Fig 3B,D; supplementary Fig S4F online).
PMID:19686686	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Fig. 1e)
PMID:19686686	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Fig. 1e)
PMID:19686686	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Fig. 1e)
PMID:19686686	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Fig. 1e)
PMID:19686686	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Fig. 1e)
PMID:19686686	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Fig. 1e)
PMID:19686686	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Fig. 1e)
PMID:19686686	GO:1990023	mitotic spindle midzone	(Fig. 4a)
PMID:19686686	GO:1990023	mitotic spindle midzone	(Fig. 4a)
PMID:19686686	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPBC15D4.01c	(Fig. 5C)
PMID:19686686	FYPO:0003268	decreased rate of mitotic spindle elongation	(Fig. 5C)
PMID:19686686	FYPO:0003350	abolished protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPAPB1A10.09	(Fig. 5C)
PMID:19686686	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B	(Fig. 5C)
PMID:19686686	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAPB1A10.09 [assayed_using] PomBase:SPBC15D4.01c	(Figure 3D)
PMID:19686686	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAPB1A10.09 [assayed_using] PomBase:SPBC15D4.01c	(Figure 3D)
PMID:19686686	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAPB1A10.09 [assayed_using] PomBase:SPBC15D4.01c	(Figure 3D)
PMID:19686686	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAPB1A10.09 [assayed_using] PomBase:SPBC15D4.01c	(Figure 3D)
PMID:19686686	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAPB1A10.09 [assayed_using] PomBase:SPBC15D4.01c	(Figure 3D)
PMID:19686686	GO:0005515	protein binding [happens_during] mitotic anaphase [part_of] mitotic spindle elongation (spindle phase three)	(comment: CHECK interacts with unmodified Ase1 PR:000027520)
PMID:19686686	GO:0005515	protein binding [happens_during] mitotic anaphase [part_of] mitotic spindle elongation (spindle phase three)	(comment: CHECK interacts with unmodified Klp9 PR:000027705)
PMID:19686686	GO:0005654	nucleoplasm [exists_during] mitotic interphase	(comment: CHECK interphase, prophase, metaphase,anaphase A)
PMID:19686686	GO:0005654	nucleoplasm [exists_during] mitotic prophase	(comment: CHECK interphase, prophase, metaphase,anaphase A)
PMID:19686686	GO:0005654	nucleoplasm [exists_during] mitotic anaphase A	(comment: CHECK interphase, prophase, metaphase,anaphase A)
PMID:19686686	GO:0005654	nucleoplasm [exists_during] mitotic metaphase	(comment: CHECK interphase, prophase, metaphase,anaphase A)
PMID:19686686	GO:1990023	mitotic spindle midzone [exists_during] mitotic anaphase B	(comment: CHECK mitotic anaphase B)
PMID:19686686	GO:1990295	post-anaphase microtubule array [exists_during] mitotic anaphase B	(comment: CHECK mitotic anaphase B, mitotic telophase)
PMID:19686686	GO:1990295	post-anaphase microtubule array [exists_during] mitotic telophase	(comment: CHECK mitotic anaphase B, mitotic telophase)
PMID:19686686	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPAPB1A10.09	(comment: cdc2 dependent phophorylation) (fig. 4B)
PMID:19686686	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPBC15D4.01c	(comment: cdc2 dependent phophorylation) (fig. 5B)
PMID:19686686	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	(comment: with monopolar spindle)
PMID:19693008	FYPO:0003557	increased antisense RNA level [has_severity] medium	(Delta)pht1 caused a disproportionate increase in antisense transcripts at many (,5-8%) euchromatic loci (Fig. 1e-g and Supplementary Fig. 5), as confirmed by PCR with strand-specific reverse transcription (RT-PCR; Fig. 1f).
PMID:19693008	GO:0000791	euchromatin [coincident_with] intergenic_region	At euchromatic loci, H2A.Z localizes preferentially in intergenic regions (Supplementary Fig. 3b)
PMID:19693008	FYPO:0003557	increased antisense RNA level [has_severity] high	Combining Dago1 with Dpht1 resulted in synergistic upregulation of antisense transcripts, as in Dclr4 Dpht1 (Fig. 2a). When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	FYPO:0003557	increased antisense RNA level [has_severity] high	Deletion of exosome subunit rrp6 led to an antisense profile closely resembling that of Dclr4 Dpht1, with read-through antisense RNA covering entire ORFs at convergent genes (Fig. 3b). When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	FYPO:0005071	increased chromatin silencing at centromere	Dpht1 causes a slight increase in silencing at the pericentromeric region, but H3K9me distribution at heterochromatic loci is not severely altered (Supplementary Fig. 4a).
PMID:19693008	FYPO:0006996	normal antisense RNA level [has_severity] medium	However, antisense RNAs did not accumulate extensively in Dswi6 cells and the synergistic increase in antisense RNAs observed in the Dclr4 Dpht1 mutant was not observed in the Dswi6 Dpht1 mutant (Fig. 2a). Thus, ClrC and Ago1 contribute to antisense suppression by a new mechanism(s).
PMID:19693008	FYPO:0003557	increased antisense RNA level [has_severity] high	When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	FYPO:0003557	increased antisense RNA level [has_severity] high	When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	FYPO:0003557	increased antisense RNA level [has_severity] medium	When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	FYPO:0003557	increased antisense RNA level [has_severity] medium	When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	FYPO:0003557	increased antisense RNA level [has_severity] medium	When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	FYPO:0003557	increased antisense RNA level [has_severity] medium	When Dpht1 was combined with mutant alleles of clr4 or rik1—components of the Clr4-containing methyltransferase complex (ClrC)7—the resultant double mutants showed severe growth defects and a large, synergistic increase in antisense RNAs at .20% of genes (Fig. 2a and Supplementary Figs 5 and 7a, b). Consistent with ClrC directly participating in antisense suppression, Rik1 was found at the convergent loci (Supplementary Fig. 7c).
PMID:19693008	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_protein] PomBase:SPBC11B10.10c	affected chromatin association of Swr1, distribution of H2A.Z across the genome (Supplementary Fig. 2c).
PMID:19693008	FYPO:0003557	increased antisense RNA level [has_severity] medium	the synergistic increase in antisense RNAs observed in the Dclr4 Dpht1 mutant was not observed in the Dswi6 Dpht1 mutant (Fig. 2a).
PMID:19696784	FYPO:0000255	increased nuclear protein level during vegetative growth [assayed_using] PomBase:SPAC890.02c	(Fig 3B)
PMID:19696784	FYPO:0004539	short interphase microtubules present in increased numbers [assayed_using] PomBase:SPCC895.07	(Fig 3B)
PMID:19696784	FYPO:0000255	increased nuclear protein level during vegetative growth [assayed_using] PomBase:SPCC895.07	(Fig 3B)
PMID:19696784	FYPO:0006191	decreased protein localization to nucleus, with protein mislocalized to cytoplasm during mitosis [assayed_using] PomBase:SPAC890.02c	(Fig. 1C)
PMID:19696784	FYPO:0006191	decreased protein localization to nucleus, with protein mislocalized to cytoplasm during mitosis [assayed_using] PomBase:SPCC895.07	(Fig. 1C)
PMID:19696784	FYPO:0004419	abolished protein localization to cytoplasm with increased protein localization to nucleus [assayed_using] PomBase:SPAC890.02c	(Fig. 2A,B)
PMID:19696784	FYPO:0005672	decreased protein localization to nucleus during mitosis [assayed_using] PomBase:SPAC890.02c	(Figure 5)
PMID:19696784	FYPO:0006185	decreased protein localization to nucleus during prophase I [assayed_using] PomBase:SPAC890.02c	supplementary Fig S6 online
PMID:19713940	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC4F8.13c	(comment: CONDITION observed after short-duration overexpression)
PMID:19713940	FYPO:0002437	thick actin cables	(comment: CONDITION temperature restrictive for cdc25-22)
PMID:19713940	FYPO:0002437	thick actin cables	(comment: CONDITION temperature restrictive for cdc25-22)
PMID:19713940	FYPO:0002437	thick actin cables	(comment: CONDITION temperature restrictive for cdc25-22)
PMID:19713940	GO:0051015	actin filament binding	(comment: assayed using N-terminal Rng2-Ns fragment or calponin homology domain (CHD) fragment)
PMID:19714215	GO:0003713	transcription coactivator activity [has_input] PomBase:SPAPB8E5.05	A few genes, however, seem to be positively regulated by Yox1p (Figure 3A,B). An example is mfm2 (Figure 3A), encoding a precursor for the M-factor peptide (a mating pheromone) [33], and the neighbouring SPAC513.04, a sequence orphan that is divergently transcribed from mfm2.
PMID:19714215	GO:0003713	transcription coactivator activity [has_input] PomBase:SPAC513.04	A few genes, however, seem to be positively regulated by Yox1p (Figure 3A,B). An example is mfm2 (Figure 3A), encoding a precursor for the M-factor peptide (a mating pheromone) [33], and the neighbouring SPAC513.04, a sequence orphan that is divergently transcribed from mfm2.
PMID:19714215	GO:1990841	promoter-specific chromatin binding [occurs_in] MCB	Among 24 genes proposed to be MBF targets (Figure 1A) [14], the promoters of 19 genes were substantially enriched in the Yox1p ChIPs, including yox1 itself (Figure 1B).
PMID:19714215	GO:0003713	transcription coactivator activity [has_input] PomBase:SPAC11E3.06	Another example is map1, encoding a MADS-box transcription factor involved in the transcriptional response during mating
PMID:19714215	GO:0030907	MBF transcription complex	HA-tagged Yox1p revealed an interaction between Cdc10p and Yox1p (Figure 2A). Moreover, anti-myc immuno complexes prepared from cells expressing Res2p-myc, Yox1p-HA or both showed an interaction between Res2p and Yox1p (Figure 2B) These results are confirmed by independent data from a recent mass spectrometry-based analysis of affinity-purified Res2p and Nrm1p complexes [20]. Based on these mass spectrometry data, Yox1p interacts with both Res2p and Nrm1p, with coverage of Yox1p by specific peptides being similar to the MBF component Cdc10p (data not shown). Together, these data indicate that Yox1p physically associates with the MBF complex and thus represents a new component of MBF.
PMID:19714215	GO:1990841	promoter-specific chromatin binding [occurs_in] MCB	MBF, we performed ChIP-chip using an antibody against the MBF component Cdc10p. As for Yox1p, among the 24 proposed MBF targets, the promoters of the same 19 genes, including cdc10 itself and yox1, were substantially enriched in the Cdc10p ChIPs (Figure 1C)
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC21B10.13c	Taken together, these data show that yox1 is transcriptionally activated by MBF, and Yox1p in turn binds itself to MBF target genes.
PMID:19714215	GO:0003714	transcription corepressor activity [happens_during] mitotic G2 phase [has_input] PomBase:SPBC336.12c	Taken together, we conclude that cell-cycle regulated transcription of Yox1p/Cdc10p target genes is highly deficient in yox1D cells, reflecting that these genes are no longer down-regulated after S-phase.
PMID:19714215	GO:0003714	transcription corepressor activity [happens_during] mitotic M phase [has_input] PomBase:SPBC336.12c	Taken together, we conclude that cell-cycle regulated transcription of Yox1p/Cdc10p target genes is highly deficient in yox1D cells, reflecting that these genes are no longer down-regulated after S-phase.
PMID:19714215	FYPO:0000239	increased transcription from MCB promoter [assayed_transcript] PomBase:SPAC1F7.05	The Yox1p/Cdc10p target genes showed consistently higher Pol II occupancy in yox1D than in wild-type cells (Figure 3C,D)
PMID:19714215	FYPO:0005301	increased level of cell cycle regulated gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1F7.05	The cell cycle-regulated target genes bound by both Yox1p and Cdc10p tended to be more highly expressed in yox1D than in wild-type cells (Figure 3A,B). In yox1D cells, on the other hand, the Yox1p/Cdc10p targets showed little or no cell-cycle regulation, whereas the cell-cycle regulation of Ace2p targets was not affected (Figure 4A).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1F7.06	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC1442.01	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC660.13c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC144.13c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC887.14c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC644.14c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC338.17c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC17H9.20	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC3H5.06c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC11B10.10c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCPB1C11.02	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAP14E8.02	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC660.14	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC513.03	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC622.09	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC550.13	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAPB2B4.03	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC17H9.19c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC428.18	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1F7.05	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC14C8.07c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC336.12c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC70.08c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC694.06c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC644.05c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC63.14	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC63.13	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC553.07c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC513.05	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1306.02	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC3B9.01	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC336.13c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC290.04	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC16A3.07c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1347.01c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1306.01c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC110.02	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAP14E8.03	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC17H9.18c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC338.08	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC622.08c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC25D12.04	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1778.04	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC14C8.06	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC644.15	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC14C8.12	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1F7.04	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC110.04c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAP8A3.03	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPNCRNA.93	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC14C8.05c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC119.04	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC25D12.03c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC11E3.06	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC22H10.12c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1347.02	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC70.10	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC70.09c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC660.15	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC660.12c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC63.12c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC513.04	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC513.02	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC428.17c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC338.18	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC336.14c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC32C12.03c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC290.03c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1F7.01c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC17H9.17c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1778.03c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC14C8.11c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC14C8.10	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC14C8.09c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC1450.16c	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC11E3.07	The promoters of 76 genes were substantially and consistently enriched in both Cdc10p and Yox1p ChIPs, including the 19 previously discussed MBF target genes (Fig 5A,B; Table S3).
PMID:19714215	FYPO:0000650	increased septation index [has_severity] low	The septation index was marginally higher in yox1D compared to wild-type cells (10.4% vs 9.4%), suggesting a slight delay in cytokinesis and/or cell separation.
PMID:19714215	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	The yox1D cells were about 14% longer on average than wild-type cells during septation (17.4 mm vs 15.3 mm) (Figure 4C).
PMID:19714215	FYPO:0006349	abolished protein localization to chromatin at promoter [assayed_protein] PomBase:SPBC21B10.13c [assayed_region] PomBase:SPAC1F7.05	This analysis revealed that Yox1p binding to the cdc22 promoter depends on both of the MBF components tested, Res2p and Nrm1p (Figure 2C). We conclude that Yox1p can bind to MBF- regulated promoters only via intact MBF.
PMID:19714215	FYPO:0006349	abolished protein localization to chromatin at promoter [assayed_protein] PomBase:SPBC21B10.13c [assayed_region] PomBase:SPAC1F7.05	This analysis revealed that Yox1p binding to the cdc22 promoter depends on both of the MBF components tested, Res2p and Nrm1p (Figure 2C). We conclude that Yox1p can bind to MBF- regulated promoters only via intact MBF.
PMID:19714215	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC144.14	kinesin-like protein, which was bound by both Yox1p and Cdc10p and induced in yox1D cells, suggesting that klp8 is regulated by both Ace2p and MBF.
PMID:19714215	PomGeneEx:0000018	protein level increased [during] mitotic S phase	the Yox1p levels were low during M/G1-phase but then strongly increased during S-phase (Figure 2D, top), peaking about 40 minutes after the peak of yox1 mRNA levels.
PMID:19714215	FYPO:0001357	normal vegetative cell population growth	yox1D cells were viable and did not show any overall growth defect (Figure 4B).
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 1A)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 1A)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 1A)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 1A)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 1A)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 1A)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 1A)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 1A)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 1A)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 1A)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 1A)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 1A)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 1A)
PMID:19723888	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1C)
PMID:19723888	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1C)
PMID:19723888	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1C)
PMID:19723888	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1C)
PMID:19723888	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1C)
PMID:19723888	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1C)
PMID:19723888	FYPO:0000274	increased duration of mitotic M phase [has_severity] high	(Fig. 1C)
PMID:19723888	FYPO:0000274	increased duration of mitotic M phase [has_severity] high	(Fig. 1C)
PMID:19723888	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1C)
PMID:19723888	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1C,D)
PMID:19723888	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1D)
PMID:19723888	FYPO:0000274	increased duration of mitotic M phase [has_severity] medium	(Fig. 1D)
PMID:19723888	FYPO:0000274	increased duration of mitotic M phase [has_severity] medium	(Fig. 1D)
PMID:19723888	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPCC1259.13	(Fig. 2)
PMID:19723888	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPCC1259.13	(Fig. 2)
PMID:19723888	FYPO:0000650	increased septation index [has_severity] high	(Fig. 2A III)
PMID:19723888	FYPO:0001903	normal septation index	(Fig. 2A III)
PMID:19723888	FYPO:0001903	normal septation index	(Fig. 2A III)
PMID:19723888	FYPO:0000650	increased septation index	(Fig. 2A III)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(Figure 1B)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Figure 1B)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(Figure 1B)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Figure 1B)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Figure 1B)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Figure 1B)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Figure 1B)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Figure 1B)
PMID:19723888	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Figure 1B)
PMID:19723888	FYPO:0001903	normal septation index	(Figure 2B)
PMID:19736319	GO:0005737	cytoplasm [exists_during] mitotic telophase	(Fig. 4B)
PMID:19736319	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	(Fig. 4B)
PMID:19736319	FYPO:0007582	increased duration of septation initiation network signaling [assayed_using] PomBase:SPAC1565.06c [has_penetrance] high	(Fig. 4D)
PMID:19736319	FYPO:0005369	abolished cell population growth at low temperature	(Fig. S1B)
PMID:19736319	FYPO:0001493	inviable elongated multinucleate vegetative cell	(Fig. S1C)
PMID:19736319	FYPO:0007583	decreased protein localization to cytoplasm during mitotic telophase [assayed_using] PomBase:SPAC1006.08 [has_severity] high	(comment: CHECK 2%) fig 6a
PMID:19736319	FYPO:0001875	decreased asymmetric protein localization, with protein localized to both mitotic spindle pole bodies [assayed_using] PomBase:SPAC1006.08 [has_severity] high	(comment: CHECK 2%) fig 6a. (comment: to dauughter)
PMID:19736319	FYPO:0002000	inviable septated mononucleate vegetative cell	(comment: CHECL add to def, septated in interphase. one compartment is anucleate)
PMID:19736319	FYPO:0005055	binucleate multiseptate cell, septa grouped	(comment: arrested normal size (multiple rounds of cytokinesis) in interphase)
PMID:19758558	FYPO:0001269	abolished protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPBC1861.01c	(Fig. S3D)
PMID:19798055	FYPO:0005452	increased break-induced loss of heterozygosity	(comment: decreased overall)
PMID:19804755	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPCC338.08 [occurs_in] site of double-strand break [part_of] double-strand break repair	(comment: ctp-Phosphorylated)
PMID:19804755	MOD:01455	O-phosphorylated residue	(comment: residues include one or more of S77, T78, T79, S87, and T89, and others)
PMID:19879140	GO:0008017	microtubule binding	(comment: Biochemistry)
PMID:19879140	FYPO:0001944	abolished microtubule binding	(comment: MT spindown assay)
PMID:19879140	FYPO:0006725	normal microtubule binding	(comment: MT spindown assay.)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	GO:0000812	Swr1 complex	(Figure 2b)
PMID:19915592	FYPO:0002061	inviable vegetative cell population	(comment: CHECK lethal >34°C) (Fig. 1c).
PMID:19915592	FYPO:0000283	mitotic chromosome fragmentation upon segregation	(iii) entanglement leading to breakage, where broken pieces of chromatin with no kinetochore lag on the spindle (Fig. 4b).
PMID:19915592	FYPO:0006372	incomplete meiotic chromosome segregation, with chromosomal bridge	(iii) entanglement leading to breakage, where broken pieces of chromatin with no kinetochore lag on the spindle (Fig. 4b).
PMID:19915592	GO:0000785	chromatin	Cell fractionation showed that Pht1Ac is chromatin-associated, though acetylation is not required for entry to this cellular compartment (Figs. 1e-f)
PMID:19915592	FYPO:0000227	chromosome loss during mitotic chromosome segregation	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0000227	chromosome loss during mitotic chromosome segregation	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0000227	chromosome loss during mitotic chromosome segregation	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0000227	chromosome loss during mitotic chromosome segregation	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0000227	chromosome loss during mitotic chromosome segregation	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0000227	chromosome loss during mitotic chromosome segregation	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0000227	chromosome loss during mitotic chromosome segregation	Knockout or depletion of H2A.Z in Sc 15 or mammalian cells 5 leads to increased rates of chromosome loss. This phenotype was also observed if any component of the Sp Pht1Ac pathway is disrupted, including mutants in swr1 (and msc1), pht1 (pht1Δ, −4KR or −4KQ), or mst1 (Supplementary Table 2 and 16,25,26).
PMID:19915592	FYPO:0001355	decreased vegetative cell population growth	This partial rescue was specific, as pht1Δ was synthetic with rad21-K1, a mutant in the condensin-related complex cohesin, which holds sister-chromatids together prior to anaphase onset.
PMID:19915592	FYPO:0001355	decreased vegetative cell population growth	This partial rescue was specific, as pht1Δ was synthetic with rad21-K1, a mutant in the condensin-related complex cohesin, which holds sister-chromatids together prior to anaphase onset.
PMID:19915592	GO:0140849	ATP-dependent H2AZ histone chaperone activity [has_input] PomBase:SPBC11B10.10c	p SWR-C required for the efficient acetylation of the histone (Fig. 2b), most likely because of inefficient assembly of the variant into chromatin in each background (Fig. 2c). Thus a pathway first identified in Sc also operates in Sp: SWR-C inserts Pht1 into chromatin, where it is acetylated by Mst1.
PMID:19915592	FYPO:0000331	decreased histone acetylation during vegetative growth [assayed_using] PomBase:SPBC11B10.10c	reduction in Pht1Ac (Fig. 1d), indicating that Pht1 acetylation is Mst1-dependent.
PMID:19933844	GO:0140861	DNA repair-dependent chromatin remodeling	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0045815	transcription initiation-coupled chromatin remodeling	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0045815	transcription initiation-coupled chromatin remodeling	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0045815	transcription initiation-coupled chromatin remodeling	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0045815	transcription initiation-coupled chromatin remodeling	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0140861	DNA repair-dependent chromatin remodeling	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0140861	DNA repair-dependent chromatin remodeling	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19933844	GO:0140861	DNA repair-dependent chromatin remodeling	Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism.
PMID:19942659	GO:0003978	UDP-glucose 4-epimerase activity	(comment: major)
PMID:19942659	GO:0003978	UDP-glucose 4-epimerase activity [happens_during] cellular response to glucose starvation	(comment: minor)
PMID:19942659	FYPO:0003728	abolished protein galactosylation during vegetative growth	Like the gms1D mutant, neither the uge1D strain nor the uge1Dgal10D strain reacted with PNA (Fig. 2b
PMID:19942852	FYPO:0002061	inviable vegetative cell population	(Fig. 1)
PMID:19942852	FYPO:0001489	inviable vegetative cell [has_penetrance] high	(Fig. 1)
PMID:19942852	FYPO:0001489	inviable vegetative cell [has_penetrance] high	(Fig. 1)
PMID:19942852	FYPO:0002061	inviable vegetative cell population	(Fig. 1)
PMID:19942852	FYPO:0005380	normal mitotic spindle pole body duplication	(Fig. 1D)
PMID:19942852	FYPO:0005380	normal mitotic spindle pole body duplication	(Fig. 1D)
PMID:19942852	FYPO:0006593	decreased mitotic spindle microtubule nucleation from spindle pole body	(Fig. 1D)
PMID:19942852	FYPO:0006593	decreased mitotic spindle microtubule nucleation from spindle pole body	(Fig. 1D)
PMID:19942852	FYPO:0000274	increased duration of mitotic M phase	(Fig. 1D)
PMID:19942852	FYPO:0000274	increased duration of mitotic M phase	(Fig. 1D)
PMID:19942852	FYPO:0006173	abolished mitotic spindle elongation during prophase [has_penetrance] 80	(Fig. 1D)
PMID:19942852	FYPO:0006173	abolished mitotic spindle elongation during prophase [has_penetrance] 80	(Fig. 1D)
PMID:19942852	FYPO:0005029	decreased gamma-tubulin complex localization to mitotic spindle pole body [has_penetrance] 80 [assayed_using] PomBase:SPBC428.20c [has_severity] high	(Fig. 3)
PMID:19942852	FYPO:0006594	normal gamma-tubulin complex localization to mitotic spindle pole body [has_penetrance] 80 [assayed_using] PomBase:SPBC428.20c [has_severity] high	(Fig. 3)
PMID:19942852	FYPO:0005029	decreased gamma-tubulin complex localization to mitotic spindle pole body [has_penetrance] 80 [assayed_using] PomBase:SPBC365.15 [has_severity] high	(Fig. 3)
PMID:19942852	FYPO:0005612	normal protein localization to nuclear envelope [assayed_using] PomBase:SPBC649.05	(Fig. 6a)
PMID:19942852	FYPO:0005612	normal protein localization to nuclear envelope [assayed_using] PomBase:SPAC1786.03	(Fig. 6a)
PMID:19942852	FYPO:0006592	monopolar mitotic spindle nucleated from old spindle pole body [has_penetrance] 80	(Fig. S2, 3)
PMID:19942852	FYPO:0006592	monopolar mitotic spindle nucleated from old spindle pole body [has_penetrance] 80	(Fig. S2, 3)
PMID:19948483	FYPO:0004382	meroterically attached lagging mitotic chromosomes [has_penetrance] 22	(Fig. 3)
PMID:19948483	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:19948483	FYPO:0005045	abnormal mitotic sister chromatid segregation with lagging chromosomes and decreased rate of mitotic spindle elongation	(Fig. 3)
PMID:19948483	FYPO:0008007	mitotic spindle collapse during anaphase B elongation with progressive spindle pole congression	(Fig. 3)
PMID:19948484	GO:0005637	nuclear inner membrane [exists_during] mitotic cell cycle phase	(comment: they say periphery in the text but it has TM domains)
PMID:19948484	GO:0005637	nuclear inner membrane [exists_during] meiotic cell cycle phase	(comment: they say periphery in the text but it has TM domains)
PMID:19965387	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 2C)
PMID:19965387	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 2C)
PMID:19965387	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 2C)
PMID:19965387	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 2C)
PMID:19965387	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Fig. 2E)
PMID:19965387	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Fig. 2E)
PMID:19965387	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Fig. 2E)
PMID:19965387	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Fig. 2E)
PMID:19965387	FYPO:0003182	sister chromatid nondisjunction at meiosis II	(Fig. 2F)
PMID:19965387	FYPO:0003182	sister chromatid nondisjunction at meiosis II	(Fig. 2F)
PMID:19965387	FYPO:0003182	sister chromatid nondisjunction at meiosis II	(Fig. 2F)
PMID:19965387	FYPO:0003182	sister chromatid nondisjunction at meiosis II	(Fig. 2F)
PMID:19965387	FYPO:0006455	abolished protein localization to meiotic spindle during meiosis I [assayed_using] PomBase:SPBP35G2.03c	(Fig. 3A)
PMID:19965387	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_using] PomBase:SPAC15A10.15	(Fig. 3A)
PMID:19965387	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_using] PomBase:SPAC15A10.15	(Fig. 3A)
PMID:19965387	FYPO:0006455	abolished protein localization to meiotic spindle during meiosis I [assayed_using] PomBase:SPBP35G2.03c	(Fig. 3A)
PMID:19965387	FYPO:0006455	abolished protein localization to meiotic spindle during meiosis I [assayed_using] PomBase:SPAC15A10.15	(Fig. 3A)
PMID:19965387	FYPO:0006456	abolished protein localization to meiotic spindle during meiosis II [assayed_using] PomBase:SPAC15A10.15	(Fig. 3A)
PMID:19965387	FYPO:0006456	abolished protein localization to meiotic spindle during meiosis II [assayed_using] PomBase:SPBC29A10.14	(Fig. 3A)
PMID:19965387	FYPO:0006455	abolished protein localization to meiotic spindle during meiosis I [assayed_using] PomBase:SPAC15A10.15	(Fig. 3A)
PMID:19965387	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_using] PomBase:SPAC15A10.15	(Fig. 3A)
PMID:19965387	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_using] PomBase:SPAC15A10.15	(Fig. 3A)
PMID:19965387	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_using] PomBase:SPAC15A10.15	(Fig. 3A)
PMID:19965387	FYPO:0001093	abolished chromatin binding [assayed_using] PomBase:SPBP35G2.03c	(Fig. 4G)
PMID:19965387	FYPO:0001093	abolished chromatin binding [assayed_using] PomBase:SPBP35G2.03c	(Fig. 4G)
PMID:19965387	FYPO:0002577	decreased chromatin binding [assayed_using] PomBase:SPBP35G2.03c	(Fig. 4G)
PMID:19965387	FYPO:0001093	abolished chromatin binding [assayed_using] PomBase:SPBP35G2.03c	(Fig. 4G)
PMID:19965387	GO:0099115	chromosome, subtelomeric region [exists_during] mitotic G2 phase	(Fig. 4c)
PMID:19965387	GO:0005721	pericentric heterochromatin [exists_during] mitotic M phase	(Fig. 4c)
PMID:19965387	FYPO:0006423	decreased meiotic sister chromatid cohesion at centromere during meiosis I	(Fig. S3)
PMID:19965387	FYPO:0006423	decreased meiotic sister chromatid cohesion at centromere during meiosis I	(Fig. S3)
PMID:19965387	FYPO:0006456	abolished protein localization to meiotic spindle during meiosis II [assayed_using] PomBase:SPBC29A10.14	(Fig. S3)
PMID:19965387	FYPO:0006456	abolished protein localization to meiotic spindle during meiosis II [assayed_using] PomBase:SPBC29A10.14	(Fig. S3)
PMID:19965387	FYPO:0006423	decreased meiotic sister chromatid cohesion at centromere during meiosis I	(Fig. S3)
PMID:19965387	FYPO:0006423	decreased meiotic sister chromatid cohesion at centromere during meiosis I	(Fig. S3)
PMID:19965387	FYPO:0006456	abolished protein localization to meiotic spindle during meiosis II [assayed_using] PomBase:SPAC15A10.15	(Fig. S5)
PMID:19965387	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_using] PomBase:SPCC320.13c	(Fig. S6)
PMID:19965387	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_using] PomBase:SPCC320.13c	(Fig. S6)
PMID:19965387	FYPO:0006455	abolished protein localization to meiotic spindle during meiosis I [assayed_using] PomBase:SPCC188.02	(Fig. S6)
PMID:19965387	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_using] PomBase:SPCC320.13c	(Fig. S6)
PMID:19965387	FYPO:0006455	abolished protein localization to meiotic spindle during meiosis I [assayed_using] PomBase:SPCC188.02	(Fig. S6)
PMID:19965387	FYPO:0006455	abolished protein localization to meiotic spindle during meiosis I [assayed_using] PomBase:SPCC188.02	(Fig. S6)
PMID:19965387	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_using] PomBase:SPCC320.13c	(Fig. S6)
PMID:19965387	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_enzyme] PomBase:SPCC1322.12c [assayed_substrate] PomBase:SPCC622.08c [assayed_substrate] PomBase:SPAC19G12.06c	(comment: CHECK H2A-S121) phosphorylation was completely abolished in bub1-KD cells, although a similar amount of H2A was detected (Fig. 1G).
PMID:19965387	GO:0072371	histone H2AS121 kinase activity [has_input] PomBase:SPCC622.08c [part_of] homologous chromosome segregation [happens_during] meiosis I cell cycle phase	(comment: GO:0072371 obsolete histone H2AS121 kinase activity)
PMID:19965387	GO:0072371	histone H2AS121 kinase activity [has_input] PomBase:SPAC19G12.06c [part_of] homologous chromosome segregation [happens_during] meiosis I cell cycle phase	(comment: GO:0072371 obsolete histone H2AS121 kinase activity)
PMID:19965387	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC19G12.06c	This signal was abolished in cell extracts prepared from h2a-SA cells, in which Ser 121 is replaced with alanine (H2A-S121A) in both the hta1+ and hta2+ genes (Fig. 1G).
PMID:19965387	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC622.08c	This signal was abolished in cell extracts prepared from h2a-SA cells, in which Ser 121 is replaced with alanine (H2A-S121A) in both the hta1+ and hta2+ genes (Fig. 1G).
PMID:19965387	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPBP35G2.03c [occurs_in] inner kinetochore [part_of] homologous chromosome segregation [happens_during] meiosis I cell cycle phase	fusion experiments (Figure 3)
PMID:19965387	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPBP35G2.03c [occurs_in] inner kinetochore [part_of] homologous chromosome segregation [happens_during] meiosis I cell cycle phase	fusion experiments (Figure 3)
PMID:19965387	GO:0140463	chromatin-protein adaptor activity [occurs_in] inner kinetochore [has_input] PomBase:SPAC15A10.15 [part_of] homologous chromosome segregation [happens_during] meiosis I cell cycle phase	fusion experiments (Figure 3)
PMID:19965387	GO:0140463	chromatin-protein adaptor activity [occurs_in] inner kinetochore [has_input] PomBase:SPAC15A10.15 [part_of] homologous chromosome segregation [happens_during] meiosis I cell cycle phase	fusion experiments (Figure 3)
PMID:20062003	FYPO:0006076	siRNA absent from cell	(Fig. 2D)
PMID:20062003	FYPO:0007010	secondary siRNA absent from cell	(Fig. 3)
PMID:20062003	FYPO:0007009	decreased heterochromatin assembly by small RNA	(Fig. 4)
PMID:20062003	FYPO:0007009	decreased heterochromatin assembly by small RNA	(Fig. 4)
PMID:20062003	FYPO:0007009	decreased heterochromatin assembly by small RNA	(Fig. 4)
PMID:20062003	FYPO:0007009	decreased heterochromatin assembly by small RNA	(Fig. 4)
PMID:20062003	FYPO:0007009	decreased heterochromatin assembly by small RNA	(Fig. 4)
PMID:20062003	FYPO:0007009	decreased heterochromatin assembly by small RNA	(Fig. 4)
PMID:20062003	FYPO:0007009	decreased heterochromatin assembly by small RNA	(Fig. S1)
PMID:20062003	FYPO:0007009	decreased heterochromatin assembly by small RNA	(Fig. S1)
PMID:20062003	FYPO:0007009	decreased heterochromatin assembly by small RNA	(Fig. S1)
PMID:20075862	FYPO:0001408	sensitive to heat shock	(Figure 3a left panel)
PMID:20089861	FYPO:0008054	decreased homocitrate synthase inhibition by L-lysine	Indeed, the R288K and Q364R mutations in SpHCS confer diminished sensitivity to feedback inhibition by L-lysine in vitro and in vivo (Table 2 and Fig. 4)
PMID:20089861	FYPO:0008054	decreased homocitrate synthase inhibition by L-lysine	Indeed, the R288K and Q364R mutations in SpHCS confer diminished sensitivity to feedback inhibition by L-lysine in vitro and in vivo (Table 2 and Fig. 4)
PMID:20094029	GO:0005634	nucleus	(comment: Forms gamma H2A dependent nuclear foci when over-expressed)
PMID:20110347	FYPO:0004895	normal rate of actomyosin contractile ring contraction	(comment: CONDITION 25 degrees)
PMID:20110347	FYPO:0004430	premature actomyosin contractile ring contraction	(comment: CONDITION 25 degrees)
PMID:20110347	FYPO:0003339	decreased rate of actomyosin contractile ring assembly	(comment: CONDITION 25 degrees)
PMID:20110347	FYPO:0001357	normal vegetative cell population growth	(comment: CONDITION 25 degrees)
PMID:20110347	FYPO:0001355	decreased vegetative cell population growth	(comment: CONDITION 25 or 32 degrees; latter semi-permissive for cdc8-27 alone)
PMID:20110347	FYPO:0001253	elongated multinucleate multiseptate vegetative cell, single septa between nuclei [has_penetrance] 60	(comment: CONDITION 32 degrees)
PMID:20110347	FYPO:0001355	decreased vegetative cell population growth	(comment: CONDITION 32 degrees)
PMID:20110347	FYPO:0004895	normal rate of actomyosin contractile ring contraction	(comment: CONDITION 32 degrees)
PMID:20110347	FYPO:0000133	elongated multinucleate vegetative cell [has_penetrance] 5	(comment: CONDITION 32 degrees; semi-permissive for cdc8-27 alone)
PMID:20118936	FYPO:0008341	decreased nucleosome occupancy in gene body	(Fig. 5)
PMID:20123974	FYPO:0000487	increased meiotic recombination	(comment: increased unequal sister chromatid recombination)
PMID:20123974	FYPO:0000487	increased meiotic recombination	(comment: increased unequal sister chromatid recombination)
PMID:20123974	FYPO:0000487	increased meiotic recombination	(comment: increased unequal sister chromatid recombination)
PMID:20123974	FYPO:0000485	decreased meiotic recombination	also ctp1,rec12,rad22,rti1,rad51,dmc1 (comment: increased unequal sister chromatid recombination)
PMID:20129053	FYPO:0003701	poly(A)+ RNA-containing focus present in nucleus	snoRNAs with extended poly(A) tails accumulate in these foci
PMID:20129053	FYPO:0003701	poly(A)+ RNA-containing focus present in nucleus	snoRNAs with extended poly(A) tails accumulate in these foci
PMID:20130084	FYPO:0001915	abolished prospore membrane formation [assayed_enzyme] PomBase:SPCC1183.12	. Growing FSMs were observed adjacent to each of the SPBs in 100% of the cells expressing wild-type Spspo13+ (n = 20), but no FSMs were formed in cells expressing Spspo13-F79A (Figure 7) (n = 20). The GEF activity of SpSpo13 is therefore required for FSM assembly in S. pombe.
PMID:20130084	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPAC9E9.07c	A 6XHis-tagged version of SpYpt2 was purified from E. coli, and the ability of SpSpo13 to stimulate GDP release was examined (Figure 8A). Similar to what was observed with ScSec4 as a substrate (Figure 4B), SpSpo13 stimulated GDP release, although not as efficiently as Sc- Sec2. Thus, SpSpo13 can act on SpYpt2.
PMID:20130084	GO:0003924	GTPase activity	A 6XHis-tagged version of SpYpt2 was purified from E. coli, and the ability of SpSpo13 to stimulate GDP release was examined (Figure 8A). Similar to what was observed with ScSec4 as a substrate (Figure 4B), SpSpo13 stimulated GDP release, although not as efficiently as Sc- Sec2. Thus, SpSpo13 can act on SpYpt2.
PMID:20130084	GO:0035974	meiotic spindle pole body [exists_during] meiosis I cell cycle phase	Spo13-mRFP was visible at the SPB, beginning with cells in meiosis I and persisted at the SPB throughout meiosis II, as reported previously (Nakase et al., 2008; Figure 6B).
PMID:20130084	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	Spo13-mRFP was visible at the SPB, beginning with cells in meiosis I and persisted at the SPB throughout meiosis II, as reported previously (Nakase et al., 2008; Figure 6B).
PMID:20130084	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_enzyme] PomBase:SPCC1183.12	The localization of SpSpo13F79A-mRFP was indistinguishable from the wild-type protein (Figure 6C), indicating that the mutant protein is expressed and properly localized.
PMID:20130084	FYPO:0008290	abolished guanyl-nucleotide exchange factor activity [assayed_enzyme] PomBase:SPCC1183.12	The pull-down assay revealed that GST- SpSpo13F79A still bound to the nucleotide-free form of ScSec4 but at a lower level than wild-type GST-SpSpo13 (Figure 5A). In the GEF assay, adding GST-SpSpo13F79A did not stimulate mant-GDP dissociation, indicating that the mutant protein has lost GEF activity in vitro (Figure 5B).
PMID:20140190	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPBC216.05	(comment: CHECK full-length Rad3 or Rad3-kd-delta)
PMID:20140190	FYPO:0003109	abolished protein localization to telomere during vegetative growth [assayed_using] PomBase:SPBC216.05	(comment: full-length Rad3 or Rad3-kd-delta)
PMID:20140190	FYPO:0004656	increased protein localization to telomere during vegetative growth [assayed_using] PomBase:SPBC6B1.09c	(comment: same as nbs1-c60-delta alone)
PMID:20140190	FYPO:0004656	increased protein localization to telomere during vegetative growth [assayed_using] PomBase:SPBC6B1.09c	(comment: same as nbs1-c60-delta alone)
PMID:20164182	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20164182	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: unstressed cells)
PMID:20178743	FYPO:0006076	siRNA absent from cell	(Fig. 1B and C)
PMID:20178743	FYPO:0004205	decreased siRNA level [has_severity] high	(Fig. 1B and C)
PMID:20178743	FYPO:0004205	decreased siRNA level [has_severity] high	(Fig. 1B and C)
PMID:20178743	FYPO:0006076	siRNA absent from cell	(Fig. 1B and C)
PMID:20178743	FYPO:0006076	siRNA absent from cell	(Fig. 1B and C)
PMID:20178743	FYPO:0006076	siRNA absent from cell	(Fig. 1B and C)
PMID:20178743	FYPO:0004205	decreased siRNA level [has_severity] low	(Fig. 1B and C)
PMID:20178743	FYPO:0004205	decreased siRNA level [has_severity] medium	(Fig. 1B and C)
PMID:20178743	FYPO:0004205	decreased siRNA level [has_severity] high	(Fig. 1B and C)
PMID:20178743	FYPO:0004205	decreased siRNA level [has_severity] high	(Fig. 1B and C)
PMID:20178743	FYPO:0004205	decreased siRNA level [has_severity] high	(Fig. 1B and C)
PMID:20178743	FYPO:0004205	decreased siRNA level [has_severity] high	(Fig. 1B and C)
PMID:20178743	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	(Fig. 2A and B)
PMID:20178743	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	(Fig. 2A and B)
PMID:20178743	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] high	(Fig. 2A and B)
PMID:20178743	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	(Fig. 2C)
PMID:20178743	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	(Fig. 2C)
PMID:20178743	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] high	(Fig. 3A and B)
PMID:20178743	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] medium	(Fig. 3A and B)
PMID:20178743	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] high	(Fig. 3A and B)
PMID:20178743	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] medium	(Fig. 3B)
PMID:20178743	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] medium	(Fig. 3B)
PMID:20178743	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level	(Fig. 3C)
PMID:20178743	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. 4I)
PMID:20178743	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. 4I)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 5 and Fig. S5)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 5 and Fig. S5)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 5 and Fig. S5)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 5C and E)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 5C and E)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 5C and E)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] low	(Fig. 5C and E)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 5D)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] low	(Fig. 5E)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 5E)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 5E)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] low	(Fig. 5E)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] low	(Fig. 5G and Fig. S5B)
PMID:20178743	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] low	(Fig. 5G and Fig. S5B)
PMID:20178743	FYPO:0003093	increased Argonaute-associated RNA length	(Fig. 6B, D and E)
PMID:20178743	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] low	(Fig. S2D)
PMID:20178743	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] low	(Fig. S2D)
PMID:20178743	GO:1990817	poly(A) RNA polymerase activity	Cid12 had robust adenylation activity when assembled into the RDRC complex, containing either wild-type Rdp1 or catalytically inactive Rdp1D903A (Figure 2G, lanes 1, 3, and 4), suggesting that Cid12 activity was allosterically regulated.
PMID:20178743	GO:1990431	priRNA 3'-end processing	we provide evidence that siRNAs undergo processing at their 3'ends, which involves the addition of untemplated nucleotides by the Cid12 and Cid14 nucleotidyltransferases
PMID:20178743	GO:1990431	priRNA 3'-end processing	we provide evidence that siRNAs undergo processing at their 3'ends, which involves the addition of untemplated nucleotides by the Cid12 and Cid14 nucleotidyltransferases
PMID:20211136	FYPO:0004170	abolished histone H3-K9 dimethylation at centromere during vegetative growth	(comment: abolished at exogenous RNA polII transcribed gene)
PMID:20211136	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(comment: endogenous ade6)
PMID:20211136	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPCC736.11	(comment: not sure which clrc subunit it binds to?)
PMID:20211136	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] low	(comment: this is the endogenous dg repeat)
PMID:20226666	FYPO:0007743	premature septum assembly during mitotic interphase [has_penetrance] 34.1	(Figure 1)
PMID:20226666	FYPO:0007742	premature actomyosin contractile ring assembly during mitotic interphase [has_penetrance] 90.2	(Figure 1)
PMID:20226666	FYPO:0007664	mononucleate monoseptate vegetative cell with anucleate compartment	(Figure 1) (comment: CHECK in interphase)
PMID:20226666	FYPO:0000229	cut	(Figure 1) (comment: CHECK in interphase)
PMID:20230746	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC290.04	(comment: involved in negative regulation of transcription via transcription factor catabolism)
PMID:20299449	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] medium	(Fig. 1B and C)
PMID:20299449	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] medium	(Fig. 1B and C)
PMID:20299449	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. 1B,C)
PMID:20299449	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] low	(Fig. 1C)
PMID:20299449	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	(Fig. 1E)
PMID:20299449	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	(Fig. 1E)
PMID:20299449	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	(Fig. 1E)
PMID:20299449	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	(Fig. 1E)
PMID:20299449	FYPO:0004237	increased protein localization to heterochromatin at centromere outer repeat region [assayed_using] PomBase:SPBC28F2.12 [has_severity] high	(Fig. 1F)
PMID:20299449	FYPO:0004237	increased protein localization to heterochromatin at centromere outer repeat region [assayed_using] PomBase:SPBC28F2.12 [has_severity] medium	(Fig. 1F)
PMID:20299449	FYPO:0004237	increased protein localization to heterochromatin at centromere outer repeat region [assayed_using] PomBase:SPBC28F2.12 [has_severity] high	(Fig. 1F)
PMID:20299449	FYPO:0004237	increased protein localization to heterochromatin at centromere outer repeat region [assayed_using] PomBase:SPBC28F2.12 [has_severity] high	(Fig. 1F)
PMID:20299449	FYPO:0000892	increased histone H3-K9 acetylation during vegetative growth	(Fig. 2A)
PMID:20299449	FYPO:0004238	increased histone H3-K4 acetylation during vegetative growth	(Fig. 2A)
PMID:20299449	FYPO:0001442	decreased histone H3-K9 acetylation during vegetative growth	(Fig. 2A)
PMID:20299449	FYPO:0004240	decreased histone H3-K56 acetylation during vegetative growth	(Fig. 2A)
PMID:20299449	FYPO:0008270	increased H3-K56 acetylation during vegetative growth	(Fig. 2A)
PMID:20299449	FYPO:0004239	decreased histone H3-K4 acetylation during vegetative growth	(Fig. 2B)
PMID:20299449	FYPO:0003235	normal histone H3-K9 methylation at centromere outer repeat during vegetative growth	(Fig. 4A)
PMID:20299449	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_protein] PomBase:SPCC338.17c	(Fig. 4B)
PMID:20299449	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPBC800.03 [has_severity] low	(Fig. 4C)
PMID:20299449	FYPO:0004237	increased protein localization to heterochromatin at centromere outer repeat region [has_severity] medium [assayed_protein] PomBase:SPAC18G6.02c	(Fig. 4D)
PMID:20299449	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] low [assayed_protein] PomBase:SPAC664.01c	(Fig. 4E)
PMID:20299449	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] medium [assayed_protein] PomBase:SPBC16C6.10	(Fig. 4F)
PMID:20299449	MOD:00723	N-acetylated L-lysine	(comment: IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT)
PMID:20299449	MOD:00723	N-acetylated L-lysine [added_during] mitotic S phase	(comment: IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT)
PMID:20299449	MOD:00723	N-acetylated L-lysine [added_during] mitotic S phase	(comment: IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT)
PMID:20299449	MOD:00723	N-acetylated L-lysine [added_by] PomBase:SPAC637.12c	(comment: IMP evidence for sir2 being the major HDAC, IDA for mst1 being HAT)
PMID:20299449	GO:0141222	histone H3K4 deacetylase activity, NAD-dependent	Taken together, these results show that H3K4ac exists in S. pombe, and that Mst1 and the sirtuin Sir2 are the major HAT and HDAC, respectively, for H3K4.
PMID:20299449	GO:0044016	histone H3K4 acetyltransferase activity	Taken together, these results show that H3K4ac exists in S. pombe, and that Mst1 and the sirtuin Sir2 are the major HAT and HDAC, respectively, for H3K4. Fig. 2
PMID:20356456	GO:0008379	thioredoxin peroxidase activity	(comment: The peroxidase activity of BCP (bacterioferritin comigratory protein) was similar to that of TPx.)
PMID:20356456	GO:0140309	unfolded protein holdase activity	PMP20, and GPx inhibited thermal aggregation of citrate synthase at 43(o)C,
PMID:20360683	FYPO:0003917	decreased nonsense-mediated decay	(comment: assayed using GFP reporter with or without premature stop codons)
PMID:20360683	FYPO:0003917	decreased nonsense-mediated decay	(comment: assayed using GFP reporter with or without premature stop codons)
PMID:20360683	FYPO:0003947	normal nonsense-mediated decay	(comment: assayed using ypt3 reporter with or without premature stop codons)
PMID:20360683	FYPO:0003947	normal nonsense-mediated decay	(comment: assayed using ypt3 reporter with or without premature stop codons)
PMID:2038306	FYPO:0002700	increased protein kinase activity [has_penetrance] high [assayed_enzyme] PomBase:SPBC11B10.09	(comment: CDC2HS is not recognised by anti cdc2 antibody 4711 and so does not contribute to the level of kinase activity assayed.) (comment: S. pombe cdc2+ is on a multi copy plasmid pMNScdc2 Figure 4A lane 1)
PMID:2038306	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(comment: CHECK CDC2HS complements cdc2delete phenotype) Figure 4B)
PMID:2038306	FYPO:0002176	viable vegetative cell with normal cell size [has_penetrance] high	(comment: CHECK the endogenous copy of cdc2 has been replaced by cdc2 from human cells CDC2HS) (comment: S. pombe cdc2+ is expressed from episomal pMNScdc2 in presence of thiamine. The cdc2 is therefore not really over expressed but I was unable to say it was 'not assayed) Figure 3C
PMID:2038306	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(comment: CHECK the endogenous copy of cdc2 has been replaced by cdc2 from human cells CDC2HS. S. pombe cdc2+ is on an episomal plasmid pMNScdc2 Figure 3D)
PMID:2038306	FYPO:0001382	decreased protein kinase activity [has_penetrance] high [assayed_enzyme] PomBase:SPBC11B10.09	(comment: cdc2-DL5 is expressed from episomal pMNScdc2DL5) (comment: CDC2HS is not recognised by anti cdc2 antibody 4711 and so does not contribute to the level of cdc2-DL5 kinase activity Figure 4A)
PMID:2038306	FYPO:0001382	decreased protein kinase activity [has_penetrance] high [assayed_enzyme] PomBase:SPBC11B10.09	(comment: cdc2-DL5 is over expressed from episomal pMNScdc2DL5) (comment: CDC2HS is not recognised by anti cdc2 antibody 4711 and so does not contribute to the level of cdc2-DL5 kinase activity assayed.) (Figure 4A)
PMID:2038306	FYPO:0004255	inviable elongated mononucleate vegetative cell [has_penetrance] high	(comment: cdc2-DL5 is over expressed from episomal pMNScdc2DL5. The endogenous cdc2+ has been replaced by the human cdc2 gene CDC2HS.) Same phenotype as shown in Figure 2
PMID:2038306	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(comment: co ip of cdc2-DL5 and endogenous CDC2HS with anti cdc13 SP4 shows reduced kinase activity compared to CDC2HS alone Figure 7. cdc2-DL5 is on episomal pMNS cdc2DL5. The authors argue that inactive cdc2-DL5 may titrate away factors required for cdc2 kinase activity but unless I have misunderstood the experiment I think this could just as well be interpreted as SP4 iping a mixture of active and inactive cdc2 kinase activity and thus less total cdc2 kinase activity)
PMID:2038306	FYPO:0000049	inviable cell [has_penetrance] high	(comment: pMNScdc2-DL5 fails to rescue cdc2-33 mutant at the restrictive temperature. Do not say how this was assayed)
PMID:2038306	FYPO:0000049	inviable cell [has_penetrance] high	(comment: pMNScdc2-DL5 is an episomal plasmid.)
PMID:2038306	FYPO:0004255	inviable elongated mononucleate vegetative cell [has_penetrance] high	(comment: pMNScdc2-DL5 is integrated Cells observed after 12 hours over expression) Figure 2. (comment: In the paper they call this plasmid pMNSDL5 I have added cdc2-DL5 for clarity) (comment: The pMNS21L plasmid used for isolating this cdc2 mutant has since been rename pREP1.)
PMID:2038306	FYPO:0005023	inviable elongated septated mononucleate vegetative cell [has_penetrance] high	(comment: pMNScdc2-DL5 is integrated cells observed after 30 hours over expression) (Figure 2) (comment: In the paper they call this plasmid pMNSDL5 I have added cdc2-DL5 for clarity). (comment: The pMNS21L plasmid used for isolating this cdc2 mutant has since been rename pREP1.)
PMID:2038306	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 5	(comment: pMNScdc2-DL5 is integrated)
PMID:2038306	FYPO:0001430	abnormal mitotic cell cycle arrest with unreplicated DNA [has_penetrance] 6	Data not shown. (comment: pMNScdc2-DL5 is integrated)
PMID:2038306	FYPO:0000444	abnormal mitotic cell cycle arrest with replicated DNA [has_penetrance] high	Data not shown. (comment: pMNScdc2-DL5 is integrated)
PMID:20383139	FYPO:0001355	decreased vegetative cell population growth	(Fig. 1b)
PMID:20383139	FYPO:0001357	normal vegetative cell population growth	(Fig. 1b)
PMID:20383139	FYPO:0001357	normal vegetative cell population growth	(Fig. 1b)
PMID:20383139	FYPO:0001357	normal vegetative cell population growth	(Fig. 1b)
PMID:20383139	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] ~18	(Fig. 1d)
PMID:20383139	FYPO:0001513	normal mitotic sister chromatid segregation	(Fig. 1d)
PMID:20383139	FYPO:0003970	incomplete mitotic sister chromatid segregation, with chromatin bridge [has_penetrance] ~70	(Fig. 1e)
PMID:20383139	FYPO:0003970	incomplete mitotic sister chromatid segregation, with chromatin bridge [has_penetrance] ~18	(Fig. 1e)
PMID:20383139	FYPO:0003550	decreased protein level during meiosis [assayed_using] PomBase:SPAC23C11.16	(Fig. 2b)
PMID:20383139	FYPO:0002799	normal protein degradation [assayed_using] PomBase:SPBC29A10.14	(Fig. 2b)
PMID:20383139	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPBC29A10.14	(Fig. 2b)
PMID:20383139	FYPO:0000734	abnormal meiotic spindle [assayed_using] PomBase:SPAC23C11.16	(Fig. 2b)
PMID:20383139	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC29A10.14 [part_of] meiotic sister chromatid arm separation	(Fig. 3a)
PMID:20383139	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC29A10.14 [part_of] meiotic sister chromatid arm separation	(Fig. 3a)
PMID:20383139	GO:0072542	protein phosphatase activator activity [part_of] meiotic centromeric cohesion protection in anaphase I [has_input] PomBase:SPBC16H5.07c	(Fig. 3a)
PMID:20383139	GO:0004722	protein serine/threonine phosphatase activity [has_input] PomBase:SPBC29A10.14 [part_of] meiotic centromeric cohesion protection in anaphase I	(Fig. 3a) (comment: par1, the regulatory subunit was used in the assay)
PMID:20383139	FYPO:0006083	abnormal sporulation resulting in formation of ascus with four spores [has_penetrance] 20	(Fig. 3c)
PMID:20383139	FYPO:0003378	abolished meiosis I [has_penetrance] 80	(Fig. 3c)
PMID:20383139	FYPO:0006528	decreased proteolysis during meiotic cell cycle [assayed_using] PomBase:SPBC29A10.14	(Fig. 4c)
PMID:20383139	FYPO:0006532	normal protein localization to centromere during meiotic prophase II [assayed_using] PomBase:SPBC29A10.14	(Fig. 5B)
PMID:20383139	FYPO:0006530	abolished protein localization to centromere during meiotic prophase II [assayed_using] PomBase:SPBC29A10.14 [has_penetrance] ~90	(Fig. 5b)
PMID:20383139	FYPO:0006530	abolished protein localization to centromere during meiotic prophase II [assayed_using] PomBase:SPBC29A10.14 [has_penetrance] ~90	(Fig. 5b)
PMID:20383139	FYPO:0006530	abolished protein localization to centromere during meiotic prophase II [assayed_using] PomBase:SPBC29A10.14 [has_penetrance] ~90	(Fig. 5b)
PMID:20383139	FYPO:0006530	abolished protein localization to centromere during meiotic prophase II [assayed_using] PomBase:SPCC188.02	(Fig. 5c)
PMID:20383139	FYPO:0003790	normal protein localization during meiosis [assayed_using] PomBase:SPCC188.02	(Fig. 5c)
PMID:20383139	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 20	(Fig. S1a)
PMID:20383139	GO:0000228	nuclear chromosome [exists_during] meiosis I cell cycle phase	(Fig. S5)
PMID:20383139	GO:0000228	nuclear chromosome [exists_during] meiosis I cell cycle phase	(Fig. S5)
PMID:20383139	FYPO:0006315	abolished homologous chromosome segregation [has_penetrance] 70	(comment: CHECK separation)
PMID:20388730	FYPO:0004483	abnormal vacuole fusion during cellular hypotonic response	By contrast, imt1imt2imt3 cells had slightly smaller vacuoles compared with those of wild-type cells under normal conditions (Fig. 6)
PMID:20388730	FYPO:0002788	small vacuoles during vegetative growth	By contrast, imt1imt2imt3 cells had slightly smaller vacuoles compared with those of wild-type cells under normal conditions (Fig. 6)
PMID:20388730	GO:0005886	plasma membrane	Expressed in wild-type S. pombe grown in rich medium, Aat1-GFP exhibited punctate fluorescence, suggesting that Aat1-GFP localized to the Golgi apparatus (Fig. 8A,B). When the cells were shifted to a nitrogen-free medium, Aat1-GFP was transported from the Golgi apparatus to the plasma membrane within 30 minutes, followed by endocytosis and transport to the vacuolar lumen.
PMID:20388730	GO:0051999	mannosyl-inositol phosphorylceramide biosynthetic process	Interestingly, a significant amount of IPC accumulated and MIPC decreased in sur2 cells. The scs7 mutation also caused a reduction in MIPC content. These results suggest that Imt proteins exhibit weak activity towards dihydroceramide-containing IPC, such that a reduction in MIPC was observed in sur2 and scs7 mutants.
PMID:20388730	FYPO:0008261	decreased cellular mannosylinositol phosphorylceramide level	Interestingly, a significant amount of IPC accumulated and MIPC decreased in sur2 cells. The scs7 mutation also caused a reduction in MIPC content. These results suggest that Imt proteins exhibit weak activity towards dihydroceramide-containing IPC, such that a reduction in MIPC was observed in sur2 and scs7 mutants.
PMID:20388730	FYPO:0008261	decreased cellular mannosylinositol phosphorylceramide level	Interestingly, a significant amount of IPC accumulated and MIPC decreased in sur2 cells. The scs7 mutation also caused a reduction in MIPC content. These results suggest that Imt proteins exhibit weak activity towards dihydroceramide-containing IPC, such that a reduction in MIPC was observed in sur2 and scs7 mutants.
PMID:20388730	GO:0051999	mannosyl-inositol phosphorylceramide biosynthetic process	Interestingly, a significant amount of IPC accumulated and MIPC decreased in sur2 cells. The scs7 mutation also caused a reduction in MIPC content. These results suggest that Imt proteins exhibit weak activity towards dihydroceramide-containing IPC, such that a reduction in MIPC was observed in sur2 and scs7 mutants.
PMID:20388730	FYPO:0000034	abnormal endocytosis during vegetative growth	Interestingly, endocytosis of Aat1-GFP was severely impaired and Aat1-GFP remained at the plasma membrane after 5 hours of incubation (Fig. 8A). Thus, we conclude that the MIPC- deficient mutant is impaired in its ability to internalize plasma-membrane proteins to the vacuole.
PMID:20388730	FYPO:0005508	abnormal plasma membrane to vacuole transport	Interestingly, endocytosis of Aat1-GFP was severely impaired and Aat1-GFP remained at the plasma membrane after 5 hours of incubation (Fig. 8A). Thus, we conclude that the MIPC- deficient mutant is impaired in its ability to internalize plasma-membrane proteins to the vacuole.
PMID:20388730	GO:0051999	mannosyl-inositol phosphorylceramide biosynthetic process	MIPC was not detected, IPC had accumulated and one unidentified sphingolipid spot was observed (Fig. 2A). These results indicate that all three imt genes are required for MIPC synthesis and that MIPC was not produced in imt1imt2imt3 disruptant mutants.
PMID:20388730	GO:0051999	mannosyl-inositol phosphorylceramide biosynthetic process	MIPC was not detected, IPC had accumulated and one unidentified sphingolipid spot was observed (Fig. 2A). These results indicate that all three imt genes are required for MIPC synthesis and that MIPC was not produced in imt1imt2imt3 disruptant mutants.
PMID:20388730	GO:0051999	mannosyl-inositol phosphorylceramide biosynthetic process	MIPC was not detected, IPC had accumulated and one unidentified sphingolipid spot was observed (Fig. 2A). These results indicate that all three imt genes are required for MIPC synthesis and that MIPC was not produced in imt1imt2imt3 disruptant mutants.
PMID:20388730	FYPO:0008262	mannosylinositol phosphorylceramide absent from cell	MIPC was not detected, IPC had accumulated and one unidentified sphingolipid spot was observed (Fig. 2A). These results indicate that all three imt genes are required for MIPCsynthesis and that MIPC was not produced in imt1imt2imt3 disruptant mutants.
PMID:20388730	FYPO:0000098	sensitive to calcium	Sensitivity to Ca2+ was determined by a visual spot assay on YES medium (Fig. 5). Single imt mutants did not exhibit obvious Ca2+ sensitivity, whereas the imt1imt2imt3 mutant did.
PMID:20388730	FYPO:0000024	stubby vegetative cell	"Single and double disruptants had a normal cell shape, but the imt1imt2imt3 disruptants were round or pear shaped under normal growth conditions (Fig. 4). (comment: note that these do not look particularly rounded or pear-shaped and fit our ""stubby"" morphology better)"
PMID:20388730	GO:0005802	trans-Golgi network	These results indicate that all three Imt-GFP fusion proteins primarily localize to the Golgi and trans-Golgi network, similar to S. cerevisiae Sur1p (Lisman et al., 2004).
PMID:20388730	GO:0005802	trans-Golgi network	These results indicate that all three Imt-GFP fusion proteins primarily localize to the Golgi and trans-Golgi network, similar to S. cerevisiae Sur1p (Lisman et al., 2004).
PMID:20388730	GO:0005802	trans-Golgi network	These results indicate that all three Imt-GFP fusion proteins primarily localize to the Golgi and trans-Golgi network, similar to S. cerevisiae Sur1p (Lisman et al., 2004).
PMID:20388730	FYPO:0000135	abnormal plasma membrane sterol distribution	Whereas imt1imt2imt3 cells exhibited enhanced levels of fluorescence, sterols were detected throughout the plasma membrane (Fig. 7). These results suggest that aberrant localization or enrichment of sterols in the plasma membrane caused sensitivity to polyene antibiotics in MIPC-deficient cells.
PMID:20388730	FYPO:0000076	resistance to nystatin	imt1imt2imt3 cells were also found to be sensitive to 3 g/ml nystatin and to 0.5 g/ml amphotericin B (Fig. 5).
PMID:20388730	FYPO:0002642	sensitive to amphotericin B	imt1imt2imt3 cells were also found to be sensitive to 3 g/ml nystatin and to 0.5 g/ml amphotericin B (Fig. 5).
PMID:20404084	FYPO:0006549	decreased gene expression [assayed_using] PomBase:SPAP7G5.06	Adding rapamycin to oca2 or cha4 cells that were grown with ammonia led to a reduction of transcripts B and C and to an increase of transcript A, a profile closer to the one displayed by wt cells grown with this nitrogen source (see Fig. S2B in the supplemental material). This observation could thus explain the improved growth phenotype of oca2 and cha4 in the presence of the drug
PMID:20404084	FYPO:0006549	decreased gene expression [assayed_using] PomBase:SPAP7G5.06	Adding rapamycin to oca2 or cha4 cells that were grown with ammonia led to a reduction of transcripts B and C and to an increase of transcript A, a profile closer to the one displayed by wt cells grown with this nitrogen source (see Fig. S2B in the supplemental material). This observation could thus explain the improved growth phenotype of oca2 and cha4 in the presence of the drug
PMID:20404084	FYPO:0005014	decreased histone H4-K12 acetylation during vegetative growth [assayed_region] PomBase:SPAC869.10c	Again, oca2 cells gave similar lower levels of H4K12 acetylation at this locus in both nitrogen sources (Fig. 4C, right).
PMID:20404084	FYPO:0000077	resistance to rapamycin	As with oca2 , cha4 and ago1 are resistant to rapamycin (see Fig. S2A in the supplemental material).
PMID:20404084	FYPO:0000077	resistance to rapamycin	As with oca2 , cha4 and ago1 are resistant to rapamycin (see Fig. S2A in the supplemental material).
PMID:20404084	FYPO:0007506	increased protein localization to chromatin at promoter [assayed_region] PomBase:SPAP7G5.06 [assayed_using] RNA polymerase II, core complex	Chromatin from cha4 cells grown in either ammonia or proline gave a Pol II profile similar to that of oca2 cells, except that Pol II levels over probe 1 were lower (Fig. 4A, right).
PMID:20404084	FYPO:0000243	normal growth on proline nitrogen source	Finally, hat1 cells grew normally in both ammonia and proline.
PMID:20404084	FYPO:0000242	normal growth on ammonia nitrogen source	Finally, hat1 cells grew normally in both ammonia and proline.
PMID:20404084	FYPO:0005014	decreased histone H4-K12 acetylation during vegetative growth [assayed_using] PomBase:SPAP7G5.06 [has_severity] low	Furthermore, H4K12 acetylation at per1 was higher in oca2 clr6-1 than in oca2 cells, indicating that reduced H4K12 acetylation in oca2 cells grown in ammonia is due to increased Clr6 activity (Fig. 5D, compare left and middle)
PMID:20404084	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPAP7G5.06	In RNA from cha4 cells grown in ammonia, we de- tected transcripts A, B, and C, similar to oca2 (Fig. 3A, lanes 5, 11, and 17). However, cha4 cells grown in proline produced transcript A but only small amounts of transcripts B and C, a profile more similar to that of wt cells grown in ammonia. Therefore, cha4 cells showed aberrant expression of per1 in both nitrogen sources, whereas oca2 cells showed a defect only in ammonia.
PMID:20404084	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPAP7G5.06	In RNA from cha4 cells grown in ammonia, we de- tected transcripts A, B, and C, similar to oca2 (Fig. 3A, lanes 5, 11, and 17). However, cha4 cells grown in proline produced transcript A but only small amounts of transcripts B and C, a profile more similar to that of wt cells grown in ammonia. Therefore, cha4 cells showed aberrant expression of per1 in both nitrogen sources, whereas oca2 cells showed a defect only in ammonia.
PMID:20404084	FYPO:0000077	resistance to rapamycin	In addition, oca2 cells are resistant to rapamycin in minimal medium with ammonia (even though growth is already slow), another similarity to S. cerevisiae Npr1 (40) (see Fig. S2A in the supplemental material).
PMID:20404084	FYPO:0000142	gene expression phenotype [assayed_using] PomBase:SPAP7G5.06	In contrast to oca2 , the oca2 clr6-1 double mutant did not produce transcripts B and C when grown in ammonia, sug- gesting that Clr6 activity is responsible for their aberrant expression in oca2 (Fig. 5C, compare lanes 1 and 7 with lanes 3 and 9).
PMID:20404084	FYPO:0005014	decreased histone H4-K12 acetylation during vegetative growth [assayed_region] PomBase:SPAP7G5.06 [has_severity] high	In contrast, H4K12 acetylation was low in the oca2 strain for both nitro- gen sources (Fig. 4B, middle).
PMID:20404084	FYPO:0000243	normal growth on proline nitrogen source	Interestingly, we found that the loss of oca2 leads to a slow-growth phenotype when cells are grown in minimal medium (EMM) with ammo- nia as the nitrogen source, but cells grow normally in proline or glutamate (Fig. 1B), suggesting that Oca2 has a role in the response to nitrogen availability similar to that of Npr1.
PMID:20404084	FYPO:0001234	slow vegetative cell population growth [has_severity] high	Interestingly, we found that the loss of oca2 leads to a slow-growth phenotype when cells are grown in minimal medium (EMM) with ammo- nia as the nitrogen source, but cells grow normally in proline or glutamate (Fig. 1B), suggesting that Oca2 has a role in the response to nitrogen availability similar to that of Npr1.
PMID:20404084	FYPO:0000243	normal growth on proline nitrogen source	Interestingly, we found that the loss of oca2 leads to a slow-growth phenotype when cells are grown in minimal medium (EMM) with ammo- nia as the nitrogen source, but cells grow normally in proline or glutamate (Fig. 1B), suggesting that Oca2 has a role in the response to nitrogen availability similar to that of Npr1.
PMID:20404084	FYPO:0000250	decreased cell population growth on proline nitrogen source [has_severity] medium	Likewise, cells lacking Ago1 showed a moderately slow growth phenotype in proline but a severe growth defect in ammonia.
PMID:20404084	FYPO:0001234	slow vegetative cell population growth [has_severity] high	Likewise, cells lacking Ago1 showed a moderately slow growth phenotype in proline but a severe growth defect in ammonia.
PMID:20404084	GO:0004674	protein serine/threonine kinase activity	Oca2-His6 expressed in Sf9 insect cells phosphorylates myelin basic protein (MBP) in vitro, confirming that Oca2 has kinase activity (see Fig. S1A in the supplemental material). Moreover, we found that Oca2 preferentially phosphorylates serines and threonines surrounded by basic residues (see Fig. S1B in the supplemental material).
PMID:20404084	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC1683.13c	Oca2-His6 expressed in Sf9 insect cells phosphorylates myelin basic protein (MBP) in vitro, confirming that Oca2 has kinase activity (see Fig. S1A in the supplemental material). Moreover, we found that Oca2 preferentially phosphorylates serines and threonines surrounded by basic residues (see Fig. S1B in the supplemental material).
PMID:20404084	FYPO:0000250	decreased cell population growth on proline nitrogen source [has_severity] high	Prw1 is a subunit of the Clr6-containing HDAC; we therefore looked at the growth phenotype of a strain carrying the clr6-1 mutant allele (11). clr6-1 mutant cells grew slightly more slowly in ammonia, but their growth was severely impaired in proline, thus showing growth characteristics opposite to those of oca2 , cha4 , and ago1 .
PMID:20404084	FYPO:0001234	slow vegetative cell population growth [has_severity] low	Prw1 is a subunit of the Clr6-containing HDAC; we therefore looked at the growth phenotype of a strain carrying the clr6-1 mutant allele (11). clr6-1 mutant cells grew slightly more slowly in ammonia, but their growth was severely impaired in proline, thus showing growth characteristics opposite to those of oca2 , cha4 , and ago1 .
PMID:20404084	FYPO:0007506	increased protein localization to chromatin at promoter [assayed_region] PomBase:SPAP7G5.06 [assayed_using] RNA polymerase II, core complex	The Pol II profile for chromatin from oca2 cells grown in ammonia was similar to that of wt cells grown in proline, with high levels of binding over the per1 coding and upstream re- gions (Fig. 4A, middle). oca2 cells grown in proline showed similar high levels of Pol II binding, particularly in the region 2 kb upstream of the AUG (probe 1). These results are con- sistent with the Northern blot data (Fig. 3A).
PMID:20404084	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPAP7G5.06	The expression of six genes was increased 1.5-fold (Fig. 2A), among them per1. AND We found that in an oca2 strain grown in EMM with ammonia, the levels of per1 and put4 transcripts were upregulated between 2- and 3-fold compared to a wt strain, confirming the expression- profiling analysis (Fig. 2B).
PMID:20404084	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPAC869.10c	The expression of six genes was increased 1.5-fold (Fig. 2A), among them per1. AND We found that in an oca2 strain grown in EMM with ammonia, the levels of per1 and put4 transcripts were upregulated between 2- and 3-fold compared to a wt strain, confirming the expression- profiling analysis (Fig. 2B).
PMID:20404084	FYPO:0007631	increased histone H4-K12 acetylation during vegetative growth [assayed_region] PomBase:SPAP7G5.06	These results suggest that Clr6, but not Hat1, is involved in deacety- lation of H4K12 at the per1 locus and in expression of tran- script B. Consistently, clr6-1 mutant cells displayed a growth defect with proline as the nitrogen source, whereas hat1 cells grew normally (Fig. 1B).
PMID:20404084	FYPO:0005014	decreased histone H4-K12 acetylation during vegetative growth [assayed_region] PomBase:SPAP7G5.06	We also looked at the profile of H4K12 acetylation in cha4 cells (Fig. 4B, right). In the presence of ammonia, levels of H4K12 acetylation over the per1 ORF were lower than the in wt strain, similar to the oca2 strain.
PMID:20404084	FYPO:0005014	decreased histone H4-K12 acetylation during vegetative growth [assayed_region] PomBase:SPAC869.10c	We also looked at the profile of H4K12 acetylation in cha4 cells (Fig. 4B, right). In the presence of ammonia, levels of H4K12 acetylation over the per1 ORF were lower than the in wt strain, similar to the oca2 strain.
PMID:20404084	FYPO:0007631	increased histone H4-K12 acetylation during vegetative growth [assayed_region] PomBase:SPAP7G5.06	We also looked at the profile of H4K12 acetylation in cha4 cells (Fig. 4B, right). In the presence of ammonia, levels of H4K12 acetylation over the per1 ORF were lower than the in wt strain, similar to the oca2 strain.
PMID:20404084	FYPO:0001234	slow vegetative cell population growth [has_severity] high	cha4 cells had a phenotype similar to that of oca2 cells, with slow growth in EMM containing ammonia as the nitrogen source but normal growth in proline.
PMID:20404084	FYPO:0000243	normal growth on proline nitrogen source	cha4 cells had a phenotype similar to that of oca2 cells, with slow growth in EMM containing ammonia as the nitrogen source but normal growth in proline.
PMID:20404084	GO:0006808	regulation of nitrogen utilization	suggesting that Oca2 has a role in the response to nitrogen availability similar to that of Npr1.
PMID:20404084	GO:0019740	nitrogen utilization	suggesting that Oca2 has a role in the response to nitrogen availability similar to that of Npr1.
PMID:20404084	GO:0006808	regulation of nitrogen utilization	suggesting that Oca2 has a role in the response to nitrogen availability similar to that of Npr1.
PMID:20434336	GO:0032541	cortical endoplasmic reticulum [exists_during] mitotic interphase	(Fig. 1)
PMID:20434336	GO:0032153	cell division site [exists_during] mitotic M phase	(Fig. 1)
PMID:20434336	GO:0032541	cortical endoplasmic reticulum [exists_during] mitotic interphase	(Fig. 1)
PMID:20434336	GO:0032541	cortical endoplasmic reticulum [exists_during] mitotic M phase	(Fig. 1)
PMID:20434336	GO:0032541	cortical endoplasmic reticulum [exists_during] mitotic interphase	(Fig. 1)
PMID:20434336	GO:0032541	cortical endoplasmic reticulum [exists_during] mitotic M phase	(Fig. 1)
PMID:20434336	GO:0005635	nuclear envelope	(Fig. 1)
PMID:20434336	GO:0032153	cell division site [exists_during] mitotic M phase	(Fig. 1)
PMID:20434336	GO:0032153	cell division site [exists_during] mitotic M phase	(Fig. 1)
PMID:20434336	GO:0032541	cortical endoplasmic reticulum [exists_during] mitotic M phase	(Fig. 1)
PMID:20434336	GO:0005635	nuclear envelope	(Fig. 1)
PMID:20434336	FYPO:0000354	abnormal endoplasmic reticulum morphology [has_severity] high	(Fig. 2D) (comment: tubular/cortical)
PMID:20434336	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] >40	(Fig. 3)
PMID:20434336	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] ~20	(Fig. 3)
PMID:20434336	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] ~90-95	(Fig. 3)
PMID:20434336	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] ~90-95	(Fig. 3)
PMID:20434336	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] ~20	(Fig. 3)
PMID:20434336	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] 92	(Fig. 3)
PMID:20434336	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC926.03	(Fig. 3C)
PMID:20434336	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC32H8.12c	(Fig. 3C)
PMID:20434336	FYPO:0006434	decreased protein localization to medial cortical node, with protein distributed in cell cortex, during vegetative growth [assayed_using] PomBase:SPCC4B3.15	(Fig. 3C) (comment: protein distributed in cortex)
PMID:20434336	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPBC1539.04	(Fig. 4E)
PMID:20434336	FYPO:0003778	decreased protein localization to endoplasmic reticulum tubular network [assayed_using] PomBase:SPBC31A8.01c	(Figure 2A and 2B)
PMID:20434336	FYPO:0003778	decreased protein localization to endoplasmic reticulum tubular network [assayed_using] PomBase:SPCC830.08c	(Figure 2A and 2B)
PMID:20434336	FYPO:0003778	decreased protein localization to endoplasmic reticulum tubular network [assayed_using] PomBase:SPBC31A8.01c	(Figure 2A and 2B)
PMID:20434336	FYPO:0003778	decreased protein localization to endoplasmic reticulum tubular network [assayed_using] PomBase:SPCC830.08c	(Figure 2A and 2B)
PMID:20434336	FYPO:0003778	decreased protein localization to endoplasmic reticulum tubular network [assayed_using] PomBase:SPBC1539.04	(Figure 2A and 2B)
PMID:20434336	FYPO:0000354	abnormal endoplasmic reticulum morphology [assayed_using] PomBase:SPCC830.08c	(Figure 2A and 2B)
PMID:20434336	FYPO:0000354	abnormal endoplasmic reticulum morphology [assayed_using] PomBase:SPCC830.08c	(Figure 2A and 2B) (comment: cortical/tubular)
PMID:20434336	FYPO:0000354	abnormal endoplasmic reticulum morphology [assayed_using] PomBase:SPCC830.08c	(Figure 2A and 2B) (comment: cortical/tubular)
PMID:20434336	GO:0180020	membrane bending activity [part_of] endoplasmic reticulum tubular network membrane organization [occurs_in] cell division site	(Figure S1B)
PMID:20434336	GO:0180020	membrane bending activity [part_of] endoplasmic reticulum tubular network membrane organization [occurs_in] cell division site	(Figure S1C)
PMID:20434336	FYPO:0000339	mislocalized septum during vegetative growth [has_severity] high	(Figure S3A)
PMID:20434336	GO:1990608	mitotic spindle pole body localization	data not shown
PMID:20452294	FYPO:0005221	normal protein oligomerization	(comment: PCNA trimerization)
PMID:20452294	FYPO:0005221	normal protein oligomerization	(comment: PCNA trimerization)
PMID:20452294	FYPO:0005183	abolished protein polyubiquitination during cellular response to UV	(comment: assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all)
PMID:20452294	FYPO:0005183	abolished protein polyubiquitination during cellular response to UV	(comment: assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all)
PMID:20452294	FYPO:0005183	abolished protein polyubiquitination during cellular response to UV	(comment: assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all)
PMID:20452294	FYPO:0005183	abolished protein polyubiquitination during cellular response to UV	(comment: assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all)
PMID:20452294	FYPO:0005183	abolished protein polyubiquitination during cellular response to UV	(comment: assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all)
PMID:20452294	FYPO:0005183	abolished protein polyubiquitination during cellular response to UV	(comment: assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all)
PMID:20452294	FYPO:0005183	abolished protein polyubiquitination during cellular response to UV	(comment: assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all)
PMID:20452294	FYPO:0005183	abolished protein polyubiquitination during cellular response to UV	(comment: assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all)assayed with Ub-Pcn1 fusion; wild type Pcn1 absent; Pcn1-K164R present but previously shown not to be ubiquitinated at all
PMID:20517925	FYPO:0004964	actin cortical patches present in decreased numbers	(Fig. 1B)
PMID:20517925	FYPO:0004652	normal actomyosin contractile ring morphology	(Fig. 1B)
PMID:20517925	FYPO:0005430	aggregated actin cortical patches during vegetative growth	(Fig. 1B)
PMID:20517925	FYPO:0007151	long actin cables	(Fig. 1B) oreover, actin cables often significantly overgrew in these cells while the actin ring formation seemed to be unaffected.
PMID:20517925	FYPO:0006207	decreased rate of actin filament depolymerization [has_severity] high	(Fig. 3D)
PMID:20517925	FYPO:0006207	decreased rate of actin filament depolymerization	(Fig. 3D)
PMID:20517925	FYPO:0001011	filamentous actin absent	(Fig. S1)
PMID:20517925	FYPO:0002022	normal actin cortical patch morphology	(comment: CHECK formation)
PMID:20547592	FYPO:0002177	viable vegetative cell with normal cell morphology [has_penetrance] complete	(Fig. 1)
PMID:20547592	FYPO:0002060	viable vegetative cell population	(Fig. 1)
PMID:20547592	FYPO:0001383	normal DNA content [has_penetrance] complete	(Fig. 1) (comment: nuclear)
PMID:20547592	FYPO:0000158	DNA content increased during vegetative growth	(Fig. 1c)
PMID:20547592	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to heat	(Fig. 2e) suggesting that Vgl1 might escort RNA from ER-associated polyribosomes to the cytosol under thermal stress.
PMID:20547592	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to glucose starvation	(Fig. 5a)
PMID:20547592	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to arsenite ion	(Fig. 5b)
PMID:20547592	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to osmotic stress	(Fig. 5b)
PMID:20547592	FYPO:0005488	sensitive to arsenite	(Fig. 5e)
PMID:20547592	FYPO:0002350	normal stress granule assembly during vegetative growth	(Fig. 6D)
PMID:20547592	FYPO:0002350	normal stress granule assembly during vegetative growth	(Fig. 6c)
PMID:20547592	FYPO:0001387	loss of viability at high temperature	(Figure 4)
PMID:20547592	GO:0005783	endoplasmic reticulum [exists_during] cellular response to nitrogen starvation	(Figure 5A)
PMID:20547592	GO:0005783	endoplasmic reticulum [exists_during] cellular response to oxidative stress	(Figure 5A)
PMID:20547592	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to heat	(Figure 6E)
PMID:20547592	GO:0005737	cytoplasm [exists_during] cellular response to heat	(Figure 6a)
PMID:20547592	FYPO:0002130	abolished protein phosphorylation during cellular response to heat [assayed_using] PomBase:SPAC3G9.09c	(Figure 7A)
PMID:20547592	FYPO:0002350	normal stress granule assembly during vegetative growth	(Figure 7B)
PMID:20547592	FYPO:0001487	normal RNA level during cellular response to heat	(Figure 8A and B) (comment: (fairly similar expression orofiles))
PMID:20603077	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPAC1F5.04c	Cdc12 pulls down only 27% as much Cdc15 in a similar block and release experiment (Supp. Fig. 1B)
PMID:20605454	FYPO:0005048	increased protein localization to chromatin at RNA polymerase II promoter during vegetative growth [assayed_using] PomBase:SPCC1442.10c	(comment: CHECK at act1 & sam1)
PMID:20605454	FYPO:0005048	increased protein localization to chromatin at RNA polymerase II promoter during vegetative growth [assayed_using] PomBase:SPCC1442.10c	(comment: CHECK at act1 & sam1)
PMID:20605454	FYPO:0005049	decreased protein localization to chromatin at RNA polymerase II promoter during nitrogen starvation [assayed_using] PomBase:SPCC1442.10c	(comment: CHECK at ste11)
PMID:20605454	FYPO:0005050	decreased chromatin binding during cellular response to nitrogen starvation [assayed_using] PomBase:SPCC1442.10c	(comment: CHECK at ste11)
PMID:20605454	FYPO:0005047	decreased protein localization to chromatin at RNA polymerase II promoter during vegetative growth [assayed_using] PomBase:SPCC1442.10c	(comment: CHECK at ste11)
PMID:20605454	FYPO:0005047	decreased protein localization to chromatin at RNA polymerase II promoter during vegetative growth [assayed_using] PomBase:SPCC1442.10c	(comment: CHECK at ste11)
PMID:20605454	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC28F2.12	(comment: pol II CTD; probably S2 but can't rule out effect on S7)
PMID:20605454	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC28F2.12	(comment: polII CTD; probably S5 but can't rule out effect on S7)
PMID:20622008	FYPO:0002353	decreased chromatin silencing	(comment: at genes)
PMID:20622014	FYPO:0005083	normal protein localization to chromatin at ncRNA gene [assayed_using] PomBase:SPBC28F2.12	(comment: pol II localization to sme2 locus)
PMID:20622014	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [has_severity] high [assayed_using] PomBase:SPBC29A10.02	(comment: temperature restrictive for mmi1-ts3)
PMID:20622014	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [has_severity] low [assayed_using] PomBase:SPAC14C4.03	(comment: temperature restrictive for mmi1-ts3)
PMID:20622014	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [has_severity] low [assayed_using] PomBase:SPAC25G10.04c	(comment: temperature restrictive for mmi1-ts3)
PMID:20622014	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [has_severity] high [assayed_using] PomBase:SPAC1556.06	(comment: temperature restrictive for mmi1-ts3)
PMID:20622014	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [has_severity] low [assayed_using] PomBase:SPAC27D7.13c	(comment: temperature restrictive for mmi1-ts3)
PMID:20623139	FYPO:0000086	sensitive to tacrolimus [has_severity] high	(comment: CHECK high expressivity)
PMID:20623139	FYPO:0000086	sensitive to tacrolimus [has_severity] low	(comment: CHECK low expressivity)
PMID:20624975	FYPO:0005423	decreased mitotic spindle microtubule depolymerization during mitotic anaphase A	(Fig. 5C)
PMID:20624975	FYPO:0005423	decreased mitotic spindle microtubule depolymerization during mitotic anaphase A	(Fig. S5B-E)
PMID:20624975	FYPO:0000904	decreased microtubule polymerization or depolymerization	(comment: depolymerization (cytoplasmic?))
PMID:2065367	FYPO:0001938	decreased cytochrome-c oxidase activity [has_penetrance] medium	(comment: incomplete penetrance due to translational frameshifting)
PMID:2065367	FYPO:0004017	normal cytochrome-c oxidase activity [has_penetrance] medium	(comment: incomplete penetrance due to translational frameshifting)
PMID:2065367	FYPO:0004018	normal mitochondrial electron transport, NADH to ubiquinone [has_penetrance] medium	(comment: incomplete penetrance due to translational frameshifting)
PMID:2065367	FYPO:0004020	decreased mitochondrial electron transport, succinate to ubiquinone [has_penetrance] medium	(comment: incomplete penetrance due to translational frameshifting)
PMID:2065367	FYPO:0003394	decreased mitochondrial electron transport, NADH to ubiquinone [has_penetrance] medium	(comment: incomplete penetrance due to translational frameshifting)
PMID:2065367	FYPO:0004019	normal mitochondrial electron transport, succinate to ubiquinone [has_penetrance] medium	(comment: incomplete penetrance due to translational frameshifting)
PMID:2065367	FYPO:0000684	decreased cell population growth on glycerol carbon source	(comment: severity is variable, and segregates over successive generations (but not 2:2))
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] LTR_retrotransposon [removed_during] mitotic G2 phase	(comment: Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] LTR_retrotransposon [added_during] mitotic S phase [removed_during] mitotic G2 phase	(comment: Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] LTR_retrotransposon [added_during] mitotic S phase	(comment: Phosphorylated at Tf2-type retrotransposons and wtf elements during S-phase)| (comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] regional_centromere_inner_repeat_region	(comment: Phosphorylated at centromeres during S-phase) (comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] regional_centromere_outer_repeat_region [removed_during] mitotic G2 phase	(comment: Phosphorylated at centromeres during S-phase) (comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] regional_centromere_inner_repeat_region	(comment: Phosphorylated at centromeres during S-phase) (comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] regional_centromere_outer_repeat_region [removed_during] mitotic G2 phase	(comment: Phosphorylated at centromeres during S-phase) (comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] mating_type_region [removed_during] mitotic G2 phase	(comment: Phosphorylated at mating type locus during S-phase) (comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] mating_type_region [removed_during] mitotic G2 phase	(comment: Phosphorylated at mating type locus during S-phase), (comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] mating_type_region [added_during] mitotic S phase	(comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] regional_centromere_outer_repeat_region [added_during] mitotic S phase	(comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] regional_centromere_inner_repeat_region	(comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] regional_centromere_outer_repeat_region [added_during] mitotic S phase	(comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] regional_centromere_inner_repeat_region	(comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [present_during] mitotic S phase	(comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [absent_during] mitotic G2 phase	(comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [present_during] mitotic S phase	(comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [absent_during] mitotic G2 phase	(comment: Rad3 dependent)
PMID:20661445	MOD:00696	phosphorylated residue [coincident_with] mating_type_region [added_during] mitotic S phase	(comment: Rad3 dependent)
PMID:20679485	GO:0140172	histone H2AT120pho reader activity [has_input] hta1/Phos(S128) [part_of] mitotic G2 DNA damage checkpoint signaling	Crb2 binds phosphorylated histone H2A (Hta1 Serine-129 and Hta2 Serine-128) through its C-terminal BRCT domains
PMID:20679485	GO:0140173	histone H2AS139pho reader activity [has_input] hta2/Phos:(S121) [part_of] mitotic G2 DNA damage checkpoint signaling	Crb2 binds phosphorylated histone H2A (Hta1 Serine-129 and Hta2 Serine-128) through its C-terminal BRCT domains
PMID:20705466	FYPO:0000745	delayed onset of actin cortical patch internalization [has_severity] low	(comment: temperature semi-permissive for cdc8-27)
PMID:20705466	FYPO:0005628	decreased rate of cell separation after cytokinesis [has_severity] low	(comment: temperature semi-permissive for cdc8-27)
PMID:20705466	FYPO:0000745	delayed onset of actin cortical patch internalization [has_severity] low	(comment: temperature semi-permissive for cdc8-27)
PMID:20705466	FYPO:0000190	abnormal actin cortical patch localization during vegetative growth [has_severity] low	(comment: temperature semi-permissive for cdc8-27)
PMID:20705471	FYPO:0000745	delayed onset of actin cortical patch internalization [has_severity] low	(comment: temperature permissive for cdc8-27)
PMID:20736315	FYPO:0001426	abnormal negative regulation of mitotic DNA replication initiation resulting in partial rereplication [has_penetrance] high	(Fig. 1B)
PMID:20736315	FYPO:0004597	replication origin firing during mitotic G2 phase [has_penetrance] high	(Fig. 1B)
PMID:20736315	FYPO:0000216	abnormal negative regulation of mitotic DNA replication initiation [has_penetrance] high	(Fig. 4)
PMID:20739936	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1)
PMID:20739936	FYPO:0007244	decreased protein localization to kinetochore during mitotic metaphase [has_severity] high [assayed_using] PomBase:SPCC962.02c	(Fig. 1, S4, S5)
PMID:20739936	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Fig. 1b)
PMID:20739936	FYPO:0004382	meroterically attached lagging mitotic chromosomes [has_penetrance] 10	(Fig. 1c)
PMID:20739936	FYPO:0004382	meroterically attached lagging mitotic chromosomes [has_penetrance] 40	(Fig. 1c)
PMID:20739936	FYPO:0004382	meroterically attached lagging mitotic chromosomes [has_penetrance] medium [has_severity] medium	(Fig. 1d, 1k)
PMID:20739936	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC11B10.09 [added_during] mitotic prometaphase	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC11B10.09 [added_during] mitotic prometaphase	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC11B10.09 [added_during] mitotic prometaphase	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC11B10.09 [added_during] mitotic prometaphase	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC11B10.09 [added_during] mitotic prometaphase	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC11B10.09 [added_during] mitotic prometaphase	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC11B10.09 [added_during] mitotic prometaphase	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC11B10.09 [added_during] mitotic prometaphase	(Fig. 1e) also The in vivo phosphorylation of Bir1 at prometaphase but not interphase was further confirmed by a phospho-specific antibody against one of the CDK sites, Bir1-pS244 (Supplementary Fig. 2).
PMID:20739936	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPCC962.02c [happens_during] mitotic M phase [part_of] positive regulation of mitotic sister chromatid biorientation	(Fig. 1e, Fig. 1f)
PMID:20739936	FYPO:0005366	abolished protein phosphorylation during mitosis	(Fig. 1h)
PMID:20739936	FYPO:0005366	abolished protein phosphorylation during mitosis	(Fig. 1i)
PMID:20739936	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1j)
PMID:20739936	FYPO:0000964	normal growth on thiabendazole [has_severity] high	(Fig. 1j)
PMID:20739936	FYPO:0004382	meroterically attached lagging mitotic chromosomes [has_penetrance] ~20	(Fig. 1k)
PMID:20739936	FYPO:0004328	normal protein localization during mitosis [assayed_using] PomBase:SPCC320.13c	(Fig. 2a)
PMID:20739936	FYPO:0004328	normal protein localization during mitosis [assayed_using] PomBase:SPCC962.02c	(Fig. 2a)
PMID:20739936	FYPO:0007244	decreased protein localization to kinetochore during mitotic metaphase [has_severity] high [assayed_using] PomBase:SPCC320.13c	(Fig. 2a, 2b, S5)
PMID:20739936	FYPO:0007244	decreased protein localization to kinetochore during mitotic metaphase [has_severity] high [assayed_using] PomBase:SPCC320.13c	(Fig. 2a, 2b, S5)
PMID:20739936	FYPO:0007244	decreased protein localization to kinetochore during mitotic metaphase [has_severity] high [assayed_using] PomBase:SPCC320.13c	(Fig. 2a, 2b, S5)
PMID:20739936	FYPO:0001270	complete but unequal mitotic sister chromatid segregation [has_penetrance] 15	(Fig. S1)
PMID:20739936	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 45	(Fig. S1) Nuclear staining of anaphase cells showed that the cdc13-M7 mutant, but not the conventional cdc13-117 mutant, often exhibited lagging chromosomes at anaphase (Fig. 1c).
PMID:20739936	FYPO:0005215	decreased protein localization to kinetochore during mitotic M phase [assayed_using] PomBase:SPCC320.13c	(Fig. S6)
PMID:20739936	FYPO:0005779	normal protein localization to kinetochore during mitosis [assayed_using] PomBase:SPCC320.13c	(Fig. S6)
PMID:20739936	FYPO:0003503	normal vegetative cell length	(comment: CHECK figb)
PMID:20739936	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC962.02c [assayed_using] PomBase:SPAC15A10.15	Bir1-N-5A abolished the interaction with Sgo2, whereas Bir1-N-5D retained the interaction (Fig. 2h)
PMID:20739936	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC962.02c [assayed_using] PomBase:SPAC15A10.15	Bir1-N-5A abolished the interaction with Sgo2, whereas Bir1-N-5D retained the interaction (Fig. 2h)
PMID:20739936	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPCC962.02c [occurs_at] regional_centromere_central_core [part_of] mitotic sister chromatid biorientation	Supplementary Fig. 8a)
PMID:20739936	GO:0005515	protein binding [part_of] mitotic sister chromatid biorientation	Supplementary Fig. 8a)
PMID:20739936	FYPO:0000964	normal growth on thiabendazole [has_severity] high	suppressed at comparable level to Bir1-CD, These results indicate that once they are tethered at centromeres, the functionality is indistinguishable between Bir1 and Bir1-8A. Supporting this conclusion, complex formation of the CPC was intact in bir1-8A cells (Supplementary Fig. 7).
PMID:20799962	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: same as rid1-1 alone)
PMID:20799962	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: same as rid2-1 alone)
PMID:20805322	FYPO:0003989	inviable stubby mononucleate vegetative cell [has_penetrance] 45	(Fig. 1A and Table I)
PMID:20805322	GO:0032956	regulation of actin cytoskeleton organization	(comment: CHECK negative reg of polarization/remodelling)
PMID:20805322	FYPO:0003332	normal protein kinase activity during mitotic interphase [assayed_enzyme] PomBase:SPAC821.12	(comment: assayed substrate MBP)
PMID:20805322	FYPO:0003332	normal protein kinase activity during mitotic interphase [assayed_enzyme] PomBase:SPAC821.12	(comment: assayed substrate MBP)
PMID:20805322	FYPO:0003331	decreased protein kinase activity during mitotic interphase [assayed_enzyme] PomBase:SPAC821.12 [has_severity] medium	(comment: assayed substrate MBP)
PMID:20805322	FYPO:0003331	decreased protein kinase activity during mitotic interphase [assayed_enzyme] PomBase:SPAC821.12 [has_severity] medium	(comment: assayed substrate MBP)
PMID:20805322	FYPO:0003331	decreased protein kinase activity during mitotic interphase [assayed_enzyme] PomBase:SPAC821.12 [has_severity] low	(comment: assayed substrate MBP)
PMID:20805322	FYPO:0003331	decreased protein kinase activity during mitotic interphase [assayed_enzyme] PomBase:SPAC821.12 [has_severity] high	(comment: assayed substrate MBP)
PMID:20805322	FYPO:0003332	normal protein kinase activity during mitotic interphase [assayed_enzyme] PomBase:SPBC17F3.02	(comment: assayed substrate casein)
PMID:20807799	GO:0005884	actin filament [exists_during] mitotic interphase	(comment: CHECK GO:0051329= mitotic interphase)
PMID:20807799	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic M phase	(comment: CHECK PR:000037081= tropomyosin cdc8, acetylated form (fission yeast))
PMID:20807799	FYPO:0003371	abolished protein localization to actomyosin contractile ring, with protein mislocalized to cytoplasm [assayed_using] PomBase:SPAC27F1.02c	(comment: CHECK acetylated Cdc82 so could use PR:000037081)
PMID:20807799	MOD:00427	methylated residue [added_by] PomBase:SPCC16C4.12	"(comment: vw: I used ""added by naa20 which is the catalytic subunit for naa25"")"
PMID:20826461	GO:0005628	prospore membrane [exists_during] meiosis II cell cycle phase	(Fig. 1)
PMID:20826461	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Fig. 1)
PMID:20826461	GO:0043332	mating projection tip	(Fig. 1C
PMID:20826461	FYPO:0003845	normal protein localization to prospore membrane [assayed_using] PomBase:SPAC17G8.10c	(Fig. 1F
PMID:20826461	FYPO:0003845	normal protein localization to prospore membrane [assayed_using] PomBase:SPAC17G8.10c	(Fig. 1F
PMID:20826461	FYPO:0000681	abnormal sporulation resulting in formation of two-spore ascus [has_penetrance] 17	(Fig. 2A)
PMID:20826461	FYPO:0004077	abnormal sporulation resulting in formation of ascus with single large spore [has_penetrance] 8	(Fig. 2A)
PMID:20826461	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 60	(Fig. 2A)
PMID:20826461	FYPO:0007170	normal number of nuclei in ascus [has_penetrance] 99	(Fig. 2B)
PMID:20826461	FYPO:0000583	abolished sporulation [has_penetrance] ~20	(Fig. 2C)
PMID:20826461	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] ~60	(Fig. 2C)
PMID:20826461	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] ~60	(Fig. 2C)
PMID:20826461	FYPO:0000583	abolished sporulation [has_penetrance] ~20	(Fig. 2C)
PMID:20826461	FYPO:0004953	abnormal prospore membrane	(Fig. 4)
PMID:20826461	FYPO:0006055	normal protein localization to meiotic spindle pole body during meiosis II [assayed_using] PomBase:SPAC9G1.09	(Fig. 5)
PMID:20826461	FYPO:0001874	abnormal asymmetric protein localization, with protein localized to both mitotic spindle pole bodies [assayed_using] PomBase:SPAC23C11.16	(Fig. 5)
PMID:20826461	FYPO:0006055	normal protein localization to meiotic spindle pole body during meiosis II [assayed_using] PomBase:SPBC21.06c	(Fig. 5)
PMID:20826461	FYPO:0006055	normal protein localization to meiotic spindle pole body during meiosis II [assayed_using] PomBase:SPCC1739.11c	(Fig. 5)
PMID:20826461	GO:0072687	meiotic spindle [exists_during] meiosis I cell cycle phase	(Fig. 6)
PMID:20826461	GO:0090619	meiotic spindle pole [exists_during] meiosis II cell cycle phase	(Fig. 6)
PMID:20826461	FYPO:0005414	increased protein level during meiosis II [assayed_using] PomBase:SPCC417.06c	(Fig. 6)
PMID:20826461	GO:0072687	meiotic spindle [exists_during] meiosis II cell cycle phase	(Fig. 6)
PMID:20826805	GO:0032153	cell division site [exists_during] mitotic anaphase B	(comment: if it is there after cytokinesis + during anaphase B, then I guess it is safe to say that it is there during cytokinesis too..)
PMID:20826805	GO:0032153	cell division site [exists_during] mitotic cytokinesis	(comment: if it is there after cytokinesis + during anaphase B, then I guess it is safe to say that it is there during cytokinesis too..)
PMID:20826805	GO:0000920	septum digestion after cytokinesis	(comment: seems to play a minor role - ppk11 physically interacts with pmo25. ppk11 deletion mutants have less pmo25 at the cell division site. This is not so important under optimal conditions but becomes important when cells are stressed. The phenotype of MOR mutants is excaberated by ppk11-delta.)
PMID:20826805	GO:2000100	regulation of establishment or maintenance of bipolar cell polarity regulating cell shape	(comment: seems to play a minor role - ppk11 physically interacts with pmo25. ppk11 deletion mutants have less pmo25 at the cell division site. This is not so important under optimal conditions but becomes important when cells are stressed. The phenotype of MOR mutants is excaberated by ppk11-delta.)
PMID:20826805	GO:2000100	regulation of establishment or maintenance of bipolar cell polarity regulating cell shape	(comment: seems to play a minor role - ppk11 physically interacts with pmo25. ppk11 deletion mutants have less pmo25 at the cell division site. This is not so important under optimal conditions but becomes important when cells are stressed. The phenotype of MOR mutants is excaberated by ppk11-delta.)
PMID:20829365	FYPO:0001420	normal vegetative cell population growth rate	(Figure 1a)
PMID:20829365	FYPO:0001309	increased viability in stationary phase	(Figure 1a)
PMID:20829365	FYPO:0001103	resistance to hydrogen peroxide	(Figure 2a)
PMID:20829365	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPCC757.07c	(Figure 2a)
PMID:20829365	FYPO:0004083	normal protein level [assayed_using] PomBase:SPAC1071.10c	(Figure 3)
PMID:20829365	FYPO:0004874	decreased glucose consumption	(Figure 3)
PMID:20829365	FYPO:0001158	normal cellular pH	(Figure 3)
PMID:20829365	FYPO:0000840	normal RNA level [assayed_using] PomBase:SPAC1071.10c	(Figure 3)
PMID:20829365	FYPO:0001168	decreased ATPase activity	(Figure 3)
PMID:20829365	FYPO:0007098	normal growth on vanadate	(Figure 5)
PMID:20833892	FYPO:0001915	abolished prospore membrane formation [has_penetrance] 95	(Fig. 3B) WT 10%
PMID:20854854	FYPO:0000118	multiseptate vegetative cell [has_penetrance] high	(Fig. 1a)
PMID:20854854	FYPO:0001120	pear-shaped vegetative cell [has_penetrance] low	(Fig. 1a)
PMID:20854854	FYPO:0001120	pear-shaped vegetative cell [has_penetrance] high	(Fig. 1a)
PMID:20854854	FYPO:0001234	slow vegetative cell population growth	(Fig. 1b)
PMID:20854854	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 1b)
PMID:20854854	FYPO:0002061	inviable vegetative cell population	(Fig. 1c)
PMID:20854854	FYPO:0000106	sensitive to hygromycin B	(Fig. 1c)
PMID:20854854	FYPO:0002637	normal growth on hygromycin B	(Fig. 1c)
PMID:20854854	FYPO:0002447	abnormal protein N-linked glycosylation during vegetative growth	(Fig. 3)
PMID:20854854	FYPO:0002447	abnormal protein N-linked glycosylation during vegetative growth	(Fig. 3)
PMID:20854854	GO:0052925	dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity [part_of] dolichol-linked oligosaccharide biosynthetic process	(comment: I don't understand the chemistry well enough to know how the HPLC shows this but I think this is enough evidence?)
PMID:20876564	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A and B)
PMID:20876564	FYPO:0004103	viable spherical vegetative cell	(Fig. 1A)
PMID:20876564	FYPO:0004103	viable spherical vegetative cell	(Fig. 1A)
PMID:20876564	FYPO:0004103	viable spherical vegetative cell	(Fig. 1A)
PMID:20876564	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	(Fig. 1A)
PMID:20876564	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:20876564	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:20876564	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 1A)
PMID:20876564	FYPO:0000841	sensitive to sodium dodecyl sulfate	(Fig. 1B)
PMID:20876564	GO:0044732	mitotic spindle pole body	(Fig. 1C)
PMID:20876564	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 2A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 2A)
PMID:20876564	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 2A)
PMID:20876564	FYPO:0001357	normal vegetative cell population growth	(Fig. 2A)
PMID:20876564	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2A)
PMID:20876564	FYPO:0006117	multiseptate spheroid vegetative cell	(Fig. 2B)
PMID:20876564	FYPO:0002177	viable vegetative cell with normal cell morphology	(Fig. 2B)
PMID:20876564	FYPO:0005211	decreased protein localization to mitotic spindle pole body during anaphase [has_severity] low [assayed_protein] PomBase:SPBC21.06c	(Fig. 3A)
PMID:20876564	FYPO:0005211	decreased protein localization to mitotic spindle pole body during anaphase [has_severity] low [assayed_protein] PomBase:SPBC21.06c	(Fig. 3A)
PMID:20876564	FYPO:0007568	normal protein localization to mitotic spindle pole body during anaphase [assayed_protein] PomBase:SPBC21.06c	(Fig. 3A)
PMID:20876564	FYPO:0005211	decreased protein localization to mitotic spindle pole body during anaphase [has_severity] high [assayed_protein] PomBase:SPBC21.06c	(Fig. 3A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 4A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:20876564	FYPO:0000674	normal cell population growth at high temperature	(Fig. 4A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:20876564	FYPO:0000674	normal cell population growth at high temperature	(Fig. 4A)
PMID:20876564	FYPO:0000674	normal cell population growth at high temperature	(Fig. 4A)
PMID:20876564	FYPO:0000674	normal cell population growth at high temperature	(Fig. 4A)
PMID:20876564	FYPO:0000674	normal cell population growth at high temperature	(Fig. 4A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:20876564	FYPO:0000674	normal cell population growth at high temperature	(Fig. 4A)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:20876564	FYPO:0000674	normal cell population growth at high temperature	(Fig. 4B)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4B)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4B)
PMID:20876564	FYPO:0000674	normal cell population growth at high temperature	(Fig. 4B)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4B)
PMID:20876564	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4B)
PMID:20876564	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4B)
PMID:20876564	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4B)
PMID:20876564	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4B)
PMID:20876564	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4B)
PMID:20876564	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4B)
PMID:20876564	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth	(Fig. 6A)
PMID:20876564	FYPO:0007388	misoriented mitotic spindle	(Fig. 6A)
PMID:20876564	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 6B)
PMID:20876564	FYPO:0003028	normal actin cortical patch localization during mitosis	(Fig. 6C)
PMID:20876564	FYPO:0003028	normal actin cortical patch localization during mitosis	(Fig. 6C)
PMID:20876564	FYPO:0003028	normal actin cortical patch localization during mitosis	(Fig. 6D)
PMID:20876564	FYPO:0003028	normal actin cortical patch localization during mitosis	(Fig. 6D)
PMID:20876564	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth	(Fig. 6D)
PMID:20885790	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(comment: less sensitive than ssb3delta alone)
PMID:20890290	GO:0030695	GTPase regulator activity [has_input] PomBase:SPBC25B2.01 [part_of] cytoplasmic translational termination	Second, eRF1 and Dom34 increase the binding of GTP to eRF3 and Hbs1, respectively, and GTP increases the binding of eRF1 and Dom34 to eRF3 and Hbs1, respectively28,32,33 (Fig. 6 and Supplementary Table 1). These interactions suggest that in both complexes the status of the nucleotide affects the interaction of the proteins and thereby modulates the function of the complex.
PMID:20890290	GO:0030695	GTPase regulator activity [has_input] PomBase:SPCC584.04 [part_of] cytoplasmic translational termination	Second, eRF1 and Dom34 increase the binding of GTP to eRF3 and Hbs1, respectively, and GTP increases the binding of eRF1 and Dom34 to eRF3 and Hbs1, respectively28,32,33 (Fig. 6 and Supplementary Table 1). These interactions suggest that in both complexes the status of the nucleotide affects the interaction of the proteins and thereby modulates the function of the complex.
PMID:20919928	GO:0005737	cytoplasm	. In contrast to Mak1, Mak2, Mak3, Mcs4, and Prr1, the single phosphorelay protein Mpr1 was located in both the cytoplasmic and the nuclear compartments of the cell (Fig. 4), suggesting that Mpr1 may function to relay signals to the nuclear response regulator Prr1, in addition to Mcs4 (see below).
PMID:20919928	GO:0005634	nucleus	. In contrast to Mak1, Mak2, Mak3, Mcs4, and Prr1, the single phosphorelay protein Mpr1 was located in both the cytoplasmic and the nuclear compartments of the cell (Fig. 4), suggesting that Mpr1 may function to relay signals to the nuclear response regulator Prr1, in addition to Mcs4 (see below).
PMID:20919928	GO:0005829	cytosol	The three histidine kinases, Mak1, Mak2, and Mak3, were found to be cytoplasmic and visibly excluded from the nucleus (Fig. 4).
PMID:20919928	GO:0005829	cytosol	The three histidine kinases, Mak1, Mak2, and Mak3, were found to be cytoplasmic and visibly excluded from the nucleus (Fig. 4).
PMID:20919928	GO:0005829	cytosol	The three histidine kinases, Mak1, Mak2, and Mak3, were found to be cytoplasmic and visibly excluded from the nucleus (Fig. 4).
PMID:20924116	FYPO:0006555	abnormal multiple protein binding to DNA	ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA
PMID:20924116	FYPO:0006555	abnormal multiple protein binding to DNA	ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA
PMID:20924116	FYPO:0006555	abnormal multiple protein binding to DNA	ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA
PMID:20924116	FYPO:0006555	abnormal multiple protein binding to DNA	ternary complex normally forms with Swi1-Swi3 and Mrc1 on DNA
PMID:20929775	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPAC664.01c	(comment: CHECK K9 methyl;ated)
PMID:20929775	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPAC664.01c	(comment: CHECK K9-mehtylated)
PMID:20929775	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPAC664.01c	(comment: CHECK K9-mehtylated)
PMID:20929775	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPCC962.02c [part_of] mitotic sister chromatid biorientation	(comment: CHECK phosphorylated)
PMID:20929775	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPCC962.02c [part_of] mitotic sister chromatid biorientation	(comment: CHECK phosphorylated)
PMID:20929775	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPCC962.02c [part_of] mitotic sister chromatid biorientation	(comment: CHECK phosphorylated)
PMID:20935472	GO:0000776	kinetochore [exists_during] mitotic metaphase	(comment: CHECK during metaphase)
PMID:20935472	FYPO:0004383	premature protein localization to mitotic spindle [assayed_using] PomBase:SPBC6B1.04	Thus, we conclude that Cdc2 activity prevents precocious localization of Mde4 to the metaphase spindle.
PMID:20937798	FYPO:0000096	sensitive to cadmium [has_severity] low	(Supp. Fig. 1)
PMID:20967229	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1)
PMID:20967229	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1)
PMID:20967229	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:20967229	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1A)
PMID:20967229	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1A)
PMID:20967229	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1A)
PMID:20967229	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1A)
PMID:20967229	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1A)
PMID:20967229	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1A)
PMID:20967229	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1A)
PMID:20967229	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1A)
PMID:20967229	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1A)
PMID:20967229	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1A)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:20967229	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1A)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:20967229	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1A)
PMID:20967229	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1A)
PMID:20967229	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1A)
PMID:20967229	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1A)
PMID:20967229	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1A)
PMID:20967229	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1A)
PMID:20967229	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1A)
PMID:20967229	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 1A)
PMID:20967229	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1A)
PMID:20967229	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1A)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 1A)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 1A)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 1A)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 1A)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 1A)
PMID:20967229	FYPO:0001690	normal growth on camptothecin	(Fig. 1A)
PMID:20967229	FYPO:0001690	normal growth on camptothecin	(Fig. 1A)
PMID:20967229	FYPO:0001690	normal growth on camptothecin	(Fig. 1B)
PMID:20967229	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1B)
PMID:20967229	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1B)
PMID:20967229	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1B)
PMID:20967229	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1B)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1B)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1B)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 1B)
PMID:20967229	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1B)
PMID:20967229	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1B)
PMID:20967229	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1B)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:20967229	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1B)
PMID:20967229	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1B)
PMID:20967229	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1B)
PMID:20967229	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1B)
PMID:20967229	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1B)
PMID:20967229	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1B)
PMID:20967229	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 1B)
PMID:20967229	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 1B)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:20967229	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1B)
PMID:20967229	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1B)
PMID:20967229	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1B)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 1B)
PMID:20967229	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1B)
PMID:20967229	FYPO:0001690	normal growth on camptothecin	(Fig. 1B)
PMID:20967229	FYPO:0001690	normal growth on camptothecin	(Fig. 1B)
PMID:20967229	FYPO:0001690	normal growth on camptothecin	(Fig. 1B)
PMID:20967229	FYPO:0001690	normal growth on camptothecin	(Fig. 1B)
PMID:20967229	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1B)
PMID:20967229	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2A)
PMID:20967229	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2A)
PMID:20967229	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2A)
PMID:20967229	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2A)
PMID:20967229	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2A)
PMID:20967229	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2A)
PMID:20967229	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2A)
PMID:20967229	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2A)
PMID:20967229	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2A)
PMID:20967229	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2B)
PMID:20967229	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2B)
PMID:20967229	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2B)
PMID:20967229	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2B)
PMID:20967229	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2B)
PMID:20967229	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2B)
PMID:20967229	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2B)
PMID:20967229	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2B)
PMID:20967229	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC216.06c [assayed_protein] PomBase:SPBC30D10.04	(Fig. 2B)
PMID:20967229	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(Fig. 4A)
PMID:20967229	FYPO:0001234	slow vegetative cell population growth [has_severity] low	(Fig. 4A)
PMID:20967229	FYPO:0001234	slow vegetative cell population growth [has_severity] low	(Fig. 4A)
PMID:20967229	FYPO:0001122	elongated vegetative cell	(Fig. 4B)
PMID:20967229	FYPO:0001122	elongated vegetative cell	(Fig. 4B)
PMID:20967229	FYPO:0001122	elongated vegetative cell	(Fig. 4B)
PMID:20967229	FYPO:0001122	elongated vegetative cell	(Fig. 4B)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4B)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4B)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4B)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4B)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4B)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4B)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4B)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4B)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4B)
PMID:20967229	FYPO:0001122	elongated vegetative cell	(Fig. 4C)
PMID:20967229	FYPO:0001122	elongated vegetative cell	(Fig. 4C)
PMID:20967229	FYPO:0001122	elongated vegetative cell	(Fig. 4C)
PMID:20967229	FYPO:0001122	elongated vegetative cell	(Fig. 4C)
PMID:20967229	FYPO:0001122	elongated vegetative cell	(Fig. 4C)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4C)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4C)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4C)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4C)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4C)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4C)
PMID:20967229	FYPO:0003503	normal vegetative cell length	(Fig. 4C)
PMID:20967229	FYPO:0001122	elongated vegetative cell	(Fig. 4C)
PMID:20967229	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPCC18B5.11c	(Fig. 6A)
PMID:20967229	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPCC18B5.11c [has_severity] high	(Fig. 6A)
PMID:20967229	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPCC18B5.11c [has_severity] medium	(Fig. 6A)
PMID:20967229	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPCC18B5.11c [has_severity] low	(Fig. 6A)
PMID:20967229	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPCC18B5.11c [has_severity] high	(Fig. 6A)
PMID:20967229	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] 50	(Fig. 6B)
PMID:20967229	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] 45	(Fig. 6B)
PMID:20967229	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] 50	(Fig. 6B)
PMID:20967229	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] 15	(Fig. 6B)
PMID:20967229	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] 45	(Fig. 6B)
PMID:20967229	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] 50	(Fig. 6B)
PMID:20967229	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] 40	(Fig. 6B)
PMID:20967229	FYPO:0006521	abnormal mitotic sister chromatid cohesion	(Fig. 7A-B)
PMID:20967229	FYPO:0006521	abnormal mitotic sister chromatid cohesion	(Fig. 7A-B)
PMID:20967229	FYPO:0006521	abnormal mitotic sister chromatid cohesion	(Fig. 7A-B)
PMID:20967229	FYPO:0006521	abnormal mitotic sister chromatid cohesion	(Fig. 7A-B)
PMID:20967229	FYPO:0006521	abnormal mitotic sister chromatid cohesion	(Fig. 7A-B)
PMID:20967229	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 7C)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 7C)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 7C)
PMID:20967229	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. 7C)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 7C)
PMID:20967229	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 7C)
PMID:20967229	FYPO:0001357	normal vegetative cell population growth	(Fig. 7C)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 7C)
PMID:20967229	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 7C)
PMID:20967229	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 7C)
PMID:20967229	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 7C)
PMID:20967229	FYPO:0000069	resistance to thiabendazole	(Fig. 7C)
PMID:20967229	FYPO:0000069	resistance to thiabendazole	(Fig. 7C)
PMID:20967229	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 7C)
PMID:20967229	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 7C)
PMID:20967229	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 7C)
PMID:20967237	FYPO:0004318	abolished mitotic spindle assembly checkpoint [has_severity] high	(Fig. 1A,B) In the presence of MBC the % cut cells in wild type is almost identical to mad2 Delta at 32 and 35°c suggesting that the spindle assembly checkpoint is not active or overidden above 32°C in wild type cells in presence of MBC.
PMID:20967237	FYPO:0007858	mitotic DNA re-replication in absence of mitotic spindle [has_penetrance] high	(Fig. 1C)
PMID:20967237	FYPO:0007858	mitotic DNA re-replication in absence of mitotic spindle	(Fig. 1D)
PMID:20967237	FYPO:0007858	mitotic DNA re-replication in absence of mitotic spindle [has_penetrance] high	(Fig. 1D)
PMID:20967237	FYPO:0007858	mitotic DNA re-replication in absence of mitotic spindle [has_penetrance] high	(Fig. 1D)
PMID:20967237	FYPO:0000446	cell cycle arrest at mitotic G2/M phase transition [has_penetrance] high	(Fig. 1D) microtubules absent
PMID:20967237	FYPO:0007858	mitotic DNA re-replication in absence of mitotic spindle [has_penetrance] high	(Fig. 1E)
PMID:20967237	FYPO:0005779	normal protein localization to kinetochore during mitosis [assayed_using] PomBase:SPBC20F10.06	(Fig. 2A)
PMID:20967237	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 2B) in this case (high temp + MBC) cells can proceed through cell cycle and replicate their DNA
PMID:20967237	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. 2B) in this case (high temp no MBC) the checkpoint is active at high temperature and cells are blocked in cell cycle progression at 36°C.
PMID:20967237	FYPO:0004367	normal mitotic spindle assembly	(Fig. 2c)
PMID:20967237	FYPO:0007858	mitotic DNA re-replication in absence of mitotic spindle	(Fig. 2c) in presence of MBC cells re-enter S phase earlier than in the absence of MBC
PMID:20967237	FYPO:0002004	microtubules absent from cell	(Fig. 3B) just a short microtubule stub remains
PMID:20967237	FYPO:0000133	elongated multinucleate vegetative cell	(Fig. 3C)
PMID:20967237	FYPO:0007859	nuclear division in absence of mitotic spindle	(Fig. 3D)
PMID:20967237	FYPO:0007859	nuclear division in absence of mitotic spindle [has_penetrance] 30	(Fig. 3E)
PMID:20967237	FYPO:0003342	elongated multinucleate cell [has_penetrance] 28	(Fig. 3F)
PMID:20967237	FYPO:0004562	binucleate aseptate vegetative cell [has_penetrance] medium	(Fig. 3G) (comment: suggests nuclear fission is independent of spindle checkpoint)
PMID:20967237	FYPO:0007860	spindle pole body separation in absence of mitotic spindle [has_penetrance] high	(Fig. 4A)
PMID:20967237	FYPO:0007861	sister chromatid separation during nuclear fission [has_penetrance] 73	(Fig. 4B)
PMID:20967237	FYPO:0007861	sister chromatid separation during nuclear fission [has_penetrance] 70	(Fig. 4C) (comment: followed the presence of clp1 in the nucleolus to monitor cen3)
PMID:20967237	FYPO:0007859	nuclear division in absence of mitotic spindle [has_penetrance] low	(Fig. 4D)
PMID:20967237	FYPO:0007859	nuclear division in absence of mitotic spindle [has_penetrance] low	(Fig. 4E)
PMID:20967237	FYPO:0007862	centromere clustering at nuclear periphery during nuclear division in absence of mitotic spindle	(Fig. 5A)
PMID:20967237	FYPO:0001734	abolished mitotic spindle pole body separation [has_penetrance] high	(Fig. 6D,E) in presence of LatA + MBC there is no SPB separation compared to + MBC only where SPBs can separate
PMID:20967237	FYPO:0007859	nuclear division in absence of mitotic spindle	Video S3
PMID:20967237	FYPO:0007861	sister chromatid separation during nuclear fission [has_penetrance] high	data not shown
PMID:20974849	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	(Fig. 1A)
PMID:20974849	FYPO:0000012	mitotic G2/M phase transition delay	(Fig. 1B)
PMID:20974849	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1C)
PMID:20974849	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 1C)
PMID:20974849	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1C)
PMID:20974849	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 1C)
PMID:20974849	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1C)
PMID:20974849	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1C)
PMID:20974849	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 1D)
PMID:20974849	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high	(Fig. 1D)
PMID:20974849	FYPO:0000405	normal mitotic G2/M phase transition	(Fig. 3A)
PMID:20974849	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 3A)
PMID:20974849	FYPO:0002516	premature mitotic G2/M phase transition [has_severity] low	(Fig. 3A)
PMID:20974849	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	(Fig. 3A)
PMID:20974849	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	(Fig. 3B)
PMID:20974849	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 3B)
PMID:20974849	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 3B)
PMID:20974849	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high	(Fig. 3B)
PMID:20974849	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 3B)
PMID:20974849	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 3B)
PMID:20974849	FYPO:0002516	premature mitotic G2/M phase transition [has_severity] high	(Fig. 3C)
PMID:20974849	FYPO:0002516	premature mitotic G2/M phase transition [has_severity] medium	(Fig. 3C)
PMID:20974849	FYPO:0002516	premature mitotic G2/M phase transition [has_severity] medium	(Fig. 3C)
PMID:20974849	FYPO:0002516	premature mitotic G2/M phase transition [has_severity] high	(Fig. 3C)
PMID:20974849	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	(Fig. 4A)
PMID:20974849	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC24H6.05	(Fig. 4B)
PMID:20974849	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC18B5.03 [has_severity] medium	(Fig. 4C)
PMID:20974849	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC18B5.03	(Fig. 4C)
PMID:20974849	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC18B5.03 [has_severity] low	(Fig. 4C)
PMID:20974849	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC2F7.03c	(Fig. 5A)
PMID:20974849	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC644.06c	(Fig. 5B)
PMID:20974849	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAC57A10.02	(Fig. 5C)
PMID:20974849	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC57A10.02 [has_severity] low	(Fig. 5C)
PMID:20974849	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC57A10.02	(Fig. 5D)
PMID:20974849	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC644.06c	(Fig. 5D)
PMID:20974849	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high	(Fig. 5E)
PMID:20974849	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 5E)
PMID:20974849	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC18B5.03 [has_severity] medium	(Fig. 5F)
PMID:20974849	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC18B5.03 [has_severity] high	(Fig. 5F)
PMID:20974849	FYPO:0000405	normal mitotic G2/M phase transition	(Fig. 5G)
PMID:20974849	FYPO:0002516	premature mitotic G2/M phase transition [has_severity] low	(Fig. 5G)
PMID:20974849	GO:0010971	positive regulation of G2/M transition of mitotic cell cycle	As a whole, our findings suggest that both Cdr2-dependent and -independent mechanisms are responsible for the increased Wee1 levels and the G2/M defect in cpc2D cells.
PMID:20974849	GO:0043024	ribosomal small subunit binding	Importantly, by using a strain expressing a mutant version of Cpc2 (R36D/K38E) with reduced ability to associate with ribosomes in vivo (22), we also showed that ribosome binding of Cpc2 is critical for proper control of cell size at the G2/M boundary (Fig. 4A).
PMID:20980623	GO:0035974	meiotic spindle pole body	(Fig. 2)
PMID:20980623	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC17G8.10c	(Fig. S1)
PMID:20980623	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC17G8.10c	(Fig. S1)
PMID:20980623	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] ~75-80	(Figure 3B,4B) the initiation of spore formation was delayed for +2 h compared with wild-type cells, and also the efficiency of spore formation was dramatically dropped with only +60% of cells containing spores
PMID:20980623	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores	(Figure 4E)
PMID:20980623	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores	(Figure 4E)
PMID:20980623	FYPO:0007246	abolished protein localization to meiotic spindle pole body during anaphase II [assayed_using] PomBase:SPAC17G8.10c	At anaphase II, however, many of the Dma1-GFP signals did not accumulate at SPBs (Fig 2 B&C)
PMID:20980623	FYPO:0007245	normal meiotic spindle pole body [assayed_using] PomBase:SPAC1F3.06c	Supplemental Figure S3
PMID:20980623	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC1F3.06c	Supplemental Figure S3
PMID:20980623	FYPO:0000583	abolished sporulation	dma1+ spg1-106 and dma1+ mob1-1 cells were completely unable to sporulate under conditions in which single spg1-106 or mob1-1 mutants were not apparently compromised for sporulation (Figure 8, A and B), suggesting that Dma1 might function in parallel with Spg1 and Mob1 in sporulation.
PMID:20980623	FYPO:0000583	abolished sporulation	dma1+ spg1-106 and dma1+ mob1-1 cells were completely unable to sporulate under conditions in which single spg1-106 or mob1-1 mutants were not apparently compromised for sporulation (Figure 8, A and B), suggesting that Dma1 might function in parallel with Spg1 and Mob1 in sporulation.
PMID:20980623	FYPO:0000583	abolished sporulation	dma1+ spg1-106 and dma1+ mob1-1 cells were completely unable to sporulate under conditions in which single spg1-106 or mob1-1 mutants were not apparently compromised for sporulation (Figure 8, A and B), suggesting that Dma1 might function in parallel with Spg1 and Mob1 in sporulation.
PMID:20980623	FYPO:0004953	abnormal prospore membrane [assayed_using] PomBase:SPAC1F3.06c	several types of defects in FSM development in dma1+ cells (Figure 6B). These defects roughly fell into three classes: (1) initially FSM formation was normal and appeared as sphere structure, but subsequently it became smaller or collapsed (asterisks in Figure 6B); (2) crescent-shaped structures did not properly develop into cup-like structures (open arrows in Figure 6B); and (3) crescent-shaped structures broke into multiple GFP-Psy1- contaning structures which could not develop into round mature FSMs (arrows in Figure 6B).
PMID:20980623	FYPO:0000587	delayed onset of sporulation	the initiation of spore formation was delayed for +2 h compared with wild-type cells, and also the efficiency of spore formation was dramatically dropped with only +60% of cells containing spores (Figure 3B).
PMID:21035342	GO:0019887	protein kinase regulator activity [has_input] PomBase:SPBC30D10.10c [part_of] positive regulation of TORC2 signaling	"(comment: CHECK this is a bit of a fudge. It should probably be molecular signal transducer but that does not exist and I am prevented from using high level terms) vw: From review:Rab small GTPase emerges as a regulator of TOR complex 2""Consistently, we successfully collected genetic and biochemical data to supportthe notion that Sat1 and Sat4 form a GEF complex for Ryh1 GTPase in S. pombe. (7).I agree the data supports this model. Moreover, the Ryh1 I44E mutant fails to promote TORC2 signaling, implying that GTP-dependent interaction of Ryh1 with TORC2 via the effector domain drives TORC2-Gad8 signaling."
PMID:21035342	GO:0019887	protein kinase regulator activity	(comment: vw: bit61 is importabt for torc2 regulation by ryh1)
PMID:21035342	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPAC4C5.02c [part_of] positive regulation of TORC2 signaling	"From review: Rab small GTPase emerges as a regulator of TOR complex 2 ""Consistently, we successfully collected genetic and biochemical data to support the notion that Sat1 and Sat4 form a GEF complex for Ryh1 GTPase in S. pombe. (7)."
PMID:21035342	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPAC4C5.02c [part_of] positive regulation of TORC2 signaling	"From review: Rab small GTPase emerges as a regulator of TOR complex 2 ""Consistently, we successfully collected genetic and biochemical data to support the notion that Sat1 and Sat4 form a GEF complex for Ryh1 GTPase in S. pombe. (7)."
PMID:21095590	FYPO:0001931	abnormal mitotic cell cycle regulation during cellular response to gamma radiation	(Fig. 5b)
PMID:21095590	FYPO:0001931	abnormal mitotic cell cycle regulation during cellular response to gamma radiation	(Fig. 5b)
PMID:21095590	GO:0045739	positive regulation of DNA repair	phosphorylation of rad9 by DDK releases rad9 from damaged chromatin and allows repair factors to come in... (Figure 6)
PMID:21095590	GO:0045739	positive regulation of DNA repair	phosphorylation of rad9 by DDK releases rad9 from damaged chromatin and allows repair factors to come in... (Figure 6)
PMID:21095590	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC664.07c [happens_during] cellular response to camptothecin [part_of] positive regulation of DNA repair	phosphorylation of rad9 by DDK releases rad9 from damaged chromatin and allows repair factors to come in... (Figure 6)
PMID:21098122	FYPO:0004261	decreased protein phosphorylation during mitotic G2 phase during cellular response to ionizing radiation [assayed_using] PomBase:SPCC1259.13 [has_severity] high	(comment: CHECK MOVE TO ALLELE COMMENTS nuclease-dead allele)
PMID:21098122	FYPO:0000268	sensitive to UV during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000085	sensitive to camptothecin	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000268	sensitive to UV during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000085	sensitive to camptothecin	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000268	sensitive to UV during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000085	sensitive to camptothecin	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098122	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21098141	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to osmotic stress	(comment: In stress granules after hyperosmotic shock (1 M KCl) but not after glucose deprivation)
PMID:21099360	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c [has_severity] medium	(comment: CONDITION 25 degrees)
PMID:21099360	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPBC216.05 [assayed_substrate] PomBase:SPAC694.06c	(comment: CONDITION 25 degrees)
PMID:21099360	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c [has_severity] medium	(comment: CONDITION 25 degrees) (comment: same as hsk1-89 alone
PMID:21099360	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c [has_severity] medium	(comment: CONDITION 25 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c [has_severity] medium	(comment: CONDITION 25 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c [has_severity] medium	(comment: CONDITION 25 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c	(comment: CONDITION 30 degrees)
PMID:21099360	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c [has_severity] high	(comment: CONDITION 30 degrees)
PMID:21099360	FYPO:0001355	decreased vegetative cell population growth	(comment: CONDITION 30 degrees)
PMID:21099360	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c [has_severity] high	(comment: CONDITION 30 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c [has_severity] high	(comment: CONDITION 30 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c [has_severity] high	(comment: CONDITION 30 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c [has_severity] high	(comment: CONDITION 30 degrees) (comment: same as hsk1-89 alone)
PMID:21099360	FYPO:0001357	normal vegetative cell population growth	(comment: CONDITION 30 degrees) restrictive for hsk1-89 alone
PMID:21099360	FYPO:0001382	decreased protein kinase activity	(comment: MBP substrate)
PMID:21099360	GO:0000785	chromatin [coincident_with] origin_of_replication [exists_during] mitotic S phase	(comment: at ars2004 and oriChr2-1266, during early S phase)
PMID:21099360	GO:0031573	mitotic intra-S DNA damage checkpoint signaling	(comment: hsk1 phenotypes more informative than mrc1 itself)
PMID:21099360	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC694.06c	(comment: in SQ/TQ clusters) (comment: CHECK activated_by(CHEBI:29035))
PMID:21099360	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC694.06c [happens_during] cellular response to hydroxyurea	(comment: not in SQ/TQ clusters)
PMID:21099360	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(comment: same as hsk1-89 alone)
PMID:21099360	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(comment: same as hsk1-89 alone)
PMID:21099360	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(comment: same as hsk1-89 alone)
PMID:21107719	GO:0071944	cell periphery	(comment: CHECK localization independent of actin cytoskeleton (assayed using latrunculin A) and microtubule cytoskeleton (assayed using carbendazim))
PMID:21118717	GO:0047555	3',5'-cyclic-GMP phosphodiesterase activity	Active against both cAMP and cGMP based on its ability to confer resistance to exogenous cyclic nucleotides. Fig. 1A, B
PMID:21118717	GO:0004115	3',5'-cyclic-AMP phosphodiesterase activity	Active against both cAMP and cGMP based on its ability to confer resistance to exogenous cyclic nucleotides. Fig. 1A, B
PMID:21118717	GO:0004016	adenylate cyclase activity [part_of] adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway	Deletion of both cyr1/git2 and cgs2 produces cells that are hypersensitive to both exogenous cAMP and cGMP as these can activate PKA at low micromolar concentrations. Fig. 1A, B
PMID:21148300	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(comment: Cdc42-GTP assayed with CRIB)
PMID:21148300	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(comment: Cdc42-GTP assayed with CRIB)
PMID:21148300	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(comment: Cdc42-GTP assayed with CRIB)
PMID:21148300	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(comment: Cdc42-GTP assayed with CRIB)
PMID:21151114	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] long_terminal_repeat	(comment: CHECK SO:0000286 = LTR)
PMID:21151114	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] long_terminal_repeat	(comment: CHECK SO:0000286 = LTR)
PMID:21151114	GO:0000785	chromatin [coincident_with] five_prime_UTR	(comment: independent of Clr4)
PMID:21151114	GO:0000785	chromatin [coincident_with] origin_of_replication	(comment: independent of Clr4)
PMID:21151114	GO:0000785	chromatin [coincident_with] rRNA_gene	(comment: independent of Clr4)
PMID:21151114	GO:0000785	chromatin [coincident_with] snoRNA_gene	(comment: independent of Clr4)
PMID:21151114	GO:0000785	chromatin [coincident_with] snRNA_gene	(comment: independent of Clr4)
PMID:21151114	GO:0033562	co-transcriptional gene silencing by RNA interference machinery [occurs_at] long_terminal_repeat	(comment: independent of Clr4)
PMID:21151114	GO:0000785	chromatin [coincident_with] long_terminal_repeat	(comment: independent of Clr4)
PMID:21151114	GO:0033562	co-transcriptional gene silencing by RNA interference machinery [occurs_at] long_terminal_repeat	(comment: independent of Clr4)
PMID:21151114	GO:0000785	chromatin [coincident_with] ncRNA_gene	(comment: independent of Clr4)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECK i) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21182284	MOD:00046	O-phospho-L-serine	(comment: CHECKi) unknown kinase ii) asynchronous cells iii) unknown)
PMID:21211723	GO:0033696	heterochromatin boundary formation	(comment: CHECK not sure if this is quite the correct term, but it is the old spreading term)
PMID:21211723	FYPO:0004347	increased histone H3-K9 acetylation at protein coding gene during vegetative growth	Based on the genetic analyses, it was possible that Asf1/HIRA facilitate histone deacetylation by Clr6. Asf1 co-immunoprecipitated with Clr6 complex subunits Alp13 and Clr6 (Figure 3B). Moreover, asf1-1 and hip1Δ exhibited a substantial increase in bulk H3K9ac levels, in a manner similar to alp13Δ (Figure 3C).). To confirm this further, we performed ChIP-chip analyses of H3K9ac. Both alp13Δ and asf1-1 mutants showed widespread increase in H3K9ac, as compared to the wild-type cells. Notably, although 30% of the probes in our microarray correspond to intergenic regions, nearly all probes affected by asf1-1 and alp13Δ reside in coding regions (Figure 3D and 3E).
PMID:21211723	FYPO:0004347	increased histone H3-K9 acetylation at protein coding gene during vegetative growth	Based on the genetic analyses, it was possible that Asf1/HIRA facilitate histone deacetylation by Clr6. Asf1 co-immunoprecipitated with Clr6 complex subunits Alp13 and Clr6 (Figure 3B). Moreover, asf1-1 and hip1Δ exhibited a substantial increase in bulk H3K9ac levels, in a manner similar to alp13Δ (Figure 3C).). To confirm this further, we performed ChIP-chip analyses of H3K9ac. Both alp13Δ and asf1-1 mutants showed widespread increase in H3K9ac, as compared to the wild-type cells. Notably, although 30% of the probes in our microarray correspond to intergenic regions, nearly all probes affected by asf1-1 and alp13Δ reside in coding regions (Figure 3D and 3E).
PMID:21211723	FYPO:0007217	decreased histone H3-K9 acetylation at protein coding gene during vegetative growth	Based on the genetic analyses, it was possible that Asf1/HIRA facilitate histone deacetylation by Clr6. Asf1 co-immunoprecipitated with Clr6 complex subunits Alp13 and Clr6 (Figure 3B). Moreover, asf1-1 and hip1Δ exhibited a substantial increase in bulk H3K9ac levels, in a manner similar to alp13Δ (Figure 3C).). To confirm this further, we performed ChIP-chip analyses of H3K9ac. Both alp13Δ and asf1-1 mutants showed widespread increase in H3K9ac, as compared to the wild-type cells. Notably, although 30% of the probes in our microarray correspond to intergenic regions, nearly all probes affected by asf1-1 and alp13Δ reside in coding regions (Figure 3D and 3E).
PMID:21211723	FYPO:0004347	increased histone H3-K9 acetylation at protein coding gene during vegetative growth	Based on the genetic analyses, it was possible that Asf1/HIRA facilitate histone deacetylation by Clr6. Asf1 co-immunoprecipitated with Clr6 complex subunits Alp13 and Clr6 (Figure 3B). Moreover, asf1-1 and hip1Δ exhibited a substantial increase in bulk H3K9ac levels, in a manner similar to alp13Δ (Figure 3C).). To confirm this further, we performed ChIP-chip analyses of H3K9ac. Both alp13Δ and asf1-1 mutants showed widespread increase in H3K9ac, as compared to the wild-type cells. Notably, although 30% of the probes in our microarray correspond to intergenic regions, nearly all probes affected by asf1-1 and alp13Δ reside in coding regions (Figure 3D and 3E).
PMID:21211723	FYPO:0003074	abolished protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPBC31F10.13c	ChIP-chip showed that Hip1 was enriched throughout heterochromatin domains in the wild-type cells (Figure 2D, 2E, and S3). In the absence of Swi6, Hip1 localization was restricted to transcribed dg/dh repeats, and it failed to spread outward to the surrounding sequences (Figure 2D, 2E, and S3).
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] high	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] high	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] high	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] high	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] low	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] low	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] high	Consistent with both TGS and cis-PTGS contributing to heterochromatin silencing, combining asf1-1 or hip1Δ with tas3Δ resulted in synergistic defects in heterochromatic silencing (Figure 3A).
PMID:21211723	FYPO:0000470	decreased mating type switching [has_severity] high	Defective mating-type switching in heterochromatin mutants results in poor iodine staining of colonies, in contrast to the dark staining of wild-type colonies (Jia et al., 2004). asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F).
PMID:21211723	FYPO:0000470	decreased mating type switching [has_severity] high	Defective mating-type switching in heterochromatin mutants results in poor iodine staining of colonies, in contrast to the dark staining of wild-type colonies (Jia et al., 2004). asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F).
PMID:21211723	FYPO:0000470	decreased mating type switching [has_severity] high	Defective mating-type switching in heterochromatin mutants results in poor iodine staining of colonies, in contrast to the dark staining of wild-type colonies (Jia et al., 2004). asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F).
PMID:21211723	FYPO:0000470	decreased mating type switching [has_severity] high	Defective mating-type switching in heterochromatin mutants results in poor iodine staining of colonies, in contrast to the dark staining of wild-type colonies (Jia et al., 2004). asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F).
PMID:21211723	FYPO:0000470	decreased mating type switching [has_severity] high	Defective mating-type switching in heterochromatin mutants results in poor iodine staining of colonies, in contrast to the dark staining of wild-type colonies (Jia et al., 2004). asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F).
PMID:21211723	FYPO:0000470	decreased mating type switching [has_severity] high	Defective mating-type switching in heterochromatin mutants results in poor iodine staining of colonies, in contrast to the dark staining of wild-type colonies (Jia et al., 2004). asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F).
PMID:21211723	FYPO:0000963	normal growth on hydroxyurea	However, both Asf1 and Clr6 complex-II mutants were not sensitive to hydoxyurea (Figure S6)
PMID:21211723	FYPO:0000963	normal growth on hydroxyurea	However, both Asf1 and Clr6 complex-II mutants were not sensitive to hydoxyurea (Figure S6)
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] low	However, when asf1-1 or hip1Δ were combined with clr6 or alp13 mutant alleles, double mutants did not show additive defects on silencing as compared to the single mutants (Figure 3A and S4).
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] low	However, when asf1-1 or hip1Δ were combined with clr6 or alp13 mutant alleles, double mutants did not show additive defects on silencing as compared to the single mutants (Figure 3A and S4).
PMID:21211723	FYPO:0005516	decreased nucleosome occupancy in euchromatin	In general, changes observed in clr3 and asf1 single mutants were weaker as compared to asf1clr3 double mutant that showed substantial reduction in the nucleosome occupancy (Figure 5).
PMID:21211723	FYPO:0008150	increased rDNA intergenic repeat RNA level	Interestingly, asf1-1, but not hip1Δ, also showed substantial increase in the levels of transcripts derived from intergenic portions of rDNA repeat loci (Figure S5B).
PMID:21211723	FYPO:0005917	increased subtelomeric heterochromatin RNA level	Moreover, asf1-1 and hip1Δ showed upregulation of sense and antisense transcripts corresponding to subtelomeric genes located within heterochromatic domains (Figure S5A).
PMID:21211723	FYPO:0005917	increased subtelomeric heterochromatin RNA level	Moreover, asf1-1 and hip1Δ showed upregulation of sense and antisense transcripts corresponding to subtelomeric genes located within heterochromatic domains (Figure S5A).
PMID:21211723	FYPO:0003557	increased antisense RNA level	Notably, asf1-1 produced a disproportionate increase in antisense transcripts - constituting a large proportion of probes upregulated. Detailed expression profiling of individual loci showed that the antisense transcripts upregulated in asf1-1 mutants were also upregulated in hip1Δ and alp13Δ cells (Figure 4A and 4B).
PMID:21211723	GO:0045815	transcription initiation-coupled chromatin remodeling	Thus, in addition to silencing heterochromatic repeats, Asf1 prevents antisense transcription at euchromatic loci.
PMID:21211723	FYPO:0000085	sensitive to camptothecin	We also found that asf1-1 cells were hypersensitive to genotoxic agents such as bleomycin, camptothecin and methylmethane sulfonate (Figure S6)
PMID:21211723	FYPO:0000089	sensitive to methyl methanesulfonate	We also found that asf1-1 cells were hypersensitive to genotoxic agents such as bleomycin, camptothecin and methylmethane sulfonate (Figure S6)
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] medium	We also found that double mutants carrying mutations in clr3 or mit1 along with either asf1-1 or hip1Δ showed cumulative derepression of repeat elements (Figure 3A and S4), indicating overlapping functions for Asf1/HIRA and SHREC.
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] high	We also found that double mutants carrying mutations in clr3 or mit1 along with either asf1-1 or hip1Δ showed cumulative derepression of repeat elements (Figure 3A and S4), indicating overlapping functions for Asf1/HIRA and SHREC.
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] high	We also found that double mutants carrying mutations in clr3 or mit1 along with either asf1-1 or hip1Δ showed cumulative derepression of repeat elements (Figure 3A and S4), indicating overlapping functions for Asf1/HIRA and SHREC.
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] high	We also found that double mutants carrying mutations in clr3 or mit1 along with either asf1-1 or hip1Δ showed cumulative derepression of repeat elements (Figure 3A and S4), indicating overlapping functions for Asf1/HIRA and SHREC.
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] low	We also found that double mutants carrying mutations in clr3 or mit1 along with either asf1-1 or hip1Δ showed cumulative derepression of repeat elements (Figure 3A and S4), indicating overlapping functions for Asf1/HIRA and SHREC.
PMID:21211723	FYPO:0007339	increased cen-dg RNA level [has_severity] high	We also found that double mutants carrying mutations in clr3 or mit1 along with either asf1-1 or hip1Δ showed cumulative derepression of repeat elements (Figure 3A and S4), indicating overlapping functions for Asf1/HIRA and SHREC.
PMID:21211723	FYPO:0008151	decreased nucleosome occupancy at centromeric heterochromatin	We observed nucleosome free regions at 5′ ends of genes followed by positioned nucleosomes in open reading frames (Figure S7A). Comparison of nucleosome occupancy across heterochromatin domains in asf1, clr3 or asf1clr3 mutant cells to wild-type cells identified several sites showing depletion of nucleosomes in mutant cells.
PMID:21211723	FYPO:0005516	decreased nucleosome occupancy in euchromatin	We observed nucleosome free regions at 5′ ends of genes followed by positioned nucleosomes in open reading frames (Figure S7A). Comparison of nucleosome occupancy across heterochromatin domains in asf1, clr3 or asf1clr3 mutant cells to wild-type cells identified several sites showing depletion of nucleosomes in mutant cells.
PMID:21211723	FYPO:0005516	decreased nucleosome occupancy in euchromatin	We observed nucleosome free regions at 5′ ends of genes followed by positioned nucleosomes in open reading frames (Figure S7A). Comparison of nucleosome occupancy across heterochromatin domains in asf1, clr3 or asf1clr3 mutant cells to wild-type cells identified several sites showing depletion of nucleosomes in mutant cells.
PMID:21211723	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth	Whereas asf1-1 cells showed slight reduction in levels of H3K9me, Swi6 and Chp2, the levels of these factors in hip1Δ appeared comparable to wild type (Figure 2A and 2B).
PMID:21211723	FYPO:0003235	normal histone H3-K9 methylation at centromere outer repeat during vegetative growth	Whereas asf1-1 cells showed slight reduction in levels of H3K9me, Swi6 and Chp2, the levels of these factors in hip1Δ appeared comparable to wild type (Figure 2A and 2B).
PMID:21211723	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	asf1-1 alleviated silencing of the ura4+ inserted at the outer centromeric repeat region (otr1R::ura4+) and within a centromere-homologous (cenH) element at the silent mat locus (Kint2::ura4+), in a manner similar to HIRA null mutants (Figure 1C).
PMID:21211723	FYPO:0000470	decreased mating type switching	asf1-1 and HIRA mutants were defective in mating-type switching, as indicated by the light iodine staining of the colonies (Figure 1F)
PMID:21211723	FYPO:0000095	sensitive to bleomycin	more sensitive to bleomycin-induced damage, as indicated by the disappearance of full- length chromosome bands and the appearance of a smear of broken DNA fragments (Figure 4E).
PMID:21215368	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1C)
PMID:21215368	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. 1C)
PMID:21215368	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	(Fig. 1C, 1E)
PMID:21215368	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. 1C, 1E)
PMID:21215368	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. 1C, 1E)
PMID:21215368	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. 1C, 1E)
PMID:21215368	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	(Fig. 1C, 1E)
PMID:21215368	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 1C, 1E)
PMID:21215368	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1C-E)
PMID:21215368	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. 1C-E)
PMID:21215368	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. 1C-E)
PMID:21215368	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. 1C-E)
PMID:21215368	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1C-E)
PMID:21215368	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. 1C-E)
PMID:21215368	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1D)
PMID:21215368	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. 1D)
PMID:21215368	FYPO:0006995	normal chromatin silencing at centromere inner repeat	(Fig. 1D, 1E)
PMID:21215368	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 1D, 1E)
PMID:21215368	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. 1D, 1E)
PMID:21215368	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1D, 1E)
PMID:21215368	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] low	(Fig. 1D, 1E)
PMID:21215368	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] low	(Fig. 1D, 1E)
PMID:21215368	FYPO:0003555	normal chromatin silencing at subtelomere	(Fig. 1D, 1E)
PMID:21215368	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 1D, 1E)
PMID:21215368	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1D, 1E)
PMID:21215368	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. 1D, 1E)
PMID:21215368	FYPO:0002358	normal histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth	(Fig. 1F)
PMID:21215368	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 1F, 7C)
PMID:21215368	FYPO:0004137	decreased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth	(Fig. 1F, 7C)
PMID:21215368	FYPO:0000846	decreased protein degradation during vegetative growth [assayed_protein] PomBase:SPCC622.16c	(Fig. 2)
PMID:21215368	FYPO:0004545	decreased proteasomal ubiquitin-dependent protein degradation [assayed_protein] PomBase:SPCC622.16c	(Fig. 2)
PMID:21215368	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC622.16c	(Fig. 4A)
PMID:21215368	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC622.16c [has_severity] medium	(Fig. 4A, 6B)
PMID:21215368	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC622.16c	(Fig. 4B)
PMID:21215368	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC622.16c	(Fig. 4B)
PMID:21215368	FYPO:0003010	increased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC622.16c	(Fig. 4C)
PMID:21215368	FYPO:0003010	increased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC622.16c	(Fig. 4C)
PMID:21215368	FYPO:0004066	increased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPCC622.16c [assayed_region] PomBase:SPBC32H8.11	(Fig. 4D)
PMID:21215368	FYPO:0004066	increased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPCC622.16c [assayed_region] PomBase:SPBC32H8.11	(Fig. 4D)
PMID:21215368	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC622.16c	(Fig. 6A)
PMID:21215368	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC622.16c [has_severity] medium	(Fig. 6B)
PMID:21215368	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC622.16c [has_severity] high	(Fig. 6B)
PMID:21215368	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC2D10.17	(Fig. 6C)
PMID:21215368	FYPO:0008422	decreased protein localization to pericentric heterochromatin [assayed_protein] PomBase:SPCC622.16c	(Fig. 6D)
PMID:21215368	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC622.16c [assayed_region] PomBase:SPBCPT2R1.07c	(Fig. 6D)
PMID:21215368	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC622.16c	(Fig. 6D)
PMID:21215368	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC622.16c	(Fig. 6E)
PMID:21215368	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	(Fig. 7A)
PMID:21215368	FYPO:0004541	increased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. 7A)
PMID:21215368	FYPO:0006995	normal chromatin silencing at centromere inner repeat	(Fig. 7A)
PMID:21215368	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 7A, 7B)
PMID:21215368	FYPO:0004376	increased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 7A, 7B)
PMID:21215368	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 7A, 7B)
PMID:21215368	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 7C)
PMID:21215368	FYPO:0006429	normal histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth	(Fig. 7C)
PMID:21215368	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 7C)
PMID:21215368	FYPO:0006995	normal chromatin silencing at centromere inner repeat	(Fig. S1B)
PMID:21215368	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	(Fig. S1B)
PMID:21215368	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. S1B)
PMID:21215368	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. S1B)
PMID:21215368	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. S1B)
PMID:21215368	FYPO:0006995	normal chromatin silencing at centromere inner repeat	(Fig. S1B)
PMID:21215368	FYPO:0006995	normal chromatin silencing at centromere inner repeat	(Fig. S1B)
PMID:21215368	FYPO:0006995	normal chromatin silencing at centromere inner repeat	(Fig. S1B)
PMID:21215368	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. S1B)
PMID:21215368	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. S1B)
PMID:21215368	FYPO:0006995	normal chromatin silencing at centromere inner repeat	(Fig. S1B)
PMID:21215368	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. S1C, S1D)
PMID:21215368	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. S1C, S1D)
PMID:21215368	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. S1C, S1D)
PMID:21215368	FYPO:0006299	increased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. S1C, S1D)
PMID:21215368	FYPO:0006299	increased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. S1C, S1D)
PMID:21215368	FYPO:0006299	increased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. S1C, S1D)
PMID:21215368	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. S1C, S1D)
PMID:21215368	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	(Fig. S1C, S1D)
PMID:21215368	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. S1C, S1D)
PMID:21215368	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. S1C, S1D)
PMID:21215368	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. S1C, S1D)
PMID:21215368	FYPO:0003555	normal chromatin silencing at subtelomere	(Fig. S1E)
PMID:21215368	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. S1E)
PMID:21215368	FYPO:0003555	normal chromatin silencing at subtelomere	(Fig. S1E)
PMID:21215368	FYPO:0003555	normal chromatin silencing at subtelomere	(Fig. S1E)
PMID:21215368	FYPO:0003555	normal chromatin silencing at subtelomere	(Fig. S1E)
PMID:21215368	FYPO:0003555	normal chromatin silencing at subtelomere	(Fig. S1E)
PMID:21215368	FYPO:0003555	normal chromatin silencing at subtelomere	(Fig. S1E)
PMID:21215368	FYPO:0003555	normal chromatin silencing at subtelomere	(Fig. S1E)
PMID:21215368	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	(Fig. S1E)
PMID:21215368	FYPO:0003555	normal chromatin silencing at subtelomere	(Fig. S1E)
PMID:21215368	FYPO:0003555	normal chromatin silencing at subtelomere	(Fig. S1E)
PMID:21215368	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1F, S1G)
PMID:21215368	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1F, S1G)
PMID:21215368	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. S1F, S1G)
PMID:21215368	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. S1F, S1G)
PMID:21215368	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. S1F, S1G)
PMID:21215368	FYPO:0004376	increased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1F, S1G)
PMID:21215368	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1F, S1G)
PMID:21215368	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1F, S1G)
PMID:21215368	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. S1F, S1G)
PMID:21215368	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. S1F, S1G)
PMID:21215368	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. S1F, S1G)
PMID:21215368	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process [has_input] PomBase:SPCC622.16c	Here we show that Cul4-Ddb1Cdt2 targets Epe1 in vivo (Figure 2) and that the putative substrate recognition subunit Cdt2 interacts with Epe1 (Figure 3).
PMID:21215368	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process [has_input] PomBase:SPCC622.16c	Here we show that Cul4-Ddb1Cdt2 targets Epe1 in vivo (Figure 2) and that the putative substrate recognition subunit Cdt2 interacts with Epe1 (Figure 3).
PMID:21217703	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1778.02 [assayed_protein] PomBase:SPAC16A10.07c [has_severity] high	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1778.02 [assayed_protein] PomBase:SPAC16A10.07c [has_severity] high	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1778.02 [assayed_protein] PomBase:SPAC16A10.07c [has_severity] high	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1778.02 [assayed_protein] PomBase:SPAC16A10.07c	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1778.02 [assayed_protein] PomBase:SPAC16A10.07c	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1778.02 [assayed_protein] PomBase:SPAC16A10.07c	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1778.02 [assayed_protein] PomBase:SPAC16A10.07c [has_severity] high	An arginine substitution of Ile379 or Leu383 of Taz1 or Ile655 of SpRap1 at the center of the hydrophobic interface completely abolished the Taz1RBM-SpRap1RCT interaction (Fig. 6a).
PMID:21217703	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] high	Consistent with the published results, deletion of taz1+ or rap1+ from yeast cells resulted in a dramatic increase in telomere length and length heterogeneity compared to wild-type cells (Fig. 6c).
PMID:21217703	FYPO:0002907	circularized chromosome during mitotic G1 phase	Three mutants (Taz1 I379R, Taz1 L383R, and Rap1 I655R) with no detectable Taz1-SpRap1 interaction clearly exhibited altered mobility bands representing intra-chromosome fusions (Fig. 6e).
PMID:21217703	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] high	Three point mutants (Taz1 I379R, Taz1 L383R, and Rap1 I655R) that completely abolished the Taz1-SpRap1 interaction in the ITC assay displayed a rap1Δ- and taz1Δ-like telomere length defect (Figs. 6b and 6c)
PMID:21256022	GO:0005515	protein binding	(comment: binding site L405 ndc80 loop)
PMID:21300781	FYPO:0001355	decreased vegetative cell population growth	(Fig. 7)
PMID:21300781	MOD:00064	N6-acetyl-L-lysine [added_by] PomBase:SPBC16A3.11 [added_during] mitotic S phase	(comment: Lysine 105 and Lysine 106 are acetylated in an Eso1 dependent manner. Psm3 acetylation on K105 K106 contribute to counteract the cohesin release activity of Wpl1)
PMID:21300781	MOD:00064	N6-acetyl-L-lysine [added_by] PomBase:SPBC16A3.11 [added_during] mitotic S phase	(comment: Lysine 105 and Lysine 106 are acetylated in an Eso1 dependent manner. Psm3 acetylation on K105 K106 contribute to counteract the cohesin release activity of Wpl1)
PMID:21300781	MOD:00064	N6-acetyl-L-lysine [present_during] mitotic G2 phase	(comment: Lysine 105 and Lysine 106 are acetylated in an Eso1 dependent manner. Psm3 acetylation on K105 K106 contribute to counteract the cohesin release activity of Wpl1)
PMID:21300781	MOD:00064	N6-acetyl-L-lysine [present_during] mitotic G2 phase	(comment: Lysine 105 and Lysine 106 are acetylated in an Eso1 dependent manner. Psm3 acetylation on K105 K106 contribute to counteract the cohesin release activity of Wpl1)
PMID:21307936	GO:0005515	protein binding	(Supp. Fig. 9A)
PMID:21317872	FYPO:0002930	decreased poly(A) tail length [assayed_using] PomBase:SPBC29A10.14	(comment: poly(A) tails longer in rrp6delta alone, but wild type not shown for meiotic cell cycle so can't annotate rrp6delta phenotype as normal or increased length)
PMID:21317872	FYPO:0002930	decreased poly(A) tail length [assayed_using] PomBase:SPBC29A10.02	(comment: poly(A) tails longer in rrp6delta alone, but wild type not shown for meiotic cell cycle so can't annotate rrp6delta phenotype as normal or increased length)
PMID:21317872	GO:0071920	cleavage body	Red1 localizes to cleavage bodies in mitotically dividing cells and cooperates with polyadenylation factors to hyperadenylate meiotic mRNAs. (A) Red1 dots co-localize with cleavage factor, Pcf11; the canonical poly(A) polymerase, Pla1; a nuclear exosome subunit, Rrp6; and a nuclear poly(A)-binding protein, Pab2.
PMID:21317872	GO:0071920	cleavage body	Red1 localizes to cleavage bodies in mitotically dividing cells and cooperates with polyadenylation factors to hyperadenylate meiotic mRNAs. (A) Red1 dots co-localize with cleavage factor, Pcf11; the canonical poly(A) polymerase, Pla1; a nuclear exosome subunit, Rrp6; and a nuclear poly(A)-binding protein, Pab2.
PMID:21317872	GO:0071920	cleavage body	Red1 localizes to cleavage bodies in mitotically dividing cells and cooperates with polyadenylation factors to hyperadenylate meiotic mRNAs. (A) Red1 dots co-localize with cleavage factor, Pcf11; the canonical poly(A) polymerase, Pla1; a nuclear exosome subunit, Rrp6; and a nuclear poly(A)-binding protein, Pab2.
PMID:21317872	GO:0071920	cleavage body	Red1 localizes to cleavage bodies in mitotically dividing cells and cooperates with polyadenylation factors to hyperadenylate meiotic mRNAs. (A) Red1 dots co-localize with cleavage factor, Pcf11; the canonical poly(A) polymerase, Pla1; a nuclear exosome subunit, Rrp6; and a nuclear poly(A)-binding protein, Pab2.
PMID:21317872	GO:0071920	cleavage body	Red1 localizes to cleavage bodies in mitotically dividing cells and cooperates with polyadenylation factors to hyperadenylate meiotic mRNAs. (A) Red1 dots co-localize with cleavage factor, Pcf11; the canonical poly(A) polymerase, Pla1; a nuclear exosome subunit, Rrp6; and a nuclear poly(A)-binding protein, Pab2.
PMID:21357609	FYPO:0000809	abnormal mitochondrion organization	(comment: Mitochondrial dye showed diffuse staining. they think it is a loss of membrane potential so the dye is not drawn in properly)
PMID:21357609	GO:0034246	mitochondrial transcription factor activity [part_of] transcription initiation at mitochondrial promoter [occurs_in] mitochondrion	(comment: Overexpression of Mtf1 and Rpo41 can induce mitochondrial transcription. Mtf1 and Rpo41 can bind and transcribe mitochondrial promoters in vitro and the initiating nucleotides were the same in vivo and in vitro. Mtf1 is required for efficient transcription.)
PMID:21376595	GO:0106006	cytoskeletal protein-membrane anchor activity [has_input] PomBase:SPAC4F8.13c [occurs_in] medial cortex [part_of] mitotic actomyosin contractile ring assembly	We conclude that Mid1p recruits Rng2p to cortical nodes at the division site and that Rng2p, in turn, recruits other components of the actomyosin ring to cortical nodes, thereby ensuring correct placement of the division site.
PMID:21376600	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC4B3.15 [assayed_protein] PomBase:SPAC23C11.16	(Fig. 1B)
PMID:21376600	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC4B3.15 [assayed_protein] PomBase:SPAC23C11.16	(Fig. 1B)
PMID:21376600	FYPO:0001838	decreased protein phosphorylation during vegetative growth [has_severity] high [assayed_protein] PomBase:SPCC4B3.15	(Fig. 1C)
PMID:21376600	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPAC23C11.16	(Fig. 1C, D and 2A, E)
PMID:21376600	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC11B10.09	(Fig. 1C, D and 2A, E)
PMID:21376600	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC4B3.15 [assayed_protein] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 1E)
PMID:21376600	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC23C11.16	(Fig. 2A and E)
PMID:21376600	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC23C11.16	(Fig. 2A and E)
PMID:21376600	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC23C11.16	(Fig. 2A and E)
PMID:21376600	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC23C11.16	(Fig. 2A and E)
PMID:21376600	MOD:00046	O-phospho-L-serine	(Fig. 2A and E)
PMID:21376600	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC23C11.16	(Fig. 2A and E)
PMID:21376600	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 50	(Fig. 2B)
PMID:21376600	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 65	(Fig. 2B)
PMID:21376600	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 17	(Fig. 2B)
PMID:21376600	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 70	(Fig. 2B)
PMID:21376600	FYPO:0001368	normal actomyosin contractile ring assembly	(Fig. 3)
PMID:21376600	FYPO:0000161	abnormal actomyosin contractile ring assembly [has_penetrance] 60	(Fig. 3C)
PMID:21376600	FYPO:0000161	abnormal actomyosin contractile ring assembly [has_penetrance] 10	(Fig. 3C)
PMID:21376600	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 60	(Fig. 3D)
PMID:21376600	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 30	(Fig. 3D)
PMID:21376600	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 20	(Fig. 3D)
PMID:21376600	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 95	(Fig. 3D)
PMID:21376600	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] 95	(Fig. 4B)
PMID:21376600	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] 60	(Fig. 4B)
PMID:21376600	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 30	(Fig. S2B)
PMID:21376600	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 20	(Fig. S2B)
PMID:21376600	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 20	(Fig. S2B)
PMID:21376600	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 20	(Fig. S2B)
PMID:21376600	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 20	(Fig. S2B)
PMID:21376600	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 30	(Fig. S2B)
PMID:21376600	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 80	(Fig. S2B)
PMID:21376600	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 80	(Fig. S2B)
PMID:21376600	FYPO:0006326	decreased protein localization to medial cortical node [has_penetrance] 60 [assayed_protein] PomBase:SPCC4B3.15	(Fig. S2E)
PMID:21376600	FYPO:0003338	abnormal actomyosin contractile ring morphology [has_penetrance] complete	(Fig. S2E)
PMID:21376600	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 60	(Fig. S3H)
PMID:21376600	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 50	(Fig. S3H)
PMID:21376600	FYPO:0002561	abolished protein localization to actomyosin contractile ring [has_penetrance] complete [assayed_protein] PomBase:SPAC23C11.16	Plo1 localization to the contractile ring was abolished in the Mid1-T517A mutant (Figures S1C and S1D; 0 of 66 mitotic T517A cells with Plo1-GFP at the contractile ring compared to 26 of 58 in control mitotic cells)
PMID:21376600	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC4B3.15 [part_of] positive regulation of mitotic actomyosin contractile ring assembly [occurs_in] nucleus	Plo1 phosphorylates several residues within the first 100 amino acids of Mid1, which directly interact with the IQGAP Rng2 [17], and influences the timing of myosin II recruitment. Plo1 thereby facilitates contractile ring assembly at mitotic onset.
PMID:21376600	GO:1903501	positive regulation of mitotic actomyosin contractile ring assembly	These data altogether reveal mechanisms by which Plo1 acts as a key temporal coordinator of contractile ring assembly events in fission yeast.
PMID:21389117	FYPO:0000587	delayed onset of sporulation	(Fig. 1B) 4 nuclei appear later than normal.
PMID:21389117	FYPO:0001000	normal cell cycle arrest in mitotic G1 phase during nitrogen starvation	(Fig. 1B) 4 nuclei appear later than normal.
PMID:21389117	FYPO:0005412	delayed onset of meiosis II	(Fig. 1B) 4 nuclei appear later than normal.
PMID:21389117	FYPO:0003379	abolished meiosis II	(Fig. 1c) no tetranucleates
PMID:21389117	FYPO:0003379	abolished meiosis II	(Fig. 2A)
PMID:21389117	FYPO:0004994	delayed onset of meiosis I [has_severity] high	(Fig. 2A)
PMID:21389117	FYPO:0003380	decreased frequency of meiosis I [has_severity] high	(Fig. 2A)
PMID:21389117	FYPO:0004994	delayed onset of meiosis I	(Fig. 2B)
PMID:21389117	FYPO:0003379	abolished meiosis II	(Fig. 2B)
PMID:21389117	FYPO:0003380	decreased frequency of meiosis I	(Fig. 2B)
PMID:21389117	GO:0031145	anaphase-promoting complex-dependent catabolic process [has_input] PomBase:SPAC5D6.08c	(Fig. 6C)
PMID:21389117	GO:0031145	anaphase-promoting complex-dependent catabolic process [has_input] PomBase:SPAC5D6.08c	(Fig. 6C)
PMID:21389117	GO:0005515	protein binding	(Fig. 7A)
PMID:21389117	GO:0005515	protein binding	(Fig. 7A)
PMID:21389117	GO:0005515	protein binding	(Fig. 7A)
PMID:21389117	GO:0005515	protein binding	(Fig. 7A)
PMID:21389117	FYPO:0005382	delayed exit from meiosis	(comment: CHECK also fzr2 &3)
PMID:21389117	GO:0031145	anaphase-promoting complex-dependent catabolic process [has_input] PomBase:SPAC5D6.08c [happens_during] meiotic anaphase I	(comment: I'm not completely sure if the Slp1-APC degrades mes1 or only ubiquitinates it, but this is most likely correct?...)
PMID:21389117	FYPO:0005382	delayed exit from meiosis	(comment: also fzr3)
PMID:21422229	GO:0008093	cytoskeletal anchor activity [part_of] mitotic actomyosin contractile ring assembly [has_input] PomBase:SPAC926.03	Rng2 subsequently recruits the myosin­II subunits Myo2 and Rlc1.
PMID:21429938	FYPO:0000581	decreased spore germination frequency [has_severity] low	(comment: cross between h+ and h- deletions, allowed to sporulate immediately)
PMID:21429938	FYPO:0000581	decreased spore germination frequency [has_severity] medium	(comment: cross between h+ and h- deletions, allowed to sporulate immediately)
PMID:21429938	FYPO:0000581	decreased spore germination frequency [has_severity] high	(comment: cross between h+ and h- deletions, allowed to sporulate immediately)
PMID:21429938	FYPO:0002485	decreased intergenic meiotic recombination	(comment: cross between h+ and h- deletions, allowed to sporulate immediately)
PMID:21436456	FYPO:0002359	normal histone H3-K9 dimethylation at telomere during vegetative growth	(Figure S3) mlo3∆ cells maintain H3K9me2 and Swi6 localization at centromeres, mating type locus and subtelomeric loci
PMID:21436456	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_protein] PomBase:SPAC664.01c	(Figure S3) mlo3∆ cells maintain H3K9me2 and Swi6 localization at centromeres, mating type locus and subtelomeric loci
PMID:21436456	FYPO:0000862	normal histone H3-K9 dimethylation at centromere during vegetative growth	(Figure S3) mlo3∆ cells maintain H3K9me2 and Swi6 localization at centromeres, mating type locus and subtelomeric loci
PMID:21436456	GO:0140746	siRNA catabolic process	(comment: vw: I did not use processing because this seems to be catabolism) Thus, in addition to creating H3K9me binding sites for RITS, Clr4 physically and functionally links RITS to Mlo3 to mediate processing of centromeric transcripts.
PMID:21436456	MOD:00663	methylated lysine [added_by] PomBase:SPBC428.08c	A methylation assay using recombinant Mlo3 carrying single- or double-mutant combinations showed that Clr4 methylates K167 of Mlo3 in vitro (Fig. 2B).
PMID:21436456	FYPO:0004488	abolished protein lysine methylation during vegetative growth [assayed_protein] PomBase:SPBC1D7.04	A methylation assay using recombinant Mlo3 carrying single- or double-mutant combinations showed that Clr4 methylates K167 of Mlo3 in vitro (Fig. 2B).
PMID:21436456	GO:0005515	protein binding	A yeast two-hybrid screen using full-length Clr4 as the bait identified Mlo3 (12) as an interacting protein (table S1). Mlo3 is related to Saccharomyces cerevisiae Yra1 and mammalian Aly/REF (13) and is required for nuclear export of RNA (13). Immunoprecipitation analysis detected Mlo3 interacting with Clr4 (Fig. 1A) and another ClrC subunit, Rik1 (fig. S1). Moreover, recombinant Mlo3 bound Clr4, and this interaction was mediated by the amino-terminal (amino acids 1 to 55) and carboxy-terminal (amino acids 134 to 199) regions of Mlo3 (fig. S2), known to bind mRNA export machinery (13). Thus, Clr4 associates with Mlo3 in vitro and in vivo.
PMID:21436456	FYPO:0003557	increased antisense RNA level	Because clr4Δ and ago1Δ enhance antisense RNA levels when combined with a variant histone h2a.zΔ (10), we examined the mlo3-A mutant transcriptome with or without H2A.Z. Like clr4Δ and ago1Δ, mlo3-A also showed weak up- regulation of antisense RNAs (4.7% genes) (fig. S9).
PMID:21436456	FYPO:0003557	increased antisense RNA level [has_severity] low	Expression profiling of mlo3Δ cells on both DNA strands showed dramatic accumulation of antisense RNAs at euchromatic loci (~23.5% of genes) (fig. S7), in particular at convergent genes (fig. S8)
PMID:21436456	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level	Further reduction in siRNAs was observed in mlo3-A H3K9R double mutant (Fig. 2D), although a residual signal seemed to be present when compared to clr4Δ.
PMID:21436456	FYPO:0005523	increased reverse centromeric outer repeat transcript level [has_severity] medium	However, mlo3Δ resulted in a considerable increase in the levels of centromeric repeat transcripts, although to a lesser extent than in clr4Δ (Fig. 1B).
PMID:21436456	FYPO:0005523	increased reverse centromeric outer repeat transcript level [has_severity] high	However, mlo3Δ resulted in a considerable increase in the levels of centromeric repeat transcripts, although to a lesser extent than in clr4Δ (Fig. 1B).
PMID:21436456	FYPO:0005523	increased reverse centromeric outer repeat transcript level [has_severity] high	However, mlo3Δ resulted in a considerable increase in the levels of centromeric repeat transcripts, although to a lesser extent than in clr4Δ (Fig. 1B).
PMID:21436456	FYPO:0005522	increased forward centromeric outer repeat transcript level	However, mlo3Δ resulted in a considerable increase in the levels of centromeric repeat transcripts, although to a lesser extent than in clr4Δ (Fig. 1B).
PMID:21436456	FYPO:0003557	increased antisense RNA level [has_severity] medium	However, the mlo3-A h2a.zΔ double mutant showed a synergistic increase in antisense RNAs (18.6% of genes) (Fig. 3C and figs. S8 and S9)Because clr4Δ and ago1Δ enhance antisense RNA levels when combined with a variant histone h2a.zΔ (10), we examined the mlo3-A mutant transcriptome with or without H2A.Z. Like clr4Δ and ago1Δ, mlo3-A also showed weak up- regulation of antisense RNAs (4.7% genes) (fig. S9).
PMID:21436456	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level	Indeed, mlo3Δ caused severe reduction in the levels of centromeric siRNAs (Fig. 1D).
PMID:21436456	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level	Interestingly, mlo3-A caused a decrease in levels of centromeric siRNA as compared to WT (Fig. 2D).
PMID:21436456	FYPO:0003557	increased antisense RNA level [assayed_transcript] PomBase:SPNCRNA.2244	Mlo3 is required for suppression of antisense RNAs targeted by Clr4 and by the exosome. (A) Strand-specific RTPCR of RNA isolated from WT and mlo3Δ
PMID:21436456	FYPO:0003557	increased antisense RNA level [assayed_transcript] PomBase:SPNCRNA.5527	Mlo3 is required for suppression of antisense RNAs targeted by Clr4 and by the exosome. (A) Strand-specific RTPCR of RNA isolated from WT and mlo3Δ
PMID:21436456	FYPO:0003557	increased antisense RNA level [assayed_transcript] PomBase:SPNCRNA.5580	Mlo3 is required for suppression of antisense RNAs targeted by Clr4 and by the exosome. (A) Strand-specific RTPCR of RNA isolated from WT and mlo3Δ
PMID:21436456	GO:0000791	euchromatin	Mlo3 showed a broad distribution at euchromatic loci and a relative depletion at heterochromatic regions (Figure S5 and S6).
PMID:21436456	GO:0016279	protein-lysine N-methyltransferase activity [has_input] PomBase:SPBC1D7.04	Recombinant Clr4 could methylate the carboxyterminal region of Mlo3, but not the amino-terminal or middle region (Fig. 2A). Within the carboxy-terminal region, lysines 165 and 167 are in a sequence context that resembles H3K9. We mutated these and lysines 179 and 180 to alanine. A methylation assay using recombinant Mlo3 carrying single- or double-mutant combinations showed that Clr4 methylates K167 of Mlo3 in vitro (Fig. 2B).
PMID:21436456	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.04 [assayed_protein] PomBase:SPAC18G6.02c	This interaction was not sensitive to DNase I and RNase A treatment but was severely compromised upon loss of Clr4 (Fig. 1C), suggesting that Clr4 connects Mlo3 to RNA interference (RNAi).
PMID:21436456	GO:0071040	nuclear polyadenylation-dependent antisense transcript catabolic process	Thus, Mlo3 physically associates with TRAMP, a complex involved in the surveillance and degradation of aberrant RNA by the exosome. In this regard, the antisense profile of mlo3Δ closely resembles that of rrp6Δ (Fig. 3, C and E, and fig. S8).
PMID:21436456	GO:0005515	protein binding [part_of] siRNA processing [occurs_in] pericentric heterochromatin	We found that Mlo3 coimmunoprecipitated with Chp1, a subunit of RITS (Fig. 1C).
PMID:21437270	FYPO:0005371	increased linear minichromosome loss during vegetative growth	(comment: ch16)
PMID:21441914	FYPO:0000085	sensitive to camptothecin	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000268	sensitive to UV during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000268	sensitive to UV during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000085	sensitive to camptothecin	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000085	sensitive to camptothecin	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000088	sensitive to hydroxyurea	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000268	sensitive to UV during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000088	sensitive to hydroxyurea	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000088	sensitive to hydroxyurea	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000085	sensitive to camptothecin	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000085	sensitive to camptothecin	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000088	sensitive to hydroxyurea	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000268	sensitive to UV during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000268	sensitive to UV during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21441914	FYPO:0000088	sensitive to hydroxyurea	(comment: no expressivity extension because of decreased growth when untreated)
PMID:21444718	FYPO:0000963	normal growth on hydroxyurea	However, like pli1 cells, SUMOD81R mutants are not appreciably sensitive to genotoxins (Fig. 4A)
PMID:21444718	FYPO:0000963	normal growth on hydroxyurea	However, like pli1 cells, SUMOD81R mutants are not appreciably sensitive to genotoxins (Fig. 4A)
PMID:21444718	FYPO:0001690	normal growth on camptothecin	However, like pli1 cells, SUMOD81R mutants are not appreciably sensitive to genotoxins (Fig. 4A)
PMID:21444718	FYPO:0001690	normal growth on camptothecin	However, like pli1 cells, SUMOD81R mutants are not appreciably sensitive to genotoxins (Fig. 4A)
PMID:21444718	FYPO:0000957	normal growth on methyl methanesulfonate	However, like pli1 cells, SUMOD81R mutants are not appreciably sensitive to genotoxins (Fig. 4A)
PMID:21444718	FYPO:0002061	inviable vegetative cell population	In addition, an nse2-SA SUMOD81R double mutant is synthetically sick and phenocopies an nse2-SA pli1 double mutant (55) (Fig. 4C).
PMID:21444718	FYPO:0000088	sensitive to hydroxyurea	In addition, we identified two mutations, P21L and F24S, at the noncovalent Ubc9:SLD2 interface that also result in HU sensitivity (Fig. 2C).
PMID:21444718	FYPO:0000088	sensitive to hydroxyurea	In addition, we identified two mutations, P21L and F24S, at the noncovalent Ubc9:SLD2 interface that also result in HU sensitivity (Fig. 2C).
PMID:21444718	FYPO:0000085	sensitive to camptothecin [has_severity] high	Interestingly, rad60E380R mutant cells are hypersensitive to the same DNA-damaging agents as nse2-SA cells (Fig. 4A).
PMID:21444718	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	Interestingly, rad60E380R mutant cells are hypersensitive to the same DNA-damaging agents as nse2-SA cells (Fig. 4A).
PMID:21444718	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	Interestingly, rad60E380R mutant cells are hypersensitive to the same DNA-damaging agents as nse2-SA cells (Fig. 4A).
PMID:21444718	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	Interestingly, rad60E380R mutant cells are hypersensitive to the same DNA-damaging agents as nse2-SA cells (Fig. 4A).
PMID:21444718	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	Interestingly, rad60E380R mutant cells are hypersensitive to the same DNA-damaging agents as nse2-SA cells (Fig. 4A).
PMID:21444718	FYPO:0000085	sensitive to camptothecin [has_severity] high	Interestingly, rad60E380R mutant cells are hypersensitive to the same DNA-damaging agents as nse2-SA cells (Fig. 4A).
PMID:21444718	FYPO:0005630	decreased cellular HMW SUMO conjugate level	Interestingly, upon STUbL inactivation SUMOD81R forms a major di-SUMO species but none of the higher-molecular- weight chains observed with wild-type SUMO (Fig. 5B).
PMID:21444718	FYPO:0000088	sensitive to hydroxyurea	K14E at the E1 binding site, which caused HU sensitivity (Fig. 2C)
PMID:21444718	FYPO:0006887	normal protein sumoylation during vegetative growth	SUMOD81R is conjugation proficient as it produced a sumoylation pattern indistinguish- able from that of the wild type (Fig. 3C).
PMID:21444718	FYPO:0000957	normal growth on methyl methanesulfonate	Strikingly, compared to SUMO , SUMOD81R cells exhibited nearly wild-type growth rates and sensitivity to genotoxins (Fig. 3D).
PMID:21444718	FYPO:0005629	increased cellular HMW SUMO conjugate level	The rad60E380R mutant exhibits elevated SUMO conjugates before and after HU treatment, which, based on the foregoing results, is most likely the result of replicative stress in the sickly rad60E380R strain. Therefore
PMID:21444718	FYPO:0001355	decreased vegetative cell population growth	Therefore, we tested for an analogous genetic interaction be- tween rad60E380R and SUMOD81R. Whereas either single mu- tant grows well, the rad60E380R SUMOD81R double mutant is extremely synthetically sick (Fig. 4B), exhibiting a similar phe- notype to the rad60E380R pli1 mutant (39).
PMID:21444718	FYPO:0001355	decreased vegetative cell population growth	Therefore, we tested for an analogous genetic interaction be- tween rad60E380R and SUMOD81R. Whereas either single mu- tant grows well, the rad60E380R SUMOD81R double mutant is extremely synthetically sick (Fig. 4B), exhibiting a similar phe- notype to the rad60E380R pli1 mutant (39).
PMID:21444718	GO:0061656	SUMO conjugating enzyme activity [has_input] PomBase:SPAC16A10.06c	These data provide compelling support for the role of Ubc9:SUMO in facilitating Pli1-dependent sumoylation, which is toxic in STUbL mutant cells.
PMID:21444718	GO:0061656	SUMO conjugating enzyme activity [has_input] PomBase:SPAC1687.05	These data provide compelling support for the role of Ubc9:SUMO in facilitating Pli1-dependent sumoylation, which is toxic in STUbL mutant cells.
PMID:21444718	GO:0016925	protein sumoylation	Thus, both Pli1 and the noncovalent Ubc9:SUMO complex are critical for bulk sumoylation but not for modifying key targets in the DNA repair response
PMID:21444718	GO:0016925	protein sumoylation	Thus, both Pli1 and the noncovalent Ubc9:SUMO complex are critical for bulk sumoylation but not for modifying key targets in the DNA repair response
PMID:21444718	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC30D11.13 [assayed_protein] PomBase:SPBC365.06	We confirmed this hypothesis through in vitro binding assays of recombinant SUMO and Ubc9/ Ubc9H20D (Fig. 3A).
PMID:21444718	FYPO:0005630	decreased cellular HMW SUMO conjugate level [has_severity] high	We next analyzed total SUMO conjugates in SUMOD81R cells by Western blotting for comparison with those in reference strains. Notably, in both SUMOD81R and pli1 cells, the wild-type pattern of SUMO conjugates was undetectable (Fig. 3E). In contrast, bulk SUMO conjugates were readily detected in cells lacking Nse2 SUMO ligase activity (nse2-SA) or the Ubc9:SLD2 complex (Fig. 3E, rad60E380R)
PMID:21444718	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC365.06 [assayed_protein] PomBase:SPAC30D11.13	We tested in vitro interaction between His6-SLD2 and recombinant wild-type GST-Ubc9 or GST-Ubc9H20D by GSH-Sepharose pulldown and Western analysis, revealing that GST-Ubc9H 2 0 D abolishes the interaction (Fig. 2A).
PMID:21444718	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC30D11.13 [assayed_protein] PomBase:SPBC1921.02	We tested in vitro interaction between His6-SLD2 and recombinant wild-type GST-Ubc9 or GST-Ubc9H20D by GSH-Sepharose pulldown and Western analysis, revealing that GST-Ubc9H20D abolishes the interaction (Fig. 2A).
PMID:21444751	FYPO:0002826	normal gamma-tubulin complex assembly	Collectively, these results indicate that in fission yeast, a ?-TuRC- like complex exists as a stable structure in vivo independent of the Mto1/2 complex
PMID:21449049	FYPO:0007100	abnormal cell cycle arrest in meiotic prophase I with clustered telomeres	mei4-N136A combined with pat1-114 was efficiently blocked at the meiosis I onset with telomere clustered at SPBs (in the bouquet configuration) at 32˚C, which arrest can be released by a temperature shift down to 25˚C.
PMID:21449049	FYPO:0007100	abnormal cell cycle arrest in meiotic prophase I with clustered telomeres	mei4-N136A combined with pat1-114 was efficiently blocked at the meiosis I onset with telomere clustered at SPBs (in the bouquet configuration) at 32˚C, which arrest can be released by a temperature shift down to 25˚C.
PMID:21450810	FYPO:0006983	abnormal termination of RNA polymerase III transcription [assayed_using] seryl_tRNA	C11-F32S was more active in yJI1 than in yYH1, while wild-type C11 had no effect (Sector 4).
PMID:21450810	FYPO:0006983	abnormal termination of RNA polymerase III transcription [assayed_using] seryl_tRNA	Rpc2-T455I was clearly more active (white) in yJI1 than in yYH1, consistent with dT(6) readthrough as expected.
PMID:21481773	GO:0004857	enzyme inhibitor activity [part_of] positive regulation of SREBP signaling pathway [happens_during] cellular response to hypoxia [has_input] PomBase:SPBC6B1.08c	(comment: CHECK inhibitor GO:0031543 peptidyl-proline dioxygenase activity) Importantly, Sre1N also failed to accumulate in NLS-ofd1 nro1Δ cells in the absence of oxygen despite the restored Ofd1 nuclear localization (Fig. 4B, lanes 10-12). Taken together, these data support previous studies and demonstrate that Nro1 functions as a direct inhibitor of Ofd1 in Sre1N
PMID:21481773	FYPO:0008205	increased protein localization to nucleus during hypoxia [assayed_protein] PomBase:SPBC19C2.09	(comment: CHECK sre1 n terminus isoform***********)In nro1Δ cells with Ofd1 retained in the cytosol due to the loss of Nro1-mediated nuclear localization, Sre1N failed to accumulate in anaerobic conditions (Fig. 4B, lanes 7-9).
PMID:21481773	FYPO:0008206	abolished protein localization to nucleus during hypoxia [assayed_protein] PomBase:SPBC19C2.09	(comment: CHECK sre1 n terminus isoform***********.) As previously reported, Sre1N accumulated in sre1N cells under anaerobic conditions (Fig. 4B, lanes 1-3)(Lee et al., 2009).
PMID:21481773	GO:0061608	nuclear import signal receptor activity [has_input] PomBase:SPCC4B3.07 [part_of] protein import into nucleus	(comment: CHECK with ofd1)
PMID:21481773	FYPO:0003189	decreased protein import into nucleus [assayed_protein] PomBase:SPBC6B1.08c	In sre1N nro1Δ cells, Ofd1 showed diffuse cytosolic staining indicating that Nro1 is required for Ofd1 nuclear localization. Staining for Ofd1 was specific as ofd1Δ cells showed no signal. Together, these results show that nuclear localization of Ofd1 is linked to Nro1.
PMID:21481773	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPBC6B1.08c	Ofd1 was enriched in the nucleus with little cytosolic staining consistent with previous findings (Fig. 3A)(
PMID:21481773	FYPO:0006099	decreased protein localization to cytoplasm [assayed_protein] PomBase:SPBC6B1.08c	Ofd1 was enriched in the nucleus with little cytosolic staining consistent with previous findings (Fig. 3A)(
PMID:21518960	FYPO:0005107	normal regulation of mitotic DNA replication initiation	(comment: assayed at ars1 and ars2004)
PMID:21518960	FYPO:0005109	premature protein localization to chromatin at replication origin [assayed_using] PomBase:SPAC17D4.02	(comment: assayed at ars1 and ars2004)
PMID:21518960	FYPO:0005107	normal regulation of mitotic DNA replication initiation	(comment: assayed at ars1 and ars2004)
PMID:21518960	FYPO:0003498	premature mitotic DNA replication initiation [has_severity] low	(comment: assayed at ars1 and ars2004, early-firing origins)
PMID:21518960	FYPO:0001249	increased origin firing efficiency	(comment: assayed at ars1 and ars2004, early-firing origins)
PMID:21518960	FYPO:0001249	increased origin firing efficiency	(comment: assayed at ars1 and ori1-200, early-firing origins; only affects origins normally bound by Mrc1)
PMID:21518960	FYPO:0003923	decreased rate of mitotic DNA replication elongation [has_severity] low	(comment: assayed elongation from ars1 and ars2004, early-firing origins)
PMID:21518960	FYPO:0005108	normal rate of mitotic DNA replication elongation	(comment: assayed elongation from ori1-200)
PMID:21518960	GO:0000785	chromatin [coincident_with] origin_of_replication [exists_during] mitotic S phase	(comment: predominantly at early-firing origins including ars1 and ars2004, but not AT1041; Mrc1 associates with origins later than MCM complex, but slightly earlier than Cdc45)
PMID:21536008	GO:0016651	oxidoreductase activity, acting on NAD(P)H	"(comment: heterologous cytc as acceptor. they had to include this as etp1 wouldn't accept an electron otherwise.) ""S. pombe does not express any endogenous mitochondrial cytochromes P450 that could act as terminal electron acceptors"""
PMID:21540296	FYPO:0002061	inviable vegetative cell population	(Fig. 1a)
PMID:21540296	FYPO:0002060	viable vegetative cell population	(Fig. 1a)
PMID:21540296	FYPO:0002061	inviable vegetative cell population	(Fig. 1a)
PMID:21540296	FYPO:0005442	abnormal telomeric DNA separation [has_penetrance] 76	(Fig. 4)
PMID:21540296	MOD:00046	O-phospho-L-serine	(Fig. 5c)
PMID:21540296	FYPO:0003970	incomplete mitotic sister chromatid segregation, with chromatin bridge [has_penetrance] 10-20	(Fig. 7a)
PMID:21540296	FYPO:0003970	incomplete mitotic sister chromatid segregation, with chromatin bridge [has_penetrance] <10	(Fig. 7a)
PMID:21540296	FYPO:0003970	incomplete mitotic sister chromatid segregation, with chromatin bridge [has_penetrance] 20-50	(Fig. 7a)
PMID:21540296	FYPO:0003970	incomplete mitotic sister chromatid segregation, with chromatin bridge [has_penetrance] 20-50	(Fig. 7a)
PMID:21540296	FYPO:0003970	incomplete mitotic sister chromatid segregation, with chromatin bridge [has_penetrance] <10	(Fig. 7a)
PMID:21540296	FYPO:0003970	incomplete mitotic sister chromatid segregation, with chromatin bridge [has_penetrance] 20-50	(Fig. 7a)
PMID:21540296	FYPO:0003844	abolished mitotic chromosome condensation [has_penetrance] high	(Figure 7c) (comment: no rescue of cnd-2)
PMID:21540296	FYPO:0001513	normal mitotic sister chromatid segregation [has_penetrance] high	(Figure 7e)
PMID:21540296	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase [has_penetrance] 100	(comment: t-shift on mitotic entry) Fig. 1c
PMID:21540296	FYPO:0005424	decreased mitotic chromosome condensation during telophase	(comment: t-shift on mitotic entry) Fig. 1c
PMID:21540296	FYPO:0001513	normal mitotic sister chromatid segregation	(comment: t-shift on mitotic entry) Fig. 1c
PMID:21540296	FYPO:0003594	normal anaphase-promoting complex-dependent protein catabolic process [assayed_using] PomBase:SPBC582.03	(comment: t-shift on mitotic entry) Fig. 1c
PMID:21540296	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase [has_penetrance] 100	(comment: t-shift on mitotic entry) Fig. 1c
PMID:21540296	FYPO:0003166	monoseptate vegetative cell with binucleate and anucleate compartments [has_penetrance] >50	(comment: t-shift on mitotic entry) Fig. 1d
PMID:21540296	FYPO:0001055	cut following normal mitotic chromosome condensation [has_penetrance] 10	(comment: t-shift on mitotic entry) Fig. 1d
PMID:21561865	MOD:00047	O-phospho-L-threonine [increased_during] cellular response to hydroxyurea	(comment: present at basal level; increased in presence of hydroxyurea)
PMID:21561865	MOD:00047	O-phospho-L-threonine [increased_during] cellular response to hydroxyurea	(comment: present at basal level; increased in presence of hydroxyurea)
PMID:21610214	GO:0043169	cation binding	(comment: sulphate)
PMID:21633354	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPCC306.03c	(comment: CHECK condensin, which subunit assayed?)
PMID:21633354	FYPO:0003075	normal protein kinase activity [assayed_using] PomBase:SPCC320.13c	(comment: H3-pS10 used to detect ark1 activity)
PMID:21633354	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPCC306.03c	(comment: all tested chromosome loci) (Fig. 2g).
PMID:21633354	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPCC306.03c	(comment: all tested chromosome loci) (Fig. 2g).
PMID:21633354	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPCC320.13c	(comment: centromeric)
PMID:21633354	FYPO:0003286	decreased mitotic chromosome condensation	(comment: decreased along arms)
PMID:21633354	FYPO:0001357	normal vegetative cell population growth	In contrast, the growth defect and TBZ sensitivity of pcs1Δ cells are not suppressed by the sfc3-1 mutation, whereas they are suppressed by an increase in kinetochore condensin (Fig. 1d).
PMID:21633354	FYPO:0000091	sensitive to thiabendazole [has_severity] low	we engineered a Cnd2-Cnp3C fusion protein, which targets kinetochores through the Cnp3C domain32, even in pcs1Δ cells. The expression of this fusion protein largely suppresses the growth defect, sensitivity to thiabendazole (TBZ, a microtubule destabilizing drug) and the incidence of lagging chromosomes in pcs1Δ cells, whereas neither Cnd2 nor Cnp3C protein alone suppresses these phenotypes (Fig. 1c and Supplementary Fig. 7). These
PMID:21652630	FYPO:0002858	increased (1->3)-beta-D-glucan level at cell tip	(Fig S4B) (comment:t septal material hanging around one cell end)
PMID:21652630	FYPO:0000421	abolished endocytosis during vegetative growth	(Fig. S5A)
PMID:21664573	FYPO:0005735	increased protein localization to kinetochore during mitotic M phase [assayed_using] PomBase:SPBC776.02c [has_penetrance] medium	(Fig. 1A)
PMID:21664573	FYPO:0005735	increased protein localization to kinetochore during mitotic M phase [assayed_using] PomBase:SPBC776.02c	(Fig. 1A)
PMID:21664573	FYPO:0005735	increased protein localization to kinetochore during mitotic M phase [assayed_using] PomBase:SPBC776.02c [has_penetrance] high	(Fig. 1A)
PMID:21664573	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint	(Fig. 2b)
PMID:21664573	FYPO:0005726	abolished deactivation of mitotic spindle assembly checkpoint	(Fig. 2b, c)
PMID:21664573	FYPO:0002061	inviable vegetative cell population	(Fig. 3A) bub3 Δklp5 double mutants arrest as inviable micro-colonies of cells
PMID:21664573	FYPO:0001234	slow vegetative cell population growth	(Fig. 3a)
PMID:21664573	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint	(Fig. 3b)
PMID:21664573	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint	(Fig. 3b)
PMID:21664573	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint	(Fig. 3b)
PMID:21664573	FYPO:0005728	normal deactivation of mitotic spindle assembly checkpoint	(Fig. 4c) (comment: NORMAL SILENCING)
PMID:21664573	FYPO:0005728	normal deactivation of mitotic spindle assembly checkpoint	(Fig. 4d) (comment: NORMAL SILENCING)
PMID:21664573	FYPO:0005728	normal deactivation of mitotic spindle assembly checkpoint	(Fig. 4d) (comment: NORMAL SILENCING)
PMID:21664573	FYPO:0002060	viable vegetative cell population	(Figure 1D, Supplemental Figure 2A)
PMID:21664573	FYPO:0002060	viable vegetative cell population	(Figure 1D, Supplemental Figure 2A)
PMID:21664573	FYPO:0002060	viable vegetative cell population	(Figure 1D, Supplemental Figure 2A)
PMID:21664573	FYPO:0002060	viable vegetative cell population	(Figure 1D, Supplemental Figure 2A)
PMID:21664573	FYPO:0005726	abolished deactivation of mitotic spindle assembly checkpoint	(Figure 4E).
PMID:21664573	FYPO:0005726	abolished deactivation of mitotic spindle assembly checkpoint	(Figure 4E).
PMID:21664573	GO:0005515	protein binding [part_of] deactivation of mitotic spindle assembly checkpoint	(Figure 5B)
PMID:21664573	GO:0005515	protein binding [part_of] mitotic sister chromatid biorientation	(Figure 5B)
PMID:21664573	GO:0005515	protein binding [part_of] mitotic sister chromatid biorientation	(Figure 5B)
PMID:21664573	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC2F12.13 [assayed_using] PomBase:SPBC776.02c	(Figure 5B)
PMID:21664573	GO:0005515	protein binding [part_of] deactivation of mitotic spindle assembly checkpoint	(Figure 5B)
PMID:21664573	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC1685.15c	(Figure 5B)
PMID:21664573	FYPO:0002060	viable vegetative cell population	(Supplemental Figure 2B)
PMID:21664573	FYPO:0002060	viable vegetative cell population	(Supplemental Figure 2B)
PMID:21664573	FYPO:0002060	viable vegetative cell population	(Supplemental Figure 2B)
PMID:21664573	FYPO:0002060	viable vegetative cell population	(Supplemental Figure 2B)
PMID:21664573	FYPO:0002061	inviable vegetative cell population	(Supplemental Figure 2B)
PMID:21664573	FYPO:0000168	abnormal mitotic spindle assembly checkpoint	(comment: CHECK ABOLISHED) Fig 2C
PMID:21664573	GO:0005515	protein binding [part_of] deactivation of mitotic spindle assembly checkpoint	(comment: CHECK in vitro) (Figure 1C, 2D)
PMID:21676862	GO:0071933	Arp2/3 complex binding	(Fig. 1)
PMID:21693583	FYPO:0006116	abolished protein localization to actin cortical patch [assayed_using] PomBase:SPBC146.13c	(Fig. 8A)
PMID:21693583	FYPO:0001234	slow vegetative cell population growth	(Fig. 8B)
PMID:21693583	FYPO:0000646	swollen vegetative cell [has_penetrance] 10	(Fig. 8B)
PMID:2170029	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(comment: CHECK high temp is permissive)
PMID:2170029	FYPO:0001757	decreased protein phosphatase activity [has_severity] medium	(comment: CHECK high temp is permissive)
PMID:2170029	FYPO:0001234	slow vegetative cell population growth	(comment: CHECK high temp is permissive)
PMID:2170029	FYPO:0001757	decreased protein phosphatase activity [has_severity] high	(comment: CHECK standard temp is restrictive)
PMID:2170029	FYPO:0002061	inviable vegetative cell population	comment: CHECK temperature restrictive for dis2cs alone)
PMID:2170029	FYPO:0002061	inviable vegetative cell population	comment: CHECK temperature restrictive for dis2cs alone)
PMID:2170029	FYPO:0001234	slow vegetative cell population growth	comment: CHECK temperature restrictive for dis2cs alone)
PMID:2170029	FYPO:0001234	slow vegetative cell population growth	comment: CHECK temperature restrictive for dis2cs alone)
PMID:2170029	FYPO:0001234	slow vegetative cell population growth	comment: CHECK temperature restrictive for dis2cs alone)
PMID:2170029	FYPO:0001234	slow vegetative cell population growth	comment: CHECK temperature restrictive for dis2cs alone)
PMID:21703453	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00047	O-phospho-L-threonine	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPAC2F7.03c	(comment: I guess some might be false positives but Sophie said it should be ok.)
PMID:21703453	GO:0051285	cell cortex of cell tip	(comment: Requires auto-phosphorylation to be restricted to cell tips -not restricted to cell tips for Pom1-6A and Pom1-KD alleles)
PMID:21703453	GO:0051286	cell tip	(comment: Requires auto-phosphorylation to be restricted to cell tips -not restricted to cell tips for Pom1-6A and Pom1-KD alleles)
PMID:21703453	GO:0051286	cell tip	(comment: Requires auto-phosphorylation to be restricted to cell tips -not restricted to cell tips for Pom1-6A and Pom1-KD alleles)
PMID:21703453	MOD:00047	O-phospho-L-threonine [removed_by] PomBase:SPBC776.02c	(comment: required for detachment from plasma membrane)
PMID:21703453	MOD:00046	O-phospho-L-serine [removed_by] PomBase:SPBC776.02c	(comment: required for detachment from plasma membrane)
PMID:21703453	GO:0005886	plasma membrane	"recombinant Pom1 N-terminus (MBP-Pom11-699) was able to bind directly to several, but not all, negatively charged lipids, namely phosphatidylserine, phosphatidylinositol phosphates, and cardiolipin in a protein-lipid overlay assay (Figure 2D). Phosphatidylserine and phosphatidylinositol phosphates are components of the plasma membrane. Cardiolipin is mostly found in the inner mitochondrial membrane, and so it is unclear whether this interaction exists in vivo. We also note that, probably due to its high global positive charge (+15.5 for MBP-Pom11-699, +25 for Pom11-699 at pH 7), MBP-Pom11-699 bound the nitrocellulose membrane, resulting in significant background. Together, these experiments suggest that Pom1 directly associates with lipids at the plasma membrane through its basic region."""
PMID:2172964	FYPO:0000761	increased conjugation frequency	(comment: both partners cyr1delta)
PMID:21757403	GO:0045022	early endosome to late endosome transport	(comment: based on the data this should really be endosome to vacuole -GO does not exist)
PMID:21775631	FYPO:0001915	abolished prospore membrane formation	(Figure 1A, Figure 5D)
PMID:21775631	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC6G9.04	(Figure S2A)
PMID:21775631	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC6G9.04	(Figure S2A)
PMID:21775631	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC6G9.04	(Figure S2A)
PMID:21775631	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC1F3.06c	(Figure S2B)
PMID:21775631	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPCC1183.12	(Figure S2B)
PMID:21775631	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPBC16C6.14	(Figure S2B)
PMID:21811607	FYPO:0001460	increased transcription from CDRE promoter in response to calcium ion	(comment: basal transcription is meaningless because emm contains calcium)
PMID:21813639	GO:0033260	nuclear DNA replication [happens_during] mitotic S phase	(comment: CHECK candidate for involved_in_or_involved_in_regulation_of qualifier)
PMID:21828039	FYPO:0006170	decreased RNA level during cellular response to copper ion starvation during meiotic cell cycle [assayed_transcript] PomBase:SPCC1393.10	(Fig. 3)
PMID:21828039	FYPO:0006146	normal RNA level during cellular response to copper ion starvation during meiotic cell cycle [assayed_transcript] PomBase:SPAPB1A11.01	(Fig. 3)
PMID:21828039	FYPO:0003805	decreased cell population growth on non-fermentable carbon source [has_severity] high	(Fig. 4B)
PMID:21828039	FYPO:0003805	decreased cell population growth on non-fermentable carbon source [has_severity] high	(Fig. 4B)
PMID:21828039	FYPO:0003805	decreased cell population growth on non-fermentable carbon source [has_severity] high	(Fig. 4B)
PMID:21828039	FYPO:0003805	decreased cell population growth on non-fermentable carbon source [has_severity] low	(Fig. 4B)
PMID:21828039	FYPO:0003284	decreased copper import [has_severity] high	(Fig. 4G)
PMID:21828039	FYPO:0003284	decreased copper import [has_severity] medium	(Fig. 4G)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21828039	PomGeneEx:0000011	RNA level increased [during] cellular response to copper ion starvation	(Table 2)
PMID:21832151	GO:0005768	endosome [exists_during] meiotic interphase II	(comment: endosomal localization requires F-actin -assayed using latrunculin A)
PMID:21847092	GO:0008270	zinc ion binding	(comment: bound by the C-terminal dsrbd domain)
PMID:21849474	FYPO:0006617	viable elongated vegetative cell with increased cell diameter	(Fig. 1A)
PMID:21849474	FYPO:0006617	viable elongated vegetative cell with increased cell diameter	(Fig. 1A)
PMID:21849474	FYPO:0006617	viable elongated vegetative cell with increased cell diameter	(Fig. 1A)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 1A)
PMID:21849474	FYPO:0006617	viable elongated vegetative cell with increased cell diameter	(Fig. 1A)
PMID:21849474	FYPO:0006617	viable elongated vegetative cell with increased cell diameter	(Fig. 1A)
PMID:21849474	FYPO:0006617	viable elongated vegetative cell with increased cell diameter	(Fig. 1A)
PMID:21849474	FYPO:0006617	viable elongated vegetative cell with increased cell diameter	(Fig. 1A)
PMID:21849474	FYPO:0006617	viable elongated vegetative cell with increased cell diameter	(Fig. 1A,2A)
PMID:21849474	FYPO:0006617	viable elongated vegetative cell with increased cell diameter	(Fig. 1A,2A)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 1B)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 1B)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 1B)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 1B)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 1B)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 1B)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 1B)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 1B)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 1B)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 1B)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 1B)
PMID:21849474	FYPO:0001293	normal cell wall biogenesis	(Fig. 2B)
PMID:21849474	FYPO:0001293	normal cell wall biogenesis	(Fig. 2B)
PMID:21849474	FYPO:0001294	normal actin cortical patch localization	(Fig. 2C)
PMID:21849474	FYPO:0001294	normal actin cortical patch localization	(Fig. 2C)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 3) (comment: CHECK no increase in cell width compared to single mutants)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter [has_severity] high	(Fig. 3) (comment: cell width is wider than either of the single mutants)
PMID:21849474	FYPO:0002380	viable spheroid vegetative cell [has_severity] high	(Fig. 3) (comment: increased cell width compared to single mutants)
PMID:21849474	FYPO:0002380	viable spheroid vegetative cell [has_severity] high	(Fig. 3) (comment: increased cell width compared to single mutants)
PMID:21849474	GO:0097575	lateral cell cortex	(Fig. 4A)
PMID:21849474	FYPO:0000644	normal protein localization during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPAC22H10.07	(Fig. 4B)
PMID:21849474	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPAC16E8.09 [has_penetrance] high	(Fig. 4B)
PMID:21849474	GO:0031520	plasma membrane of cell tip	(Fig. 4B, 8) (comment: localisation is actin dependent)
PMID:21849474	GO:0031520	plasma membrane of cell tip	(Fig. 4B, 8) (comment: localisation is actin dependent)
PMID:21849474	FYPO:0000782	mislocalized protein during vegetative growth [assayed_using] PomBase:SPAC16E8.09 [has_penetrance] high	(Fig. 4C)
PMID:21849474	FYPO:0001370	abnormal protein localization [has_penetrance] high [assayed_using] PomBase:SPAC22H10.07	(Fig. 4D)
PMID:21849474	FYPO:0000443	abnormal protein localization during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPAC22H10.07	(Fig. 4D)
PMID:21849474	FYPO:0001584	abnormal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03 [has_penetrance] medium	(Fig. 5)
PMID:21849474	FYPO:0001585	abolished protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03 [has_penetrance] high	(Fig. 5)
PMID:21849474	FYPO:0002871	decreased protein localization to growing cell tip [assayed_using] PomBase:SPAC110.03 [has_penetrance] medium	(Fig. 5)
PMID:21849474	FYPO:0001587	normal protein localization to cell tip during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPAC16E8.09	(Fig. 6A) (comment: CHECK fusion protein driven from nmt41 promoter)
PMID:21849474	FYPO:0002104	viable vegetative cell with normal cell shape [has_penetrance] high [assayed_using] PomBase:SPAC16E8.09	(Fig. 6B) (comment: CHECK fusion protein driven from nmt41 promoter)
PMID:21849474	FYPO:0003316	normal protein localization to growing cell tip [assayed_using] PomBase:SPBC1604.14c	(Fig. 6C)
PMID:21849474	FYPO:0002871	decreased protein localization to growing cell tip [assayed_using] PomBase:SPBC1604.14c	(Fig. 6C)
PMID:21849474	FYPO:0006098	abnormal protein localization to cytoplasm [assayed_using] PomBase:SPBC28E12.03	(Fig. 7A,B)
PMID:21849474	FYPO:0006536	increased protein localization to cell periphery during vegetative growth [assayed_using] PomBase:SPBC28E12.03	(Fig. 7A,B) localisation of rga4 by blt1+ is more extensive than wild type rga4 localisation but rescues the wide cell phenotype of the rga4 deletion
PMID:21849474	GO:0031520	plasma membrane of cell tip	(Fig. 9) (comment: cdc42-CRIB-GFP localisation is actin dependent and sensitive to low levels (10mM) Lat A)
PMID:21849474	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPBC28E12.03	(Figure 4A)
PMID:21849474	FYPO:0003627	normal protein localization [assayed_using] PomBase:SPBC28E12.03	(Figure 4A)
PMID:21849474	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPBC28E12.03	(Figure 4A)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0006616	viable vegetative cell with increased cell diameter	Table 1 (comment: CHECK not suppressed by sorbitol)
PMID:21849474	FYPO:0002104	viable vegetative cell with normal cell shape	Table 1 (comment: CHECK wide phenotype suppressed by sorbitol)
PMID:21849474	FYPO:0006617	viable elongated vegetative cell with increased cell diameter	Table 1A
PMID:21885283	GO:0034314	Arp2/3 complex-mediated actin nucleation	(Figure 2A)
PMID:21885283	FYPO:0000422	decreased endocytosis during vegetative growth	(Figure 2A)
PMID:21885283	FYPO:0000422	decreased endocytosis during vegetative growth	(Figure 2A)
PMID:21885283	FYPO:0006116	abolished protein localization to actin cortical patch [assayed_using] PomBase:SPBC12C2.05c	(Figure 3B)
PMID:21885283	FYPO:0005476	decreased filamentous actin level	(Figure 3B)
PMID:21885283	GO:0106006	cytoskeletal protein-membrane anchor activity [has_input] PomBase:SPAC4F10.15c [part_of] Arp2/3 complex-mediated actin nucleation	(Figure 3C)
PMID:21885283	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC12C2.05c [assayed_using] PomBase:SPAC4F10.15c	(Figure 3D)
PMID:21885283	FYPO:0006120	decreased protein localization to actin cortical patch [assayed_using] PomBase:SPAC20G8.05c	(Figure 3G)
PMID:21885283	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC20G8.05c	(Figure S1K)
PMID:21885283	FYPO:0000744	normal protein localization to actin cortical patch [assayed_using] PomBase:SPAC20G8.05c	(Figure S1K)
PMID:21885283	GO:0030479	actin cortical patch [exists_during] mitotic interphase	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	GO:0000935	division septum [exists_during] mitotic M phase	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic M phase	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	GO:0051285	cell cortex of cell tip [exists_during] mitotic M phase	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic M phase	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	GO:0030139	endocytic vesicle	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic M phase	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	GO:0030479	actin cortical patch [exists_during] mitotic interphase	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	GO:0030479	actin cortical patch [exists_during] mitotic M phase	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	GO:0030479	actin cortical patch [exists_during] mitotic interphase	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	GO:0030479	actin cortical patch [exists_during] mitotic M phase	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	GO:0005737	cytoplasm [exists_during] mitotic interphase	(Figures 1A, 1B and S1B - S1I; TableI)
PMID:21885283	FYPO:0000190	abnormal actin cortical patch localization during vegetative growth	(Figures 2I - 2K and S3G - S3O)
PMID:21885283	FYPO:0000190	abnormal actin cortical patch localization during vegetative growth	(Figures 2I - 2K and S3G - S3O)
PMID:21885283	FYPO:0006120	decreased protein localization to actin cortical patch [has_penetrance] 70-80 [assayed_using] PomBase:SPBC32H8.12c	(Figures 2L, S3P- S3R)
PMID:21885283	FYPO:0006120	decreased protein localization to actin cortical patch [has_penetrance] 70-80 [assayed_using] PomBase:SPBC32H8.12c	(Figures 2L, S3P- S3R)
PMID:21885283	FYPO:0006120	decreased protein localization to actin cortical patch [has_penetrance] 70-80 [assayed_using] PomBase:SPBC32H8.12c	(Figures 3B)
PMID:21885283	FYPO:0002061	inviable vegetative cell population	(Table II)
PMID:21885283	FYPO:0000082	decreased cell population growth at high temperature	(Table II)
PMID:21885283	FYPO:0002060	viable vegetative cell population	Table I
PMID:21885283	FYPO:0002060	viable vegetative cell population	Table I
PMID:21885283	FYPO:0002060	viable vegetative cell population	Table I
PMID:21885283	FYPO:0002060	viable vegetative cell population	Table I
PMID:21885283	FYPO:0002060	viable vegetative cell population	Table I
PMID:21885283	FYPO:0002060	viable vegetative cell population	Table II
PMID:21892171	FYPO:0006992	normal chromatin silencing at centromere otr1R	(Fig. 1a).
PMID:21892171	FYPO:0006992	normal chromatin silencing at centromere otr1R	(Supplementary Fig. 1)
PMID:21892171	FYPO:0006992	normal chromatin silencing at centromere otr1R	(Supplementary Fig. 1)
PMID:21892171	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] high	(comment: ***ABOLISHED*****) Whereas ago1Δ alleviated silencing of a ura4+ reporter inserted at an outer centromeric repeat region (otr1R::ura4+), simultaneous deletions of mlo3 and ago1 restored centromeric silencing (Fig. 1a). T
PMID:21892171	GO:0000791	euchromatin	As expected for a factor involved in mRNP formation26,30, Mlo3 interacted with a euchromatic gene (fbp1) transcript (Fig. 1f).
PMID:21892171	FYPO:0000091	sensitive to thiabendazole [has_severity] high	As expected, cells carrying ago1Δ or dcr1Δ showed severe sensitivity to TBZ, (Figure 1e)
PMID:21892171	FYPO:0000091	sensitive to thiabendazole [has_severity] low	As expected, cells carrying ago1Δ or dcr1Δ showed severe sensitivity to TBZ, (Figure 1e)
PMID:21892171	FYPO:0000091	sensitive to thiabendazole [has_severity] low	As expected, cells carrying ago1Δ or dcr1Δ showed severe sensitivity to TBZ, (Figure 1e)
PMID:21892171	FYPO:0000084	sensitive to 6-azauracil	Deletion of tfs1, which led to 6- azauracil (6-AU) sensitivity (Fig. 2a)
PMID:21892171	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_protein] PomBase:SPCC11E10.08	However, we found that simultaneous deletion of mlo3 and ago1 restored Rik1 enrichment at cenH (Fig. 6b).
PMID:21892171	GO:0000775	chromosome, centromeric region	Importantly, Mlo3 also interacted with dh transcript (Fig. 1f), consistent with results of ChIP analyses showing Mlo3 enrichment at transcribing centromeric repeats30.As expected for a factor involved in mRNP formation26,30, Mlo3 interacted with a euchromatic gene (fbp1) transcript (Fig. 1f).
PMID:21892171	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] medium	In contrast, mlo3Δ resulted in considerable restoration of H3K9me at centromeres in clr3Δ ago1Δ cells (Fig. 3b).
PMID:21892171	FYPO:0003097	abolished histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] high	More importantly, mlo3Δ restored H3K9me and Swi6 localization at otr1R::ura4+ and endogenous centromeric repeats in ago1Δ mutant (Fig. 1 c-d)
PMID:21892171	FYPO:0003235	normal histone H3-K9 methylation at centromere outer repeat during vegetative growth	More importantly, mlo3Δ restored H3K9me and Swi6 localization at otr1R::ura4+ and endogenous centromeric repeats in ago1Δ mutant (Fig. 1 c-d)
PMID:21892171	FYPO:0003235	normal histone H3-K9 methylation at centromere outer repeat during vegetative growth	More importantly, mlo3Δ restored H3K9me and Swi6 localization at otr1R::ura4+ and endogenous centromeric repeats in ago1Δ mutant (Fig. 1 c-d)
PMID:21892171	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] low	Moreover, cid14Δ suppressed the silencing defect caused by ago1Δ, as indicated by reduction in the levels of dg/dh transcript in cid14Δ ago1Δ as compared to ago1Δ (Fig. 4c).
PMID:21892171	FYPO:0003009	increased protein localization to centromere outer repeat [assayed_protein] PomBase:SPBC28F2.12 [has_severity] medium	Mutant cells lacking SHREC subunit Clr3 show marked increase in RNAPII occupancy at centromeric repeats10,11,31
PMID:21892171	FYPO:0003009	increased protein localization to centromere outer repeat [assayed_protein] PomBase:SPBC28F2.12 [has_severity] low	Mutant cells lacking SHREC subunit Clr3 show marked increase in RNAPII occupancy at centromeric repeats10,11,31
PMID:21892171	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] medium	Remarkably, loss of Cid14 subunit of TRAMP affects RNAi-independent heterochromatin formation in a manner similar to mlo3Δ. Loss of Cid14 restored H3K9me at otr1R::ura4+ and centromeric repeats in ago1Δ mutant (Fig. 4a-b).
PMID:21892171	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] low	Whereas ago1Δ alleviated silencing of a ura4+ reporter inserted at an outer centromeric repeat region (otr1R::ura4+), simultaneous deletions of mlo3 and ago1 restored centromeric silencing (Fig. 1a). T
PMID:21892171	FYPO:0004065	abnormal transcription elongation from RNA polymerase II promoter	and changes in the distribution of RNAPII at body of genes (Supplementary Fig. 3c)
PMID:21892171	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] high	combining rrp6Δ with ago1Δ largely abolished H3K9me levels at otr1R::ura4+ and dg repeats (Fig. 5c).
PMID:21892171	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] low	mlo3Δ also restored silencing and heterochromatin formation at centromeres in dcr1Δ mutant (Supplementary Fig. 2a).
PMID:21892171	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] low	resulted in variegated suppression of silencing defects in ago1Δ and dcr1Δ mutants (Fig. 2b and Supplementary Fig. 2b)
PMID:21892171	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] high	trs1delta failed to restore H3K9me at otr1R::ura4+ in clr3Δ ago1Δ cells (Fig. 3a).
PMID:21892171	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] high	trs1delta failed to restore H3K9me at otr1R::ura4+ in clr3Δ ago1Δ cells (Fig. 3a).
PMID:21892183	GO:0008017	microtubule binding [part_of] negative regulation of plus-end directed microtubule sliding	(comment: CHECK microtubule sliding brake https://www.ebi.ac.uk/interpro/entry/InterPro/IPR007882/#PUB00070924)
PMID:21920317	FYPO:0005636	delayed onset of protein localization from kinetochore to spindle during meiosis I [has_penetrance] 14 [assayed_using] PomBase:SPCC320.13c	( Figure 1B)
PMID:21920317	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 1.8	(Fig. 1D)
PMID:21920317	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 40	(Fig. 1D)
PMID:21920317	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 1.8	(Fig. 1D)
PMID:21920317	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 40	(Fig. 1D)
PMID:21920317	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 25-30	(Fig. 1D)
PMID:21920317	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 1.8	(Fig. 1D)
PMID:21920317	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 40	(Fig. 1D)
PMID:21920317	FYPO:0002219	normal chromosome disjunction at meiosis I [has_penetrance] <98.2	(Fig. 1D) although sister kinetochore sometimes split, segregation ends up mostly normal
PMID:21920317	FYPO:0002219	normal chromosome disjunction at meiosis I [has_penetrance] <98.2	(Fig. 1D) although sister kinetochore split, segregation ends up mostly normal
PMID:21920317	FYPO:0002219	normal chromosome disjunction at meiosis I [has_penetrance] <98.2	(Fig. 1D) although sister kinetochore split, segregation ends up mostly normal
PMID:21920317	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 55-60	(Fig. 4)
PMID:21920317	FYPO:0005383	normal duration of meiosis I	(Fig. 4A)
PMID:21920317	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 5	(Fig. 4B)
PMID:21920317	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 60	(Fig. 4B)
PMID:21920317	FYPO:0005642	abnormal meiotic homologous chromosome biorientation with abnormal kinetochore orientation [assayed_using] PomBase:SPCC320.13c	(Fig. 6)
PMID:21920317	FYPO:0000131	abnormal mitotic spindle elongation [has_penetrance] 14	(Figure 1A) continuous rate of spindle elongation (I)
PMID:21920317	FYPO:0005384	meiosis I metaphase/anaphase transition delay [has_penetrance] 83	(Figure 1A) phase II (metaphase) was substantially extended
PMID:21920317	FYPO:0005512	increased activation of meiosis I spindle assembly checkpoint	(Figure 1B) We found that virtually all rec12D cells (n = 240) eventually relocalized Ark1 to the spindle (Figure 1B), indicating that the SAC ultimately becomes satisfied in achiasmate meiosis.
PMID:21920317	FYPO:0003177	abnormal meiotic homologous chromosome biorientation	(Figure 1C, 1D) (comment: CHECK bipolar attachment of univalents)
PMID:21920317	FYPO:0004667	normal meiotic sister chromatid cohesion at centromere [has_penetrance] 14	(Figure S3A)
PMID:21920317	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 60-70	(comment: CHECK >inc merotelic kinetochore attachment)
PMID:21920317	GO:0031619	homologous chromosome orientation in meiotic metaphase I	(comment: prevents bipolar attachment (Ask Takeshi if this fits better rec role))
PMID:21920317	GO:0031619	homologous chromosome orientation in meiotic metaphase I	(comment: prevents bipolar attachment)
PMID:21920317	GO:0031619	homologous chromosome orientation in meiotic metaphase I	(comment: prevents bipolar attachment)
PMID:21931816	FYPO:0004067	decreased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_using] PomBase:SPBC28F2.12	(comment: Ser-2 of the heptad repeat)
PMID:21945095	GO:0000785	chromatin [coincident_with] origin_of_replication [exists_during] mitotic S phase	(comment: CHECK during mitotic DNA replication initiation)
PMID:21945095	GO:0000785	chromatin [coincident_with] origin_of_replication [exists_during] mitotic S phase	(comment: CHECK during mitotic DNA replication initiation)
PMID:21945095	GO:0000785	chromatin [coincident_with] origin_of_replication [exists_during] mitotic S phase	(comment: CHECK during mitotic DNA replication initiation)
PMID:21945095	GO:0031261	DNA replication preinitiation complex	(comment: also inferred from interaction with Cdc23 and from timing of localization to chromatin at origins)
PMID:21945095	GO:0000785	chromatin [part_of] nuclear replication fork	(comment: during replication fork processing)
PMID:21945095	GO:0000785	chromatin [part_of] nuclear replication fork	(comment: during replication fork processing)
PMID:21945095	GO:0000785	chromatin [part_of] nuclear replication fork	(comment: during replication fork processing)
PMID:21945095	GO:0000785	chromatin [part_of] nuclear replication fork	(comment: during replication fork processing)
PMID:21949882	GO:0016706	2-oxoglutarate-dependent dioxygenase activity	(comment: CHECK moved down from GO:0016706 30/8/2014 . activated_by(CHEBI:29033))
PMID:21965289	FYPO:0005726	abolished deactivation of mitotic spindle assembly checkpoint [assayed_protein] PomBase:SPBC582.03	(Figure S2A).
PMID:21965289	FYPO:0001840	increased minichromosome loss during vegetative growth [has_penetrance] 27	(Table 1).
PMID:21965289	FYPO:0001840	increased minichromosome loss during vegetative growth [has_penetrance] 25	(Table 1).
PMID:21965289	GO:0061499	outer plaque of mitotic spindle pole body [exists_during] mitotic anaphase B	During anaphase B, Nsk1 appears as two prominent dots that seem to colocalize with SPBs, before it returns to the nucleolus at the end of anaphase B, indicating that Nsk1 undergoes cell cycle-dependent changes in its localization (Figure 2A). (vw Plus that it is at the SPB-kinetochore interface)
PMID:21965289	GO:0005654	nucleoplasm [exists_during] mitotic prometaphase [exists_during] mitotic metaphase	During prometaphase and metaphase, Nsk1 localizes broadly throughout the nucleoplasm, suggesting it is released from the nucleolus at the G2/M transition (Figure 2A).
PMID:21965289	FYPO:0000443	abnormal protein localization during vegetative growth [assayed_protein] PomBase:SPAC3G9.01	FIGURE 5: Dephosphorylation of Nsk1 by Clp1 promotes its association to the kinetochore-SPB junction.
PMID:21965289	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase [has_penetrance] 9	In 9.0% of interphase Δnsk1 cells, one pair of sister kinetochores failed to cluster near the SPB during interphase (Figure 7A).
PMID:21965289	GO:0008608	attachment of spindle microtubules to kinetochore	In the absence of Nsk1, some kinetochores become detached from spindle poles during anaphase B
PMID:21965289	FYPO:0002060	viable vegetative cell population	Indeed, we found that Δdis2, but not Δnsk1, mutants suppress the proliferation defect of a temperature-sensitive ark1-T7 mutant, indicating that Nsk1 does not counteract Ark1 function (Figure S2B)
PMID:21965289	FYPO:0002061	inviable vegetative cell population	Indeed, we found that Δdis2, but not Δnsk1, mutants suppress the proliferation defect of a temperature-sensitive ark1-T7 mutant, indicating that Nsk1 does not counteract Ark1 function (Figure S2B)
PMID:21965289	FYPO:0002060	viable vegetative cell population	Indeed, we found that Δdis2, but not Δnsk1, mutants suppress the proliferation defect of a temperature-sensitive ark1-T7 mutant, indicating that Nsk1 does not counteract Ark1 function (Figure S2B)
PMID:21965289	FYPO:0002061	inviable vegetative cell population	Indeed, we found that Δdis2, but not Δnsk1, mutants suppress the proliferation defect of a temperature-sensitive ark1-T7 mutant, indicating that Nsk1 does not counteract Ark1 function (Figure S2B)
PMID:21965289	FYPO:0001840	increased minichromosome loss during vegetative growth [has_penetrance] 2.4	Nevertheless, the chromosome loss rate was considerably worse in Δnsk1 Δmad2 cells than in Δnsk1 single mutant (Table 1).
PMID:21965289	FYPO:0001840	increased minichromosome loss during vegetative growth [has_penetrance] 1	Nevertheless, the chromosome loss rate was considerably worse in Δnsk1 Δmad2 cells than in Δnsk1 single mutant (Table 1).
PMID:21965289	FYPO:0001840	increased minichromosome loss during vegetative growth [has_penetrance] 1	Nevertheless, the chromosome loss rate was considerably worse in Δnsk1 Δmad2 cells than in Δnsk1 single mutant (Table 1).
PMID:21965289	FYPO:0000141	abnormal mitotic sister chromatid segregation	Nevertheless, we found that both Δnsk1 and Δdis2 cells missegregate chromosome 1, and that this is exacerbated in Δnsk1 Δdis2 double mutants (Figure 1C).
PMID:21965289	FYPO:0000141	abnormal mitotic sister chromatid segregation	Nevertheless, we found that both Δnsk1 and Δdis2 cells missegregate chromosome 1, and that this is exacerbated in Δnsk1 Δdis2 double mutants (Figure 1C).
PMID:21965289	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase [has_penetrance] 9	Similar results were obtained when kinetochore position was assessed with other GFP-tagged kinetochore proteins and in clp1(C286S) mutant, in which relocalization of Nsk1 to the kinetochore-SPB junction is impaired (Figure S6A).
PMID:21965289	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 5	Since Δnsk1 Δdis2 double mutants displayed mitotic abnormalities, we chose Nsk1 for further analysis (Figure 1B).
PMID:21965289	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	The delay in anaphase onset observed in Δnsk1 cells is abolished by deletion of either mad2 or mad3, indicating that this is due either to activation of, or failure to silence, the SAC (Figure 1E).
PMID:21965289	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	The delay in anaphase onset observed in Δnsk1 cells is abolished by deletion of either mad2 or mad3, indicating that this is due either to activation of, or failure to silence, the SAC (Figure 1E).
PMID:21965289	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC3G9.01 [happens_during] mitotic metaphase	These data indicate that Nsk1 is phosphorylated by Cdk1/Cdc2 kinase on multiple sites in early mitosis, and this prevents Nsk1 localization to the spindle and kinetochore-SPB interface until it is dephosphorylated by Clp1 at anaphase onset.
PMID:21965289	GO:0098653	centromere clustering [happens_during] mitotic anaphase B	This strongly suggests that Nsk1 is required for accurate chromosome segregation, promoting the tethering of kinetochores to SPBs during anaphase B (see Discussion). In 9.0% of interphase Δnsk1 cells, one pair of sister kinetochores failed to cluster near the SPB during interphase (Figure 7A).
PMID:21965289	FYPO:0005728	normal deactivation of mitotic spindle assembly checkpoint [assayed_protein] PomBase:SPBC582.03	To distinguish between these possibilities, we monitored Cdc13 (Cyclin B) destruction in single cells following chemical inactivation of Ark1 (Aurora B) kinase in mitotically arrested nda3- KM311 cells. The nda3-KM311 allele encodes a cold-sensitive β-tubulin protein that causes cells to arrest in mitosis at 18°C with no microtubules (Hiraoka et al., 1984). We found that loss of nsk1 had no effect in this assay, indicating that Nsk1 is not required to silence the SAC (Figure S2A).
PMID:21965289	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC3G9.01	To our surprise, although loss of Msd1 or Alp7 had little or no effect on Nsk1 localization, we were unable to observe Nsk1 at the spindle pole in the absence of Dlc1 in fixed-cell preparations (Figure 6A).
PMID:21965289	FYPO:0005957	decreased protein dephosphorylation during vegetative growth [assayed_protein] PomBase:SPAC3G9.01	To test whether Nsk1 is dephosphorylated by the proline-directed Cdc14- like phosphatase Clp1, cell cycle-dependent modification of Nsk1 was examined in nda3-KM311 nsk1-gfp clp1(C286S) cells, which express a substrate-trapping allele of Clp1 that binds, but does not release, its phosphosubstrates (Jia et al., 1995; Chen et al., 2008). In these cells, the proportion of faster-migrating Nsk1 increases only very slowly after release into anaphase, suggesting that Clp1 dephosphorylates Nsk1 (Figure 5, A and B). Consistent with this, we found that Clp1(C286S) coimmunoprecipitates with Nsk1 from cell lysates (Figure 5C)
PMID:21965289	GO:0004722	protein serine/threonine phosphatase activity [has_input] PomBase:SPAC3G9.01 [happens_during] mitotic anaphase A	To test whether Nsk1 is dephosphorylated by the proline-directed Cdc14- like phosphatase Clp1, cell cycle-dependent modification of Nsk1 was examined in nda3-KM311 nsk1-gfp clp1(C286S) cells, which express a substrate-trapping allele of Clp1 that binds, but does not release, its phosphosubstrates (Jia et al., 1995; Chen et al., 2008). In these cells, the proportion of faster-migrating Nsk1 increases only very slowly after release into anaphase, suggesting that Clp1 dephosphorylates Nsk1 (Figure 5, A and B). Consistent with this, we found that Clp1(C286S) coimmunoprecipitates with Nsk1 from cell lysates (Figure 5C)
PMID:21965289	GO:0005730	nucleolus [exists_during] mitotic interphase	We found that Nsk1 localizes predominantly in the nucleolus during interphase, as judged by colocalization with fission yeast fibrillarin, Fib1 (Beauregard et al., 2009; Figures 2A and S3A).
PMID:21965289	FYPO:0000324	mitotic metaphase/anaphase transition delay [has_penetrance] 10	We found that both Δnsk1 and Δdis2 cells are delayed in the timing of anaphase onset and that this effect is exacerbated in Δnsk1 Δdis2 double mutants (Figure 1D).
PMID:21965289	FYPO:0000324	mitotic metaphase/anaphase transition delay [has_penetrance] 15	We found that both Δnsk1 and Δdis2 cells are delayed in the timing of anaphase onset and that this effect is exacerbated in Δnsk1 Δdis2 double mutants (Figure 1D).
PMID:21965289	FYPO:0000324	mitotic metaphase/anaphase transition delay [has_penetrance] 10	We found that both Δnsk1 and Δdis2 cells are delayed in the timing of anaphase onset and that this effect is exacerbated in Δnsk1 Δdis2 double mutants (Figure 1D).
PMID:21965289	FYPO:0005362	abnormal mitotic metaphase chromosome recapture	Whereas cells lacking Nsk1 displayed no defect in kinetochore retrieval, cells lacking either Dis2 or Dam1 were substantially impaired (Figure 8D).
PMID:21965289	GO:1902425	positive regulation of attachment of mitotic spindle microtubules to kinetochore	dis2 is required for the retreival of unclustered kinetochores in nsk delete (additive chromosome segregation defects)
PMID:21979813	GO:0033558	protein lysine deacetylase activity [has_input] PomBase:SPAC10F6.09c	(Fig. 1B)
PMID:21979813	FYPO:0000209	abnormal attachment of spindle microtubules to kinetochore during meiosis I	(Fig. 2B) (comment: CHECK abolished kinetochore mono orientation at meiosis I)
PMID:21979813	FYPO:0000209	abnormal attachment of spindle microtubules to kinetochore during meiosis I	(Fig. 2B) (comment: CHECK abolished mono orientation at meiosis I)
PMID:21979813	FYPO:0006425	normal meiotic sister chromatid cohesion at centromere during meiosis I [has_severity] high	(Fig. 2C)
PMID:21979813	FYPO:0006424	abolished meiotic sister chromatid cohesion at centromere during meiosis I [has_severity] high	(Fig. 2C)
PMID:21979813	FYPO:0006424	abolished meiotic sister chromatid cohesion at centromere during meiosis I [has_severity] high	(Fig. 2C)
PMID:21979813	FYPO:0006424	abolished meiotic sister chromatid cohesion at centromere during meiosis I [has_severity] high	(Fig. 2C)
PMID:21979813	FYPO:0006425	normal meiotic sister chromatid cohesion at centromere during meiosis I [has_penetrance] high	(Fig. 4A, 4B)
PMID:21979813	FYPO:0005642	abnormal meiotic homologous chromosome biorientation with abnormal kinetochore orientation [has_penetrance] low	(Fig. 4E) (comment: CHECK decreased kinetochore mono orientation at meiosis I)
PMID:21979813	FYPO:0005642	abnormal meiotic homologous chromosome biorientation with abnormal kinetochore orientation [has_penetrance] low	(Fig. 4E) (comment: CHECK decreased kinetochore mono orientation at meiosis I)
PMID:21979813	FYPO:0005642	abnormal meiotic homologous chromosome biorientation with abnormal kinetochore orientation [has_penetrance] low	(Fig. 4E) (comment: CHECK decreased kinetochore mono orientation at meiosis I)
PMID:21981922	FYPO:0003620	normal pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05	Analysis of RNA from cid14D cells showed normal levels of rpl30-2 pre-mRNA and mRNA (Figure 2A, lane 3, and Figures 2B and 2C)
PMID:21981922	FYPO:0003620	normal pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05	Consistent with this, rpl30-2 expression levels were unaffected in the rrp6D strain when rpl30-2 was expressed from the intronless construct (Figure 1B, lanes 4 and 6), similar to results using the pab2D mutant (Figure 1B, lane 5).
PMID:21981922	FYPO:0001908	increased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05 [has_severity] high	However, the deletion of cid14 in the pab2D strain increased the levels of rpl30-2 mRNA and pre-mRNA compared to the single pab2D strain (Figure 2A, compare lanes 2 and 4).
PMID:21981922	FYPO:0002937	decreased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05	If negative control of pre-mRNA decay is mainly responsible for the upregulation of rpl30-2 after heat shock, we predicted that rpl30-2 expression from the intronless construct, which is insensitive to Pab2/Rrp6-mediated pre-mRNA decay (Figures 1B and 1C), would not respond to heat stress. Accordingly, a wild-type strain that expressed the intronless version of rpl30-2 showed no increase in mRNA levels after heat shock (Figure 4C, lanes 1 and 2, and Figure 4D).
PMID:21981922	FYPO:0001908	increased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05 [has_severity] medium	Importantly, Pab2 variants F75R and R-to-A did not rescue the increased levels of rpl30-2 transcripts observed in the pab2D strain (Figure 3E, lanes 2-4), although the two Pab2 variants defective in poly(A) binding were expressed at levels similar to wild-type Pab2 (Figure 3F).
PMID:21981922	FYPO:0001908	increased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05 [has_severity] medium	Importantly, Pab2 variants F75R and R-to-A did not rescue the increased levels of rpl30-2 transcripts observed in the pab2D strain (Figure 3E, lanes 2-4), although the two Pab2 variants defective in poly(A) binding were expressed at levels similar to wild-type Pab2 (Figure 3F).
PMID:21981922	FYPO:0002937	decreased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05	In agreement with the direct role of Rpl30-1 in the control of rpl30-2 expression, excess Rpl30-1 resulted in decreased levels of rpl30-2 mRNA (Figure 6D, lane 4).
PMID:21981922	FYPO:0001908	increased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05 [has_severity] high	In contrast, no cumulative increase in the levels of rpl30-2 transcripts was observed in the pab2D rrp6D double-mutant strain relative to the single rrp6D strain (Figure 2A, lanes 7 and 8, and Figures 2B and 2C).
PMID:21981922	FYPO:0001908	increased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05	In contrast, the expression of nonpolyadenylated rpl30-2 from the ribozyme construct was largely insensitive to Pab2- and Rrp6-dependent degradation (Figure 3C, lanes 4-6).
PMID:21981922	FYPO:0003620	normal pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05	Interestingly, the intronless rpl30-2 construct resulted in increased levels of mRNA relative to the intron-containing construct (Figure 1B, lanes 1 and 4); yet, mRNA levels were not increased in the pab2D strain when rpl30-2 was expressed from the intronless construct (Figure 1B, lanes 4 and 5, and Figure 1C).
PMID:21981922	FYPO:0001908	increased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05 [has_severity] high	Northern blot analysis of RNA prepared from the rrp6D strain revealed robust upregulation of rpl30-2 mRNA and pre-mRNA, 5- and 18-fold, respectively (Figure 2A, lane 7, and Figures 2B and 2C)
PMID:21981922	FYPO:0002937	decreased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05	RNA level expressed from the ribosomal protein-coding gene, rpl30-2, was increased by 4.5-fold in the absence of Pab2 (Lemay et al., 2010). To independently validate this result, we compared rpl30-2 mRNA levels between wild-type and pab2D strains by northern analysis and confirmed a 3-fold incemperature-dependent upregulation of rpl30-2 required Pab2, as it was not observed in a pab2D strain that is defective in pre-mRNA decay (Figure 4A, lanes 3 and 4, and Figure 4B).
PMID:21981922	FYPO:0001908	increased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05 [has_severity] medium	RNA level expressed from the ribosomal protein-coding gene, rpl30-2, was increased by 4.5-fold in the absence of Pab2 (Lemay et al., 2010). To independently validate this result, we compared rpl30-2 mRNA levels between wild-type and pab2D strains by northern analysis and confirmed a 3-fold increase of rpl30-2 mRNA in pab2 null cells (Figure 1A, lanes 1 and 2). The use of an intron-specific probe confirmed that the slowermigrating rpl30-2 transcript is the unspliced pre-mRNA (Figure 1A, lane 4).
PMID:21981922	FYPO:0003620	normal pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05	Similar results were obtained with a conditional strain in which the genomic copy of mtr4 is expressed from the thiamine-sensitive nmt1+ promoter: depletion of Mtr4 did not affect rpl30-2 premRNA and mRNA levels (Figure 2D, compare lanes 3 and 7)
PMID:21981922	FYPO:0002926	abolished poly(A) RNA binding	Similarly, a Pab2 variant in which the 11 arginine residues within the arginine/glycine-rich domain were substituted to alanine (R-to-A) showed no poly(A) binding (Figure S3)
PMID:21981922	FYPO:0002937	decreased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05 [has_severity] high	Strikingly, we noted a 6-fold decrease in the percentage of unspliced rpl30-2 transcript in the absence of Rpl30-1 relative to the wild-type (Figure S5A)
PMID:21981922	FYPO:0001908	increased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05 [has_severity] high	however, depletion of Mtr4 in the pab2D strain increased the levels of rpl30-2 mRNA and pre-mRNA compared to the single pab2D strain (Figure 2D, compare lanes 4 and 8).
PMID:21981922	FYPO:0003620	normal pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05	primarily mediated in the nucleus, as the deletion of ski7, which encodes a cytosolic-specific exosome cofactor, did not perturb rpl30-2 expression (Figure 2A, lane 9, and Figures 2B and 2C).
PMID:21981922	FYPO:0001908	increased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05 [has_severity] high	rpl30-2 mRNA and pre-mRNA were higher in the pab2D dis3-54 double-mutant strain compared to the single dis3-54 mutant (Figure 2A, compare lanes 5 and 6, and Figures 2B and 2C).
PMID:21981922	FYPO:0003620	normal pre-mRNA level [assayed_transcript] PomBase:SPAC9G1.03c	specific to one of the two rpl30 paralogs, as the expression of rpl30-1 was unchanged in pab2D cells (Figure 1A).
PMID:21981922	FYPO:0002926	abolished poly(A) RNA binding	the ability of Pab2 to bind a poly(A) substrate was completely lost after the substitution of a conserved phenylalanine (F75R) residue within the RNA recognition motif of Pab2 (Figures S3C and S3D).
PMID:21981922	PomGeneEx:0000011	RNA level increased [during] cellular response to heat	we found a 2-fold increase in rpl30-2 mRNA levels after shifting cells growing at 25C to 37C (Figure 4A, lanes 1 and 2, and Figure 4B).
PMID:21981922	FYPO:0001908	increased pre-mRNA level [assayed_transcript] PomBase:SPAC1250.05 [has_severity] low	whereas rpl30-2 mRNA and pre-mRNA were upregulated 1.5- and 3.5- fold, respectively, using RNA from the dis3 mutant (Figure 2A, lane 5, and Figures 2B and 2C).
PMID:22017871	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_at] sterol_regulatory_element [happens_during] cellular response to hypoxia	(Fig. 7c)
PMID:22017871	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process [part_of] negative regulation of SREBP signaling pathway [has_input] PomBase:SPBC19C2.09	(comment: al: ubiquitin dependent due to need for rhp6)
PMID:22017871	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process [part_of] negative regulation of SREBP signaling pathway [has_input] PomBase:SPBC19C2.09	(comment: al: ubiquitin dependent due to need for rhp6)
PMID:22017871	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process [part_of] cellular response to hyperoxia [has_input] PomBase:SPBC19C2.09	(comment: al: ubiquitin dependent due to need for rhp6)
PMID:22024164	FYPO:0002061	inviable vegetative cell population	(comment: 30 degrees)
PMID:22024164	FYPO:0001387	loss of viability at high temperature	"(comment: 30 degrees, ""high"" compared to 25 degrees)"
PMID:22024164	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 30 degrees)
PMID:22024164	FYPO:0001357	normal vegetative cell population growth	(comment: actually 25 degrees, but calling it low to make distinction from inviable at 30)
PMID:22024164	FYPO:0001250	decreased origin firing efficiency	(comment: assayed using ars2004; not abolished as in hsk1delta alone (but single mutant not shown))
PMID:22024164	FYPO:0001250	decreased origin firing efficiency	(comment: assayed using ars2004; not abolished as in hsk1delta alone (but single mutant not shown))
PMID:22024164	FYPO:0001249	increased origin firing efficiency	(comment: at late-firing or dormant origins)
PMID:22024164	FYPO:0001249	increased origin firing efficiency	(comment: at late-firing or dormant origins; genome-wide detection)
PMID:22024164	FYPO:0001249	increased origin firing efficiency	(comment: early-firing origins; HU absent)
PMID:22024167	FYPO:0006307	decreased actin filament severing [has_severity] high	(comment: >50% activity)
PMID:22033972	GO:0032798	Swi5-Sfr1 complex	(comment: structure)
PMID:2203537	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication [has_severity] high	(Figure 3A)
PMID:2203537	FYPO:0001791	abnormal mitotic spindle pole body duplication [has_severity] high	(Figure 3A)
PMID:2203537	FYPO:0003756	multiple mitotic spindles with abolished sister chromatid separation [has_penetrance] 10-20	(Figure 3A)
PMID:2203537	FYPO:0003758	mitotic spindle elongation without chromosome separation [has_penetrance] 30	(comment: 30% at 120 min. (archery bow))
PMID:2203537	FYPO:0001055	cut following normal mitotic chromosome condensation [has_penetrance] 85	(comment: 85% at 160 min)
PMID:22042620	FYPO:0000276	monopolar mitotic spindle [has_penetrance] 88	(Fig. 1, A and B)
PMID:22042620	FYPO:0007426	abolished new mitotic spindle pole body insertion into nuclear envelope	(Fig. 3, S3) for comparative images of an inserted pro-metaphase wild-type SPB, see Fig. S1 B
PMID:22042620	GO:0006998	nuclear envelope organization	(Fig. 7)
PMID:22042620	GO:0006998	nuclear envelope organization	(Fig. 7)
PMID:22042620	FYPO:0000135	abnormal plasma membrane sterol distribution	(Fig. 7) (comment: indicated by NDB cholesterol)
PMID:22042620	FYPO:0000276	monopolar mitotic spindle [has_penetrance] 88	(Fig. S2, B and C)
PMID:22042620	FYPO:0002328	sensitive to terbinafine	(Fig. S5B)
PMID:22042620	FYPO:0002237	sensitive to cerulenin	(Fig. S5B)
PMID:22042620	FYPO:0002328	sensitive to terbinafine	(Fig. S5B)
PMID:22042620	FYPO:0002237	sensitive to cerulenin	(Fig. S5B)
PMID:22042620	FYPO:0002328	sensitive to terbinafine	(Fig. S5B)
PMID:22042620	FYPO:0002328	sensitive to terbinafine	(Fig. S5B)
PMID:22042620	FYPO:0000338	abnormal mitotic spindle	(Fig. S5B)
PMID:22042869	FYPO:0000470	decreased mating type switching [has_penetrance] high	(Fig. 2A and B)
PMID:22042869	FYPO:0000472	normal mating type switching	(Fig. 2A)
PMID:22042869	FYPO:0000472	normal mating type switching	(Fig. 2A)
PMID:22042869	FYPO:0000470	decreased mating type switching [has_penetrance] high	(Fig. 2A)
PMID:22042869	FYPO:0000470	decreased mating type switching [has_penetrance] high	(Fig. 2B)
PMID:22042869	FYPO:0000470	decreased mating type switching [has_penetrance] high	(Fig. 2B)
PMID:22042869	GO:0000785	chromatin [coincident_with] PomBase:SPAC1142.03c	(Fig. 3B)
PMID:22042869	GO:0000785	chromatin [coincident_with] PomBase:SPBC409.03	(Fig. 3B)
PMID:22042869	GO:0000785	chromatin [coincident_with] PomBase:SPAPB1A10.02	(Fig. 3B)
PMID:22042869	GO:0000785	chromatin [coincident_with] PomBase:SPAP11E10.02c	(Fig. 3B)
PMID:22042869	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC1142.03c	(Fig. 4A)
PMID:22042869	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC409.03	(Fig. 4B)
PMID:22042869	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC1142.03c	(Fig. 5)
PMID:22042869	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [assayed_region] PomBase:SPAC1142.03c [assayed_protein] PomBase:SPBC23G7.09	(Fig. 6A and B)
PMID:22042869	FYPO:0004345	decreased protein localization to chromatin at long terminal repeat [assayed_protein] PomBase:SPBC23G7.09	(Fig. 6A)
PMID:22042869	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC1142.03c [has_severity] high	(Fig. 6C)
PMID:22042869	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPBC23G7.09 [part_of] gene conversion at mating-type locus	Abp1 bound to the swi2 promoter region facilitates preferential targeting of Mc, which normally binds an M-box sequence motif to activate M-specific genes
PMID:22042869	GO:0000785	chromatin [coincident_with] solo_LTR	Abp1 is localized at the swi2 promoter (Fig. 6A), in addition to its localization at LTRs.
PMID:22042869	GO:0000785	chromatin [coincident_with] PomBase:SPAC1142.03c	Abp1 is localized at the swi2 promoter (Fig. 6A), in addition to its localization at LTRs.
PMID:22042869	GO:0000785	chromatin [coincident_with] solo_LTR	Several Mc peaks correspond to WTF (With Tf) elements on chromosome 3 and solo LTRs dispersed across the genome (Fig. 3).
PMID:22064476	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific	(comment: tested using several genes, and reporter construct to test mutations at or near splice sites)
PMID:22081013	FYPO:0004742	normal chromatin silencing at centromere outer repeat [assayed_transcript] regional_centromere_outer_repeat_transcript	(Fig. 3f)
PMID:22081013	FYPO:0004604	decreased chromatin silencing at subtelomere [assayed_transcript] PomBase:SPAC212.11 [has_severity] medium	(Fig. 3f) In marked contrast, subtelomeric tlh transcripts (Figure 3a) accumulated in chp1ΔC strains (Figure 3b,e Supplementary Figure 9).
PMID:22081013	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Fig. 3g)
PMID:22081013	FYPO:0004604	decreased chromatin silencing at subtelomere [assayed_transcript] PomBase:SPAC212.11 [has_severity] medium	In marked contrast, subtelomeric tlh transcripts (Figure 3a) accumulated in chp1ΔC strains (Figure 3b,e Supplementary Figure 9).
PMID:22081013	FYPO:0004742	normal chromatin silencing at centromere outer repeat [assayed_transcript] regional_centromere_outer_repeat_transcript	Real time PCR analyses of transcripts derived from the dg or dh outer repeats of the centromere (Figure 3a) demonstrated that whereas cells lacking Chp1 displayed strong accumulation of transcripts, centromeric heterochromatin was unaffected by the loss of the PIN domain in chp1ΔC strains (Figure 3b,c,d Supplementary Figure 9).
PMID:22084197	GO:0006284	base-excision repair	(comment: CHECK FYPO:0007229)
PMID:22085934	FYPO:0006001	abolished protein localization to P-bodies [assayed_protein] PomBase:SPBC3B9.21	(Figure 6A)
PMID:22085934	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC19A8.12	(Supplementary Figure S8C
PMID:22085934	GO:0005515	protein binding	In summary, our data show that the Edc3 and Scd6 LSm domains compete for the same Dcp2- binding motifs and that both interactions are mutually exclusive
PMID:22085934	GO:0005515	protein binding	We used Dcp2 constructs of increasing length (Figure 1D) and found that a Dcp2 region located between residues 255 and 266 is required for the interaction with Edc3 (Figure 1D, lane 3 versus lanes 1 and 2). B
PMID:22093869	FYPO:0003928	altered double-strand break repair junction in presence of persistent double-strand breaks	(comment: The phenotype is assessed by the high-throughput sequencing)
PMID:22093869	FYPO:0003928	altered double-strand break repair junction in presence of persistent double-strand breaks	(comment: The phenotype is assessed by the high-throughput sequencing)
PMID:22093869	FYPO:0003928	altered double-strand break repair junction in presence of persistent double-strand breaks	(comment: The phenotype is assessed by the high-throughput sequencing)
PMID:22093869	FYPO:0003928	altered double-strand break repair junction in presence of persistent double-strand breaks	(comment: The phenotype is assessed by the high-throughput sequencing)
PMID:22119525	FYPO:0001226	inviable mononucleate vegetative cell with mislocalized septum and anucleate compartment	(Fig. 2A)
PMID:22132152	FYPO:0001198	increased cellular calcium level	(Fig. 1,7)
PMID:22132152	FYPO:0006706	abolished calcium-transporting ATPase activity	(Fig. 2)
PMID:22132152	FYPO:0006707	decreased calcium ion transport from cytosol to endoplasmic reticulum	(Fig. 2,4)
PMID:22132152	FYPO:0001457	sensitive to tunicamycin	(Fig. 5)
PMID:22132152	FYPO:0000843	sensitive to dithiothreitol	(Fig. 5)
PMID:22132152	FYPO:0005514	protein mislocalized to vacuole [assayed_using] PomBase:SPAC22A12.15c	(Fig. 6)
PMID:22132152	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPAC22A12.15c	(Fig. 6)
PMID:22132152	FYPO:0002714	protein mislocalized to Golgi apparatus [assayed_using] PomBase:SPAC22A12.15c	(Fig. 6)
PMID:22132152	FYPO:0001758	increased protein phosphatase activity [assayed_enzyme] PomBase:SPBP4H10.04	(Fig. 8) (comment: CHECK increased calcinurin activity)
PMID:22132152	GO:0005789	endoplasmic reticulum membrane	in agreement, the corresponding fractions 15-22 isolated from the fission yeast strain expressing GFP-tagged Cta4p were immuno-reactive with anti-GFP antibodies
PMID:22134091	FYPO:0006180	increased microtubule polymerization	(Fig. 1c)
PMID:22134091	FYPO:0001400	normal interphase microtubules [has_penetrance] ~5	(Fig. 2)
PMID:22134091	FYPO:0004439	long curved mitotic spindle during anaphase [has_penetrance] ~5	(Fig. 2A,B)
PMID:22134091	FYPO:0000338	abnormal mitotic spindle [has_penetrance] ~40	(Fig. 2B)
PMID:22134091	FYPO:0000903	decreased rate of microtubule depolymerization during vegetative growth	(Fig. 3)
PMID:22134091	FYPO:0000903	decreased rate of microtubule depolymerization during vegetative growth	(Fig. 3)
PMID:22134091	FYPO:0002636	delayed onset of mitotic spindle elongation	(Fig. 7F)
PMID:22134091	FYPO:0002636	delayed onset of mitotic spindle elongation	(Fig. 7F)
PMID:22134091	FYPO:0000276	monopolar mitotic spindle	(Fig. S1B-j)
PMID:22134091	FYPO:0000964	normal growth on thiabendazole	(Fig. S2)
PMID:22134091	FYPO:0000274	increased duration of mitotic M phase	(Fig. S3A)
PMID:22134091	FYPO:0003307	increased mitotic index	(comment: 22.3%)
PMID:22134091	FYPO:0001943	abnormal microtubule binding	(comment: increased affinity)
PMID:22140232	GO:0005634	nucleus [exists_during] cellular response to glucose starvation	(Fig. 2A). We found that Ssp2-GFP mainly localized in the nucleus both in glucose-starved cells and in cells grown in glucose-rich medium
PMID:22140232	GO:0005634	nucleus [exists_during] cellular response to glucose stimulus	(Fig. 2A). We found that Ssp2-GFP mainly localized in the nucleus both in glucose-starved cells and in cells grown in glucose-rich medium
PMID:22140232	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [happens_during] cellular response to glucose stimulus [occurs_in] nucleus	(comment: OK, this MF is a bit of a stretch, but based on everything we know phenotypes, export of phosphorylated -typical TF regulation, ortholog etc, I'm confident these phenotypes can be used with curator knowledge to infer this)
PMID:22140232	FYPO:0003032	decreased RNA level during glucose starvation [assayed_using] PomBase:SPAC13F5.03c	(comment: same as ssp2delta alone)
PMID:22140232	FYPO:0001176	decreased cell population growth on sucrose carbon source	(comment: same as ssp2delta alone)
PMID:22140232	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] high	(comment: same as ssp2delta alone)
PMID:22140232	FYPO:0005742	decreased invertase activity during glucose starvation	(comment: same as ssp2delta alone)
PMID:22140232	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] high	(comment: same as ssp2delta alone)
PMID:22140232	FYPO:0003032	decreased RNA level during glucose starvation [assayed_using] PomBase:SPBC1198.14c [has_severity] high	(comment: same as ssp2delta alone)
PMID:22140232	FYPO:0005746	decreased protein export from nucleus during glucose starvation [assayed_using] PomBase:SPBC1D7.02c	(comment: same as ssp2delta alone)
PMID:22140232	FYPO:0003032	decreased RNA level during glucose starvation [assayed_using] PomBase:SPCC191.11	(comment: same as ssp2delta alone)
PMID:22140232	MOD:01455	O-phosphorylated residue [added_during] cellular response to glucose starvation [added_by] PomBase:SPCC74.03c	(comment: ssp2 inferred from mutant phenotype)
PMID:22144463	GO:1902794	siRNA-independent facultative heterochromatin formation	(comment: CHECK during vegetative growth, near genes normally expressed in meiotic cell cycle)
PMID:22144463	GO:1902794	siRNA-independent facultative heterochromatin formation	(comment: CHECK during vegetative growth, near genes normally expressed in meiotic cell cycle)
PMID:22144463	GO:1902801	regulation of siRNA-independent facultative heterochromatin formation	(comment: CHECK negative ::)
PMID:22144463	FYPO:0007213	decreased histone H3-K9 dimethylation at heterochromatin island during vegetative growth [has_severity] high	Deletion of sir2 encoding a nicotinamide adenine dinucleotide- dependent HDAC (3) caused defective H3K9me at the majority of islands (fig. S5A), but SHREC subunits were dispensable (fig. S5B).
PMID:22144463	FYPO:0007530	abolished histone H3-K9 dimethylation at heterochromatin island at meiotic gene during vegetative growth	Insertion of the mei4 DSR at the 3′ untranslated region of ura4 resulted in H3K9me at this site, especially when ura4-DSR was expressed (Fig. 2C), and ssm4 lacking its DSR failed to nucleate H3K9me (fig. S8).
PMID:22144463	FYPO:0007213	decreased histone H3-K9 dimethylation at heterochromatin island during vegetative growth [has_severity] low	The loss of Dicer (Dcr1) or Argonaute (Ago1) caused only partial or no reduction in H3K9me at heterochromatin islands except island 5, which showed considerable reduction of H3K9me (fig. S4, A and B). . Moreover, de novo targeting of H3K9me to ssm4 and mei4 occurred even in the absence of Ago1, albeit at levels lower than those of the wild type (fig. S4C), suggesting that additional RNAi-independent mechanism(s) target heterochromatin to meiotic loci. W
PMID:22144909	GO:0008353	RNA polymerase II CTD heptapeptide repeat kinase activity [has_input] PomBase:SPBC28F2.12 [part_of] regulation of transcription by RNA polymerase II [part_of] positive regulation of induction of conjugation with cellular fusion	(comment: CHECK serine 2)
PMID:22172946	FYPO:0003559	sensitive to doxorubicin [has_severity] low	(Fig. 1a)
PMID:22172946	FYPO:0003559	sensitive to doxorubicin [has_severity] low	(Fig. 1a)
PMID:22172946	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to heat	(Fig. 2)
PMID:22172946	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to heat	(Fig. 2)
PMID:22172946	MOD:00046	O-phospho-L-serine [present_during] cellular response to heat	(Fig. 3)
PMID:22173095	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPAC22E12.03c	(Fig. 7)
PMID:22173095	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC22E12.03c	(Fig. 7) (comment: sdj mutant is unstable)
PMID:22173095	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC22E12.03c	(Fig. 7) (comment: sdj mutant is unstable)
PMID:22173095	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC22E12.03c [assayed_using] PomBase:SPAC22E12.03c	(comment: CHECK abolished homodimerization) Fig. 6
PMID:22180499	FYPO:0003335	increased galactose-specific flocculation	(comment: CHECK flocculation inhibited by galactose)
PMID:22184248	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	(Fig. 1B) As shown in Fig. 1B, when Mph1-KD was expressed from pREP41, it caused a weak growth inhibition, which was partially relieved by deletion of mad2+ or mph1+, indicating that expression of Mph1-KD from pREP41 caused a weak delay in mitotic progression as well as a growth defect for a reason unrelated to the checkpoint activation. We speculate that partially degraded Mph1-KD proteins (Fig. S2B) might be toxic to some extent.
PMID:22184248	FYPO:0001234	slow vegetative cell population growth	(Fig. 1B) As shown in Fig. 1B, when Mph1-KD was expressed from pREP41, it caused a weak growth inhibition, which was partially relieved by deletion of mad2+ or mph1+, indicating that expression of Mph1-KD from pREP41 caused a weak delay in mitotic progression as well as a growth defect for a reason unrelated to the checkpoint activation. We speculate that partially degraded Mph1-KD proteins (Fig. S2B) might be toxic to some extent.
PMID:22184248	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	(Fig. 1B) As shown in Fig. 1B, when Mph1-KD was expressed from pREP41, it caused a weak growth inhibition, which was partially relieved by deletion of mad2+ or mph1+, indicating that expression of Mph1-KD from pREP41 caused a weak delay in mitotic progression as well as a growth defect for a reason unrelated to the checkpoint activation. We speculate that partially degraded Mph1-KD proteins (Fig. S2B) might be toxic to some extent.
PMID:22184248	FYPO:0002061	inviable vegetative cell population	(Fig. 1a)
PMID:22184248	FYPO:0002061	inviable vegetative cell population	(Fig. 1a)
PMID:22184248	FYPO:0002060	viable vegetative cell population	(Figure 1a)
PMID:22184248	FYPO:0002060	viable vegetative cell population	(Figure 1a)
PMID:22184248	FYPO:0002060	viable vegetative cell population	(Figure 1a)
PMID:22184248	FYPO:0002060	viable vegetative cell population	(Figure 1a)
PMID:22184248	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	As shown in Fig. 3A, expression of Mph1-Ndc80-GFP from pREP81 caused an arrest in the wild-type background.
PMID:22184248	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	As shown in Fig. 3A, expression of Mph1-Ndc80-GFP from pREP81 caused an arrest in the wild-type background.
PMID:22184248	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	It failed to cause an arrest in a strain lacking mad2+, indicating that the arrest was due to activation of the spindle checkpoint.
PMID:22184248	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	We also examined localization of Mad2. Mad2 remained on kinetochores in more than 80% of the cells, indicating that the spindle checkpoint was kept active (Fig. S1 B and C)
PMID:22184248	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	When Mad2 was turned on, the index of the chromosome condensation gradually increased from 0 to more than 50%. Binucleate cells, which passed through anaphase, however, did not increase. These results indicated that when Mad2 was turned on, the cells, which were initially at the boundary of G2/M, were arrested before anaphase (Fig. 5B).
PMID:22235339	GO:0016706	2-oxoglutarate-dependent dioxygenase activity [has_input] PomBase:SPCC622.08c	(comment: also assayed using bulk histones from calf thymus)
PMID:22235339	GO:0016706	2-oxoglutarate-dependent dioxygenase activity [has_input] PomBase:SPAC19G12.06c [happens_during] cellular response to hypoxia	(comment: also assayed using bulk histones from calf thymus)
PMID:22235339	FYPO:0004872	abolished 2-oxoglutarate dioxygenase activity [assayed_enzyme] PomBase:SPAP8A3.02c	(comment: also assayed using bulk histones from calf thymus)
PMID:22267499	FYPO:0001357	normal vegetative cell population growth	(Figure 1A)
PMID:22267499	FYPO:0001357	normal vegetative cell population growth	(Figure 1A)
PMID:22267499	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Figure 1A)
PMID:22267499	FYPO:0002061	inviable vegetative cell population	(Figure 1A)
PMID:22267499	FYPO:0001234	slow vegetative cell population growth [has_severity] low	(Figure 1A)
PMID:22267499	FYPO:0001234	slow vegetative cell population growth [has_severity] low	(Figure 1A)
PMID:22267499	FYPO:0000648	viable small vegetative cell	(Figure 4b)
PMID:22267499	FYPO:0004103	viable spherical vegetative cell	(Figure 4b)
PMID:22267499	FYPO:0004103	viable spherical vegetative cell	(Figure 4b)
PMID:22267499	FYPO:0000648	viable small vegetative cell	(Figure 4b)
PMID:22267499	FYPO:0000648	viable small vegetative cell	(Figure 4b)
PMID:22267499	FYPO:0000648	viable small vegetative cell	(Figure 4b)
PMID:22267499	FYPO:0006802	dispersed filamentous actin	(Figure 4b)
PMID:22267499	FYPO:0006802	dispersed filamentous actin	(Figure 4b)
PMID:22267499	FYPO:0006802	dispersed filamentous actin	(Figure 4b)
PMID:22267499	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 23.1	(Table 2)
PMID:22267499	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 26.2	(Table 2)
PMID:22267499	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 21.8	(Table 3)
PMID:22267499	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 20.5	(Table 3)
PMID:22267499	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 10.0	(Table 3)
PMID:22267499	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 46.1	(Table 3)
PMID:22267499	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 6.6	(Table 3)
PMID:22267499	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 48.1	(Table 3)
PMID:22267499	GO:0005737	cytoplasm	Both the GFP-Ypa1p and GFP-Ypa2p proteins showed a uniform cytoplasmic localization and a faint nuclear signal.
PMID:22267499	GO:0005737	cytoplasm	Both the GFP-Ypa1p and GFP-Ypa2p proteins showed a uniform cytoplasmic localization and a faint nuclear signal.
PMID:22267499	FYPO:0000648	viable small vegetative cell	Measurement of ypa2-D cells revealed that they divide at a reduced cell length at both the permissive and restrictive temperatures, similar to ppa2-D (Table 2).
PMID:22267499	FYPO:0002061	inviable vegetative cell population	The double mutant ppa2-6 ppa1-D was synthetically lethal (Table 4), even when tetrads were dissected at 36 and 32, the permissive temperature for ppa2-6.
PMID:22267499	FYPO:0002061	inviable vegetative cell population	The double mutant ppa2-6 ppa1-D was synthetically lethal (Table 4), even when tetrads were dissected at 36 and 32, the permissive temperature for ppa2-6.
PMID:22267499	FYPO:0002061	inviable vegetative cell population	The double mutant ppa2-6 ppa1-D was synthetically lethal (Table 4), even when tetrads were dissected at 36 and 32, the permissive temperature for ppa2-6.
PMID:22267499	FYPO:0002061	inviable vegetative cell population	The double mutant ppa2-6 ppa1-D was synthetically lethal (Table 4), even when tetrads were dissected at 36 and 32, the permissive temperature for ppa2-6.
PMID:22267499	FYPO:0002280	inviable after spore germination, single cell division	The double mutant wee1-50 ypa2-D was synthetically lethal, with the germinating spore giving rise to one or two small, rounded cells at 29 (DNS)
PMID:22267499	FYPO:0002061	inviable vegetative cell population	The double mutant wee1-50 ypa2-D was synthetically lethal, with the germinating spore giving rise to one or two small, rounded cells at 29 (DNS)
PMID:22267499	GO:0031029	regulation of septation initiation signaling	These data therefore implicate Ypa2p and Ppa2p in establishing SIN protein asymmetry during anaphase.
PMID:22267499	GO:0031029	regulation of septation initiation signaling	Together, these data lead us to conclude that Ypa2p is involved in determining the timing of mitotic commitment, establishing cell morphology, positioning of the division site, regulation of the SIN, and in completion of cytokinesis.
PMID:22267499	FYPO:0002430	inviable after spore germination, multiple cell divisions	ppa2-6 is cold sensitive and undergoes only a few divisions after a shift to 19 (Table S1, Figure 1, A and B).
PMID:22267499	FYPO:0002061	inviable vegetative cell population	ppa2-6 is cold sensitive and undergoes only a few divisions after a shift to 19 (Table S1, Figure 1, A and B).
PMID:22268381	FYPO:0000091	sensitive to thiabendazole	(Fig. 4)
PMID:22268381	FYPO:0000091	sensitive to thiabendazole	(Fig. 4)
PMID:22268381	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 6-7	(Fig. 5)
PMID:22268381	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 33	(Fig. 5)
PMID:22268381	FYPO:0001513	normal mitotic sister chromatid segregation	(Fig. 5)
PMID:22268381	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 13	(Fig. 5)
PMID:22268381	FYPO:0000220	increased centromeric outer repeat transcript level	(comment: Pericentric transcript levels are increased in sal3 mutants)
PMID:22268381	GO:0061608	nuclear import signal receptor activity [has_input] PomBase:SPAC6F12.09 [part_of] protein import into nucleus	Consistent with the scenario in which Rdp1 is a cargo for Sal3, we were able to detect stable interaction between tagged Rdp1 and Sal3 by co-immunoprecipitation (Figure 2B).
PMID:22268381	FYPO:0001424	abolished protein localization to nucleus during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPAC6F12.09	GFP-Rdp1 was not detected in the nuclei of most cells (Figure 1B).
PMID:22268381	FYPO:0001424	abolished protein localization to nucleus during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPAC6F12.09	GFP-Rdp1 was not detected in the nuclei of most cells (Figure 1B).
PMID:22268381	FYPO:0003094	decreased centromeric outer repeat transcript level	Moreover, expression of the Rdp1-SV40-NLS construct appeared to suppress centromeric transcript levels below that those found in wild type
PMID:22268381	FYPO:0003094	decreased centromeric outer repeat transcript level	Moreover, expression of the Rdp1-SV40-NLS construct appeared to suppress centromeric transcript levels below that those found in wild type
PMID:22268381	FYPO:0000838	normal protein localization to nucleus during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPCC188.13c	localization of Dcr1-GFP and GFP-Ago1 was not affected by the loss of Sal3 activity (Figure S1).
PMID:22268381	FYPO:0000838	normal protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPCC736.11	localization of Dcr1-GFP and GFP-Ago1 was not affected by the loss of Sal3 activity (Figure S1).
PMID:22279046	FYPO:0001249	increased origin firing efficiency	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000085	sensitive to camptothecin	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000088	sensitive to hydroxyurea	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000268	sensitive to UV during vegetative growth	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000268	sensitive to UV during vegetative growth	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000085	sensitive to camptothecin	(comment: same as hsk1-89 alone)
PMID:22279046	FYPO:0000088	sensitive to hydroxyurea	(comment: same as hsk1-89 alone)
PMID:22291963	GO:0005634	nucleus	(comment: CHECK in asf1-33 at higher temperature)
PMID:22291963	FYPO:0000455	increased number of double-strand break sites during vegetative growth [has_severity] low	(comment: CHECK mild expressivity)
PMID:22292001	FYPO:0000678	unequal homologous chromosome segregation	(Fig. 2)
PMID:22292001	FYPO:0006426	normal attachment of spindle microtubules to kinetochore during meiosis I	(Fig. 2)
PMID:22292001	FYPO:0007104	abnormal homologous chromosome arm segregation	(Fig. 2)
PMID:22292001	FYPO:0006419	increased duration of Rad51 focus presence during meiotic cell cycle	(Fig. 3d)
PMID:22292001	FYPO:0007105	increased duration of Rad52 focus presence during meiotic cell cycle	(Fig. 3e)
PMID:22292001	FYPO:0007105	increased duration of Rad52 focus presence during meiotic cell cycle	(Fig. 3e)
PMID:22292001	FYPO:0000678	unequal homologous chromosome segregation	(Fig. 4)
PMID:22292001	FYPO:0000913	abnormal sporulation resulting in formation of ascus containing non-uniform spores	(Figure 1a)
PMID:22292001	FYPO:0007101	bent spindle during meiosis I	(Figure 1d)
PMID:22292001	FYPO:0007103	spindle collapse during meiosis I	(Figure 1d)
PMID:22292001	FYPO:0007102	multiple spindles during meiosis II	(Figure 1d)
PMID:22292001	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Figure 5)
PMID:22292001	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Figure 5)
PMID:22292001	FYPO:0000674	normal cell population growth at high temperature	(Figure 5)
PMID:22292001	FYPO:0001164	normal growth on glucose carbon source [has_severity] medium	(Figure 5)
PMID:22292001	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Figure 5)
PMID:22292001	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Figure 5)
PMID:22292001	FYPO:0001978	bent mitotic spindle [has_penetrance] medium	(Figure 5c)
PMID:22292001	FYPO:0007106	normal mitotic spindle morphology [has_penetrance] medium	(Figure 5c)
PMID:22292001	FYPO:0001978	bent mitotic spindle [has_penetrance] low	(Figure 5c)
PMID:22292001	FYPO:0001978	bent mitotic spindle [has_penetrance] medium	(Figure 5c)
PMID:22292001	FYPO:0007102	multiple spindles during meiosis II	(Figure 5d)
PMID:22292001	FYPO:0007102	multiple spindles during meiosis II	(Figure 5d)
PMID:22292001	FYPO:0007102	multiple spindles during meiosis II	(Figure 5d)
PMID:22292001	FYPO:0007101	bent spindle during meiosis I	(comment: CHECK during meiosis I)
PMID:22292001	FYPO:0007101	bent spindle during meiosis I	(comment: CHECK during meiosis I)
PMID:22292001	FYPO:0007101	bent spindle during meiosis I	(comment: CHECK during meiosis I)
PMID:22292001	GO:0000712	resolution of meiotic recombination intermediates	"(comment: CHECK strong contender for GO's ""acts upstream of or within"" (RO:0002264) gp-term relation)"
PMID:22292001	GO:0000712	resolution of meiotic recombination intermediates	"(comment: CHECK strong contender for GO's ""acts upstream of or within"" (RO:0002264) gp-term relation)"
PMID:22328580	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to glucose starvation	(Fig. 1)
PMID:22328580	FYPO:0003151	decreased protein level during cellular response to heat [assayed_using] PomBase:SPBP8B7.21	(Fig. 3A)
PMID:22328580	FYPO:0003151	decreased protein level during cellular response to heat [assayed_using] PomBase:SPBP8B7.11	(Fig. 3A)
PMID:22328580	FYPO:0002350	normal stress granule assembly during vegetative growth	(Fig. 3B, 4A and B)
PMID:22328580	FYPO:0002350	normal stress granule assembly during vegetative growth	(Fig. 3B, 4A and B)
PMID:22328580	FYPO:0002350	normal stress granule assembly during vegetative growth	(Fig. 4D)
PMID:22328580	FYPO:0002350	normal stress granule assembly during vegetative growth	(Fig. 4D)
PMID:22328580	FYPO:0002350	normal stress granule assembly during vegetative growth	(Fig. 4D)
PMID:22328580	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to glucose starvation	(Figure 2D)
PMID:22328580	FYPO:0002350	normal stress granule assembly during vegetative growth	(Figure 4A and B)
PMID:22328580	FYPO:0002350	normal stress granule assembly during vegetative growth	(Figure 4A and B)
PMID:22328580	FYPO:0002350	normal stress granule assembly during vegetative growth	(Figure 4A and B)
PMID:22328580	FYPO:0002350	normal stress granule assembly during vegetative growth	(Figure 4A and B)
PMID:22328580	FYPO:0002350	normal stress granule assembly during vegetative growth	(Figure 4A and B)
PMID:22328580	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to glucose starvation	(Figures 5D, 6C)
PMID:22328580	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to glucose starvation	(Figures 5D, 6C)
PMID:22328580	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to glucose starvation	(Figures 5D, 6C)
PMID:22344254	FYPO:0001234	slow vegetative cell population growth	(Fig. 1A) Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	FYPO:0001234	slow vegetative cell population growth	(Fig. 1A) Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 1A) Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	FYPO:0001234	slow vegetative cell population growth	(Fig. 1A) Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	FYPO:0001234	slow vegetative cell population growth	(Fig. 1A) Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	FYPO:0001234	slow vegetative cell population growth	(Fig. 1A) Loss of Gtr1 or Gtr2 resulted in the inability of the cells to grow properly, and they divided with a doubling time longer than that of wild-type cells
PMID:22344254	FYPO:0003031	mating without nitrogen starvation	(Fig. 1B, 1C) respectively Gtr2, and in particular Gtr1, inhibit sexual differentiation in rich medium.
PMID:22344254	FYPO:0003031	mating without nitrogen starvation	(Fig. 1B, 1C) respectively Gtr2, and in particular Gtr1, inhibit sexual differentiation in rich medium.
PMID:22344254	FYPO:0000280	sterile	(Fig. 4a)
PMID:22344254	FYPO:0000280	sterile	(Fig. 4a)
PMID:22344254	GO:0000329	fungal-type vacuole membrane	(Fig. 6)
PMID:22344254	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC13G6.07c	(comment: CHECK ***********nitrogen replete/with aa. AND during aa starvation***********)vam6D mutant cells showed similar Rps6 phosphorylation levels to that of wild-type cells in the absence of amino acids. However, in contrast to wild-type cells, vam6D cells did not show an increase in Rps6 phosphorylation in the presence of amino acids.
PMID:22344254	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC13G6.07c	(comment: CHECK ********nitrogen replete/with aa)
PMID:22344254	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC13G6.07c	(comment: CHECK *****nitrogen replete/with aa*****) vam6D mutant cells showed similar Rps6 phosphorylation levels to that of wild-type cells in the absence of amino acids. However, in contrast to wild-type cells, vam6D cells did not show an increase in Rps6 phosphorylation in the presence of amino acids.
PMID:22344254	GO:0000329	fungal-type vacuole membrane	As shown in Fig. 3, GFP-Tor2, GFP-Mip1 and Pop3-GFP showed similar GFP signals that colocalized with FM4-64 staining. Thus, the three components of the TORC1 complex showed vacuolar membrane localization, independently of the presence or not of amino acids in the medium.
PMID:22344254	GO:0000329	fungal-type vacuole membrane	As shown in Fig. 3, GFP-Tor2, GFP-Mip1 and Pop3-GFP showed similar GFP signals that colocalized with FM4-64 staining. Thus, the three components of the TORC1 complex showed vacuolar membrane localization, independently of the presence or not of amino acids in the medium.
PMID:22344254	GO:0005774	vacuolar membrane	As shown in Fig. 3, GFP-Tor2, GFP-Mip1 and Pop3-GFP showed similar GFP signals that colocalized with FM4-64 staining. Thus, the three components of the TORC1 complex showed vacuolar membrane localization, independently of the presence or not of amino acids in the medium.
PMID:22344254	FYPO:0002716	normal vacuole fusion during vegetative growth	FM4-64 stained only small vesicles in the cytoplasm of vam6D cells, confirming a defect in vacuolar fusion in these cells.
PMID:22344254	FYPO:0004482	abnormal vacuole fusion during vegetative growth	FM4-64 stained only small vesicles in the cytoplasm of vam6D cells, confirming a defect in vacuolar fusion in these cells.
PMID:22344254	FYPO:0004482	abnormal vacuole fusion during vegetative growth	FM4-64 stained only small vesicles in the cytoplasm of vam6D cells, confirming a defect in vacuolar fusion in these cells.
PMID:22344254	FYPO:0001234	slow vegetative cell population growth	The doubling time of vam6D was shorter in the presence of amino acids, indicating that these cells were still able to respond, at least partially, to the presence of amino acids (Fig. 5A) and that Vam6 has an important role in regulating cell growth in S. pombe but is not essential for responding to the availability of amino acids.
PMID:22344254	GO:0000329	fungal-type vacuole membrane	The observed pattern was identical, regardless of the presence or not of amino acids in the medium. To confirm the localization to the vacuole membrane, we stained the gtr1-gfp cells with the lipophilic vacuolar membrane fluorescent dye FM4-64. As shown in Fig. 2B, Gtr1-GFP colocalized with FM4-64 staining, indicating that Gtr1-GFP is concentrated at the membranes of vacuoles in S. pombe.
PMID:22344254	GO:0000329	fungal-type vacuole membrane	The observed pattern was identical, regardless of the presence or not of amino acids in the medium. To confirm the localization to the vacuole membrane, we stained the gtr1-gfp cells with the lipophilic vacuolar membrane fluorescent dye FM4-64. As shown in Fig. 2B, Gtr1-GFP colocalized with FM4-64 staining, indicating that Gtr1-GFP is concentrated at the membranes of vacuoles in S. pombe.
PMID:22344254	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPBC337.13c [part_of] positive regulation of TORC1 signaling	These results suggest that Vam6 functions upstream of Gtr1, possibly by acting as a GEF.
PMID:22344254	FYPO:0001357	normal vegetative cell population growth	We introduced Gtr1Q61L in a vam6D background and found that the double mutant was able to grow normally (Fig. 5B), indicating that constitutively active Gtr1 rescues the cell growth defect of the vam6D mutant.
PMID:22344254	GO:1990131	Gtr1-Gtr2 GTPase complex	We observed that Gtr2-RFP co-precipitated with Gtr1 (Fig. 2D) and that the Gtr1-Gtr2 interaction was stronger in cells growing in the presence of amino acids, indicating that the formation of the heterodimer is stimulated by amino acids.
PMID:22344254	GO:0043539	protein serine/threonine kinase activator activity [has_input] PomBase:SPBC216.07c [part_of] positive regulation of TORC1 signaling [occurs_in] fungal-type vacuole membrane [happens_during] response to amino acid	the Gtr1-Gtr2 heterodimer and TORC1 are located in the vacuolar membrane independently of the presence of amino acids. However, only when amino acids are present in the medium does the Gtr1-Gtr2 heterodimer interact physically with TORC1 and activate the TOR pathway to induce cell growth and repress sexual differentiation.
PMID:22344254	GO:0043539	protein serine/threonine kinase activator activity [has_input] PomBase:SPBC216.07c [part_of] positive regulation of TORC1 signaling [occurs_in] fungal-type vacuole membrane [happens_during] response to amino acid	the Gtr1-Gtr2 heterodimer and TORC1 are located in the vacuolar membrane independently of the presence of amino acids. However, only when amino acids are present in the medium does the Gtr1-Gtr2 heterodimer interact physically with TORC1 and activate the TOR pathway to induce cell growth and repress sexual differentiation.
PMID:22344694	GO:0005515	protein binding [has_input] pap1/Ox+ [part_of] positive regulation of transcription by RNA polymerase II [happens_during] cellular response to oxidative stress	(comment: not shown direct binding but want to capture the fact that it binds the oxidised form)
PMID:22344694	GO:0005515	protein binding [has_input] pap1/Ox+ [part_of] positive regulation of transcription by RNA polymerase II [happens_during] cellular response to oxidative stress	(comment: not shown direct binding but want to capture the fact that it binds the oxidised form)
PMID:22347452	FYPO:0004045	elongated tetranucleate vegetative cell with fragmented septum	(Figure 2c)
PMID:22347452	GO:0005634	nucleus	Consistent with a role in chromatin modification, all three proteins localized to the nucleus (Figure 4A).
PMID:22347452	GO:0005634	nucleus	Consistent with a role in chromatin modification, all three proteins localized to the nucleus (Figure 4A).
PMID:22347452	GO:0005634	nucleus	Consistent with a role in chromatin modification, all three proteins localized to the nucleus (Figure 4A).
PMID:22347452	GO:0034967	Set3 complex	Taken together, these data demonstrate that Hif2p, Set3p, and Snt1p exist as part of a nuclear-localized protein complex in S. pombe.
PMID:22347452	GO:0034967	Set3 complex	Taken together, these data demonstrate that Hif2p, Set3p, and Snt1p exist as part of a nuclear-localized protein complex in S. pombe.
PMID:22347452	GO:0034967	Set3 complex	Taken together, these data demonstrate that Hif2p, Set3p, and Snt1p exist as part of a nuclear-localized protein complex in S. pombe.
PMID:22347452	FYPO:0004513	resistance to latrunculin A	This reverse genetic approach identified a strain bearing a deletion in the annotated open reading frame, SPCC1235.09, which encodes a WD repeat domain protein (Figure 1).
PMID:22349564	FYPO:0001437	normal growth on antimycin A	(Figure 1A)
PMID:22349564	FYPO:0000441	resistance to antimycin A	(Figure 1A)
PMID:22349564	FYPO:0003730	abolished cell population growth on galactose carbon source	(Figure 1A)
PMID:22349564	FYPO:0003730	abolished cell population growth on galactose carbon source	(Figure 1A)
PMID:22349564	FYPO:0003730	abolished cell population growth on galactose carbon source	(Figure 1A)
PMID:22349564	FYPO:0001437	normal growth on antimycin A	(Figure 1A)
PMID:22349564	FYPO:0007623	decreased mitochondrial respiratory chain complex III assembly	(Figure 1B)
PMID:22349564	FYPO:0007623	decreased mitochondrial respiratory chain complex III assembly	(Figure 1B)
PMID:22349564	FYPO:0004529	normal mitochondrial translation [assayed_using] PomBase:SPMIT.01	(Figure 1C)
PMID:22349564	FYPO:0004529	normal mitochondrial translation [assayed_using] PomBase:SPMIT.01	(Figure 1C)
PMID:22349564	FYPO:0004529	normal mitochondrial translation [assayed_using] PomBase:SPMIT.04	(Figure 1C)
PMID:22349564	FYPO:0004529	normal mitochondrial translation [assayed_using] PomBase:SPMIT.05	(Figure 1C)
PMID:22349564	FYPO:0004529	normal mitochondrial translation [assayed_using] PomBase:SPMIT.04	(Figure 1C)
PMID:22349564	FYPO:0004529	normal mitochondrial translation [assayed_using] PomBase:SPMIT.05	(Figure 1C)
PMID:22349564	FYPO:0004960	normal mitochondrial RNA level [assayed_using] PomBase:SPMIT.11	(Figure 2A) Both the cytb and cox2 mRNAs were present at normal levels in the Δcbp6 mutant
PMID:22349564	FYPO:0004960	normal mitochondrial RNA level [assayed_using] PomBase:SPMIT.05	(Figure 2A) Both the cytb and cox2 mRNAs were present at normal levels in the Δcbp6 mutant
PMID:22349564	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.11	(Figure 2C) Thus, virtually all of the Cytb protein synthesized in the Δcbp6 mutant is degraded
PMID:22349564	FYPO:0007623	decreased mitochondrial respiratory chain complex III assembly	(Figure 2D) In both Δcbp6 and control Δcytb mitochondria, complex III was completely lacking (lanes 3 and 4)
PMID:22349564	FYPO:0003730	abolished cell population growth on galactose carbon source	(Figure 4B) A deletion mutants showed a clear growth defect on galactose medium
PMID:22349564	FYPO:0001938	decreased cytochrome-c oxidase activity	(Figure 5E)
PMID:22349564	GO:0005739	mitochondrion	(Figure S4A, B, C)
PMID:22349564	FYPO:0004529	normal mitochondrial translation [assayed_using] PomBase:SPMIT.01	As expected, Δppr4 cells clearly lacked Cox1
PMID:22349564	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.01	Cox1 was clearly less stable in the Δmss51 mutant than in the wild-type, while Cox2 was poorly labeled in the mutant even before starting the chase, as noted before (Figure 5C).
PMID:22349564	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.11	Cox2 was detectable in Δmss51 purified mitochondria, although its level was greatly reduced (Figure 5C), consistent with the reduced 35S labeling (Figure 5A)
PMID:22349564	FYPO:0004529	normal mitochondrial translation [assayed_using] PomBase:SPMIT.05	Cytb, Cox1, 2 and 3 were clearly visible, although Cox2 was less strongly labeled in both mutants, especially Δmss51 (Figure 5A)
PMID:22349564	FYPO:0004529	normal mitochondrial translation [assayed_using] PomBase:SPMIT.04	Cytb, Cox1, 2 and 3 were clearly visible, although Cox2 was less strongly labeled in both mutants, especially Δmss51 (Figure 5A)
PMID:22349564	FYPO:0004529	normal mitochondrial translation [assayed_using] PomBase:SPMIT.01	Cytb, Cox1, 2 and 3 were clearly visible, although Cox2 was less strongly labeled in both mutants, especially Δmss51 (Figure 5A)
PMID:22349564	FYPO:0004960	normal mitochondrial RNA level [assayed_using] PomBase:SPMIT.01	Northern blots revealed no defect in the accumulation of mature messengers (Figure 5B)
PMID:22349564	FYPO:0004960	normal mitochondrial RNA level [assayed_using] PomBase:SPMIT.11	Northern blots revealed no defect in the accumulation of mature messengers (Figure 5B)
PMID:22349564	FYPO:0000441	resistance to antimycin A	Similarly to the Δcbp3 and Δcbp6 mutants, Δmss51 cells were resistant to antimycin A on glucose medium, showing that they contain a functional complex V
PMID:22349564	GO:0031966	mitochondrial membrane	The tagged Mss51 was detected only in the mitochondrial fraction and like Cox2 was strongly resistant to carbonate extraction (Figure 4A), indicating that it is a membrane protein.
PMID:22349564	FYPO:0007623	decreased mitochondrial respiratory chain complex III assembly [has_severity] high	absent respiratory complex III Figure 2D In both Δcbp6 and control Δcytb mitochondria, complex III was completely lacking (lanes 3 and 4)
PMID:22349564	FYPO:0007122	decreased mitochondrial respiratory chain complex assembly [has_severity] high	absent respiratory complex III. Figure 2D As expected, the higher molecular weight bands of complex III were absent in the Δppr4 mutant, which lacks complex IV
PMID:22349564	FYPO:0007624	decreased mitochondrial respiratory chain complex IV assembly	Δmss51 cells showed normal cytochrome b and c1 peaks, but cytochromes aa3 were not detectable.
PMID:22354040	GO:0042162	telomeric repeat DNA binding	(Fig. 7)
PMID:22354040	FYPO:0005649	increased duration of protein localization to telomere [assayed_using] PomBase:SPBC660.13c	(Fig. 7A)
PMID:22354040	FYPO:0002134	decreased protein-RNA interaction [assayed_using] telomerase_RNA	(Fig. 7B)
PMID:22354040	GO:0070034	telomerase RNA binding [has_input] PomBase:SPNCRNA.214	(Fig. 7B)
PMID:22354040	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPNCRNA.214 [assayed_using] PomBase:SPBC660.13c	(Fig. 7c)
PMID:22354040	FYPO:0002239	shortened telomeres during vegetative growth	(Figure 8A)
PMID:22375066	GO:0140648	positive regulation of cell cycle switching, mitotic to meiotic cell cycle	AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	GO:0010514	induction of conjugation with cellular fusion	AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	GO:0010514	induction of conjugation with cellular fusion	AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	GO:0140648	positive regulation of cell cycle switching, mitotic to meiotic cell cycle	AMPK is required for proper advance entry into mitosis in nitrogen-starved cells and arrest in G1 before Start.
PMID:22375066	GO:0031588	nucleotide-activated protein kinase complex	These results indicated that Ssp2 interacts physically with Amk2 and Cbs2 in vivo, showing that AMPK is indeed a αβγ heterotrimer and that these three subunits interact even under optimal growth conditions.
PMID:22375066	GO:0031588	nucleotide-activated protein kinase complex	These results indicated that Ssp2 interacts physically with Amk2 and Cbs2 in vivo, showing that AMPK is indeed a αβγ heterotrimer and that these three subunits interact even under optimal growth conditions.
PMID:22375066	GO:0031588	nucleotide-activated protein kinase complex	These results indicated that Ssp2 interacts physically with Amk2 and Cbs2 in vivo, showing that AMPK is indeed a αβγ heterotrimer and that these three subunits interact even under optimal growth conditions.
PMID:22375066	GO:0004674	protein serine/threonine kinase activity [part_of] positive regulation of cell cycle switching, mitotic to meiotic cell cycle [occurs_in] nucleus [happens_during] cellular response to nitrogen starvation	This finding suggested that inactive AMPK is excluded from the nucleus and, upon activation by glucose or nitrogen starvation, part of the AMPK moves into the nucleus.
PMID:22375066	GO:0004674	protein serine/threonine kinase activity [part_of] regulation of cell cycle switching, mitotic to meiotic cell cycle [occurs_in] nucleus [happens_during] cellular response to glucose starvation	This result shows that Ssp2 phosphorylation by Ssp1 is required to trigger the nuclear accumulation of the former upon nitrogen or glucose starvation, and that if Ssp2 is not phosphorylated it remains in a cytoplasmic localization, regardless of the nutritional conditions of the cell.
PMID:22426534	GO:0000785	chromatin [coincident_with] mating_type_region_replication_fork_barrier	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	GO:0000785	chromatin [coincident_with] rDNA_replication_fork_barrier	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	GO:0000785	chromatin [coincident_with] rDNA_replication_fork_barrier	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	GO:0000785	chromatin [coincident_with] PomBase:SPBC32H8.12c	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	GO:0000785	chromatin [coincident_with] PomBase:SPCC622.09	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	GO:0000785	chromatin [coincident_with] PomBase:SPBC32H8.12c	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	GO:0000785	chromatin [coincident_with] PomBase:SPCC622.09	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	GO:0000785	chromatin [coincident_with] PomBase:SPCC622.08c	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	GO:0000785	chromatin [coincident_with] PomBase:SPCC622.08c	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22426534	GO:0000785	chromatin [coincident_with] mating_type_region_replication_fork_barrier	(comment: genes in extensions are assayed as represntative of highly transcribed genes)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 46	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 8	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 81	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 61	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0002253	normal septum location	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 17	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 6	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 76	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 31	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 64	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 57	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 72	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 65	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 79	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 67	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0002253	normal septum location	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0002253	normal septum location	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0002253	normal septum location	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 12	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 45	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 57	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 49	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 51	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 52	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 5	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 6	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 23	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 37	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 15	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 46	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 83	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 64	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0002253	normal septum location	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 66	(Fig. 1B, Table 1)
PMID:22427686	FYPO:0007156	increased protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15 [has_severity] medium	(Fig. 2C)
PMID:22427686	FYPO:0006326	decreased protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15 [has_severity] medium	(Fig. 2C)
PMID:22427686	FYPO:0000838	normal protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	(Fig. 2C)
PMID:22427686	FYPO:0006326	decreased protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15 [has_severity] medium	(Fig. 2C)
PMID:22427686	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15 [has_severity] high	(Fig. 2C)
PMID:22427686	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15 [has_severity] high	(Fig. 2C)
PMID:22427686	FYPO:0001368	normal actomyosin contractile ring assembly	(Fig. 2H)
PMID:22427686	FYPO:0001368	normal actomyosin contractile ring assembly	(Fig. 2H)
PMID:22427686	FYPO:0001368	normal actomyosin contractile ring assembly	(Fig. 2H)
PMID:22427686	FYPO:0007139	abolished protein localization to medial cortical node during mitotic interphase [has_penetrance] 70 [assayed_protein] PomBase:SPCC4B3.15	(Fig. 3B)
PMID:22427686	FYPO:0007139	abolished protein localization to medial cortical node during mitotic interphase [assayed_protein] PomBase:SPCC4B3.15 [has_penetrance] complete	(Fig. 3B)
PMID:22427686	FYPO:0007139	abolished protein localization to medial cortical node during mitotic interphase [assayed_protein] PomBase:SPCC4B3.15 [has_penetrance] complete	(Fig. 3B)
PMID:22427686	FYPO:0007139	abolished protein localization to medial cortical node during mitotic interphase [assayed_protein] PomBase:SPCC4B3.15 [has_penetrance] 25	(Fig. 3B)
PMID:22427686	FYPO:0007139	abolished protein localization to medial cortical node during mitotic interphase [assayed_protein] PomBase:SPCC4B3.15 [has_penetrance] 25	(Fig. 3B)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 60	(Fig. 4C)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 45	(Fig. 4C)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 25	(Fig. 4C)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 30	(Fig. 4C)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 30	(Fig. 4C)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 30	(Fig. 4C)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 25	(Fig. 4C)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 25	(Fig. 4C)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 50	(Fig. 4C)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 10	(Fig. 4C)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 10	(Fig. 4C)
PMID:22427686	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 35	(Fig. 4C)
PMID:22427686	FYPO:0001584	abnormal protein localization to cell tip during vegetative growth [assayed_protein] PomBase:SPAC31A2.16	(Fig. 4D)
PMID:22427686	FYPO:0006637	decreased protein localization to cell cortex of cell tip, with protein distributed in cortex [assayed_protein] PomBase:SPCC4B3.15 [has_severity] medium	(Fig. 4F)
PMID:22427686	FYPO:0006637	decreased protein localization to cell cortex of cell tip, with protein distributed in cortex [assayed_protein] PomBase:SPCC4B3.15 [has_severity] high	(Fig. 4F)
PMID:22427686	FYPO:0000729	delayed onset of actomyosin contractile ring assembly [has_severity] medium	(Fig. 5B and C)
PMID:22427686	FYPO:0006326	decreased protein localization to medial cortical node [assayed_protein] PomBase:SPAC926.03	(Fig. 5D)
PMID:22427686	FYPO:0003338	abnormal actomyosin contractile ring morphology	(Fig. 6A)
PMID:22427686	FYPO:0003338	abnormal actomyosin contractile ring morphology	(Fig. 6B)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 10	(Fig. 6E)
PMID:22427686	FYPO:0002253	normal septum location	(Fig. 6E)
PMID:22427686	FYPO:0002253	normal septum location	(Fig. 6E)
PMID:22427686	FYPO:0001390	misoriented septum during vegetative growth [has_penetrance] 10	(Fig. 6E)
PMID:22427686	FYPO:0002999	normal protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	(Fig. 6F and G)
PMID:22427686	FYPO:0002999	normal protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	(Fig. 6F and G)
PMID:22427686	FYPO:0000729	delayed onset of actomyosin contractile ring assembly [has_severity] high	(Fig. 6H)
PMID:22427686	FYPO:0000729	delayed onset of actomyosin contractile ring assembly [has_severity] medium	(Fig. 6H)
PMID:22427686	FYPO:0000729	delayed onset of actomyosin contractile ring assembly [has_severity] medium	(Fig. 6H)
PMID:22427686	FYPO:0000729	delayed onset of actomyosin contractile ring assembly [has_severity] high	(Fig. 6H)
PMID:22427686	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC57A10.02 [assayed_protein] PomBase:SPCC4B3.15	(Fig. S2A)
PMID:22427686	FYPO:0003919	abolished protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0001424	abolished protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0001424	abolished protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0001424	abolished protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0003919	abolished protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0001424	abolished protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0003919	abolished protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0001424	abolished protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0001424	abolished protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0001424	abolished protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0003919	abolished protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0003919	abolished protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0003919	abolished protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0003919	abolished protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0003919	abolished protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0003919	abolished protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22427686	FYPO:0006638	decreased protein localization to medial cortex, with protein distributed in cell cortex, during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	Table 1
PMID:22431512	GO:1990188	euchromatin binding [occurs_at] CRE	(comment: localization independent of Ago1)
PMID:22431512	GO:1990188	euchromatin binding [occurs_at] CRE	(comment: localization independent of Ago1)
PMID:22431512	GO:0000791	euchromatin [coincident_with] CRE	(comment: localization independent of Ago1)
PMID:22431512	GO:0000791	euchromatin [coincident_with] CRE	(comment: localization independent of Ago1)
PMID:22437499	FYPO:0005446	abolished molecular function	Disrupting the Leu-binding pocket by replacing Val 196 with a bulky methionine, and substituting Ser for the Cdh1 equivalents of Asp 173, Asp 457 and Glu 458 at the putative Arg-binding site, eliminated the ability of Cdh1 to stimulate APC/C activity (Fig. 4e and Supplementary Fig. 6) but had no affect on co-activator binding to the APC/C (Supplementary Fig. 7)
PMID:22437499	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC1795.01c [assayed_protein] PomBase:SPBC20F10.06	This mutation dissociated Mad3 from a Cdc20-C-Mad2 heterodimer when size-exclusion chromatography was performed (Supplementary Fig. 4).
PMID:22437499	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC1795.01c [assayed_protein] PomBase:SPAC821.08c	This mutation dissociated Mad3 from a Cdc20-C-Mad2 heterodimer when size-exclusion chromatography was performed (Supplementary Fig. 4).
PMID:22438582	GO:0035974	meiotic spindle pole body [exists_during] meiotic anaphase I	(Figure 1)
PMID:22438582	GO:0035974	meiotic spindle pole body [exists_during] meiotic anaphase I	(Figure 1)
PMID:22438582	GO:0035974	meiotic spindle pole body [exists_during] meiotic anaphase I	(Figure 1)
PMID:22438582	GO:0035974	meiotic spindle pole body [exists_during] meiotic M phase	(Figure 1)
PMID:22438582	GO:0035974	meiotic spindle pole body [exists_during] meiotic M phase	(Figure 1)
PMID:22438582	GO:0035974	meiotic spindle pole body [exists_during] meiotic M phase	(Figure 1)
PMID:22438582	GO:0035974	meiotic spindle pole body [exists_during] meiotic M phase	(Figure 1)
PMID:22438582	GO:0000776	kinetochore [exists_during] meiotic prophase I	(Figure 1)
PMID:22438582	GO:0035974	meiotic spindle pole body [exists_during] meiotic anaphase I	(Figure 1)
PMID:22438582	FYPO:0000151	abnormal meiotic chromosome segregation	(Figure 4B)
PMID:22438582	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC23C11.16	(Figure 5)
PMID:22438582	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC23C11.16	(Figure 5)
PMID:22438582	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC23C11.16	(Figure 5A)
PMID:22438582	FYPO:0007256	premature protein localization to meiotic spindle pole body during prophase I [assayed_using] PomBase:SPBC649.05	(Figure 5A)
PMID:22438582	FYPO:0007256	premature protein localization to meiotic spindle pole body during prophase I [assayed_using] PomBase:SPAC6G9.06c	(Figure 5A)
PMID:22438582	FYPO:0007257	delayed onset of protein localization to meiotic spindle pole body during meiosis I [assayed_using] PomBase:SPAC6G9.06c	(Figure 5F)
PMID:22438582	FYPO:0004609	spindle pole bodies present in increased numbers during meiosis [assayed_using] PomBase:SPAC6G9.06c	(Figure 6A)
PMID:22438582	FYPO:0003263	abnormal sporulation resulting in formation of ascus with more than four spores [assayed_using] PomBase:SPBC649.05	(Figure 6A)
PMID:22438582	FYPO:0003263	abnormal sporulation resulting in formation of ascus with more than four spores [assayed_using] PomBase:SPAC6G9.06c	(Figure 6A)
PMID:22438582	FYPO:0004609	spindle pole bodies present in increased numbers during meiosis [assayed_using] PomBase:SPBC649.05	(Figure 6A)
PMID:22438582	FYPO:0000583	abolished sporulation	(Figure S6)
PMID:22438582	FYPO:0000583	abolished sporulation	(Figure S6)
PMID:22438582	GO:1990395	meiotic spindle pole body organization	(comment: CHECK MEIOTIC !) Plo1 protein reorganize spindle body during meiosis: Plo1 starts to localize to spindle pole body at the onset of meiosis I, and recruits Cut12 (and Pcp1), which was absent during meiotic prophase.
PMID:2245912	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] variable severity	(Table 4)
PMID:2245912	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] variable severity	(Table 4)
PMID:2245912	FYPO:0001491	viable vegetative cell	(Table 5)
PMID:2245912	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(Table 6)
PMID:2245912	FYPO:0001492	viable elongated vegetative cell	(comment: Table 5 This mutant is a revertant of cdc2-M35)
PMID:2245912	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(comment: Table 5 no genetic interaction with stf1-1)
PMID:2245912	FYPO:0001122	elongated vegetative cell [has_penetrance] high	(comment: cells heterozygous for stf1-1 are more elongated that stf1-1 homozygous cells)
PMID:2245912	FYPO:0000150	abnormal colony morphology [has_severity] high	(comment: cells heterozygous for stf1-1 form small colonies at restrictive temperature ~20-200 cells)
PMID:2245912	FYPO:0001122	elongated vegetative cell [has_penetrance] high	(comment: cells homozygous for stf1-1 are not as elongated as stf1-1 heterozygous cells at restrictive temperature)
PMID:2245912	FYPO:0000150	abnormal colony morphology [has_severity] high	(comment: cells homozygous for stf1-1 form small colonies at restrictive temperature ~20-200 cells)
PMID:2245912	FYPO:0001490	inviable elongated vegetative cell	(comment: dis2+ over expression reverses the stf1-1 suppression cdc25-22)
PMID:2245912	FYPO:0001122	elongated vegetative cell [has_penetrance] high	(comment: same phenotype as cells homozygous for stf1-1)
PMID:2245912	FYPO:0000150	abnormal colony morphology [has_severity] high	(comment: same phenotype as cells homozygous for stf1-1)
PMID:2245912	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] high	(comment: stf1-1/stf1-2 cells are not as elongated as stf1-1 heterozygous cells at restrictive temperature)
PMID:2245912	FYPO:0001122	elongated vegetative cell [has_penetrance] high	(comment: stf1-1/stf1-3 cells are not as elongated as stf1-1 heterozygous cells at restrictive temperature)
PMID:2245912	FYPO:0000150	abnormal colony morphology [has_severity] high	(comment: stf1-1/stf1-3 cells form small colonies at restrictive temperature ~20-200 cells)
PMID:2245912	FYPO:0004922	inviable elongated mononucleate aseptate cell with cell cycle arrest at mitotic G2/M phase transition [has_penetrance] high	(comment: the restrictive temperature for a cdc25-22 diploid is 32°C)
PMID:2245912	FYPO:0000674	normal cell population growth at high temperature	Table 3 (comment: suppressor of cdc25-22)
PMID:2245912	FYPO:0000674	normal cell population growth at high temperature	Table 4 (comment: stf1-1 is a suppressor of cdc25-M51)
PMID:2245912	FYPO:0001492	viable elongated vegetative cell	Table 4 (comment: stf1-1 is a suppressor of cdc25-M51)
PMID:2245912	FYPO:0000674	normal cell population growth at high temperature	Table 4 (comment: suppressor of cdc25-22)
PMID:2245912	FYPO:0000674	normal cell population growth at high temperature	Table 4 (comment: suppressor of cdc25-22)
PMID:2245912	FYPO:0001492	viable elongated vegetative cell	Table 4 (comment: suppressor of cdc25-22)
PMID:2245912	FYPO:0001492	viable elongated vegetative cell	Table 4 (comment: suppressor of cdc25-22)
PMID:2245912	FYPO:0000674	normal cell population growth at high temperature	Table 4 (comment: suppressor of cdc25-disruption occasional cdc- cells observed)
PMID:2245912	FYPO:0001492	viable elongated vegetative cell	Table 4 (comment: suppressor of cdc25-disruption occasional cdc- cells observed)
PMID:2245912	FYPO:0001492	viable elongated vegetative cell	Table 5 (comment: This mutant is a revertant of cdc2-M35)
PMID:2245912	FYPO:0006822	viable small vegetative cell with normal cell growth rate	Table 5 (comment: cdc2-1w and stf1-1 have additive effect on cdc25-22 cell size at restrictive temperature)
PMID:2245912	FYPO:0001492	viable elongated vegetative cell	Table 5 (comment: cdc2-1w rescues cdc25-22 but cells are long)
PMID:2245912	FYPO:0006822	viable small vegetative cell with normal cell growth rate	Table 5 (comment: cdc2-3w and stf1-1 have additive effect on cdc25-22 cell size at restrictive temperature)
PMID:2245912	FYPO:0001490	inviable elongated vegetative cell	Table 5 (comment: no genetic interaction with stf1-1 cdc2-59 is a cold sensitive cdc2 mutant cdc at low (25°C) temperature and wee at high temperature (35°C))
PMID:2245912	FYPO:0001492	viable elongated vegetative cell	Table 5 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0006822	viable small vegetative cell with normal cell growth rate	Table 5 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0006822	viable small vegetative cell with normal cell growth rate	Table 5 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0001490	inviable elongated vegetative cell	Table 5 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0001490	inviable elongated vegetative cell	Table 5 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0001490	inviable elongated vegetative cell	Table 5 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0006822	viable small vegetative cell with normal cell growth rate	Table 5 no genetic interaction with stf1-1
PMID:2245912	FYPO:0006822	viable small vegetative cell with normal cell growth rate	Table 6 (comment: wee1-50 and stf1-1 have an additive effect to suppress cdc25-22 phenotype at the restrictive temperature)
PMID:2245912	FYPO:0001492	viable elongated vegetative cell [has_severity] low	Table 7 (comment: Cells are slightly shorter at high temperature when stf1-1 present)
PMID:2245912	FYPO:0001492	viable elongated vegetative cell [has_severity] low	Table 7 (comment: Cells are slightly shorter at high temperature when stf1-1 present)
PMID:2245912	FYPO:0001490	inviable elongated vegetative cell	Table 8 (comment: no genetic interaction with stf1-1)
PMID:2245912	FYPO:0001492	viable elongated vegetative cell	Table 8 (comment: no genetic interaction with stf1-1)
PMID:22474355	FYPO:0005918	decreased protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPCC1393.05	ChIP analyses showed that Ers1 localization at the mating type locus (cenH) and telomeres was severely decreased in swi6Δ and clr4Δ cells (Fig. S5A).
PMID:22474355	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC1393.05	ChIP analyses showed that Ers1 localization at the mating type locus (cenH) and telomeres was severely decreased in swi6Δ and clr4Δ cells (Fig. S5A).
PMID:22474355	FYPO:0005918	decreased protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPCC1393.05	ChIP analyses showed that Ers1 localization at the mating type locus (cenH) and telomeres was severely decreased in swi6Δ and clr4Δ cells (Fig. S5A).
PMID:22474355	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC1393.05	ChIP analyses showed that Ers1 localization at the mating type locus (cenH) and telomeres was severely decreased in swi6Δ and clr4Δ cells (Fig. S5A).
PMID:22474355	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPCC1393.05	In contrast, EGFP-Ers1C62 showed a more diffuse signal with weak nuclear dots (Fig. 4B and Fig. S4 C and D), suggesting that the correct localization of Ers1 was impaired by the C62 mutation.
PMID:22474355	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPCC1393.05	In contrast, a high level of Ers1 was detected at telomeres in hrr1Δ cells (Fig. S5C).
PMID:22474355	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC428.08c [has_penetrance] high	In swi6Δ cells, Chp1 association with the centromeric dg or dh repeat locus decreased partially (70- 80%) but was still much greater than that observed in clr4Δ cells (Fig. 5 A and B).
PMID:22474355	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC1393.05 [assayed_protein] PomBase:SPAC664.01c	Moreover, the interaction between Ers1 and Swi6 was weakened by the presence of the C62 mutation (Fig. 4 D and E). Taken together, these results suggested that Ers1 associates with both Hrr1 and Swi6, and that the C62 mutation impairs both associations.
PMID:22474355	FYPO:0003744	abolished protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPCC1393.05	Moreover, the nuclear dot localization of EGFP-Ers1WT was completely abolished in clr4Δ cells (Fig. 4C), indicating that the activity of Clr4 was also required for Ers1 localization in the nucleus.
PMID:22474355	GO:0005721	pericentric heterochromatin	Similar to that previously observed, EGFP-Ers1WT showed a distinct nuclear dot pattern in WT cells consistent with a localization to heterochromatin (Fig. 4B and Fig. S4B)
PMID:22474355	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPCC1739.03	The localizations of Hrr1-Flag and Rdp1-Flag at centromeric repeats were also found to be severely compromised in both ers1Δ and swi6Δ mutant cells (Fig. 5 A and B).
PMID:22474355	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC6F12.09	The localizations of Hrr1-Flag and Rdp1-Flag at centromeric repeats were also found to be severely compromised in both ers1Δ and swi6Δ mutant cells (Fig. 5 A and B).
PMID:22474355	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC6F12.09	The localizations of Hrr1-Flag and Rdp1-Flag at centromeric repeats were also found to be severely compromised in both ers1Δ and swi6Δ mutant cells (Fig. 5 A and B).
PMID:22474355	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPCC1739.03	The localizations of Hrr1-Flag and Rdp1-Flag at centromeric repeats were also found to be severely compromised in both ers1Δ and swi6Δ mutant cells (Fig. 5 A and B).
PMID:22474355	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPCC1739.03 [part_of] siRNA-mediated pericentric heterochromatin formation	This is also consistent with a previous report that the deletion of swi6+ decreases the centromeric localization of Rdp1 (14). These results support the idea that the heterochromatic localization of RDRC requires Ers1 and that, in turn, Ers1 localization depends on Swi6.
PMID:22474355	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPCC1739.03 [has_penetrance] high	This was in contrast to Hrr1 or Rdp1, whose association was severely reduced in swi6Δ cells (10-20%) to levels comparable to those of clr4Δ cells.
PMID:22474355	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [has_penetrance] high [assayed_protein] PomBase:SPAC6F12.09	This was in contrast to Hrr1 or Rdp1, whose association was severely reduced in swi6Δ cells (10-20%) to levels comparable to those of clr4Δ cells.
PMID:22474355	FYPO:0005072	normal protein localization to centromeric chromatin [assayed_protein] PomBase:SPCC1393.05	To test the hypothesis that the nuclear dot localization of Ers1 was attributable to an interaction with H3K9me-bound CD proteins, EGFP-Ers1WT localization was next examined in swi6Δ, chp1Δ, and chp2Δ cells. The localization of EGFP-Ers1WT was clearly abolished in swi6Δ cells similar to that observed in clr4Δ, whereas WT localization patterns were retained in the chp1Δ and chp2Δ cells (Fig. 4C and Fig. S4C).
PMID:22474355	FYPO:0005072	normal protein localization to centromeric chromatin [assayed_protein] PomBase:SPCC1393.05	To test the hypothesis that the nuclear dot localization of Ers1 was attributable to an interaction with H3K9me-bound CD proteins, EGFP-Ers1WT localization was next examined in swi6Δ, chp1Δ, and chp2Δ cells. The localization of EGFP-Ers1WT was clearly abolished in swi6Δ cells similar to that observed in clr4Δ, whereas WT localization patterns were retained in the chp1Δ and chp2Δ cells (Fig. 4C and Fig. S4C).
PMID:22474355	FYPO:0003744	abolished protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPCC1393.05	To test the hypothesis that the nuclear dot localization of Ers1 was attributable to an interaction with H3K9me-bound CD proteins, EGFP-Ers1WT localization was next examined in swi6Δ, chp1Δ, and chp2Δ cells. The localization of EGFP-Ers1WT was clearly abolished in swi6Δ cells similar to that observed in clr4Δ, whereas WT localization patterns were retained in the chp1Δ and chp2Δ cells (Fig. 4C and Fig. S4C).
PMID:22474355	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	defective siRNA production (Fig. 1C)
PMID:22474355	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_using] dh_repeat [has_severity] high	derepression of a ura4+ marker gene integrated into the outermost Fig. 1. (otr) pericentromeric repeat of chromosome 1 (otr1R::ura4+) (Fig. 1a)
PMID:22474355	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_using] dh_repeat [has_severity] medium	derepression of a ura4+ marker gene integrated into the outermost Fig. 1. (otr) pericentromeric repeat of chromosome 1 (otr1R::ura4+) (Fig. 1a)
PMID:22474355	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_using] dh_repeat [has_severity] medium	derepression of a ura4+ marker gene integrated into the outermost Fig. 1. (otr) pericentromeric repeat of chromosome 1 (otr1R::ura4+) (Fig. 1a)
PMID:22474355	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_using] dh_repeat [has_severity] medium	derepression of a ura4+ marker gene integrated into the outermost Fig. 1. (otr) pericentromeric repeat of chromosome 1 (otr1R::ura4+) (Fig. 1a)
PMID:22474355	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_using] dh_repeat [has_severity] medium	derepression of a ura4+ marker gene integrated into the outermost Fig. 1. (otr) pericentromeric repeat of chromosome 1 (otr1R::ura4+) (Fig. 1a)
PMID:22474355	FYPO:0000220	increased centromeric outer repeat transcript level	increased levels of noncoding centromeric transcripts (Fig. 1B)
PMID:22474355	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPCC1393.05 [part_of] siRNA-mediated pericentric heterochromatin formation	suggesting that a physical association with Swi6, but not the other CD proteins, was required for the heterochromatic localization of Ers1.
PMID:22484924	FYPO:0003482	increased punctate cytoplasmic protein localization [assayed_using] PomBase:SPBC16C6.06	(Fig. 2D)
PMID:22484924	FYPO:0000847	increased protein degradation during vegetative growth [assayed_using] PomBase:SPBC16C6.06	(Fig. 2c)
PMID:22484924	FYPO:0005489	protein mislocalized to vacuolar membrane [assayed_using] PomBase:SPBC16C6.06	(Fig. 2d)
PMID:22484924	FYPO:0004482	abnormal vacuole fusion during vegetative growth	(Fig. 4)
PMID:22484924	FYPO:0000423	decreased rate of endocytosis during vegetative growth	(Fig. 4) (comment: (I moved this down from abnormal endocytisis, is that OK?))
PMID:22484924	FYPO:0003577	abolished plasma membrane to vacuole transport after nitrogen starvation [assayed_using] PomBase:SPBC359.03c	(Fig. 5c)
PMID:22484924	GO:0006895	Golgi to endosome transport	(comment: CHECK (protein))
PMID:22484924	FYPO:0005547	decreased protein targeting to vacuole, with protein secreted [assayed_using] PomBase:SPAC24C9.08	(comment: vw, moved down to -decreased protein targeting to vacuole, with protein secreted)
PMID:22496451	FYPO:0002894	decreased transcription during cellular response to calcium ion [assayed_using] CDRE_motif	"(comment: allele tyep ""unknown"" because neither nt nor aa position 324 is A)"
PMID:22508988	GO:0005515	protein binding	(Fig. 1) (comment: carboxy terminal region)
PMID:22508988	GO:0005515	protein binding	(Fig. 1) (comment: carboxy terminal region)
PMID:22508988	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC32H8.10 [assayed_using] PomBase:SPCC330.10	(Fig. 1a)
PMID:22508988	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC32H8.10 [assayed_using] PomBase:SPCC330.10	(Fig. 1a)
PMID:22508988	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC28F2.12 [assayed_using] PomBase:SPBC32F12.06	(Fig. 1a)
PMID:22508988	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC32H8.10 [assayed_using] PomBase:SPCC330.10	(Fig. 1a) (comment: CHECK in vitro /in vivo)
PMID:22508988	FYPO:0003075	normal protein kinase activity [assayed_substrate] PomBase:SPBC32H8.10	(Fig. 1e) (comment: CHECK in vitro)
PMID:22508988	FYPO:0006821	slow vegetative cell growth	(Fig. 2b)
PMID:22508988	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 2c)
PMID:22508988	FYPO:0003670	sensitive to mycophenolic acid [has_severity] high	(Fig. 2c)
PMID:22508988	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2c)
PMID:22508988	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	(Fig. 2c)
PMID:22508988	FYPO:0001357	normal vegetative cell population growth	(Fig. 2c)
PMID:22508988	FYPO:0002141	normal cell population growth at low temperature	(Fig. 2c)
PMID:22508988	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2c)
PMID:22508988	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	(Fig. 2c)
PMID:22508988	FYPO:0003670	sensitive to mycophenolic acid [has_severity] high	(Fig. 2c) MPA exacerbates growth impairment in mutants defective in transcript elongation (8, 11, 50), although the precise mechanism of this effect is unknown (34)
PMID:22508988	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPAC23C4.19	(Fig. 2d) (comment: CHECK Spt5-T1P (CTD repeat 1 residue))
PMID:22508988	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPAC23C4.19	(Fig. 2d) (comment: CHECK Spt5-T1P (CTD repeat 1 residue))
PMID:22508988	FYPO:0004083	normal protein level [assayed_using] PomBase:SPBC32F12.06	(Fig. 3B)
PMID:22508988	FYPO:0004083	normal protein level [assayed_using] PomBase:SPCC330.10	(Fig. 3B)
PMID:22508988	FYPO:0006631	decreased protein localization to chromatin [assayed_using] PomBase:SPCC330.10	(Fig. 4A, B)
PMID:22508988	FYPO:0006631	decreased protein localization to chromatin [assayed_using] PomBase:SPBC32F12.06	(Fig. 4A, B)
PMID:22508988	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC19F8.07	(Fig. 6C) Immunoblot analysis indicated that Mcs6 phosphorylates Ser2, Ser5, and Ser7
PMID:22508988	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC28F2.12	(Fig. 6C) Immunoblot analysis indicated that Mcs6 phosphorylates Ser2, Ser5, and Ser7
PMID:22508988	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC19F8.07	(Fig. 6C) Immunoblot analysis indicated that Mcs6 phosphorylates Ser2, Ser5, and Ser7
PMID:22508988	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC19F8.07	(Fig. 6C) Immunoblot analysis indicated that Mcs6 phosphorylates Ser2, Ser5, and Ser7
PMID:22508988	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPBC32H8.10	. The preference of the conserved Cdk9 catalytic domain in fission yeast and metazoans for Ser7-modified CTD substrates, moreover, implies a conserved mechanism to impose order on the Pol II transcription cycle.
PMID:22508988	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC28F2.12	S. pombe Cdk9 also generated Ser2-P and Ser5-P signals but was relatively inefficient at phosphorylating Ser7.
PMID:22508988	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC32H8.10	S. pombe Cdk9 also generated Ser2-P and Ser5-P signals but was relatively inefficient at phosphorylating Ser7.
PMID:22508988	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC32H8.10	S. pombe Cdk9 also generated Ser2-P and Ser5-P signals but was relatively inefficient at phosphorylating Ser7.
PMID:22508988	GO:0004674	protein serine/threonine kinase activity	We also compared the activities of kinase complexes generated by translation in vitro toward Spt5. By this measurement also, Cdk9 and Cdk9􏰂C were stimulated to similar extents by Csk1 (Fig. 1F),(comment: is this an physiological substrate?)
PMID:22558440	GO:0006357	regulation of transcription by RNA polymerase II [happens_during] meiosis I cell cycle phase	(comment: I specifically used that term name because I did not want to discriminate whether Cuf2 is a negative or a positive regulator of transcription even though in the paper we have put emphasis on the fact that meiotic genes are up-regulated in the absence of Cuf2 (so that Cuf2 would be a repressor). The reason is that there are also many other genes that are down-regulated in the cuf2delta mutant compare to WT. We still don't know which effect is direct and/or indirect. Thus, we don't want to exclude that Cuf2 might act as an activator, a repressor or both, for now.)
PMID:22558440	GO:0006357	regulation of transcription by RNA polymerase II [happens_during] meiosis II cell cycle phase	(comment: I specifically used that term name because I did not want to discriminate whether Cuf2 is a negative or a positive regulator of transcription even though in the paper we have put emphasis on the fact that meiotic genes are up-regulated in the absence of Cuf2 (so that Cuf2 would be a repressor). The reason is that there are also many other genes that are down-regulated in the cuf2delta mutant compare to WT. We still don't know which effect is direct and/or indirect. Thus, we don't want to exclude that Cuf2 might act as an activator, a repressor or both, for now.)
PMID:22573890	FYPO:0004076	inviable after spore germination, single or double cell division, elongated multiseptate cell [has_penetrance] 10-20	(Fig. 2a)
PMID:22573890	FYPO:0000021	spheroid vegetative cell [has_penetrance] 20	(Fig. 2a) (comment: CHECK WT 10% @36degrees)
PMID:22573890	GO:0000935	division septum [exists_during] mitotic M phase	(Fig. 3A)
PMID:22573890	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic M phase	(Fig. 3A)
PMID:22573890	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	(Fig. 3A)
PMID:22573890	FYPO:0006187	normal rate of actomyosin contractile ring assembly	(Fig. 5)
PMID:22573890	FYPO:0004895	normal rate of actomyosin contractile ring contraction	(Fig. 5)
PMID:22573890	FYPO:0004653	delayed onset of actomyosin contractile ring contraction	(Fig. 5)
PMID:22573890	FYPO:0006559	delayed onset of mitotic spindle disassembly	(Fig. 5) (comment: 6 min late)
PMID:22573890	FYPO:0000651	increased duration of septum assembly	(Fig. 6)
PMID:22573890	FYPO:0000650	increased septation index	(Fig. 6)
PMID:22573890	GO:0005938	cell cortex [exists_during] cell quiescence	(Fig. S2)
PMID:22573890	FYPO:0004495	inviable branched, swollen, elongated, multiseptate vegetative cell [has_penetrance] high	(Figure 2B, C)
PMID:22582262	GO:0007129	homologous chromosome pairing at meiosis	"rec12 phenotype indicates that Sme2 role in synapsis is independent of meiotic recombination; (comment: NEEDS TO BE REGULATION OF SYNAPSISa change to the GO ""pairing"" definition requested""https://sourceforge.net/p/geneontology/ontology-requests/10607/)"
PMID:22582262	GO:0007129	homologous chromosome pairing at meiosis	"rec12 phenotype indicates that Sme2 role in synapsis is independent of meiotic recombination; (comment: NEEDS TO BE REGULATION OF SYNAPSISa change to the GO ""pairing"" definition requested""https://sourceforge.net/p/geneontology/ontology-requests/10607/)"
PMID:22645648	FYPO:0002672	normal growth on rapamycin	(Figure 1a)
PMID:22645648	FYPO:0002061	inviable vegetative cell population	(Figure 1a)
PMID:22645648	FYPO:0002060	viable vegetative cell population	(Figure 1a)
PMID:22645648	FYPO:0002061	inviable vegetative cell population	(Figure 1a, 6a)
PMID:22645648	FYPO:0000012	mitotic G2/M phase transition delay	(Figure 4a, b)
PMID:22645648	FYPO:0001019	monopolar actin cortical patch localization during vegetative growth	(Figure 4d)
PMID:22645648	FYPO:0005430	aggregated actin cortical patches during vegetative growth	(Figure 4d)
PMID:22645648	FYPO:0001122	elongated vegetative cell	(Figure 4e)
PMID:22645648	FYPO:0002672	normal growth on rapamycin	(Figure 6)
PMID:22645648	FYPO:0002061	inviable vegetative cell population	(Figure 6)
PMID:22645648	FYPO:0002060	viable vegetative cell population	(Figure 6)
PMID:22645648	GO:0038202	TORC1 signaling	(comment: TOR kinase activity was measured using immunoprecipitated proteins) (Fig. 2)
PMID:22645654	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 1d)
PMID:22645654	FYPO:0000088	sensitive to hydroxyurea	(Fig. 1d)
PMID:22645654	FYPO:0001930	abnormal cellular response to gamma radiation	(Fig. 1d)
PMID:22645654	FYPO:0000085	sensitive to camptothecin	(Fig. 1d)
PMID:22645654	FYPO:0004031	decreased UV-damage excision repair	(Fig. 1f) (comment: evidence:immunoblot using anti-thymine dimer anitbodies)
PMID:22645654	FYPO:0003844	abolished mitotic chromosome condensation	(Fig. 1g)
PMID:22645654	FYPO:0001387	loss of viability at high temperature	(Fig. 1h)
PMID:22645654	FYPO:0002060	viable vegetative cell population	(Fig. 2b, c)
PMID:22645654	FYPO:0001926	normal cellular response to hydroxyurea	(Fig. 2b, c)
PMID:22645654	FYPO:0000268	sensitive to UV during vegetative growth	(Fig. 2d, e, f)
PMID:22645654	FYPO:0000088	sensitive to hydroxyurea	(Fig. 2e)
PMID:22645654	FYPO:0000268	sensitive to UV during vegetative growth	(Fig. 2e)
PMID:22645654	FYPO:0002573	increased number of Ssb1 foci	(Fig. 3a-g) (comment: evidence: immunpflouresence)
PMID:22645654	FYPO:0002573	increased number of Ssb1 foci	(Fig. 4)
PMID:22645654	FYPO:0004385	decreased single-stranded DNA binding	(Fig. 5)
PMID:22645654	FYPO:0005438	abnormal DNA/DNA annealing activity	(Fig. 5)
PMID:22645654	FYPO:0004385	decreased single-stranded DNA binding	(Fig. 7)
PMID:22645654	GO:1990814	DNA/DNA annealing activity	Data from three experiments: DNA reannealing (renaturation assay) using heat-denatured DNA (ssDNA); Removal of RPA proteins associated with ssDNA, RPA-coated heat-denatured DNA (ssDNA) is renaturated; Removal of RNA associated with ssDNA, RNA/DNA hybrid is denatured by renaturation activity of condensin SMC
PMID:22658721	FYPO:0004371	decreased duration of S-phase DNA damage checkpoint	(comment: CHECK NMeed to check, its decreased duration of replication arrest?)
PMID:22658721	GO:0032132	O6-alkylguanine-DNA binding [part_of] transcription-coupled nucleotide-excision repair	(comment: bulky)
PMID:22658721	GO:0032132	O6-alkylguanine-DNA binding [part_of] global genome nucleotide-excision repair	(comment: small)
PMID:22660415	GO:0000776	kinetochore [exists_during] mitotic prometaphase	(Fig. 1A)
PMID:22660415	FYPO:0008165	decreased protein localization to kinetochore during mitotic prometaphase [assayed_protein] PomBase:SPCC1322.12c [has_penetrance] medium	(Fig. 1B) This Bub1 enrichment is diminished in the spc7-23 mutant at a restrictive temperature24 (Fig. 1b).
PMID:22660415	FYPO:0008166	abolished protein localization to kinetochore during mitotic prometaphase [assayed_protein] PomBase:SPCC1322.12c	(Fig. 1C)
PMID:22660415	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_protein] PomBase:SPBC106.01	(Fig. 1D)
PMID:22660415	FYPO:0008164	abnormal protein localization to kinetochore during mitotic M phase [assayed_protein] PomBase:SPCC1322.12c	(Fig. 1E)
PMID:22660415	FYPO:0008166	abolished protein localization to kinetochore during mitotic prometaphase [assayed_protein] PomBase:SPCC1322.12c	(Fig. 2G)
PMID:22660415	FYPO:0007399	normal protein localization to kinetochore during mitotic interphase [assayed_protein] PomBase:SPAC23H3.08c	(Fig. 2I)
PMID:22660415	FYPO:0007174	abnormal protein localization to kinetochore during mitotic interphase [assayed_protein] PomBase:SPCC1322.12c [has_severity] high	(Fig. 2I)
PMID:22660415	FYPO:0007399	normal protein localization to kinetochore during mitotic interphase [assayed_protein] PomBase:SPCC1795.01c	(Fig. 2I)
PMID:22660415	FYPO:0007399	normal protein localization to kinetochore during mitotic interphase [assayed_protein] PomBase:SPCC1795.01c	(Fig. 2I)
PMID:22660415	FYPO:0007174	abnormal protein localization to kinetochore during mitotic interphase [assayed_protein] PomBase:SPAC23H3.08c [has_severity] high	(Fig. 2I)
PMID:22660415	FYPO:0007399	normal protein localization to kinetochore during mitotic interphase [assayed_protein] PomBase:SPAC23H3.08c	(Fig. 2I)
PMID:22660415	FYPO:0007174	abnormal protein localization to kinetochore during mitotic interphase [assayed_protein] PomBase:SPCC1795.01c [has_severity] high	(Fig. 2I)
PMID:22660415	FYPO:0007399	normal protein localization to kinetochore during mitotic interphase [assayed_protein] PomBase:SPCC1322.12c	(Fig. 2I)
PMID:22660415	FYPO:0007399	normal protein localization to kinetochore during mitotic interphase [assayed_protein] PomBase:SPCC1322.12c	(Fig. 2I)
PMID:22660415	FYPO:0007174	abnormal protein localization to kinetochore during mitotic interphase [assayed_protein] PomBase:SPCC1322.12c [has_severity] high	(Fig. 2I)
PMID:22660415	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC1020.02 [assayed_protein] PomBase:SPAC23H3.08c	(Fig. 4B)
PMID:22660415	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC1020.02 [assayed_protein] PomBase:SPCC1322.12c	(Fig. 4B)
PMID:22660415	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC1020.02 [assayed_protein] PomBase:SPCC1322.12c	(Fig. 4B)
PMID:22660415	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC1020.02 [assayed_protein] PomBase:SPAC23H3.08c	(Fig. 4B)
PMID:22660415	FYPO:0003591	abnormal protein complex binding [assayed_protein] PomBase:SPCC1020.02 [assayed_protein] PomBase:SPCC1322.12c [assayed_protein] PomBase:SPAC23H3.08c	(Fig. 4C)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 90	(Fig. 5A)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 40	(Fig. 5A)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 40	(Fig. 5A)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 90	(Fig. 5A)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 90	(Fig. 5A)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 90	(Fig. 5A)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 40	(Fig. 5A)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 40	(Fig. 5A)
PMID:22660415	FYPO:0008165	decreased protein localization to kinetochore during mitotic prometaphase [assayed_protein] PomBase:SPBC3D6.04c [has_penetrance] medium	(Fig. 5B)
PMID:22660415	FYPO:0008166	abolished protein localization to kinetochore during mitotic prometaphase [assayed_protein] PomBase:SPBC3D6.04c	(Fig. 5B)
PMID:22660415	FYPO:0008166	abolished protein localization to kinetochore during mitotic prometaphase [assayed_protein] PomBase:SPBC3D6.04c	(Fig. 5B)
PMID:22660415	FYPO:0008165	decreased protein localization to kinetochore during mitotic prometaphase [assayed_protein] PomBase:SPBC3D6.04c [has_severity] high	(Fig. 5B)
PMID:22660415	FYPO:0008166	abolished protein localization to kinetochore during mitotic prometaphase [assayed_protein] PomBase:SPBC3D6.04c	(Fig. 5B)
PMID:22660415	FYPO:0008165	decreased protein localization to kinetochore during mitotic prometaphase [assayed_protein] PomBase:SPBC3D6.04c [has_severity] medium	(Fig. 5B)
PMID:22660415	FYPO:0008166	abolished protein localization to kinetochore during mitotic prometaphase [assayed_protein] PomBase:SPBC3D6.04c	(Fig. 5B)
PMID:22660415	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] low	(Fig. 5C)
PMID:22660415	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] medium	(Fig. 5C)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 90	(Fig. 5C)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 10	(Fig. 5C)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 10	(Fig. 5C)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 10	(Fig. 5C)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 10	(Fig. 5C)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 10	(Fig. 5C)
PMID:22660415	FYPO:0005780	decreased response to mitotic spindle assembly checkpoint signaling [has_penetrance] 10	(Fig. 5C)
PMID:22660415	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] medium	(Fig. 5C)
PMID:22660415	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] low	(Fig. 5C)
PMID:22660415	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] high	(Fig. 5C)
PMID:22660415	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] high	(Fig. 5C)
PMID:22660415	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 5E)
PMID:22660415	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 5E)
PMID:22660415	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. 5E)
PMID:22660415	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 5E)
PMID:22660415	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 5E)
PMID:22660415	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 5E)
PMID:22660415	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 5E)
PMID:22660415	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 5E)
PMID:22660415	FYPO:0002678	abolished protein phosphorylation [assayed_protein] PomBase:SPCC1020.02	(Fig. 5E)
PMID:22660415	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. 5F)
PMID:22660415	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] medium	(Fig. 5F)
PMID:22660415	FYPO:0001357	normal vegetative cell population growth	(Fig. 5F)
PMID:22660415	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. 5F)
PMID:22660415	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] medium	(Fig. 5F)
PMID:22660415	FYPO:0008166	abolished protein localization to kinetochore during mitotic prometaphase [assayed_protein] PomBase:SPCC1795.01c [has_penetrance] medium	Accordingly, Bub3 and Mad3 localized at kinetochores in a manner identical to Bub1 in spc7-12A and spc7-12E cells
PMID:22660415	FYPO:0008166	abolished protein localization to kinetochore during mitotic prometaphase [assayed_protein] PomBase:SPAC23H3.08c	Accordingly, Bub3 and Mad3 localized at kinetochores in a manner identical to Bub1 in spc7-12A and spc7-12E cells
PMID:22660415	FYPO:0004318	abolished mitotic spindle assembly checkpoint	Accordingly, the ectopic localization of Bub1 and the mitotic delay induced by Cnp3C-Mph1 were abolished by the spc7-12A mutation (Supplementary Fig. S3a)
PMID:22660415	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC106.01	During this analysis, we found that at least four sites (Thr 77, Thr 338, Thr 507 and Thr 552) are phosphorylated by Mph1 in vitro (Supplementary Fig. S2).
PMID:22660415	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC106.01	During this analysis, we found that at least four sites (Thr 77, Thr 338, Thr 507 and Thr 552) are phosphorylated by Mph1 in vitro (Supplementary Fig. S2).
PMID:22660415	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC106.01	During this analysis, we found that at least four sites (Thr 77, Thr 338, Thr 507 and Thr 552) are phosphorylated by Mph1 in vitro (Supplementary Fig. S2).
PMID:22660415	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC106.01	During this analysis, we found that at least four sites (Thr 77, Thr 338, Thr 507 and Thr 552) are phosphorylated by Mph1 in vitro (Supplementary Fig. S2).
PMID:22660415	FYPO:0005232	normal protein complex binding [assayed_protein] PomBase:SPCC1020.02 [assayed_protein] PomBase:SPCC1322.12c [assayed_protein] PomBase:SPAC23H3.08c	However, the coexpression of Bub1 and Bub3 enabled this complex to interact with Spc7-12E. Fig. 4C
PMID:22660415	GO:0000776	kinetochore [exists_during] mitotic prometaphase	Moreover, fission yeast Mph1 (MPS1 homologue), which also localizes to kinetochores only at prometaphase (Supplementary Fig. S1a and Fig. 1D)
PMID:22660415	FYPO:0001268	abnormal protein localization to kinetochore during vegetative growth [assayed_protein] PomBase:SPCC1322.12c	Strikingly, in spc7-12E cells, Bub1 localized at kinetochores throughout the entire cell cycle. Fig. 2H, I and S3C
PMID:22660415	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	The expression of this fusion protein impairs normal cell growth because of robust SAC activation (Supplementary Fig. S1b,c)
PMID:22660415	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC1020.02 [part_of] mitotic spindle assembly checkpoint signaling [occurs_in] outer kinetochore [happens_during] mitotic metaphase	Thus, Thr 77 and the MELT repeats in Spc7 are in vitro target sites of Mph1 kinase. Fig. 2
PMID:22660415	GO:0090266	regulation of mitotic cell cycle spindle assembly checkpoint	Thus, the dual regulation of Bub1 by Bub3, suppression of ectopic activation out of the kinetochore and the promotion of its kinetochore recruitment, may play a key role in establishing the robust kinetochore-based SAC activation system.
PMID:22660415	FYPO:0005042	normal protein localization to kinetochore [assayed_protein] PomBase:SPCC1020.02	although the kinetochore localization of Spc7-12A protein was intact (Fig. 2f)
PMID:22665807	FYPO:0004449	decreased protein phosphorylation during mitotic metaphase [assayed_enzyme] PomBase:SPAC24H6.05 [has_severity] high	(Fig. 1c)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high [has_severity] high	(Fig. 1d)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium [has_penetrance] high	(Fig. 1d)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium [has_penetrance] high [has_severity] variable severity	(Fig. 2A)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium [has_penetrance] high [has_severity] variable severity	(Fig. 2A)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high [has_severity] high [has_severity] variable severity	(Fig. 2A)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high [has_severity] high [has_severity] variable severity	(Fig. 2A)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high [has_severity] high [has_severity] variable severity	(Fig. 2A)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high [has_severity] high [has_severity] variable severity	(Fig. 2A)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high [has_severity] high [has_severity] variable severity	(Fig. 2A)
PMID:22665807	FYPO:0000833	normal protein level during vegetative growth [assayed_enzyme] PomBase:SPAC24H6.05	(Fig. 3a)
PMID:22665807	FYPO:0004474	normal mitotic cell cycle DNA replication checkpoint	(Fig. 3b)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high	(Fig. 4b)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high	(Fig. 4b)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high	(Fig. 4b)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 4b)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	(Fig. 4b)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	(Fig. 4b)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high	(Fig. 4b)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	(Fig. 4b)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	(Fig. 4b)
PMID:22665807	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	(Fig. 4b)
PMID:22665807	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(Figure 2A)
PMID:22665807	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC11B10.09 [removed_by] PomBase:SPAC1782.09c [present_during] mitotic M phase	Table S1, Figure S1
PMID:22665807	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09 [removed_by] PomBase:SPAC1782.09c [present_during] mitotic M phase	Table S1, Figure S1
PMID:22665807	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09 [removed_by] PomBase:SPAC1782.09c [present_during] mitotic M phase	Table S1, Figure S1
PMID:22665807	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC11B10.09 [removed_by] PomBase:SPAC1782.09c [present_during] mitotic M phase	Table S1, Figure S1
PMID:22665807	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09 [removed_by] PomBase:SPAC1782.09c [present_during] mitotic M phase	Table S1, Figure S1
PMID:22665807	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09 [removed_by] PomBase:SPAC1782.09c [present_during] mitotic M phase	Table S1, Figure S1
PMID:22665807	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09 [removed_by] PomBase:SPAC1782.09c [present_during] mitotic M phase	Table S1, Figure S1
PMID:22665807	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC11B10.09 [removed_by] PomBase:SPAC1782.09c [present_during] mitotic M phase	Table S1, Figure S1
PMID:22665807	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC11B10.09 [removed_by] PomBase:SPAC1782.09c [present_during] mitotic M phase	Table S1, Figure S1
PMID:22665807	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09 [removed_by] PomBase:SPAC1782.09c [present_during] mitotic M phase	Table S1, Figure S1
PMID:22665807	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09 [removed_by] PomBase:SPAC1782.09c [present_during] mitotic M phase	Table S1, Figure S1
PMID:22682245	GO:1990601	5' overhang single-stranded DNA endonuclease activity	(comment: cleaves unpaired nascent DNA in replication forks)
PMID:22682245	FYPO:0002061	inviable vegetative cell population	(comment: implies that dna2 E560A alone is inviable)
PMID:22682245	FYPO:0002060	viable vegetative cell population	(comment: implies that dna2 K961T alone is viable)
PMID:22683269	GO:0003723	RNA binding	(comment: assayed using bulk RNA)
PMID:22684255	PomGeneEx:0000018	protein level increased [during] mitotic G2 phase	(Figure 1a)
PMID:22684255	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPAC19E9.02	(Figure 1b)
PMID:22684255	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPAC19E9.02	(Figure 1b)
PMID:22684255	FYPO:0006291	increased protein level during mitotic G2 phase [assayed_using] PomBase:SPAC19E9.02	(Figure 1g)
PMID:22684255	FYPO:0006291	increased protein level during mitotic G2 phase [assayed_using] PomBase:SPAC19E9.02	(Figure 1g)
PMID:22684255	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC24B11.11c [added_during] mitotic G2 phase	(Figure 2f lanes 1, 2)
PMID:22684255	MOD:00046	O-phospho-L-serine [removed_by] PomBase:SPAC24B11.11c [added_during] mitotic G2 phase	(Figure 2f lanes 1, 2)
PMID:22684255	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC24B11.11c [added_during] mitotic G2 phase	(Figure 2f lanes 1, 2)
PMID:22684255	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Figure 3A; Table 1) indicating that inhibition of Sid2 or Fin1 delayed the timing of mitotic commitment until a new size threshold for division was me
PMID:22684255	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Figure 3A; Table 1) indicating that inhibition of Sid2 or Fin1 delayed the timing of mitotic commitment until a new size threshold for division was me
PMID:22684255	FYPO:0003306	decreased mitotic index	(Figure 3a)
PMID:22684255	FYPO:0003306	decreased mitotic index	(Figure 3a)
PMID:22684255	GO:0010971	positive regulation of G2/M transition of mitotic cell cycle	(Figure 4b) confirming that each kinase promotes mitotic commitment.
PMID:22684255	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Figure 4d)
PMID:22684255	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Figure 4d)
PMID:22684255	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Figure 4d)
PMID:22684255	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Figure 4d)
PMID:22684255	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Figure 4d)
PMID:22684255	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Figure 4d)
PMID:22684255	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Figure 4d)
PMID:22684255	FYPO:0000405	normal mitotic G2/M phase transition	(Figure 4d)
PMID:22684255	FYPO:0000405	normal mitotic G2/M phase transition	(Figure 4d)
PMID:22684255	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Figure 4d)
PMID:22684255	FYPO:0003306	decreased mitotic index	(Figure 4d)
PMID:22684255	GO:0010971	positive regulation of G2/M transition of mitotic cell cycle	(comment: CHECK mitotic commitment)
PMID:22684255	GO:0004674	protein serine/threonine kinase activity [part_of] positive regulation of G2/M transition of mitotic cell cycle [occurs_in] cytoplasm	(comment: CHECK upstream of pom1)
PMID:22696680	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	(Fig. 1A)
PMID:22696680	GO:0072686	mitotic spindle [exists_during] mitotic M phase	(Fig. 1A)
PMID:22696680	FYPO:0004731	normal protein localization to interphase microtubule plus-end	(Figure 1)
PMID:22696680	FYPO:0004731	normal protein localization to interphase microtubule plus-end	(Figure 1)
PMID:22696680	FYPO:0002760	short cytoplasmic microtubules	(Figure 1)
PMID:22696680	FYPO:0002760	short cytoplasmic microtubules	(Figure 1)
PMID:22696680	FYPO:0002112	viable curved vegetative cell	(Figure 2A)
PMID:22696680	FYPO:0001234	slow vegetative cell population growth	(Figure 2A)
PMID:22696680	FYPO:0002818	microtubule bundles present in decreased numbers	(Figure 2B)
PMID:22696680	FYPO:0005797	short microtubule bundle	(Figure 2C)
PMID:22696680	FYPO:0005681	decreased microtubule polymerization	(Figure 2D,2F)
PMID:22696680	FYPO:0005682	decreased microtubule depolymerization during vegetative growth	(Figure 2D,2F)
PMID:22696680	GO:0061863	microtubule plus end polymerase activity	(Figure 3) Supplemental Table S2, and Supplemental Figure S4
PMID:22696680	GO:1904511	cytoplasmic microtubule plus-end [exists_during] mitotic interphase	(comment: growing end ) (Fig. 1A)
PMID:22696680	FYPO:0004731	normal protein localization to interphase microtubule plus-end [assayed_using] PomBase:SPAC3C7.12	Supplemental Figure S1, C-E
PMID:22696680	FYPO:0004731	normal protein localization to interphase microtubule plus-end [assayed_using] PomBase:SPBC1604.20c	Supplemental Figure S1, C-E
PMID:22696680	FYPO:0004731	normal protein localization to interphase microtubule plus-end [assayed_using] PomBase:SPAC18G6.15	Supplemental Figure S1, C-E
PMID:22705791	FYPO:0003164	abolished nuclease activity	(comment: CHECK not sure if it is endo, exo or both? so went with more general term)
PMID:22705791	GO:0004518	nuclease activity	(comment: CHECK not sure if it is endo, exo, or both. It is def acting on DNA. More specific terms for DNA specify endo or exo.)
PMID:22711988	FYPO:0001269	abolished protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPAPB17E12.06	(comment: implies that MIND complex is required for Sos7 to localize to the kinetochore)
PMID:22711988	GO:0000776	kinetochore	(comment: kinetochore localization requires MIND complex)
PMID:22718908	FYPO:0006728	abolished mitotic DNA replication initiation	BrdU incorporation
PMID:22718908	FYPO:0006728	abolished mitotic DNA replication initiation	BrdU incorporation
PMID:22718908	FYPO:0006727	abolished mitotic DNA replication elongation	BrdU incorporation
PMID:22718908	FYPO:0006728	abolished mitotic DNA replication initiation	BrdU incorporation
PMID:22718908	FYPO:0006733	normal CMG complex progression from replication origin [has_severity] high	inferred from localization of proteins distal to origin
PMID:22718908	FYPO:0006731	decreased CMG complex progression from replication origin [has_severity] high	inferred from localization of proteins distal to origin
PMID:22718908	FYPO:0006731	decreased CMG complex progression from replication origin [has_severity] high	inferred from localization of proteins distal to origin
PMID:22718908	FYPO:0006731	decreased CMG complex progression from replication origin [has_severity] low	inferred from localization of proteins distal to origin
PMID:22718908	FYPO:0006726	normal CMG complex assembly	inferred from normal localization of CMG proteins at origin
PMID:22723423	GO:0000400	four-way junction DNA binding	(comment: Fml1 binds to the four-way junction at a displacement (D) loop.)
PMID:22723423	GO:0009378	four-way junction helicase activity	(comment: Fml1 catalyses the dissociation of displacement (D) loops)
PMID:22727667	GO:0062072	histone H3K9me2/3 reader activity [has_input] hht1/Me(K9) [part_of] siRNA-mediated pericentric heterochromatin formation [occurs_in] nucleosome	(comment: binds H3K9me)
PMID:22727667	GO:0062072	histone H3K9me2/3 reader activity [has_input] hht3/Me(K9) [part_of] siRNA-mediated pericentric heterochromatin formation [occurs_in] nucleosome	(comment: binds H3K9me)
PMID:22727667	GO:0062072	histone H3K9me2/3 reader activity [has_input] hht2/Me(K9) [part_of] siRNA-mediated pericentric heterochromatin formation [occurs_in] nucleosome	(comment: binds H3K9me)
PMID:22737087	FYPO:0007391	inviable aneuploid spore [has_penetrance] high	(Fig. 1 Table 1) (comment: affects C1 more than C2 type colonies)
PMID:22737087	FYPO:0007391	inviable aneuploid spore [has_penetrance] high	(Fig. 1, Table 1) (comment: affects C1 and C2 type colonies)
PMID:22737087	FYPO:0007391	inviable aneuploid spore [has_penetrance] high	(Fig. 1, Table 1) (comment: affects C1 and C2 type colonies)
PMID:22737087	FYPO:0007391	inviable aneuploid spore [has_penetrance] high	(Fig. 1, Table 1) (comment: affects C1 type colonies)
PMID:22737087	FYPO:0007391	inviable aneuploid spore [has_penetrance] high	(Fig. 1, Table 1) (comment: affects C1 type colonies)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2)
PMID:22737087	FYPO:0007391	inviable aneuploid spore [has_penetrance] high	(Fig. 2)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2) (comment: decreased aneuploid cell viability during vegetative growth)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2) (comment: decreased aneuploid cell viability during vegetative growth)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2) (comment: decreased aneuploid cell viability during vegetative growth)
PMID:22737087	FYPO:0001357	normal vegetative cell population growth	(Fig. 2) (comment: normal population growth in presence of aneuploid cells)
PMID:22737087	FYPO:0001357	normal vegetative cell population growth	(Fig. 2) (comment: normal population growth in presence of aneuploid cells)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 2) (comment: reduced growth may not be specific to aneuploidy as it also interact with gtb1 though looks quite good to me)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2) (comment: reduced growth may not be specific to aneuploidy as it also interacts with gtb1)
PMID:22737087	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 3A) (comment: This strain is disomic for Chromosome 3)
PMID:22737087	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 3A) (comment: This strain is disomic for Chromosome 3)
PMID:22737087	FYPO:0007392	increased loss of disomic chromosome 3 [has_severity] high	(Fig. 3B) ((comment: This strain is disomic for Chromosome 3)
PMID:22737087	FYPO:0007392	increased loss of disomic chromosome 3 [has_severity] high	(Fig. 3B) (comment: This strain is disomic for Chromosome 3)
PMID:22737087	FYPO:0007391	inviable aneuploid spore	(Fig. 4) (comment: Type C1 colonies have highly elongated cells and are due to various types of aneuploidy. Authors suggest that not3 is required to maintain cell growth)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 6)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 6)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 6)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 6)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 6)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 6) (comment: reduced growth may not be specific to aneuploidy as it also interacts with gtb1-93)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S1) (comment: CHECK decreased aneuploid cell viability during vegetative growth)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. S1) (comment: decreased aneuploid cell viability during vegetative growth)
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S1) (comment: decreased aneuploid cell viability during vegetative growth)
PMID:22737087	FYPO:0001326	altered RNA level during vegetative growth	(comment: All the genes affect by at least 1.5 fold (141) are reported in Table S2)
PMID:22737087	FYPO:0001326	altered RNA level during vegetative growth	(comment: All the genes affect by at least 1.5 fold (17) are reported in Table S2)
PMID:22737087	FYPO:0001326	altered RNA level during vegetative growth	(comment: All the genes affect by at least 1.5 fold (61) are reported in Table S2)
PMID:22737087	FYPO:0007392	increased loss of disomic chromosome 3 [has_severity] high	Table 2 (comment: This strain is disomic for Chromosome 3)
PMID:22737087	FYPO:0007392	increased loss of disomic chromosome 3 [has_severity] high	Table 2 (comment: This strain is disomic for Chromosome 3)
PMID:22737087	FYPO:0007392	increased loss of disomic chromosome 3 [has_severity] high	Table 2 (comment: This strain is disomic for Chromosome 3)
PMID:22737087	FYPO:0007392	increased loss of disomic chromosome 3 [has_severity] high	Table 2 (comment: This strain is disomic for Chromosome 3)
PMID:22737087	FYPO:0007391	inviable aneuploid spore [has_penetrance] high	Table1 Fig1 (comment: affects C1 and C2 type colonies)
PMID:22737087	FYPO:0007391	inviable aneuploid spore	data not shown
PMID:22737087	FYPO:0007391	inviable aneuploid spore	data not shown
PMID:22737087	FYPO:0007391	inviable aneuploid spore	data not shown
PMID:22737087	FYPO:0007391	inviable aneuploid spore	data not shown
PMID:22737087	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	data not shown
PMID:22768388	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 1A)
PMID:22768388	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 1A)
PMID:22768388	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC57A10.02	(Fig. 4C)
PMID:22768388	FYPO:0000082	decreased cell population growth at high temperature	(Figure 1A)
PMID:22768388	FYPO:0000082	decreased cell population growth at high temperature	(Figure 1A)
PMID:22768388	FYPO:0000082	decreased cell population growth at high temperature	(Figure 1A)
PMID:22768388	FYPO:0001492	viable elongated vegetative cell	(Figure 1B)
PMID:22768388	FYPO:0000118	multiseptate vegetative cell	(Figure 1B)
PMID:22768388	FYPO:0000118	multiseptate vegetative cell	(Figure 1B)
PMID:22768388	FYPO:0001492	viable elongated vegetative cell	(Figure 1B)
PMID:22768388	FYPO:0001234	slow vegetative cell population growth	(Figure 1C)
PMID:22768388	FYPO:0001357	normal vegetative cell population growth	(Figure 1C)
PMID:22768388	FYPO:0001357	normal vegetative cell population growth	(Figure 1C)
PMID:22768388	FYPO:0001234	slow vegetative cell population growth	(Figure 1C)
PMID:22768388	FYPO:0001357	normal vegetative cell population growth	(Figure 1C)
PMID:22768388	FYPO:0001234	slow vegetative cell population growth	(Figure 1C)
PMID:22768388	FYPO:0005177	abolished tRNA wobble position uridine thiolation	(Figure S1C)
PMID:22768388	FYPO:0002672	normal growth on rapamycin	(Figure S1E)
PMID:22768388	FYPO:0002672	normal growth on rapamycin	(Figure S1E)
PMID:22768388	FYPO:0000674	normal cell population growth at high temperature	(Figure S1E)
PMID:22768388	FYPO:0000674	normal cell population growth at high temperature	(Figure S1E)
PMID:22768388	FYPO:0000674	normal cell population growth at high temperature	(Figure S1E)
PMID:22768388	FYPO:0000674	normal cell population growth at high temperature	(Figure S1E)
PMID:22768388	FYPO:0002672	normal growth on rapamycin	(Figure S1E)
PMID:22768388	FYPO:0002672	normal growth on rapamycin	(Figure S1E)
PMID:22768388	FYPO:0002834	decreased chromatin silencing at centromere	(Figure S4)
PMID:22768388	FYPO:0003218	abolished tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridine biosynthesis	(Figures S1C and S1D)
PMID:22768388	FYPO:0003503	normal vegetative cell length	data not shown
PMID:22768388	FYPO:0002360	normal chromatin silencing at centromere	data not shown
PMID:22792081	GO:0005515	protein binding	(comment: CHECK This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues.)
PMID:22792081	GO:0005515	protein binding [has_input] crb2/Phos(T73,S80) [part_of] mitotic G2 DNA damage checkpoint signaling	(comment: CHECK This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues.)
PMID:22792081	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPCC1259.13 [part_of] mitotic G2 DNA damage checkpoint signaling	(comment: CHECK This interaction depends on the phosphorylation of Crb2 on the T73 and S80 residues.)
PMID:22809626	GO:0005515	protein binding [happens_during] mitotic anaphase	"(comment: happens during metaphase and happens during anaphase. I can't say ""decreased during cytokinesis"", only option would be to say ""not during cytokinesis"" which isn't strictly true.)"
PMID:22809626	GO:0005515	protein binding [happens_during] mitotic metaphase	"(comment: happens during metaphase and happens during anaphase. I can't say ""decreased during cytokinesis"", only option would be to say ""not during cytokinesis"" which isn't strictly true.)"
PMID:22809626	GO:0005515	protein binding [happens_during] mitotic anaphase	"(comment: happens during metaphase and happens during anaphase. I can't say ""decreased during cytokinesis"", only option would be to say ""not during cytokinesis"" which isn't strictly true.)"
PMID:22809626	GO:0005515	protein binding [happens_during] mitotic metaphase	"(comment: happens during metaphase and happens during anaphase. I can't say ""decreased during cytokinesis"", only option would be to say ""not during cytokinesis"" which isn't strictly true.)"
PMID:22825872	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC106.01	(Fig. 2A) When proper chromosome attachment was prevented by a conditional mutation in kinesin-5 (cut7-446), Mph1 localized to kinetochores, but the enrichment was abrogated by chemical genetic inhibition of Ark1 with the small molecule 1NM-PP1 (Fig. 3A).
PMID:22825872	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC106.01	(Fig. 3B) Indeed, Ark1 and Mph1 are fully or partially required for the kinetochore enrichment of all other SAC proteins (Fig. 4A; supplementary material Figs S5-S10).
PMID:22825872	FYPO:0003307	increased mitotic index	(Fig. 3C) (inhibiting Ark1 does not rescue the Mph1-kinetochore targeting, arguing that Ark1 is upstream)
PMID:22825872	FYPO:0003307	increased mitotic index	(Fig. 3C)increased mitotic index (Fig. S4A)
PMID:22825872	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC106.01	(Fig. 4A and S1)
PMID:22825872	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC3D6.04c	(Fig. 4A and S7)
PMID:22825872	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c	(Fig. 4A and S7)
PMID:22825872	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC20F10.06	(Fig. 4A and S8)
PMID:22825872	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC20F10.06	(Fig. 4A and S8)
PMID:22825872	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPCC1795.01c	(Fig. 4A and S9)
PMID:22825872	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPCC1322.12c	(Fig. 4B and S5)
PMID:22825872	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPCC1322.12c	(Fig. 4B)
PMID:22825872	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c	(Fig. 4C)
PMID:22825872	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC3D6.04c	(Fig. 4C).
PMID:22825872	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPCC1322.12c	(Fig. S5)
PMID:22825872	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPAC23H3.08c	(Fig. S6) Indeed, Ark1 and Mph1 are fully or partially required for the kinetochore enrichment of all other SAC proteins (Fig. 4A; supplementary material Figs S5-S10).
PMID:22825872	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c	(Fig. S7)
PMID:22825872	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC20F10.06	(Fig. S8)
PMID:22825872	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPCC1795.01c	(Fig. S9F)
PMID:22825872	FYPO:0005366	abolished protein phosphorylation during mitosis [assayed_using] PomBase:SPAC1834.04	(Figure S4B and C)
PMID:22825872	FYPO:0005366	abolished protein phosphorylation during mitosis [assayed_using] PomBase:SPBC1105.11c	(Figure S4B and C)
PMID:22825872	FYPO:0005366	abolished protein phosphorylation during mitosis [assayed_using] PomBase:SPBC8D2.04	(Figure S4B and C)
PMID:22825872	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC20F10.06	(Figure S8E and F) Indeed, Ark1 and Mph1 are fully or partially required for the kinetochore enrichment of all other SAC proteins (Fig. 4A; supplementary material Figs S5-S10).
PMID:22825872	FYPO:0003307	increased mitotic index [has_severity] medium	(comment: CHECK 35% cells) (Fig. 1E,F).
PMID:22825872	FYPO:0003307	increased mitotic index [has_severity] high	(comment: CHECK 60% cells) Forced recruitment of wild-type Mph1 to kinetochores lead to apronounced delay in mitosis and a growth defect (Fig. 1E,F)
PMID:22825872	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(comment: CHECK ditto)
PMID:22825872	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	In the presence of Mph1-D1-150, the SAC was still functional in bub3D cells, although the mitotic delay was shorter than in mph1-D1-150 or bub3D cells (Fig. 2C).
PMID:22825872	FYPO:0004318	abolished mitotic spindle assembly checkpoint	In the presence of Mph1-D1-302, the SAC response in bub3D cells was abrogated (Fig. 2C), demonstrating that recruitment of Mph1 to kinetochores is necessary for SAC function in bub3D cells.
PMID:22825872	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c	Indeed, Ark1 and Mph1 are fully or partially required for the kinetochore enrichment of all other SAC proteins (Fig. 4A; supplementary material Figs S5-S10).
PMID:22825872	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC106.01	Mph1 localizes to unattached kinetochores in bub3D cells (Fig. 2A).
PMID:22825872	FYPO:0003762	normal mitotic spindle assembly checkpoint	The shorter truncation (Mph1-D1-150) maintained kinetochore localization and SAC signaling
PMID:22825872	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC106.01	The shorter truncation (Mph1-D1-150) maintained kinetochore localization and SAC signaling
PMID:22825872	GO:0090267	positive regulation of mitotic cell cycle spindle assembly checkpoint	Together this suggests that Ark1 is directly and continuously required to maintain Mph1 localization to kinetochores.
PMID:22825872	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC106.01	abolished both kinetochore localization and SAC signaling (Fig. 1C,D), suggesting that kinetochore localization is crucial for SAC activity.
PMID:22825872	FYPO:0003762	normal mitotic spindle assembly checkpoint	and the fraction of cells, in which a signal could be detected (supplementary material Fig. S1), were similar between bub3+ and bub3D cells
PMID:22825872	FYPO:0004318	abolished mitotic spindle assembly checkpoint	and the fraction of cells, in which a signal could be detected (supplementary material Fig. S1), were similar between bub3+ and bub3D cells
PMID:22825872	FYPO:0003736	normal mitotic index	rescued by deletion of mad2, which (forced recruitment of Mph1 artificially promoted SAC signaling andthat the fusion to Mis12 did not impair kinetochore function.
PMID:22848669	FYPO:0001470	normal growth on tacrolimus [has_severity] high	(Figure 2)
PMID:22848669	FYPO:0000098	sensitive to calcium [has_severity] high	(Figure 2)
PMID:22848669	FYPO:0006836	sensitive to magnesium chloride [has_severity] high	(Figure 2)
PMID:22848669	FYPO:0000086	sensitive to tacrolimus [has_severity] high	(Figure 2)
PMID:22848669	FYPO:0005970	normal growth on magnesium chloride [has_severity] high	(Figure 2)
PMID:22848669	FYPO:0005970	normal growth on magnesium chloride [has_severity] high	(Figure 3B)
PMID:22848669	FYPO:0006836	sensitive to magnesium chloride [has_severity] high	(Figure 3B)
PMID:22848669	FYPO:0006836	sensitive to magnesium chloride [has_severity] high	(Figure 3B)
PMID:22848669	FYPO:0006836	sensitive to magnesium chloride [has_severity] high	(Figure 3B)
PMID:22848669	FYPO:0006836	sensitive to magnesium chloride [has_severity] high	(Figure 3B)
PMID:22848669	FYPO:0006836	sensitive to magnesium chloride [has_severity] high	(Figure 3B)
PMID:22848669	FYPO:0006836	sensitive to magnesium chloride [has_severity] high	(Figure 3B)
PMID:22848669	FYPO:0005970	normal growth on magnesium chloride [has_severity] high	(Figure 3B)
PMID:22848669	FYPO:0005970	normal growth on magnesium chloride [has_severity] high	(Figure 3B)
PMID:22848669	FYPO:0005970	normal growth on magnesium chloride [has_severity] high	(Figure 3B)
PMID:22848669	FYPO:0005970	normal growth on magnesium chloride [has_severity] high	(Figure 3B)
PMID:22848669	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC1705.03c	(Figure 3C) The immunoblot analysis detected an appreciable amount of Ecm33 fragments A, C, F, G, and I
PMID:22848669	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC1705.03c	(Figure 3C) The immunoblot analysis detected an appreciable amount of Ecm33 fragments A, C, F, G, and I
PMID:22848669	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC1705.03c	(Figure 3C) The immunoblot analysis detected an appreciable amount of Ecm33 fragments A, C, F, G, and I
PMID:22848669	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC1705.03c	(Figure 3C) The immunoblot analysis detected an appreciable amount of Ecm33 fragments A, C, F, G, and I
PMID:22848669	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC1705.03c	(Figure 3C) The immunoblot analysis detected an appreciable amount of Ecm33 fragments A, C, F, G, and I
PMID:22848669	FYPO:0001983	protein absent from cell [assayed_protein] PomBase:SPAC1705.03c	(Figure 3C) but failed to detect fragment B, D, E, H, J or K.
PMID:22848669	FYPO:0001983	protein absent from cell [assayed_protein] PomBase:SPAC1705.03c	(Figure 3C) but failed to detect fragment B, D, E, H, J or K.
PMID:22848669	FYPO:0001983	protein absent from cell [assayed_protein] PomBase:SPAC1705.03c	(Figure 3C) but failed to detect fragment B, D, E, H, J or K.
PMID:22848669	FYPO:0001983	protein absent from cell [assayed_protein] PomBase:SPAC1705.03c	(Figure 3C) but failed to detect fragment B, D, E, H, J or K.
PMID:22848669	FYPO:0001983	protein absent from cell [assayed_protein] PomBase:SPAC1705.03c	(Figure 3C) but failed to detect fragment B, D, E, H, J or K.
PMID:22848669	FYPO:0001983	protein absent from cell [assayed_protein] PomBase:SPAC1705.03c	(Figure 3C) but failed to detect fragment B, D, E, H, J or K.
PMID:22848669	FYPO:0008258	decreased protein localization to cell surface [assayed_protein] PomBase:SPAC1705.03c	(comment: ****decreased to cell surface, mislocalized to cytoplasm*****) In Dapm1 cells, in contrast, GFP-Ecm33 primarily localized as dot-like structures that were observed in the cytoplasm (Figure 6A, arrows) as well as at the cell surface and the division site (Figure 6A, arrowheads).
PMID:22848669	FYPO:0008260	decreased protein localization to cell surface, protein mislocalized to endoplasmic reticulum [assayed_protein] PomBase:SPAC1705.03c	As expected, GFP-Ecm33 primarily localized to the ER and to the cell surface in the its8-1 mutant cells (Figure 4D, arrows), suggesting that the impairment of GPI anchor synthesis caused the defective attachment of GPI-anchor to the Ecm33 protein thereby resulting in the abnormal GFP-Ecm33 localization in the ER.
PMID:22848669	GO:0009986	cell surface	Ecm33 localized to the cell surface or the medial regions. (Figure 4)
PMID:22848669	FYPO:0000086	sensitive to tacrolimus [has_severity] low	Likewise, these three genes complemented the FK506-sensitive phenotype of the cis4-1 mutant (Figure 1A).
PMID:22848669	FYPO:0000086	sensitive to tacrolimus [has_severity] low	Likewise, these three genes complemented the FK506-sensitive phenotype of the cis4-1 mutant (Figure 1A).
PMID:22848669	FYPO:0000086	sensitive to tacrolimus [has_severity] high	Likewise, these three genes complemented the FK506-sensitive phenotype of the cis4-1 mutant (Figure 1A).
PMID:22848669	FYPO:0000086	sensitive to tacrolimus [has_severity] medium	Likewise, these three genes complemented the FK506-sensitive phenotype of the cis4-1 mutant (Figure 1A).
PMID:22848669	FYPO:0006836	sensitive to magnesium chloride [has_severity] low	Notably, overexpression of the ecm33+ gene partially suppressed the MgCl2 sensitivity of cis4-1 mutant, and overexpression of the aah3+ and gaz2+ genes more strongly suppressed the MgCl2 sensitivity of the cis4-1 mutant (Figure 1A).
PMID:22848669	FYPO:0006836	sensitive to magnesium chloride [has_severity] medium	Notably, overexpression of the ecm33+ gene partially suppressed the MgCl2 sensitivity of cis4-1 mutant, and overexpression of the aah3+ and gaz2+ genes more strongly suppressed the MgCl2 sensitivity of the cis4-1 mutant (Figure 1A).
PMID:22848669	FYPO:0006836	sensitive to magnesium chloride [has_severity] low	Notably, overexpression of the ecm33+ gene partially suppressed the MgCl2 sensitivity of cis4-1 mutant, and overexpression of the aah3+ and gaz2+ genes more strongly suppressed the MgCl2 sensitivity of the cis4-1 mutant (Figure 1A).
PMID:22848669	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	On the effect of temperature, in the its8-1Dcis4 double mutants, these cells exhibited more marked temperature sensitivity than that of the its8-1 single mutants (Figure 5B), suggesting that there is a genetic interaction between Its8 and Cis4.
PMID:22848669	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	On the effect of temperature, in the its8-1Dcis4 double mutants, these cells exhibited more marked temperature sensitivity than that of the its8-1 single mutants (Figure 5B), suggesting that there is a genetic interaction between Its8 and Cis4.
PMID:22848669	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	On the effect of temperature, in the its8-1Dcis4 double mutants, these cells exhibited more marked temperature sensitivity than that of the its8-1 single mutants (Figure 5B), suggesting that there is a genetic interaction between Its8 and Cis4.
PMID:22848669	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	On the effect of temperature, in the its8-1Dcis4 double mutants, these cells exhibited more marked temperature sensitivity than that of the its8-1 single mutants (Figure 5B), suggesting that there is a genetic interaction between Its8 and Cis4.
PMID:22848669	FYPO:0007589	protein mislocalized to endosome [assayed_protein] PomBase:SPBC1E8.05	Similarly, in the wild-type cells, GFP-Gaz2 also clearly localized at the cell surface and medial regions (Figure 6C), while in Dapm1 cells, GFP-Gaz2 localized as intracellular dot-like structures (Figure 6C).
PMID:22848669	FYPO:0007589	protein mislocalized to endosome [assayed_protein] PomBase:SPBC1E8.05	Similarly, in the wild-type cells, GFP-Gaz2 also clearly localized at the cell surface and medial regions (Figure 6C), while in Dapm1 cells, GFP-Gaz2 localized as intracellular dot-like structures (Figure 6C).
PMID:22848669	FYPO:0006836	sensitive to magnesium chloride [has_severity] high	The cis4-1 mutant cells grew well in rich YPD medium, however, in the presence of 0.15 M MgCl2, the cis4-1 cells failed to grow, whereas wild-type cells grew well (Figure 1A).
PMID:22848669	FYPO:0000086	sensitive to tacrolimus [has_severity] high	The results showed that the addition of Zn2+ to the medium significantly rescued the high temperature-sensitive and FK506-sensitive phenotypes of the its8-1 mutant (Figure 5A)
PMID:22848669	FYPO:0001470	normal growth on tacrolimus [has_severity] high	The results showed that the addition of Zn2+ to the medium significantly rescued the high temperature-sensitive and FK506-sensitive phenotypes of the its8-1 mutant (Figure 5A)
PMID:22848669	GO:0099638	endosome to plasma membrane protein transport	Thus, GFP-Ecm33 localized at Golgi/endosome structures in addition to the cell surface and the division site in these mutants, suggesting that GPI-anchored proteins were not correctly transported and were retained at the Golgi/endosome structures in these membrane trafficking mutants
PMID:22848669	FYPO:0007589	protein mislocalized to endosome [assayed_protein] PomBase:SPAC1705.03c	Thus, GFP-Ecm33 localized at Golgi/endosome structures in addition to the cell surface and the division site in these mutants, suggesting that GPI-anchored proteins were not correctly transported and were retained at the Golgi/endosome structures in these membrane trafficking mutants
PMID:22848669	FYPO:0007589	protein mislocalized to endosome [assayed_protein] PomBase:SPAC1705.03c	Thus, GFP-Ecm33 localized at Golgi/endosome structures in addition to the cell surface and the division site in these mutants, suggesting that GPI-anchored proteins were not correctly transported and were retained at the Golgi/endosome structures in these membrane trafficking mutants
PMID:22848669	GO:0099638	endosome to plasma membrane protein transport	Thus, GFP-Ecm33 localized at Golgi/endosome structures in addition to the cell surface and the division site in these mutants, suggesting that GPI-anchored proteins were not correctly transported and were retained at the Golgi/endosome structures in these membrane trafficking mutants
PMID:22848669	FYPO:0007589	protein mislocalized to endosome [assayed_protein] PomBase:SPAC1705.03c	Thus, GFP-Ecm33 localized at Golgi/endosome structures in addition to the cell surface and the division site in these mutants, suggesting that GPI-anchored proteins were not correctly transported and were retained at the Golgi/endosome structures in these membrane trafficking mutants
PMID:22848669	GO:0099638	endosome to plasma membrane protein transport	Thus, GFP-Ecm33 localized at Golgi/endosome structures in addition to the cell surface and the division site in these mutants, suggesting that GPI-anchored proteins were not correctly transported and were retained at the Golgi/endosome structures in these membrane trafficking mutants
PMID:22848669	FYPO:0002060	viable vegetative cell population	We constructed a null mutation in the ecm33+ and gaz2+ genes, respectively (see Materials and Methods) and found that the gaz2 deletion mutant was also viable (Figure 2A, upper panel), indicating that Gaz2 is not essential for cell viability.
PMID:22848669	FYPO:0002060	viable vegetative cell population	We constructed a null mutation in the ecm33+ and gaz2+ genes, respectively (see Materials and Methods) and found that the gaz2 deletion mutant was also viable (Figure 2A, upper panel), indicating that Gaz2 is not essential for cell viability.
PMID:22891259	GO:0032153	cell division site	(Fig. 1)
PMID:22891259	GO:0032153	cell division site	(Fig. 1)
PMID:22891259	GO:0031671	primary cell septum biogenesis	(comment: Explosive cell separation due to a weak primary septum. Absence of a secondary septum. )
PMID:22891673	FYPO:0000424	delayed onset of endocytosis during vegetative growth	(comment: Assayed by FM4-64 uptake)
PMID:22891673	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization	(comment: At the end of ring constriction Filamentous projections from the unclosed ring toward the cytoplasm)
PMID:22891673	FYPO:0002438	short, misoriented actin cables	(comment: Weak actin cables)
PMID:22891673	FYPO:0002526	sensitive to latrunculin B	(comment: assayed at 32C, which is semi-permissive for sec3-913)
PMID:22891673	FYPO:0000639	delayed onset of septum assembly	(comment: decreased septum closure)
PMID:22891673	FYPO:0000639	delayed onset of septum assembly	(comment: decreased/delayed septum closure)
PMID:22891673	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	(comment: normal localization in several mutants indicates that Sec3 localization is independent of exocytosis and vesicle-mediated transport along microtubules)
PMID:22891673	FYPO:0000650	increased septation index	(comment: septation index constantly high)
PMID:22891673	FYPO:0000650	increased septation index	(comment: septation index increased gradually over time)
PMID:22895252	GO:0030466	silent mating-type cassette heterochromatin formation	(Fig. S2)
PMID:22905165	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPBC1289.01c [has_penetrance] 30	(Fig. 1B)
PMID:22905165	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPBC1289.01c	(Fig. 1B) in which the SIN signal does not turn off, Cfh3p localized to the edge of the growing septa and it remained at the septal area after the septa had been completed. Thus, Cfh3p can arrive at the cell midzone in the absence of the SIN pathway but it requires that the SIN signal must be turned off for it to be removed from the cell equator after mitosis
PMID:22905165	FYPO:0002527	increased duration of protein localization to cell division site [assayed_using] PomBase:SPBC1289.01c	(Fig. 1B) in which the SIN signal does not turn off, Cfh3p localized to the edge of the growing septa and it remained at the septal area after the septa had been completed. Thus, Cfh3p can arrive at the cell midzone in the absence of the SIN pathway but it requires that the SIN signal must be turned off for it to be removed from the cell equator after mitosis
PMID:22905165	FYPO:0001401	abnormal protein localization to cell division site [has_penetrance] high [assayed_using] PomBase:SPBC1709.01	(Fig. S1)
PMID:22905165	FYPO:0001401	abnormal protein localization to cell division site [has_penetrance] high [assayed_using] PomBase:SPBC16A3.01	(Fig. S1)
PMID:22905165	FYPO:0001401	abnormal protein localization to cell division site [has_penetrance] high [assayed_using] PomBase:SPAC20G8.05c	(Fig. S1)
PMID:22905165	FYPO:0001401	abnormal protein localization to cell division site [has_penetrance] high [assayed_using] PomBase:SPAP8A3.08	(Fig. S1)
PMID:22905165	FYPO:0002869	decreased protein localization to cell division site [has_penetrance] high [assayed_using] PomBase:SPBC19G7.05c	(Figure S2) (comment: A protein distributed in cortex)
PMID:22905165	FYPO:0003338	abnormal actomyosin contractile ring morphology [has_penetrance] high	(comment: Cdc15-GFP)
PMID:22905165	FYPO:0003338	abnormal actomyosin contractile ring morphology [has_penetrance] medium	(comment: Cdc15-GFP) However, we observed that a number of the Cdc15-GFP and the GFP-Cdc4 rings were asymmetric or broken.
PMID:22905165	FYPO:0003338	abnormal actomyosin contractile ring morphology [has_penetrance] high	(comment: Cdc15-GFP) Supplemental Figure S3
PMID:22905165	FYPO:0002719	decreased protein localization to septum [has_penetrance] medium [assayed_using] PomBase:SPBC19G7.05c	(comment: GFP-Bgs1)
PMID:22905165	FYPO:0003316	normal protein localization to growing cell tip [assayed_using] PomBase:SPBC19G7.05c	(comment: GFP-Bgs1)
PMID:22905165	GO:0000935	division septum [exists_during] mitotic M phase	(comment: GFP-Cfh3) Figure 1A
PMID:22905165	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	(comment: GFP-Cfh3) Figure 1A
PMID:22905165	FYPO:0003338	abnormal actomyosin contractile ring morphology [has_penetrance] medium	(comment: used sorbitol but multiple stresses were tested) Cdc15-GFP However, we observed that a number of the Cdc15-GFP and the GFP-Cdc4 rings were asymmetric or broken.
PMID:22912768	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPCC11E10.01	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22912768	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBPB10D8.02c	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22912768	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC750.07c	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22912768	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBPB2B2.06c	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22912768	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBPB10D8.01	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22912768	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC1289.14	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22912768	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC212.08c	(comment: mah: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03))
PMID:22918943	GO:0110115	Cdr2 medial cortical node complex	(Figure 1A, 2A)
PMID:22918943	GO:0071341	medial cortical node	(Figure 1A, 2A)
PMID:22918943	FYPO:0003339	decreased rate of actomyosin contractile ring assembly	(Figure 3A)
PMID:22918943	FYPO:0001364	abnormal actomyosin contractile ring contraction	(Figure 3A)
PMID:22918943	FYPO:0007115	abolished protein localization to medial cortical node, with protein mislocalized to cytoplasm during mitotic interphase [assayed_using] PomBase:SPAC20G8.05c	(Figure 5, I, J, and L)
PMID:22918943	FYPO:0007115	abolished protein localization to medial cortical node, with protein mislocalized to cytoplasm during mitotic interphase [assayed_using] PomBase:SPCC645.05c	(Figure 5, I, J, and L)
PMID:22918943	FYPO:0007115	abolished protein localization to medial cortical node, with protein mislocalized to cytoplasm during mitotic interphase [assayed_using] PomBase:SPAC4F8.13c	(Figure 5, I, J, and L)
PMID:22918943	FYPO:0004594	branched, elongated, septated cell	(Figure 7)
PMID:22918943	FYPO:0001370	abnormal protein localization [assayed_using] PomBase:SPCC1223.06	(Figure 7)
PMID:22918952	FYPO:0006232	abolished protein phosphorylation during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC1782.09c	(comment: unspecfied RxxS site(s))
PMID:22918952	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC1782.09c	(comment: unspecfied RxxS site(s))
PMID:22918954	FYPO:0003210	mislocalized, misoriented septum [has_severity] low	(Fig. 3B)
PMID:22918954	FYPO:0003210	mislocalized, misoriented septum [has_severity] low	(Fig. 3B)
PMID:22918954	FYPO:0003210	mislocalized, misoriented septum [has_severity] high	(Fig. 3B)
PMID:22918954	FYPO:0003203	curved septum	(Fig. 3B)
PMID:22918954	FYPO:0004750	elongated septated vegetative cell	(Fig. 3B)
PMID:22918954	FYPO:0003210	mislocalized, misoriented septum [has_severity] medium	(Fig. 3B)
PMID:22918954	FYPO:0003210	mislocalized, misoriented septum [has_severity] medium	(Fig. 3B)
PMID:22918954	FYPO:0003210	mislocalized, misoriented septum [has_severity] medium	(Fig. 3B)
PMID:22918954	FYPO:0003210	mislocalized, misoriented septum [has_severity] low	(Fig. 3B)
PMID:22918954	FYPO:0000339	mislocalized septum during vegetative growth [has_severity] high	(Fig. 3B) (comment: COMMENT CHECK asymettrically localized septum)
PMID:22918954	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPCC4B3.15	(Figure 4)
PMID:22918954	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_using] PomBase:SPCC4B3.15	(Figure 4)
PMID:22918954	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPCC4B3.15	(Figure 4)
PMID:22918954	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPCC4B3.15	(Figure 4)
PMID:22918954	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPCC4B3.15	(Figure 4)
PMID:22918954	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPCC4B3.15	(Figure 4)
PMID:22918954	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPCC4B3.15	(Figure 4)
PMID:22959349	MOD:00046	O-phospho-L-serine [present_during] mitotic cell cycle	(comment: Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.)
PMID:22959349	MOD:00046	O-phospho-L-serine [added_during] mitotic M phase	(comment: Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.)
PMID:22959349	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09 [added_during] mitotic M phase	(comment: Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.)
PMID:22959349	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09 [added_during] mitotic M phase	(comment: Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.)
PMID:22959349	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC11B10.09 [added_during] mitotic M phase	(comment: Cdc2 phosphorylates Rap1 at Thr378, Ser422, and Ser513 during M phase. Ser456 of Rap1 is also phosphorylated during M phase by an unknown kinase. Ser213 of Rap1 is phosphorylated throughout the cell cycle. These phosphorylations are required for the efficient detachment of telomeres from the nuclear envelope.)
PMID:22959349	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC1778.02	(comment: at Ser/Thr-Pro site)
PMID:22959349	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC1778.02	(comment: at Ser/Thr-Pro site)
PMID:22959349	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC1778.02	(comment: at Ser/Thr-Pro site)
PMID:22959349	GO:1904537	negative regulation of mitotic telomere tethering at nuclear periphery [happens_during] mitotic M phase	(comment: cdc2 phosphorylates rap1. phosphorylated rap1 binds bqt4 less efficiently. rap1-bqt4 binding is required for telomere tethering at nuclear periphery. In WT cells telomere tethering is abolished during M phase)
PMID:22976295	GO:0038202	TORC1 signaling	"(comment: I guess everything in the signaling cascade that isn't the ""final effector"" is part of the signaling cascade?)"
PMID:22976295	GO:0038202	TORC1 signaling	"(comment: I guess everything in the signaling cascade that isn't the ""final effector"" is part of the signaling cascade?)"
PMID:22976295	MOD:00046	O-phospho-L-serine [present_during] cellular response to ammonium ion	(comment: blotted for rps601 & rps602 simultaneously)
PMID:22976295	MOD:00046	O-phospho-L-serine [absent_during] cellular response to nitrogen starvation	(comment: blotted for rps601 & rps602 simultaneously)
PMID:22976295	MOD:00046	O-phospho-L-serine [present_during] cellular response to cycloheximide	(comment: blotted for rps601 & rps602 simultaneously)
PMID:22976295	MOD:00046	O-phospho-L-serine [present_during] cellular response to ammonium ion	(comment: blotted for rps601 & rps602 simultaneously)
PMID:22976295	MOD:00046	O-phospho-L-serine [absent_during] cellular response to nitrogen starvation	(comment: blotted for rps601 & rps602 simultaneously)
PMID:22976295	MOD:00046	O-phospho-L-serine [present_during] cellular response to cycloheximide	(comment: blotted for rps601 & rps602 simultaneously)
PMID:22976295	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAPB1E7.12	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPAPB1E7.12	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC13G6.07c [assayed_using] PomBase:SPAPB1E7.12	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPAC13G6.07c	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC13G6.07c	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAPB1E7.12	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC13G6.07c	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC13G6.07c [assayed_using] PomBase:SPAPB1E7.12	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC13G6.07c [assayed_using] PomBase:SPAPB1E7.12	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC13G6.07c	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAPB1E7.12	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC13G6.07c	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAPB1E7.12	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAPB1E7.12	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC13G6.07c	(comment: both rps proteins in extension because blot is for both of them)
PMID:22976295	GO:0004711	ribosomal protein S6 kinase activity [has_input] PomBase:SPAC13G6.07c [part_of] positive regulation of cytoplasmic translation	(comment: in vitro assay using rps602 so I am inferring rps601)
PMID:22976295	GO:0004711	ribosomal protein S6 kinase activity [has_input] PomBase:SPAPB1E7.12 [part_of] positive regulation of cytoplasmic translation	(comment: in vitro assay using rps602 so I am inferring rps601)
PMID:22976295	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_enzyme] PomBase:SPCC4G3.08 [assayed_substrate] PomBase:SPAPB1E7.12	In this experiment, we utilized a Psk1 mutant (Thr415Glu), a phospho-mimetic mutant of its hydrophobic motif, as the mutant exhibited higher activity than the wild-type protein. As shown in Fig. 2C, the Psk1 protein phosphorylated Rsp6 in vitro. However, the Rsp6 mutant that has two potential serine phosphorylation sites changed to alanine was not phosphorylated by Psk1.
PMID:22976295	FYPO:0002700	increased protein kinase activity [assayed_enzyme] PomBase:SPCC4G3.08	data not shown
PMID:22987637	FYPO:0005759	increased protein localization to chromatin at late replication origin [assayed_using] PomBase:SPAC24H6.06	"(comment: for evidence, ""BrdU incorporation assay evidence used in manual assertion"" (ECO:0001155) would be applicable.)"
PMID:22987637	FYPO:0005758	abnormal regulation of mitotic DNA replication initiation from late origin	"(comment: for evidence, ""BrdU incorporation assay evidence used in manual assertion"" (ECO:0001155) would be applicable.)"
PMID:22990236	FYPO:0004988	abnormal RNA level oscillation during mitotic cell cycle [assayed_using] dh_repeat	(comment: CHECK SO:0001899 = dh repeat)
PMID:23032292	FYPO:0000854	abnormal nucleosome positioning in euchromatin	(comment: CHECK spacing is wrong as well as occupancy)
PMID:23035257	GO:0044183	protein folding chaperone [has_input] PomBase:SPAC1002.08c	(comment: this isn't reall demonstrated here but it can ne imputed form this experiment and prior knowledge)
PMID:23051734	GO:0070649	formin-nucleated actin cable assembly	(comment: required for wild-type rates of actin cable retrograde flow in myo52∆ cells)
PMID:23066505	GO:0036498	IRE1-mediated unfolded protein response	(comment: CHECK RIDD? - there is no RIDD term in GO, Val wants to wait with this)
PMID:23066505	GO:0004521	RNA endonuclease activity [has_input] PomBase:SPAC22A12.15c [part_of] IRE1-mediated unfolded protein response	(comment: ire1 breaks down mRNAs during ER stress, however bip1 is unusual in that ire1 cleavage stabilizes it)
PMID:23071723	FYPO:0000972	increased number of Rad52 foci during vegetative growth	(comment: CHECK throughout cell cycle, with peak at M/G1)
PMID:23084836	GO:0000792	heterochromatin [coincident_with] transposable_element	(Fig. 1A)
PMID:23084836	GO:0005721	pericentric heterochromatin	(Fig. 1A)
PMID:23084836	GO:0099115	chromosome, subtelomeric region	(Fig. 1A)
PMID:23084836	FYPO:0002902	decreased protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPCC126.02c	(Figure 6E) H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively
PMID:23084836	FYPO:0003003	increased protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPBC543.03c	(Figure 6E). H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively
PMID:23084836	FYPO:0003003	increased protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPCC126.02c	(Figure 6E). H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively
PMID:23084836	FYPO:0002902	decreased protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPBC543.03c	(Figure 6E). H3K56 acetylation antagonizes Tf clustering at centromeres. binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectivelyWe examined how H3K56 acetylation antagonizes Tf clustering at centromeres. Remarkably, binding of Ku was reduced and enhanced in hst4Δ and rtt109Δ cells, respectively, suggesting that H3K56 acetylation has an inhibitory effect on Ku binding to Tf elements (Figure 6E).
PMID:23084836	FYPO:0002335	normal chromatin silencing	(Figure S1C)
PMID:23084836	FYPO:0002335	normal chromatin silencing	(Figure S1C)
PMID:23084836	FYPO:0007270	decreased Tf body tethering to centromere	(Figures 6A, 6B) (comment: CHECK: see above)
PMID:23084836	FYPO:0005545	decreased Tf body formation	(Figures 6A, 6B) (comment: see above)
PMID:23084836	FYPO:0005545	decreased Tf body formation	(Figures 6A, 6B) (comment: see above)
PMID:23084836	FYPO:0007270	decreased Tf body tethering to centromere	(Figures 6A, 6B) (comment: see above)
PMID:23084836	FYPO:0007270	decreased Tf body tethering to centromere	(Figures 6A, 6B) hst4Δ and clr6-1 HDAC mutations, but not other HDAC mutations, significantly compromised Tf clustering and the association of Tf cluster with centromeres; Figures 6A and 6B)
PMID:23084836	FYPO:0007269	normal interphase mitotic telomere clustering during vegetative growth	(Figures S2A, S2B)
PMID:23084836	FYPO:0007261	decreased telomere tethering at nuclear periphery during vegetative growth [has_severity] high	(Figures S2A, S2B). AND As previously shown, telomere tethering was significantly compromised in rap1Δ and bqt4Δ cells (Figure S2C; Chikashige et al., 2009).
PMID:23084836	FYPO:0007270	decreased Tf body tethering to centromere	(comment: NOTE IS STILL LOCALIZED TO NUCLEAR ERIPHERY) Remarkably, the association of Tf elements with centromeres was significantly compromised in pkuΔ cells (P < 0.00001, Mann-Whitney U test; Figures 3D and 3E).
PMID:23084836	FYPO:0007270	decreased Tf body tethering to centromere	(comment: NOTE IS STILL LOCALIZED TO NUCLEAR ERIPHERY) Remarkably, the association of Tf elements with centromeres was significantly compromised in pkuΔ cells (P < 0.00001, Mann-Whitney U test; Figures 3D and 3E).
PMID:23084836	FYPO:0004890	increased telomere-nuclear envelope distance during mitosis	As previously shown, telomere tethering was significantly compromised in rap1Δ and bqt4Δ cells (Figure S2C; Chikashige et al., 2009).
PMID:23084836	FYPO:0004890	increased telomere-nuclear envelope distance during mitosis	As previously shown, telomere tethering was significantly compromised in rap1Δ and bqt4Δ cells (Figure S2C; Chikashige et al., 2009).
PMID:23084836	FYPO:0005545	decreased Tf body formation	Interestingly, Tf clustering was impaired by pku70Δ and pku80Δ at a level similar to that observed in abp1Δ cells (Figure 2A).
PMID:23084836	FYPO:0005545	decreased Tf body formation	Interestingly, Tf clustering was impaired by pku70Δ and pku80Δ at a level similar to that observed in abp1Δ cells (Figure 2A).
PMID:23084836	FYPO:0005545	decreased Tf body formation	Interestingly, Tf clustering was impaired by pku70Δ and pku80Δ at a level similar to that observed in abp1Δ cells (Figure 2A).
PMID:23084836	FYPO:0007271	increased Tf body tethering to centromere	Moreover, only the rtt109Δ HAT mutations, but not other HAT mutations, significantly promoted the association of Tf cluster with centromeres, whereas none of the HAT mutations affected Tf clustering (Figures 6C and 6D).
PMID:23084836	FYPO:0007269	normal interphase mitotic telomere clustering during vegetative growth	The FISH data revealed that telomere clustering was not affected by pku70Δ and pku80Δ, but telomere tethering to the nuclear periphery was significantly compromised by pkuΔ (P < 0.001, Mann-Whitney U test), suggesting that telomere clustering and tethering to the nuclear periphery are distinct processes (Figures S2A and S2B)
PMID:23084836	FYPO:0007270	decreased Tf body tethering to centromere	We found that Tf clustering and the association of Tf cluster with centromeres were significantly compromised in the cut14-208 condensin mutant Figures 4A and 4B)
PMID:23084836	FYPO:0005545	decreased Tf body formation	We found that Tf clustering and the association of Tf cluster with centromeres were significantly compromised in the cut14-208 condensin mutant Figures 4A and 4B)
PMID:23084836	FYPO:0007272	decreased protein localization to nucleoplasm during cellular response to DNA damage [assayed_using] PomBase:SPCC126.02c	We observed that Ku localization was diffuse after DNA damage, but this diffusion was inhibited by rtt109Δ (Figure 7D)
PMID:23084836	FYPO:0001870	normal centromere clustering at nuclear periphery during vegetative growth	clustering and tethering of centromeres to the nuclear periphery were not affected in pku70Δ and pku80Δ cells, although Ku does localize at centromeres (Figures 1E, 3A, and 3B)
PMID:23084836	FYPO:0001870	normal centromere clustering at nuclear periphery during vegetative growth	clustering and tethering of centromeres to the nuclear periphery were not affected in pku70Δ and pku80Δ cells, although Ku does localize at centromeres (Figures 1E, 3A, and 3B)
PMID:23087209	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC24B11.11c	Sid2 kinase phosphorylates Klp2 on serine residues 113 and 123 based on both in vitro and in vivo evidence. Phosphorylation on these residues disrupts interaction of Klp2 with Mal3.
PMID:23087209	MOD:00046	O-phospho-L-serine	Sid2 kinase phosphorylates Klp2 on serine residues 113 and 123 based on both in vitro and in vivo evidence. Phosphorylation on these residues disrupts interaction of Klp2 with Mal3.
PMID:23087209	MOD:00046	O-phospho-L-serine	Sid2 kinase phosphorylates Klp2 on serine residues 113 and 123 based on both in vitro and in vivo evidence. Phosphorylation on these residues disrupts interaction of Klp2 with Mal3.
PMID:23093942	FYPO:0003587	loss of gross chromosomal rearrangement during replication fork processing	(comment: assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7)
PMID:23093942	FYPO:0001740	increased gross chromosomal rearrangement	(comment: assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7)
PMID:23093942	FYPO:0003587	loss of gross chromosomal rearrangement during replication fork processing	(comment: assayed by PCR in strain with RTS1 replication fork barrier inserted near ori3006/7)
PMID:23093942	FYPO:0003588	increased gross chromosomal rearrangement during replication fork processing	(comment: assayed in strain with RTS1 replication fork barrier inserted near ori3006/7)
PMID:23093942	FYPO:0001740	increased gross chromosomal rearrangement	(comment: assayed in strain with RTS1 replication fork barrier inserted near ori3006/7)
PMID:23093943	FYPO:0003535	decreased bipolar index	(Fig. 1b)
PMID:23093943	FYPO:0001018	abolished NETO [has_penetrance] ~66	(Fig. 1b, 2)
PMID:23093943	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC83.18c	(Fig. 3C)
PMID:23093943	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC83.18c	(Fig. 3C)
PMID:23093943	FYPO:0001018	abolished NETO [has_penetrance] 25-30	(Fig. 4c)
PMID:23093943	FYPO:0001018	abolished NETO [has_penetrance] 50	(Fig. 4c)
PMID:23093943	FYPO:0001018	abolished NETO [has_penetrance] ~45-50	(Fig. 4c)
PMID:23093943	FYPO:0001018	abolished NETO [has_penetrance] 50	(Fig. 4c,6a)
PMID:23093943	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC83.18c	(Fig. S3F)
PMID:23093943	FYPO:0007709	decreased protein localization to cell cortex of non-growing cell tip [assayed_using] PomBase:SPCC645.07	(Figure 1F-1G)
PMID:23093943	FYPO:0005465	normal cell polarity [assayed_using] PomBase:SPBC83.18c	(Figure 3D-3F)
PMID:23093943	FYPO:0007031	abolished protein localization to cell cortex of cell tip during mitotic interphase [assayed_using] PomBase:SPBC83.18c	(Figure 3G)
PMID:23093943	FYPO:0000026	abnormal vegetative cell polarity	(Figure 4A-4C, S3A-S3B)
PMID:23093943	FYPO:0000026	abnormal vegetative cell polarity	(Figure 4A-4C, S3A-S3B)
PMID:23093943	FYPO:0007451	normal protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPBC1706.01	(Figure S1B-S1C)
PMID:23093943	FYPO:0007709	decreased protein localization to cell cortex of non-growing cell tip [assayed_using] PomBase:SPAC23C4.02	(Figure S1B-S1C)
PMID:23093943	FYPO:0007451	normal protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPCC1223.06	(Figure S1B-S1C)
PMID:23093943	FYPO:0001355	decreased vegetative cell population growth	(Figure S1F)
PMID:23093943	FYPO:0002061	inviable vegetative cell population	(Figure S1F)
PMID:23093943	FYPO:0001355	decreased vegetative cell population growth	(Figure S1F)
PMID:23093943	FYPO:0001018	abolished NETO [has_penetrance] 30	(Figure S5B)
PMID:23093943	FYPO:0001018	abolished NETO [has_penetrance] 30	(Figure S5B)
PMID:23093943	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	As was observed previously [28], cytoplasmic Fic1-GFP localizes to cell tips during interphase and later to the CR during cell division (Figure 3A).
PMID:23093943	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic M phase	As was observed previously [28], cytoplasmic Fic1-GFP localizes to cell tips during interphase and later to the CR during cell division (Figure 3A).
PMID:23093943	FYPO:0003776	increased pseudohyphal growth	Cells lacking Fic1 or its interacting partners Cyk3 or Imp2 were significantly more invasive than wild-type cells (Figure 9A-9B).
PMID:23093943	FYPO:0003776	increased pseudohyphal growth	Cells lacking Fic1 or its interacting partners Cyk3 or Imp2 were significantly more invasive than wild-type cells (Figure 9A-9B).
PMID:23093943	FYPO:0003776	increased pseudohyphal growth	Cells lacking Fic1 or its interacting partners Cyk3 or Imp2 were significantly more invasive than wild-type cells (Figure 9A-9B).
PMID:23093943	GO:1902404	mitotic actomyosin contractile ring contraction	Consistent with early cytokinesis events proceeding appropriately without Fic1, time-lapse imaging of myosin regulatory light chain Rlc1-GFP [47,48] along with spindle pole body marker Sid4-GFP revealed that the CR formed and constricted normally in fic1D cells (Figure 5C-5D). However, at the termination of CR constriction, parts of the CR persisted at the division plane (Figure 5E-5G and Figure S4D).
PMID:23093943	GO:0140472	cell cortex of non-growing cell tip [exists_during] mitotic interphase	Cyk3-GFP localized to the CR and division site during cytokinesis, and it was retained at new ends immediately following cell division (Figure 4F).
PMID:23093943	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic M phase	Cyk3-GFP localized to the CR and division site during cytokinesis, and it was retained at new ends immediately following cell division (Figure 4F).
PMID:23093943	FYPO:0003013	abnormal actomyosin contractile ring disassembly [has_penetrance] 8	Fic1 most likely functions during late stages of cytokinesis. In line with this idea, the percentage of fic1D cells that had undergone ingression but were still joined at their division sites was more than four times that of wild-type cells (Figure 5A-5B).
PMID:23093943	FYPO:0003776	increased pseudohyphal growth	In addition to these strains, we found other cytokinesis mutants exhibiting high degrees of monopolar growth (spn1D, cdc7-24, and vps24D) to also be highly invasive and to form pseudohyphal projections into 2% agar (Figure 9A-9B and Figure S7A)
PMID:23093943	FYPO:0001018	abolished NETO [has_penetrance] 30-40	Loss of Eng1 or its cooperating glucanase, Agn1 [34], resulted in high percentages of monopolar growth (Figure 6C-6D and Figure S5A)
PMID:23093943	FYPO:0001018	abolished NETO [has_penetrance] 30-40	Loss of Eng1 or its cooperating glucanase, Agn1 [34], resulted in high percentages of monopolar growth (Figure 6C-6D and Figure S5A)
PMID:23093943	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC83.18c [assayed_using] PomBase:SPAC20G8.05c	Mutation of PxxPs 10 and 11 in combination, or P257 of PxxP 11 alone, abolished the two-hybrid interaction (Figure S3D), and the P257A mutation eliminated co-immunoprecipitation of Fic1- FLAG3 with Cdc15 in vivo (Figure 4D).
PMID:23093943	FYPO:0000013	T-shaped vegetative cell [has_penetrance] 10	T-shapes always arose in cells that the tea1D growth pattern dictated should grow at their new ends (Figure 2D-2E) but that actually grew at neither (Figure 2E and 2G)
PMID:23112169	GO:0032132	O6-alkylguanine-DNA binding	(comment: binds O6-alkylguanine, 2-aminopurine and 2,6-diaminopurine)
PMID:23122962	GO:0000307	cyclin-dependent protein kinase holoenzyme complex	A tandem affinity purification (TAP) identified physical partners of Cdk11, including an uncharacterized cyclin (SPAC1296.05c) that was confirmed to bind Cdk11 in independent coimmunoprecipitation experiments (Figure 1C and 1D).
PMID:23122962	GO:0000307	cyclin-dependent protein kinase holoenzyme complex	A tandem affinity purification (TAP) identified physical partners of Cdk11, including an uncharacterized cyclin (SPAC1296.05c) that was confirmed to bind Cdk11 in independent coimmunoprecipitation experiments (Figure 1C and 1D).
PMID:23122962	GO:2001178	positive regulation of mediator complex assembly	At the contrary, the interaction between the kinase module subunit Cdk8 and the head subunit Med27 was completely abrogated when Cdk11 was inactivated (Figure 4B, middle panel). This role of Cdk11 in Mediator integrity was likely mediated by phosphorylation of Med27 and Med4 on the sites identified above (Figures 3 and 4A), because the interaction between Cdk8 and either the Med27 or Med4 phosphorylation mutants was specifically lost (Figure 4B, right panel). In contrast, the phosphorylation mutants of Med27 and Med4 still interacted with the middle subunit Med7 (Figure 4B, right panel). These data indicate that the association of the kinase submodule and the S-Mediator requires the phosphorylation of Med27 and Med4 by Cdk11.
PMID:23122962	GO:2001178	positive regulation of mediator complex assembly	At the contrary, the interaction between the kinase module subunit Cdk8 and the head subunit Med27 was completely abrogated when Cdk11 was inactivated (Figure 4B, middle panel). This role of Cdk11 in Mediator integrity was likely mediated by phosphorylation of Med27 and Med4 on the sites identified above (Figures 3 and 4A), because the interaction between Cdk8 and either the Med27 or Med4 phosphorylation mutants was specifically lost (Figure 4B, right panel). In contrast, the phosphorylation mutants of Med27 and Med4 still interacted with the middle subunit Med7 (Figure 4B, right panel). These data indicate that the association of the kinase submodule and the S-Mediator requires the phosphorylation of Med27 and Med4 by Cdk11.
PMID:23122962	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC18H10.15	Combining the large-scale phosphoproteome data set and sequence alignment (Figures S4B and S4C), we determined that putative phosphoacceptors and in vitro analysis demonstrated that Cdk11 phosphorylates Med4 on three residues (Figure 3B: S115, S204, and S218
PMID:23122962	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC18H10.15	Combining the large-scale phosphoproteome data set and sequence alignment (Figures S4B and S4C), we determined that putative phosphoacceptors and in vitro analysis demonstrated that Cdk11 phosphorylates Med4 on three residues (Figure 3B: S115, S204, and S218
PMID:23122962	GO:0005634	nucleus	Fluorescence microscopy revealed that Cdk11 was expressed and mainly concentrated in the nucleus (Figure 1A).
PMID:23122962	FYPO:0004067	decreased phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	In addition, while the inactivation of the well-described CTD serine 5 or serine 2 kinases (Mcs6 [Cdk7] and Lsk1 [Cdk12], respectively) specifically decreased the phosphorylation level of these two residues in vivo, the absence of cdk11 had no effect (Figure 1F).
PMID:23122962	FYPO:0004068	decreased phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	In addition, while the inactivation of the welldescribed CTD serine 5 or serine 2 kinases (Mcs6 [Cdk7] and Lsk1 [Cdk12], respectively) specifically decreased the phosphorylation level of these two residues in vivo, the absence of cdk11 had no effect (Figure 1F).
PMID:23122962	GO:0000785	chromatin	The previously reported connection between Cdk11 and transcription, together with its nuclear localization and copurification with transcription regulators (although at weak level) led us to test its chromatin association. Gene-specific chromatin immunoprecipitation (ChIP) experiments showed that Cdk11- hemagglutinin (HA) was enriched onto chromatin compared to an untagged control (data not shown), and a genome-wide ChIP-on-chip analysis showed a broad distribution of Cdk11- HA.
PMID:23122962	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPAC17C9.05c	Therefore, we found no evidence of Cdk11 being a genuine CTD kinase in fission yeast.
PMID:23122962	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPBC1105.06	Therefore, we found no evidence of Cdk11 being a genuine CTD kinase in fission yeast.
PMID:23122962	GO:0060261	positive regulation of transcription initiation by RNA polymerase II	This possibility was confirmed by global expression profiling, showing that only 55 genes were significantly affected in the absence of Cdk11. (.....and srb mediator association) showed that the absence of either cdk11 or cdk8 resulted in very similar defects (up- or downregulation) that were more pronounced in the cdk8 mutant (Figure 2C). Quantitative RT-PCR confirmed this effect on representative genes and showed, in addition, that the expression defects were not cumulated in the double cdk8 cdk11 mutant (Figure 2D).
PMID:23122962	GO:0008353	RNA polymerase II CTD heptapeptide repeat kinase activity [has_input] PomBase:SPBC28F2.12	in contrast to Mcs6 (the Cdk7 ortholog), which readily phosphorylated the GST-CTD fusion in vitro (Figure 1E) (Drogat and Hermand, 2012)
PMID:23122962	GO:0140834	RNA polymerase II CTD heptapeptide repeat S2 kinase activity [has_input] PomBase:SPBC28F2.12	in contrast to Mcs6 (the Cdk7 ortholog), which readily phosphorylated the GST-CTD fusion in vitro (Figure 1E) (Drogat and Hermand, 2012)
PMID:23128140	GO:0051010	microtubule plus-end binding	(comment: NMR + substrate)
PMID:23133674	GO:0140378	protein complex scaffold activity [has_input] PomBase:SPAC19G12.13c	(Fig. 1) (comment: Y2H)
PMID:23133674	GO:0140378	protein complex scaffold activity [has_input] PomBase:SPAC16A10.07c	(comment: Y2H) fig 1
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPAC4A8.05c	(Fig. 1)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPCC1442.04c	(Fig. 1)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPCC1442.04c	(Fig. 1)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPAC4A8.05c	(Fig. 1)
PMID:23151475	FYPO:0008426	increased heterochromatin assembly by siRNA [assayed_region] PomBase:SPAC4A8.05c [has_severity] high	(Fig. 1, 4B)
PMID:23151475	FYPO:0008426	increased heterochromatin assembly by siRNA [assayed_region] PomBase:SPCC1442.04c [has_severity] high	(Fig. 1, 4C)
PMID:23151475	FYPO:0006369	increased histone H3-K9 dimethylation at heterochromatin domain during vegetative growth	(Fig. 1D, 2B, 3B, 4)
PMID:23151475	FYPO:0008426	increased heterochromatin assembly by siRNA [assayed_region] PomBase:SPAPB15E9.03c [has_severity] high	(Fig. 2, 4A)
PMID:23151475	FYPO:0004207	increased siRNA level [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] medium	(Fig. 2A)
PMID:23151475	FYPO:0004207	increased siRNA level [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] medium	(Fig. 2A)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPAPB15E9.03c	(Fig. 2A, 2B)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPAPB15E9.03c	(Fig. 2A, 2B)
PMID:23151475	FYPO:0004207	increased siRNA level [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] high	(Fig. 2A, 2E)
PMID:23151475	FYPO:0004207	increased siRNA level [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] low	(Fig. 2E)
PMID:23151475	FYPO:0004207	increased siRNA level [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] low	(Fig. 2E)
PMID:23151475	FYPO:0004207	increased siRNA level [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] low	(Fig. 2E)
PMID:23151475	FYPO:0004207	increased siRNA level [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] low	(Fig. 2E)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPCC1442.04c	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1442.04c [has_severity] high	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1442.04c [has_severity] high	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1442.04c [has_severity] high	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] medium	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] medium	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] medium	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1442.04c [has_severity] high	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPCC1442.04c	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPCC1442.04c	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAPB15E9.03c	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPCC1442.04c	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC4A8.05c [has_severity] high	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC4A8.05c [has_severity] high	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC4A8.05c [has_severity] high	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC4A8.05c [has_severity] high	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC4A8.05c [has_severity] medium	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC4A8.05c [has_severity] medium	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC4A8.05c [has_severity] low	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC4A8.05c [has_severity] low	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] high	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] high	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] medium	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] medium	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] medium	(Fig. 3A)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1442.04c [has_severity] low	(Fig. 3A, 4D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.08 [has_severity] medium	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.08 [has_severity] medium	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.08 [has_severity] low	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.03 [has_severity] medium	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC14C4.07	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC14C4.07	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC14C4.07	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.07 [has_severity] medium	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.07 [has_severity] medium	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC14C4.03	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.03 [has_severity] medium	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.03 [has_severity] medium	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.03 [has_severity] medium	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.08 [has_severity] medium	(Fig. 3D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.08 [has_severity] medium	(Fig. 3D)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPAPB15E9.03c	(Fig. 4A)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPAPB15E9.03c	(Fig. 4A)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPAPB15E9.03c	(Fig. 4A)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPAPB15E9.03c	(Fig. 4A)
PMID:23151475	FYPO:0008426	increased heterochromatin assembly by siRNA [assayed_region] PomBase:SPAPB15E9.03c [has_severity] low	(Fig. 4A)
PMID:23151475	FYPO:0008426	increased heterochromatin assembly by siRNA [assayed_region] PomBase:SPAPB15E9.03c [has_severity] low	(Fig. 4A)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPAC4A8.05c	(Fig. 4B)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPAC4A8.05c	(Fig. 4B)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPAC4A8.05c	(Fig. 4B)
PMID:23151475	FYPO:0008426	increased heterochromatin assembly by siRNA [assayed_region] PomBase:SPAC4A8.05c [has_severity] low	(Fig. 4B)
PMID:23151475	FYPO:0008426	increased heterochromatin assembly by siRNA [assayed_region] PomBase:SPAC4A8.05c [has_severity] low	(Fig. 4B)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPAC4A8.05c	(Fig. 4B)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPCC1442.04c	(Fig. 4C)
PMID:23151475	FYPO:0008426	increased heterochromatin assembly by siRNA [assayed_region] PomBase:SPCC1442.04c [has_severity] high	(Fig. 4C)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPCC1442.04c	(Fig. 4C)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPCC1442.04c	(Fig. 4C)
PMID:23151475	FYPO:0007225	normal heterochromatin assembly by small RNA [assayed_region] PomBase:SPCC1442.04c	(Fig. 4C)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1442.04c [has_severity] high	(Fig. 4D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC4A8.05c [has_severity] high	(Fig. 4D)
PMID:23151475	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC4A8.05c [has_severity] low	(Fig. 4D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1442.04c [has_severity] high	(Fig. 4D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] medium	(Fig. 4D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB15E9.03c [has_severity] high	(Fig. 4D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAPB15E9.03c	(Fig. 4D)
PMID:23151475	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC4A8.05c [has_severity] high	(Fig. 4D)
PMID:23188080	FYPO:0004287	decreased double-strand break repair via nonhomologous end joining	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23188080	FYPO:0004287	decreased double-strand break repair via nonhomologous end joining	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23188080	FYPO:0004287	decreased double-strand break repair via nonhomologous end joining	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23188080	FYPO:0004287	decreased double-strand break repair via nonhomologous end joining	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23188080	FYPO:0004287	decreased double-strand break repair via nonhomologous end joining	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23188080	FYPO:0004287	decreased double-strand break repair via nonhomologous end joining	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23188080	FYPO:0004287	decreased double-strand break repair via nonhomologous end joining	(comment: affects intermolecular, but not intramolecular, end joining)
PMID:23200991	GO:0090726	cortical dynamic polarity patch [exists_during] cellular response to pheromone	(comment: Observed with probe for active Cdc42 (CRIB))
PMID:23200991	GO:0043332	mating projection tip [exists_during] cell morphogenesis involved in conjugation with cellular fusion	(comment: Observed with probe for active Cdc42 (CRIB))
PMID:23200991	GO:1902917	positive regulation of mating projection assembly	(comment: inferred from localization plus GTPase activity)
PMID:2320127	MOD:00046	O-phospho-L-serine	(Fig. 1c) Serine is the major phosphoamino acid
PMID:2320127	MOD:00047	O-phospho-L-threonine	(Fig. 1c) threonine is the minor phosphoamino acid
PMID:2320127	FYPO:0000836	increased protein level [assayed_using] PomBase:SPAC24H6.05	(Fig. 4a) Cells blocked in G2
PMID:2320127	FYPO:0000836	increased protein level [assayed_using] PomBase:SPAC24H6.05	(Fig. 4a) Cells blocked in mitosis
PMID:23209828	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process [has_input] PomBase:SPAC1783.07c	(Comment: MBC sensitivity phenotype and ubiquitylation and degradation phenotype)
PMID:23209828	GO:0061630	ubiquitin protein ligase activity [has_input] PomBase:SPAC18B11.07c [has_input] PomBase:SPAC1783.07c	(comment: MBC resistance phenotype and pap1 ubiquitylation phenotype)
PMID:23209828	GO:0061631	ubiquitin conjugating enzyme activity	(comment: MBC resistance phenotype and pap1 ubiquitylation phenotype)
PMID:23209828	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process [has_input] PomBase:SPAC1783.07c	(comment: MBC sensitivity phenotype and ubiquitylation and degradation phenotype)
PMID:23209828	MOD:01148	ubiquitinylated lysine [added_by] PomBase:SPBC19C7.02	(comment: Pap1 is ubiquitylated by Rhp6 and Ubr1)
PMID:23209828	MOD:01148	ubiquitinylated lysine [added_by] PomBase:SPAC18B11.07c	(comment: Pap1 is ubiquitylated by Rhp6 and Ubr1)
PMID:23211746	FYPO:0002553	abnormal double-strand break processing	(comment: gel electrophoresis + southern blot)
PMID:23211746	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: same as chk1delta alone)
PMID:23211746	FYPO:0000268	sensitive to UV during vegetative growth	(comment: same as chk1delta alone)
PMID:23211746	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC1259.13	(comment: same as exo1delta alone)
PMID:23211746	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: same as exo1delta alone)
PMID:23211746	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC1259.13	(comment: same as rad2delta alone)
PMID:23211746	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: same as rad2delta alone)
PMID:23223230	FYPO:0001551	increased protein level during cellular response to zinc ion starvation [assayed_transcript] PomBase:SPCC13B11.01	However, the larger band preferentially accumulated under zinc-replete conditions in wild-type cells and constitutively accumulated in SPCC13B11.02c cells. Thus, changes in adh1AS levels influence the levels of Adh1 protein, suggesting that this mechanism may exist to conserve zinc.
PMID:23223230	PomGeneEx:0000012	RNA level decreased [in_presence_of] zinc ion	In the array analysis, one of the most repressed genes in response to zinc deficiency was adh1, whereas one of the most highly expressed transcripts under this condition was an antisense transcript at this locus (Fig. 1A).
PMID:23223230	PomGeneEx:0000011	RNA level increased [during] cellular response to zinc ion starvation	In the array analysis, one of the most repressed genes in response to zinc deficiency was adh1, whereas one of the most highly expressed transcripts under this condition was an antisense transcript at this locus (Fig. 1A).
PMID:23223230	PomGeneEx:0000012	RNA level decreased [during] cellular response to zinc ion starvation	In the array analysis, one of the most repressed genes in response to zinc deficiency was adh1, whereas one of the most highly expressed transcripts under this condition was an antisense transcript at this locus (Fig. 1A).
PMID:23223230	PomGeneEx:0000011	RNA level increased [in_presence_of] zinc ion	Taken together, the Northern and array analyses indicate that adh1AS transcripts preferentially accumulate in zinc-limited cells, whereas adh1 mRNAs accumulate in zinc-replete cells.
PMID:23223230	FYPO:0001547	increased RNA level during cellular response to zinc ion starvation [assayed_transcript] PomBase:SPCC13B11.01	When adh1AS and adh1 transcript levels were examined in SPCC13B11.02c cells, the adh1AS transcript was not detected, and adh1 mRNAs were detected in both zinc-limited and zinc-replete cells (Fig. 1C).
PMID:23223230	FYPO:0001889	RNA absent from cell [assayed_transcript] PomBase:SPNCRNA.1710	When adh1AS and adh1 transcript levels were examined in SPCC13B11.02c cells, the adh1AS transcript was not detected, and adh1 mRNAs were detected in both zinc-limited and zinc-replete cells (Fig. 1C).
PMID:23231582	FYPO:0007506	increased protein localization to chromatin at promoter [assayed_using] PomBase:SPBC27B12.11c	(comment: CHECK at pho1+ and SPBC1271.09)
PMID:23231582	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [happens_during] cellular response to phosphate starvation	(comment: also inferred from chromatin localization and reporter gene expression)
PMID:23231582	GO:0000122	negative regulation of transcription by RNA polymerase II	(comment: represses Pho7-mediated transcription activation in phosphate-replete conditions; does not regulate Pho7 DNA binding)
PMID:23236291	GO:1900735	positive regulation of flocculation	(Figure 1A and 1B)
PMID:23236291	FYPO:0003335	increased galactose-specific flocculation	(Figure 1A)
PMID:23236291	FYPO:0003318	abolished galactose-specific flocculation during vegetative growth	(Figure 1B)
PMID:23236291	FYPO:0000155	increased flocculation	(Figure 3)
PMID:23236291	FYPO:0000155	increased flocculation	(Figure 3)
PMID:23236291	FYPO:0000155	increased flocculation	(Figure 3)
PMID:23236291	FYPO:0000155	increased flocculation	(Figure 3)
PMID:23236291	FYPO:0000155	increased flocculation	(Figure 3)
PMID:23236291	FYPO:0000155	increased flocculation	(Figure 3)
PMID:23236291	FYPO:0000155	increased flocculation	(Figure 3)
PMID:23236291	FYPO:0000155	increased flocculation	(Figure 3)
PMID:23236291	GO:1900735	positive regulation of flocculation	(Figure 6A and 6C)
PMID:23236291	FYPO:0005504	abolished galactose-specific flocculation	(Figure 6A)
PMID:23236291	FYPO:0004153	increased flocculation in stationary phase	(Figure 7A)
PMID:23236291	FYPO:0004153	increased flocculation in stationary phase	(Figure 7A)
PMID:23236291	FYPO:0003335	increased galactose-specific flocculation	(Figure 8A)
PMID:23236291	FYPO:0003318	abolished galactose-specific flocculation during vegetative growth	(Figure 8B)
PMID:23236291	FYPO:0003318	abolished galactose-specific flocculation during vegetative growth	(Figure 8B)
PMID:23236291	FYPO:0003335	increased galactose-specific flocculation	(Figure 8B)
PMID:23236291	FYPO:0000155	increased flocculation	(Figure 8D)
PMID:23236291	FYPO:0000155	increased flocculation	(Figure 8D)
PMID:23236291	FYPO:0003776	increased pseudohyphal growth	(Figure 8D)
PMID:23236291	FYPO:0003335	increased galactose-specific flocculation	(Figure 8D)
PMID:23236291	FYPO:0000155	increased flocculation	(Figure 8D)
PMID:23236291	FYPO:0000155	increased flocculation	(Figure 8D)
PMID:23236291	FYPO:0000155	increased flocculation	(Figure 8D)
PMID:23236291	FYPO:0005277	multinucleate multiseptate cell	(Figure 8E)
PMID:23236291	FYPO:0001252	multinucleate multiseptate vegetative cell	(Figure 8E)
PMID:23236291	GO:0000785	chromatin [coincident_with] CArG_box	(comment: CHECK Requested new term from Sequence Ontology: CArG-box)
PMID:23245849	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1D)
PMID:23245849	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1D)
PMID:23245849	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1D)
PMID:23245849	GO:0005634	nucleus	(Figure 1C)
PMID:23245849	GO:0140431	DNA-(abasic site) binding	Mag2 binds stronger to the abasic oligonucleotide than to non-damaged DNA (Figure 2), with a dissociation rate constant more than 15 times higher for non-damaged DNA (kd 26 × 10−3 s −1) as compared to DNA containing the AP site analogue tetrahydrofuran (THF) (kd 1.6 × 10−3 s−1). Mag2 injected on sensor chips coated with oligonucleotides containing a single ethenoadenine or 8-oxoguanine lesion showed the same resonance levels as non-damaged DNA (data not shown), demonstrating that Mag2 preferentially binds to AP sites in DNA.
PMID:23245849	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	Supp S1 Also the MMS sensitivity of the nth1 − mutant was suppressed by the deletion of mag1 but not mag2 (Figure S1), which contrasts previous results (Kanamitsu et al., 2007). We do not know the reason for this discrepancy, but it could be because of different strain backgrounds, as the strains used by Kanamisu and co-workers tolerate much higher MMS doses (0.03% versus 0.007% in our experiments)
PMID:23254763	FYPO:0003727	galactose absent from cell wall glycoprotein glycan	(Fig. 3) galactose-specific HRP-PNA staining was used to detect quantitative differences in the galactosylation of cell-surface proteins
PMID:23254763	FYPO:0006807	decreased galactose level in cell surface glycoprotein glycan	(Fig. 3) galactose-specific HRP-PNA staining was used to detect quantitative differences in the galactosylation of cell-surface proteins
PMID:23254763	FYPO:0001317	normal RNA level during vegetative growth	(Fig. 5a) There was no difference in ght2+ expression levels between wild-type and uge1Δgal10Δ cells that have a reduced level of cytosolic UDP-galactose (Suzuki et al. 2010), indicating that expression of ght2+ is not influenced by intracellular UDP-galactose concentration
PMID:23254763	FYPO:0001317	normal RNA level during vegetative growth	(Fig. 5a) There was no difference in ght2+ expression levels between wild-type and uge1Δgal10Δ cells that have a reduced level of cytosolic UDP-galactose (Suzuki et al. 2010), indicating that expression of ght2+ is not influenced by intracellular UDP-galactose concentration
PMID:23254763	FYPO:0001317	normal RNA level during vegetative growth	(Fig. 5a) There was no difference in ght2+ expression levels between wild-type and uge1Δgal10Δ cells that have a reduced level of cytosolic UDP-galactose (Suzuki et al. 2010), indicating that expression of ght2+ is not influenced by intracellular UDP-galactose concentration
PMID:23254763	FYPO:0000106	sensitive to hygromycin B [has_severity] high	(Figure 2)
PMID:23254763	FYPO:0000106	sensitive to hygromycin B [has_severity] high	(Figure 2)
PMID:23254763	FYPO:0000106	sensitive to hygromycin B [has_severity] high	(Figure 2)
PMID:23254763	FYPO:0000106	sensitive to hygromycin B [has_severity] high	(Figure 2)
PMID:23254763	FYPO:0000106	sensitive to hygromycin B [has_severity] high	(Figure 2)
PMID:23254763	FYPO:0000106	sensitive to hygromycin B [has_severity] high	(Figure 2)
PMID:23254763	FYPO:0000106	sensitive to hygromycin B [has_severity] high	(Figure 2)
PMID:23254763	FYPO:0000106	sensitive to hygromycin B [has_severity] high	(Figure 2)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	FYPO:0000106	sensitive to hygromycin B [has_severity] high	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	FYPO:0002061	inviable vegetative cell population	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	FYPO:0002061	inviable vegetative cell population	(Figure 2) (comment: CONDITION +25 μg/ml Hyg.B)
PMID:23254763	GO:0005354	galactose transmembrane transporter activity [part_of] galactose import across plasma membrane	(comment: CHECK complemented by S. cerevisiae GAL2)
PMID:23260662	GO:0071515	mating-type locus imprinting	(Fig. 3A)
PMID:23260662	GO:0011000	replication fork arrest at mating type locus	(comment: inferred directness from effects of different alleles and of mutations elsewhere (swi1delta, clr4delta, or mat1-SS2))
PMID:23260662	GO:0071515	mating-type locus imprinting	(comment: inferred directness from effects of different alleles and of mutations elsewhere (swi1delta, clr4delta, or mat1-SS2))
PMID:23260662	GO:1902681	regulation of replication fork arrest at rDNA repeats	(comment: inferred indirectness from author description and different effect of swi1delta)
PMID:23260662	FYPO:0003081	decreased genetic imprinting at mating-type locus [has_severity] high	(comment: same as lsd1-E918 single mutant)
PMID:23260662	FYPO:0003081	decreased genetic imprinting at mating-type locus [has_severity] high	(comment: same as lsd1-E918 single mutant)
PMID:23260662	FYPO:0003081	decreased genetic imprinting at mating-type locus [has_severity] high	(comment: same as lsd1-E918 single mutant)
PMID:23260662	FYPO:0003081	decreased genetic imprinting at mating-type locus [has_severity] high	(comment: same as lsd1-E918 single mutant)
PMID:23273506	FYPO:0000695	increased DNA-1,N6-ethenoadenine N-glycosylase activity	(Figures 4B and 4C) Asp56Ser mutation endows Mag2 with the ability to excise εA at levels similar to Mag1.
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK Phosphorylation site S265 was identified by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S118, S143, and T379 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S147, S242, S270, S316, and S354 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S148 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S183 and S372 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S183 and S372 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S196 and S252 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S196 and S252 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S216 and S298 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S216 and S298 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S220 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK S244, S278, S501, S755, T831, and S852 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S267 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S301 and S499 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S301 and S499 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S303 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S321 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S332, S700, and S732 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S345 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S370 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S372 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S411 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S430, T451, S479, S491, T509, and T577 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S436 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S48, S71, S103, S113, S140, S171, S195, S206, S221, S236, T240, T255, S257, S289, S344, S379, S399, and T411 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S502 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S558 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S57 and S206 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S57 and S206 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S65 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S674 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S74 and S95 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK S74 and S95 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK T106 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK T123 and S334 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK T123 and S334 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK T123 and S334 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK T297 and S364 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK T297 and S364 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK T554 was identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00047	O-phospho-L-threonine	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	MOD:00046	O-phospho-L-serine	(comment: CHECK T61, T71, S75, S156, S171, S361, S497, and S947 were identified as phosphorylation sites by mass spectrometry.)
PMID:23297348	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC1739.11c	(comment: serine residues, presumably some or all of those mutated)
PMID:23297348	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC1739.11c	(comment: serine residues, presumably some or all of those mutated)
PMID:23297348	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC1739.11c	(comment: serine residues, presumably some or all of those mutated)
PMID:23297348	GO:0005654	nucleoplasm	Localization of Clp1 to nucleoplasm requires the presence of the nuclear localization sequence (NLS), which was identified to locate right at the end of the C-terminal.
PMID:23297348	GO:0006606	protein import into nucleus	Sal3 is required for the nuclear import of Clp1 as shown by microscopy.
PMID:23311928	FYPO:0001357	normal vegetative cell population growth	(comment: non-flocculating cells)
PMID:23314747	GO:0000785	chromatin [coincident_with] AACCCT_box	(comment: AACCCT box, subtelomere)
PMID:23314747	GO:0000785	chromatin [coincident_with] regional_centromere_central_core	(comment: AACCCT box, subtelomere)
PMID:23314747	GO:0000785	chromatin [coincident_with] subtelomere	(comment: AACCCT box, subtelomere)
PMID:23314747	FYPO:0004904	decreased protein localization to centromere central core during vegetative growth [assayed_using] PomBase:SPBC1105.17	Cnp1 localisation to centromere reduced in teb1-1 cells grown at 36C (based on immunofluorescence)
PMID:23314747	FYPO:0002687	normal telomere length during vegetative growth	Southern Blot of teb1-1 cells grown at permissive and restrictive temperatures shows no change in telomere length, compared to wild type cells
PMID:23333317	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 1) Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 1) Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 1) Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 1) Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 1) Rescue of cdc25-22 but not restored to full growth (partial rescue)
PMID:23333317	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 1) Rescue of cdc25-22 but not restored to full growth (partial rescue). [ie The cut12.s11 (G71V) mutation enables cdc25+ null cells (cdc25.D) to form microcolonies of 1 to 20 cells [14]. ]
PMID:23333317	FYPO:0000674	normal cell population growth at high temperature	"(Fig. 1A, 2A) vw""Fig 1. Rescue of cdc25-22 but not restored to full growth (partial rescue)"""
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05	(Fig. 1C) (comment: 2 hybrid)
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] high	(Fig. 1C) (comment: 2 hybrid)
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] high	(Fig. 1C) (comment: 2 hybrid)
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] high	(Fig. 1C) (comment: 2 hybrid)
PMID:23333317	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] high	(Fig. 1C) increased interaction in 2 hybrid
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 1D)
PMID:23333317	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] high	(Fig. 1D)
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 1D)
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05	(Fig. 1D, E)
PMID:23333317	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] high	(Fig. 1E)
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] high	(Fig. 1E)
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] high	(Fig. 1E)
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] high	(Fig. 1E)
PMID:23333317	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05	(Fig. 1E)
PMID:23333317	FYPO:0000674	normal cell population growth at high temperature [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 1H) cdc25-22 cut12R531STOP can grow at higher temperature in presence of cut12. G71V mutation. (comment: vw changed form increased to normal, compared to WT)
PMID:23333317	FYPO:0000674	normal cell population growth at high temperature [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 1H) cdc25-22 cut12R531STOP can grow at higher temperature in presence of cut12. G71V mutation. (comment: vw changed form increased to normal, compared to WT)
PMID:23333317	GO:0035591	signaling adaptor activity [has_input] PomBase:SPAC23C11.16 [part_of] G2/M transition of mitotic cell cycle [occurs_in] mitotic spindle pole body [happens_during] mitotic G2 phase	(Fig. 1b, F and G) (comment: CHECK T75T78 PHOSPHORYLATED FORM)
PMID:23333317	GO:0035591	signaling adaptor activity [has_input] PomBase:SPBC776.02c [occurs_in] mitotic spindle pole body [happens_during] mitotic G2 phase [part_of] negative regulation of G2/M transition of mitotic cell cycle	(Fig. 1b, F and G) (comment: CHECK T75T78 UNPHOSPHORYLATED FORM)
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 1c) (comment: 2-hybrid)
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 1c) (comment: 2-hybrid)
PMID:23333317	FYPO:0000674	normal cell population growth at high temperature	(Fig. 2E)
PMID:23333317	FYPO:0000674	normal cell population growth at high temperature	(Fig. 2E) phospho mimetic cdc12 mutant rescues cdc25 mutant
PMID:23333317	FYPO:0000674	normal cell population growth at high temperature	(Fig. 2E) phospho mimetic cdc12 mutant rescues cdc25 mutant
PMID:23333317	FYPO:0000674	normal cell population growth at high temperature	(Fig. 2E) phospho mimetic cdc12 mutant rescues cdc25 mutant
PMID:23333317	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 2E) single mutant T75D does not rescue cdc25-22 as well as double T75DT78D or singleT78D mutants. (comment: vw: changed to decreased)
PMID:23333317	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 2E) single mutant T78D does not rescue cdc25-22 as well as double T75DT78D. (vw changed from increased to decreased as we are comparing to WT , bottom row)
PMID:23333317	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 2E) unphosphorylatable cut12 mutants are unable to rescue cdc25 mutant (comment: vw changed from decreased to abolished?)
PMID:23333317	FYPO:0000674	normal cell population growth at high temperature	(Fig. 2G)
PMID:23333317	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] variable severity	(Fig. 2H)
PMID:23333317	FYPO:0007474	variable cell size at division [has_severity] variable severity	(Fig. 2H)
PMID:23333317	FYPO:0001492	viable elongated vegetative cell [has_severity] variable severity	(Fig. 2H) (comment: VWI added this and man=de the original 'abnormal cell size' small (variable size at division, mixed sized see #3800)
PMID:23333317	FYPO:0007385	increased duration of protein-protein interaction [assayed_using] PomBase:SPBC649.05 [assayed_using] PomBase:SPBC776.02c	(Fig. 2I) Fig3C double mutant cut12.T75A T78A binds dis2
PMID:23333317	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC649.05 [assayed_using] PomBase:SPBC776.02c	(Fig. 2I) single mutant cut12. T75A binds dis2
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC649.05 [assayed_using] PomBase:SPBC776.02c	(Fig. 2I) single mutant cut12. T75D reduces dis2 binding
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC649.05 [assayed_using] PomBase:SPBC776.02c	(Fig. 2I) single mutant cut12. T78D reduces dis2 binding
PMID:23333317	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC649.05 [assayed_using] PomBase:SPBC776.02c	(Fig. 2I) single mutant cut12.T78A binds Dis2
PMID:23333317	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 4A) (comment: an antibody that recognized Cut12 when phosphorylated on T75) [Figure S2C] alone established that MPF phosphorylates T75 in vitro [Figure 4D]).
PMID:23333317	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC649.05 [has_penetrance] high	(Fig. 4A) HU arrest Fig4E synchronous culture
PMID:23333317	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC649.05 [has_penetrance] high	(Fig. 4A) fin1 activation is dependent on sid1
PMID:23333317	FYPO:0007385	increased duration of protein-protein interaction [assayed_using] PomBase:SPBC649.05 [assayed_using] PomBase:SPBC776.02c [has_severity] high	(Fig. 4E) in absence of fin1 activity dis2 remains bound to cut 12
PMID:23333317	FYPO:0002033	abolished protein phosphorylation during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC649.05	(Fig. 4F) T75 T78 no longer phosphorylated and dis2 remains bound to cut12
PMID:23333317	FYPO:0007385	increased duration of protein-protein interaction [has_penetrance] high [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPBC649.05	(Fig. 4F) dis2 remains bound to cut12
PMID:23333317	FYPO:0002821	decreased protein localization to mitotic spindle pole body during interphase [assayed_using] PomBase:SPAC23C11.16 [has_penetrance] high [has_severity] medium	(Fig. 5A) No increase in recruitment of plo1 to SPB when fin1 is active if T75 T78 mutated to A
PMID:23333317	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_penetrance] high	(Fig. 5A) plo1 localisation to SPB is dependent on fin1 activity
PMID:23333317	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_penetrance] high	(Fig. 5A) plo1 localisation to SPB is dependent on fin1 activity
PMID:23333317	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] low	(Fig. 5B)
PMID:23333317	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 5B)
PMID:23333317	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 5B)
PMID:23333317	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05 [has_severity] low	(Fig. 5B)
PMID:23333317	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 5B)
PMID:23333317	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 5B)
PMID:23333317	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 5B)
PMID:23333317	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 5B)
PMID:23333317	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] high	(Fig. 5B)
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 5B)
PMID:23333317	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 5B)
PMID:23333317	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 5B)
PMID:23333317	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 5B)
PMID:23333317	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 5B)
PMID:23333317	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] high	(Fig. 5B)
PMID:23333317	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] high	(Fig. 5B)
PMID:23333317	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05 [has_severity] medium	(Fig. 5B)
PMID:23333317	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05 [has_severity] low	(Fig. 5B)
PMID:23333317	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] low	(Fig. 5B)
PMID:23333317	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05 [has_severity] high	(Fig. 5B)
PMID:23333317	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05	(Fig. 5B)
PMID:23333317	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05	(Fig. 5B)
PMID:23333317	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05 [has_severity] low	(Fig. 5B)
PMID:23333317	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] high	(Fig. 5B)
PMID:23333317	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC23C11.16 [assayed_using] PomBase:SPBC649.05 [has_severity] high	(Fig. 5B)
PMID:23333317	FYPO:0007475	delayed onset of protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] low	(Fig. 5B) (comment: CHECK DELAYED)
PMID:23333317	FYPO:0007475	delayed onset of protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] low	(Fig. 5B) (comment: CHECK DELAYED)
PMID:23333317	FYPO:0007475	delayed onset of protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] low	(Fig. 5B) (comment: CHECK DELAYED)
PMID:23333317	FYPO:0003331	decreased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 5B) plo1 decreased specific activity
PMID:23333317	FYPO:0003331	decreased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 5B) plo1 decreased specific activity
PMID:23333317	FYPO:0003331	decreased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 5B) plo1 decreased specific activity
PMID:23333317	FYPO:0007183	increased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] high	(Fig. 5B) plo1 increased specific activity
PMID:23333317	FYPO:0007183	increased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] high	(Fig. 5B) plo1 increased specific activity
PMID:23333317	FYPO:0007183	increased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] low	(Fig. 5B) plo1 increased specific activity
PMID:23333317	FYPO:0007183	increased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] low	(Fig. 5B) plo1 increased specific activity
PMID:23333317	FYPO:0007183	increased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] high	(Fig. 5B) plo1 increased specific activity
PMID:23333317	FYPO:0007183	increased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 5B) plo1 increased specific activity
PMID:23333317	FYPO:0007183	increased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 5B) plo1 increased specific activity
PMID:23333317	FYPO:0007183	increased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] high	(Fig. 5B) plo1 increased specific activity
PMID:23333317	FYPO:0007183	increased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 5B) plo1 increased specific activity
PMID:23333317	FYPO:0007183	increased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 5B) plo1 increased specific activity
PMID:23333317	FYPO:0007183	increased protein kinase activity during mitotic interphase [assayed_using] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 5B) plo1 increased specific activity
PMID:23333317	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_severity] medium	(Fig. 5B) premature recruitment of protein to the mitotic SPB
PMID:23333317	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPBC649.05 [part_of] positive regulation of G2/M transition of mitotic cell cycle [occurs_in] mitotic spindle pole body [happens_during] mitotic G2 phase	(comment: CHECK T75)
PMID:23333317	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC649.05 [part_of] positive regulation of G2/M transition of mitotic cell cycle [occurs_in] mitotic spindle pole body [happens_during] mitotic G2 phase	(comment: CHECK T75T78)
PMID:23333317	FYPO:0006824	premature protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C11.16 [has_penetrance] high	(comment: vw: could this one be abolished?) (Fig. 5A) No change in recruitment of plo1 to SPB when fin1 is inactivated T75 T78 mutated to D
PMID:23348717	FYPO:0003301	delayed onset of protein degradation via N-end rule pathway during meiosis [assayed_using] PomBase:SPBC29A10.14	(comment: also assayed using AspRec8c-FGFP construct, which persists longer than unmodified full-length Rec8)
PMID:23348717	FYPO:0003299	normal protein degradation via N-end rule pathway during vegetative growth	(comment: assayed using ArgDHFRts-HA-Mcm4ts construct or AspRec8c-FGFP construct)
PMID:23348717	FYPO:0003300	decreased protein degradation via N-end rule pathway during vegetative growth [has_severity] high	(comment: assayed using ArgDHFRts-HA-Mcm4ts construct or AspRec8c-FGFP construct)
PMID:23348717	FYPO:0003300	decreased protein degradation via N-end rule pathway during vegetative growth [has_severity] high	(comment: assayed using AspRec8c-FGFP construct)
PMID:23348717	FYPO:0003300	decreased protein degradation via N-end rule pathway during vegetative growth [has_severity] high	(comment: assayed using AspRec8c-FGFP construct)
PMID:23348717	FYPO:0003300	decreased protein degradation via N-end rule pathway during vegetative growth [has_severity] high	(comment: assayed using cell growth with AspRec8c-FGFP-Mei2SATA construct -degradation frees Mei2SATA to arrest cell cycle)
PMID:23349636	GO:0031146	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [has_input] PomBase:SPBC25H2.13c	(comment: CHECK more specifically, response to mitotic DNA replication checkpoint signaling)
PMID:23349808	GO:0071341	medial cortical node [exists_during] mitotic interphase	(comment: CHECK during G2 phase of mitotic cell cycle)
PMID:23349808	GO:0071341	medial cortical node [exists_during] mitotic interphase	(comment: CHECK during G2 phase of mitotic cell cycle)
PMID:23349808	GO:0071341	medial cortical node [exists_during] mitotic interphase	(comment: CHECK during G2 phase of mitotic cell cycle)
PMID:23349808	GO:0071341	medial cortical node [exists_during] mitotic interphase	(comment: CHECK during G2 phase of mitotic cell cycle)
PMID:23349808	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic M phase	(comment: CHECK during cytokinesis)
PMID:23394829	GO:0044732	mitotic spindle pole body [exists_during] mitotic metaphase	(comment: CHECK also present in early anaphase; disappears by late anaphase)
PMID:23394829	GO:0044732	mitotic spindle pole body	(comment: CHECK also present in early anaphase; disappears by late anaphase)
PMID:23395004	FYPO:0003615	decreased meiotic DNA double-strand break formation	((comment: rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag))
PMID:23395004	FYPO:0003615	decreased meiotic DNA double-strand break formation	(comment: ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag))
PMID:23395004	FYPO:0003615	decreased meiotic DNA double-strand break formation	(comment: ChIP-CHIP, rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag))
PMID:23395004	FYPO:0007657	decreased protein localization to linear element at meiotic recombination hotspot [assayed_using] PomBase:SPBC577.05c	(comment: ChIP-CHIP, rec27-205::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0000909	abnormal protein localization to linear element [assayed_using] PomBase:SPBC36B7.06c	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0000909	abnormal protein localization to linear element [assayed_using] PomBase:SPBC36B7.06c	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0000909	abnormal protein localization to linear element [assayed_using] PomBase:SPBC36B7.06c	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0004585	abnormal linear element morphology	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0004585	abnormal linear element morphology	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0004585	abnormal linear element morphology	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0004585	abnormal linear element morphology	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0000909	abnormal protein localization to linear element [assayed_using] PomBase:SPBC36B7.06c	(comment: mug20::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0003181	abolished meiotic DNA double-strand break formation	(comment: rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag))
PMID:23395004	FYPO:0003615	decreased meiotic DNA double-strand break formation	(comment: rec12-201::6His-2FLAG(C-terminal 6His-2FLAG tag))
PMID:23395004	FYPO:0004585	abnormal linear element morphology	(comment: rec25-204::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0000909	abnormal protein localization to linear element [assayed_using] PomBase:SPAC17A5.18c	(comment: rec25-204::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0000909	abnormal protein localization to linear element [assayed_using] PomBase:SPBC577.05c	(comment: rec27-205::GFP-kanMX6(C-terminal GFP tag))
PMID:23395004	FYPO:0004585	abnormal linear element morphology	(comment: rec27-205::GFP-kanMX6(C-terminal GFP tag))
PMID:23427262	FYPO:0005215	decreased protein localization to kinetochore during mitotic M phase [assayed_using] PomBase:SPAC890.02c	(comment: vw: after attachment)
PMID:23427262	FYPO:0005215	decreased protein localization to kinetochore during mitotic M phase [assayed_using] PomBase:SPCC895.07	(comment: vw: after attachment)
PMID:23442800	GO:1902426	deactivation of mitotic spindle assembly checkpoint	(comment: required for ubiquitination of Slp1)
PMID:23462181	GO:0044732	mitotic spindle pole body [exists_during] mitotic interphase	(Fig. 2A and B)
PMID:23462181	GO:0000935	division septum	(Fig. 2A and B)
PMID:23462181	GO:0051286	cell tip	(Fig. 2A and B)
PMID:23462181	GO:0005730	nucleolus	(Fig. 2A and B)
PMID:23462181	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	(Fig. 2A and B)
PMID:23496905	FYPO:0005818	normal protein neddylation [assayed_using] PomBase:SPAC17G6.12	(Fig. 2)
PMID:23496905	FYPO:0005818	normal protein neddylation [assayed_using] PomBase:SPAC17G6.12	(Fig. 2)
PMID:23496905	FYPO:0005818	normal protein neddylation [assayed_using] PomBase:SPAC17G6.12	(Fig. 2)
PMID:23496905	FYPO:0005818	normal protein neddylation [assayed_using] PomBase:SPAC17G6.12	(Fig. 2)
PMID:23496905	GO:0000338	protein deneddylation	(Fig. 2)
PMID:23496905	FYPO:0005822	decreased NEDD8-specific protease activity [assayed_using] PomBase:SPAC17G6.12 [has_severity] medium	(Fig. 4) (comment: CHECK 40% act remaining)
PMID:23496905	FYPO:0005822	decreased NEDD8-specific protease activity [assayed_using] PomBase:SPAC17G6.12 [has_severity] medium	(Fig. 4) (comment: CHECK 60%)
PMID:23496905	FYPO:0002060	viable vegetative cell population	(Figure 1)
PMID:23496905	FYPO:0002060	viable vegetative cell population	(Figure 1)
PMID:23496905	FYPO:0002060	viable vegetative cell population	(Figure 1)
PMID:23496905	FYPO:0002060	viable vegetative cell population	(Figure 1)
PMID:23496905	FYPO:0002060	viable vegetative cell population	(Figure 1)
PMID:23496905	FYPO:0005820	increased protein neddylation during vegetative growth [assayed_using] PomBase:SPAC17G6.12	(Figure 2)
PMID:23496905	GO:0019784	deNEDDylase activity [has_input] PomBase:SPBC12D12.08c [part_of] protein deneddylation	(Figure 3)
PMID:23496905	GO:0019784	deNEDDylase activity [has_input] PomBase:SPBC12D12.08c [part_of] protein deneddylation	(Figure 3)
PMID:23496905	GO:0019784	deNEDDylase activity [has_input] PomBase:SPBC12D12.08c [part_of] protein deneddylation	(Figure 3)
PMID:23496905	GO:0019784	deNEDDylase activity [has_input] PomBase:SPBC12D12.08c [part_of] protein deneddylation	(Figure 3)
PMID:23503588	FYPO:0002064	abolished 3'-5'-exoribonuclease activity	(comment: CHECK in vitro)
PMID:23555033	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_at] CSL_response_element	(comment: CHECK occurs_at CSL_response_element in vivo)
PMID:23555033	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_at] CSL_response_element	(comment: CHECK occurs_at CSL_response_element, overexpression, in vitro)
PMID:23555033	GO:0045944	positive regulation of transcription by RNA polymerase II	(comment: CHECK overexpression)
PMID:23555033	FYPO:0000659	abolished DNA binding [assayed_using] PomBase:SPCC1223.13 [assayed_using] CSL_response_element	(comment: CHECK to CSL_response_element)
PMID:23555033	FYPO:0000659	abolished DNA binding [assayed_using] PomBase:SPCC736.08 [assayed_using] CSL_response_element	(comment: CHECK to CSL_response_element)
PMID:23576550	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC16A3.15c	(comment: anti-alpha-tubulin antibody used; included both pombe alpha-tubulin gene names in extension)
PMID:23576550	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC800.05c	(comment: anti-alpha-tubulin antibody used; included both pombe alpha-tubulin gene names in extension)
PMID:23609449	FYPO:0000663	decreased catalytic activity [assayed_enzyme] PomBase:SPAC1002.03c	(Figure 10) (comment: CHECK check specificity). Taken together, the results demonstrate that substitution of Trp-409 in the context of the full-length GIIβ has a moderate to high (60% inhibitory) effect on GII activity.
PMID:23609449	FYPO:0000663	decreased catalytic activity [assayed_enzyme] PomBase:SPAC1002.03c	(Figure 10) (comment: HECK check specificity)
PMID:23609449	GO:0140767	enzyme-substrate adaptor activity	(comment: binds the non trimmed part of the N-glycan)
PMID:23615450	FYPO:0004653	delayed onset of actomyosin contractile ring contraction	(Fig. 5)
PMID:23615450	FYPO:0003289	abnormal protein localization to medial cortical node [assayed_using] PomBase:SPAC20G8.05c	(Figure 1C and Supplemental Figure S1C)
PMID:23615450	FYPO:0001365	decreased rate of actomyosin contractile ring contraction [assayed_using] PomBase:SPAC20G8.05c	(Figure 1D)
PMID:23615450	FYPO:0003919	abolished protein localization to medial cortical node [assayed_using] PomBase:SPCC645.05c	(Figure 1E and Supplemental Figure S1C)
PMID:23615450	FYPO:0003919	abolished protein localization to medial cortical node [assayed_using] PomBase:SPAC4F8.13c	(Figure 1E and Supplemental Figure S1C)
PMID:23615450	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPBC1A4.05	(Figure 1E and Supplemental Figure S1C)
PMID:23615450	FYPO:0000161	abnormal actomyosin contractile ring assembly	(Figure 3).
PMID:23615450	FYPO:0002061	inviable vegetative cell population	(Figure 3).
PMID:23615450	FYPO:0002061	inviable vegetative cell population	(Figure 3).
PMID:23615450	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC4F8.13c [has_penetrance] 3	(Figure 4C)
PMID:23615450	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC4F8.13c [has_penetrance] 18	(Figure 4C)
PMID:23615450	FYPO:0001357	normal vegetative cell population growth	(Figure 4F)
PMID:23615450	FYPO:0001496	viable elongated multiseptate vegetative cell	(Figure 4F)
PMID:23615450	FYPO:0001917	inviable elongated mononucleate monoseptate vegetative cell [has_penetrance] low	(Figure 4F) (comment: inferred penetrance because growth not m,uch affected)
PMID:23615450	GO:0051015	actin filament binding	(comment: Kd ≈ 20 μM) Supplemental Figure S5B
PMID:23615450	FYPO:0002060	viable vegetative cell population	(comment: complements deletion)
PMID:23615450	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPAC4F8.13c	(comment: complements deletion)
PMID:23615450	FYPO:0002060	viable vegetative cell population	(comment: complements deletion)
PMID:23615450	FYPO:0002060	viable vegetative cell population	(comment: complements deletion)
PMID:23615450	FYPO:0002060	viable vegetative cell population	(comment: complements deletion)
PMID:23615450	FYPO:0001368	normal actomyosin contractile ring assembly	(comment: complements deletion)
PMID:23615450	FYPO:0004097	normal actomyosin contractile ring contraction	(comment: complements deletion)
PMID:23615450	FYPO:0001368	normal actomyosin contractile ring assembly	(comment: complements deletion)
PMID:23615450	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC24B11.11c	(comment: complements deletion) Figure 6A
PMID:23615450	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC428.13c	(comment: complements deletion) Figure 6A
PMID:23615450	FYPO:0006326	decreased protein localization to medial cortical node [assayed_using] PomBase:SPCC645.05c	(comment: complements deletion) Figure 6A
PMID:23615450	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPCC645.05c	(comment: complements deletion) Figure 6A
PMID:23615450	FYPO:0000639	delayed onset of septum assembly	(comment: complements deletion) Figure 6A
PMID:23615450	FYPO:0007139	abolished protein localization to medial cortical node during mitotic interphase [assayed_using] PomBase:SPAC4F8.13c	(comment: in interphase)
PMID:23615450	GO:0005515	protein binding	Supplemental Figure S9C)
PMID:23628763	FYPO:0002773	third meiotic division	(Fig. 2)
PMID:23628763	FYPO:0003451	abolished protein localization to nucleus during meiotic anaphase II [assayed_using] PomBase:SPCC584.02	(Fig. 3c)
PMID:23628763	FYPO:0001093	abolished chromatin binding [assayed_using] PomBase:SPCC584.02	(Fig. 3c)
PMID:23628763	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1198.12 [happens_during] meiosis II cell cycle phase [part_of] positive regulation of transcription by RNA polymerase II	(comment: inferred from chromatin binding at promoter, and phenotypes)
PMID:23628763	GO:0045944	positive regulation of transcription by RNA polymerase II	(commnent: boosts expression of the APC activator Fzr1/Mfr1)
PMID:23658229	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC1F8.05	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC1289.14	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC359.02	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBP4G3.03	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC212.06c	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPCC330.03c	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC212.08c	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23658229	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC750.07c	(comment: deleted this extension because it refers to a pseudogene: annotation_extension=assayed_using(PomBase:SPBPB10D8.03) (mah 2014-08-05))
PMID:23664927	GO:0140662	ATP-dependent protein folding chaperone	(comment: Hsp90 of S. pombe existed as a dimer and exhibited ATP-dependent conformational changes. It captured unfolded proteins in the ATP-free open conformation and protected them from thermal aggregation. Hsp90 of S. pombe was also able to refold thermally denatured firefly luciferase.)
PMID:23664927	GO:0001671	ATPase activator activity [has_input] PomBase:SPAC926.04c	(comment: The co-chaperones Sti1 and Aha1 bound Hsp90 and modulated its activity. Because the affinity of Sti1 was higher than that of Aha1, the effect of Sti1 appeared to dominate when both co-chaperones existed simultaneously.)
PMID:23664927	GO:0042030	ATPase inhibitor activity [has_input] PomBase:SPAC926.04c	(comment: The co-chaperones Sti1 and Aha1 bound Hsp90 and modulated its activity. Because the affinity of Sti1 was higher than that of Aha1, the effect of Sti1 appeared to dominate when both co-chaperones existed simultaneously.)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPCC364.07	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC19F5.04	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC3E7.16c	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC227.18	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC1002.09c	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC4G9.10	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC10F6.13c	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC56E4.03	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC418.01c	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC19F5.04	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC3E7.16c	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC227.18	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC1002.09c	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC4G9.10	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC10F6.13c	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPCC364.07	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAC56E4.03	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC418.01c	(comment: RNA level increases upon amitrole exposure in wild type but not mutant)
PMID:23671279	FYPO:0001097	sensitive to amitrole	(comment: same as cpc2delta alone)
PMID:23671279	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC3G9.09c [has_severity] medium	(comment: same as cpc2delta alone)
PMID:23671279	FYPO:0001097	sensitive to amitrole	(comment: same as either single mutant)
PMID:23671279	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC3G9.09c	(comment: same as gcn2delta alone)
PMID:23671279	GO:0140469	GCN2-mediated signaling	(comment: vw edited)
PMID:23671279	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC3G9.09c [has_severity] high	(comment: worse than cpc2delta alone)
PMID:23677513	FYPO:0000095	sensitive to bleomycin	(comment: CHECK same as hus1delta alone)
PMID:23677513	FYPO:0002345	sensitive to oxaliplatin	(comment: CHECK same as hus1delta alone)
PMID:23677513	FYPO:0002344	sensitive to phleomycin	(comment: CHECK same as hus1delta alone)
PMID:23677513	FYPO:0000102	sensitive to cisplatin	(comment: CHECK same as hus1delta alone)
PMID:23677513	FYPO:0002344	sensitive to phleomycin	(comment: CHECK same as rad9delta alone)
PMID:23677513	FYPO:0000095	sensitive to bleomycin	(comment: CHECK same as rad9delta alone)
PMID:23677513	FYPO:0002345	sensitive to oxaliplatin	(comment: CHECK same as rad9delta alone)
PMID:23677513	FYPO:0000102	sensitive to cisplatin	(comment: CHECK same as rad9delta alone)
PMID:23687372	FYPO:0000712	delayed onset of cell cycle arrest in mitotic G1 phase in response to nitrogen starvation	(comment: CHECK move down to G1, nitrogen induced)
PMID:23687372	MOD:00696	phosphorylated residue [added_during] G1 to G0 transition [added_by] PomBase:SPAC20G4.03c	(comment: CHECK occurs_during G1 to G0 transition)
PMID:23687372	MOD:00696	phosphorylated residue [added_during] G1 to G0 transition [added_by] PomBase:SPBC36B7.09	(comment: CHECK occurs_during G1 to G0 transition)
PMID:23687372	MOD:00696	phosphorylated residue [added_during] G1 to G0 transition [added_by] PomBase:SPAC222.07c	(comment: CHECK occurs_during G1 to G0 transition)
PMID:23687372	GO:0004694	eukaryotic translation initiation factor 2alpha kinase activity [has_input] PomBase:SPAC3G9.09c [happens_during] G1 to G0 transition [happens_during] cellular response to glucose starvation	(comment: CHECK occurs_during G1 to Go transition)
PMID:23687372	FYPO:0000708	decreased mating efficiency	(comment: homothallic h90)
PMID:23687372	FYPO:0000708	decreased mating efficiency	(comment: homothallic h90)
PMID:23695302	FYPO:0000223	elongated multiseptate vegetative cell	(comment: they don't say whether the OEP populations continue to grow like normal (viable/inviable).) Also data not shown.
PMID:23754748	FYPO:0002059	inviable cell population	(Figure S1)
PMID:23770677	GO:0000146	microfilament motor activity [part_of] mitotic actomyosin contractile ring contraction	We incubated cell ghosts in the presence of ATP and the myosin-II ATPase inhibitor blebbistatin (0.1 mM; ref. 17). Whereas rings underwent rapid contraction in the absence of blebbistatin, ring contraction was abolished in the presence of blebbistatin (Fig. 3a, nD8).
PMID:23770679	FYPO:0004159	abnormal homologous chromosome segregation [has_penetrance] 60	(Fig. 2G)
PMID:23770679	FYPO:0007112	decreased rate of microtubule depolymerization involved in meiotic centromere clustering during meiotic prophase I	(Fig. 2b-d) (comment: CHECK involved in kinetochore retrieval during meiotic prophase)
PMID:23770679	FYPO:0007112	decreased rate of microtubule depolymerization involved in meiotic centromere clustering during meiotic prophase I	(Fig. 2b-d) (comment: CHECK involved in kinetochore retrieval during meiotic prophase)
PMID:23770679	FYPO:0004159	abnormal homologous chromosome segregation [has_penetrance] 80	(Fig. 2g)
PMID:23770679	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPAC589.08c	(Fig. 3b)
PMID:23770679	FYPO:0007109	normal meiotic centromere clustering during meiotic prometaphase I	(Fig. 3d)
PMID:23770679	FYPO:0007108	abnormal meiotic centromere clustering during meiotic prophase I	(Fig. 3d)
PMID:23770679	FYPO:0007110	microtubule bundles present in decreased numbers at spindle pole body during meiosis I	(Fig. 4c)
PMID:23770679	FYPO:0007110	microtubule bundles present in decreased numbers at spindle pole body during meiosis I	(Fig. 4c)
PMID:23770679	FYPO:0004214	normal protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPAC890.02c	(Fig. 4d)
PMID:23770679	FYPO:0004214	normal protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPAC589.08c	(Fig. 4d)
PMID:23770679	FYPO:0000209	abnormal attachment of spindle microtubules to kinetochore during meiosis I	(Fig. 5b)
PMID:23770679	FYPO:0006427	abolished attachment of spindle microtubules to kinetochore during meiosis I	(Fig. 5b)
PMID:23770679	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPAC890.02c	(Fig. 5d,e) (comment: CHECK unattached)
PMID:23770679	FYPO:0004763	abolished protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPAC890.02c	(Fig. 6a)
PMID:23770679	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPAC890.02c [assayed_using] PomBase:SPCC895.07	(Fig. 6c) (comment: CHeCK or abolished)
PMID:23770679	FYPO:0000899	normal microtubule cytoskeleton organization during vegetative growth [assayed_using] PomBase:SPAC890.02c [assayed_using] PomBase:SPCC895.07	(Fig. 7)
PMID:23770679	FYPO:0000209	abnormal attachment of spindle microtubules to kinetochore during meiosis I	(Fig. 7c)
PMID:23770679	FYPO:0007108	abnormal meiotic centromere clustering during meiotic prophase I	(Figure 2a)
PMID:23770679	FYPO:0000678	unequal homologous chromosome segregation [has_penetrance] 78	(Figure 4)
PMID:23770679	FYPO:0007108	abnormal meiotic centromere clustering during meiotic prophase I	(Figure 4c)
PMID:23770679	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC890.02c [part_of] meiotic centromere clustering	(Figure 6b,d) (comment: d used chromosome tethered polo mutants, I didn't curate these phenotypes)
PMID:23770679	GO:0000776	kinetochore [exists_during] meiotic prophase I	(comment: CHECK Is this phase correct)
PMID:23770679	GO:0000776	kinetochore [exists_during] meiotic prophase I	(comment: CHECK Is this phase correct?)
PMID:23770679	GO:0000776	kinetochore [exists_during] meiotic prophase I	(comment: CHECK Is this phase correct?)
PMID:23770679	FYPO:0007107	normal microtubule cytoskeleton organization during meiosis I	(comment: CHECK meiosis I)
PMID:23770679	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPAC890.02c	(comment: polo consensus) fig 6b
PMID:23770679	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC890.02c [assayed_using] PomBase:SPCC895.07	Supp Fig S6
PMID:23770679	FYPO:0001357	normal vegetative cell population growth [assayed_using] PomBase:SPAC890.02c [assayed_using] PomBase:SPCC895.07	Supp Fig S6
PMID:23770679	GO:1990571	meiotic centromere clustering	The Alp7-Alp14 complex localises to kinetochores prior to meiosis I independently of microtubules, which does not seem to occur in mitosis.
PMID:23770679	GO:1990571	meiotic centromere clustering	The Alp7-Alp14 complex localises to kinetochores prior to meiosis I independently of microtubules, which does not seem to occur in mitosis.
PMID:23770679	GO:1990571	meiotic centromere clustering	The Alp7-Alp14 complex localises to kinetochores prior to meiosis I independently of microtubules, which does not seem to occur in mitosis.
PMID:23770679	GO:0005515	protein binding [part_of] meiotic centromere clustering [occurs_in] kinetochore [happens_during] meiotic prometaphase I	The Nuf2 complex interacts with the Alp7-Alp14 complex phosphorylated by the polo kinase Plo1
PMID:23770679	GO:0140483	kinetochore adaptor activity [has_input] alp7/Phos:(S248,T297,T351,S402) [part_of] meiotic centromere clustering [occurs_in] kinetochore	The Nuf2 complex interacts with the Alp7-Alp14 complex phosphorylated by the polo kinase Plo1
PMID:23851719	GO:0140673	transcription elongation-coupled chromatin remodeling	(comment: results in retaining specifically modified histone H3 at the genes in question)
PMID:23874237	FYPO:0003218	abolished tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridine biosynthesis [assayed_using] glutamyl_tRNA	(comment: CHECK The SO ID's correspond to tRNA lys/gln/glu)
PMID:23874237	FYPO:0003218	abolished tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridine biosynthesis [assayed_using] glutaminyl_tRNA	(comment: CHECK The SO ID's correspond to tRNA lys/gln/glu)
PMID:23874237	FYPO:0003218	abolished tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridine biosynthesis [assayed_using] lysyl_tRNA	(comment: CHECK The SO ID's correspond to tRNA lys/gln/glu)
PMID:23874237	GO:0140018	regulation of cytoplasmic translational fidelity [happens_during] cellular response to oxidative stress	We have determined that the main H2O2-dependent genes, including those coding for the transcription factors Atf1 and Pcr1, are highly expressed mRNAs containing a biased number of lysine-coding codons AAA versus AAG. Thus, their mRNAs are poorly translated after stress in cells lacking Sin3/Elp3 or Ctu2, whereas a mutated atf1 transcript with AAA-to-AAG lysine codons is efficiently translated in all strain backgrounds.
PMID:23874237	GO:0140018	regulation of cytoplasmic translational fidelity [happens_during] cellular response to oxidative stress	We have determined that the main H2O2-dependent genes, including those coding for the transcription factors Atf1 and Pcr1, are highly expressed mRNAs containing a biased number of lysine-coding codons AAA versus AAG. Thus, their mRNAs are poorly translated after stress in cells lacking Sin3/Elp3 or Ctu2, whereas a mutated atf1 transcript with AAA-to-AAG lysine codons is efficiently translated in all strain backgrounds.
PMID:23885124	GO:0044732	mitotic spindle pole body	(comment: throughout cell cycle; present in approximately equal stoichiometry with Alp4/GCP2 (immunoblotting and quantification of GFP-Mzt1 and GFP-Alp4 signals at the SPB))
PMID:23885124	GO:0008275	gamma-tubulin small complex	(comment: throughout cell cycle; present in approximately equal stoichiometry with Alp4/GCP2 (immunoblotting and quantification of GFP-Mzt1 and GFP-Alp4 signals at the SPB))
PMID:23907979	FYPO:0000105	sensitive to cyclosporin A [has_severity] medium	(Figure 4A) expression of rho1+, rgf1+, and rgf2+ restored the growth of an mtl2D mutant in the presence of the antifungal agent, whereas overexpression of rgf3+ did not suppress the growth defect.
PMID:23907979	FYPO:0000105	sensitive to cyclosporin A [has_severity] medium	(Figure 4A) expression of rho1+, rgf1+, and rgf2+ restored the growth of an mtl2D mutant in the presence of the antifungal agent, whereas overexpression of rgf3+ did not suppress the growth defect.
PMID:23907979	FYPO:0000105	sensitive to cyclosporin A [has_severity] medium	(Figure 4A) expression of rho1+, rgf1+, and rgf2+ restored the growth of an mtl2D mutant in the presence of the antifungal agent, whereas overexpression of rgf3+ did not suppress the growth defect.
PMID:23907979	FYPO:0001357	normal vegetative cell population growth	(Figure 4B) the activation of Rho1p, through the expression of a constitutively active form of Rho1p or overexpression of the wild-type Rho1p or Rgf1p, efficiently restored the growth of a strain (P81nmt-mtl2 wsc1D) unable to grow in the presence of thiamine (promoter off).
PMID:23907979	FYPO:0000021	spheroid vegetative cell	(comment: described as rounded , but more 'stubby')
PMID:23907979	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPCC645.07	. Interestingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPAC1006.06	. Interestingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPCC645.06c	. Interestingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	FYPO:0000841	sensitive to sodium dodecyl sulfate [has_severity] high	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	FYPO:0000097	sensitive to caffeine during vegetative growth [has_severity] high	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	FYPO:0003656	sensitive to vanadate [has_severity] high	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	FYPO:0005889	sensitive to sodium chloride [has_severity] high	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	Deletion of mtl2+ rendered cells hypersensitive to caffeine, vanadate, NaCl, H2O2, and SDS (see Fig. S1).
PMID:23907979	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC1F7.04	GTP bound modified form . Interestingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC1F7.04	GTP bound modified form. Interestingly, mtl2D and wsc1D mutants contained much less Rho1p-GTP than wild-type cells when the cultures were grown in the presence of 0.1 lg/mL of Csp for 16 h prior to harvesting (Fig. 4C)
PMID:23907979	FYPO:0004978	increased protein localization to new growing cell tip [assayed_protein] PomBase:SPBC30B4.01c	In tea4D cells, Wsc1p-GFP localized mainly to the growing tip that was stained with Cfw (Fig. 3C).
PMID:23907979	FYPO:0002627	altered level of substance in cell wall during vegetative growth	Moreover, when we looked at the cell wall composition of mtl2D mutants we found a decrease in the total amount of glucose incorporated in the cell wall as compared with wild-type cells (30% in wild-type cells and 25% in mtl2D). The difference was mainly due to a decrease in the b-glucan content (17% in the wild type and 13% in the mtl2D) (Fig. 1E).
PMID:23907979	GO:0005886	plasma membrane	Mtl2p-GFP showed an even membrane distribution with little intra- cellular signals.
PMID:23907979	FYPO:0000647	vegetative cell lysis	Repression of mtl2+ promoted cell lysis and the cells shrunk without the release of cytoplasmic material.
PMID:23907979	FYPO:0007910	increased vegetative cell shrinkage	Repression of mtl2+ promoted cell lysis and the cells shrunk without the release of cytoplasmic material.
PMID:23907979	FYPO:0000760	normal mating	The mating rate was not affected in mtl2Δh+ × mtl2Δh− or wsc1Δh+ × wsc1Δh− homozygous crosses
PMID:23907979	FYPO:0000760	normal mating	The mating rate was not affected in mtl2Δh+ × mtl2Δh− or wsc1Δh+ × wsc1Δh− homozygous crosses
PMID:23907979	FYPO:0001357	normal vegetative cell population growth	The wsc1D and mtl2D mutants grew well under standard growth conditions at both 28 and 37°C and entered the stationary phase at the same time as the wild-type cultures.
PMID:23907979	FYPO:0001357	normal vegetative cell population growth	The wsc1D and mtl2D mutants grew well under standard growth conditions at both 28 and 37°C and entered the stationary phase at the same time as the wild-type cultures.
PMID:23907979	FYPO:0001357	normal vegetative cell population growth	The wsc1D and mtl2D mutants grew well under standard growth conditions at both 28 and 37°C and entered the stationary phase at the same time as the wild-type cultures.
PMID:23907979	FYPO:0002061	inviable vegetative cell population	The wsc1Drgf2D double mutant was viable, but we failed to find any double- mutant spore wsc1Drgf1D. T
PMID:23907979	FYPO:0002159	decreased 1,3-beta-D-glucan synthase activity [has_severity] low	We found that GS activity was slightly reduced in mtl2D null cells (Fig. 1D)
PMID:23907979	GO:0031520	plasma membrane of cell tip	Wsc1p-GFP was found along the entire plasma membrane, but appeared much more concentrated in patches at the cell ends. We also noted that Wsc1p-GFP accumulated in intracellular compartments (Fig. 3C and D).
PMID:23907979	GO:0005886	plasma membrane	Wsc1p-GFP was found along the entire plasma membrane, but appeared much more concentrated in patches at the cell ends. We also noted that Wsc1p-GFP accumulated in intracellular compartments (Fig. 3C and D).
PMID:23907979	FYPO:0000105	sensitive to cyclosporin A [has_severity] medium	mtl2D cells were unable to grow on plates supplemented with 0.5 lg/mL Csp, whereas the wild-type cells were able to withstand concentrations of up to 5 lg/ mL
PMID:23907979	FYPO:0000105	sensitive to cyclosporin A [has_severity] medium	mtl2D cells were unable to grow on plates supplemented with 0.5 lg/mL Csp, whereas the wild-type cells were able to withstand concentrations of up to 5 lg/ mL
PMID:23907979	FYPO:0000105	sensitive to cyclosporin A [has_severity] high	mtl2D cells were unable to grow on plates supplemented with 0.5 lg/mL Csp, whereas the wild-type cells were able to withstand concentrations of up to 5 lg/ mL
PMID:23907979	FYPO:0001315	normal vegetative cell morphology	wsc1D and mtl2D cells did not exhibit any evident morphological changes (Fig. 1B)
PMID:23907979	FYPO:0001315	normal vegetative cell morphology	wsc1D and mtl2D cells did not exhibit any evident morphological changes (Fig. 1B)
PMID:23907979	FYPO:0000105	sensitive to cyclosporin A [has_severity] medium	wsc1D cell growth was inhibited above 2 lg/mL of Csp (Fig. 1C)
PMID:23907979	FYPO:0000647	vegetative cell lysis [has_penetrance] 15	~8% of the cells in the wsc1D mutant and 15% of the cells in mtl2D were lysed (Fig. 1B)
PMID:23907979	FYPO:0000647	vegetative cell lysis [has_penetrance] 8	~8% of the cells in the wsc1D mutant and 15% of the cells in mtl2D were lysed (Fig. 1B)
PMID:23936074	FYPO:0003011	increased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPBC1105.17	(comment: CHECK increased staining of all chromatin)
PMID:23936074	FYPO:0003010	increased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_using] PomBase:SPBC1105.17	(comment: assayed using minichromosomes and internal telomeric repeat arrays)
PMID:23956092	FYPO:0001496	viable elongated multiseptate vegetative cell	(comment: was branched, elongated, multiseptate cell )
PMID:23962284	GO:0004864	protein phosphatase inhibitor activity [has_input] PomBase:SPAC57A7.08	(comment: recombinant hal3 not a strong inhibitor in vitro)
PMID:23962284	FYPO:0002059	inviable cell population	(comment: we don't know if they germinate or not)
PMID:23966468	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPAC16A10.04	(comment: This is inferred from a combination of genetic interactions, localizations and phenocopy experiments, it has not been directly assayed but it feels 'safe')
PMID:23966468	GO:1902408	mitotic cytokinesis, division site positioning	Taken together, our data indicate that Nod1 and Gef2 function cooperatively in a protein complex to regulate fission yeast cytokinesis.
PMID:23966468	GO:1902408	mitotic cytokinesis, division site positioning	Taken together, our data indicate that Nod1 and Gef2 function cooperatively in a protein complex to regulate fission yeast cytokinesis.
PMID:23977061	FYPO:0000538	decreased protein secretion during vegetative growth [assayed_using] PomBase:SPAC821.09	effect on secretion is specific for cell wall enzymes; secretion of acid phosphatase is normal (comment: but assayed acid phosphatase activity in medium, so can't tell which gene(s))
PMID:23986474	FYPO:0001696	sensitive to protein kinase inhibitor [has_severity] high	(Fig. 1)
PMID:23986474	FYPO:0001696	sensitive to protein kinase inhibitor [has_severity] high	(Fig. 1)
PMID:23986474	FYPO:0001696	sensitive to protein kinase inhibitor [has_severity] high	(Fig. 1)
PMID:23986474	FYPO:0001696	sensitive to protein kinase inhibitor [has_severity] high	(Fig. 1) Chronic exposure to analogue through growth on solid medium reiterated the acute impact of analogue inhibition in liquid culture (Fig. 1A) and established that plo1.as8 is most effectively inhibited by 3BrB- PP1 (Fig. 1B).
PMID:23986474	FYPO:0001696	sensitive to protein kinase inhibitor [has_severity] high	(Fig. 1) Chronic exposure to analogue through growth on solid medium reiterated the acute impact of analogue inhibition in liquid culture (Fig. 1A) and established that plo1.as8 is most effectively inhibited by 3BrB- PP1 (Fig. 1B).
PMID:23986474	FYPO:0001696	sensitive to protein kinase inhibitor [has_severity] medium	(Fig. 2B) orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none
PMID:23986474	FYPO:0001696	sensitive to protein kinase inhibitor [has_severity] medium	(Fig. 2B) orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none
PMID:23986474	FYPO:0001696	sensitive to protein kinase inhibitor [has_severity] medium	(Fig. 2B) orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none
PMID:23986474	FYPO:0001696	sensitive to protein kinase inhibitor [has_severity] medium	(Fig. 2B) orb5.as2 displayed moderate sensitivity to 30 mM of 3BrB-PP1, whereas orb5.as1 showed none
PMID:23986474	FYPO:0001696	sensitive to protein kinase inhibitor [has_severity] high	(Fig. 2B). The M167F mutation in either the orb5.as1 or orb5.as2 backbone generated the orb5.as8 and orb5.as9 alleles, which were more sensitive to analogue inhibition than the respective parental allele
PMID:23986474	FYPO:0001696	sensitive to protein kinase inhibitor [has_severity] high	(Fig. 2B). The M167F mutation in either the orb5.as1 or orb5.as2 backbone generated the orb5.as8 and orb5.as9 alleles, which were more sensitive to analogue inhibition than the respective parental allele
PMID:23986474	FYPO:0002061	inviable vegetative cell population	(Fig. 3c)
PMID:23986474	FYPO:0001357	normal vegetative cell population growth	(Fig. 3c) We therefore compared the ability of wee1.as1 and wee1.as8 to suppress cdc25.22 lethality at 36 ̊C. Inhibition of Wee1.as8 but not Wee1.as1 activity with analogue addition suppressed cdc25.22 lethality at 36 ̊C (Fig. 3B). A comparison of four ATP analogues revealed that the suppression (and therefore Wee1 inhibition) was most effective with 3BrB-PP1 (Fig. 3C).
PMID:23986474	FYPO:0001357	normal vegetative cell population growth	(Fig. 3c) We therefore compared the ability of wee1.as1 and wee1.as8 to suppress cdc25.22 lethality at 36 ̊C. Inhibition of Wee1.as8 but not Wee1.as1 activity with analogue addition suppressed cdc25.22 lethality at 36 ̊C (Fig. 3B). A comparison of four ATP analogues revealed that the suppression (and therefore Wee1 inhibition) was most effective with 3BrB-PP1 (Fig. 3C).
PMID:23986474	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 4c)
PMID:23986474	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(Table 1; Fig. 3A)
PMID:23986474	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(Table 1; Fig. 3A)
PMID:23986474	FYPO:0003165	cut [has_penetrance] 20	Analogue-released wee1.as8 cdc25.22 cut9.665 cells transiently accumulated much higher levels of metaphase spindles than wild-type cells before they ‘leaked’ through this mitotic arrest to execute telophase and cytokinesis with the classic ‘cut’ phenotype that originally led to the identification of the cut9.665 mutation (Fig. 6A,B)
PMID:23986474	FYPO:0002061	inviable vegetative cell population	DNS
PMID:23986474	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	DNS
PMID:23986474	FYPO:0000444	abnormal mitotic cell cycle arrest with replicated DNA	The static FACS profiles established that replication was indeed inhibited in analogue-released cdc10.v50 wee1.as8 cdc25.22 cells after analogue addition (Fig. 7B, right panel).
PMID:23986474	FYPO:0005344	abolished mitotic spindle midzone assembly	as arrested at 36 ̊C for 4.25 hours and released into synchronous mitosis by Wee1 inhibition using 30 mM 3BrB-PP1. The figure shows tubulin immunofluorescence and DAPI signals of cells 3 hours after release to reveal the characteristic ‘crows foot’ configuration of microtubules of cut7 mutants as the two halves of the mitotic spindle fail to interdigitate.
PMID:23986474	FYPO:0001125	normal vegetative cell shape	rb5.as8 inhibition did not produce the ‘orb’ phenotype observed in the original orb5.ts mutants at the restrictive temperature (data not shown)
PMID:24003116	GO:0000122	negative regulation of transcription by RNA polymerase II [part_of] cellular response to zinc ion	(comment: CHECK directly regulates adh4)
PMID:24003116	FYPO:0001552	increased cellular zinc level	(comment: CONDITION Grown in EMM + 200uM ZnSo) (comment: Measurements made via ICP-MS)
PMID:24003116	FYPO:0001552	increased cellular zinc level	(comment: CONDITION Grown in EMM + 200uM ZnSo). (comment: Measurements made via ICP-MS)
PMID:24003116	FYPO:0001534	decreased cellular zinc level	(comment: CONDITION Grown in EMM + 200uM ZnSo). (comment: Measurements made via ICP-MS)
PMID:24003116	GO:0005634	nucleus	(comment: CONDITION Visualized via Florescence using an integrated LOZ1::GFP construct) (comment: CONDITION grown in EMM +/- ZnSo4)
PMID:24003116	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_at] zinc_repressed_element	(comment: Via EMSA binds directly to adh4 promoter).
PMID:24006256	GO:0010971	positive regulation of G2/M transition of mitotic cell cycle	(comment: Dnt1 down-regulates Wee1 kinase. Had to remove extensions: independent_of(PomBase:Cdc25)| independent_of(PomBase:Rad3)| independent_of(PomBase:Chk1)| independent_of(PomBase:Cds1)| independent_of(PomBase:Clp1)| independent_of(PomBase:Pom1)| independent_of(PomBase:Cut12)| dependent_on(PomBase:Wee1) | acts_upstream_of(wee1))
PMID:24006256	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(comment: wee1-50 epistatic to dnt1delta; shows that cell cycle regulation by Dnt1 depends on Wee1)
PMID:24006488	FYPO:0002978	increased protein localization to chromatin during cellular response to methyl methanesulfonate [assayed_using] PomBase:SPBC21B10.13c	(Fig. 4)
PMID:24006488	FYPO:0002978	increased protein localization to chromatin during cellular response to methyl methanesulfonate [assayed_using] PomBase:SPBC21B10.13c	(Fig. 4)
PMID:24006488	FYPO:0002979	normal protein localization to chromatin during cellular response to methyl methanesulfonate [assayed_using] PomBase:SPBC21B10.13c	(Fig. 4)
PMID:24006488	FYPO:0002978	increased protein localization to chromatin during cellular response to methyl methanesulfonate [assayed_using] PomBase:SPBC336.12c	(Fig. 4)
PMID:24006488	FYPO:0002978	increased protein localization to chromatin during cellular response to methyl methanesulfonate [assayed_using] PomBase:SPBC336.12c	(Fig. 4)
PMID:24006488	FYPO:0002979	normal protein localization to chromatin during cellular response to methyl methanesulfonate [assayed_using] PomBase:SPBC336.12c	(Fig. 4)
PMID:24006488	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC1259.13 [present_during] DNA damage checkpoint signaling	(comment: Phosphorylation releases MBF from DNA and represses transcription of MBF-dependent genes.)
PMID:24006488	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC1259.13 [present_during] DNA damage checkpoint signaling	(comment: Phosphorylation releases MBF from DNA and represses transcription of MBF-dependent genes.)
PMID:24006488	MOD:00696	phosphorylated residue	(comment: annotate - Serine 114 and Threonine 115 are phosphorylated by Cds1 upon activation of the DNA replication checkpoint) (comment: Yox1 phosphorylation by Cds1 releases Yox1 from MBF and activates MBF-dependent transcription)
PMID:24006488	GO:0000122	negative regulation of transcription by RNA polymerase II [part_of] mitotic DNA damage checkpoint signaling	(comment: localizes the MBF complex)
PMID:24013500	GO:0031508	pericentric heterochromatin formation	(comment: siRNA independent)
PMID:24013500	GO:0031508	pericentric heterochromatin formation	(comment: siRNA independent)
PMID:24013500	GO:0031508	pericentric heterochromatin formation	(comment: siRNA independent)
PMID:24013500	GO:0031508	pericentric heterochromatin formation	(comment: siRNA independent)
PMID:24013500	GO:0031508	pericentric heterochromatin formation	(comment: siRNA independent)
PMID:24013500	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	A strain harboring a ura4+ reporter gene inserted into the innermost repeat (imr) region of centromere 1 displays reduced growth on 5-FOA when harboring the seb1-1 allele (Fig. 1C). I
PMID:24013500	GO:0106222	lncRNA binding [occurs_in] dg_repeat	As expected, Hrr1, an RNAi factor, also associates with dg and dh ncRNAs but not with snR30 or act1+ RNA (Supplemental Fig. S1A).
PMID:24013500	FYPO:0004170	abolished histone H3-K9 dimethylation at centromere during vegetative growth	Finally, a catalytically dead point mutation in the Clr3 HDAC or the Mit1 ATPase domain also eliminates H3K9me in dcr1-R1R2 cells (Fig. 3A).
PMID:24013500	FYPO:0004170	abolished histone H3-K9 dimethylation at centromere during vegetative growth	Finally, a catalytically dead point mutation in the Clr3 HDAC or the Mit1 ATPase domain also eliminates H3K9me in dcr1-R1R2 cells (Fig. 3A).
PMID:24013500	FYPO:0004170	abolished histone H3-K9 dimethylation at centromere during vegetative growth	Furthermore, the elimination of H3K9me2 at dg and dh repeats was also observed in strains that have the dcr1-R1R2 mutation combined with a deletion mutation that eliminates the Clr1, Chp2, or Mit1 subunits of SHREC (Fig. 3A).
PMID:24013500	FYPO:0004170	abolished histone H3-K9 dimethylation at centromere during vegetative growth	Furthermore, the elimination of H3K9me2 at dg and dh repeats was also observed in strains that have the dcr1-R1R2 mutation combined with a deletion mutation that eliminates the Clr1, Chp2, or Mit1 subunits of SHREC (Fig. 3A).
PMID:24013500	FYPO:0004170	abolished histone H3-K9 dimethylation at centromere during vegetative growth	Furthermore, the elimination of H3K9me2 at dg and dh repeats was also observed in strains that have the dcr1-R1R2 mutation combined with a deletion mutation that eliminates the Clr1, Chp2, or Mit1 subunits of SHREC (Fig. 3A).
PMID:24013500	FYPO:0000220	increased centromeric outer repeat transcript level	In contrast, a catalytically dead Dcr1 mutant (dcr1-R1R2) (Colmenares et al. 2007) displays a dramatic increase in dg and dh transcript levels (Fig. 2B).
PMID:24013500	FYPO:0000876	decreased histone H3-K9 dimethylation during vegetative growth	In the ectopic heterochromatic silencing reporter strain, the seb1-1 mutation causes an accumulation of the ura4+ transcript (Fig. 1D) and a strong defect in H3K9me2 at the ura4+ gene (Fig. 1E), supporting the growth defect observed using the 5-FOA assay.
PMID:24013500	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPAC222.09	Indeed, the level of Seb1 protein is lower in the seb1-1 mutant when compared with its level in the wild-type seb1+ strain (Supplemental Fig. S4)
PMID:24013500	FYPO:0007307	increased histone H3-K14 acetylation at centromere during vegetative growth [assayed_protein] PomBase:SPAC222.09	Moreover, we found that the seb1-1 mutation increases Pol II occupancy and H3K14 acetylation levels at dg and dh repeats (Figs. 3D,E)
PMID:24013500	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth [has_severity] medium	Similar results were obtained when comparing H3K9me2 levels at dg and dh repeats of the seb1-1 clr1D double mutant with the levels of the corresponding single mutants (Fig. 3C). T
PMID:24013500	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth [has_severity] medium	Similar results were obtained when comparing H3K9me2 levels at dg and dh repeats of the seb1-1 clr1D double mutant with the levels of the corresponding single mutants (Fig. 3C). T
PMID:24013500	FYPO:0004170	abolished histone H3-K9 dimethylation at centromere during vegetative growth	Strikingly, while the levels of H3K9me2 are reduced by only threefold to fivefold in the single mutants, H3K9me2 is virtually abolished in the dcr1-R1R2 seb1-1 double mutant to background levels comparable with those measured in the clr4D mutant (Fig. 2C).
PMID:24013500	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth [has_severity] medium	To further test whether Seb1 functions in the same pathway as SHREC in promoting H3K9me, we compared H3K9me2 levels at dg and dh repeats of the seb1-1 clr3D double mutant with those of the corresponding single mutants. Significantly, the double and single mutants display very similar levels of H3K9me2, ;20%-30% of wild-type levels (Fig. 3B).
PMID:24013500	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth [has_severity] medium	To further test whether Seb1 functions in the same pathway as SHREC in promoting H3K9me, we compared H3K9me2 levels at dg and dh repeats of the seb1-1 clr3D double mutant with those of the corresponding single mutants. Significantly, the double and single mutants display very similar levels of H3K9me2, ;20%-30% of wild-type levels (Fig. 3B).
PMID:24013500	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth [has_severity] medium	To further test whether Seb1 functions in the same pathway as SHREC in promoting H3K9me, we compared H3K9me2 levels at dg and dh repeats of the seb1-1 clr3D double mutant with those of the corresponding single mutants. Significantly, the double and single mutants display very similar levels of H3K9me2, ;20%-30% of wild-type levels (Fig. 3B).
PMID:24013500	FYPO:0002335	normal chromatin silencing	We found that all three mutations are required to produce a silencing defect on 5- FOA medium (Fig. 1B).
PMID:24013500	FYPO:0002335	normal chromatin silencing	We found that all three mutations are required to produce a silencing defect on 5- FOA medium (Fig. 1B).
PMID:24013500	FYPO:0002335	normal chromatin silencing	We found that all three mutations are required to produce a silencing defect on 5- FOA medium (Fig. 1B).
PMID:24013500	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] medium	We found that all three mutations are required to produce a silencing defect on 5- FOA medium (Fig. 1B). However, the mutant with the three amino acid changes (triple mutant) has a milder silencing defect on 5-FOA when compared with the original seb1-1 mutant.
PMID:24013500	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC800.03	We found that every subunit of SHREC tested (Clr3, Clr1, Mit1, and Chp2) is enriched at both dg and dh repeats. However, in the seb1-1 mutant, this enrichment is abolished or strongly reduced (Figs. 5A-D).
PMID:24013500	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC2D10.17	We found that every subunit of SHREC tested (Clr3, Clr1, Mit1, and Chp2) is enriched at both dg and dh repeats. However, in the seb1-1 mutant, this enrichment is abolished or strongly reduced (Figs. 5A-D).
PMID:24013500	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBP35G2.10	We found that every subunit of SHREC tested (Clr3, Clr1, Mit1, and Chp2) is enriched at both dg and dh repeats. However, in the seb1-1 mutant, this enrichment is abolished or strongly reduced (Figs. 5A-D).
PMID:24013500	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPBC16C6.10	We found that every subunit of SHREC tested (Clr3, Clr1, Mit1, and Chp2) is enriched at both dg and dh repeats. However, in the seb1-1 mutant, this enrichment is abolished or strongly reduced (Figs. 5A-D).
PMID:24013500	FYPO:0002837	normal centromeric outer repeat transcript-derived siRNA level	seb1-1 displays normal levels of pericentromeric siRNA accumulation (Fig. 2A)
PMID:24013500	GO:0106222	lncRNA binding [occurs_in] dg_repeat	to assess its association with dg and dh ncRNAs as well as the snoRNA snR30. Seb1 displays a strong association with these ncRNAs but not with the act1+ RNA (Fig. 1A).
PMID:24013500	GO:0030515	snoRNA binding	to assess its association with dg and dh ncRNAs as well as the snoRNA snR30. Seb1 displays a strong association with these ncRNAs but not with the act1+ RNA (Fig. 1A).
PMID:24013500	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth [has_severity] high	while H3K9me2 levels at the dg and dh repeats are modestly reduced in the dcr1-R1R2 single mutant, these levels are virtually eliminated in the dcr1-R1R2 clr3D double mutant, a phenotype strikingly similar to that of the dcr1-R1R2 seb1-1 double mutant (Fig. 3A).
PMID:24013504	FYPO:0003107	progressively shortening telomeres during vegetative growth	(comment: dependent_on(GO:0006312)| not_dependent_on(GO:0007004))
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0005681	spliceosomal complex	(Table 1)
PMID:24014766	GO:0005681	spliceosomal complex	(Table 1)
PMID:24014766	GO:0005681	spliceosomal complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0005682	U5 snRNP	(Table 1)
PMID:24014766	GO:0005682	U5 snRNP	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0005681	spliceosomal complex	(Table 1)
PMID:24014766	GO:0005681	spliceosomal complex	(Table 1)
PMID:24014766	GO:0005681	spliceosomal complex	(Table 1)
PMID:24014766	GO:0005682	U5 snRNP	(Table 1)
PMID:24014766	GO:0005682	U5 snRNP	(Table 1)
PMID:24014766	GO:0005682	U5 snRNP	(Table 1)
PMID:24014766	GO:0000974	Prp19 complex	(Table 1)
PMID:24014766	GO:0005682	U5 snRNP	(Table 1)
PMID:24014766	GO:0005682	U5 snRNP	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0005681	spliceosomal complex	(Table 1)
PMID:24014766	GO:0005681	spliceosomal complex	(Table 1)
PMID:24014766	GO:0005681	spliceosomal complex	(Table 1)
PMID:24014766	GO:0005681	spliceosomal complex	(Table 1)
PMID:24014766	GO:0005681	spliceosomal complex	(Table 1)
PMID:24014766	GO:0005681	spliceosomal complex	(Table 1)
PMID:24014766	GO:0005682	U5 snRNP	(Table 1)
PMID:24014766	GO:0005682	U5 snRNP	(Table 1)
PMID:24014766	GO:0005682	U5 snRNP	(Table 1)
PMID:24014766	GO:0005681	spliceosomal complex	(Table 1)
PMID:24014766	GO:0005682	U5 snRNP	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	GO:0005686	U2 snRNP	(Table 1)
PMID:24014766	FYPO:0003029	decreased mRNA splicing, via spliceosome	(comment: GENERAL SPLICING DEFECT) The ratio of mature to premature signal for the tbp1_a intron was almost identical for the two truncations (2.1 ± 0.2 for cwf10-ΔNTE versus 2.0 ± 0.3 for cwf10 2-23Δ), while the ratio in the wild-type strain was 9.7 ± 1.5 (Fig. 6H). Th
PMID:24014766	GO:0045292	mRNA cis splicing, via spliceosome	1,193 introns (of 5,361 possible introns) whose splicing efficiency was significantly compromised in the mutant.
PMID:24014766	FYPO:0002061	inviable vegetative cell population	Although cwf10 2-135Δ aligns with snu114ΔN (Fig. 1B), the S. pombe allele did not support growth at either 25°C or 32°C when integrated at the endogenous locus (data not shown), while the S. cerevisiae allele is viable at temperatures below 40°C (30).
PMID:24014766	FYPO:0003029	decreased mRNA splicing, via spliceosome	GENERAL SPLICING DEFECT RT-PCR analysis of tbp1_a, an mRNA intron highly sensitive to splicing defects (53), indicated that cwf10-ΔNTE cells grown at 25°C accumulate unspliced transcript (Fig. 2C). retrotransposon silencing by mRNA destabilization
PMID:24014766	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPAC644.12 [has_severity] medium	In the cwf10-ΔNTE background, levels of Brr2 and Prp3 were similar to levels seen in wild-type cells; however, both Cdc5 and Prp1 levels were reduced to 70% and 65%, respectively (Fig. 2I).
PMID:24014766	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC29E6.02	In the cwf10-ΔNTE background, levels of Brr2 and Prp3 were similar to levels seen in wild-type cells; however, both Cdc5 and Prp1 levels were reduced to 70% and 65%, respectively (Fig. 2I).
PMID:24014766	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC9.03c	In the cwf10-ΔNTE background, levels of Brr2 and Prp3 were similar to levels seen in wild-type cells; however, both Cdc5 and Prp1 levels were reduced to 70% and 65%, respectively (Fig. 2I).
PMID:24014766	FYPO:0000835	decreased protein level [has_severity] medium [assayed_protein] PomBase:SPBC6B1.07	In the cwf10-ΔNTE background, levels of Brr2 and Prp3 were similar to levels seen in wild-type cells; however, both Cdc5 and Prp1 levels were reduced to 70% and 65%, respectively (Fig. 2I).
PMID:24014766	FYPO:0001234	slow vegetative cell population growth	The cwf10-ΔNTE strain formed slightly smaller colonies on solid media at all temperatures tested (Fig. 2A) and exhibited slow growth in liquid culture at 25°C and 36°C compared with wild-type cells (Fig. 2B and data not shown)
PMID:24014766	FYPO:0001234	slow vegetative cell population growth	The cwf10-ΔNTE strain formed slightly smaller colonies on solid media at all temperatures tested (Fig. 2A) and exhibited slow growth in liquid culture at 25°C and 36°C compared with wild-type cells (Fig. 2B and data not shown)
PMID:24014766	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPBC215.12	Using quantitative Western blotting, we found that levels of Cwf10 were consistently higher in cwf10-ΔNTE cells than in wild-type cells when quantified against the loading control Cdc2 (Cdk1) (Fig. 2I)
PMID:24021628	GO:0006360	transcription by RNA polymerase I	(comment: CHECK heterologous complemetation of S. c HMO1)
PMID:24039245	GO:0035372	protein localization to microtubule [has_input] PomBase:SPAC664.10	(comment: CHECK in vitro assay with purified proteins)
PMID:24047646	GO:0051286	cell tip [exists_during] mitotic interphase [exists_during] mitotic M phase	(Fig. 1)
PMID:24047646	GO:0032153	cell division site [exists_during] mitotic interphase	(Fig. 1)
PMID:24047646	GO:0032153	cell division site [exists_during] mitotic interphase	(Fig. 1)
PMID:24047646	GO:0071341	medial cortical node	(Fig. 1)
PMID:24047646	GO:0051286	cell tip [exists_during] mitotic G2 phase	(Fig. 1) In early G2 nif1 localisation is monopolar and in late G2 it is bipolar
PMID:24047646	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(Fig. 3, Table 1)
PMID:24047646	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(Fig. 3, Table 1)
PMID:24047646	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(Fig. 3, Table 1)
PMID:24047646	FYPO:0005207	normal mitotic cell cycle regulation upon nitrogen source shift	(Fig. 6) shows nif1delta cells still have G2-M size control
PMID:24047646	FYPO:0005207	normal mitotic cell cycle regulation upon nitrogen source shift	(Fig. 6) shows pom1delta cells still have G2-M size control
PMID:24047646	FYPO:0005206	abnormal mitotic cell cycle regulation upon nitrogen source shift	(Fig. 6) shows wee1-50 cells at restrictive temperature have lost G2-M size control
PMID:24055157	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC244.01c [part_of] negative regulation of septation initiation signaling	(comment: assayed with human CK1)
PMID:24055157	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC244.01c [part_of] negative regulation of septation initiation signaling	(comment: assayed with human CK1, process from phenotypes (dma1 dependent pathway))
PMID:24055157	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC17G8.10c	Although Dma1-GFP still localized to SPBs in sid4(T275A) mutant cells (Figure S1F)
PMID:24055157	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC17G8.10c	Although Dma1-GFP still localized to SPBs in sid4(T275A) mutant cells (Figure S1F)
PMID:24055157	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC17G8.10c	Although Dma1-GFP still localized to SPBs in sid4(T275A) mutant cells (Figure S1F)
PMID:24055157	FYPO:0000912	abolished protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPBC244.01c	Although mutating S278 to alanine abolished Sid4 ubiquitination (Figure 1D)
PMID:24055157	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC3H7.15	Hhp1-GFP localization at SPBs is Sid4 independent (Figure S3E)
PMID:24055157	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC23C4.12	Hhp1-GFP localization at SPBs is Sid4 independent (Figure S3E)
PMID:24055157	GO:0005816	spindle pole body	In cells growing asynchronously, both Hhp1-GFP and Hhp2-GFP localized to the nucleus SPBs, and the cell division site, although Hhp2-GFP was more prominent at the division site compared to Hhp1-GFP (Figure 3B).
PMID:24055157	GO:0005634	nucleus	In cells growing asynchronously, both Hhp1-GFP and Hhp2-GFP localized to the nucleus SPBs, and the cell division site, although Hhp2-GFP was more prominent at the division site compared to Hhp1-GFP (Figure 3B).
PMID:24055157	FYPO:0002060	viable vegetative cell population	In corroboration of these findings, sid4(T275A) mutants were refractory to dma1 overexpression lethality (Figure 2D).
PMID:24055157	MOD:00696	phosphorylated residue [present_during] mitotic spindle checkpoint signaling	In dma1Δ cells, a single slower migrating form of Sid4 was detected, which was collapsed by phosphatase treatment, indicating that Sid4 is phosphorylated in vivo (Figure 1A, lanes 3 and 4). In vivo radiolabeling experiments validated Sid4 as a phospho-protein and revealed that Sid4 is phosphorylated on serines and threonines (Figure S1A-C).
PMID:24055157	GO:0035591	signaling adaptor activity [has_input] PomBase:SPAC17G8.10c [part_of] negative regulation of septation initiation signaling	Thus, phosphorylation on both T275 and S278 is necessary and sufficient to support binding of the Dma1 FHA domain to Sid4 and Sid4 ubiquitination.
PMID:24055157	FYPO:0004537	mitotic spindle assembly checkpoint override	cells bypassed the arrest after 5 hrs (Figure 2C).
PMID:24055157	FYPO:0004537	mitotic spindle assembly checkpoint override	cells bypassed the arrest after 5 hrs (Figure 2C). ......These data indicate that mutating T275 eliminates Dma1-dependent checkpoint signaling.
PMID:24055157	FYPO:0002635	normal protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPBC244.01c	mutating S278 to a glutamate did not affect Sid4 ubiquitination (Figure 1D).
PMID:2406029	FYPO:0002061	inviable vegetative cell population	(Fig. 6A)
PMID:2406029	FYPO:0002061	inviable vegetative cell population	(Fig. 6A)
PMID:2406029	FYPO:0002061	inviable vegetative cell population	(Fig. 6A)
PMID:2406029	FYPO:0001916	elongated mononucleate vegetative cell	(comment: same as cdc2-ww single mutant)
PMID:24074952	MOD:00047	O-phospho-L-threonine	(comment: CHECK residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215)
PMID:24074952	MOD:00047	O-phospho-L-threonine	(comment: CHECK residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215)
PMID:24074952	MOD:00047	O-phospho-L-threonine	(comment: CHECK residue=T235 | residue=T187, annotation_extension=added_by(CDK COMPLEX, CDC2 AND CDC13) | residue=T215)
PMID:24081329	FYPO:0001908	increased pre-mRNA level [assayed_using] PomBase:SPAC1250.05	(comment: evidence: for all FYPO:0001908 = northern blot)
PMID:24095277	GO:0000175	3'-5'-RNA exonuclease activity [has_input] regional_centromere_outer_repeat_transcript	(comment: CHECK has substrates centromere outer repeat transcripts and polyA mRNA. Activated by mg2+)
PMID:24095277	GO:0004535	poly(A)-specific ribonuclease activity [has_input] polyadenylated_mRNA	(comment: CHECK has substrates centromere outer repeat transcripts and polyA mRNA. Activated by mg2+)
PMID:24095277	GO:0016891	RNA endonuclease activity producing 5'-phosphomonoesters, hydrolytic mechanism	(comment: does it produce 5' monoesters?)
PMID:24115772	GO:0005737	cytoplasm [exists_during] mitotic interphase	(comment: CHECK during(GO:0051329))
PMID:24115772	GO:1903475	mitotic actomyosin contractile ring assembly	(comment: dependent on septation initiation signaling (GO:0031028))
PMID:24118096	GO:0110052	toxic metabolite repair	(comment: Trx1's involvement in tis process is to recycle mxr1 for met-O conversion to met )
PMID:24127216	FYPO:0002998	abolished actomyosin contractile ring assembly, clumped medial cortical nodes	(Fig. 1A)
PMID:24127216	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPAC1F5.04c	(Fig. 1B)
PMID:24127216	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPAC1F5.04c	(Fig. 1B)
PMID:24127216	FYPO:0003000	abolished actin filament polymerization	(Fig. 1D-G)
PMID:24127216	GO:0030041	actin filament polymerization	(Fig. 1D-G)
PMID:24127216	FYPO:0003000	abolished actin filament polymerization	(Fig. 1G-G)
PMID:24127216	FYPO:0002998	abolished actomyosin contractile ring assembly, clumped medial cortical nodes	(Fig. 1H)
PMID:24127216	FYPO:0001365	decreased rate of actomyosin contractile ring contraction	(Fig. 2A)
PMID:24127216	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPCC895.05	(Fig. 2A)
PMID:24127216	FYPO:0003014	decreased rate of actomyosin contractile ring disassembly	(Fig. 2A)
PMID:24127216	FYPO:0003001	actin filaments present in increased numbers	(Fig. 3E)
PMID:24127216	FYPO:0003001	actin filaments present in increased numbers	(Fig. 3E)
PMID:24127216	FYPO:0001368	normal actomyosin contractile ring assembly	(Fig. S1a)
PMID:24127216	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic anaphase B	(comment: CHECK exists during anaphase A and anaphase B)
PMID:24127216	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic anaphase A	(comment: CHECK exists during anaphase A and anaphase B)
PMID:24146635	FYPO:0000082	decreased cell population growth at high temperature	(comment: 36 degrees (not brief heat shock))
PMID:24146635	GO:1902716	cell cortex of growing cell tip [exists_during] cellular response to heat [exists_during] monopolar cell growth	(comment: CONDITION prolonged heat exposure (more than ~45 min))
PMID:24146635	GO:1902716	cell cortex of growing cell tip [exists_during] cellular response to heat [exists_during] monopolar cell growth	(comment: CONDITION prolonged heat exposure (more than ~45 min))
PMID:24146635	GO:1902716	cell cortex of growing cell tip [exists_during] cellular response to heat [exists_during] monopolar cell growth	(comment: CONDITION prolonged heat exposure (more than ~45 min))
PMID:24146635	GO:1902716	cell cortex of growing cell tip [exists_during] cellular response to heat [exists_during] monopolar cell growth	(comment: CONDITION prolonged heat exposure (more than ~45 min))
PMID:24146635	GO:1902716	cell cortex of growing cell tip [exists_during] cellular response to heat [exists_during] monopolar cell growth	(comment: CONDITION prolonged heat exposure (more than ~45 min))
PMID:24146635	GO:1902716	cell cortex of growing cell tip [exists_during] cellular response to heat [exists_during] monopolar cell growth	(comment: CONDITION prolonged heat exposure (more than ~45 min))
PMID:24146635	GO:0097575	lateral cell cortex [exists_during] cellular response to heat	(comment: CONDITION shorter duration of heat exposure (up to ~45 min))
PMID:24146635	GO:0097575	lateral cell cortex [exists_during] cellular response to heat	(comment: CONDITION shorter duration of heat exposure (up to ~45 min))
PMID:24146635	GO:0097575	lateral cell cortex [exists_during] cellular response to heat	(comment: CONDITION shorter duration of heat exposure (up to ~45 min))
PMID:24146635	FYPO:0001326	altered RNA level during vegetative growth	(comment: Global gene expression profile (RNAseq) of deletion similar to that of heat-stressed wild type.)
PMID:24146635	FYPO:0001326	altered RNA level during vegetative growth	(comment: Global gene expression profile (RNAseq) of deletion similar to that of heat-stressed wild type.)
PMID:24146635	GO:0005737	cytoplasm [exists_during] cellular response to heat	(comment: punctate; shorter duration of heat exposure (up to ~45 min))
PMID:24146635	GO:1902716	cell cortex of growing cell tip [exists_during] mitotic G2 phase	Both Gef1-3YFP and Scd1-GFP exhibited bipolar localization in majority of late wild type cells
PMID:24146635	GO:1902716	cell cortex of growing cell tip [exists_during] mitotic G2 phase	Both Gef1-3YFP and Scd1-GFP exhibited bipolar localization in majority of late wild type cells
PMID:24147005	FYPO:0006538	spheroid cell during cellular response to pheromone	(Figure 6A)
PMID:24147005	FYPO:0006539	multiseptate cell during cellular response to pheromone	(Figure 7c)
PMID:24155978	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Fig. 5S)
PMID:24155978	FYPO:0002878	increased transcription during glucose starvation [assayed_using] PomBase:SPAC6F12.02 [has_severity] high	(Fig. 5X)
PMID:24155978	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [happens_during] cellular response to glucose starvation	(comment: all independent of Sty1 (effects of H2O2 & NAC unchanged in sty1delta))
PMID:24161933	GO:0005634	nucleus [exists_during] mitotic M phase	(Fig. 1)
PMID:24161933	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_penetrance] 30	(Fig. 2d)
PMID:24161933	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_penetrance] 51	(Fig. 5a)
PMID:24161933	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC3D6.04c [has_severity] high	(comment: 10% of endogenous mad1 level), Fig. S4
PMID:24161933	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPBC20F10.06	(comment: 10% of endogenous mad2 level), Fig. S4
PMID:24161933	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC3D6.04c [has_severity] medium	(comment: 30% of endogenous mad1 level), Fig. S4
PMID:24161933	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC1795.01c [has_severity] medium	(comment: 30% of endogenous mad3 level), Fig. S4
PMID:24161933	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC3D6.04c [has_severity] high	(comment: 300% of endogenous mad1 level), Fig. S4
PMID:24161933	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC821.08c [has_severity] medium	(comment: 40% of endogenous slp1 level), Fig. S4
PMID:24161933	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC3D6.04c [has_severity] high	(comment: 500% of endogenous mad1 level), Fig. S4
PMID:24161933	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC20F10.06 [has_severity] medium	(comment: 65% of endogenous mad2 level), Fig. S4
PMID:24161933	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(comment: CHECK abundances of 40% or lower), cells lacked checkpoint activity.
PMID:24161933	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_penetrance] 88	Even reduction to about 10% of the original Mad1 level, which is hardly visible by fluorescence microscopy (Fig. 2e), did not fully abolish the SAC
PMID:24161933	FYPO:0003762	normal mitotic spindle assembly checkpoint	In cells with 30% Mad1, the checkpoint was markedly impaired in minimal medium, although largely functional in rich medium
PMID:24167631	FYPO:0001178	loss of viability upon nitrogen starvation	(comment: mah: CHECK FYPO:0001178 + PECO:0000240 captures info for requested new term (Term name: loss of viability upon long-term nutrient starvation Definition: A cell population phenotype in which a smaller than normal proportion of the population remains viable when cells in a culture in stationary phase are deprived of nitrogen. Use this term to annotate experiments in which a culture is cultivated in stationary phase under nitrogen-depleted conditions for a long time (more than 1 week), and then the number of cells viable enough to form a colony upon return to conditions supporting vegetative growth is measured and compared to wild type)
PMID:24186976	GO:0005515	protein binding	(Supp Fig. 7)
PMID:24186976	GO:0005515	protein binding	(Supp Fig. 7)
PMID:24223771	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	(Fig. 4B)
PMID:24223771	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	(Fig. 4B)
PMID:24223771	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 4B)
PMID:24223771	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 4B, 6A)
PMID:24223771	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	(Fig. 6)
PMID:24223771	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 6A)
PMID:24223771	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 6B)
PMID:24223771	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 6B)
PMID:24223771	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 6B)
PMID:24223771	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 6C)
PMID:24223771	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 6C)
PMID:24223771	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	(Fig. S3)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24223771	PomGeneEx:0000011	RNA level increased [in_presence_of] 5-fluorouracil	(Table 1)
PMID:24224056	FYPO:0002924	decreased cell population growth on maltose carbon source	The decrease in cell growth on maltose medium is suppressed by neighboring wild-type cells but not by agl1 delta cells, which are defective in maltase secretion.
PMID:24224056	GO:0045944	positive regulation of transcription by RNA polymerase II	in response to carbon source change from glucose to maltose (comment: CHECK regulates agl1)
PMID:24224056	GO:0045944	positive regulation of transcription by RNA polymerase II	in response to carbon source change from glucose to maltose (comment: CHECK regulates agl1)
PMID:24239120	FYPO:0004307	long mitotic spindle during metaphase	(Fig. 1)
PMID:24239120	FYPO:0006259	normal mitotic spindle length during metaphase	(Fig. 1)
PMID:24239120	FYPO:0006259	normal mitotic spindle length during metaphase	(Fig. 1)
PMID:24239120	FYPO:0006259	normal mitotic spindle length during metaphase	(Fig. 1)
PMID:24239120	FYPO:0006259	normal mitotic spindle length during metaphase	(Fig. 1)
PMID:24239120	FYPO:0006259	normal mitotic spindle length during metaphase	(Fig. 1)
PMID:24239120	FYPO:0006259	normal mitotic spindle length during metaphase	(Fig. 1)
PMID:24239120	FYPO:0004395	short bipolar mitotic spindle during metaphase	(Fig. 1)
PMID:24239120	FYPO:0004395	short bipolar mitotic spindle during metaphase [has_severity] low	(Fig. 1)
PMID:24239120	FYPO:0004307	long mitotic spindle during metaphase [has_severity] low	(Fig. 1)
PMID:24239120	FYPO:0004307	long mitotic spindle during metaphase	(Fig. 1)
PMID:24239120	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 2) (comment: CHECK This is a rescue of FYPO:0000324)
PMID:24239120	FYPO:0006259	normal mitotic spindle length during metaphase	(Fig. 2) (comment: CHECK This is a rescue of FYPO:0004395)
PMID:24239120	FYPO:0006259	normal mitotic spindle length during metaphase	(Fig. 2) (comment: CHECK This is a rescue of FYPO:0004395)
PMID:24239120	FYPO:0004101	lagging mitotic chromosomes, with complete sister chromatid separation [has_penetrance] 40	(Fig. 3)
PMID:24239120	FYPO:0001270	complete but unequal mitotic sister chromatid segregation [has_penetrance] 10	(Fig. 3)
PMID:24239120	FYPO:0004101	lagging mitotic chromosomes, with complete sister chromatid separation [has_penetrance] 20	(Fig. 3)
PMID:24239120	FYPO:0001270	complete but unequal mitotic sister chromatid segregation [has_penetrance] 20	(Fig. 3)
PMID:24239120	FYPO:0004101	lagging mitotic chromosomes, with complete sister chromatid separation [has_penetrance] 40	(Fig. 3)
PMID:24239120	FYPO:0007961	transient abrupt spindle length decrease at anaphase onset	(Fig. 4)
PMID:24239120	FYPO:0004101	lagging mitotic chromosomes, with complete sister chromatid separation [has_penetrance] 10	(Fig. 4)
PMID:24239120	FYPO:0007959	increased rate of mitotic spindle elongation during prophase	(Fig. S1)
PMID:24239120	FYPO:0007960	decreased rate of mitotic spindle elongation during prophase	(Fig. S1)
PMID:24239120	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. S1) ((comment: CHECK This is a rescue of FYPO:0000324)
PMID:24239120	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. S1) ((comment: CHECK This is a rescue of FYPO:0000324)
PMID:24239120	FYPO:0004307	long mitotic spindle during metaphase [has_severity] low	(Fig. S1) (comment: CHECK This is a partial rescue of FYPO:0004307)
PMID:24239120	FYPO:0000324	mitotic metaphase/anaphase transition delay [has_severity] high	(Fig. S1) (comment: The authors define it as prolongued prophase-metaphase , but since they use the degradation as cdc13 as a marker it really is anaphase onset that is measured.)
PMID:24239120	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. S1) (comment: The authors define it as prolongued prophase-metaphase , but since they use the degradation as cdc13 as a marker it really is anaphase onset that is measured.)
PMID:24239120	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. S1) (comment: The authors define it as prolongued prophase-metaphase , but since they use the degradation as cdc13 as a marker it really is anaphase onset that is measured.)
PMID:24239120	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. S1) (comment: The authors define it as prolongued prophase-metaphase , but since they use the degradation as cdc13 as a marker it really is anaphase onset that is measured.)
PMID:24240238	FYPO:0002687	normal telomere length during vegetative growth	(comment: Southern blot to detect telomeric sequence)
PMID:24240238	FYPO:0002687	normal telomere length during vegetative growth	(comment: Southern blot to detect telomeric sequence)
PMID:24240238	FYPO:0002687	normal telomere length during vegetative growth	(comment: Southern blot to detect telomeric sequence)
PMID:24240238	FYPO:0002687	normal telomere length during vegetative growth	(comment: Southern blot to detect telomeric sequence)
PMID:24240238	FYPO:0002019	elongated telomeres during vegetative growth	(comment: Southern blot to detect telomeric sequence)
PMID:24240238	FYPO:0002019	elongated telomeres during vegetative growth	(comment: Southern blot to detect telomeric sequence)
PMID:24240238	FYPO:0002687	normal telomere length during vegetative growth	(comment: Southern blot to detect telomeric sequence)
PMID:24240238	FYPO:0004744	normal heterochromatin maintenance involved in chromatin silencing at centromere outer repeat	(comment: experiment introduced otr::ura4+ in either a silenced state (from wild-type cells) or a desilenced state (from clr4delta cells) into poz1delta dcr1delta cells by genetic crosses)
PMID:24240238	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(comment: silencing normal as long as heterochromatin assembly can take place normally)
PMID:24244528	FYPO:0007603	decreased microfilament motor activity	(comment: CHECK atpase activity assay) However, -E1 motors exhibited relatively low activity under either condition (Figure S1). These experiments performed in the absence of actin suggest that defects in -E1 motors are not specific to actin displacement and motility, and probably reflect a general defect in conformation and function.
PMID:24244528	FYPO:0003526	decreased actin filament-based movement	However, most filaments (99%) bound by -E1 were non-motile while most filaments bound by wild-type Myo2p were motile (Movie S2).
PMID:24244528	FYPO:0002276	increased protein degradation [assayed_using] PomBase:SPCC645.05c	However, the lower molecular weight form of -E1 failed to accumulate over time following protease addition (Figure 4C), suggesting an altered conformation more sensitive to proteolysis.
PMID:24244528	GO:0044183	protein folding chaperone [has_input] PomBase:SPCC645.05c	Our data indicates that Rng3p is required to establish active Myo2p motors.The control experiments (where cells were shifted to 37uC at 22hours post-induction) indicated that Rng3p was not essential formaintaining Myo2p motility once an active population of motorshad been synthesized, as previously reported [24]...........Collectively our findings suggest that Rng3p is required to generate an active and stable population of Myo2p motors.
PMID:24247430	GO:0031139	positive regulation of conjugation with cellular fusion	(comment: I think this is real i.e. downregulation of growth to allow differentiation)
PMID:24291789	GO:0032116	SMC loading complex	(Fig. 1a)
PMID:24291789	GO:0032116	SMC loading complex	(Fig. 1a)
PMID:24291789	GO:0003690	double-stranded DNA binding [part_of] mitotic sister chromatid cohesion	(Fig. 1c,d)
PMID:24291789	GO:0003690	double-stranded DNA binding [part_of] mitotic sister chromatid cohesion	(Fig. 1c,d)
PMID:24291789	GO:0007064	mitotic sister chromatid cohesion	(Fig. 2E,F; Fig. 3a,b)
PMID:24291789	GO:0003690	double-stranded DNA binding	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0003690	double-stranded DNA binding	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0003690	double-stranded DNA binding	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0030892	mitotic cohesin complex	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0030892	mitotic cohesin complex	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0030892	mitotic cohesin complex	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0030892	mitotic cohesin complex	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0003690	double-stranded DNA binding	(Fig. 2a,b; Extended Data Fig. 2a)
PMID:24291789	GO:0007064	mitotic sister chromatid cohesion	(Fig. 2e) Fig. 2f) Fig. 3a,b).
PMID:24291789	GO:0007064	mitotic sister chromatid cohesion	(Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently.
PMID:24291789	GO:0007064	mitotic sister chromatid cohesion	(Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently.
PMID:24291789	GO:0007064	mitotic sister chromatid cohesion	(Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently.
PMID:24291789	GO:0007064	mitotic sister chromatid cohesion	(Fig. 3b), suggesting that cohesin in principle achieves topological loading onto DNA independently of a cohesin loader, albeit inefficiently.
PMID:24291789	GO:0005515	protein binding [part_of] mitotic sister chromatid cohesion	(Fig. 4b)
PMID:24297439	GO:0005515	protein binding	(comment: Two hybrid interaction using Gpa2K270E activated protein with Sck1.)
PMID:24297439	GO:0005515	protein binding	(comment: Two hybrid interaction using Gpa2K270E activated protein with Sck1.)
PMID:24297439	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC23H3.13c [part_of] negative regulation of adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway	(comment: it's a bit indirect, but they show this via consensus site mutations....I think it is borderline ok)
PMID:24297439	FYPO:0006822	viable small vegetative cell with normal cell growth rate	Effect of sck1 deletion to increase cell length in git3 delete cells depends on Gpa2 activity. Otherwise, Sck1 acts in parallel with Pka1 to increase cell length.
PMID:24313451	GO:0101005	deubiquitinase activity	(comment: assayed using cell extract, overexpressed protien and synthetic UB conjugate)
PMID:24314397	GO:0030378	serine racemase activity	(comment: inhibited by α-(hydroxymethyl)serine CHEBI:28187)
PMID:24316795	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC57A10.02 [part_of] negative regulation of G2/M transition of mitotic cell cycle	(comment: CHECK Phosphorylates cdr2 at S755 in vitro)
PMID:24316795	FYPO:0001018	abolished NETO	(comment: CONDITION high concentration (1 uM) 3MB-PP1)
PMID:24316795	FYPO:0000339	mislocalized septum during vegetative growth	(comment: CONDITION high concentration (1 uM) 3MB-PP1)
PMID:24316795	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(comment: CONDITION high concentration (1 uM) 3MB-PP1)
PMID:24316795	FYPO:0002556	decreased protein localization to medial cortex, with protein distributed in cell cortex near non-growing end, during vegetative growth [assayed_using] PomBase:SPAC57A10.02	(comment: CONDITION high concentration (1 uM) 3MB-PP1)
PMID:24316795	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(comment: CONDITION low concentration (<0.25 uM) 3MB-PP1)
PMID:24316795	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(comment: CONDITION low concentration (<0.25 uM) 3MB-PP1)
PMID:24316795	FYPO:0003150	decreased NETO	(comment: CONDITION low concentration (<0.25 uM) 3MB-PP1)
PMID:24316795	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAC57A10.02	(comment: CONDITION low concentration (<0.25 uM) 3MB-PP1)
PMID:24316795	GO:0031569	mitotic G2 cell size control checkpoint signaling	(comment: Cdr2 phosphorylated by Pom1 at the CTD negatively regulates its activity)
PMID:24316795	GO:0010971	positive regulation of G2/M transition of mitotic cell cycle	(comment: Negatively regulated by Pom1 via phosphorylation of C-ter)
PMID:24316795	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1-as1 protein may preferentially localize to non-growing end.)
PMID:24316795	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(comment: high overexpression)
PMID:24316795	FYPO:0001124	normal vegetative cell size	(comment: moderate overexpression)
PMID:24316795	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] low	(comment: same as cdr2-S755A-758A alone)
PMID:24316795	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] low	(comment: same as cdr2-S755A-758A alone)
PMID:24327658	GO:0005515	protein binding	(comment: Binds specifically to active Sre1 transcription factor and not full-length precursor)
PMID:24327658	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC1861.01c	(comment: CHECK in vitro kinase assay using recombinant Sre1 aa 1-440)
PMID:24327658	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC19C2.09	(comment: CHECK in vitro kinase assay using recombinant Sre1 aa 1-440)
PMID:24327658	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC23C4.12	(comment: CHECK in vitro kinase assay using recombinant Sre1 aa 1-440)
PMID:24327658	FYPO:0003251	decreased transcription from SRE promoter	(comment: Ok as a single mutant despite sre1-N mutant?)
PMID:24327658	GO:0000122	negative regulation of transcription by RNA polymerase II	(comment: accelerates degradation of active Sre1 transcription factor)
PMID:24327658	GO:0010895	negative regulation of ergosterol biosynthetic process	(comment: hhp2 deletion increases steady-state ergosterol)
PMID:24344203	FYPO:0001382	decreased protein kinase activity [assayed_using] PomBase:SPCC24B10.07	(comment: isp7+ overexpression decreases Gad8's kinase activity towards substrate Fkh2)
PMID:24344203	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAPB1E7.12	(comment: same as isp7+ overexpression alone)
PMID:24344203	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAPB1E7.12	(comment: same as isp7+ overexpression alone)
PMID:24475199	FYPO:0002834	decreased chromatin silencing at centromere	(comment: Expression level up 2 times)
PMID:24475199	FYPO:0002834	decreased chromatin silencing at centromere	(comment: Expression level up 2 times)
PMID:24475199	FYPO:0002834	decreased chromatin silencing at centromere	(comment: Expression level up 2 times)
PMID:24475199	FYPO:0002834	decreased chromatin silencing at centromere	(comment: Expression level up 2 times)
PMID:24475199	FYPO:0002834	decreased chromatin silencing at centromere	(comment: Expression level up 2.5 times)
PMID:24475199	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: Expression level up 22 times)
PMID:24475199	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: Expression level up 23 times)
PMID:24475199	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: Expression level up 25 times)
PMID:24475199	FYPO:0002834	decreased chromatin silencing at centromere	(comment: Expression level up 3 times)
PMID:24475199	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: Expression level up 31 times)
PMID:24475199	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: Expression level up 35 times)
PMID:24475199	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: Expression level up 38 times)
PMID:24475199	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: Expression level up 43 times)
PMID:24475199	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: Expression level up 8 times.)
PMID:24477934	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig 1F)
PMID:24477934	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig 2D and E) (comment: (mad1 localized did not rescue)
PMID:24477934	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c	(Fig. 1 C,D)
PMID:24477934	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c [has_severity] high	(Fig. 1A, C-D)
PMID:24477934	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c	(Fig. 1A, C-E)
PMID:24477934	FYPO:0007383	abolished protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC20F10.06	(Fig. 1A, C-E)
PMID:24477934	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c [has_severity] high	(Fig. 1A, C-E)
PMID:24477934	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1F)
PMID:24477934	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1F)
PMID:24477934	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1F)
PMID:24477934	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c	(Fig. 1I-L)
PMID:24477934	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1I-L)
PMID:24477934	FYPO:0005042	normal protein localization to kinetochore [assayed_using] PomBase:SPCC1322.12c	(Fig. 1I-L)
PMID:24477934	FYPO:0005042	normal protein localization to kinetochore [assayed_using] PomBase:SPBC3D6.04c	(Fig. 3B,C)
PMID:24477934	FYPO:0005042	normal protein localization to kinetochore [assayed_using] PomBase:SPBC3D6.04c	(Fig. 3B,C)
PMID:24477934	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] high	(Fig. 3D)
PMID:24477934	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] high	(Fig. 3D)
PMID:24477934	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC3D6.04c [assayed_using] PomBase:SPBC20F10.06	(Fig. 3F)
PMID:24477934	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC20F10.06 [assayed_using] PomBase:SPBC3D6.04c	(Fig. S1A and D)
PMID:24477934	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPCC1322.12c	(Fig. S1B)
PMID:24477934	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPAC23H3.08c	(Fig. S1B)
PMID:24477934	FYPO:0005042	normal protein localization to kinetochore [assayed_using] PomBase:SPAC23H3.08c	(Fig. S1I)
PMID:24477934	FYPO:0005042	normal protein localization to kinetochore [assayed_using] PomBase:SPCC1795.01c	(Fig. S1I)
PMID:24477934	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC20F10.06	(Fig. S1I)
PMID:24477934	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c	(Fig. S2C,D,E)
PMID:24477934	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c	(Fig. S2C,D,E)
PMID:24477934	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c [has_severity] medium	(Fig. S2C,D,E)
PMID:24477934	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC3D6.04c	(Fig. S2C,D,E)
PMID:24477934	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. S2F)
PMID:24477934	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_penetrance] 10	(Fig. S2F)
PMID:24477934	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. S2F)
PMID:24477934	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_penetrance] high	(Fig. S2F)
PMID:24477934	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c	(Fig. S4A)
PMID:24477934	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPBC3D6.04c	(Fig. S4A)
PMID:24477934	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. S4a)
PMID:24477934	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. S4a)
PMID:24477934	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. S4a)
PMID:24477934	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. S4a)
PMID:24477934	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. S4a)
PMID:24477934	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. S4a)
PMID:24477934	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC3D6.04c	(Fig. S4a)
PMID:24477934	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC3D6.04c	(Fig. S4a)
PMID:24477934	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC3D6.04c	(Fig. S4a)
PMID:24477934	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC3D6.04c	(Fig. S4a)
PMID:24477934	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC3D6.04c	(Fig. S4a)
PMID:24477934	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC3D6.04c	(Fig. S4a)
PMID:24477934	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC3D6.04c	(Fig. S4a)
PMID:24477934	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	(Fig. S4a)
PMID:24477934	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	(Fig. S4a)
PMID:24477934	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	(Fig. S4a)
PMID:24477934	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC20F10.06 [assayed_using] PomBase:SPBC3D6.04c	(Figure 1H)
PMID:24477934	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC20F10.06 [assayed_using] PomBase:SPBC3D6.04c [has_severity] high	(Figure 1H)
PMID:24477934	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC20F10.06 [assayed_using] PomBase:SPBC3D6.04c [has_severity] medium	(Figure 1H)
PMID:24477934	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Figure 2B)
PMID:24477934	GO:0140483	kinetochore adaptor activity [has_input] PomBase:SPBC20F10.06 [part_of] mitotic spindle assembly checkpoint signaling	A complex between the checkpoint proteins Mad1 and Mad2 provides a platform for Mad2:Mad2 dimerization at unattached kinetochores, which enables Mad2 to delay anaphase. Here, we show that mutations in Bub1 and within the Mad1 C-terminal domain impair the kinetochore localization of Mad1:Mad2 and abrogate checkpoint activity. Artificial kinetochore recruitment of Mad1 in these mutants co-recruits Mad2; however, the checkpoint remains non-functional. We identify specific mutations within the C-terminal head of Mad1 that impair checkpoint activity without affecting the kinetochore localization of Bub1, Mad1 or Mad2. Hence, Mad1 potentially in conjunction with Bub1 has a crucial role in checkpoint signalling in addition to presenting Mad2.
PMID:24478458	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC645.07 [part_of] mitotic intra-S DNA damage checkpoint signaling [occurs_in] nucleus	(comment: phosphorylates rgf1 during HU response, to maintain of protein lcoation in nucleus)
PMID:24493644	FYPO:0000781	decreased transcription during vegetative growth [assayed_using] PomBase:SPBP4G3.02	(Fig. 5)
PMID:24498240	FYPO:0001382	decreased protein kinase activity [assayed_substrate] PomBase:SPBC119.08 [has_severity] high	(Figure 3A) indicates that deletion of rho2+ gene alleviated the increased Pmk1 basal phosphorylation present in pck1D cells.
PMID:24498240	FYPO:0001382	decreased protein kinase activity [assayed_substrate] PomBase:SPBC119.08 [has_severity] medium	(Figure 3A) indicates that deletion of rho2+ gene alleviated the increased Pmk1 basal phosphorylation present in pck1D cells.
PMID:24498240	FYPO:0002700	increased protein kinase activity [assayed_substrate] PomBase:SPBC119.08 [has_severity] high	(Figure 3A) indicates that deletion of rho2+ gene alleviated the increased Pmk1 basal phosphorylation present in pck1D cells.
PMID:24498240	FYPO:0001382	decreased protein kinase activity [assayed_substrate] PomBase:SPBC119.08 [has_severity] low	(comment: CHECK in response to oxidative stress) As shown in Figure 2B, Pmk1 activation in rho2D cells subjected to oxidative stress was not affected by simultaneous expression of the rho1-596 hypoactive allele.
PMID:24498240	FYPO:0001382	decreased protein kinase activity [assayed_substrate] PomBase:SPBC119.08 [has_severity] low	(comment: CHECK in response to oxidative stress) On the contrary, MAPK activation triggered by oxidative (hydrogen peroxide) and cell wall (Caspofungin) stresses is only partially dependent on this GTPase (Figure 2B and C)
PMID:24498240	FYPO:0005969	resistance to magnesium chloride [assayed_substrate] PomBase:SPBC119.08 [has_severity] high	(comment: note in Figure 3B the robust growth of rho1-596 rho2D pck1D cells in medium supplemented with 0.2 M MgCl2 as compared to rho2D pck1D cells).
PMID:24498240	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPBC119.08	Also, Pmk1 hyperactivation triggered by rho2+ overexpression is fully attenuated in mutants lacking Pck2 (Figure 1A).
PMID:24498240	FYPO:0002700	increased protein kinase activity [assayed_substrate] PomBase:SPBC119.08	Also, Pmk1 hyperactivation triggered by rho2+ overexpression is fully attenuated in mutants lacking Pck2 (Figure 1A).
PMID:24498240	GO:0043539	protein serine/threonine kinase activator activity [has_input] PomBase:SPBC12D12.04c [part_of] positive regulation of cell integrity MAPK cascade	As a whole, these results sustain that Rho1 GTPase is a true positive regulator of the cell integrity pathway which operates during vegetative growth in an alternative fashion to Rho2 and using Pck2 as a main target.
PMID:24498240	FYPO:0002061	inviable vegetative cell population [has_severity] low	As expected, both wild type and rho1- 596 cells were VIC negative under any condition (Figure 1D).
PMID:24498240	FYPO:0005969	resistance to magnesium chloride [has_severity] low	As seen in Figure 1E, rho2D cells showed a partial VIC phenotype in medium supplemented with 0.2 M MgCl2 and became VIC negative in the presence of 0.3 M MgCl2.
PMID:24498240	FYPO:0005969	resistance to magnesium chloride [has_severity] low	As seen in Figure 1E, rho2D cells showed a partial VIC phenotype in medium supplemented with 0.2 M MgCl2 and became VIC negative in the presence of 0.3 M MgCl2.
PMID:24498240	FYPO:0001382	decreased protein kinase activity [assayed_substrate] PomBase:SPBC119.08 [has_severity] medium	However, a careful examination of these experiments revealed that Pmk1 basal phosphorylation in rho1-596 rho2D cells was actually lower than in rho2D cells, and this difference was statistically significant (P,0.04; Figure 1C). On the contrary, basal Pmk1 activity was nearly identical in pck2D and rho1-596 pck2D cells (Figure 1D), strongly suggesting that enhanced Pmk1 activation in rho1-596 cells is transmitted to the MAPK cascade mainly through Pck2.
PMID:24498240	FYPO:0001382	decreased protein kinase activity [assayed_substrate] PomBase:SPBC119.08 [has_severity] high	However, in comparison to either control or rho2D and rho1-596 single mutant cells, MAPK activation was severely compromised in cells from the rho2D rho1-596 double mutant treated with Caspofungin (Figure 2C).
PMID:24498240	FYPO:0005969	resistance to magnesium chloride [has_severity] medium	Importantly, the VIC phenotype in rho1-596 rho2D double mutant was markedly enhanced as compared to that shown by rho2D cells (Figure 1E), which is in good agreement with basal Pmk1 phosphorylation data (Figure 1C).
PMID:24498240	GO:1903139	positive regulation of cell integrity MAPK cascade	In this study we show for the first time that Rho1 and Pck1 are true activators of this signalling cascade in addition to Rho2 and Pck2 under specific environmental contexts
PMID:24498240	GO:1903139	positive regulation of cell integrity MAPK cascade [happens_during] cellular response to stress	In this study we show for the first time that Rho1 and Pck1 are true activators of this signalling cascade in addition to Rho2 and Pck2 under specific environmental contexts
PMID:24498240	FYPO:0008263	abolished protein kinase activity in response to osmotic stress [assayed_substrate] PomBase:SPBC119.08 [has_severity] high	Pmk1 activation induced by hypo- and hyper-osmotic stress totally depends upon the signaling mediated by Rho2 (Figure 2A)
PMID:24498240	GO:1903139	positive regulation of cell integrity MAPK cascade	Previous work demonstrated that Rho2 GTPase, one of the six Rho GTPases found in S. pombe proteome (Rho1 to Rho5, and Cdc42) which controls cell polarity and cell wall biosynthesis, is a positive regulator operating upstream of the CIP [13,14]
PMID:24498240	FYPO:0002700	increased protein kinase activity [assayed_substrate] PomBase:SPBC119.08 [has_severity] high	Rho1 GTPase might modulate the activity Pmk1 by acting upstream of Pck2 because it has been described that overexpression of wild type or a constitutively active allele of rho1+ (G15V mutant) induced a marked hyperactivation of Pmk1 (Figure 1B
PMID:24498240	GO:0043539	protein serine/threonine kinase activator activity [has_input] PomBase:SPBC12D12.04c [part_of] positive regulation of cell integrity MAPK cascade	Taken as a whole, these results support that Pck1 might act as a Rho1 target during signal transmission to the CIP, although its role within this pathway seems restricted to specific situations.
PMID:24514900	FYPO:0000413	abolished cell fusion during mating [has_penetrance] high	(comment: CHECK high penetrance)
PMID:24514900	FYPO:0004184	sensitive to papuamide B during vegetative growth [has_severity] low	(comment: CHECK low expressivity)
PMID:24514900	GO:0000755	cytogamy	(comment: Required for phosphatidyl serine reorganization at the inner leaflet of plasma membrane during cell fusion)
PMID:24521463	FYPO:0002060	viable vegetative cell population	(comment: decreased cell pop is not a child of this term)
PMID:24554432	GO:2000114	regulation of establishment of cell polarity	(comment: CHECK necessary to trigger cell shape change upon Tea4 targeting to cell sides by fusion with Cdr2)
PMID:24554432	GO:2000784	positive regulation of establishment of cell polarity regulating cell shape	(comment: CHECK necessary to trigger cell shape change upon Tea4 targeting to cell sides by fusion with Cdr2)
PMID:24554432	GO:2000114	regulation of establishment of cell polarity	(comment: CHECK sufficient to trigger cell shape change when targeted to cell sides by fusion with Cdr2)
PMID:24554432	GO:2000784	positive regulation of establishment of cell polarity regulating cell shape	(comment: CHECK sufficient to trigger cell shape change when targeted to cell sides by fusion with Cdr2)
PMID:24554432	GO:0030010	establishment of cell polarity	(comment: CHECK sufficient to trigger cell shape change when targeted to cell sides by fusion with Cdr2; tea1/pom1 double mutant phenotype shows that Tea4 role is independent of Pom1)
PMID:24569997	FYPO:0006170	decreased RNA level during cellular response to copper ion starvation during meiotic cell cycle [assayed_using] PomBase:SPAC1142.05 [has_penetrance] complete	(Fig. 1)
PMID:24569997	FYPO:0006147	decreased level of early meiotic gene mRNA during cellular response to copper ion starvation during meiotic cell cycle [assayed_using] PomBase:SPBC23G7.16	(Fig. 1)
PMID:24569997	FYPO:0006170	decreased RNA level during cellular response to copper ion starvation during meiotic cell cycle [assayed_using] PomBase:SPCC1393.10	(Fig. 1)
PMID:24569997	FYPO:0006170	decreased RNA level during cellular response to copper ion starvation during meiotic cell cycle [assayed_using] PomBase:SPBC23G7.16	(Fig. 2)
PMID:24569997	FYPO:0003282	decreased superoxide dismutase activity [assayed_enzyme] PomBase:SPAC821.10c	(Figure 5B)
PMID:24569997	FYPO:0003282	decreased superoxide dismutase activity [assayed_enzyme] PomBase:SPAC821.10c	(Figure 5B)
PMID:24569997	FYPO:0006145	decreased RNA level during cellular response to copper ion during meiotic cell cycle [assayed_using] PomBase:SPBC23G7.16	(comment: CHECK *******during copper excess******) fig2
PMID:24569997	FYPO:0006145	decreased RNA level during cellular response to copper ion during meiotic cell cycle [assayed_using] PomBase:SPBC23G7.16	(comment: CHECK *******during copper excess******) fig2
PMID:24569997	GO:0005628	prospore membrane [exists_during] meiotic metaphase II	(comment: Observed at this location during spore maturation by indirect immunofluorescence)
PMID:24583014	FYPO:0007401	abnormal protein localization to kinetochore during mitotic anaphase [assayed_using] PomBase:SPBC3D6.04c	(Fig. 1A)
PMID:24583014	FYPO:0007401	abnormal protein localization to kinetochore during mitotic anaphase [assayed_using] PomBase:SPBC20F10.06	(Fig. 1A)
PMID:24583014	FYPO:0007401	abnormal protein localization to kinetochore during mitotic anaphase [assayed_using] PomBase:SPAC23H3.08c	(Fig. 1A)
PMID:24583014	FYPO:0007401	abnormal protein localization to kinetochore during mitotic anaphase [assayed_using] PomBase:SPCC320.13c	(Fig. 1A) indicating that CDK1 activity remained high
PMID:24583014	FYPO:0007401	abnormal protein localization to kinetochore during mitotic anaphase [assayed_using] PomBase:SPCC1795.01c	(Fig. 1B)
PMID:24583014	FYPO:0005410	normal protein degradation during mitosis [assayed_using] PomBase:SPBC14C8.01c	(Fig. 1D, 1E)
PMID:24583014	FYPO:0007403	increased duration of anaphase-promoting complex presence	(Fig. 2A) (comment: complex seen here in anaphase although it normally forms in prometaphase and disassembles before anaphase)
PMID:24583014	FYPO:0005684	increased duration of mitotic prometaphase	(Fig. 2B, 2C)
PMID:24583014	FYPO:0006646	normal duration of mitotic prometaphase	(Fig. 2B, 2C)
PMID:24583014	FYPO:0007404	decreased protein degradation during mitotic anaphase [assayed_using] PomBase:SPBC14C8.01c	(Fig. 3A, 3B, 3C) securin abnormally stabilized during anaphase
PMID:24583014	FYPO:0000274	increased duration of mitotic M phase	(Fig. S1B, S1C)
PMID:24583014	FYPO:0004301	normal mitotic sister chromatid separation	(Figure S1B)
PMID:24637836	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(comment: CHECK weak sensitivity)
PMID:24637836	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(comment: CHECK weak sensitivity)
PMID:24637836	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(comment: CHECK weak sensitivity)
PMID:24637836	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(comment: CHECK weak sensitivity)
PMID:24637836	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(comment: CHECK weak sensitivity)
PMID:24637836	GO:0005737	cytoplasm	(comment: Fluorescence microscopy of Sec13 tagged with GFP at either its N-terminal or C-terminal end.)
PMID:24637836	FYPO:0001355	decreased vegetative cell population growth	Our strains expressing GFP-tagged nucleoporins were all viable, but four of them (spNup45-GFP, spNup184-GFP, GFP-spRae1, and spNup189n-GFP) showed growth deficiencies
PMID:24652833	GO:0009262	deoxyribonucleotide metabolic process	(comment: it affects suc22 binding to cdc22. There is no evidence thta it is involved in catabolism and I dont think I can make a MF from it.)
PMID:24652833	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process [happens_during] cellular response to hydroxyurea [has_input] PomBase:SPAC3F10.19	(comment: no MF possible)
PMID:24662054	GO:0140750	nucleosome array spacer activity	(comment: binds both DNA and histone. Not sure if the H3 preference is an artefact of in vitro system)
PMID:24662054	GO:0031491	nucleosome binding [occurs_in] heterochromatin	(comment: binds both DNA and histone. Not sure if the H3 preference is an artefact of in vitro system)
PMID:24663817	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1D)
PMID:24663817	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 1D)
PMID:24663817	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1D)
PMID:24663817	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1D, Fig. 2B)
PMID:24663817	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 1D, Fig. 2B)
PMID:24663817	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 1D, Fig. 2B)
PMID:24663817	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1D,2B)
PMID:24663817	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1D,2B)
PMID:24663817	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 1D,2B)
PMID:24663817	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 3)
PMID:24663817	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 3)
PMID:24663817	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3D)
PMID:24663817	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 3D)
PMID:24663817	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 3D)
PMID:24663817	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3D)
PMID:24663817	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPCC1259.13 [has_severity] medium	(Fig. 3a, b)
PMID:24663817	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPCC1259.13	(Fig. 3a,b)
PMID:24663817	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPCC18B5.11c	(Fig. 3a,b) (comment: CHECK cds1-T11)
PMID:24663817	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC23C4.18c [assayed_using] PomBase:SPAC664.07c	(Fig. 5A and B)
PMID:24663817	MOD:00696	phosphorylated residue	(comment: CHECK affected by rad4)
PMID:24663817	GO:0035591	signaling adaptor activity [has_input] PomBase:SPAC23C4.18c	(comment: CHECK phosphorylated rad9)
PMID:24663817	FYPO:0002898	abolished protein phosphorylation during cellular response to DNA damage [assayed_using] PomBase:SPCC1259.13	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)
PMID:24663817	FYPO:0002898	abolished protein phosphorylation during cellular response to DNA damage [assayed_using] PomBase:SPCC1259.13	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)
PMID:24663817	FYPO:0002897	decreased protein phosphorylation during cellular response to DNA damage [assayed_using] PomBase:SPCC1259.13 [has_severity] low	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)
PMID:24663817	FYPO:0002897	decreased protein phosphorylation during cellular response to DNA damage [assayed_using] PomBase:SPCC1259.13 [has_severity] low	C13Y and K56R mutations completely eliminated the phosphorylation of Chk1 in MMS-treated cells (Fig. 3A)The slight decrease in Cds1 phosphorylation may be caused indirectly by a minor defect in DNA replication
PMID:24663817	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC342.05 [assayed_using] PomBase:SPAC23C4.18c	C13Y-K56R mutation abolished the interaction with Crb2 (Fig. 5C), not Rad9 (Fig. 5A and B).
PMID:24663817	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC23C4.18c [assayed_using] PomBase:SPAC664.07c	C13Y-K56R mutation abolished the interaction with Crb2 (Fig. 5C), not Rad9 (Fig. 5A and B).
PMID:24663817	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC23C4.18c [assayed_using] PomBase:SPAC664.07c	Consistent with the previous report [58], the interaction between Rad9 and Rad4 was dependent on Rad9 phosphorylation because the phosphorylation site mutant Rad9-T412A could not pull-down Rad4 (Fig. 5A, first lane on the left) and the interaction between Rad9 and Rad4 was sensitive to l-phosphatase treatment (Fig. S5A).
PMID:24663817	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC23C4.18c [assayed_using] PomBase:SPAC664.07c	E368K mutation abolished the binding to Rad9 as previously reported [47] (Fig. 5A and B)
PMID:24663817	FYPO:0000725	resistance to methyl methanesulfonate	Interestingly, the DC mutant with the deletion of the whole C-terminus between amino acid 498 and 648 was resistant to HU and MMS almost like the wild type cells (Fig. 1D and 2B). The only difference we could readily find for the DC mutant was that the protein level was higher than in the wild type cells (Fig. 2C), suggesting that the C-terminus may not contain a robust AAD (see below).
PMID:24663817	GO:0035591	signaling adaptor activity [has_input] PomBase:SPCC1259.13 [part_of] mitotic G2 DNA damage checkpoint signaling	The C13Y and K56R mutations abolished the scaffolding function of Rad4 required for the activation of Chk1 but not Rad3
PMID:24663817	FYPO:0002061	inviable vegetative cell population	We found that combinations of the previously reported E368K mutation [47] with K56R or F303S were lethal suggesting a defect in DNA replication.
PMID:24663817	FYPO:0002061	inviable vegetative cell population	We found that combinations of the previously reported E368K mutation [47] with K56R or F303S were lethal suggesting a defect in DNA replication.
PMID:24710126	FYPO:0003410	increased spatial extent of CENP-A containing chromatin assembly	(comment: CHECK convert to double mutant (cnp1 overexpression))
PMID:24710126	FYPO:0005071	increased chromatin silencing at centromere	(comment: central core)
PMID:24710126	FYPO:0005071	increased chromatin silencing at centromere	(comment: central core)
PMID:24713849	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC29A10.14	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC29A10.14	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC2G2.09c	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC29A10.02	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC32H8.11	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC32H8.11	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC2G2.09c	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC29A10.14	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC29A10.02	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC32H8.11	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC2G2.09c	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC29A10.02	(comment: CHECK mei4 ssm4 crs1 rec8 spo5)
PMID:24713849	GO:1990477	MTREC complex	(comment: Observed in cells undergoing vegetative growth)
PMID:24713849	GO:1990477	MTREC complex	(comment: Observed in cells undergoing vegetative growth)
PMID:24713849	GO:1990477	MTREC complex	(comment: Observed in cells undergoing vegetative growth)
PMID:24713849	GO:1990477	MTREC complex	(comment: Observed in cells undergoing vegetative growth)
PMID:24713849	GO:1990477	MTREC complex	(comment: Observed in cells undergoing vegetative growth)
PMID:24713849	GO:1990477	MTREC complex	(comment: Observed in cells undergoing vegetative growth)
PMID:24741065	GO:0004674	protein serine/threonine kinase activity [directly_negatively_regulates] PomBase:SPAC27D7.03c [part_of] negative regulation of cell cycle switching, mitotic to meiotic cell cycle	(comment: CHECK phosphorylation of mei2 targets it for degradation via the proteasome)
PMID:24741065	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process [has_input] PomBase:SPAC27D7.03c	(comment: tor2 phosphorylates mei2. Phosphorylated mei2 is ubiquitylated which targets it for degradation via the proteasome.)
PMID:24755092	GO:0010494	cytoplasmic stress granule	(comment: Exo2-GFP localizes to stress granules)
PMID:24755092	GO:0010494	cytoplasmic stress granule	(comment: SPAC12G12.09-mCherry localizes to stress granules)
PMID:24758716	GO:0019172	glyoxalase III activity	(comment: major)
PMID:24758716	GO:0019172	glyoxalase III activity	(comment: major)
PMID:24758716	GO:0019172	glyoxalase III activity	(comment: minor Hsp3106 has a lower in vitro glyoxalase III activity than Hsp3101 and Hsp3102)
PMID:24768994	GO:0005635	nuclear envelope	(Figure 2A)
PMID:24768994	GO:0005515	protein binding	(Figure 2B)
PMID:24768994	GO:0005515	protein binding	(Figure 2B)
PMID:24768994	GO:0006606	protein import into nucleus [has_input] PomBase:SPCC1739.13	(Figure 2C)
PMID:24768994	GO:0005634	nucleus	(Figure 3)
PMID:24768994	GO:0005737	cytoplasm	(Figure 3)
PMID:24768994	FYPO:0000684	decreased cell population growth on glycerol carbon source	(Figure 5)
PMID:24768994	FYPO:0000684	decreased cell population growth on glycerol carbon source	(Figure 5)
PMID:24768994	FYPO:0001407	decreased cell population growth on glucose carbon source	(Figure 5)
PMID:24774534	FYPO:0002060	viable vegetative cell population	(Fig. 6)
PMID:24774534	FYPO:0002060	viable vegetative cell population	(Fig. 6)
PMID:24774534	FYPO:0002060	viable vegetative cell population	(Fig. 6)
PMID:24774534	FYPO:0002060	viable vegetative cell population	(Fig. 6)
PMID:24774534	FYPO:0002060	viable vegetative cell population	(Fig. 6)
PMID:24774534	FYPO:0002060	viable vegetative cell population	(Fig. 6)
PMID:24774534	FYPO:0002060	viable vegetative cell population	(Fig. 6)
PMID:24774534	FYPO:0002060	viable vegetative cell population	(Fig. 6)
PMID:24774534	FYPO:0002061	inviable vegetative cell population	(Fig. 6)
PMID:24774534	FYPO:0002060	viable vegetative cell population	(Fig. 6)
PMID:24774534	FYPO:0002061	inviable vegetative cell population	(Fig. 6)
PMID:24787148	GO:0004857	enzyme inhibitor activity [has_input] PomBase:SPAC19B12.10	(comment: ubiquitin monmomer inhibits sst2)
PMID:24790093	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC890.02c [assayed_protein] PomBase:SPCC962.03c	(comment: Yeast two hybrid)
PMID:24790095	GO:0110085	mitotic actomyosin contractile ring	(comment: CHECK exists_during( metaphase? anaphase A????))
PMID:24790095	GO:0110085	mitotic actomyosin contractile ring	(comment: CHECK exists_during( metaphase? anaphase A????))
PMID:24790095	GO:0071341	medial cortical node [exists_during] mitotic interphase	(comment: CHECK mitotic interphase)
PMID:24806815	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPACUNK4.14 [occurs_in] site of double-strand break	(chromatin localisation requires phosphorylated histone H2A.)
PMID:24806815	GO:0005515	protein binding [has_input] hta1/Phos(S121)	Mdb1 binds to Hta1 phosphorylated on Ser-129. (comment: CHECK PR:000027566 = H2A phosphorylated on S129)
PMID:24806815	GO:0035861	site of double-strand break	This localisation requires phosphorylated histone H2A.
PMID:24815688	FYPO:0003743	decreased cell population growth during glucose starvation	"(comment: CHECK transferres from term suggestion to allow approval decreased growth under low-glucose conditions Definition: ""decreased growth under low-glucose conditions"" is an ""decreased cell population growth"" that occurs specifically on media supplied with a lower concentration of glucose than regular media. ditto all the others)"
PMID:24818994	GO:0016929	deSUMOylase activity [has_input] PomBase:SPAC17C9.03 [has_input] PomBase:SPBC365.06 [part_of] regulation of cytoplasmic translation	(Figure 1A)
PMID:24818994	GO:0070139	SUMO-specific endopeptidase activity	(Figure 1A)
PMID:24818994	GO:0070139	SUMO-specific endopeptidase activity [has_input] PomBase:SPBC365.06 [part_of] protein processing	(Figure 1A)
PMID:24818994	GO:0016929	deSUMOylase activity	(Figure 1A)
PMID:24818994	FYPO:0002061	inviable vegetative cell population	(Figure 1D)
PMID:24818994	FYPO:0000088	sensitive to hydroxyurea	(Figure 1D)
PMID:24818994	FYPO:0000104	sensitive to cycloheximide	(Figure 1D)
PMID:24818994	MOD:01149	sumoylated lysine [removed_by] PomBase:SPAC17A5.07c	(Figure 5A)
PMID:24818994	GO:0005634	nucleus	(Figures 3 and 6)
PMID:24818994	GO:0005737	cytoplasm	(Figures 3 and 6)
PMID:24818994	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to salt stress	(Figures 3 and 6)
PMID:24818994	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to salt stress	(Figures 3 and 6)
PMID:24818994	GO:0005737	cytoplasm	(comment: minor)
PMID:24831008	FYPO:0006830	normal RNA level during cellular response to replete zinc [assayed_using] PomBase:SPBC16D10.06	(Fig. 1)
PMID:24831008	FYPO:0006830	normal RNA level during cellular response to replete zinc [assayed_using] PomBase:SPBC16D10.06	(Fig. 1)
PMID:24831008	FYPO:0007050	increased RNA level during stress response to zinc ion [assayed_using] PomBase:SPAC5H10.06c	(Fig. 2)
PMID:24831008	FYPO:0007050	increased RNA level during stress response to zinc ion [assayed_using] PomBase:SPAC5H10.06c	(Fig. 2)
PMID:24831008	FYPO:0007050	increased RNA level during stress response to zinc ion [assayed_using] PomBase:SPAC5H10.06c	(Fig. 2)
PMID:24831008	FYPO:0005291	increased RNA level during cellular response to zinc ion [assayed_using] PomBase:SPAC5H10.06c	(Fig. 2)
PMID:24831008	FYPO:0007050	increased RNA level during stress response to zinc ion [assayed_using] PomBase:SPAC5H10.06c	(Fig. 2)
PMID:24831008	FYPO:0000658	decreased DNA binding [has_severity] high [assayed_using] PomBase:SPAC25B8.19c	(Fig. 4)
PMID:24831008	FYPO:0000658	decreased DNA binding [has_severity] high [assayed_using] PomBase:SPAC25B8.19c	(Fig. 4)
PMID:24831008	FYPO:0005018	decreased double-stranded DNA binding [assayed_using] PomBase:SPAC25B8.19c [has_severity] high	(Fig. 4g)
PMID:24831008	FYPO:0007049	decreased RNA level during stress response to zinc ion [assayed_using] PomBase:SPAC5H10.06c	(Figure 7) the goal of the experiments in this figure is to map the minimal region of loz1 that is required for zinc-responsiveness by generating gene fusion with MtfA, a transcription factor from Aspergillus nidulans that contains a double zinc finger domain with high similarity to Loz1 from S. pombe, but contains no other similarity. When expressed in S. pombe this gene fusion was regulated by zinc, suggesting that the region necessary for zinc responsiveness in S. pombe, maps to the zinc finger domains
PMID:24831008	FYPO:0006830	normal RNA level during cellular response to replete zinc [assayed_using] PomBase:SPAC5H10.06c	(Figure 7) the goal of the experiments in this figure is to map the minimal region of loz1 that is required for zinc-responsiveness by generating gene fusion with MtfA, a transcription factor from Aspergillus nidulans that contains a double zinc finger domain with high similarity to Loz1 from S. pombe, but contains no other similarity. When expressed in S. pombe this gene fusion was regulated by zinc, suggesting that the region necessary for zinc responsiveness in S. pombe, maps to the zinc finger domains and an upstream accessory domain
PMID:24831008	FYPO:0006830	normal RNA level during cellular response to replete zinc [assayed_using] PomBase:SPBC16D10.06	(Figure 7) the goal of the experiments in this figure is to map the minimal region of loz1 that is required for zinc-responsiveness by generating gene fusion with MtfA, a transcription factor from Aspergillus nidulans that contains a double zinc finger domain with high similarity to Loz1 from S. pombe, but contains no other similarity. When expressed in S. pombe this gene fusion was regulated by zinc, suggesting that the region necessary for zinc responsiveness in S. pombe, maps to the zinc finger domains and an upstream accessory domain
PMID:24831008	FYPO:0007050	increased RNA level during stress response to zinc ion [assayed_using] PomBase:SPBC16D10.06 [has_severity] medium	RNA transcript expression is increased during the stress response to zinc ions, but the increase is less than the transcript levels seen with full de-repression
PMID:24831008	FYPO:0007050	increased RNA level during stress response to zinc ion [assayed_using] PomBase:SPBC16D10.06 [has_severity] medium	RNA transcript expression is increased during the stress response to zinc ions, but the increase is less than the transcript levels seen with full de-repression
PMID:24831008	FYPO:0007050	increased RNA level during stress response to zinc ion [assayed_using] PomBase:SPBC16D10.06 [has_severity] medium	RNA transcript expression is increased during the stress response to zinc ions, but the increase is less than the transcript levels seen with full de-repression
PMID:24838944	GO:0035974	meiotic spindle pole body [exists_during] meiotic anaphase II	(Fig. 1A,1 B)
PMID:24838944	GO:0035974	meiotic spindle pole body [exists_during] meiotic prophase II	(Fig. 1C)
PMID:24838944	GO:0035974	meiotic spindle pole body [exists_during] meiotic metaphase II	(Fig. 1C)
PMID:24838944	GO:0035974	meiotic spindle pole body [exists_during] meiosis I cell cycle phase	(Fig. 1C)
PMID:24838944	GO:0035974	meiotic spindle pole body [exists_during] meiotic prophase II	(Fig. 1D)
PMID:24838944	GO:0035974	meiotic spindle pole body [exists_during] meiotic metaphase II	(Fig. 1D)
PMID:24838944	GO:0035974	meiotic spindle pole body [exists_during] meiosis I cell cycle phase	(Fig. 1D)
PMID:24838944	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_protein] PomBase:SPBC21.06c	(Fig. 2A)
PMID:24838944	FYPO:0007256	premature protein localization to meiotic spindle pole body during prophase I [assayed_protein] PomBase:SPBC21.06c	(Fig. 2A)
PMID:24838944	FYPO:0003542	abolished protein localization to meiotic spindle pole body [assayed_protein] PomBase:SPAC6F6.08c	(Fig. 2C)
PMID:24838944	FYPO:0003542	abolished protein localization to meiotic spindle pole body [assayed_protein] PomBase:SPAC222.10c	(Fig. 2C)
PMID:24838944	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_protein] PomBase:SPAC9G1.09	(Fig. 2E)
PMID:24838944	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_protein] PomBase:SPBC21.06c	(Fig. 2E)
PMID:24838944	FYPO:0006055	normal protein localization to meiotic spindle pole body during meiosis II [assayed_protein] PomBase:SPBC21.06c	(Fig. 2F)
PMID:24838944	FYPO:0007246	abolished protein localization to meiotic spindle pole body during anaphase II [assayed_protein] PomBase:SPAC9G1.09	(Fig. 2F)
PMID:24838944	FYPO:0007246	abolished protein localization to meiotic spindle pole body during anaphase II [assayed_protein] PomBase:SPAC9G1.09	(Fig. 2G)
PMID:24838944	PomGeneEx:0000019	protein level decreased [during] meiosis II cell cycle phase	(Fig. 3A)
PMID:24838944	FYPO:0004634	normal protein level during meiosis [assayed_protein] PomBase:SPAC222.10c	(Fig. 3B)
PMID:24838944	PomGeneEx:0000019	protein level decreased [during] meiosis II cell cycle phase	(Fig. 4A)
PMID:24838944	PomGeneEx:0000019	protein level decreased [during] meiosis II cell cycle phase	(Fig. 4B)
PMID:24838944	PomGeneEx:0000019	protein level decreased [during] meiosis II cell cycle phase	(Fig. 4C)
PMID:24838944	FYPO:0008403	normal protein degradation during meiosis [assayed_protein] PomBase:SPCC1739.11c	(Fig. 4D)
PMID:24838944	FYPO:0008403	normal protein degradation during meiosis [assayed_protein] PomBase:SPBC21.06c	(Fig. 4E)
PMID:24838944	FYPO:0008403	normal protein degradation during meiosis [assayed_protein] PomBase:SPBC21.06c	(Fig. 5C)
PMID:24838944	FYPO:0008403	normal protein degradation during meiosis [assayed_protein] PomBase:SPBC21.06c	(Fig. 5D)
PMID:24838944	FYPO:0006531	delayed onset of protein degradation during meiosis [assayed_protein] PomBase:SPBC21.06c	(Fig. 6A)
PMID:24838944	FYPO:0006531	delayed onset of protein degradation during meiosis [assayed_protein] PomBase:SPCC1739.11c	(Fig. 6B)
PMID:24838944	FYPO:0006531	delayed onset of protein degradation during meiosis [assayed_protein] PomBase:SPBC244.01c	(Fig. 6C)
PMID:24838944	PomGeneEx:0000019	protein level decreased [during] meiosis II cell cycle phase	(Fig. 7A)
PMID:24838944	FYPO:0008404	abolished protein degradation during meiosis [assayed_protein] PomBase:SPBC582.06c	(Fig. 7B)
PMID:24838944	FYPO:0008404	abolished protein degradation during meiosis [assayed_protein] PomBase:SPBC582.06c	(Fig. 7C)
PMID:24838944	GO:0035974	meiotic spindle pole body [exists_during] meiotic anaphase II	(Fig. S1D)
PMID:24847916	FYPO:0003928	altered double-strand break repair junction in presence of persistent double-strand breaks	(comment: The phenotype is assessed by the high-throughput sequencing.)
PMID:24876389	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC11G7.02 [assayed_using] PomBase:SPBC18H10.20c	(comment: CHECK have guessed at deleted residues)
PMID:24876389	FYPO:0002127	increased protein localization to plasma membrane during vegetative growth [assayed_using] PomBase:SPAC869.11	(comment: CHECK internalization abolished)
PMID:24876389	FYPO:0002127	increased protein localization to plasma membrane during vegetative growth [assayed_using] PomBase:SPAC869.11	(comment: CHECK internalization abolished)
PMID:24876389	FYPO:0002127	increased protein localization to plasma membrane during vegetative growth [assayed_using] PomBase:SPAC869.11	(comment: CHECK internalization abolished)
PMID:24876389	FYPO:0002127	increased protein localization to plasma membrane during vegetative growth [assayed_using] PomBase:SPAC869.11	(comment: CHECK internalization abolished)
PMID:24876389	MOD:01148	ubiquitinylated lysine [added_by] PomBase:SPBC18H10.20c	(comment: ubiquitinated probably at K263)
PMID:24876389	GO:1990756	ubiquitin-like ligase-substrate adaptor activity [has_input] PomBase:SPAC869.11 [part_of] clathrin-dependent endocytosis	We also show that Arn1 regulates endocytosis of the Cat1 amino acid transporter.
PMID:24920274	FYPO:0007496	abolished protein localization to nuclear exosome focus at sme2 locus [assayed_using] PomBase:SPCC736.12c	(Figure 3)
PMID:24920274	FYPO:0007496	abolished protein localization to nuclear exosome focus at sme2 locus [assayed_using] PomBase:SPAC1006.03c	(Figure 3)
PMID:24920274	FYPO:0007496	abolished protein localization to nuclear exosome focus at sme2 locus [assayed_using] PomBase:SPCC736.12c	(Figure 3)
PMID:24920274	FYPO:0007496	abolished protein localization to nuclear exosome focus at sme2 locus [assayed_using] PomBase:SPAC1006.03c	(Figure 3)
PMID:24920274	FYPO:0001996	RNA absent from cell during nitrogen starvation [assayed_using] PomBase:SPBC32H8.11	(Figure S1)
PMID:24920274	FYPO:0001152	decreased RNA level during nitrogen starvation [assayed_using] PomBase:SPAC27D7.13c	(Figure S1)
PMID:24920274	FYPO:0003161	RNA absent from cell during vegetative growth [assayed_using] PomBase:SPBC32H8.11	(Figure S1)
PMID:24920274	FYPO:0003161	RNA absent from cell during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	(Figure S1)
PMID:24920274	FYPO:0001996	RNA absent from cell during nitrogen starvation [assayed_using] PomBase:SPBC32H8.11	(Figure S1)
PMID:24920274	FYPO:0001996	RNA absent from cell during nitrogen starvation [assayed_using] PomBase:SPAC27D7.13c	(Figure S1)
PMID:24920274	FYPO:0000583	abolished sporulation	(Figure S1)
PMID:24920274	FYPO:0000583	abolished sporulation	(Figure S1)
PMID:24920274	FYPO:0000584	decreased sporulation frequency [has_severity] low	(Figure S1)
PMID:24920274	FYPO:0000584	decreased sporulation frequency [has_severity] high	(Figure S1)
PMID:24920274	FYPO:0001152	decreased RNA level during nitrogen starvation [assayed_using] PomBase:SPBC32H8.11	(Figure S1)
PMID:24920274	FYPO:0001996	RNA absent from cell during nitrogen starvation [assayed_using] PomBase:SPAC27D7.13c	(Figure S1)
PMID:24920274	FYPO:0003161	RNA absent from cell during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	(Figure S1)
PMID:24920274	FYPO:0003161	RNA absent from cell during vegetative growth [assayed_using] PomBase:SPBC32H8.11	(Figure S1)
PMID:24920274	FYPO:0003059	normal RNA localization to chromatin [assayed_using] PomBase:SPNCRNA.103	(comment: CHECK abnormal RNA localization to chromatin)
PMID:24920274	GO:1990251	nuclear exosome focus [coincident_with] PomBase:SPNCRNA.103	(comment: at sme2 locus -one of several exosome foci in nucleus during vegetative growth)
PMID:24920274	GO:1990251	nuclear exosome focus [coincident_with] PomBase:SPNCRNA.103	(comment: at sme2 locus -one of several exosome foci in nucleus during vegetative growth)
PMID:24920823	FYPO:0002970	increased protein localization to mitotic spindle pole body during metaphase [assayed_using] PomBase:SPAC222.10c	(comment: CHECK Cdk1-dependent, Cdk1 non-phosphorylatable Byr4 localizes to one or both SPBs in >90% of metaphase cells)
PMID:24920823	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09	(comment: CHECK S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1))
PMID:24920823	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09	(comment: CHECK S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1))
PMID:24920823	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09	(comment: CHECK S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1))
PMID:24920823	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09	(comment: CHECK S248, T412, T502, S533: added by cyclin-dependent kinase (Cdk1))
PMID:24920823	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC11B10.09	(comment: CHECK S326, T429, S499: added by cyclin-dependent kinase (Cdk1))
PMID:24920823	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC11B10.09	(comment: CHECK S326, T429, S499: added by cyclin-dependent kinase (Cdk1))
PMID:24920823	GO:0031031	positive regulation of septation initiation signaling	(comment: CHECK Term name: supports establishment of SIN asymmetry Definition: characterized by asymmetric localization of the SIN initiator kinase Cdc7 in anaphase)
PMID:24920823	FYPO:0001876	decreased asymmetric protein localization, with protein localized to both mitotic spindle pole bodies during anaphase [assayed_using] PomBase:SPBC21.06c	(comment: CHECK affecting Cdc7)
PMID:24920823	GO:0044732	mitotic spindle pole body [exists_during] mitotic anaphase B	(comment: CHECK anaphase B)
PMID:24920823	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] low	(comment: CHECK low penetrance)
PMID:24920823	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] medium	(comment: CHECK medium penetrance)
PMID:24920823	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPAC222.10c [part_of] positive regulation of septation initiation signaling	(comment: CHECK targets Byr4 at S248A, S326A, T412A, T429A, S499A, T502A, S533A, results in Byr4 removal from metaphase spindle pole bodies)
PMID:24920823	FYPO:0004562	binucleate aseptate vegetative cell	(comment: results from collapse of actomyosin contractile ring)
PMID:24925530	FYPO:0003107	progressively shortening telomeres during vegetative growth	"""comment: starts with longer telomeres than wild type, which then shorten"""
PMID:24928430	FYPO:0009000	decreased rate of cytoplasmic microtubule polymerization during mitotic interphase	(Fig. 1)
PMID:24928430	FYPO:0008008	increased duration of cytoplasmic microtubule growth events during mitotic interphase	(Fig. 1)
PMID:24928430	FYPO:0000899	normal microtubule cytoskeleton organization during vegetative growth	(Fig. 2)
PMID:24928430	FYPO:0006103	short interphase microtubules	(Fig. 3)
PMID:24928430	FYPO:0009001	decreased duration of cytoplasmic microtubule growth events during mitotic interphase	(Fig. 3)
PMID:24928430	FYPO:0009001	decreased duration of cytoplasmic microtubule growth events during mitotic interphase	(Fig. 3) (comment: CHECK minor rescue)
PMID:24928430	FYPO:0006103	short interphase microtubules	(Fig. 3) (comment: CHECK minor rescue)
PMID:24928430	FYPO:0009001	decreased duration of cytoplasmic microtubule growth events during mitotic interphase	(Fig. 3) (comment: CHECK minor rescue)
PMID:24928430	FYPO:0006103	short interphase microtubules	(Fig. 3) (comment: CHECK minor rescue)
PMID:24928430	FYPO:0006103	short interphase microtubules	(Fig. 4) (comment: CHECK minor rescue)
PMID:24928430	FYPO:0006103	short interphase microtubules	(Fig. 4) (comment: CHECK minor rescue)
PMID:24928510	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK Phosphorylation assayed in vitro)
PMID:24928510	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK Phosphorylation assayed in vitro)
PMID:24928510	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK Phosphorylation assayed in vitro)
PMID:24928510	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC24B10.07	(comment: CHECK Phosphorylation assayed in vitro)
PMID:24928510	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK Phosphorylation assayed in vitro)
PMID:24928510	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK Phosphorylation assayed in vitro)
PMID:24928510	FYPO:0001838	decreased protein phosphorylation during vegetative growth [has_severity] medium [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK Protein phosphorylation assayed in vitro)
PMID:24928510	FYPO:0001838	decreased protein phosphorylation during vegetative growth [has_severity] medium [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK Protein phosphorylation assayed in vitro)
PMID:24928510	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	FYPO:0005197	increased protein phosphorylation during glucose starvation [has_severity] high [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	FYPO:0005197	increased protein phosphorylation during glucose starvation [has_severity] high [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	FYPO:0005197	increased protein phosphorylation during glucose starvation [has_severity] low [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24928510	FYPO:0005197	increased protein phosphorylation during glucose starvation [has_severity] medium [assayed_using] PomBase:SPBC16G5.15c	(comment: CHECK protein phosphorylation assayed in vitro)
PMID:24936793	GO:0071218	cellular response to misfolded protein	(comment: also inferrable (IC) from GO:0051787)
PMID:24939935	FYPO:0002061	inviable vegetative cell population	(Fig. 1D)
PMID:24939935	FYPO:0002061	inviable vegetative cell population	(Fig. 1D)
PMID:24939935	FYPO:0002061	inviable vegetative cell population	(Fig. 1D)
PMID:24939935	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 1D)
PMID:24939935	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1D)
PMID:24939935	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1D)
PMID:24939935	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1D)
PMID:24939935	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1D)
PMID:24939935	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1D)
PMID:24939935	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1D)
PMID:24939935	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 1D)
PMID:24939935	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 1D)
PMID:24939935	FYPO:0008181	decreased RNA polymerase II CTD Ser5-P binding	(Fig. 1G)
PMID:24939935	FYPO:0008181	decreased RNA polymerase II CTD Ser5-P binding	(Fig. 1G)
PMID:24939935	FYPO:0008181	decreased RNA polymerase II CTD Ser5-P binding	(Fig. 1G)
PMID:24939935	FYPO:0008181	decreased RNA polymerase II CTD Ser5-P binding	(Fig. 1G)
PMID:24939935	FYPO:0008181	decreased RNA polymerase II CTD Ser5-P binding	(Fig. 1G)
PMID:24939935	FYPO:0008181	decreased RNA polymerase II CTD Ser5-P binding	(Fig. 1G)
PMID:24939935	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 4D)
PMID:24939935	FYPO:0002061	inviable vegetative cell population	(Fig. 4D)
PMID:24939935	FYPO:0002061	inviable vegetative cell population	(Fig. 4D)
PMID:24939935	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 4D)
PMID:24939935	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 4D)
PMID:24939935	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 4D)
PMID:24939935	FYPO:0002061	inviable vegetative cell population	(Fig. 4D)
PMID:24939935	FYPO:0008182	decreased Spt5-CTD binding	(Fig. 4E)
PMID:24939935	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPBC2F12.08c	We report crystal structures of Pce1 bound to Pol2 CTD and Spt5 CTD ligands. Key findings are that (1) the CTDs of Pol2 and Spt5 interact with completely distinct sites on the NTase and OB domains of the fission yeast GTase, respectively, and (2) whereas the interface of GTase with the Pol2 CTD is dependent on Ser5 phosphorylation, GTase binding to Spt5 CTD is antagonized by Thr1 phosphorylation.
PMID:24939935	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPBC2F12.08c	We report crystal structures of Pce1 bound to Pol2 CTD and Spt5 CTD ligands. Key findings are that (1) the CTDs of Pol2 and Spt5 interact with completely distinct sites on the NTase and OB domains of the fission yeast GTase, respectively, and (2) whereas the interface of GTase with the Pol2 CTD is dependent on Ser5 phosphorylation, GTase binding to Spt5 CTD is antagonized by Thr1 phosphorylation.
PMID:24945319	GO:0005847	mRNA cleavage and polyadenylation specificity factor complex	(comment: I don't really know how to do this: I would like to say that SPAC824.04, Ppn1 and Dis2 are part of a protein module associated with the CPF. We have named this module the DPS module. Lack of this module does not affect the formation of the core CPF (all other CPF sub-units remain associated as a complex). )
PMID:24945319	GO:0005847	mRNA cleavage and polyadenylation specificity factor complex	(comment: I don't really know how to do this: I would like to say that SPAC824.04, Ppn1 and Dis2 are part of a protein module associated with the CPF. We have named this module the DPS module. Lack of this module does not affect the formation of the core CPF (all other CPF sub-units remain associated as a complex). )
PMID:24945319	GO:0005847	mRNA cleavage and polyadenylation specificity factor complex	(comment: I don't really know how to do this: I would like to say that SPAC824.04, Ppn1 and Dis2 are part of a protein module associated with the CPF. We have named this module the DPS module. Lack of this module does not affect the formation of the core CPF (all other CPF sub-units remain associated as a complex). )
PMID:24947517	FYPO:0001315	normal vegetative cell morphology	(Fig. 1B)
PMID:24947517	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:24947517	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:24947517	FYPO:0000650	increased septation index	(Fig. 1C)
PMID:24947517	FYPO:0000673	normal septum assembly	(Fig. 1D)
PMID:24947517	FYPO:0005628	decreased rate of cell separation after cytokinesis	(Fig. 1D) (comment: decreased rate of cell separation)
PMID:24947517	FYPO:0000164	abnormal cell separation after cytokinesis [has_severity] high	(Fig. 1E)
PMID:24947517	FYPO:0000164	abnormal cell separation after cytokinesis [has_severity] high	(Fig. 1E)
PMID:24947517	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] high	(Fig. 1F)
PMID:24947517	FYPO:0003369	sensitive to sodium fluoride [has_severity] high	(Fig. 1F)
PMID:24947517	FYPO:0003369	sensitive to sodium fluoride [has_severity] low	(Fig. 1F)
PMID:24947517	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] low	(Fig. 1F)
PMID:24947517	GO:0036391	medial cortex septin ring [exists_during] mitotic telophase	(Fig. 3A)
PMID:24947517	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPBC29A3.17	(Fig. 3F)
PMID:24947517	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPBC29A3.17	(Fig. 3F)
PMID:24947517	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPBC29A3.17	(Fig. 3F)
PMID:24947517	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPAC23C4.08	(Fig. 4A)
PMID:24947517	FYPO:0004085	decreased vegetative cell growth [has_severity] low	(Fig. 4A)
PMID:24947517	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPAC110.03	(Fig. 4A)
PMID:24947517	FYPO:0004085	decreased vegetative cell growth [has_severity] low	(Fig. 4A)
PMID:24947517	FYPO:0004085	decreased vegetative cell growth [has_penetrance] medium	(Fig. 4A)
PMID:24947517	FYPO:0004085	decreased vegetative cell growth [has_severity] low	(Fig. 4A)
PMID:24947517	GO:0005515	protein binding	(Fig. 4C, 4D, 4E)
PMID:24947517	FYPO:0003337	increased protein localization to septum [assayed_using] PomBase:SPAC23C4.08	(Fig. 5A)
PMID:24947517	GO:0032153	cell division site	(Fig. 5A)
PMID:24947517	GO:0005886	plasma membrane	(Fig. 5A)
PMID:24947517	FYPO:0002674	normal protein localization to plasma membrane [assayed_using] PomBase:SPCC825.03c	(Fig. 5B)
PMID:24947517	FYPO:0002061	inviable vegetative cell population	(Fig. 6A)
PMID:24947517	FYPO:0002061	inviable vegetative cell population	(Fig. 6A)
PMID:24947517	FYPO:0002061	inviable vegetative cell population	(Fig. 6B)
PMID:24947517	FYPO:0000223	elongated multiseptate vegetative cell [has_severity] low	(Fig. 6B)
PMID:24947517	FYPO:0001972	abnormal cell separation after cytokinesis resulting in septated cell [has_severity] high	(Fig. 6B)
PMID:24947517	FYPO:0002060	viable vegetative cell population	(Fig. 6B)
PMID:24947517	FYPO:0001972	abnormal cell separation after cytokinesis resulting in septated cell [has_severity] low	(Fig. 6B)
PMID:24947517	FYPO:0002060	viable vegetative cell population	(Fig. 6B)
PMID:24947517	FYPO:0002061	inviable vegetative cell population	(Fig. 6C)
PMID:24947517	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 6C, 6D)
PMID:24947517	FYPO:0004256	viable lemon-shaped cell [has_severity] high	(Fig. 6D)
PMID:24947517	GO:0016192	vesicle-mediated transport	(Fig. 6D)
PMID:24947517	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPBC29A3.17	(Figure 3C)
PMID:24947517	FYPO:0002555	abolished protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPBC29A3.17	(Figure 3C)
PMID:24947517	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAPYUG7.03c	Data not shown
PMID:24947517	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAC4F10.11	Data not shown
PMID:24947517	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC970.09	Data not shown
PMID:24947517	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC1235.10c	Data not shown
PMID:24954111	FYPO:0006363	monopolar spindle during meiosis I [has_penetrance] 36	(Fig. 1)
PMID:24954111	FYPO:0006364	spindle microtubules detached from spindle pole body during meiosis I [has_penetrance] 27	(Fig. 1)
PMID:24954111	FYPO:0004569	normal spindle during meiosis I [has_penetrance] 38	(Fig. 1) In wild-type cells, monopolar or nonpolar spindles were not observed (Fig. 4C).
PMID:24954111	FYPO:0000678	unequal homologous chromosome segregation	(Fig. 6A,B) even in the presence of the bipolar spindle
PMID:24954111	FYPO:0006366	abolished meiotic telomere clustering	(comment: never observed 37/37)
PMID:24954111	FYPO:0006366	abolished meiotic telomere clustering	(comment: never observed 54/54)
PMID:24954111	FYPO:0005652	abnormal spindle morphology during meiosis I [has_penetrance] 10	bipolar spindle defects caused by the loss of telomere clustering were rescued by stopping nuclear movement.
PMID:24954111	FYPO:0005652	abnormal spindle morphology during meiosis I [has_penetrance] 10	bipolar/spindle defects caused by the loss of telomere clustering were rescued by stopping nuclear movement.
PMID:24954111	FYPO:0004159	abnormal homologous chromosome segregation [has_penetrance] 50	spindle defects caused by the loss of telomere clustering were rescued by stopping nuclear movement.
PMID:24957674	GO:0000785	chromatin [coincident_with] terminator	(comment: CHECK SO:0000141 = The sequence of DNA located either at the end of the transcript that causes RNA polymerase to terminate transcription. SO:0000186 - LTR SO:0000101 - transposable element)
PMID:24957674	GO:0000785	chromatin [coincident_with] transposable_element	(comment: CHECK SO:0000141 = The sequence of DNA located either at the end of the transcript that causes RNA polymerase to terminate transcription. SO:0000186 - LTR SO:0000101 - transposable element)
PMID:24957674	GO:0000785	chromatin [coincident_with] LTR_retrotransposon	(comment: CHECK SO:0000141 = The sequence of DNA located either at the end of the transcript that causes RNA polymerase to terminate transcription. SO:0000186 - LTR SO:0000101 - transposable element)
PMID:24957674	GO:0006325	chromatin organization	xap5 genetically interacts with pht1 to repress antisense transcripts. In the ∆xap5∆pht1 double mutants the level of antisense transcription is exacerbated as observed using RNA-seq. Selected loci also showed antisense RNA production in histone deacetylase (HDACs) gene mutants.
PMID:24963130	FYPO:0002636	delayed onset of mitotic spindle elongation	(comment: 2 sub populations spindle elongation delayed during anaphase. A spindle elongation delayed during anaphase B)
PMID:24972934	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] 3	(Fig. 1)
PMID:24972934	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] 20	(Fig. 1)
PMID:24972934	FYPO:0008401	premature cell separation after cytokinesis	(Fig. 3)
PMID:24972934	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] 1	(Fig. 4B)
PMID:24972934	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] 2	(Fig. 4B)
PMID:24972934	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] 2	(Fig. 4B)
PMID:24972934	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] 2	(Fig. 4B)
PMID:24972934	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] 1	(Fig. 4B)
PMID:24972934	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] 2	(Fig. 4B)
PMID:24972934	FYPO:0001223	binucleate multiseptate vegetative cell [has_penetrance] 12	(Fig. 4D)
PMID:24972934	FYPO:0001223	binucleate multiseptate vegetative cell [has_penetrance] 20	(Fig. 4D)
PMID:24972934	FYPO:0001223	binucleate multiseptate vegetative cell [has_penetrance] 20	(Fig. 4D)
PMID:24972934	FYPO:0001223	binucleate multiseptate vegetative cell [has_penetrance] 35	(Fig. 4D)
PMID:24972934	FYPO:0001223	binucleate multiseptate vegetative cell [has_penetrance] 12	(Fig. 4D)
PMID:24972934	GO:0004674	protein serine/threonine kinase activity [part_of] negative regulation of mitotic cytokinesis [has_input] PomBase:SPBC17F3.02	(Fig. 5)
PMID:24972934	FYPO:0001122	elongated vegetative cell [has_severity] low	(Fig. 5C)
PMID:24972934	FYPO:0001122	elongated vegetative cell [has_severity] high	(Fig. 5C)
PMID:24972934	FYPO:0001122	elongated vegetative cell [has_severity] high	(Fig. 5C)
PMID:24972934	FYPO:0003440	cell lysis during cytokinesis	(Fig. 5D and E)
PMID:24972934	FYPO:0003440	cell lysis during cytokinesis	(Fig. 5D and E)
PMID:24972934	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC887.09c [part_of] negative regulation of mitotic cytokinesis	Here we identified an additional mechanism of MOR inhibition by the SIN through Sid2 phosphorylation of Sog2.
PMID:24982431	FYPO:0002558	normal protein localization to medial cortex during vegetative growth [assayed_protein] PomBase:SPAC57A10.02	A C-terminal region composed of the Cdr2 basic motif and KA-1 domain (residues 591–747), hereafter called Cdr2-Cter, was sufficient for cortex binding (Fig. 2 A)
PMID:24982431	GO:0110115	Cdr2 medial cortical node complex	Figure 1C
PMID:24982431	FYPO:0010037	decreased protein localization to medial cortex with protein mislocalized to cell tip during vegetative growth [assayed_protein] PomBase:SPAC57A10.02	Finally, we introduced the mutations of hydrophobic residues of the 4–5 loop in full-length Cdr2 (Cdr2FF*). This led to fewer medial nodes and a small pool of the mutant protein at the cell tips (Figs. 3 E, 4 A, and S2 A).
PMID:24982431	FYPO:0003716	abolished protein localization to lateral cortical node, with protein mislocalized to nucleus [assayed_protein] PomBase:SPAC57A10.02 [has_penetrance] high	In combination with mutation of the five basic residues close to the 3–4 loop, this led to complete detachment of Cdr2 from the cortex. Thus, the basic motif cooperates with Cdr2 KA-1 to promote Cdr2 anchoring at the cortex.
PMID:24982431	FYPO:0004735	abolished protein localization to medial cortical node, with protein mislocalized to cytoplasm [assayed_protein] PomBase:SPAC57A10.02	Mutagenesis of these basic residues to noncharged polar amino acids (N or Q) showed that these residues have an important role in targeting Cdr2 to the cortex (Fig. 1 C).
PMID:24982431	FYPO:0003716	abolished protein localization to lateral cortical node, with protein mislocalized to nucleus [assayed_protein] PomBase:SPAC57A10.02	Mutations in any of the three  helices completely detached Cdr2 from the cortex (Fig. S1 A) and induced Cdr2 relocalization to the nucleus, indicating that the lipid-binding function of this domain may be conserved.
PMID:24982431	FYPO:0003716	abolished protein localization to lateral cortical node, with protein mislocalized to nucleus [assayed_protein] PomBase:SPAC57A10.02	Mutations in any of the three  helices completely detached Cdr2 from the cortex (Fig. S1 A) and induced Cdr2 relocalization to the nucleus, indicating that the lipid-binding function of this domain may be conserved.
PMID:24982431	FYPO:0003716	abolished protein localization to lateral cortical node, with protein mislocalized to nucleus [assayed_protein] PomBase:SPAC57A10.02	Mutations in any of the three  helices completely detached Cdr2 from the cortex (Fig. S1 A) and induced Cdr2 relocalization to the nucleus, indicating that the lipid-binding function of this domain may be conserved.
PMID:24982431	FYPO:0003716	abolished protein localization to lateral cortical node, with protein mislocalized to nucleus [assayed_protein] PomBase:SPAC57A10.02 [has_penetrance] high	Mutations of two other basic residues from helix 1 (R624 and R628) did not affect Cdr2 association with the cortex on their own but led to a complete detachment when combined with mutations of the aforementioned five basic residues.
PMID:24982431	FYPO:0003716	abolished protein localization to lateral cortical node, with protein mislocalized to nucleus [assayed_protein] PomBase:SPAC57A10.02 [has_penetrance] high	Node assembly was also largely disrupted when mid1400–450 was combined with the Cdr2FF* mutation, which was deficient for KA-1–dependent clustering (Fig. 4 A).
PMID:24982431	MOD:00046	O-phospho-L-serine	Proteomic analysis of phosphopeptides from Cdr2-mEGFP immunoprecipitated from wild-type cells revealed four sites phosphorylated in vivo within the Cdr2-Cter basic motif (S604, S607, S616, and S618; Figs. 7 C and S4 A).
PMID:24982431	MOD:00046	O-phospho-L-serine	Proteomic analysis of phosphopeptides from Cdr2-mEGFP immunoprecipitated from wild-type cells revealed four sites phosphorylated in vivo within the Cdr2-Cter basic motif (S604, S607, S616, and S618; Figs. 7 C and S4 A).
PMID:24982431	MOD:00046	O-phospho-L-serine	Proteomic analysis of phosphopeptides from Cdr2-mEGFP immunoprecipitated from wild-type cells revealed four sites phosphorylated in vivo within the Cdr2-Cter basic motif (S604, S607, S616, and S618; Figs. 7 C and S4 A).
PMID:24982431	MOD:00046	O-phospho-L-serine	Proteomic analysis of phosphopeptides from Cdr2-mEGFP immunoprecipitated from wild-type cells revealed four sites phosphorylated in vivo within the Cdr2-Cter basic motif (S604, S607, S616, and S618; Figs. 7 C and S4 A).
PMID:24982431	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC57A10.02 [assayed_protein] PomBase:SPAC57A10.02	Remarkably, mutations of the hydrophobic residues F704 and F705 to aspartic acid (D) abolished Cdr2- Cter clustering (Fig. 3, A and B). Moreover, the interaction between differentially tagged Cdr2-CterFF* mutants was strongly impaired in pull-down experiments (Fig. 3 C).
PMID:24982431	GO:0001786	phosphatidylserine binding	Similar to the Kcc4 KA-1 domain (Moravcevic et al., 2010), recombinant Cdr2- Cter also bound in vitro on lipid strips to phosphatidylserine, a major acidic phospholipid of the plasma membrane (Fig. S1 C).
PMID:24982431	FYPO:0006638	decreased protein localization to medial cortex, with protein distributed in cell cortex, during vegetative growth [assayed_protein] PomBase:SPAC57A10.02	Strikingly, neither Cdr2N-Kcc4C chimera nor Cdr2FF* mutant formed nodes in the presence of Pom1-chimera and redistributed toward the cell tips in a smoother pattern (Figs. 6 A and S3 C).
PMID:24982431	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [assayed_protein] PomBase:SPAC57A10.02	These mutants also produced longer cells, with stronger Cdr2 localization defects correlating with longer delays in mitotic entry (Table S3),
PMID:24982431	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [assayed_protein] PomBase:SPAC57A10.02	These mutants also produced longer cells, with stronger Cdr2 localization defects correlating with longer delays in mitotic entry (Table S3),
PMID:24982431	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [assayed_protein] PomBase:SPAC57A10.02	These mutants also produced longer cells, with stronger Cdr2 localization defects correlating with longer delays in mitotic entry (Table S3),
PMID:24982431	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [assayed_protein] PomBase:SPAC57A10.02	These mutants also produced longer cells, with stronger Cdr2 localization defects correlating with longer delays in mitotic entry (Table S3),
PMID:24982431	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [assayed_protein] PomBase:SPAC57A10.02	These mutants also produced longer cells, with stronger Cdr2 localization defects correlating with longer delays in mitotic entry (Table S3),
PMID:24982431	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [assayed_protein] PomBase:SPAC57A10.02	These mutants also produced longer cells, with stronger Cdr2 localization defects correlating with longer delays in mitotic entry (Table S3),
PMID:24982431	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [assayed_protein] PomBase:SPAC57A10.02	These mutants also produced longer cells, with stronger Cdr2 localization defects correlating with longer delays in mitotic entry (Table S3),
PMID:24982431	FYPO:0002557	decreased protein localization to medial cortex during vegetative growth [assayed_protein] PomBase:SPAC57A10.02	We found that in pom1 cells, the Cdr2 domain spanned approximately two thirds of the cell length compared with approximately one third in wild-type, from cell birth through cell division (Fig. 5, A and E).
PMID:24982431	FYPO:0003712	lateral cortical nodes present in increased numbers [assayed_protein] PomBase:SPAC57A10.02	We found that in pom1 cells, the Cdr2 domain spanned approximately two thirds of the cell length compared with approximately one third in wild-type, from cell birth through cell division (Fig. 5, A and E).
PMID:24982431	FYPO:0010030	medial cortical nodes present in decreased number	We thus tested next whether their combination could recapitulate Pom1 inhibition of node assembly. To do so, we produced a double cdr2bsc-3D mid1400–450 mutant to mimic the dual regulation performed by Pom1. In this context, Cdr2 node assembly was strongly affected specifically in the number of nodes (Fig. 8, A and B).
PMID:24982431	FYPO:0008075	increased protein localization to cell cortex of cell tip during vegetative growth [assayed_protein] PomBase:SPAC57A10.02	We thus tested whether Pom1 also acts on the Cdr2 C terminus (Fig. 7, A and B). Analysis of Cdr2-Cter distribution on the cortex revealed that it was largely excluded from both cell tips in most wild-type cells but enriched at one or both cell tips in the majority of pom1 cells, reminiscent of the localization of full- length Cdr2 in pom1 cells
PMID:24997422	FYPO:0001164	normal growth on glucose carbon source	). Interestingly, growth of transformants overexpressing truncated Fxn1 with a disrupted mitochondrial localization sequence (Fxn1Δ2-11) is similar to pREP3X at all concentrations of thiamine (Fig. 1A). These observations demonstrate that the growth inhibition resulting from Fxn1 overexpression is related to mitochondrial levels or improper processing of Fxn1.
PMID:25002536	GO:0000785	chromatin [coincident_with] ncRNA_gene	(comment: LTR and ncRNA)
PMID:25002536	GO:0000785	chromatin [coincident_with] long_terminal_repeat	(comment: LTR and ncRNA)
PMID:25002536	GO:0000785	chromatin [coincident_with] long_terminal_repeat	(comment: occurs at LTR and ncRNA)
PMID:25002536	GO:0000785	chromatin	(comment: occurs at LTR and ncRNA)
PMID:25002536	GO:0000785	chromatin	(comment: occurs at LTR and ncRNA)
PMID:25002536	GO:0000785	chromatin [coincident_with] ncRNA_gene	(comment: occurs at LTR and ncRNA)
PMID:25009287	GO:1990463	lateral cortical node	(comment: Skb1 and Slf1 (SPAC821.03C) mutually depend to form node-like structures on the plasma membrane.)
PMID:25009287	GO:1990463	lateral cortical node	(comment: Skb1 and Slf1 (SPAC821.03C) mutually depend to form node-like structures on the plasma membrane.)
PMID:25009287	GO:0043495	protein-membrane adaptor activity [has_input] PomBase:SPBC16H5.11c [part_of] lateral cortical node assembly	Here we show that Skb1 forms nodes by interacting with the novel protein Slf1, which is a limiting factor for node formation in cells. Using quantitative fluorescence microscopy and in vitro assays, we demonstrate that Skb1-Slf1 nodes are megadalton structures that are anchored to the membrane by a lipid-binding region in the Slf1 C-terminus.
PMID:25015293	FYPO:0001252	multinucleate multiseptate vegetative cell [has_penetrance] 19 [has_severity] medium	(comment: multinucleate inferred from DNA content)
PMID:25015293	FYPO:0001252	multinucleate multiseptate vegetative cell [has_penetrance] 35 [has_severity] high	(comment: multinucleate inferred from DNA content)
PMID:25015293	FYPO:0001252	multinucleate multiseptate vegetative cell [has_penetrance] 19 [has_severity] medium	(comment: multinucleate inferred from DNA content)
PMID:25015293	FYPO:0001252	multinucleate multiseptate vegetative cell [has_penetrance] 35 [has_severity] high	(comment: multinucleate inferred from DNA content)
PMID:25015293	FYPO:0001252	multinucleate multiseptate vegetative cell [has_penetrance] 19 [has_severity] medium	(comment: multinucleate inferred from DNA content)
PMID:25015293	FYPO:0006060	abolished protein localization to septin ring [assayed_using] PomBase:SPAC4F10.11 [has_penetrance] 80	(comment: same as spt20delta alone)
PMID:25015293	FYPO:0006060	abolished protein localization to septin ring [assayed_using] PomBase:SPAC4F10.11 [has_penetrance] 80	(comment: same as spt20delta alone)
PMID:25015293	FYPO:0006060	abolished protein localization to septin ring [assayed_using] PomBase:SPAC4F10.11 [has_penetrance] 80	(comment: same as spt20delta alone)
PMID:25040903	FYPO:0001492	viable elongated vegetative cell	(Figure S1C)
PMID:25040903	FYPO:0000024	stubby vegetative cell	(Figure S1C)
PMID:25040903	FYPO:0002031	abnormal actin cable morphology [has_penetrance] 60-70	(Figure S1E)
PMID:25040903	FYPO:0001019	monopolar actin cortical patch localization during vegetative growth [has_penetrance] 60-70	(Figure S1E)
PMID:25057016	FYPO:0003840	sensitive to carbendazim [has_severity] high	(Fig. 1)
PMID:25057016	FYPO:0003840	sensitive to carbendazim	(Fig. 1)
PMID:25057016	FYPO:0003840	sensitive to carbendazim	(Fig. 1)
PMID:25057016	FYPO:0003840	sensitive to carbendazim [has_severity] high	(Fig. 1)
PMID:25057016	FYPO:0003566	delayed onset of mitotic spindle pole body separation	(Fig. 2)
PMID:25057016	FYPO:0003566	delayed onset of mitotic spindle pole body separation	(Fig. 2)
PMID:25057016	FYPO:0005779	normal protein localization to kinetochore during mitosis [assayed_protein] PomBase:SPAC890.02c	(Fig. 3)
PMID:25057016	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC2G2.14	(Fig. 3)
PMID:25057016	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC890.02c	(Fig. 3)
PMID:25057016	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC890.02c [assayed_protein] PomBase:SPBC2G2.14	(Fig. 4)
PMID:25057016	FYPO:0003840	sensitive to carbendazim	(Fig. 4)
PMID:25057016	FYPO:0003566	delayed onset of mitotic spindle pole body separation	(Fig. 4)
PMID:25057016	FYPO:0009114	transient monopolar mitotic spindle	(Fig. 4)
PMID:25057016	FYPO:0005779	normal protein localization to kinetochore during mitosis [assayed_protein] PomBase:SPAC890.02c	(Fig. 4)
PMID:25057016	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC890.02c	(Fig. 4)
PMID:25057016	FYPO:0005779	normal protein localization to kinetochore during mitosis [assayed_protein] PomBase:SPAC890.02c	(Fig. 4)
PMID:25057016	FYPO:0003840	sensitive to carbendazim	(Fig. 4)
PMID:25057016	FYPO:0003566	delayed onset of mitotic spindle pole body separation	(Fig. 4)
PMID:25057016	FYPO:0009114	transient monopolar mitotic spindle	(Fig. 4)
PMID:25057016	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC890.02c	(Fig. 4)
PMID:25057016	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC890.02c [assayed_protein] PomBase:SPBC2G2.14	(Fig. 4)
PMID:25057016	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC890.02c [assayed_protein] PomBase:SPBC2G2.14	(Fig. 4) (comment: BiFC)
PMID:25057016	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC890.02c [assayed_protein] PomBase:SPBC2G2.14	(Fig. 4) (comment: BiFC)
PMID:25057016	FYPO:0000228	lagging mitotic chromosomes	(Fig. 6)
PMID:25057016	FYPO:0000228	lagging mitotic chromosomes	(Fig. 6)
PMID:25057016	FYPO:0000228	lagging mitotic chromosomes	(Fig. 6)
PMID:25057016	FYPO:0000030	abnormal mitotic chromosome congression [has_penetrance] 56	(Fig. S1D)
PMID:25057016	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC890.02c [assayed_protein] PomBase:SPCC895.07	(Fig. S5D)
PMID:25057016	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPAC890.02c [occurs_in] mitotic spindle pole body [part_of] initial mitotic spindle pole body separation [happens_during] mitotic prophase	(comment: Thorough experiments throughout using both full deletions as well as phospho mutants. Direct physical interaction is confirmed by Y2H)
PMID:25057016	GO:0000776	kinetochore [exists_during] mitotic M phase	Good evidence for this is the colocalisation with cnp3 in Fig. 3A in the csi1D background, where alp7 does not go to the spindle, or nda3 mutant where the spindle does not form, but alp7 still goes to the kinetochore, as seen by cnp3
PMID:25081204	GO:0106057	negative regulation of calcineurin-mediated signaling	(comment: prz1 is the pombe equivalent to NFAT -functional equivalent rather than ortholog)
PMID:25081204	GO:0106057	negative regulation of calcineurin-mediated signaling	(comment: prz1 is the pombe equivalent to NFAT -functional equivalent rather than ortholog)
PMID:25102102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC3G9.11c [happens_during] cellular response to starvation	Among the four predicted genes for pyruvate decarboxylase, only the Phx1-dependent genes (pdc201+ and pdc202+) contributed to long-term survival as judged by mutation and overexpression studies. These findings indicate that the Phx1-mediated long-term survival is achieved primarily through increasing the synthesis and activity of pyruvate decarboxylase. Consistent with this hypothesis, we observed that Phx1 curtailed respiration when cells entered stationary phase.
PMID:25102102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC13A11.06 [happens_during] cellular response to starvation	Among the four predicted genes for pyruvate decarboxylase, only the Phx1-dependent genes (pdc201+ and pdc202+) contributed to long-term survival as judged by mutation and overexpression studies. These findings indicate that the Phx1-mediated long-term survival is achieved primarily through increasing the synthesis and activity of pyruvate decarboxylase. Consistent with this hypothesis, we observed that Phx1 curtailed respiration when cells entered stationary phase.
PMID:25103238	GO:0140480	mitotic spindle pole body insertion into the nuclear envelope	(comment: Failure of NE fenestration during in the double tts1del cut11-6 mutant)
PMID:25103238	FYPO:0003567	abnormal mitotic spindle pole body insertion into nuclear envelope	(comment: Failure of NE fenestration during in the double tts1del cut11-6 mutant)
PMID:25106870	GO:0003887	DNA-directed DNA polymerase activity	(Fig. 1)
PMID:25106870	GO:0004523	RNA-DNA hybrid ribonuclease activity	(Fig. 5)
PMID:25106870	GO:1990516	ribonucleotide excision repair	(comment: Incision of ribonucleotides paired to 8oxoguanine in the DNA)
PMID:25106870	GO:0070716	mismatch repair involved in maintenance of fidelity involved in DNA-dependent DNA replication	(comment: RER should probably be a child of this)
PMID:25106870	GO:0042276	error-prone translesion synthesis	Tolerance of the 8oxoguanine lesion during DNA gap-filling inserting the ribonucleotide ATP. This acitivity can be coupled to the non-homologous end joining (NHEJ) of double strand breaks (DSBs). (comment: changed from dna repair to translesion synthesis. /AL)
PMID:25109267	GO:1990748	cellular detoxification	(comment: CONDITION Ricinoleic acid, RA moieties from phospholipids)
PMID:25122751	FYPO:0003908	increased stress response gene antisense RNA level	(comment: At stress response genes)
PMID:25195688	GO:1990536	phosphoenolpyruvate transmembrane import into Golgi lumen	(comment: CHECK transmembrane import into Golgi lumen)
PMID:25195688	GO:1990536	phosphoenolpyruvate transmembrane import into Golgi lumen	(comment: CHECK transmembrane import into Golgi lumen)
PMID:25203555	GO:0140656	endodeoxyribonuclease activator activity [has_input] PomBase:SPCC970.01	(comment: CHECK regulator of structure-specific DNA nuclease)
PMID:25203555	GO:0005515	protein binding	(comment: not sure)
PMID:25204792	GO:0031137	regulation of conjugation with cellular fusion [part_of] cellular response to zinc ion starvation	(comment: CHECK defect in sexual development in response to zinc or iron limitation)
PMID:25204792	GO:0031137	regulation of conjugation with cellular fusion [part_of] cellular response to iron ion starvation	(comment: CHECK defect in sexual development in response to zinc or iron limitation)
PMID:25245948	GO:0031509	subtelomeric heterochromatin formation	(Fig. 1)
PMID:25245948	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC19G12.13c	(comment: cDNA; no introns)
PMID:25245948	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] low	(comment: cDNA; no introns)
PMID:25245948	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC1778.02	(comment: cDNA; no introns)
PMID:25245948	FYPO:0003555	normal chromatin silencing at subtelomere	(comment: cDNA; no introns)
PMID:25245948	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC19G12.13c	(comment: cDNA; no introns)
PMID:25245948	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC1778.02	(comment: cDNA; no introns)
PMID:25254656	FYPO:0003328	misoriented interphase microtubules	(Figure 3A)
PMID:25254656	FYPO:0005799	decreased microtubule dwell time at cell tip	(Figure 3B, Figure 3C)
PMID:25254656	FYPO:0005485	abolished inositol phosphate phosphatase activity	(Figure 3C)
PMID:25254656	FYPO:0006892	abolished inositol hexakisphosphate kinase activity	(Figure 3C)
PMID:25254656	FYPO:0006893	decreased inositol hexakisphosphate kinase activity	(Figure 3C) (comment: the N erminal domain has a dominent -ve effect in in vitro assay (not expression should ne n/a))
PMID:25254656	FYPO:0005682	decreased microtubule depolymerization during vegetative growth	(Figure 4A)
PMID:25254656	FYPO:0006103	short interphase microtubules [has_penetrance] medium	(Figure 4E)
PMID:25254656	FYPO:0006103	short interphase microtubules [has_penetrance] high	(Figure 4E)
PMID:25254656	FYPO:0003328	misoriented interphase microtubules	(Figure S15)
PMID:25254656	FYPO:0000091	sensitive to thiabendazole	(Figure S2A)
PMID:25254656	GO:0000828	inositol hexakisphosphate kinase activity	(comment: CHECK in vitro) Figure S1A, right pane
PMID:25254656	GO:0052843	inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity	(comment: CHECK in vitro) Figure S1A, right pane
PMID:25313826	GO:1990426	mitotic recombination-dependent replication fork processing	the CAF-1 complex promotes Replication-coupled homologous recombination at blocked replication forks.
PMID:25313826	GO:1990426	mitotic recombination-dependent replication fork processing	the CAF-1 complex promotes Replication-coupled homologous recombination at blocked replication forks.
PMID:25313826	GO:1990426	mitotic recombination-dependent replication fork processing	the CAF-1 complex promotes Replication-coupled homologous recombination at blocked replication forks.
PMID:25318672	FYPO:0006934	normal cellular triglyceride level	(comment: Determined by thin layer chromatography TLC)
PMID:25318672	FYPO:0006934	normal cellular triglyceride level	(comment: Determined by thin layer chromatography TLC)
PMID:25318672	FYPO:0006934	normal cellular triglyceride level	(comment: Determined by thin layer chromatography TLC)
PMID:25318672	FYPO:0002227	increased cellular triglyceride level during vegetative growth [has_penetrance] high [has_severity] high	(comment: Determined by thin layer chromatography, TLC)
PMID:25318672	FYPO:0000674	normal cell population growth at high temperature	(comment: Mutant cells grow normally in liquid minimal medium supplemented with choline.)
PMID:25318672	FYPO:0000674	normal cell population growth at high temperature	(comment: Mutant cells grow normally in liquid minimal medium supplemented with ethanolamine.)
PMID:25318672	FYPO:0000674	normal cell population growth at high temperature	(comment: Mutant cells grow normally in liquid rich medium)
PMID:25318672	FYPO:0000354	abnormal endoplasmic reticulum morphology [has_penetrance] high [has_severity] high	(comment: The endoplasmic reticulum is wrapped around the abnormally large lipid droplets)
PMID:25318672	FYPO:0001355	decreased vegetative cell population growth	(comment: permissive temperature for bbl1-9)
PMID:25318672	FYPO:0001357	normal vegetative cell population growth	(comment: restrictive temperature for bbl1-9)
PMID:25318672	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(comment: restrictive temperature for bbl1-9)
PMID:25318672	FYPO:0002061	inviable vegetative cell population	(comment: restrictive temperature for bbl1-9)
PMID:25318672	FYPO:0007763	decreased phosphatidate cytidylyltransferase activity [assayed_enzyme] PomBase:SPBC13A2.03	At high temperature (36C), the mutant protein appeared to bind PA nearly as well as the wild-type enzyme but exhibited a strongly decreased rate of catalysis.
PMID:25318672	FYPO:0000356	abnormal lipid droplet morphology [has_penetrance] high [has_severity] high	At the restrictive temperature of 36C, cells accumulate very large lipid droplets surrounded by the endoplasmic reticulum. These lipid droplets arise from persistent growth rather than fusion.
PMID:25318672	FYPO:0001234	slow vegetative cell population growth [has_severity] high	Slow population growth rate can be rescued by supplementing the minimal medium with choline or ethanolamine, the precursors required for phospholipid biosynthesis through the de novo Kennedy pathway
PMID:25330395	FYPO:0003107	progressively shortening telomeres during vegetative growth	Tpz1-L439R,L445R disrupts interaction with Ccq1 but retain interactions with Pot1 and Poz1 based on co-IP experiments.
PMID:25330395	FYPO:0003107	progressively shortening telomeres during vegetative growth	Tpz1-L449R disrupts interaction with Ccq1 but retain interactions with Pot1 and Poz1 based on co-IP experiments. In combination with poz1 deletion, telomeres become unprotected and cells survive by circularizing chromosomes. Telomerase cannot be recruited to telomeres since Rad3/Tel1-dependent phosphorylation of Ccq1 Thr93, essential for promoting Ccq1-Est1 interaction and telomerase recruitment, is eliminated by tpz1-L449R.
PMID:25330395	FYPO:0002019	elongated telomeres during vegetative growth	Tpz1-W498R,I501R disrupts interaction with Poz1 but retain interactions with Pot1 and Ccq1 based on co-IP experiments. In combination with ccq1 deletion, telomeres become unprotected and cells survive by circularizing chromosomes. Telomerase recruitment to telomeres is increased since Rad3/Tel1-dependent phosphorylation of Ccq1 Thr93, essential for promoting Ccq1-Est1 interaction and telomerase recruitment, is increased in tpz1-W498R,I501R cells.
PMID:25330395	FYPO:0002019	elongated telomeres during vegetative growth	Tpz1-[1-485] disrupts interaction with Poz1 but retain interactions with Pot1 and Ccq1 based on co-IP experiments. In combination with ccq1 deletion, telomeres become unprotected and cells survive by circularizing chromosomes. Telomerase recruitment to telomeres is increased since Rad3/Tel1-dependent phosphorylation of Ccq1 Thr93, essential for promoting Ccq1-Est1 interaction and telomerase recruitment, is increased in tpz1-[1-485] cells.
PMID:25332400	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC664.01c	Importantly,CK2-mediated phosphorylation had a similar effect on the nucleosome-binding specificities of fly HP1a and S.pombe Swi6. (Figure 6A)
PMID:25348260	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC25G10.07c	(Fig. 3)
PMID:25348260	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC25G10.07c	(Fig. 3)
PMID:25348260	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC25G10.07c	(Fig. 3)
PMID:25348260	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC25G10.07c	(Fig. 3)
PMID:25348260	FYPO:0003277	abolished protein localization to microtubule during mitosis [assayed_protein] PomBase:SPAC25G10.07c	(Fig. 3)
PMID:25348260	FYPO:0003277	abolished protein localization to microtubule during mitosis [assayed_protein] PomBase:SPAC25G10.07c	(Fig. 3)
PMID:25348260	FYPO:0004754	abolished protein localization to mitotic spindle during mitosis [assayed_protein] PomBase:SPAC25G10.07c	(Fig. 3)
PMID:25348260	FYPO:0004754	abolished protein localization to mitotic spindle during mitosis [assayed_protein] PomBase:SPAC25G10.07c	(Fig. 3)
PMID:25348260	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC25G10.07c	(Fig. 3)
PMID:25356590	FYPO:0002917	abolished histone H3-K4 methylation during vegetative growth	(Fig. 1B)
PMID:25356590	FYPO:0002917	abolished histone H3-K4 methylation during vegetative growth	(Fig. 1B)
PMID:25356590	FYPO:0005311	normal histone H3-K4 methylation during vegetative growth	(Fig. 1B)
PMID:25356590	FYPO:0002366	decreased histone H3-K4 methylation during vegetative growth [has_severity] high	(Fig. 1B)
PMID:25356590	FYPO:0002917	abolished histone H3-K4 methylation during vegetative growth	(Fig. 1B)
PMID:25356590	FYPO:0002917	abolished histone H3-K4 methylation during vegetative growth	(Fig. 1B)
PMID:25356590	FYPO:0002917	abolished histone H3-K4 methylation during vegetative growth	(Fig. 1B)
PMID:25356590	FYPO:0004342	increased LTR-derived RNA level [has_severity] medium	(Fig. 1C)
PMID:25356590	FYPO:0008248	decreased LTR-derived RNA level [has_severity] medium	(Fig. 1C)
PMID:25356590	FYPO:0008252	normal LTR-derived RNA level	(Fig. 1C)
PMID:25356590	FYPO:0004342	increased LTR-derived RNA level [has_severity] high	(Fig. 1C)
PMID:25356590	FYPO:0008248	decreased LTR-derived RNA level [has_severity] medium	(Fig. 1C)
PMID:25356590	FYPO:0008248	decreased LTR-derived RNA level [has_severity] medium	(Fig. 1C)
PMID:25356590	FYPO:0004342	increased LTR-derived RNA level [has_severity] high	(Fig. 1C)
PMID:25356590	FYPO:0002834	decreased chromatin silencing at centromere [assayed_transcript] dg_repeat [has_severity] medium	(Fig. 1D)
PMID:25356590	FYPO:0005071	increased chromatin silencing at centromere [assayed_transcript] dg_repeat [has_severity] low	(Fig. 1D)
PMID:25356590	FYPO:0002834	decreased chromatin silencing at centromere [assayed_transcript] dg_repeat [has_severity] high	(Fig. 1D)
PMID:25356590	FYPO:0002834	decreased chromatin silencing at centromere [assayed_transcript] dg_repeat [has_severity] high	(Fig. 1D)
PMID:25356590	FYPO:0002360	normal chromatin silencing at centromere [assayed_transcript] dg_repeat	(Fig. 1D)
PMID:25356590	FYPO:0002360	normal chromatin silencing at centromere [assayed_transcript] dg_repeat	(Fig. 1D)
PMID:25356590	FYPO:0002834	decreased chromatin silencing at centromere [assayed_transcript] dg_repeat [has_severity] low	(Fig. 1D)
PMID:25356590	FYPO:0004689	increased cenH-derived RNA level [has_severity] medium	(Fig. 1E)
PMID:25356590	FYPO:0004689	increased cenH-derived RNA level [has_severity] high	(Fig. 1E)
PMID:25356590	FYPO:0004689	increased cenH-derived RNA level [has_severity] high	(Fig. 1E)
PMID:25356590	FYPO:0004689	increased cenH-derived RNA level [has_severity] high	(Fig. 1E)
PMID:25356590	FYPO:0004689	increased cenH-derived RNA level [has_severity] high	(Fig. 1E)
PMID:25356590	FYPO:0004689	increased cenH-derived RNA level [has_severity] high	(Fig. 1E)
PMID:25356590	FYPO:0008246	normal cenH-derived RNA level	(Fig. 1E)
PMID:25356590	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07 [has_severity] high	(Fig. 1F)
PMID:25356590	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07 [has_severity] high	(Fig. 1F)
PMID:25356590	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07 [has_severity] high	(Fig. 1F)
PMID:25356590	FYPO:0008247	decreased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07 [has_severity] medium	(Fig. 1F)
PMID:25356590	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07 [has_severity] high	(Fig. 1F)
PMID:25356590	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07 [has_severity] high	(Fig. 1F)
PMID:25356590	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07 [has_severity] high	(Fig. 1F)
PMID:25356590	FYPO:0008250	normal protein localization to chromatin at protein coding gene [assayed_region] PomBase:SPBC32H8.12c [assayed_protein] PomBase:SPCC306.04c	(Fig. 2A)
PMID:25356590	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [assayed_region] PomBase:SPBC32H8.12c [assayed_protein] PomBase:SPCC306.04c [has_severity] medium	(Fig. 2A)
PMID:25356590	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [assayed_region] PomBase:SPBC32H8.12c [assayed_protein] PomBase:SPCC306.04c [has_severity] medium	(Fig. 2A)
PMID:25356590	FYPO:0004066	increased protein localization to chromatin at protein coding gene [assayed_region] PomBase:SPBC32H8.12c [has_severity] low [assayed_protein] PomBase:SPCC306.04c	(Fig. 2A)
PMID:25356590	FYPO:0008250	normal protein localization to chromatin at protein coding gene [assayed_region] PomBase:SPBC32H8.12c [assayed_protein] PomBase:SPCC306.04c	(Fig. 2A)
PMID:25356590	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC306.04c [has_severity] medium	(Fig. 2C)
PMID:25356590	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC306.04c [has_severity] low	(Fig. 2C)
PMID:25356590	FYPO:0008154	normal protein localization to centromeric heterochromatin [assayed_protein] PomBase:SPCC306.04c	(Fig. 2C)
PMID:25356590	FYPO:0008154	normal protein localization to centromeric heterochromatin [assayed_protein] PomBase:SPCC306.04c	(Fig. 2C)
PMID:25356590	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC306.04c [has_severity] medium	(Fig. 2C)
PMID:25356590	FYPO:0002917	abolished histone H3-K4 methylation during vegetative growth	(Fig. 3A)
PMID:25356590	FYPO:0005311	normal histone H3-K4 methylation during vegetative growth	(Fig. 3A)
PMID:25356590	FYPO:0002917	abolished histone H3-K4 methylation during vegetative growth	(Fig. 3A)
PMID:25356590	FYPO:0004126	abolished histone H3-K4 trimethylation during vegetative growth	(Fig. 3A)
PMID:25356590	FYPO:0005311	normal histone H3-K4 methylation during vegetative growth	(Fig. 3A)
PMID:25356590	FYPO:0002366	decreased histone H3-K4 methylation during vegetative growth [has_severity] medium	(Fig. 3A)
PMID:25356590	FYPO:0004126	abolished histone H3-K4 trimethylation during vegetative growth	(Fig. 3A)
PMID:25356590	FYPO:0002917	abolished histone H3-K4 methylation during vegetative growth	(Fig. 3A)
PMID:25356590	FYPO:0008252	normal LTR-derived RNA level	(Fig. 3B)
PMID:25356590	FYPO:0008248	decreased LTR-derived RNA level [has_severity] medium	(Fig. 3B)
PMID:25356590	FYPO:0008252	normal LTR-derived RNA level	(Fig. 3B)
PMID:25356590	FYPO:0008252	normal LTR-derived RNA level	(Fig. 3B)
PMID:25356590	FYPO:0008248	decreased LTR-derived RNA level [has_severity] low	(Fig. 3B)
PMID:25356590	FYPO:0008248	decreased LTR-derived RNA level [has_severity] medium	(Fig. 3B)
PMID:25356590	FYPO:0008252	normal LTR-derived RNA level	(Fig. 3B)
PMID:25356590	FYPO:0002834	decreased chromatin silencing at centromere [assayed_transcript] dg_repeat [has_severity] low	(Fig. 3C)
PMID:25356590	FYPO:0002360	normal chromatin silencing at centromere [assayed_transcript] dg_repeat	(Fig. 3C)
PMID:25356590	FYPO:0005071	increased chromatin silencing at centromere [assayed_transcript] dg_repeat [has_severity] high	(Fig. 3C)
PMID:25356590	FYPO:0002360	normal chromatin silencing at centromere [assayed_transcript] dg_repeat	(Fig. 3C)
PMID:25356590	FYPO:0002834	decreased chromatin silencing at centromere [assayed_transcript] dg_repeat [has_severity] low	(Fig. 3C)
PMID:25356590	FYPO:0005071	increased chromatin silencing at centromere [assayed_transcript] dg_repeat [has_severity] high	(Fig. 3C)
PMID:25356590	FYPO:0005071	increased chromatin silencing at centromere [assayed_transcript] dg_repeat [has_severity] high	(Fig. 3C)
PMID:25356590	FYPO:0004689	increased cenH-derived RNA level [has_severity] medium	(Fig. 3D)
PMID:25356590	FYPO:0004689	increased cenH-derived RNA level [has_severity] high	(Fig. 3D)
PMID:25356590	FYPO:0004689	increased cenH-derived RNA level [has_severity] medium	(Fig. 3D)
PMID:25356590	FYPO:0008251	decreased silent mating-type cassette transcript-derived RNA level [has_severity] medium	(Fig. 3D)
PMID:25356590	FYPO:0004689	increased cenH-derived RNA level [has_severity] high	(Fig. 3D)
PMID:25356590	FYPO:0004689	increased cenH-derived RNA level [has_severity] high	(Fig. 3D)
PMID:25356590	FYPO:0004689	increased cenH-derived RNA level [has_severity] low	(Fig. 3D)
PMID:25356590	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07 [has_severity] low	(Fig. 3E)
PMID:25356590	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07 [has_severity] medium	(Fig. 3E)
PMID:25356590	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07 [has_severity] medium	(Fig. 3E)
PMID:25356590	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07 [has_severity] medium	(Fig. 3E)
PMID:25356590	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07 [has_severity] high	(Fig. 3E)
PMID:25356590	FYPO:0005602	normal subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07	(Fig. 3E)
PMID:25356590	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPNCRNA.07 [has_severity] high	(Fig. 3E)
PMID:25356590	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPCC306.04c	(Fig. 4A)
PMID:25356590	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPCC306.04c	(Fig. 4A)
PMID:25356590	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c [has_severity] medium	(Fig. 4A)
PMID:25356590	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c [has_severity] low	(Fig. 4A)
PMID:25356590	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c [has_severity] low	(Fig. 4A)
PMID:25356590	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPCC306.04c	(Fig. 4A)
PMID:25356590	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c	(Fig. 4A)
PMID:25356590	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c	(Fig. 4B)
PMID:25356590	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c [has_severity] low	(Fig. 4B)
PMID:25356590	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c [has_severity] medium	(Fig. 4C)
PMID:25356590	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c [has_severity] low	(Fig. 4C)
PMID:25356590	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c [has_severity] low	(Fig. 4C)
PMID:25356590	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c [has_severity] low	(Fig. 4C)
PMID:25356590	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c [has_severity] high	(Fig. 4C)
PMID:25356590	FYPO:0008255	decreased histone H3-K4 acetylation at protein coding gene during vegetative growth [has_severity] high [assayed_using] PomBase:SPBC32H8.12c	(Fig. 6B)
PMID:25356590	FYPO:0008255	decreased histone H3-K4 acetylation at protein coding gene during vegetative growth [has_severity] high [assayed_using] PomBase:SPBC32H8.12c	(Fig. 6B)
PMID:25356590	FYPO:0008254	increased histone H3-K4 acetylation at protein coding gene during vegetative growth [has_severity] medium [assayed_using] PomBase:SPBC32H8.12c	(Fig. 6B)
PMID:25356590	FYPO:0008255	decreased histone H3-K4 acetylation at protein coding gene during vegetative growth [has_severity] medium [assayed_using] PomBase:SPBC32H8.12c	(Fig. 6B)
PMID:25356590	FYPO:0008256	decreased histone H3-K4 acetylation at LTR during vegetative growth [has_severity] low	(Fig. 6C)
PMID:25356590	FYPO:0008257	increased histone H3-K4 acetylation at LTR during vegetative growth [has_severity] low	(Fig. 6C)
PMID:25356590	FYPO:0008256	decreased histone H3-K4 acetylation at LTR during vegetative growth [has_severity] medium	(Fig. 6C)
PMID:25356590	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC306.04c	(Fig. S5)
PMID:25356590	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC306.04c	(Fig. S5)
PMID:25356590	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC306.04c	(Fig. S5)
PMID:25356590	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC306.04c	(Fig. S5)
PMID:25356590	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC306.04c	(Fig. S5)
PMID:25356590	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC306.04c	(Fig. S5)
PMID:25356590	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC306.04c	(Fig. S5)
PMID:25356590	GO:0141005	transposable element silencing by heterochromatin formation	Thus, H3K4me catalyzed by Set1C could compete with Mst1- mediated H3K4ac at Tf2s to maintain the integrity of Tf bodies.
PMID:25356590	GO:0042800	histone H3K4 methyltransferase activity [part_of] subtelomeric heterochromatin formation	at the mat locus and subtelomeric repeats Set1-mediated H3K4me contributes to repression.
PMID:25356590	GO:0042800	histone H3K4 methyltransferase activity [part_of] silent mating-type cassette heterochromatin formation	at the mat locus and subtelomeric repeats Set1-mediated H3K4me contributes to repression.
PMID:25375137	FYPO:0008113	increased intron retention	Both mutants showed a build- up of intronic reads in specific sets of introns that overlapped significantly with the introns identified using microarrays (p values of 66 10247 and 86 1027 for SPBC18H10.07 and SP AC30D11.14c, respectively). Moreover, this increase was accom- panied by an accumulation of reads mapping to the corresponding exon-intron junctions, indicating that the mutations cause inefficient splicing of pre-mRNAs (Figure S2B–E).
PMID:25375137	FYPO:0008113	increased intron retention	Both mutants showed a build- up of intronic reads in specific sets of introns that overlapped significantly with the introns identified using microarrays (p values of 66 10247 and 86 1027 for SPBC18H10.07 and SP AC30D11.14c, respectively). Moreover, this increase was accom- panied by an accumulation of reads mapping to the corresponding exon-intron junctions, indicating that the mutations cause inefficient splicing of pre-mRNAs (Figure S2B–E).
PMID:25375137	FYPO:0002137	decreased RNA catabolic process during vegetative growth	By contrast, Zfs1 targets predicted from the expression analysis were highly enriched among those mRNAs that displayed increased half-lives in the zfs1D mutant (Figure 4D).
PMID:25375137	FYPO:0002137	decreased RNA catabolic process during vegetative growth	Finally, scw1 mutants showed correlated changes in mRNA stability and mRNA levels (Figure 4G).
PMID:25375137	FYPO:0002137	decreased RNA catabolic process during vegetative growth	Red1 and Pab1 are part of a system that down-regulates the expression of a group of meiotic mRNAs in vegetative cells, which are strongly overexpressed in red1D and pab2D mutants. We observed highly significant overlaps between mRNAs with increased stabilities in the mutants and those overexpressed, confirming and extending the observations that these proteins promote the decay of their mRNA targets (Figure S3A and S3B).
PMID:25375137	FYPO:0002137	decreased RNA catabolic process during vegetative growth	Red1 and Pab1 are part of a system that down-regulates the expression of a group of meiotic mRNAs in vegetative cells, which are strongly overexpressed in red1D and pab2D mutants. We observed highly significant overlaps between mRNAs with increased stabilities in the mutants and those overexpressed, confirming and extending the observations that these proteins promote the decay of their mRNA targets (Figure S3A and S3B).
PMID:25375137	FYPO:0002137	decreased RNA catabolic process during vegetative growth	Similarly, the under-expression of genes encoding mitochondrial components in rpm1 mutants was strongly correlated with decreased stability (Figure 4F).
PMID:25375137	FYPO:0002137	decreased RNA catabolic process during vegetative growth	The effect of SPAC17H9.04c, which controls a regulon of genes involved in ribosomal synthesis, was also clearly posttran- scriptional, as genes overexpressed in the mutant also showed enhanced stability (Figure 4E).
PMID:25375240	FYPO:0001270	complete but unequal mitotic sister chromatid segregation	(Figure 4G)
PMID:25375240	FYPO:0006175	abnormal protein localization to centromere during mitotic metaphase [assayed_using] PomBase:SPBC27B12.02	(Figure 5E)
PMID:25375240	FYPO:0002060	viable vegetative cell population	(Figure 7D)
PMID:25375240	FYPO:0002574	normal protein localization to centromere during vegetative growth [assayed_using] PomBase:SPBC27B12.02	(Figure 7D)
PMID:25375240	FYPO:0004396	normal mitotic spindle elongation	Tracking of the inter-SPB distance indicated that the kinetics of spindle elongation in the kis1-1 mad2D double mutant was ameliorated compared with the kis1-1 single mutant (Figure S9).
PMID:25375240	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint [assayed_using] PomBase:SPBC27B12.02	indicated by increased mad2 on unattached kinetochores
PMID:25378562	FYPO:0000116	sensitive to zinc	(comment: Sensitive to 3 mM ZnCl2)
PMID:25378562	FYPO:0000116	sensitive to zinc	(comment: Sensitive to 3 mM ZnCl2. Suppressed by overexpression of budding yeast VAM7.)
PMID:25378562	GO:0006896	Golgi to vacuole transport	Vsl1p is a partner of Pep12p, and mainly functions on the prevacuolar and vacuolar membrane.
PMID:25378562	GO:0006896	Golgi to vacuole transport	Vsl1p is a partner of Pep12p, and mainly functions on the prevacuolar and vacuolar membrane.
PMID:25378562	FYPO:0001945	normal protein secretion	mutants defective in vacuolar sorting do not deliver SpCPY to the vacuole but rather to the outside of the cells.
PMID:25378562	FYPO:0001423	normal protein targeting to vacuole	mutants defective in vacuolar sorting do not deliver SpCPY to the vacuole but rather to the outside of the cells.
PMID:25392932	GO:0000785	chromatin [coincident_with] tRNA_gene	(comment: CHECK SO:0001272 = tRNA gene)
PMID:25392932	GO:0000785	chromatin [coincident_with] tRNA_gene	(comment: CHECK SO:0001272 = tRNA gene)
PMID:25392932	GO:0006386	termination of RNA polymerase III transcription	Our data only demonstrate that this true for RNA Polymerase III(comment: // MOVED UP TO 'REGULATION' FROM NEG REG BASED ON NEW PUBLICATION)
PMID:25402480	GO:1990883	18S rRNA cytidine N-acetyltransferase activity [has_input] PomBase:SPRRNA.44	"(comment: SO:0000407 = 18s rRNA, the genes are the 18s genes of the ""correct length"" so I guess we want them in there if we want to be able to make the ""connections"" from the info in the database? Though I guess this regions isnt properly sequenced..)"
PMID:25402480	GO:1990883	18S rRNA cytidine N-acetyltransferase activity [has_input] PomBase:SPRRNA.43	"(comment: SO:0000407 = 18s rRNA, the genes are the 18s genes of the ""correct length"" so I guess we want them in there if we want to be able to make the ""connections"" from the info in the database? Though I guess this regions isnt properly sequenced..)"
PMID:25402480	GO:1990883	18S rRNA cytidine N-acetyltransferase activity [has_input] cytosolic_18S_rRNA	"(comment: SO:0000407 = 18s rRNA, the genes are the 18s genes of the ""correct length"" so I guess we want them in there if we want to be able to make the ""connections"" from the info in the database? Though I guess this regions isnt properly sequenced..)"
PMID:25402480	GO:1990883	18S rRNA cytidine N-acetyltransferase activity [has_input] PomBase:SPRRNA.46	"(comment: SO:0000407 = 18s rRNA, the genes are the 18s genes of the ""correct length"" so I guess we want them in there if we want to be able to make the ""connections"" from the info in the database? Though I guess this regions isnt properly sequenced..)"
PMID:25402480	FYPO:0002061	inviable vegetative cell population	"(comment: They couldn't make the knockout in haploid, and diploid inviable, hence inferring inviable vegetative rather than more general ""inviable cell pop"" or inviable spore pop)"
PMID:25404562	FYPO:0001234	slow vegetative cell population growth	(Fig. 2A) (comment: 11 days for visible colonies)
PMID:25404562	FYPO:0001357	normal vegetative cell population growth	(Fig. 3A)
PMID:25404562	FYPO:0007023	increased tRNA guanosine 1-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007024	decreased tRNA guanosine 7-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007017	normal tRNA pseudouridylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007022	abolished tRNA guanosine 2'-O-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007018	normal tRNA guanosine 2'-O-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007025	decreased tRNA guanosine N2-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007021	abolished tRNA cytosine 2'-O-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007020	normal tRNA guanosine N2-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007021	abolished tRNA cytosine 2'-O-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007023	increased tRNA guanosine 1-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007017	normal tRNA pseudouridylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007018	normal tRNA guanosine 2'-O-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007021	abolished tRNA cytosine 2'-O-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007023	increased tRNA guanosine 1-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007017	normal tRNA pseudouridylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007024	decreased tRNA guanosine 7-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007025	decreased tRNA guanosine N2-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007019	normal tRNA guanosine 7-methylation [assayed_using] PomBase:SPATRNAPHE.01	(Table 2)
PMID:25404562	FYPO:0007021	abolished tRNA cytosine 2'-O-methylation [assayed_using] PomBase:SPATRNAPHE.01	diploid lacked detectable Cm in its tRNAPhe and had normal levels of Gm compared with that from wild type (0.88 versus 0.90 moles/mole) (Table 3; Fig. 4A)
PMID:25404562	FYPO:0007018	normal tRNA guanosine 2'-O-methylation [assayed_using] PomBase:SPATRNAPHE.01	diploid lacked detectable Cm in its tRNAPhe and had normal levels of Gm compared with that from wild type (0.88 versus 0.90 moles/mole) (Table 3; Fig. 4A)
PMID:25404562	FYPO:0007022	abolished tRNA guanosine 2'-O-methylation [assayed_using] PomBase:SPATRNAPHE.01	strain lacked Gm34 in its tRNAPhe, and had Cm levels comparable to those of wild type (0.86 versus 0.91 moles/mole) (Table 3; Fig. 4A).
PMID:25404562	FYPO:0007019	normal tRNA guanosine 7-methylation [assayed_using] PomBase:SPATRNAPHE.01	strain lacked Gm34 in its tRNAPhe, and had Cm levels comparable to those of wild type (0.86 versus 0.91 moles/mole) (Table 3; Fig. 4A).
PMID:25404562	FYPO:0007026	decreased tRNA wybutosine biosynthesis [assayed_using] PomBase:SPATRNAPHE.01	yW formation was impaired in the Sp trm734△ mutant (44% of wild-type levels) and to a lesser extent in the Sp trm732△ mutant (73%) (Fig. 4F), consistent with the increased m1G levels (Table 3; Fig. 4A)
PMID:25404562	FYPO:0007026	decreased tRNA wybutosine biosynthesis [assayed_using] PomBase:SPATRNAPHE.01	yW formation was impaired in the Sp trm734△ mutant (44% of wild-type levels) and to a lesser extent in the Sp trm732△ mutant (73%) (Fig. 4F), consistent with the increased m1G levels (Table 3; Fig. 4A)
PMID:25410910	GO:0001164	RNA polymerase I core promoter sequence-specific DNA binding [occurs_at] homol_D_box [part_of] transcription initiation at RNA polymerase I promoter	(comment: yes it looks like pol II?! (val: changed to DNA binding term))
PMID:25411334	FYPO:0000026	abnormal vegetative cell polarity	(Fig. S2A)
PMID:25411334	FYPO:0000026	abnormal vegetative cell polarity	(Fig. S2A)
PMID:25411334	FYPO:0000026	abnormal vegetative cell polarity	(Fig. S2A)
PMID:25411338	GO:0031520	plasma membrane of cell tip	(comment: CHECK during cellular response to glucose starvation)
PMID:25411338	GO:0031520	plasma membrane of cell tip [exists_during] cellular response to glucose starvation	(comment: CHECK during cellular response to glucose starvation)
PMID:25411338	GO:0031520	plasma membrane of cell tip	(comment: CHECK during cellular response to glucose starvation)
PMID:25411338	GO:0031520	plasma membrane of cell tip	(comment: CHECK during cellular response to glucose starvation)
PMID:25411338	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] high	(comment: CHECK strong phenotype = has_severity(FYPO_EXT:0000001))
PMID:25411338	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] high	(comment: CHECK strong phenotype = has_severity(FYPO_EXT:0000001))
PMID:25411338	FYPO:0004839	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during glucose starvation [assayed_using] PomBase:SPCC1235.14	The Ght5 protein, which is localized on the plasma membrane in the WT, fails to be localized on the plasma membrane, accumulating in the cytoplasm.
PMID:25411338	FYPO:0004839	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during glucose starvation [assayed_using] PomBase:SPCC1235.14	The Ght5 protein, which is localized on the plasma membrane in the WT, fails to be localized on the plasma membrane, accumulating in the cytoplasm.
PMID:25411338	FYPO:0004839	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during glucose starvation [assayed_using] PomBase:SPCC1235.14	The Ght5 protein, which is localized on the plasma membrane in the WT, fails to be localized on the plasma membrane, accumulating in the cytoplasm.
PMID:25411338	FYPO:0004839	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during glucose starvation [assayed_using] PomBase:SPCC1235.14	The Ght5 protein, which is localized on the plasma membrane in the WT, fails to be localized on the plasma membrane, accumulating in the cytoplasm.
PMID:25411338	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPCC1235.14	The ght5 gene, the transcription of which is repressed in the WT cells, is transcribed at a high level in the presence of 111 mM glucose in the scr1 delta cells.
PMID:25411338	FYPO:0003032	decreased RNA level during glucose starvation [assayed_using] PomBase:SPCC1235.14	the level of ght5 transcription, which increases in the WT during glucose limitation, fails to increase in this mutant cells in low-glucose medium.
PMID:25411338	FYPO:0003032	decreased RNA level during glucose starvation [assayed_using] PomBase:SPCC1235.14	the level of ght5 transcription, which increases in the WT during glucose limitation, fails to increase in this mutant cells in low-glucose medium.
PMID:25414342	FYPO:0005657	normal frequency of meiotic crossover associated with gene conversion	(Fig. 4C, Table S5)
PMID:25414342	FYPO:0005657	normal frequency of meiotic crossover associated with gene conversion	(Fig. 5, Table S6)
PMID:25414342	FYPO:0003891	normal intragenic meiotic recombination	(Table S2)
PMID:25414342	FYPO:0005578	normal intergenic meiotic recombination	(Table S2)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 0.42% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 0.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S3)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 1.7% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 2B, Table S3)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 10.34% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2D, Table S6)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 10.5% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 2B, Table S3)
PMID:25414342	FYPO:0005658	abnormal frequency of meiotic crossover associated with gene conversion	(comment: CHECK 101.33% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; higher than rlp1Δ-7, lower than fml1Δ, skewed recombinant categories) (Figs. 5C, 7A, Table S6)
PMID:25414342	FYPO:0005658	abnormal frequency of meiotic crossover associated with gene conversion	(comment: CHECK 101.4% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant categories) (Fig. 5D, Table S6)
PMID:25414342	FYPO:0005658	abnormal frequency of meiotic crossover associated with gene conversion	(comment: CHECK 101.76% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant categories) (Figs. 5E, 7A, Table S6)
PMID:25414342	FYPO:0005658	abnormal frequency of meiotic crossover associated with gene conversion	(comment: CHECK 102.17% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, higher than rdl1Δ-25, lower than fml1Δ, skewed recombinant categories) (Fig. S3, Table S6)
PMID:25414342	FYPO:0004993	normal spore germination frequency	(comment: CHECK 104.8% of wild-type spore viability) (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005657	normal frequency of meiotic crossover associated with gene conversion	(comment: CHECK 106.7% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0004993	normal spore germination frequency	(comment: CHECK 108.5% of wild-type spore viability) (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005659	increased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 111.2% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant classes) (Figs. 5E, 7A, Table S6)
PMID:25414342	FYPO:0005659	increased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 111.64% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 5B, Table S6)
PMID:25414342	FYPO:0005659	increased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 114.54% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant categories) (Fig. 5D, Table S6)
PMID:25414342	FYPO:0005659	increased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 115.12% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. 5A, Table S6)
PMID:25414342	FYPO:0005659	increased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 115.17% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 5A, Table S6)
PMID:25414342	FYPO:0005659	increased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 116.19% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. 5C, Table S6)
PMID:25414342	FYPO:0005659	increased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 117% of wild-type recombination assayed at various loci) (Fig. 1, Table S2)
PMID:25414342	FYPO:0004993	normal spore germination frequency	(comment: CHECK 117.1% of wild-type spore viability) (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005659	increased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 119.91% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 5A, Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 12.19% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2B, Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 12.3% of wild-type recombination assayed between ade6-3083 and ade6-469) (Table S3)
PMID:25414342	FYPO:0005659	increased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 122.65% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 5D, Table S6)
PMID:25414342	FYPO:0005659	increased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 124.3% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship - similar to fml1delta) (Fig. 5, Table S6)
PMID:25414342	FYPO:0005659	increased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 127.22% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. 5B, Table S6)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 13.0% of wild-type spore viability, synergistic relationship) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 13.87% of wild-type spore viability) (Table S6)
PMID:25414342	FYPO:0005659	increased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 130.25% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. 5C, Table S6)
PMID:25414342	FYPO:0004993	normal spore germination frequency	(comment: CHECK 133.5% of wild-type spore viability) (Fig. 3D, Table S4)
PMID:25414342	FYPO:0005659	increased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 136.75% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. 5B, Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 14.2% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 15.19% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 15.4% of wild-type spore viability, synergistic relationship) (Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 15.53% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 15.59% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 2D, Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 16.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 18.5% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 19.1% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S3)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 2.1% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 2.2% of wild-type recombination assayed between ade6-3083 and ade6-469) (Table S3)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 2.5% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 2.55% of wild-type recombination assayed between ade6-3083 and ade6-469, synergistic relationship) (Fig. 2A, Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 20.15% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S6)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 20.24% of wild-type spore viability) (Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 21.1% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 21.2% of wild-type spore viability, 8.3-fold higher spore viability than mus81 single mutant) (Fig. 2A, Table S3)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 21.45% of wild-type spore viability, synergistic relationship) (Table S6)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 21.46% of wild-type spore viability, synergistic relationship) (Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 24.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 25.7% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 25.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 26.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S3)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 26.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 27.08% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2D, Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 27.7% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 3A, Table S4)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 28.85% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 28.9% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 28.9% of wild-type spore viability, 11.3-fold higher spore viability than mus81 single mutant) (Fig. 2A, Table S3)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 3.55% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 2A, Table S6)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 3.68% of wild-type spore viability, synergistic relationship) (Table S6)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 3.7% of wild-type spore viability, synergistic relationship) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 30.1% of wild-type recombination assayed between ade6-3083 and ade6-469) (Table S3)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 30.92% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 31.1% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Table S5)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 31.18% of wild-type spore viability) (Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 31.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 32.13% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 32.3% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 3A, Table S4)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 33.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 35.42% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2B, Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 36.3% of wild-type recombination assayed between ade6-3083 and ade6-469) (Table S3)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 36.88% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2C, Table S6)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 37.75% of wild-type spore viability, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 37.89% of wild-type recombination assayed between ade6-3083 and ade6-469, similar to dmc1Δ-12 and rlp1Δ single mutants, but higher than dmc1Δ-12 rlp1Δ double mutant) (Fig. 2E, Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 38.89% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 39.7% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 4.11% of wild-type spore viability) (Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 4.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, synergistic relationship) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 42.4% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 3A, Table S4)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 42.9% of wild-type spore viability, 16.7-fold higher spore viability than mus81 single mutant) (Fig. 2A, Table S3)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 43.6% of wild-type spore viability) (Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 44.4% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 3A, Table S4)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 44.7% of wild-type spore viability, 17.4-fold higher spore viability than mus81 single mutant) (Fig. 2A, Table S3)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 45.45% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 46.52% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 47% of wild-type spore viability) (Fig. 2A, Table S3), (comment: 18.3-fold higher spore viability than mus81 single mutant)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 48.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Fig. 3B, Table S4)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 48.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Fig. 2B, Table S4)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 49.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Fig. 3B, Table S4)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 49.2% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 3A, Table S4)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 49.8% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 50.7% of wild-type spore viability, synergistic relationship) (Table S5)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 52.08% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 53.76% of wild-type spore viability, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 54.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S5)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 54.78% of wild-type spore viability, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 55.49% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 55.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Fig. 3B, Table S4)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 55.5% of wild-type spore viability, synergistic relationship) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 55.62% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, partial rescue from rad55Δ levels) (Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 57.9% of wild-type recombination assayed between ade6-3083 and ade6-469) (Table S3)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 58.1% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S3)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 59.57% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 6.4% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Table S3)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 6.87% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2E, Table S6)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 6.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 2B, Table S3)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 60.64% of wild-type spore viability, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 61.0% of wild-type recombination assayed between ura4+-aim2 and his3+-aim) (Fig. 3B, Table S4)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 61.1% of wild-type spore viability) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 65.3% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Fig. 4B, Table S5)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 69.41% of wild-type recombination assayed between ura4+-aim2 and his3+-aim, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 7.2% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship - similar to rqh1delta) (Fig. 6, Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 7.33% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2C, Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 7.4% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2A, Table S6)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 7.8% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 2B, Table S3)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 7.8% of wild-type spore viability, synergistic relationship) (Table S6)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 73.46% of wild-type spore viability, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 75.2% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship) (Fig. S2, Table S5)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	(comment: CHECK 76.1% of wild-type recombination assayed between ade6-3083 and ade6-469) (Table S6)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 76.7% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, synergistic relationship; skewed recombinant classes) (Figs. 4C, 7A, Table S5)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 76.9% of wild-type spore viability, epistatic relationship) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 77.7% of wild-type spore viability) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 78.4% of wild-type spore viability) (Table S2)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 78.6% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 3C, Table S4)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 79.92% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim; skewed recombinant categories) (Figs. 5E, 7A, Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 8.0% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 6, Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 8.33% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2C, Table S6)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 8.87% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2B, Table S6)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 82.2% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 3C, Table S4)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 82.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 83.9% of wild-type spore viability) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 84.1% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 85.8% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 3C, Table S4)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 85.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 87.6% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 9.7% of wild-type recombination assayed between ade6-3083 and ade6-469) (Fig. 4A, Table S5)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	(comment: CHECK 9.88% of wild-type recombination assayed between ade6-3083 and ade6-469, epistatic relationship) (Fig. 2E, Table S6)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 9.9% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 2B, Table S3)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 9.9% of wild-type spore viability, synergistic relationship) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 90.5% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim) (Fig. 3C, Table S4)
PMID:25414342	FYPO:0005660	decreased frequency of meiotic crossover associated with gene conversion	(comment: CHECK 91.4% of wild-type recombination assayed between ura4+-aim2 - ade6-3083 and ade6-469 - his3+-aim, epistatic relationship) (Fig. 4C, Table S5)
PMID:25414342	FYPO:0004993	normal spore germination frequency	(comment: CHECK 91.68% of wild-type spore viability, epistatic relationship) (Table S6)
PMID:25414342	FYPO:0000581	decreased spore germination frequency	(comment: CHECK 93.8% of wild-type spore viability, epistatic relationship) (Fig. 4D, Table S5)
PMID:25414342	FYPO:0004993	normal spore germination frequency	(comment: CHECK 95.2% of wild-type spore viability) (Fig. 3D, Table S4)
PMID:25414342	FYPO:0003179	decreased intragenic meiotic recombination	33.7% of wild-type recombination assayed between ade6-3083 and ade6-469 (Fig. 4A, Table S5)
PMID:25414342	FYPO:0002485	decreased intergenic meiotic recombination	38.5% of wild-type recombination assayed between ura4+-aim2 and his3+-aim (Fig. 4B, Table S5)
PMID:25417108	FYPO:0003103	decreased mRNA-derived small RNA level	(comment: Affecting Dcr1-terminated genes)
PMID:25417108	FYPO:0004820	increased number of Rad52 foci at rDNA replication pause sites	(comment: Affecting Rad52 enrichment at rDNA)
PMID:25417108	FYPO:0004819	increased number of Rad52 foci at rDNA replication origins	(comment: Affecting Rad52 enrichment at rDNA)
PMID:25417108	FYPO:0004817	decreased rDNA antisense small RNA level	(comment: affecting antisense transcription at rDNA)
PMID:25417108	FYPO:0004818	decreased tDNA antisense small RNA level	(comment: affecting antisense transcription at tDNA)
PMID:25417108	FYPO:0004812	abnormal termination of RNA polymerase II transcription at rDNA	(comment: affecting highly transcribed genes, antisense transcription of tDNA and rDNA)
PMID:25417108	FYPO:0004814	abnormal termination of RNA polymerase II transcription at highly transcribed protein-coding genes	(comment: affecting highly transcribed genes, antisense transcription of tDNA and rDNA)
PMID:25417108	FYPO:0004813	abnormal termination of RNA polymerase II transcription at tDNA	(comment: affecting highly transcribed genes, antisense transcription of tDNA and rDNA)
PMID:25417108	GO:0006386	termination of RNA polymerase III transcription	(comment: occurs at rDNA, tRNA gene, protein coding gene)
PMID:25417108	GO:0006363	termination of RNA polymerase I transcription	(comment: occurs at rDNA, tRNA gene, protein coding gene)
PMID:25417108	GO:0006369	termination of RNA polymerase II transcription	(comment: occurs at rDNA, tRNA gene, protein coding gene)
PMID:25417108	FYPO:0002980	increased chromatin binding [assayed_using] PomBase:SPBC342.05 [assayed_using] tRNA_gene	(comment: occurs at tDNA)
PMID:25428589	FYPO:0007407	increased level of phosphate starvation gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	(repressed condition; Fig. 1c)
PMID:25428589	FYPO:0000091	sensitive to thiabendazole [has_severity] high	Cells lacking SPNCRNA.1343 (ncRNA.1343 for short) displayed a phenotype: hypersensitivity to TBZ, HU and caffeine but not to temperature extremities, ultraviolet-irradiation or oxidative stress (Supplementary Fig. 1c and Supplementary Fig. 2).
PMID:25428589	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1698	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	In addition, the transcript levels of tgp1þ, nc-tgp1, nc-1343, pho1þ and nc-pho1 were unaffected by loss of RNAi (for example, ago1D or dcr1D) or heterochromatin components (for example, clr4D or swi6D) (Fig. 5b; Supplementary Fig. 7a
PMID:25428589	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth	In agreement with this, significantly less RNAPII associates with the nc-tgp1 transcription unit in both phosphate-starved wild-type cells and phosphate-replete 1343D cells, which do not transcribe nc-tgp1 (Fig. 4c).
PMID:25428589	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1712	In contrast, nc-tgp1, nc-pho1 and sme2þ RNA levels were clearly elevated in cells lacking Mmi1-mediated exosome degradation (mmi1D and rrp6D). Th
PMID:25428589	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1698	Northern analysis identified that an B1.9kb nc-tgp1 RNA accumulates in rrp6D, mmi1D and red1D, but not in wild-type cells (Fig. 2e,f; Supplementary Fig. 4).
PMID:25428589	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1698	Northern analysis identified that an B1.9kb nc-tgp1 RNA accumulates in rrp6D, mmi1D and red1D, but not in wild-type cells (Fig. 2e,f; Supplementary Fig. 4).
PMID:25428589	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1698	Northern analysis identified that an B1.9kb nc-tgp1 RNA accumulates in rrp6D, mmi1D and red1D, but not in wild-type cells (Fig. 2e,f; Supplementary Fig. 4).
PMID:25428589	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1271.09 [happens_during] cellular response to phosphate starvation	Our ChIP analyses confirmed that Pho7-green fluorescent protein (Pho7-GFP) accumulates on the pho1 þ promoter in phosphate- depleted cells (Supplementary Fig. 8). In addition, Pho7-GFP levels accumulate over the region upstream of tgp1þ when activated (Fig. 6a
PMID:25428589	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1343	The size and levels of the nc-1343 transcript increased in exosome defective (rrp6D) cells, but not cells lacking Mmi1 or Red1 (Fig. 2c,d; Supplementary Fig. 4). T
PMID:25428589	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1343	The size and levels of the nc-1343 transcript increased in exosome defective (rrp6D) cells, but not cells lacking Mmi1 or Red1 (Fig. 2c,d; Supplementary Fig. 4). T
PMID:25428589	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1343	The size and levels of the nc-1343 transcript increased in exosome defective (rrp6D) cells, but not cells lacking Mmi1 or Red1 (Fig. 2c,d; Supplementary Fig. 4). T
PMID:25428589	FYPO:0000964	normal growth on thiabendazole [has_severity] high	To determine whether the drug sensitivity of 1343D cells is a direct result of increased tgp1þ expression, the tgp1þ gene was deleted from 1343D cells (tgp1D1343D). This manipulation restored TBZ, HU and caffeine tolerance to levels comparable with wild-type cells (Fig. 1d). We conclude that increased tgp1þ expression is directly responsible for the drug-sensitivity phenotype of cells lacking ncRNA.1343.
PMID:25428589	FYPO:0000964	normal growth on thiabendazole	Truncations of nc-1343 (that is, AD and BD) that retain its 50 end did not result in the drug-sensitivity phenotype presented by 1343D cells (Fig. 3b) and, similarly, did not induce tgp1þ expression (Fig. 3c)
PMID:25428589	FYPO:0000964	normal growth on thiabendazole	Truncations of nc-1343 (that is, AD and BD) that retain its 50 end did not result in the drug-sensitivity phenotype presented by 1343D cells (Fig. 3b) and, similarly, did not induce tgp1þ expression (Fig. 3c)
PMID:25428589	GO:0106222	lncRNA binding [occurs_in] DSR_motif	We identified a consensus DSR motif for Mmi1 binding at position þ820 nt within the nc-tgp1 transcript and RNA IP (RIP) experiments confirmed a direct interaction between Mmi1 and the nc-tgp1 RNA (Supplementary Fig. 5).
PMID:25428589	GO:0060633	negative regulation of transcription initiation by RNA polymerase II [has_input] PomBase:SPBC1271.09	We therefore conclude that tgp1(+) is regulated by transcriptional interference.
PMID:25428589	FYPO:0000091	sensitive to thiabendazole [has_severity] high	prevented nc-tgp1 transcription, induced tgp1þ expression to levels observed in 1343D levels and increased sensitivity of these cells to TBZ, HU and caffeine (Fig. 3b,c). These analyses demonstrate that it is nc-tgp1, not nc-1343, that is critical for repressing tgp1þ in the presence of phosphate.
PMID:25428987	GO:1902716	cell cortex of growing cell tip [exists_during] mitotic interphase	(comment: CHECK mitotic interphase)
PMID:25451933	FYPO:0006187	normal rate of actomyosin contractile ring assembly	(Figs. 6B and C, Table 3)
PMID:25451933	GO:0003786	actin lateral binding	(comment: competatively with cofilin)
PMID:25451933	FYPO:0007573	premature actomyosin contractile ring contraction with increased contraction rate	As a result, ring constriction in Δaip1 cells takes ∼ 5 min less than in wild type cells (Table 3). Overall, cytokinesis was ∼16 min (24%) faster in Δaip1 cells than wild type cells, because the maturation period was shorter and the rings constricted faster.
PMID:25451933	GO:0051014	actin filament severing	SpAip1 dramatically stimulated severing by 100 nM cofilin, with a maximum rate at 1.5 μM SpAip1 and lower rates at higher concentrations (Fig. 3C).At all SpAip1 concentrations tested ∼80% of new barbed ends created by severing events depolymerized (Fig. 3D) at rates that decreased insignificantly with SpAip1 concentration (Fig. 3E). These depolymerization rates were higher than published values (2), likely because severing near barbed ends was difficult to distinguish from filament depolymerization.
PMID:25451933	FYPO:0007573	premature actomyosin contractile ring contraction with increased contraction rate	Surprisingly, contractile rings began to constrict earlier in Δaip1 cells than wild type cells (Fig. 7, A and B, and Table 3), foreshortening the maturation period before constriction
PMID:25451933	FYPO:0001366	normal actin cytoskeleton organization	The fission yeast lacking Aip1 have normal appearing actin patches, cables, and contractile rings (Fig. 5B).
PMID:25471935	FYPO:0005764	increased replication fork pausing at G4 motif	(comment: assayed Cdc20 recruitment)
PMID:25472718	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:25472718	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1A)
PMID:25472718	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] >30	(Fig. 1A)
PMID:25472718	FYPO:0000324	mitotic metaphase/anaphase transition delay [has_penetrance] 53	(Fig. 1C-E) (comment: Type I)
PMID:25472718	FYPO:0001513	normal mitotic sister chromatid segregation [has_penetrance] 53	(Fig. 1C-E) (comment: Type I)
PMID:25472718	FYPO:0000324	mitotic metaphase/anaphase transition delay [has_penetrance] low	(Fig. 1C-E) (comment: Type I)
PMID:25472718	FYPO:0000324	mitotic metaphase/anaphase transition delay [has_severity] high	(Fig. 1C; Fig. 3D)
PMID:25472718	FYPO:0001513	normal mitotic sister chromatid segregation [has_penetrance] high	(Fig. 1C; Fig. 3D)
PMID:25472718	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 2A)
PMID:25472718	FYPO:0000674	normal cell population growth at high temperature	(Fig. 2A)
PMID:25472718	FYPO:0001387	loss of viability at high temperature	(Fig. 2A)
PMID:25472718	FYPO:0002902	decreased protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPBC2F12.13 [assayed_using] PomBase:SPBC1685.15c	(Fig. 2C,D)
PMID:25472718	FYPO:0000069	resistance to thiabendazole [has_severity] low	(Fig. 3A)
PMID:25472718	FYPO:0000674	normal cell population growth at high temperature	(Fig. 3A)
PMID:25472718	FYPO:0000674	normal cell population growth at high temperature	(Fig. 3A)
PMID:25472718	FYPO:0000674	normal cell population growth at high temperature	(Fig. 3A)
PMID:25472718	FYPO:0000069	resistance to thiabendazole [has_severity] low	(Fig. 3C)
PMID:25472718	FYPO:0000324	mitotic metaphase/anaphase transition delay [has_penetrance] 25	(Fig. 3d)
PMID:25472718	FYPO:0002901	normal protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPCC895.07	(Fig. 4A,B)
PMID:25472718	FYPO:0002901	normal protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPAC890.02c	(Fig. 4A,B)
PMID:25472718	FYPO:0001905	normal mitotic spindle microtubules	(Fig. 4C,D)
PMID:25472718	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC890.02c [assayed_using] PomBase:SPBC2F12.13 [has_severity] high	(Fig. 4E) reduced by >70%
PMID:25472718	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC890.02c [assayed_using] PomBase:SPBC2F12.13 [has_severity] high	(Fig. 4E) reduced by >70%
PMID:25472718	FYPO:0001387	loss of viability at high temperature	(Fig. 5A)
PMID:25472718	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 10	(Fig. 5A)
PMID:25472718	FYPO:0004310	normal duration of mitotic M phase	(Fig. 5A)
PMID:25472718	FYPO:0004307	long mitotic spindle during metaphase	(Fig. 5D)
PMID:25472718	FYPO:0006259	normal mitotic spindle length during metaphase	(Fig. 5D)
PMID:25472718	FYPO:0001387	loss of viability at high temperature	(Fig. S2B)
PMID:25472718	FYPO:0001387	loss of viability at high temperature	(Fig. S2B)
PMID:25472718	FYPO:0002061	inviable vegetative cell population	(supplementary material Fig. S1A
PMID:25472718	GO:0140210	protein transport along microtubule to kinetochore [has_input] PomBase:SPBC2F12.13 [has_input] PomBase:SPBC1685.15c	In any case, the results shown here imply that Klp5-Klp6 localises to the kinetochores through interaction with the Alp7-Alp14 complex.
PMID:25472718	GO:0140210	protein transport along microtubule to kinetochore [has_input] PomBase:SPBC2F12.13 [has_input] PomBase:SPBC1685.15c	In any case, the results shown here imply that Klp5-Klp6 localises to the kinetochores through interaction with the Alp7-Alp14 complex.
PMID:25472718	GO:0140210	protein transport along microtubule to kinetochore [has_input] PomBase:SPBC776.02c	Overall, our data suggest that Klp5-Klp6 delivers PP1 to the attached kinetochores, thereby promoting SAC silencing.
PMID:25472718	GO:0140210	protein transport along microtubule to kinetochore [has_input] PomBase:SPBC776.02c	Overall, our data suggest that Klp5-Klp6 delivers PP1 to the attached kinetochores, thereby promoting SAC silencing.
PMID:25473118	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPAC1F7.04 [occurs_in] cell division site	(Fig. 6)
PMID:25473118	GO:0043495	protein-membrane adaptor activity [has_input] PomBase:SPCC645.06c [occurs_in] cell division site	(Fig. 6)
PMID:25473118	GO:0032153	cell division site [exists_during] mitotic anaphase B	(comment: independent of actin)
PMID:25473118	FYPO:0003339	decreased rate of actomyosin contractile ring assembly	the ring seems to start off forming normally but maturation is delayed, this leads to delayed constriction.
PMID:25487150	GO:0005515	protein binding	(comment: unphosphorylated form)
PMID:25500221	FYPO:0004572	decreased exocytosis during vegetative growth [has_severity] medium	(comment: secretion of acid phosphatase)
PMID:25500221	FYPO:0004572	decreased exocytosis during vegetative growth [has_severity] medium	(comment: secretion of acid phosphatase)
PMID:25501814	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic anaphase B	(Fig. 1)
PMID:25501814	GO:0044732	mitotic spindle pole body [exists_during] mitotic anaphase	(Fig. 1)
PMID:25501814	GO:0044732	mitotic spindle pole body [exists_during] mitotic metaphase	(Fig. 1)
PMID:25501814	GO:0044732	mitotic spindle pole body [exists_during] mitotic anaphase	(Fig. 1)
PMID:25501814	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic telophase	(Fig. 1)
PMID:25501814	GO:0044732	mitotic spindle pole body [exists_during] mitotic interphase	(Fig. 1)
PMID:25501814	GO:0110115	Cdr2 medial cortical node complex [exists_during] mitotic G2 phase	(Fig. 1c)
PMID:25501814	FYPO:0007575	decreased duration of protein localization to medial cortical node [assayed_using] PomBase:SPAC57A10.02	(Fig. 2g)
PMID:25501814	FYPO:0007574	decreased duration of protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC57A10.02	(Fig. 3C).
PMID:25501814	FYPO:0001837	increased duration of protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC21.06c	Cdc7p-GFP never disappeared from the old SPB (Sohrmann et al., 1998) and the type 1 nodes did not reform (Fig. 3B; supplementary material Movie 3)
PMID:25519804	FYPO:0003911	UGA suppression [has_severity] high	(comment: CHECK high suppression of phenotype)
PMID:25519804	FYPO:0003911	UGA suppression [has_severity] high	(comment: CHECK high suppression of phenotype)
PMID:25519804	FYPO:0003911	UGA suppression	(comment: efficient suppression of ade6-M26; very poor suppression of ade6-M375)
PMID:25519804	FYPO:0003911	UGA suppression [has_severity] low	(comment: low suppression of phenotype)
PMID:25519804	FYPO:0003911	UGA suppression	(comment: suppresses ade6-M26 efficiently; suppresses ade6-M375 weakly)
PMID:25520186	MOD:00047	O-phospho-L-threonine	(comment: Auto-phosphorylation occurred in the presence of ATP in vitro)
PMID:25520186	MOD:00047	O-phospho-L-threonine	(comment: Auto-phosphorylation occurred in the presence of ATP in vitro)
PMID:25520186	MOD:00047	O-phospho-L-threonine	(comment: Auto-phosphorylation occurred in the presence of ATP in vitro)
PMID:25520186	MOD:00047	O-phospho-L-threonine	(comment: Auto-phosphorylation occurred in the presence of ATP in vitro)
PMID:25520186	MOD:00047	O-phospho-L-threonine	(comment: Auto-phosphorylation occurred in the presence of ATP in vitro)
PMID:25520186	MOD:00046	O-phospho-L-serine	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	MOD:00046	O-phospho-L-serine	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	MOD:00046	O-phospho-L-serine	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	MOD:00583	thiophosphorylated residue	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	MOD:00046	O-phospho-L-serine	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	MOD:00046	O-phospho-L-serine	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	MOD:00046	O-phospho-L-serine	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	MOD:00046	O-phospho-L-serine	(comment: Auto-thiophosphorylation occurred in the presence of ATP gamma-S in vitro)
PMID:25520186	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPBC146.03c	(comment: CHECK full-length Cut14 present; not sure how to interpret this)
PMID:25520186	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPBC146.03c	(comment: CHECK full-length Cut14 present; not sure how to interpret this)
PMID:25520186	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPBC146.03c	(comment: CHECK full-length Cut14 present; not sure how to interpret this)
PMID:25520186	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPBC146.03c	(comment: of condensin complex)
PMID:25520186	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPBP4H10.06c	(comment: of condensin complex)
PMID:25520186	FYPO:0002060	viable vegetative cell population	(comment: only captured the OEX Experiment)
PMID:25520186	FYPO:0002061	inviable vegetative cell population	(comment: only captured the OEX experiment)
PMID:25533340	FYPO:0003584	increased double-strand break repair via nonhomologous end joining	(comment: CHECK increased end-joining activity in vegetative cells)
PMID:25533340	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09 [added_during] mitotic G2 phase	(comment: CHECK phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining S192)
PMID:25533340	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09 [absent_during] mitotic G1 phase	(comment: CHECK phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining S192)
PMID:25533340	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC11B10.09 [absent_during] mitotic G1 phase	(comment: CHECK phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining T180)
PMID:25533340	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC11B10.09 [added_during] mitotic G2 phase	(comment: CHECK phosphorylated by cdc2 phosphorylated in G2 phase inhibits nonhomologous end joining T180)
PMID:25533340	GO:2001033	negative regulation of double-strand break repair via nonhomologous end joining [happens_during] mitotic G2 phase	(comment: This looks like direct regulation because it phosphorylates xlf1)
PMID:25533340	FYPO:0000482	decreased mitotic recombination	(comment: leu1)
PMID:25533348	GO:0000122	negative regulation of transcription by RNA polymerase II [has_input] PomBase:SPBC428.18	(Fig. 3A)
PMID:25533348	GO:0000122	negative regulation of transcription by RNA polymerase II [has_input] PomBase:SPCC553.07c	(Fig. 3A)
PMID:25533348	GO:0000122	negative regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC17H9.19c	(Fig. 3A)
PMID:25533348	GO:0000122	negative regulation of transcription by RNA polymerase II [has_input] PomBase:SPCC338.17c	(Fig. 3A)
PMID:25533348	GO:0000122	negative regulation of transcription by RNA polymerase II [has_input] PomBase:SPBC660.14	(Fig. 3A)
PMID:25533348	GO:0000122	negative regulation of transcription by RNA polymerase II [has_input] PomBase:SPAP14E8.02	(Fig. 3A)
PMID:25533348	GO:0000122	negative regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC1F7.05	(Fig. 3A)
PMID:25533348	GO:0000122	negative regulation of transcription by RNA polymerase II [has_input] PomBase:SPBC14C8.07c	(Fig. 3A)
PMID:25533348	GO:0000122	negative regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC644.05c	(Fig. 3A)
PMID:25533348	GO:0000122	negative regulation of transcription by RNA polymerase II [has_input] PomBase:SPAPB2B4.03	(Fig. 3A)
PMID:25533348	GO:0000122	negative regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC644.14c	(Fig. 3A)
PMID:25533348	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] 27	(comment: WT 3%)
PMID:25533348	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] 22	(comment: WT 3%)
PMID:25533348	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] 7	(comment: WT 3%)
PMID:25533348	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPBC14C8.07c	(comment: WT 3%)
PMID:25533348	FYPO:0001122	elongated vegetative cell [has_severity] high [has_severity] variable severity	(comment: greater range of lengths)
PMID:25533348	FYPO:0001122	elongated vegetative cell [has_severity] high [has_severity] variable severity	(comment: greater range of lengths)
PMID:25533348	FYPO:0001122	elongated vegetative cell [has_severity] low	(comment: same range of lengths as WT)
PMID:25533956	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPAC23C11.16	(Fig. 5e)
PMID:25533956	FYPO:0004764	normal protein localization to meiotic spindle pole body during meiosis I [assayed_using] PomBase:SPAC23C11.16	(Fig. 5e)
PMID:25533956	GO:0140483	kinetochore adaptor activity [has_input] PomBase:SPAC23C11.16	(comment: RECRUITS)
PMID:25543137	FYPO:0004808	increased cellular protein aggregate level during cellular response to heat	(comment: A prionogenic reporter (S. cerevisiae Sup35 prion domain) aggregates in cytoplasmic inclusions in dcr1Δ)
PMID:25543137	FYPO:0004810	decreased protein localization to nucleus, with protein mislocalized to cytoplasmic foci [assayed_using] PomBase:SPCC188.13c	(comment: Dcr1 is not released from cytoplasmic inclusions at 37°C in hsp104Î)
PMID:25543137	GO:0033562	co-transcriptional gene silencing by RNA interference machinery [has_input] PomBase:SPBC16D10.08c	(comment: Dcr1 represses hsp104 levels)
PMID:25543137	GO:0042026	protein refolding	(comment: hsp104 refolds dicer and is required for robust centromeric silencing at 37°C)
PMID:25543137	GO:0005737	cytoplasm [exists_during] cellular response to heat	Cytoplasmic localisation in electron-dense inclusions at 37°C
PMID:25543137	GO:0005737	cytoplasm [exists_during] cellular response to heat	Dcr1 localizes in electron-dense cytoplasmic inclusions at 37°C together with hsp104. Hsp104 is required for dissolution of these inclusions.
PMID:25543137	GO:0005737	cytoplasm	Diffuse cytoplasmic localisation at 37°C, no stress granules
PMID:25543137	GO:0005634	nucleus	Nuclear localization at 30°C
PMID:25543137	GO:0005634	nucleus	Nuclear localization at 30°C
PMID:25590601	MOD:00046	O-phospho-L-serine [added_during] cellular response to glucose stimulus	(comment: CHECK removed during glucose starvation) (comment: CHECK observed during nitrogen starvation) (comment: CHECK S546)
PMID:25590601	MOD:00046	O-phospho-L-serine [removed_during] cellular response to glucose starvation	(comment: CHECK removed during glucose starvation) (comment: CHECK observed during nitrogen starvation) (comment: CHECK S546)
PMID:25590601	MOD:00046	O-phospho-L-serine [present_during] cellular response to nitrogen starvation	(comment: CHECK removed during glucose starvation) (comment: CHECK observed during nitrogen starvation) (comment: CHECK S546)
PMID:25590601	MOD:00047	O-phospho-L-threonine [removed_during] cellular response to nitrogen starvation	(comment: CHECK removed during nitrogen starvation) (comment: T415)
PMID:25590601	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPCC24B10.07 [assayed_substrate] PomBase:SPBC16G5.15c [has_severity] high	(comment: CHECK strong phenotype = has_severity(FYPO_EXT:0000001))
PMID:25590601	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC16G5.15c [happens_during] cellular response to glucose stimulus	(comment: decreased during glucose starvation)
PMID:25590601	GO:1904515	positive regulation of TORC2 signaling [part_of] cellular response to glucose stimulus	(comment: in the presence of glucose)
PMID:25619765	FYPO:0000227	chromosome loss during mitotic chromosome segregation	(comment: cen2-lacO)
PMID:25619765	FYPO:0000227	chromosome loss during mitotic chromosome segregation	(comment: pNBg was used)
PMID:25619998	GO:0004596	protein-N-terminal amino-acid acetyltransferase activity [has_input] PomBase:SPAC1834.03c	(Figure S2)
PMID:25619998	GO:0004596	protein-N-terminal amino-acid acetyltransferase activity	(Figure S2)
PMID:25619998	GO:0004596	protein-N-terminal amino-acid acetyltransferase activity [has_input] PomBase:SPBC8D2.03c	(Figure S2)
PMID:25639242	FYPO:0007434	attenuated change in cell size at division upon shift to poor nitrogen source	(Fig. 3C)
PMID:25639242	FYPO:0007434	attenuated change in cell size at division upon shift to poor nitrogen source	(Fig. 3G)
PMID:25639242	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC31G5.12c	(Fig. 4C)
PMID:25639242	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC74.03c	(Fig. 6A)
PMID:25639242	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC74.03c	(Fig. 6G)
PMID:25639242	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC74.03c	(Fig. S4C,D)
PMID:25639242	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC31G5.12c	(Figure 2D,4B)
PMID:25639242	FYPO:0007434	attenuated change in cell size at division upon shift to poor nitrogen source	(Figure 2a)
PMID:25639242	FYPO:0007434	attenuated change in cell size at division upon shift to poor nitrogen source	(Figure 2a)
PMID:25639242	FYPO:0001492	viable elongated vegetative cell [has_severity] low	(Figure 2b) (comment: 9% longer)
PMID:25639242	FYPO:0007434	attenuated change in cell size at division upon shift to poor nitrogen source	(Figure 3B)
PMID:25639242	FYPO:0005206	abnormal mitotic cell cycle regulation upon nitrogen source shift	(Figure 3F)
PMID:25639242	FYPO:0007434	attenuated change in cell size at division upon shift to poor nitrogen source	(Figure 3F) (comment: DECOUPLED CELL GROWTH AND DIVISION)
PMID:25639242	FYPO:0007434	attenuated change in cell size at division upon shift to poor nitrogen source	(Figure 3d)
PMID:25639242	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC31G5.12c	(Figure 4C)
PMID:25639242	FYPO:0007434	attenuated change in cell size at division upon shift to poor nitrogen source	(Figure 4D)
PMID:25639242	FYPO:0007434	attenuated change in cell size at division upon shift to poor nitrogen source	(Figure 4D)
PMID:25639242	FYPO:0007434	attenuated change in cell size at division upon shift to poor nitrogen source	(Figure 4E)
PMID:25639242	FYPO:0005036	abolished protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPCC74.03c	(Figure 5a)
PMID:25639242	FYPO:0007434	attenuated change in cell size at division upon shift to poor nitrogen source	(Figure 6E)
PMID:25639242	FYPO:0007434	attenuated change in cell size at division upon shift to poor nitrogen source	(Figure 6E)
PMID:25639242	FYPO:0005035	normal protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPCC74.03c	(Figure S2)
PMID:25639242	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC74.03c	(Figure S2B)
PMID:25639242	FYPO:0002673	normal growth on torin1	(Figure S3A)
PMID:25639242	GO:0004674	protein serine/threonine kinase activity [part_of] negative regulation of TORC1 signaling	(comment: CHECK causally upstream of ssp2)
PMID:25639242	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC74.03c [part_of] negative regulation of TORC1 signaling [part_of] regulation of extent of cell growth [happens_during] cellular response to nitrogen starvation	(comment: CHECK causally upstream of ssp2)
PMID:25639242	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPCC74.03c	An increase in AMPKaSsp2 Thr189 phosphorylation was also observed in the cbs2 .D AMPKg .D double mutant (Figure S2F).
PMID:25639242	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC74.03c	However, no difference in CaMKKSsp1 protein levels or phos- ppk34 phorylation status was observed in CaMKK .D mutants compared with wild-type cells (Figures S4A and S4B
PMID:25639242	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPCC74.03c	However, no difference in CaMKKSsp1 protein levels or phos- ppk34 phorylation status was observed in CaMKK .D mutants compared with wild-type cells (Figures S4A and S4B
PMID:25688133	FYPO:0000729	delayed onset of actomyosin contractile ring assembly	(comment: 23% slower)
PMID:25688133	FYPO:0000729	delayed onset of actomyosin contractile ring assembly	(comment: 26% slower)
PMID:25688133	GO:1990808	F-bar domain binding	(comment: residues 20â€-40 in synthetic peptide/ dissociation constant of 1.1 nM)
PMID:25688133	GO:0106006	cytoskeletal protein-membrane anchor activity [part_of] mitotic actomyosin contractile ring assembly [has_input] PomBase:SPAC1F5.04c [happens_during] mitotic M phase [occurs_in] medial cortex	(comment: residues 20â€-40 in synthetic peptide/ dissociation constant of 1.1 nM)
PMID:25688133	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPAC1F5.04c	(comment: smears as does not self associate, but localizes to medial cortex)
PMID:25736293	FYPO:0000927	abolished horsetail movement [has_penetrance] 13	(Fig. 1C; supplementary material Fig. S1C)
PMID:25736293	FYPO:0000927	abolished horsetail movement [has_penetrance] 13	(Fig. 1C; supplementary material Fig. S1C)
PMID:25736293	FYPO:0000927	abolished horsetail movement [has_penetrance] 13	(Fig. 1C; supplementary material Fig. S1C)
PMID:25736293	FYPO:0005990	abnormal maintenance of protein location in cell cortex of cell tip during karyogamy [assayed_using] PomBase:SPAC458.04c	(Fig. 3B, Fig. S3B)
PMID:25736293	FYPO:0005990	abnormal maintenance of protein location in cell cortex of cell tip during karyogamy	(Fig. 3B, Fig. S3B) abolished microtubule cortical anchoring
PMID:25736293	GO:0051285	cell cortex of cell tip	(Fig. 4A)
PMID:25736293	GO:0035974	meiotic spindle pole body	(Fig. 5C)
PMID:25736293	GO:1903754	cortical microtubule plus-end	(Fig. 5C)
PMID:25736293	FYPO:0000927	abolished horsetail movement	(Fig. 5c)
PMID:25736293	FYPO:0005988	abolished microtubule anchoring at cell cortex of cell tip during meiotic cell cycle	(Fig. 5c)
PMID:25736293	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC216.02 [assayed_using] PomBase:SPBC646.17c	(Fig. 6a)
PMID:25736293	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC216.02 [assayed_using] PomBase:SPBC646.17c	(Fig. 6a)
PMID:25736293	FYPO:0005990	abnormal maintenance of protein location in cell cortex of cell tip during karyogamy [assayed_using] PomBase:SPAC458.04c	(Fig. 7A)
PMID:25736293	FYPO:0000903	decreased rate of microtubule depolymerization during vegetative growth	(Fig. 7F; supplementary material Table S1)
PMID:25736293	FYPO:0000903	decreased rate of microtubule depolymerization during vegetative growth	(Fig. 7F; supplementary material Table S1)
PMID:25736293	FYPO:0000903	decreased rate of microtubule depolymerization during vegetative growth	(Fig. 7F; supplementary material Table S1)
PMID:25736293	FYPO:0000903	decreased rate of microtubule depolymerization during vegetative growth	(Fig. 7F; supplementary material Table S1)
PMID:25736293	FYPO:0000903	decreased rate of microtubule depolymerization during vegetative growth	(Fig. 7F; supplementary material Table S1)
PMID:25736293	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 14	(Fig. 7a)
PMID:25736293	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 13	(Fig. 7a)
PMID:25736293	FYPO:0000964	normal growth on thiabendazole	(Fig. S1B)
PMID:25736293	FYPO:0002177	viable vegetative cell with normal cell morphology	(Fig. S1B)
PMID:25736293	FYPO:0002177	viable vegetative cell with normal cell morphology	(Fig. S1B)
PMID:25736293	FYPO:0002177	viable vegetative cell with normal cell morphology	(Fig. S1B)
PMID:25736293	FYPO:0000964	normal growth on thiabendazole	(Fig. S1B)
PMID:25736293	FYPO:0000964	normal growth on thiabendazole	(Fig. S1B)
PMID:25736293	FYPO:0000964	normal growth on thiabendazole	(Fig. S1B)
PMID:25736293	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 13	(Fig. S1B)
PMID:25736293	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 13	(Fig. S1B)
PMID:25736293	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 11	(Fig. S1B)
PMID:25736293	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 11	(Fig. S1B)
PMID:25736293	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC27D7.13c [assayed_using] PomBase:SPAC1805.08	(Fig. S4A)
PMID:25736293	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC27D7.13c [assayed_using] PomBase:SPAC1805.08	(Fig. S4A)
PMID:25736293	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC27D7.13c [assayed_using] PomBase:SPAC1805.08	(Fig. S4A)
PMID:25736293	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC27D7.13c [assayed_using] PomBase:SPAC1805.08	(Fig. S4A)
PMID:25736293	FYPO:0005991	normal protein localization to cell cortex of cell tip during karyogamy [assayed_using] PomBase:SPAC27D7.13c [assayed_using] PomBase:SPCC11E10.03	(Fig. S4B)
PMID:25736293	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC27D7.13c [assayed_using] PomBase:SPCC11E10.03	(Fig. S4B)
PMID:25736293	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC27D7.13c [assayed_using] PomBase:SPCC11E10.03	(Fig. S4B)
PMID:25736293	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC27D7.13c [assayed_using] PomBase:SPCC11E10.03	(Fig. S4B)
PMID:25736293	GO:0005515	protein binding	(Figure S2)
PMID:25736293	GO:0005515	protein binding	(Figure S2)
PMID:25736293	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC1347.12 [assayed_using] PomBase:SPAC27D7.13c	(Figure S2C)
PMID:25736293	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC1347.12 [assayed_using] PomBase:SPAC27D7.13c	(Figure S2C)
PMID:25736293	FYPO:0005988	abolished microtubule anchoring at cell cortex of cell tip during meiotic cell cycle	(comment: CHECK 3B?)
PMID:25736293	GO:0106006	cytoskeletal protein-membrane anchor activity [part_of] horsetail-astral microtubule organization	(comment: CHECK microtubule cortical anchor (microtubule site clamp) add to other dynactin complex)
PMID:25736293	GO:0106006	cytoskeletal protein-membrane anchor activity [part_of] horsetail-astral microtubule organization	(comment: CHECK microtubule cortical anchor (microtubule site clamp) add to other dynactin complex)
PMID:25736293	GO:0106006	cytoskeletal protein-membrane anchor activity [part_of] horsetail-astral microtubule organization	(comment: CHECK microtubule cortical anchor (microtubule site clamp) add to other dynactin complex)
PMID:25736293	GO:0106006	cytoskeletal protein-membrane anchor activity [part_of] horsetail-astral microtubule organization	(comment: CHECK microtubule cortical anchor (microtubule site clamp) add to other dynactin complex)
PMID:25736293	FYPO:0000928	abnormal protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPAC458.04c [has_severity] low	(comment: abnormal movement of dynein)
PMID:25736293	FYPO:0000928	abnormal protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPAC458.04c	(comment: abnormal movement of dynein)
PMID:25736293	GO:0005938	cell cortex	(comment: accumulates on shrinking microtubules) (Fig. 2B)
PMID:25736293	GO:0035974	meiotic spindle pole body	accumulates on shrinking microtubules (Fig. 2B)
PMID:25736293	GO:1903754	cortical microtubule plus-end	accumulates on shrinking microtubules (Fig. 2B)
PMID:25763975	FYPO:0005872	incomplete septum formed from asymmetrically located sites	Similarly, the division plane was positioned more asymmetrically in klp5Δ cells than in wild-type cells [Fig. 2(g)].
PMID:25763975	FYPO:0003302	nucleus mislocalized towards cell tip during mitotic interphase	To test these theoretical predictions, we measured the movements of the nucleus and of the SPB in a klp5Δ strain, which lacks the kinesin-8 motor Klp5 [Fig. 2(d)]. We observed that the nucleus is typically found farther away from the cell center in klp5Δ than in wild-type cells, as shown by the 1.7-fold larger standard deviation of the distribution of the nuclear position in klp5Δ cells, which is consistent with the prediction of the model [Figs. 2(b)
PMID:25778919	GO:0000781	chromosome, telomeric region [exists_during] mitotic metaphase	(Fig. 2A, 0-3 min, arrows)
PMID:25778919	FYPO:0005442	abnormal telomeric DNA separation	(Fig. 2C, 2D)
PMID:25778919	FYPO:0006267	increased telomere clustering and tethering at nuclear periphery during mitotic metaphase [has_penetrance] 86	(Fig. 2C, 2D) (comment: decreased telomere dispersion)
PMID:25778919	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B	(Fig. 2D)
PMID:25778919	FYPO:0004381	merotelic kinetochore attachment during mitosis [has_penetrance] 45	(Fig. 3)
PMID:25778919	FYPO:0004381	merotelic kinetochore attachment during mitosis [has_penetrance] 40	(Fig. 3)
PMID:25778919	FYPO:0004381	merotelic kinetochore attachment during mitosis [has_penetrance] 30	(Fig. 3D)
PMID:25778919	FYPO:0006264	decreased telomeric DNA separation during anaphase B	(Fig. 4)
PMID:25778919	FYPO:0006267	increased telomere clustering and tethering at nuclear periphery during mitotic metaphase	(Fig. 4) (comment: decreased telomere dispersion)
PMID:25778919	FYPO:0006267	increased telomere clustering and tethering at nuclear periphery during mitotic metaphase	(Fig. 4) (comment: decreased telomere dispersion)
PMID:25778919	FYPO:0006285	increased duration of protein localization to telomere during mitotic anaphase B [assayed_using] PomBase:SPCC338.17c	(Fig. 5A)
PMID:25778919	FYPO:0004329	normal mitotic rDNA separation [has_penetrance] high	(Fig. 6)
PMID:25778919	FYPO:0004330	normal mitotic telomeric DNA separation [has_penetrance] high	(Fig. 6)
PMID:25778919	FYPO:0004330	normal mitotic telomeric DNA separation [has_penetrance] high	(Fig. 7)
PMID:25778919	FYPO:0004330	normal mitotic telomeric DNA separation	(Fig. S4A)
PMID:25778919	FYPO:0004683	unequal nucleolus inheritance [has_penetrance] 86	(Fig.S2A)
PMID:25778919	GO:0120110	interphase mitotic telomere clustering	(comment: CHECK (requested negative regulation of) synonym mitotic telomere dispersion during metaphase)
PMID:25778919	GO:1905824	positive regulation of mitotic sister chromatid arm separation [occurs_at] subtelomere [happens_during] mitotic anaphase	(comment: telomere disjunction)
PMID:25778919	GO:0044820	mitotic telomere tethering at nuclear periphery	Together, these experiments suggest that Aurora-dependent removal of Swi6/HP1 and consequently cohesin Rad21 from telomeres in early mitosis contributes to telomere dispersion.
PMID:25778919	GO:0044820	mitotic telomere tethering at nuclear periphery	Together, these experiments suggest that Aurora-dependent removal of Swi6/HP1 and consequently cohesin Rad21 from telomeres in early mitosis contributes to telomere dispersion.
PMID:25793410	FYPO:0000633	sensitive to G418	(comment: CONDITION 10 ug/ml G418 for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0004752	resistance to phleomycin	(comment: CONDITION 10 ug/ml phleomycin for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0004751	resistance to G418	(comment: CONDITION 100 ug/ml G418 for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0001719	sensitive to lithium	(comment: CONDITION Sensitivity was rescued by 0.6 M KCl 4 mM lithium for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0002344	sensitive to phleomycin	(comment: CONDITION Sensitivity was rescued by 0.6 M KCl but not 60 mM KCl, 10 ug/ml phleomycin for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0002344	sensitive to phleomycin	(comment: CONDITION Sensitivity was rescued by 0.6 M KCl, 10 ug/ml phleomycin for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0003559	sensitive to doxorubicin	(comment: CONDITION Sensitivity was rescued by 0.6 M KCl, 40 ug/ml doxorubicin for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0003559	sensitive to doxorubicin	(comment: CONDITION Sensitivity was rescued by 0.6 M, but not 60 mM KCl, 40 ug/ml doxorubicin for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0002344	sensitive to phleomycin	(comment: CONDITION Sensitivity was rescued by 150 mM, but not 70 mM KCl, 10 ug/ml phleomycin for 4 h followed by recovery on YES)
PMID:25793410	FYPO:0002344	sensitive to phleomycin	(comment: CONDITION Sensitivity was rescued less efficiently than for the wt by 150 - 600 mM KCl)
PMID:25793410	MOD:01455	O-phosphorylated residue [in_presence_of] phleomycin	Rad3-dependent phosphorylation of Chk1 is observed in the presence of phleomycin, but this is suppressed by KCl concentrations above 0.3 M
PMID:25795664	FYPO:0001234	slow vegetative cell population growth	(comment: A spd1 deletion partially suppresses the synthetic growth defect in a brc1 csn1 double mutant background)
PMID:25795664	FYPO:0001234	slow vegetative cell population growth	(comment: A spd1 deletion partially suppresses the synthetic growth defect in a brc1 ddb1 double mutant background)
PMID:25795664	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(comment: spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents)
PMID:25795664	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(comment: spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents)
PMID:25795664	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(comment: spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents)
PMID:25795664	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(comment: spd1 deletion suppresses brc1delta csn1delta sensitivity to DNA damage agents)
PMID:25795664	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(comment: spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents)
PMID:25795664	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(comment: spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents)
PMID:25795664	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(comment: spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents)
PMID:25795664	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(comment: spd1 deletion suppresses brc1delta ddb1delta sensitivity to DNA damage agents)
PMID:25798942	GO:0006338	chromatin remodeling	(comment: ATPase domain mutant phenotype) (Fig. 5 and S6)
PMID:25831549	GO:0033696	heterochromatin boundary formation	(Fig. 2)
PMID:25831549	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. 2)
PMID:25831549	FYPO:0004544	increased duration of heterochromatin maintenance	(Fig. 2A)
PMID:25831549	FYPO:0004544	increased duration of heterochromatin maintenance	(Fig. 3B)
PMID:25831549	FYPO:0004544	increased duration of heterochromatin maintenance	(Fig. 3C)
PMID:25831549	FYPO:0004544	increased duration of heterochromatin maintenance	(Fig. 3D)
PMID:25831549	FYPO:0004544	increased duration of heterochromatin maintenance	(Fig. 3D)
PMID:25831549	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. 3E)
PMID:25831549	FYPO:0004745	abolished histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 7D)
PMID:25831549	FYPO:0004745	abolished histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 7D)
PMID:25831549	FYPO:0004745	abolished histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 7D)
PMID:25831549	FYPO:0004745	abolished histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 7E)
PMID:25831549	FYPO:0000887	increased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 7E)
PMID:25831549	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 7E)
PMID:25837586	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(Comment: Decreased levels of Cdc42 and Cdc42-GTP (CRIB))
PMID:25837586	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(Comment: Normal levels of Cdc42 and Cdc42-GTP (CRIB))
PMID:25837586	GO:0030427	site of polarized growth	(comment: CHECK Not affected by short-term actin cytoskeleton depolymerization by Latrunculin A)
PMID:25837586	FYPO:0005803	decreased rate of protein movement within plasma membrane at cell side [assayed_using] PomBase:SPAC110.03	(comment: CHECK more severe in presence of LatA)
PMID:25837586	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(comment: Decreased levels of Cdc42 and Cdc42-GTP)
PMID:25837586	FYPO:0002852	increased protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(comment: Increased levels of Cdc42 and Cdc42-GTP (CRIB))
PMID:25837586	FYPO:0002852	increased protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(comment: Increased levels of Cdc42 and Cdc42-GTP (CRIB))
PMID:25837586	FYPO:0000672	normal cell morphology	(comment: Internally tagged functional allele, allowing live-imaging of Cdc42)
PMID:25837586	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(comment: Normal levels of Cdc42 and Cdc42-GTP (CRIB))
PMID:25838386	FYPO:0002335	normal chromatin silencing	(Fig. S5)
PMID:25838386	FYPO:0002335	normal chromatin silencing	(Fig. S5)
PMID:25838386	FYPO:0002335	normal chromatin silencing	(Fig. S5)
PMID:25838386	FYPO:0002335	normal chromatin silencing	(Fig. S5)
PMID:25838386	FYPO:0002335	normal chromatin silencing	(Fig. S5)
PMID:25838386	FYPO:0002335	normal chromatin silencing	(Fig. S5)
PMID:25838386	FYPO:0002335	normal chromatin silencing	(Fig. S5)
PMID:25838386	FYPO:0004544	increased duration of heterochromatin maintenance	Catalytically inactivating mutations in the Fe(II) or 2-oxyglutarate binding sites of the Epe1 putative demethylase (epe1-H297A and epe1-K314A) had a similar phenotype (Fig. 4A, fig. S6, and table S3)
PMID:25838386	FYPO:0004544	increased duration of heterochromatin maintenance	Catalytically inactivating mutations in the Fe(II) or 2-oxyglutarate binding sites of the Epe1 putative demethylase (epe1-H297A and epe1-K314A) had a similar phenotype (Fig. 4A, fig. S6, and table S3)
PMID:25838386	FYPO:0004544	increased duration of heterochromatin maintenance	Of the eight tested mutants, only epe1D consistently formed red-pink colonies on +AHT plates, indicating that 4xtetO-ade6+ can remain repressed without bound TetR-Clr4* (Fig. 4A and figs. S5 and S6).
PMID:25869666	FYPO:0000513	delayed onset of nuclear fusion during mating [has_severity] medium	(Fig. 1)
PMID:25869666	FYPO:0007989	abolished nuclear congression during mating [has_penetrance] 80	(Fig. 1)
PMID:25869666	FYPO:0007989	abolished nuclear congression during mating [has_penetrance] complete	(Fig. 1)
PMID:25869666	FYPO:0000513	delayed onset of nuclear fusion during mating [has_severity] low	(Fig. 1)
PMID:25869666	FYPO:0000513	delayed onset of nuclear fusion during mating [has_severity] medium	(Fig. 1)
PMID:25869666	FYPO:0000513	delayed onset of nuclear fusion during mating [has_severity] low	(Fig. 1)
PMID:25869666	FYPO:0007989	abolished nuclear congression during mating [has_penetrance] 98	(Fig. 1)
PMID:25869666	FYPO:0000513	delayed onset of nuclear fusion during mating [has_severity] low	(Fig. 4)
PMID:25869666	FYPO:0000513	delayed onset of nuclear fusion during mating [has_severity] low	(Fig. 4)
PMID:25869666	FYPO:0007999	abolished protein localization to spindle pole body during karyogamy [assayed_protein] PomBase:SPAC1093.06c	(Fig. 4)
PMID:25869666	FYPO:0007162	increased duration of nuclear fusion during mating	(Fig. S1)
PMID:25869666	FYPO:0005814	abolished protein localization to microtubule plus-end [assayed_protein] PomBase:SPAC664.10	(Fig. S3A)
PMID:25869666	GO:0000743	nuclear migration involved in conjugation with cellular fusion	(comment: Delayed nuclear congresion in dhc1D (Fig. 1) and double deletion dhc1D klp2D completely abolishes nuclear congression (Fig. 1))
PMID:25869666	GO:0000743	nuclear migration involved in conjugation with cellular fusion	(comment: Delayed nuclear congresion in klp2D (Fig. 1) and double deletion dhc1D klp2D completely abolishes nuclear congression (Fig. 1))
PMID:25869666	GO:0000743	nuclear migration involved in conjugation with cellular fusion	(comment: Phenocopies dhc1)
PMID:25869666	GO:0008569	minus-end-directed microtubule motor activity	(comment: Single deletion slows down nuclear congression (minus-end diretcted), double deletion with dhc1 inhibits it.)
PMID:25869666	GO:0008569	minus-end-directed microtubule motor activity	(comment: Single deletion slows down nuclear congression (minus-end diretcted), double deletion with klp2 inhibits it.)
PMID:25891897	FYPO:0004760	abnormal sporulation resulting in formation of azygotic ascus with more than four spores [has_penetrance] 28	(comment: This phenotype is not seen when cells undergo azygotic meiosis)
PMID:25891897	FYPO:0000478	normal meiosis	(comment: azygotic meiosis, rem1 and crs1 do not have a major role in azygotic meiosis)
PMID:25891897	FYPO:0003379	abolished meiosis II	(comment: azygotic meiotic cell cycle/timing of pre-meiotic DNA replication is normal)
PMID:25891897	FYPO:0003378	abolished meiosis I	(comment: azygotic meiotic cell cyle)
PMID:25891897	FYPO:0000478	normal meiosis	(comment: azygotic)
PMID:25891897	FYPO:0000478	normal meiosis	(comment: azygotic/ slight advance in the timing of MI and MII)
PMID:25891897	FYPO:0000478	normal meiosis	(comment: azygotic// presence of 4x fusion protein restores the ability of cig1 cig2 puc1 rem1 quadruple deletion strain to undergo pre meiotic DNA replication)
PMID:25891897	FYPO:0004608	abnormal spindle pole body morphology during meiosis II	(comment: presence of more than 2 SPBs dots after meiotic nuclear divisions 19.6% zygotes exhibit abnormal meiotic division during zygotic meiosis)
PMID:25891897	FYPO:0000478	normal meiosis	(comment: zygotic / >80% of asci have 4 spores)
PMID:25891897	FYPO:0002151	inviable spore [has_penetrance] 29.7	(comment: zygotic meiosis random spore analysis)
PMID:25891897	FYPO:0002151	inviable spore [has_penetrance] 69	(comment: zygotic meiosis random spore analysis)
PMID:25891897	FYPO:0002151	inviable spore [has_penetrance] 94.5	(comment: zygotic meiosis random spore analysis)
PMID:25891897	FYPO:0002151	inviable spore [has_penetrance] 55.7	(comment: zygotic meiosis random spore analysis)
PMID:25891897	FYPO:0002151	inviable spore [has_penetrance] 69.4	(comment: zygotic meiosis random spore analysis)
PMID:25891897	FYPO:0003263	abnormal sporulation resulting in formation of ascus with more than four spores [has_penetrance] 60	(comment: zygotic meiosis)
PMID:25891897	FYPO:0002151	inviable spore [has_penetrance] 25	(comment: zygotic meiosis/ Random spore analysis)
PMID:25891897	FYPO:0002151	inviable spore [has_penetrance] 80	(comment: zygotic random spore analysis)
PMID:25891897	FYPO:0004077	abnormal sporulation resulting in formation of ascus with single large spore [has_penetrance] 10	(comment: zygotic)
PMID:25891897	FYPO:0000478	normal meiosis	(comment: zygotic)
PMID:25891897	FYPO:0003263	abnormal sporulation resulting in formation of ascus with more than four spores [has_penetrance] 36	(comment: zygotic)
PMID:25891897	FYPO:0002151	inviable spore [has_penetrance] 89	(comment: zygotic)
PMID:25891897	FYPO:0000681	abnormal sporulation resulting in formation of two-spore ascus [has_penetrance] 85	(comment: zygotic)
PMID:25891897	FYPO:0002151	inviable spore [has_penetrance] 20	(comment: zygotic)
PMID:25891897	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 81.3	(comment: zygotic)
PMID:25891897	FYPO:0003263	abnormal sporulation resulting in formation of ascus with more than four spores [has_penetrance] 11.6	(comment: zygotic)
PMID:25891897	FYPO:0003263	abnormal sporulation resulting in formation of ascus with more than four spores [has_penetrance] 8.6	(comment: zygotic)
PMID:25891897	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 77	(comment: zygotic)
PMID:25891897	FYPO:0000681	abnormal sporulation resulting in formation of two-spore ascus [has_penetrance] 20	(comment: zygotic)
PMID:25891897	FYPO:0002151	inviable spore [has_penetrance] 54	(comment: zygotic/ random spore analysis)
PMID:25891897	FYPO:0000478	normal meiosis	(comment: zygotic//presence of 4x fusion protein restores the ability of cig1 cig2 puc1 rem1 quadruple deletion strain to undergo pre meiotic DNA replication)
PMID:25891897	FYPO:0003563	normal meiosis I	azygotic/ slight advance in the timing of MI and MII
PMID:25959226	FYPO:0006186	increased rate of actomyosin contractile ring assembly	However, contractile ring assembly was significantly faster in mid13A than in mid1+ cells (Figure S6, C-F)
PMID:25959226	FYPO:0008077	decreased phosphatidylserine binding [has_severity] low	In contrast, monomerization only slightly reduced the affinity to PS.
PMID:25959226	FYPO:0004456	increased protein localization to nucleus	In contrast, the monomeric Mid13A remained concentrated in the nucleus and its signals on the plasma membrane were more widespread, even reached the cell poles (Figure 6E
PMID:25959226	FYPO:0006005	normal actomyosin contractile ring localization	Indeed, the morphology and positioning of the contractile ring marked with myosin regulatory light chain Rlc1 were normal in mid13A cells (Figure S6, C-D)
PMID:25959226	GO:0005546	phosphatidylinositol-4,5-bisphosphate binding	Interestingly, it binds to PI(4,5)P2 strongly, with a Kd up to 0.12 μM (Figure 3C, 3D).
PMID:25959226	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC4B3.15 [assayed_protein] PomBase:SPCC4B3.15	Mutations of the hydrophobic C2-C2 interface shifted Mid1 into monomeric state (Figure 6A)
PMID:25959226	FYPO:0000339	mislocalized septum during vegetative growth	which interacts with the N-terminus of Mid1 and stabilizes Mid1 at the division plane (Ye et al., 2012; Zhu et al., 2013). As expected, mid13A gef2Δ double mutants had strong synthetic defects in division-plane placement and septum formation at 36°C (Figure 6, F-H).
PMID:25959226	FYPO:0000339	mislocalized septum during vegetative growth	which interacts with the N-terminus of Mid1 and stabilizes Mid1 at the division plane (Ye et al., 2012; Zhu et al., 2013). As expected, mid13A gef2Δ double mutants had strong synthetic defects in division-plane placement and septum formation at 36°C (Figure 6, F-H).
PMID:25959226	FYPO:0008076	decreased phosphatidylinositol-4,5-bisphosphate binding [has_severity] high	which showed > 10-fold lower affinity to PI(4,5)P2 (Figure 3D).
PMID:25965521	FYPO:0000085	sensitive to camptothecin [has_severity] low	(comment: same as brc1delta alone; brc1 epistatic
PMID:25965521	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	FYPO:0000085	sensitive to camptothecin [has_severity] low	(comment: same as brc1delta alone; brc1 epistatic)
PMID:25965521	FYPO:0002573	increased number of Ssb1 foci	(comment: same as either single mutant)
PMID:25965521	FYPO:0002573	increased number of Ssb1 foci	(comment: same as either single mutant)
PMID:25965521	FYPO:0000085	sensitive to camptothecin	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000268	sensitive to UV during vegetative growth	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000085	sensitive to camptothecin	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000088	sensitive to hydroxyurea	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000268	sensitive to UV during vegetative growth	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000085	sensitive to camptothecin	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000088	sensitive to hydroxyurea	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000268	sensitive to UV during vegetative growth	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000088	sensitive to hydroxyurea	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000268	sensitive to UV during vegetative growth	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000085	sensitive to camptothecin	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25965521	FYPO:0000088	sensitive to hydroxyurea	(comment: same as mus81delta alone; mus81 epistatic)
PMID:25977474	FYPO:0000032	abnormal cytokinesis during vegetative growth	(comment: abnormal cleavage furrow disc formation) Fig 3
PMID:25977474	FYPO:0000032	abnormal cytokinesis during vegetative growth	(comment: abnormal cleavage furrow disc formation) Fig 3
PMID:25977474	FYPO:0000032	abnormal cytokinesis during vegetative growth	(comment: abnormal cleavage furrow disc formation) Fig 3
PMID:25977474	FYPO:0000032	abnormal cytokinesis during vegetative growth	(comment: abnormal cleavage furrow disc formation) Fig 3
PMID:25977474	FYPO:0000032	abnormal cytokinesis during vegetative growth	(comment: abnormal cleavage furrow disc formation) Fig 3
PMID:25987607	FYPO:0004395	short bipolar mitotic spindle during metaphase [has_penetrance] ~25	(Fig. 5B and Videos 1-4)
PMID:25987607	FYPO:0003787	long mitotic spindle microtubules protruding beyond spindle pole body [has_penetrance] ~15-20	(Fig. 5B and Videos 1-4)
PMID:25987607	FYPO:0002636	delayed onset of mitotic spindle elongation	(Fig. 5B and Videos 1-4)
PMID:25987607	FYPO:0006173	abolished mitotic spindle elongation during prophase	(Fig. 5B and Videos 1-4)
PMID:25987607	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	(comment: CHECK during mitotic M phase)
PMID:25987607	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	(comment: CHECK during mitotic M phase)
PMID:25987607	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	(comment: CHECK during mitotic M phase)
PMID:25987607	FYPO:0004396	normal mitotic spindle elongation	(comment: I think the pkl rigor is spb tethered here?)
PMID:25987607	GO:0008569	minus-end-directed microtubule motor activity [has_input] PomBase:SPBC13E7.06 [has_input] PomBase:SPBC32H8.09 [part_of] protein transport along microtubule to mitotic spindle pole body	(comment: I want to represent the microtubule based-transporter function and cargo)
PMID:25987607	GO:0008569	minus-end-directed microtubule motor activity [has_input] PomBase:SPBC32H8.09 [has_input] PomBase:SPBC13E7.06 [part_of] microtubule anchoring at mitotic spindle pole body	(comment: I want to represent the microtubule based-transporter function and cargo)
PMID:25987607	FYPO:0003787	long mitotic spindle microtubules protruding beyond spindle pole body	(comment: non additive)
PMID:25989903	GO:0071030	nuclear mRNA surveillance of spliceosomal pre-mRNA splicing	(comment: exosome dependent)
PMID:25989903	GO:0071030	nuclear mRNA surveillance of spliceosomal pre-mRNA splicing	(comment: exosome dependent)
PMID:25989903	GO:0071039	nuclear polyadenylation-dependent CUT catabolic process	(comment: exosome dependent)
PMID:25989903	GO:0071030	nuclear mRNA surveillance of spliceosomal pre-mRNA splicing	(comment: exosome dependent)
PMID:25989903	FYPO:0008148	increased CUT RNA level	As previously reported, deletion of rrp6 leads to strong accumulation of CUTs and a small group of mRNAs that are mostly involved in meiosis16,23,25,29,30,35.
PMID:25989903	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth	As previously reported, deletion of rrp6 leads to strong accumulation of CUTs and a small group of mRNAs that are mostly involved in meiosis16,23,25,29,30,35.
PMID:25989903	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth	Deletion of iss10 or mmi1 only affects meiotic mRNAs
PMID:25989903	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth	Deletion of iss10 or mmi1 only affects meiotic mRNAs
PMID:25989903	FYPO:0008148	increased CUT RNA level	In contrast, deletion or mutation alleles of the MTREC complex lead to significant accumulation of all types of CUTs and also meiotic mRNAs. This effect is comparable to the level of CUT accumulation in the nuclear exosome subunit rrp6 deletion (Fig. 2a,b)
PMID:25989903	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth	In contrast, deletion or mutation alleles of the MTREC complex lead to significant accumulation of all types of CUTs and also meiotic mRNAs. This effect is comparable to the level of CUT accumulation in the nuclear exosome subunit rrp6 deletion (Fig. 2a,b)
PMID:25989903	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth	In contrast, deletion or mutation alleles of the MTREC complex lead to significant accumulation of all types of CUTs and also meiotic mRNAs. This effect is comparable to the level of CUT accumulation in the nuclear exosome subunit rrp6 deletion (Fig. 2a,b)
PMID:25989903	FYPO:0008148	increased CUT RNA level	In contrast, deletion or mutation alleles of the MTREC complex lead to significant accumulation of all types of CUTs and also meiotic mRNAs. This effect is comparable to the level of CUT accumulation in the nuclear exosome subunit rrp6 deletion (Fig. 2a,b)
PMID:25989903	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth	In contrast, deletion or mutation alleles of the MTREC complex lead to significant accumulation of all types of CUTs and also meiotic mRNAs. This effect is comparable to the level of CUT accumulation in the nuclear exosome subunit rrp6 deletion (Fig. 2a,b)
PMID:25989903	FYPO:0008148	increased CUT RNA level	In contrast, deletion or mutation alleles of the MTREC complex lead to significant accumulation of all types of CUTs and also meiotic mRNAs. This effect is comparable to the level of CUT accumulation in the nuclear exosome subunit rrp6 deletion (Fig. 2a,b)
PMID:25989903	FYPO:0008113	increased intron retention [has_severity] low	Similar to previous reports, we detected significantly increased intronic reads in the exosome mutant rrp6D strain (Fig. 4a,b).
PMID:25989903	FYPO:0008113	increased intron retention	Similar to previous reports, we detected significantly increased intronic reads in the exosome mutant rrp6D strain (Fig. 4a,b).
PMID:25989903	FYPO:0008113	increased intron retention	Similar to previous reports, we detected significantly increased intronic reads in the exosome mutant rrp6D strain (Fig. 4a,b).
PMID:25989903	FYPO:0008113	increased intron retention	Similar to previous reports, we detected significantly increased intronic reads in the exosome mutant rrp6D strain (Fig. 4a,b).
PMID:25989903	FYPO:0008113	increased intron retention [has_severity] low	Similar to previous reports, we detected significantly increased intronic reads in the exosome mutant rrp6D strain (Fig. 4a,b).
PMID:25989903	FYPO:0008113	increased intron retention	Similar to previous reports, we detected significantly increased intronic reads in the exosome mutant rrp6D strain (Fig. 4a,b).
PMID:25989903	FYPO:0008152	normal CUT RNA level	Surprisingly, deletion of the S. pombe Trf4/5 orthologue, cid14, showed only a minor effect on CUTs at a genome-wide level (Fig. 2a,b)
PMID:25989903	GO:0071030	nuclear mRNA surveillance of spliceosomal pre-mRNA splicing	This analysis revealed that in the ctr1D or nrl1D mutant strains, both the intronic and also the surrounding exonic sequence coverage showed similar increases, while the expression of genes without introns was unaffected (Supplementary Fig. 4c,d). This result strongly suggests that the elevated level of intronic reads in the mutant strains is the consequence of the inefficient degradation of unspliced or mis-
PMID:25989903	GO:0071031	nuclear mRNA surveillance of mRNA 3'-end processing	meiotic genes ....Overall, our experiments show that the MTREC complex is specifically recruited to CUTs and meiotic mRNAs, and it plays a key role in their degradation by the nuclear exosome.
PMID:25993311	FYPO:0005577	decreased protein phosphorylation during meiotic cell cycle [assayed_using] PomBase:SPCC4E9.01c	(Fig. 2)
PMID:25993311	FYPO:0005577	decreased protein phosphorylation during meiotic cell cycle [assayed_using] PomBase:SPCC4E9.01c	(Fig. 2)
PMID:25993311	MOD:00696	phosphorylated residue [added_during] meiotic cell cycle phase	(Fig. 2a)
PMID:25993311	MOD:00696	phosphorylated residue [added_during] meiotic cell cycle phase	(Fig. 2a)
PMID:25993311	MOD:00696	phosphorylated residue [added_during] meiotic cell cycle phase	(Fig. 2a)
PMID:25993311	FYPO:0005986	linear elements present in decreased numbers	(Fig. 3)
PMID:25993311	FYPO:0004585	abnormal linear element morphology	(Fig. 3)
PMID:25993311	FYPO:0005986	linear elements present in decreased numbers	(Fig. 3)
PMID:25993311	FYPO:0004585	abnormal linear element morphology	(Fig. 3)
PMID:25993311	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] high	(Table 1)
PMID:25993311	FYPO:0002485	decreased intergenic meiotic recombination [has_severity] high	(Table 1)
PMID:25993311	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] high	(Table 1)
PMID:25993311	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] high	(Table 1)
PMID:25993311	GO:0090006	regulation of linear element assembly	(Table 1)
PMID:25993311	GO:0090006	regulation of linear element assembly	(Table 1)
PMID:25993311	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] high	(Table 2)
PMID:25993311	FYPO:0001033	normal double-strand break repair	(Table 2)
PMID:25993311	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] high	(Table 2)
PMID:25993311	FYPO:0000488	normal meiotic recombination	(Table 3)
PMID:25993311	FYPO:0000488	normal meiotic recombination	(Table 3)
PMID:25993311	FYPO:0000485	decreased meiotic recombination [has_severity] medium	(Table 3)
PMID:25993311	FYPO:0000488	normal meiotic recombination	Table S3
PMID:25993311	FYPO:0000488	normal meiotic recombination	Table S3
PMID:25993311	FYPO:0000488	normal meiotic recombination	Table S3
PMID:25993311	FYPO:0000488	normal meiotic recombination	Table S3
PMID:25993311	FYPO:0002151	inviable spore [has_severity] high [has_penetrance] 99	Table2
PMID:25993311	FYPO:0002151	inviable spore [has_penetrance] 65	Table2
PMID:25993311	FYPO:0002151	inviable spore [has_penetrance] 78	Table2
PMID:25993311	FYPO:0002151	inviable spore [has_penetrance] 98.6	Table2
PMID:25993311	FYPO:0002151	inviable spore [has_penetrance] 86	Table2
PMID:25993311	FYPO:0002151	inviable spore [has_penetrance] 75	Table2
PMID:25993311	FYPO:0002151	inviable spore [has_penetrance] 71	Table2
PMID:26031557	FYPO:0001861	increased minichromosome loss upon segregation during vegetative growth [has_penetrance] 8.5	(Fig. 1)
PMID:26031557	FYPO:0001861	increased minichromosome loss upon segregation during vegetative growth [has_penetrance] 8.2	(Fig. 2)
PMID:26031557	FYPO:0003787	long mitotic spindle microtubules protruding beyond spindle pole body [has_penetrance] 52	(Fig. 2)
PMID:26031557	FYPO:0001861	increased minichromosome loss upon segregation during vegetative growth [has_penetrance] 11	(Fig. 2) (comment: CHECK It's only a bit worse (+3% chromosome loss). Not sure if worth including)
PMID:26031557	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. 3)
PMID:26031557	FYPO:0007968	cut with mitotic spindle microtubules protruding beyond spindle pole body [has_penetrance] 12	(Fig. 3) MT buckling during prolonged contact with the cell tip cortex—its associated chromosome mass to the medial cell division site (Fig. 3c). Subsequent cytokinesis appeared to cut through the chromosome mass, resulting in aneuploidy in 12% of mitotic cells.
PMID:26031557	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. 3) This is important as it indicates that the delay in pkl1D is likely not due to a delay in chromosome capture, but rather spindle formation in prophase.
PMID:26031557	FYPO:0007969	short-lived long mitotic spindle microtubules protruding beyond spindle pole body [has_penetrance] 30	(Fig. 4)
PMID:26031557	FYPO:0003787	long mitotic spindle microtubules protruding beyond spindle pole body [has_penetrance] 51	(Fig. S2) In contrast, in pkl1D msd1D cells, Pkl1md-GFP localized primarily to the spindle and only partially rescued the protrusion phenotype
PMID:26031557	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis	(Fig. S2) Pkl1md-GFP localized primarily to the spindle poles
PMID:26031557	FYPO:0003787	long mitotic spindle microtubules protruding beyond spindle pole body [has_penetrance] 8	(Fig. S2) Pkl1md-GFP localized primarily to the spindle poles and almost completely rescued the protrusion phenotype
PMID:26031557	FYPO:0003787	long mitotic spindle microtubules protruding beyond spindle pole body [has_penetrance] 27	(Fig. S4)
PMID:26088418	FYPO:0006464	abnormal telomere length during vegetative growth [has_severity] high	(comment: increased length hererogeneity)
PMID:26088418	FYPO:0006464	abnormal telomere length during vegetative growth [has_severity] high	(comment: increased length hererogeneity)
PMID:26088418	FYPO:0006464	abnormal telomere length during vegetative growth	(comment: increased length hererogeneity) taz1-4A cells still exhibited extremely heterogeneous telomeres similar to taz1Δ and taz1-4R cells (Figure 1E).
PMID:26088418	FYPO:0006464	abnormal telomere length during vegetative growth [has_severity] high	(comment: increased length hererogeneity*****************) Indeed, yeast cells expressing the L431R and L445R mutants exhibited significant loss of function in telomere length regulation and showed long and highly heterogenous telomeres that were as severe as that in taz1Δ cells (Figure 1K)
PMID:26088418	FYPO:0006464	abnormal telomere length during vegetative growth [has_severity] high	(comment: increased length hererogeneity*****************) Indeed, yeast cells expressing the L431R and L445R mutants exhibited significant loss of function in telomere length regulation and showed long and highly heterogenous telomeres that were as severe as that in taz1Δ cells (Figure 1K)
PMID:26088418	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC16A10.07c	Both mutant proteins were expressed at near wild-type levels, suggesting that these acidic residues are not required for protein stability (data not shown).
PMID:26088418	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC16A10.07c	Both mutant proteins were expressed at near wild-type levels, suggesting that these acidic residues are not required for protein stability (data not shown).
PMID:26088418	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC16A10.07c	Mutant proteins were expressed at a comparable level as wild-type Taz1 (data not shown).
PMID:26088418	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPAC16A10.07c	Mutant proteins were expressed at a comparable level as wild-type Taz1 (data not shown).
PMID:26088418	FYPO:0000658	decreased DNA binding [has_severity] high	The L445R mutation caused a 10-fold decrease in DNA binding with a Kd of ~7 μM (Figure 1I), suggesting that Taz1 homodimerization is
PMID:26088418	GO:0042162	telomeric repeat DNA binding	While wild-type Taz1 bound to DNA with an equilibrium dissociation constant (Kd) of ~600 nM (Figure 1I), the L445R mutation caused a 10-fold decrease in DNA binding with a Kd of ~7 μM (Figure 1I), suggesting that Taz1 homodimerization is required for its efficient association with the telomeric DNA in vitro.
PMID:26092938	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC4A8.05c	(comment: decreased local concentration of the myosin-II)
PMID:26092938	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC4A8.05c	(comment: decreased local concentration of the myosin-II)
PMID:26092938	FYPO:0004854	increased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC4A8.05c	(comment: increased local concentration of the myosin-II)
PMID:26092938	FYPO:0006303	decreased protein localization to actomyosin contractile ring, with protein mislocalized to cytoplasm [assayed_using] PomBase:SPAC4A8.05c	(comment: large portion of the mutant forms cytoplasmic dots)
PMID:26092938	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC4A8.05c	(comment: localization of the myosin-II is abolished)
PMID:26098872	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Figure 8a)
PMID:26098872	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 8a)
PMID:26098872	FYPO:0001357	normal vegetative cell population growth	(Figure 8a)
PMID:26098872	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Figure 8b)
PMID:26098872	FYPO:0004056	decreased protein localization to nucleus, with protein mislocalized to cytoplasm [assayed_using] PomBase:SPAC26A3.08	(Figure 8c)
PMID:26108447	FYPO:0002766	resistance to clotrimazole	(Figure 6)
PMID:26108447	FYPO:0002766	resistance to clotrimazole	(Figure 6)
PMID:26108447	FYPO:0002640	sensitive to clotrimazole	(Figure 6)
PMID:26108447	FYPO:0003860	resistance to miconazole	(Figure 6)
PMID:26108447	FYPO:0003860	resistance to miconazole	(Figure 6)
PMID:26108447	FYPO:0003860	resistance to miconazole	(Figure 6)
PMID:26108447	FYPO:0003860	resistance to miconazole	(Figure 6)
PMID:26108447	FYPO:0003860	resistance to miconazole	(Figure 6)
PMID:26108447	FYPO:0003358	sensitive to miconazole	(Figure 6)
PMID:26108447	FYPO:0002766	resistance to clotrimazole	(Figure 6)
PMID:26108447	FYPO:0002766	resistance to clotrimazole	(Figure 6)
PMID:26108447	FYPO:0002766	resistance to clotrimazole	(Figure 6)
PMID:26108447	FYPO:0003860	resistance to miconazole	(Figure 6)
PMID:26108447	FYPO:0002766	resistance to clotrimazole	(Figure 6)
PMID:26108447	FYPO:0002766	resistance to clotrimazole	(Figure 6)
PMID:26122634	FYPO:0004688	decreased cytosolic large ribosomal subunit level	(comment: polysomal profiling)
PMID:26122634	FYPO:0004688	decreased cytosolic large ribosomal subunit level	(comment: polysomal profiling)
PMID:26124291	GO:0099070	static microtubule bundle [exists_during] cell quiescence	(Fig. 4 C)
PMID:26124291	GO:0099070	static microtubule bundle [exists_during] cell quiescence	(Fig. 4 C)
PMID:26124291	GO:0099070	static microtubule bundle [exists_during] cell quiescence	(Fig. 4 C)
PMID:26124291	GO:0099070	static microtubule bundle [exists_during] cell quiescence	(Fig. 4 C)
PMID:26124291	GO:0099070	static microtubule bundle [exists_during] cell quiescence	(Fig. 4 C)
PMID:26124291	GO:0099070	static microtubule bundle [exists_during] cell quiescence	(Fig. 4 C)
PMID:26124291	GO:0099079	actin body	(Fig. 6C)
PMID:26124291	GO:0099079	actin body	(Fig. 6C)
PMID:26124291	FYPO:0004614	abnormal microtubule polymerization during vegetative growth	(Fig. 7 CD) (comment: abnormal Q-MT bundle elongation upon G1 re-entry/interphase bundle reassembly)
PMID:26124291	FYPO:0005565	abnormal microtubule bundle during G0 to G1 transition	(Fig. 7E)
PMID:26124291	FYPO:0005567	T-shaped cell during G0 to G1 transition [has_penetrance] 60	(Fig. 7E,F)
PMID:26124291	GO:0099079	actin body	(Fig. S5A,C)
PMID:26124291	FYPO:0005613	normal protein localization to nuclear envelope during G0 to G1 transition [assayed_using] PomBase:SPCC417.07c	(Fig. S5E)
PMID:26124291	FYPO:0005613	normal protein localization to nuclear envelope during G0 to G1 transition [assayed_using] PomBase:SPBC902.06	(Fig. S5E)
PMID:26131711	GO:0005515	protein binding	(comment: Chk1 binds to the unphosphorylated form of Cdc2 kinase)
PMID:26131711	GO:0005515	protein binding	(comment: Chk1 binds to the unphosphorylated form of Cdc2 kinase)
PMID:26131711	GO:0005515	protein binding	(comment: Chk1 binds to the unphosphorylated form of Cdc2 kinase)
PMID:26131711	GO:0005515	protein binding	(comment: Chk1 binds to the unphosphorylated form of Cdc2 kinase)
PMID:26131711	GO:0005515	protein binding	(comment: Chk1 binds to the unphosphorylated form of Cdc2 kinase)
PMID:26131711	FYPO:0000775	abnormal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09	(comment: modified forms of Cdc2 present differ from wild type)
PMID:26131711	GO:0072435	response to mitotic G2 DNA damage checkpoint signaling	Chk1 binds to the unphosphorylated form of Cdc2 kinase
PMID:26131711	FYPO:0000775	abnormal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09	modified forms of Cdc2 differ from both wild type and cdc2-1w alone
PMID:26131711	FYPO:0000775	abnormal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09	modified forms of Cdc2 present differ from wild type, but are same as in cdc2-1w alone
PMID:26131711	FYPO:0000775	abnormal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09	modified forms of Cdc2 present differ from wild type, but are same as in cdc2-1w alone
PMID:26132084	FYPO:0003338	abnormal actomyosin contractile ring morphology	(Fig. 2A,B) fragmented with RLC strands
PMID:26132084	FYPO:0003838	abolished actomyosin contractile ring contraction [has_penetrance] low	(Fig. 2D,2E)
PMID:26132084	FYPO:0004495	inviable branched, swollen, elongated, multiseptate vegetative cell	(Fig. 3C)
PMID:26132084	FYPO:0005870	incomplete septum [has_penetrance] medium	(Fig. 3C,D)
PMID:26132084	FYPO:0005871	thin, incomplete primary cell septum	(Fig. 4C)
PMID:26132084	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC4F6.12	(Fig. 5) (comment: SH3 domain of Cdc15 is required for the proper concentration of Pxl1 at the CAR)
PMID:26132084	FYPO:0000117	abnormal septum assembly	(Fig. 6)
PMID:26132084	FYPO:0003890	abnormal primary cell septum biogenesis	(Fig. 6) Coupling of the Actomyosin ring contraction and septation onsetRing sliding even after the onset of septum synthesis, causing a longitudinal deposition along the plasma membrane of linear β-glucan as detected by CW staining until septum ingression started
PMID:26132084	FYPO:0003210	mislocalized, misoriented septum	(Figure 1)
PMID:26132084	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] 30	(Figure 1A,B)
PMID:26132084	FYPO:0005289	actomyosin contractile ring sliding	(Figure 1c)
PMID:26132084	FYPO:0005289	actomyosin contractile ring sliding [has_penetrance] 20	(Figure 3)
PMID:26132084	FYPO:0005873	increased secondary cell septum thickness	(Figure 4B)
PMID:26137436	FYPO:0002060	viable vegetative cell population	(Table 1)
PMID:26137436	GO:0008233	peptidase activity [has_input] PomBase:SPAC1486.05	we failed to detect a band corresponding to the full-length Nup189 fused with GFP (Nup98-Nup96-GFP), indicating that autocleavage occurs with no remains of the joint molecule. The same bands corresponding to Nup98 and Nup96-GFP were also detected in the splicing-defective mutant, as expected (Fig. 2B and C
PMID:26150232	GO:1903077	negative regulation of protein localization to plasma membrane	(comment: of cell tip)
PMID:26152587	FYPO:0001357	normal vegetative cell population growth	(Fig. 1a)
PMID:26152587	FYPO:0001357	normal vegetative cell population growth	(Fig. 1a)
PMID:26152587	FYPO:0003161	RNA absent from cell during vegetative growth [assayed_using] PomBase:SPAC25B8.13c	(Fig. 1a)
PMID:26152587	FYPO:0001357	normal vegetative cell population growth	(Fig. 1a)
PMID:26152587	FYPO:0001357	normal vegetative cell population growth	(Fig. 1a)
PMID:26152587	FYPO:0001357	normal vegetative cell population growth	(Fig. 1a)
PMID:26152587	FYPO:0001355	decreased vegetative cell population growth	(Fig. 1a)
PMID:26152587	FYPO:0001357	normal vegetative cell population growth	(Fig. 1a)
PMID:26152587	FYPO:0001357	normal vegetative cell population growth	(Fig. 1a)
PMID:26152587	FYPO:0006552	increased protein localization to cytoplasm [assayed_using] PomBase:SPCC1902.01	(comment: CHECK a mild phenotype)
PMID:26152587	FYPO:0006552	increased protein localization to cytoplasm [assayed_using] PomBase:SPCC1902.01	(comment: CHECK a mild phenotype)
PMID:26152587	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPCC1902.01	(comment: CONDITION 1h in proline medium)
PMID:26152587	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPCC1902.01 [has_severity] low	(comment: CONDITION 1h in proline medium) (comment: CHECK a mild phenotype)
PMID:26152587	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPCC1902.01 [has_severity] low	(comment: CONDITION 1h in proline medium) (comment: CHECK a mild phenotype)
PMID:26152587	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPCC1902.01	(comment: CONDITION 1h in proline medium) (comment: CHECK a mild phenotype)
PMID:26152587	GO:0005737	cytoplasm [exists_during] cellular response to glucose starvation	(comment: Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation)
PMID:26152587	GO:0005634	nucleus [exists_during] cellular response to nitrogen starvation	(comment: Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation)
PMID:26152587	GO:0005737	cytoplasm [exists_during] single-celled organism vegetative growth phase	(comment: Gaf1-GFP is found in the nucleus following nitrogen starvation but not glucose starvation)
PMID:26152728	GO:1990116	ribosome-associated ubiquitin-dependent protein catabolic process	(comment: =)
PMID:26152728	GO:0030163	protein catabolic process	(comment: vw: this pathway appears to be proteasome independent, likely autohagy mediated)
PMID:26152728	GO:0030163	protein catabolic process	(comment: vw: this pathway appears to be proteasome independent, likely autophagy mediated)
PMID:26152728	FYPO:0000704	abnormal protein-protein interaction [assayed_using] PomBase:SPAC22E12.03c [assayed_using] PomBase:SPAC22E12.03c	As expected, we found that GST-tagged Sdj1 was able to co-precipitate wild type His6- tagged Sdj1, but not His6-tagged Sdj1-L169P (Fig. 1B). In agreement with this, we observe that the Leu-169 residue is located in the proximity of the subunit-subunit interface in the published crystal structure of Sdj1 (33) (Fig. 1C).
PMID:26152728	FYPO:0000847	increased protein degradation during vegetative growth [assayed_using] PomBase:SPAC22E12.03c	First, we observed that the steady-state level of Sdj1-L169P was reduced compared with wild type Sdj1 (Fig. 3A). In cultures where protein synthesis was blocked by addition of cycloheximide, we found that wild type Sdj1 appeared stable, whereas the Sdj1-L169P protein was rapidly degraded (Fig. 3B). However, when the proteasome inhibitor bortezomib was added to the culture, the degradation was blocked (Fig. 3B), suggesting that the reduced Sdj1-L169P steady-state level was primarily caused by proteasomal degradation of the protein
PMID:26152728	FYPO:0004734	decreased misfolded protein degradation [assayed_using] PomBase:SPAC22E12.03c	Indeed, Sdj1-L169P was more stable in both ltn1 and rqc1 deletion strains (Fig. 5B). Although degradation was still observed in the ltn1Δ and rqc1Δ strains, Sdj1-L169P was significantly stabilized in these mutants compared with the wild type control (Fig. 5C).
PMID:26152728	FYPO:0004734	decreased misfolded protein degradation [assayed_using] PomBase:SPAC22E12.03c	Indeed, the Sdj1-L169P level was increased in ssa1, ssa2, and hsp104 null mutants, with the most marked effect observed in the ssa2Δ and hsp104Δ strains (Fig. 4B).
PMID:26152728	FYPO:0000846	decreased protein degradation during vegetative growth [assayed_using] PomBase:SPAC22E12.03c	Indeed, the Sdj1-L169P level was increased in ssa1, ssa2, and hsp104 null mutants, with the most marked effect observed in the ssa2Δ and hsp104Δ strains (Fig. 4B).
PMID:26152728	FYPO:0004734	decreased misfolded protein degradation [assayed_using] PomBase:SPAC22E12.03c	Indeed, the Sdj1-L169P level was increased in ssa1, ssa2, and hsp104 null mutants, with the most marked effect observed in the ssa2Δ and hsp104Δ strains (Fig. 4B).
PMID:26152728	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC22E12.03c [assayed_using] PomBase:SPAC13G7.02c	Interestingly, a few proteins were found to specifically interact with Sdj1-L169P (supplemental File S2). Among these were Ssa1 and Ssa2, two highly similar cytosolic Hsp70-type chaperones. To independently validate the data from mass spectrometry, we subsequently performed immunoprecipitation experiments with wild type Sdj1 and Sdj1-L169P. Indeed, we found that Hsp70 (Ssa1 and Ssa2) was specifically associated with Sdj1-L169P and not wild type Sdj1 (Fig. 4A).
PMID:26152728	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC22E12.03c [assayed_using] PomBase:SPCC1739.13	Interestingly, a few proteins were found to specifically interact with Sdj1-L169P (supplemental File S2). Among these were Ssa1 and Ssa2, two highly similar cytosolic Hsp70-type chaperones. To independently validate the data from mass spectrometry, we subsequently performed immunoprecipitation experiments with wild type Sdj1 and Sdj1-L169P. Indeed, we found that Hsp70 (Ssa1 and Ssa2) was specifically associated with Sdj1-L169P and not wild type Sdj1 (Fig. 4A).
PMID:26152728	GO:0005634	nucleus	Sdj1, carrying a C-terminal YFP, FLAG, and His6 (YFH) tag, was evenly distributed throughout the cytosol and nucleus, and did not markedly co-localize with the mitochondrial marker protein, Cox4 (Fig. 2A).
PMID:26152728	GO:0005829	cytosol	Sdj1, carrying a C-terminal YFP, FLAG, and His6 (YFH) tag, was evenly distributed throughout the cytosol and nucleus, and did not markedly co-localize with the mitochondrial marker protein, Cox4 (Fig. 2A).
PMID:26152728	FYPO:0004734	decreased misfolded protein degradation [assayed_using] PomBase:SPAC22E12.03c	only in the ltn1Δ strain did we observe an increased level of Sdj1-L169P (Fig. 5A).
PMID:26160178	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPACUNK4.14 [assayed_using] PomBase:SPACUNK4.14	(comment: CHECK affecting binding to Mdb1)
PMID:26160178	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPACUNK4.14 [assayed_using] PomBase:SPCC622.08c	(comment: CHECK affecting binding to histone H2A (hta1))
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC16.02c	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC11C11.08	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC825.05c	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC25G10.01	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC27F1.09c	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC18H10.04c	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC18H10.04c	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC19G12.07c	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC19G12.07c	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC1795.11	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC19A8.13	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBP35G2.09	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC30D11.14c	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC162.01c	(Figure 2) SR protein kinases use an evolutionarily conserved RXXSP motif for substrate recognition
PMID:26167880	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC530.14c	Dsk1 readily phosphorylated WT Bpb1 in vitro, and mutation of Bpb1 at either S131 or S133 to alanine did not abolish phosphorylation (Fig. 5a). However, mutation of both S131 and S133 did, thus indicating that these two residues are the major sites of Bpb1 phosphorylation by Dsk1 (Fig. 5a).
PMID:26167880	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC530.14c	Dsk1 readily phosphorylated WT Bpb1 in vitro, and mutation of Bpb1 at either S131 or S133 to alanine did not abolish phosphorylation (Fig. 5a). However, mutation of both S131 and S133 did, thus indicating that these two residues are the major sites of Bpb1 phosphorylation by Dsk1 (Fig. 5a).
PMID:26167880	FYPO:0003029	decreased mRNA splicing, via spliceosome	However, mutation of the conserved S131 and S133 residues to alanine in Bpb1 (denoted Bpb1-2A) caused significant intron retention in 1,598 introns (~35%) (Fig. 3b) and thus produces a defect quantitatively and qualitatively similar to inhibition of either Dsk1 (ρ = 0.62 ± 0.02; P < 10−6, two sided) or Prp4 (ρ = 0.63 ± 0.02; P < 10−6, two sided).
PMID:26167880	FYPO:0003029	decreased mRNA splicing, via spliceosome	Importantly, introns retained in a temperature-sensitive mutant of the S. pombe U2AF65 ortholog prp2 (prp2-1) (2,873 introns retained, ~62%) (Supplementary Fig. 3b) did not result in a consistent positive correlation with suboptimal cis-regulatory sequences (Fig. 4a and Supplementary Fig. 3a).
PMID:26167880	FYPO:0003029	decreased mRNA splicing, via spliceosome	Inhibition of Dsk1 and Prp4 caused a significant increase of intron retention in 1,945 (~42%) and 2,148 splicing events (~47%), respectively, thus indicating broad defects in RNA splicing (Fig. 1b). I
PMID:26167880	FYPO:0003029	decreased mRNA splicing, via spliceosome	Inhibition of Dsk1 and Prp4 caused a significant increase of intron retention in 1,945 (~42%) and 2,148 splicing events (~47%), respectively, thus indicating broad defects in RNA splicing (Fig. 1b). I
PMID:26167880	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC962.06c [part_of] mRNA cis splicing, via spliceosome	We conclude that phosphorylation of the Dsk1 substrate Bpb1 has a major effect on the genome-wide splicing pattern.
PMID:26221037	FYPO:0005629	increased cellular HMW SUMO conjugate level [has_severity] high	(comment: higher than without nup132d)
PMID:26221037	FYPO:0005619	increased level of sumoylated protein in cell [has_severity] high	(comment: higher than without nup132d)
PMID:26221037	FYPO:0000329	abnormal protein modification during vegetative growth [assayed_using] PomBase:SPAC1687.05	(comment: modification(s) not identified)
PMID:26221037	FYPO:0000329	abnormal protein modification during vegetative growth [assayed_using] PomBase:SPAC1687.05	(comment: modification(s) not identified)
PMID:26258632	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1a)
PMID:26258632	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1a)
PMID:26258632	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. 1a)
PMID:26258632	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. 1a)
PMID:26258632	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1a)
PMID:26258632	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1a)
PMID:26258632	FYPO:0005069	unequal mitotic sister chromatid segregation following normal mitosis [has_penetrance] 2	(Fig. 1b)
PMID:26258632	FYPO:0005069	unequal mitotic sister chromatid segregation following normal mitosis [has_penetrance] 3	(Fig. 1b)
PMID:26258632	FYPO:0005069	unequal mitotic sister chromatid segregation following normal mitosis [has_penetrance] 4	(Fig. 1b)
PMID:26258632	FYPO:0005069	unequal mitotic sister chromatid segregation following normal mitosis [has_penetrance] 2	(Fig. 1b)
PMID:26258632	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC3D6.04c [assayed_using] PomBase:SPAC25G10.07c	(Fig. 1e)
PMID:26258632	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC3D6.04c [assayed_using] PomBase:SPAC25G10.07c	(Fig. 1e)
PMID:26258632	GO:0000776	kinetochore [exists_during] mitotic metaphase	(Fig. 2D) (comment: CHECK unattached kinetochore nda3-KM311 arrested cell)
PMID:26258632	FYPO:0002901	normal protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPBC3D6.04c	(Fig. 2a)
PMID:26258632	FYPO:0005212	normal protein localization to kinetochore during mitotic prometaphase [assayed_using] PomBase:SPBC3D6.04c	(Fig. 2a)
PMID:26258632	FYPO:0005211	decreased protein localization to mitotic spindle pole body during anaphase [assayed_using] PomBase:SPBC3D6.04c	(Fig. 2a) (comment:diminished relocation from kinetochore)
PMID:26258632	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. 2b) (comment: mad1 localizes to unattached kinetochores) and fig 3a
PMID:26258632	FYPO:0008164	abnormal protein localization to kinetochore during mitotic M phase [assayed_protein] PomBase:SPAC25G10.07c	(Fig. 2d)
PMID:26258632	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 3 a,b)
PMID:26258632	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 3 a,b)
PMID:26258632	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 3A,B)
PMID:26258632	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 3b)
PMID:26258632	FYPO:0005069	unequal mitotic sister chromatid segregation following normal mitosis [has_penetrance] 1.5	(Fig. 3c)
PMID:26258632	FYPO:0000030	abnormal mitotic chromosome congression [has_penetrance] 27	(Fig. 5C)
PMID:26258632	FYPO:0000030	abnormal mitotic chromosome congression	"(Fig. 5c) (comment: CHECK ""gliding"" new GO term requested)"
PMID:26258632	GO:0000776	kinetochore [exists_during] mitotic prometaphase	(Figure 2a)
PMID:26258632	GO:0044732	mitotic spindle pole body [exists_during] mitotic anaphase	(Figure 2a)
PMID:26258632	FYPO:0005220	abnormal protein oligomerization	(comment: ABOLISHED tetermerization)
PMID:26258632	FYPO:0005220	abnormal protein oligomerization	(comment: ABOLISHED tetermerization) fig 4f
PMID:26258632	FYPO:0005042	normal protein localization to kinetochore [assayed_using] PomBase:SPAC25G10.07c	(comment: kinetochore localization of Cut7 is unaffected)
PMID:26264592	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:26264592	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:26264592	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:26264592	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:26264592	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:26264592	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:26264592	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2)
PMID:26264592	FYPO:0000840	normal RNA level [assayed_transcript] PomBase:SPNCRNA.1712	(Fig. 3C)
PMID:26264592	FYPO:0001889	RNA absent from cell [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 3C)
PMID:26264592	FYPO:0001889	RNA absent from cell [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 3C)
PMID:26264592	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 4A)
PMID:26264592	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 4A)
PMID:26264592	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 4A)
PMID:26264592	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 4A)
PMID:26264592	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 4A)
PMID:26264592	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 4A)
PMID:26264592	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:26264592	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:26264592	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:26264592	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:26264592	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:26264592	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:26264592	FYPO:0008028	decreased rate of acid phosphatase activation during phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5A)
PMID:26264592	FYPO:0004416	decreased RNA level during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:26264592	FYPO:0004416	decreased RNA level during cellular response to phosphate starvation [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 5B)
PMID:26264592	FYPO:0006270	increased RNA level during cellular response to phosphate starvation [assayed_transcript] PomBase:SPNCRNA.1712	(Fig. 5C)
PMID:26264592	FYPO:0002244	abolished acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:26264592	FYPO:0002244	abolished acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:26264592	FYPO:0002244	abolished acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:26264592	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:26264592	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:26264592	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:26264592	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:26264592	FYPO:0002061	inviable vegetative cell population	(Fig. 7A)
PMID:26264592	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 7A)
PMID:26264592	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	(Fig. 7A)
PMID:26264592	FYPO:0002061	inviable vegetative cell population	(Fig. 7A)
PMID:26264592	FYPO:0002061	inviable vegetative cell population	(Fig. 7A)
PMID:26264592	FYPO:0002061	inviable vegetative cell population	(Fig. 7A)
PMID:26264592	FYPO:0002061	inviable vegetative cell population	(Fig. 7A)
PMID:26264592	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 7A)
PMID:26264592	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 7A)
PMID:26264592	FYPO:0002061	inviable vegetative cell population	(Fig. 7A)
PMID:26264592	FYPO:0000080	decreased cell population growth at low temperature [has_severity] low	(Fig. 7A)
PMID:26264592	FYPO:0000080	decreased cell population growth at low temperature [has_severity] low	(Fig. 7A)
PMID:26264592	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 7A)
PMID:26264592	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 7A)
PMID:26264592	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:26264592	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S1)
PMID:26264592	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S1)
PMID:26264592	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S1)
PMID:26264592	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S1)
PMID:26264592	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S1)
PMID:26264592	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPNCRNA.1712	(Fig. S2)
PMID:26264592	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPNCRNA.1712 [has_severity] low	(Fig. S2)
PMID:26264592	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPNCRNA.1712	(Fig. S2)
PMID:26264592	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPNCRNA.1712	(Fig. S2)
PMID:26264592	FYPO:0008028	decreased rate of acid phosphatase activation during phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S3)
PMID:26264592	FYPO:0008028	decreased rate of acid phosphatase activation during phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S3)
PMID:26264592	FYPO:0008028	decreased rate of acid phosphatase activation during phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S3)
PMID:26264592	FYPO:0008028	decreased rate of acid phosphatase activation during phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S3)
PMID:26264592	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. S4)
PMID:26264592	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. S4)
PMID:26264592	GO:0140463	chromatin-protein adaptor activity [part_of] intracellular phosphate ion homeostasis	(comment: CHECK negative extracellular phosphate aquisition (S5P,P6?,S7P))
PMID:26264592	GO:0030643	intracellular phosphate ion homeostasis [has_input] PomBase:SPBC8E4.01c	(comment: CHECK negative extracellular phosphate aquisition (S5P,P6?,S7P))
PMID:26264592	GO:0030643	intracellular phosphate ion homeostasis [has_input] PomBase:SPBP4G3.02	(comment: CHECK negative extracellular phosphate aquisition (S5P,P6?,S7P))
PMID:26264592	GO:0030643	intracellular phosphate ion homeostasis	(comment: CHECK negative extracellular phosphate aquisition)
PMID:26264592	GO:0030643	intracellular phosphate ion homeostasis	(comment: CHECK negative regulation of extracellular phosphate aquisition)
PMID:26264592	GO:0030643	intracellular phosphate ion homeostasis	(comment: CHECK negative regulation of extracellular phosphate aquisition)
PMID:26275423	GO:0000775	chromosome, centromeric region	(comment: Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.)
PMID:26275423	GO:0000939	inner kinetochore	(comment: Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.)
PMID:26275423	GO:0000775	chromosome, centromeric region	(comment: Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.)
PMID:26275423	GO:0000775	chromosome, centromeric region	(comment: Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.)
PMID:26275423	GO:0000775	chromosome, centromeric region	(comment: Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.)
PMID:26275423	GO:0000775	chromosome, centromeric region	(comment: Chromatin immunoprecipitation of this protein is highly enriched for centromeric sequences.)
PMID:26365378	GO:0005515	protein binding	(Fig. S3)
PMID:26365378	GO:0005515	protein binding	(Fig. S3)
PMID:26365378	FYPO:0006274	abolished protein localization via NVT pathway [assayed_using] PomBase:SPCC1322.05c	(comment: 4h)
PMID:26365378	FYPO:0006294	normal macroautophagy during nitrogen starvation	(comment: CHECK macroautophagy? - selective autophagy is a child of macroautophagy)
PMID:26365378	FYPO:0006274	abolished protein localization via NVT pathway [assayed_using] PomBase:SPCC1322.05c	"(comment: CHECK microscopy shows ""protein localization to vacuole with protein mislocalized to cytosol"" but with additional vacuolar processing phenotypes I think we can make the BP phenotypes /AL)"
PMID:26365378	GO:0061630	ubiquitin protein ligase activity [has_input] PomBase:SPBP35G2.11c [part_of] cytoplasm to vacuole targeting by the NVT pathway	(comment: Indirect evidence, could be upstream)
PMID:26365378	GO:0061630	ubiquitin protein ligase activity [has_input] PomBase:SPBP35G2.11c [part_of] cytoplasm to vacuole targeting by the NVT pathway	(comment: Indirect evidence, could be upstream)
PMID:26365378	GO:0061630	ubiquitin protein ligase activity [has_input] PomBase:SPBP35G2.11c [part_of] cytoplasm to vacuole targeting by the NVT pathway	(comment: Indirect evidence, could be upstream)
PMID:26366556	FYPO:0001122	elongated vegetative cell [has_penetrance] low	(comment: CHECK low penetrance)
PMID:26366556	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(comment: CHECK low penetrance)
PMID:26366556	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] low	(comment: CHECK low penetrance)
PMID:26366556	GO:0019216	regulation of lipid metabolic process	(comment: ChIP-seq and microarray data indicate that Cbf11 regulates lipid metabolism genes.)
PMID:26366556	GO:0043565	sequence-specific DNA binding [occurs_at] CSL_response_element	(comment: determined by EMSA. Substrate: dsDNA oligonucleotide derived from promoters of cut6 and ptl1 genes (contain the CSL_response_element))
PMID:26366556	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC1281.06c	(comment: determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c)
PMID:26366556	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC56E4.04c	(comment: determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c)
PMID:26366556	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC22A12.06c	(comment: determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c)
PMID:26366556	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC18H10.02	(comment: determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c)
PMID:26366556	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC1450.16c	(comment: determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c)
PMID:26366556	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBP4H10.11c	(comment: determined by expression microarrays from cbf11 knock-out cells growing exponentially in YES. targets: SPAC22A12.06c, ptl1, lcf1, lcf2, cut6, SPCC1281.06c)
PMID:26366556	FYPO:0007474	variable cell size at division [has_penetrance] low	(comment: large fractions of both abnormally long and abnormally short cells are present in the population)
PMID:26366556	FYPO:0001122	elongated vegetative cell [has_penetrance] low	(comment: large fractions of both abnormally long and abnormally short cells are present in the population)
PMID:26401015	FYPO:0006450	altered histone H3 acetyltransferase substrate specificity [assayed_enzyme] PomBase:SPAC1952.05	(comment: abolishes preference for K4-trimethylated H3)
PMID:26401015	FYPO:0006452	decreased histone H3 acetyltransferase processivity [assayed_enzyme] PomBase:SPAC1952.05	(comment: acetyltransferase normally processive in presence of K4-trimethylated H3 -bound by Sgf29)
PMID:26401015	FYPO:0006452	decreased histone H3 acetyltransferase processivity [assayed_enzyme] PomBase:SPAC1952.05	(comment: acetyltransferase normally processive in presence of K4-trimethylated H3 -bound by Sgf29)
PMID:26401015	FYPO:0006450	altered histone H3 acetyltransferase substrate specificity [assayed_enzyme] PomBase:SPAC1952.05	(comment:abolishes preference for K4-trimethylated H3)
PMID:26412298	GO:0061578	K63-linked deubiquitinase activity	(comment: Inferred from in vitro biochemical assay using K63-linked di-ubiquitinase)
PMID:26422458	GO:0051537	2 iron, 2 sulfur cluster binding	Biochemical and mutagenic studies demonstrated that the [2Fe-2S]2+ cluster substantially inhibits the phosphatase activity of Asp1, thereby increasing its net kinase activity.
PMID:26424849	FYPO:0001768	abolished tRNA-Asp C38 methylation [assayed_using] aspartyl_tRNA	(comment: CHECK waiting for go-ontology/issues/12536)
PMID:26424849	GO:0016428	tRNA (cytidine-N5)-methyltransferase activity	(comment: in response to queuosine incorporation into tRNA-Asp)
PMID:26436826	FYPO:0005031	increased ribonucleotide incorporation on lagging strand [has_penetrance] medium	(comment: alkaline DNA preparation)
PMID:26436826	FYPO:0005030	increased ribonucleotide incorporation on leading strand [has_penetrance] medium	(comment: alkaline DNA preparation)
PMID:26438724	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_using] PomBase:SPAC1556.01c	(Fig. 5)
PMID:26438724	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_using] PomBase:SPAC1556.01c	(Fig. 5)
PMID:26438724	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_using] PomBase:SPAP4C9.02	(Fig. 5)
PMID:26438724	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_using] PomBase:SPAC1556.01c	(Fig. 5)
PMID:26438724	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_using] PomBase:SPAP4C9.02	(Fig. 5)
PMID:26438724	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_using] PomBase:SPAP4C9.02	(Fig. 5)
PMID:26438724	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level	(Fig. 6)
PMID:26438724	FYPO:0006362	decreased borderline-derived siRNA level	(Fig. 6)
PMID:26438724	FYPO:0004749	increased spatial extent of subtelomeric heterochromatin assembly	(Figure 4a)
PMID:26438724	FYPO:0005286	heterochromatin assembly beyond boundary element IRC1L	(Figure 4a)
PMID:26438724	FYPO:0003045	heterochromatin assembly beyond boundary element IRC1R	(Figure 4a)
PMID:26438724	FYPO:0006359	decreased protein exchange at pericentric heterochromatin [assayed_using] PomBase:SPAC664.01c	(Supp. Fig. 1b)
PMID:26438724	FYPO:0006360	increased protein exchange at pericentric heterochromatin [assayed_using] PomBase:SPAC664.01c	(Supp. Fig. 1b)
PMID:26438724	FYPO:0006370	decreased protein exchange at subtelomeric heterochromatin [assayed_using] PomBase:SPAC664.01c	(Supp. Fig. 1b)
PMID:26438724	FYPO:0000220	increased centromeric outer repeat transcript level	(Supp. Fig. 1b)
PMID:26438724	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(comment: EV3)
PMID:26438724	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] high	(comment: EV3)
PMID:26438724	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] low	(comment: EV3)
PMID:26438724	FYPO:0006361	increased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth [assayed_using] PomBase:SPAC212.11	(comment: EV3)
PMID:26438724	FYPO:0006361	increased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth [assayed_using] PomBase:SPBCPT2R1.08c	(comment: EV3)
PMID:26438724	FYPO:0004137	decreased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth	(comment: EV3)
PMID:26438724	FYPO:0002355	decreased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth	(comment: EV3)
PMID:26438724	GO:0033696	heterochromatin boundary formation	(comment: changed from: heterochromatin organization involved in chromatin silencing)
PMID:26438724	GO:0031507	heterochromatin formation	(comment: changed from: heterochromatin organization involved in chromatin silencing)
PMID:26443059	FYPO:0005053	abnormal RITS complex assembly	(comment: inferred from protein binding phenotypes)
PMID:26443059	FYPO:0005053	abnormal RITS complex assembly	(comment: inferred from protein binding phenotypes)
PMID:26443240	GO:0031117	positive regulation of microtubule depolymerization	(comment: CHECK through negative regulation of Cls1)
PMID:26443240	FYPO:0007705	normal protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1 does not relocalize to cell sides)
PMID:26443240	FYPO:0007703	abolished protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1 does not relocalize to cell sides)
PMID:26443240	FYPO:0007703	abolished protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1 does not relocalize to cell sides)
PMID:26443240	FYPO:0007703	abolished protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1 does not relocalize to cell sides)
PMID:26443240	FYPO:0007703	abolished protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1 does not relocalize to cell sides)
PMID:26443240	FYPO:0007703	abolished protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1 does not relocalize to cell sides)
PMID:26443240	FYPO:0007703	abolished protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1 does not relocalize to cell sides)
PMID:26443240	FYPO:0007704	decreased protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1 relocalization to cell sides)
PMID:26443240	FYPO:0007705	normal protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1 relocalizes to cell sides)
PMID:26443240	FYPO:0007705	normal protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1 relocalizes to cell sides)
PMID:26443240	FYPO:0007705	normal protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1 relocalizes to cell sides)
PMID:26443240	FYPO:0007705	normal protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1 relocalizes to cell sides)
PMID:26443240	FYPO:0007705	normal protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPAC2F7.03c	(comment: Pom1 relocalizes to cell sides)
PMID:26443240	FYPO:0007703	abolished protein localization to lateral cell cortex during glucose starvation [assayed_using] PomBase:SPBC1706.01	(comment: Tea4 does not relocalize to cell sides)
PMID:26443240	GO:0005634	nucleus	absent when glucose limited
PMID:26483559	FYPO:0005384	meiosis I metaphase/anaphase transition delay	(Fig. 1B)
PMID:26483559	FYPO:0005510	meiosis II metaphase/anaphase transition delay	(Fig. 1B)
PMID:26483559	FYPO:0005510	meiosis II metaphase/anaphase transition delay [has_severity] medium	(Fig. 1D)
PMID:26483559	FYPO:0005383	normal duration of meiosis I	(Fig. 1D)
PMID:26483559	FYPO:0005509	abnormal meiotic sister chromatid segregation	(Fig. 1b)
PMID:26483559	FYPO:0004213	abnormal attachment of mitotic spindle microtubules to kinetochore [has_penetrance] 67	(Fig. 2)
PMID:26483559	FYPO:0004093	normal meiotic telomere clustering	(Fig. 3A,B, S5)
PMID:26483559	FYPO:0004667	normal meiotic sister chromatid cohesion at centromere	(Fig. 4, C and D)
PMID:26483559	FYPO:0004762	abnormal protein localization to kinetochore during meiosis [assayed_using] PomBase:SPBC409.04c [has_penetrance] 53	(Fig. 6) (comment: CHECK increased or premature)
PMID:26483559	FYPO:0004762	abnormal protein localization to kinetochore during meiosis [has_penetrance] 77 [assayed_using] PomBase:SPCC1020.02	(Fig. 6) (comment: CHECK increased or premature)
PMID:26483559	FYPO:0004214	normal protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPAC27F1.04c	(Fig. 7, B and C)
PMID:26483559	FYPO:0004214	normal protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPBC11C11.03	(Fig. 7C)
PMID:26483559	FYPO:0004762	abnormal protein localization to kinetochore during meiosis [assayed_using] PomBase:SPCC1322.12c	(Fig. 8, B and C) (comment: CHECK increased or premature)
PMID:26483559	FYPO:0000579	normal spore germination	(Fig. 9A)
PMID:26483559	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Fig. 9A)
PMID:26483559	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Fig. 9A)
PMID:26483559	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Fig. 9A)
PMID:26483559	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Fig. 9A)
PMID:26483559	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Fig. 9A)
PMID:26483559	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Fig. 9A)
PMID:26483559	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	(Fig. 9A)
PMID:26483559	FYPO:0000581	decreased spore germination frequency [has_penetrance] 48	(Fig. 9A)
PMID:26483559	FYPO:0000581	decreased spore germination frequency [has_penetrance] 28	(Fig. 9A)
PMID:26483559	FYPO:0000581	decreased spore germination frequency [has_penetrance] 61	(Fig. 9A)
PMID:26483559	FYPO:0000581	decreased spore germination frequency [has_penetrance] 44	(Fig. 9A)
PMID:26483559	FYPO:0000581	decreased spore germination frequency [has_penetrance] 61	(Fig. 9A)
PMID:26483559	FYPO:0000581	decreased spore germination frequency [has_penetrance] 51	(Fig. 9A)
PMID:26483559	GO:1905318	meiosis I spindle assembly checkpoint signaling	(Fig. 9a,) there other evidence elsewhere but we don't have this annotation on mad2 at present...
PMID:26483559	FYPO:0005512	increased activation of meiosis I spindle assembly checkpoint	(Fig. S1) (comment: Assayed by assaying depletion of securin from spindle)
PMID:26483559	FYPO:0005574	abnormal nuclear transport during meiosis	(Fig. S2)
PMID:26499799	GO:0030295	protein kinase activator activity	(comment: cerevisiae substrate)
PMID:26518661	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Figure 1)
PMID:26518661	FYPO:0006985	heterochromatin assembly beyond boundary element IRL	(Figure 1)
PMID:26518661	FYPO:0001125	normal vegetative cell shape	(Figure 1)
PMID:26518661	FYPO:0000024	stubby vegetative cell	(Figure 1)
PMID:26518661	FYPO:0001355	decreased vegetative cell population growth	(Figure 2)
PMID:26518661	FYPO:0006985	heterochromatin assembly beyond boundary element IRL	(Figure 2)
PMID:26518661	FYPO:0006986	normal spatial extent of heterochromatin assembly to boundary element IRL	(Figure 2)
PMID:26518661	FYPO:0006986	normal spatial extent of heterochromatin assembly to boundary element IRL	(Figure 2)
PMID:26518661	FYPO:0006986	normal spatial extent of heterochromatin assembly to boundary element IRL	(Figure 2)
PMID:26518661	FYPO:0006986	normal spatial extent of heterochromatin assembly to boundary element IRL	(Figure 2)
PMID:26518661	FYPO:0006986	normal spatial extent of heterochromatin assembly to boundary element IRL	(Figure 2)
PMID:26518661	FYPO:0006986	normal spatial extent of heterochromatin assembly to boundary element IRL	(Figure 2)
PMID:26518661	FYPO:0006985	heterochromatin assembly beyond boundary element IRL	(Figure 2)
PMID:26518661	FYPO:0006986	normal spatial extent of heterochromatin assembly to boundary element IRL	(Figure 2)
PMID:26518661	FYPO:0006986	normal spatial extent of heterochromatin assembly to boundary element IRL	(Figure 2)
PMID:26518661	FYPO:0004138	increased histone H3-K9 dimethylation at telomere during vegetative growth	(Figure 4)
PMID:26518661	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	(Figure 4)
PMID:26518661	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_using] PomBase:SPCC70.09c	(Figure 4)
PMID:26518661	FYPO:0006988	increased histone H3-K9 dimethylation at transposable element during vegetative growth	(Figure 4)
PMID:26518661	FYPO:0006989	normal histone H3-K9 dimethylation at transposable element during vegetative growth	(Figure 4)
PMID:26518661	FYPO:0006989	normal histone H3-K9 dimethylation at transposable element during vegetative growth	(Figure 4)
PMID:26518661	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_using] PomBase:SPAC23H3.14	(Figure 4)
PMID:26518661	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_using] PomBase:SPBC24C6.09c	(Figure 4)
PMID:26518661	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_using] PomBase:SPAC13A11.03	(Figure 4)
PMID:26518661	FYPO:0000862	normal histone H3-K9 dimethylation at centromere during vegetative growth	(Figure 4)
PMID:26518661	FYPO:0006990	increased spatial extent of heterochromatin assembly at protein coding gene [assayed_using] PomBase:SPAC23H3.14	(Figure 4)
PMID:26518661	FYPO:0006991	normal spatial extent of heterochromatin assembly at protein coding gene [assayed_using] PomBase:SPAC23H3.14	(Figure 4)
PMID:26518661	FYPO:0006991	normal spatial extent of heterochromatin assembly at protein coding gene [assayed_using] PomBase:SPAC23H3.14	(Figure 4)
PMID:26518661	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_using] PomBase:SPBC32H8.11	(Figure 4)
PMID:26518661	FYPO:0006987	increased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth	(Figure 4)
PMID:26518661	FYPO:0006995	normal chromatin silencing at centromere inner repeat	(Figure 5)
PMID:26518661	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Figure 5)
PMID:26518661	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Figure 5)
PMID:26518661	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Figure 5)
PMID:26518661	FYPO:0001839	normal minichromosome loss	(Figure 5)
PMID:26518661	FYPO:0001839	normal minichromosome loss	(Figure 5)
PMID:26518661	FYPO:0005371	increased linear minichromosome loss during vegetative growth	(Figure 5)
PMID:26518661	FYPO:0006992	normal chromatin silencing at centromere otr1R	(Figure 5)
PMID:26518661	FYPO:0006992	normal chromatin silencing at centromere otr1R	(Figure 5)
PMID:26518661	FYPO:0006993	decreased chromatin silencing at centromere otr1R	(Figure 5)
PMID:26518661	FYPO:0006993	decreased chromatin silencing at centromere otr1R	(Figure 5)
PMID:26518661	FYPO:0006993	decreased chromatin silencing at centromere otr1R	(Figure 5)
PMID:26518661	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Figure 5)
PMID:26518661	FYPO:0006994	increased chromatin silencing at centromere otr1L	(Figure 5)
PMID:26518661	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Figure 5)
PMID:26518661	FYPO:0006995	normal chromatin silencing at centromere inner repeat	(Figure 5)
PMID:26518661	FYPO:0006995	normal chromatin silencing at centromere inner repeat	(Figure 5)
PMID:26518661	FYPO:0006995	normal chromatin silencing at centromere inner repeat	(Figure 5)
PMID:26518661	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure 5)
PMID:26518661	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure 5)
PMID:26518661	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure 5)
PMID:26518661	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure 5)
PMID:26518661	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure 5)
PMID:26518661	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure 5)
PMID:26518661	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure 5)
PMID:26518661	FYPO:0003094	decreased centromeric outer repeat transcript level	(Figure 5)
PMID:26518661	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Figure 7)
PMID:26518661	FYPO:0006997	decreased histone exchange at silent mating-type cassette during vegetative growth	(Figure 7)
PMID:26518661	FYPO:0007004	decreased histone exchange at protein coding gene during vegetative growth [assayed_using] PomBase:SPAC29B12.03	(Figure 7)
PMID:26518661	FYPO:0007004	decreased histone exchange at protein coding gene during vegetative growth [assayed_using] PomBase:SPAC1556.01c	(Figure 7)
PMID:26518661	FYPO:0004748	decreased histone exchange at pericentric heterochromatin	(Figure 7)
PMID:26518661	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 7)
PMID:26518661	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 7)
PMID:26518661	FYPO:0004376	increased chromatin silencing at silent mating-type cassette	(Figure 7)
PMID:26518661	FYPO:0007004	decreased histone exchange at protein coding gene during vegetative growth [assayed_using] PomBase:SPAC4H3.10c	(Figure 7)
PMID:26518661	FYPO:0007004	decreased histone exchange at protein coding gene during vegetative growth [assayed_using] PomBase:SPAPB1A10.02	(Figure 7)
PMID:26518661	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Figure 7)
PMID:26518661	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Figure 7)
PMID:26518661	FYPO:0007001	normal histone exchange at pericentric heterochromatin	(Figure 7)
PMID:26518661	FYPO:0007000	normal histone exchange at transposable element	(Figure 7)
PMID:26518661	FYPO:0007002	normal histone exchange at silent mating-type cassette	(Figure 7)
PMID:26518661	FYPO:0007003	normal histone exchange at tRNA genes	(Figure 7)
PMID:26518661	FYPO:0007002	normal histone exchange at silent mating-type cassette	(Figure 7)
PMID:26518661	FYPO:0007001	normal histone exchange at pericentric heterochromatin	(Figure 7)
PMID:26518661	FYPO:0007000	normal histone exchange at transposable element	(Figure 7)
PMID:26518661	FYPO:0006998	decreased histone exchange at transposable element during vegetative growth	(Figure 7)
PMID:26525038	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC1223.06	Cki3 interacted with the polarity factor Tea1, of which phosphorylation was dependent on Cki3 kinase activity
PMID:26527280	FYPO:0001357	normal vegetative cell population growth	(Fig. 1I)
PMID:26527280	FYPO:0001357	normal vegetative cell population growth	(Fig. 1J)
PMID:26527280	FYPO:0000274	increased duration of mitotic M phase [has_severity] high	(Fig. 3A, 3B)
PMID:26527280	FYPO:0000274	increased duration of mitotic M phase [has_severity] medium	(Fig. 3E, 3F)
PMID:26527280	FYPO:0004198	decreased protein degradation during mitosis [assayed_using] PomBase:SPBC14C8.01c	(Fig. 4D, 4E)
PMID:26527280	FYPO:0004198	decreased protein degradation during mitosis [assayed_using] PomBase:SPBC582.03 [has_severity] low	(Fig. 4G, 4H)
PMID:26527280	FYPO:0004198	decreased protein degradation during mitosis [assayed_using] PomBase:SPBC14C8.01c	(Fig. 5C)
PMID:26527280	MOD:01148	ubiquitinylated lysine [present_during] mitotic M phase	(Fig. 6G, S7F, S7G) (comment: TUBE pull-down)
PMID:26527280	FYPO:0002151	inviable spore	(Fig. 7D, 7E) (comment: tetrad dissection)
PMID:26527280	FYPO:0000274	increased duration of mitotic M phase [has_severity] medium	(Fig. S2B)
PMID:26527280	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPAC637.10c [has_severity] high	(Fig. S3A, S3B) (comment: control for increased proteasome in nucleus)
PMID:26527280	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPAC31G5.13 [has_severity] low	(Fig. S3A, S3C)
PMID:26527280	FYPO:0005410	normal protein degradation during mitosis [assayed_using] PomBase:SPBC14C8.01c	(Fig. S3D)
PMID:26527280	FYPO:0005410	normal protein degradation during mitosis [assayed_using] PomBase:SPBC14C8.01c	(Fig. S3G, S3H)
PMID:26527280	FYPO:0005410	normal protein degradation during mitosis [assayed_using] PomBase:SPBC582.03	(Fig. S3I, S3J)
PMID:26527280	FYPO:0004198	decreased protein degradation during mitosis [assayed_using] PomBase:SPBC14C8.01c [has_severity] low	(Fig. S6D)
PMID:26527280	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPBC11B10.09 [has_severity] low	(Fig. S6L, S6M)
PMID:26527280	FYPO:0000274	increased duration of mitotic M phase [has_severity] high	(Figure 2A) Plo1 to SPBs persisted for more than 20 min
PMID:26527280	FYPO:0001920	decreased protein export from nucleus [assayed_using] PomBase:SPBC11B10.09	(Figure S2F export of CDK1 from the nucleus, which depends on cyclin B degradation ,, was delayed
PMID:26527280	FYPO:0004705	delayed onset of mitotic sister chromatid separation	(Figures 3B, 3D). sister chromatid separation (which depends on securin degradation, not on cyclin B degradation) was delayed as well
PMID:26527280	FYPO:0001491	viable vegetative cell [has_penetrance] 95	(comment: tetrad dioscection) Fig. 7C, 7E
PMID:26527280	FYPO:0001491	viable vegetative cell [has_penetrance] 80	(comment: tetrad disection) Fig. 7D, 7E
PMID:26527280	FYPO:0004705	delayed onset of mitotic sister chromatid separation [has_severity] low	In contrast, there was only a very slight delay in sister chromatid separation (Figures 2A and 2B).
PMID:26527280	FYPO:0001946	abolished mitotic sister chromatid separation	chromosomes failed to split, but Plo1 was removed from SPBs with timing similar to that in wild-type cells (Figures 2A and 2C).
PMID:26527280	FYPO:0004310	normal duration of mitotic M phase	chromosomes failed to split, but Plo1 was removed from SPBs with timing similar to that in wild-type cells (Figures 2A and 2C).
PMID:26536126	FYPO:0005173	increased protein localization to cell surface	(comment: CHECK assayed_using(PomBase:fur4))
PMID:26536126	FYPO:0001012	growth auxotrophic for uracil	(comment: CHECK auxotrophic for cytosine, uridine and UMP)
PMID:26536126	FYPO:0000647	vegetative cell lysis	(comment: CHECK cell lysis on uracil depleted medium)
PMID:26536126	GO:0005783	endoplasmic reticulum	(comment: CONDITION grown in EMM or YES medium)
PMID:26536126	GO:0000139	Golgi membrane	(comment: CONDITION nitrogen rich)
PMID:26536126	GO:0000324	fungal-type vacuole	(comment: CONDITION nitrogen rich)
PMID:26536126	GO:0015210	uracil transmembrane transporter activity [happens_during] cellular response to nitrogen starvation	(comment: inability to take up 14-C uracil in fur4 deletion mutant)
PMID:26536126	GO:1905530	negative regulation of uracil import across plasma membrane	(comment: uracil uptake enhancement in pub1 deletion)
PMID:26545917	FYPO:0002060	viable vegetative cell population	(Fig. 2c)
PMID:26582768	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: CHECK Increased MMS sensitivity)
PMID:26582768	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: CHECK Increased MMS sensitivity)
PMID:26582768	GO:0140673	transcription elongation-coupled chromatin remodeling	Cells lacking abo1(+) experience both a reduction and mis-positioning of nucleosomes at transcribed sequences in addition to increased intragenic transcription, phenotypes that are hallmarks of defective chromatin re-establishment behind RNA polymerase II
PMID:26652183	FYPO:0005624	sensitive to UV during mitotic S phase [has_severity] high	(comment: CONDITION 2 or 5 J/m2 UV) Fig. 3F, Fig. S6
PMID:26652183	FYPO:0005627	increased duration of mitotic DNA damage checkpoint during cellular response to UV during mitotic S phase [has_penetrance] high [has_severity] high	(comment: CONDITION 2 or 5 J/m2 UV) Fig. 3F, Fig. S6
PMID:26652183	FYPO:0003445	increased duration of mitotic DNA damage checkpoint during cellular response to UV [has_penetrance] high [has_severity] high	(comment: CONDITION 25 J/m2 UV) delay is greater than rad51delta alone (Fig. 5A)
PMID:26652183	FYPO:0003445	increased duration of mitotic DNA damage checkpoint during cellular response to UV [has_penetrance] high [has_severity] high	(comment: CONDITION 5 J/m2 UV) Delay is greater than rad51delta alone (see Fig. S7)
PMID:26652183	FYPO:0005299	normal mitotic G2 DNA damage checkpoint during cellular response to UV [has_penetrance] high	(comment: CONDITION 5 J/m2 UV) Fig 1A, Fig. S2
PMID:26652183	FYPO:0003445	increased duration of mitotic DNA damage checkpoint during cellular response to UV [has_penetrance] high [has_severity] high	(comment: CONDITION 5 J/m2 UV) Fig. 1B
PMID:26652183	FYPO:0003445	increased duration of mitotic DNA damage checkpoint during cellular response to UV [has_penetrance] medium [has_severity] medium	(comment: CONDITION 5 J/m2 UV) Fig. 1B, Fig. 3E
PMID:26652183	FYPO:0005626	normal mitotic G2 DNA damage checkpoint during cellular response to UV during mitotic S phase [has_penetrance] complete	(comment: CONDITION 5 J/m2 UV) Fig. 3B
PMID:26652183	FYPO:0005627	increased duration of mitotic DNA damage checkpoint during cellular response to UV during mitotic S phase [has_severity] medium [has_penetrance] medium	(comment: CONDITION 5 J/m2 UV) Fig. 3C
PMID:26652183	FYPO:0005624	sensitive to UV during mitotic S phase [has_severity] high	(comment: CONDITION 5 J/m2 UV) Fig. 3C
PMID:26652183	FYPO:0005624	sensitive to UV during mitotic S phase [has_severity] high	(comment: CONDITION 5 J/m2 UV) Fig. 3D
PMID:26652183	FYPO:0005624	sensitive to UV during mitotic S phase [has_severity] high	(comment: CONDITION 5 J/m2 UV) Fig. 3E
PMID:26652183	FYPO:0005626	normal mitotic G2 DNA damage checkpoint during cellular response to UV during mitotic S phase [has_penetrance] complete	(comment: CONDITION 5 J/m2 UV) Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	FYPO:0005626	normal mitotic G2 DNA damage checkpoint during cellular response to UV during mitotic S phase [has_penetrance] complete	(comment: CONDITION 5 J/m2 UV) Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	FYPO:0005624	sensitive to UV during mitotic S phase [has_severity] high	(comment: CONDITION 5 J/m2 UV) Fig. S3
PMID:26652183	FYPO:0003445	increased duration of mitotic DNA damage checkpoint during cellular response to UV [has_severity] medium [has_penetrance] medium	(comment: CONDITION 5 J/m2 UV) Figure 1B, Figure 3D, Figure S6
PMID:26652183	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: CONDITION 5 J/m2 UV) Sensitivity is greater than rad51delta or eso1-D147N single mutants (see Fig. S7)
PMID:26652183	FYPO:0003445	increased duration of mitotic DNA damage checkpoint during cellular response to UV [has_severity] medium [has_penetrance] medium	(comment: CONDITION 5 J/m2 UV) duration is similar to eso1-D147N alone (see Fig. 3H)
PMID:26652183	FYPO:0003445	increased duration of mitotic DNA damage checkpoint during cellular response to UV [has_severity] medium [has_penetrance] medium	(comment: CONDITION 5 J/m2 UV) duration is similar to rad8delta or rhp18delta single mutants (see Fig. 3G)
PMID:26652183	FYPO:0005624	sensitive to UV during mitotic S phase [has_severity] high	(comment: CONDITION 5 J/m2 UV) sensitivity similar to rad8delta and rhp18delta single mutants (Fig. 3G)
PMID:26652183	FYPO:0005624	sensitive to UV during mitotic S phase [has_severity] high	(comment: CONDITION 5 J/m2 UV) similar sensitivity to eso1-D147N single mutant (Fig. 3H)
PMID:26652183	FYPO:0005623	sensitive to UV during late mitotic G2 phase [has_severity] low	(comment: CONDITION 5 or 10 J/m2 UV) Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	FYPO:0005623	sensitive to UV during late mitotic G2 phase [has_severity] low	(comment: CONDITION 5 or 10 J/m2 UV) Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	FYPO:0005625	normal viability following cellular response to UV during mitotic S phase	(comment: CONDITION 5 or 10 J/m2 UV) Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	FYPO:0005625	normal viability following cellular response to UV during mitotic S phase	(comment: CONDITION 5 or 10 J/m2 UV) Fig. 3I, Fig. 4A, Fig. S6
PMID:26652183	FYPO:0005623	sensitive to UV during late mitotic G2 phase [has_severity] low	(comment: CONDITION 5 or 10 J/m2 UV) similar sensitivity to rev1delta and rev3delta single mutants (Fig. 3I, Fig. 4A, Fig. S6)
PMID:26670050	FYPO:0001908	increased pre-mRNA level [assayed_using] PomBase:SPAC5D6.01	(Fig. S4B)
PMID:26670050	FYPO:0000265	sensitive to DNA damage [assayed_using] PomBase:SPCC736.12c	(Fig. S5e)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC1289.13c	(comment: CHECK SPBC1289.13c)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC1235.04c	(comment: CHECK SPCC1235.04c)
PMID:26670050	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPCC736.12c	(comment: CHECK gene affected: rps2202)
PMID:26670050	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPCC736.12c	(comment: CHECK gene locus affected: dbp2)
PMID:26670050	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPCC736.12c	(comment: CHECK gene locus affected: rps2202)
PMID:26670050	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPCC736.12c	(comment: CHECK gene locus: rps2202)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPCC1020.01c	(comment: CHECK increase > 10-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.1366	(comment: CHECK increase > 10-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPCC1393.07c	(comment: CHECK increase > 10-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPCC737.04	(comment: CHECK increase > 10-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC25G10.04c	(comment: CHECK increase > 10-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.577	(comment: CHECK increase > 10-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC57A10.04	(comment: CHECK increase > 10-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC6B12.16	(comment: CHECK increase > 10-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC3E7.02c	(comment: CHECK increase > 10-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC2G2.09c	(comment: CHECK increase > 10-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.103	(comment: CHECK increase > 40-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC646.17c	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC582.06c	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC839.06	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC6G9.13c	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.1303	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.1289	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.1330	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.584	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.1005	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.850	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.1613	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.1696	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.1405	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.1271	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBP4G3.03	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC1347.12	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBPB21E7.04c	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC577.05c	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPNCRNA.1330	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPCC4E9.01c	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC29A10.02	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC6C3.05	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC23C4.07	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC1556.06	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPCC320.07c	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.1224	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC216.02	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC17A5.18c	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPNCRNA.1608	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.1529	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.1273	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPNCRNA.585	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC869.08	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPCC338.18	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC4H3.08	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPCC757.02c	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC29A4.12c	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPCC1840.12	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC29A10.14	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC1718.02	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC22H10.13	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC13G7.02c	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBP8B7.04	(comment: CHECK increase > 5-fold)
PMID:26670050	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPCC1223.12c	(comment: CHECK increase > 50-fold)
PMID:26670050	FYPO:0002931	increased poly(A) tail length [assayed_using] PomBase:SPAC5D6.01	(comment: affects unspliced pre-mRNA)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBP8B7.16c	(comment: enrichment in CRAC > 10-fold (vw changed dpp2->dbp2))
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC19C7.07c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC57A10.08c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC1322.03	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC2D10.13	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC16A11.06c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC27D7.05c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC4F10.08	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC1652.01	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC25B8.14	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC27B12.07	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC1834.06c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC337.12	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC4G8.09	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC227.17c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC1683.04	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC21H7.02	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC4G9.07	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC18B11.07c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC1442.04c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC1B2.05	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBP8B7.15c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC725.02	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC1F3.04c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC9B6.03	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC6F6.16c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC13G7.11	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC13G6.08	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAPB1E7.06c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC1039.03	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC14F5.11c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC22F3.12c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC3G9.13c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC688.09	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0005515	protein binding [has_input] PomBase:SPCC613.12c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0005515	protein binding [has_input] PomBase:SPCC970.07c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC56E4.07	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC887.14c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC4B4.11	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC19B12.11c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC19A8.01c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC3H1.04c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC569.07	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC9E9.14	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC23G7.14	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC405.02c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC343.06c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC1183.05c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC970.02	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC1071.13	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC11E10.01	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC70.06	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC36.11	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC23C4.11	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC11E3.10	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC24C9.13c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC3C7.06c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC3E7.14	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC1604.10	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC188.04c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC4G8.08	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC359.01	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC830.09c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC13F5.01c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC609.04	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC25B2.11	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC27B12.04c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAP7G5.03	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC4G3.10c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC27E2.10c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0005515	protein binding	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC1783.06c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC1705.02	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC1F8.06	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC839.09c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC31G5.10	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC1F7.06	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC2D10.06	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC119.14	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC70.09c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC29A10.14	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC32A11.01	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC1718.02	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBP8B7.04	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC1347.12	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC216.02	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC582.06c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC646.17c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC23C4.07	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC6C3.05	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC29A10.02	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPAC57A10.04	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPCC1223.12c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0106222	lncRNA binding	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC2G2.09c	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0140517	protein-RNA adaptor activity [has_input] PomBase:SPBC32H8.11	(comment: enrichment in CRAC > 10-fold)
PMID:26670050	GO:0106222	lncRNA binding	(comment: enrichment in CRAC > 10-fold; Mmi1 binds the 5' extended region of the overlapping regulatory lncRNA prt)
PMID:26687354	GO:0030892	mitotic cohesin complex	(Figure 1C)
PMID:26687354	GO:0030892	mitotic cohesin complex	(Figure 1C)
PMID:26687354	GO:0007064	mitotic sister chromatid cohesion	(Figure 2)
PMID:26687354	GO:0007064	mitotic sister chromatid cohesion	(Figure 2)
PMID:26687354	GO:0007064	mitotic sister chromatid cohesion	(Figure 2B)
PMID:26687354	GO:0007064	mitotic sister chromatid cohesion	(Figure 2B) (comment: dependent on pds5)
PMID:26687354	FYPO:0001168	decreased ATPase activity [assayed_enzyme] mitotic cohesin complex	(Figure 3B)
PMID:26687354	FYPO:0005557	decreased mitotic cohesin unloading [assayed_enzyme] mitotic cohesin complex	(Figure 3B)
PMID:26687354	FYPO:0005557	decreased mitotic cohesin unloading	(Figure 3B)
PMID:26687354	FYPO:0001168	decreased ATPase activity [assayed_enzyme] mitotic cohesin complex	(Figure 3B)
PMID:26687354	FYPO:0001168	decreased ATPase activity [assayed_enzyme] mitotic cohesin complex	(Figure 3B)
PMID:26687354	FYPO:0005555	decreased mitotic cohesin loading	(Figure 6A)
PMID:26687354	FYPO:0005556	abolished mitotic cohesin loading	(Figure 6A)
PMID:26687354	GO:0003677	DNA binding [part_of] mitotic sister chromatid cohesion	(Figure 6B) (comment: CHECK acetylated form acts as a DNA sensor)
PMID:26687354	FYPO:0005557	decreased mitotic cohesin unloading	(Figure 6C)
PMID:26687354	GO:0061776	ATP-dependent topological DNA co-entrapment activity [part_of] mitotic sister chromatid cohesion	(Figure S4C)
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	(Fig 3A)
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] medium	(Fig 4A).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S2A)
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S2A)
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S2A)
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Both rapamycin (0.2 μg/ml) and Torin1 (2 μM) rescued the growth defects of Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 2A).
PMID:26689777	FYPO:0006148	abolished transcription during nitrogen starvation [assayed_transcript] PomBase:SPAC1039.09	By contrast, in Δlam2 cells and Δgtr2 cells, basal isp5+ transcriptional activity and its activation induced by nitrogen depletion were abolished (Fig 4B).
PMID:26689777	FYPO:0006148	abolished transcription during nitrogen starvation [assayed_transcript] PomBase:SPAC1039.09	By contrast, in Δlam2 cells and Δgtr2 cells, basal isp5+ transcriptional activity and its activation induced by nitrogen depletion were abolished (Fig 4B).
PMID:26689777	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPAPB1E7.12	By contrast, Δlam2 cells, Δgtr1 cells and Δgtr2 cells showed increased Rps6 phosphorylation under nitrogen depletion, compared with wild-type cells, especially at 15 min (Fig 5).
PMID:26689777	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPAC13G6.07c	By contrast, Δlam2 cells, Δgtr1 cells and Δgtr2 cells showed increased Rps6 phosphorylation under nitrogen depletion, compared with wild-type cells, especially at 15 min (Fig 5).
PMID:26689777	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPAC13G6.07c	By contrast, Δlam2 cells, Δgtr1 cells and Δgtr2 cells showed increased Rps6 phosphorylation under nitrogen depletion, compared with wild-type cells, especially at 15 min (Fig 5).
PMID:26689777	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPAPB1E7.12	By contrast, Δlam2 cells, Δgtr1 cells and Δgtr2 cells showed increased Rps6 phosphorylation under nitrogen depletion, compared with wild-type cells, especially at 15 min (Fig 5).
PMID:26689777	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPAPB1E7.12	By contrast, Δlam2 cells, Δgtr1 cells and Δgtr2 cells showed increased Rps6 phosphorylation under nitrogen depletion, compared with wild-type cells, especially at 15 min (Fig 5).
PMID:26689777	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPAC13G6.07c	By contrast, Δlam2 cells, Δgtr1 cells and Δgtr2 cells showed increased Rps6 phosphorylation under nitrogen depletion, compared with wild-type cells, especially at 15 min (Fig 5).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Exogenous addition of arginine to the EMM plates enhanced the cell growth of Δlam2 cells, Δgtr2 cells, Δgtr1 cells, Δnpr3 cells and Δnpr2 cells as well as wild-type cells, but did not rescue the defective cell growth of these mutant cells to the level of wild-type cells (S5 Fig).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Exogenous addition of arginine to the EMM plates enhanced the cell growth of Δlam2 cells, Δgtr2 cells, Δgtr1 cells, Δnpr3 cells and Δnpr2 cells as well as wild-type cells, but did not rescue the defective cell growth of these mutant cells to the level of wild-type cells (S5 Fig).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Exogenous addition of arginine to the EMM plates enhanced the cell growth of Δlam2 cells, Δgtr2 cells, Δgtr1 cells, Δnpr3 cells and Δnpr2 cells as well as wild-type cells, but did not rescue the defective cell growth of these mutant cells to the level of wild-type cells (S5 Fig).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Exogenous addition of arginine to the EMM plates enhanced the cell growth of Δlam2 cells, Δgtr2 cells, Δgtr1 cells, Δnpr3 cells and Δnpr2 cells as well as wild-type cells, but did not rescue the defective cell growth of these mutant cells to the level of wild-type cells (S5 Fig).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Exogenous addition of arginine to the EMM plates enhanced the cell growth of Δlam2 cells, Δgtr2 cells, Δgtr1 cells, Δnpr3 cells and Δnpr2 cells as well as wild-type cells, but did not rescue the defective cell growth of these mutant cells to the level of wild-type cells (S5 Fig).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Exogenous addition of arginine to the EMM plates enhanced the cell growth of Δlam2 cells, Δgtr2 cells, Δgtr1 cells, Δnpr3 cells and Δnpr2 cells as well as wild-type cells, but did not rescue the defective cell growth of these mutant cells to the level of wild-type cells (S5 Fig).
PMID:26689777	GO:0000329	fungal-type vacuole membrane	First, we observed the localization of Gtr1-GFP expressed under nmt1 pro- moter. In wild-type cells, hypotonic stress induced a fusion of vacuoles, and Gtr1-GFP and Gtr2-GFP were localized at vacuolar membranes. (Figure. 8A-B)
PMID:26689777	GO:0000329	fungal-type vacuole membrane	First, we observed the localization of Gtr1-GFP expressed under nmt1 pro- moter. In wild-type cells, hypotonic stress induced a fusion of vacuoles, and Gtr1-GFP and Gtr2-GFP were localized at vacuolar membranes. (Figure. 8A-B)
PMID:26689777	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC337.13c	In immunoblotting, the protein levels of Gtr1-GFP and Gtr2-GFP, but not of GFP control vector, were reduced in Δlam2 cells, Δnpr3 cells and Δnpr2 cells, compared with wild-type cells (Fig 8C)
PMID:26689777	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC337.13c	In immunoblotting, the protein levels of Gtr1-GFP and Gtr2-GFP, but not of GFP control vector, were reduced in Δlam2 cells, Δnpr3 cells and Δnpr2 cells, compared with wild-type cells (Fig 8C)
PMID:26689777	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC337.13c	In immunoblotting, the protein levels of Gtr1-GFP and Gtr2-GFP, but not of GFP control vector, were reduced in Δlam2 cells, Δnpr3 cells and Δnpr2 cells, compared with wild-type cells (Fig 8C)
PMID:26689777	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC777.05	In immunoblotting, the protein levels of Gtr1-GFP and Gtr2-GFP, but not of GFP control vector, were reduced in Δlam2 cells, Δnpr3 cells and Δnpr2 cells, compared with wild-type cells (Fig 8C)
PMID:26689777	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC777.05	In immunoblotting, the protein levels of Gtr1-GFP and Gtr2-GFP, but not of GFP control vector, were reduced in Δlam2 cells, Δnpr3 cells and Δnpr2 cells, compared with wild-type cells (Fig 8C)
PMID:26689777	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC777.05	In immunoblotting, the protein levels of Gtr1-GFP and Gtr2-GFP, but not of GFP control vector, were reduced in Δlam2 cells, Δnpr3 cells and Δnpr2 cells, compared with wild-type cells (Fig 8C)
PMID:26689777	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC777.05	In immunoblotting, the protein levels of Gtr1-GFP and Gtr2-GFP, but not of GFP control vector, were reduced in Δlam2 cells, Δnpr3 cells and Δnpr2 cells, compared with wild-type cells (Fig 8C)
PMID:26689777	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC337.13c	In immunoblotting, the protein levels of Gtr1-GFP and Gtr2-GFP, but not of GFP control vector, were reduced in Δlam2 cells, Δnpr3 cells and Δnpr2 cells, compared with wild-type cells (Fig 8C)
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	In Δlam2 cells, Δgtr1 cells and Δgtr2 cells, the mRNA level of cat1+ was increased compared with wild-type cells (Fig 3A).
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	In Δlam2 cells, Δgtr1 cells and Δgtr2 cells, the mRNA level of cat1+ was increased compared with wild-type cells (Fig 3A).
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	In Δlam2 cells, Δgtr1 cells and Δgtr2 cells, the mRNA level of cat1+ was increased compared with wild-type cells (Fig 3A).
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09	In Δlam2 cells, Δgtr2 cells and Δgtr1 cells, the mRNA level of isp5+ was decreased, compared with wild- type cells (Fig 4A).
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09	In Δlam2 cells, Δgtr2 cells and Δgtr1 cells, the mRNA level of isp5+ was decreased, compared with wild- type cells (Fig 4A).
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09	In Δlam2 cells, Δgtr2 cells and Δgtr1 cells, the mRNA level of isp5+ was decreased, compared with wild- type cells (Fig 4A).
PMID:26689777	FYPO:0004457	decreased protein localization to nucleus during nitrogen starvation [assayed_protein] PomBase:SPCC1902.01	In Δlam2 cells, Δgtr2 cells and Δgtr1 cells, the nuclear localization of Gaf1-YFP was not observed within 30 min after nitrogen depletion. Although a subset of these mutant cells showed the nuclear locali- zation of Gaf1-YFP at 60 and 120 min, its nuclear localization appeared to be partial, compared with wild-type cells (Fig 4C).
PMID:26689777	FYPO:0004457	decreased protein localization to nucleus during nitrogen starvation [assayed_protein] PomBase:SPCC1902.01	In Δlam2 cells, Δgtr2 cells and Δgtr1 cells, the nuclear localization of Gaf1-YFP was not observed within 30 min after nitrogen depletion. Although a subset of these mutant cells showed the nuclear locali- zation of Gaf1-YFP at 60 and 120 min, its nuclear localization appeared to be partial, compared with wild-type cells (Fig 4C).
PMID:26689777	FYPO:0004457	decreased protein localization to nucleus during nitrogen starvation [assayed_protein] PomBase:SPCC1902.01	In Δlam2 cells, Δgtr2 cells and Δgtr1 cells, the nuclear localization of Gaf1-YFP was not observed within 30 min after nitrogen depletion. Although a subset of these mutant cells showed the nuclear locali- zation of Gaf1-YFP at 60 and 120 min, its nuclear localization appeared to be partial, compared with wild-type cells (Fig 4C).
PMID:26689777	FYPO:0006233	decreased protein localization to vacuolar membrane [assayed_protein] PomBase:SPCC777.05	In Δlam2 cells, Δnpr2 cells and Δnpr3 cells, vacuoles were smaller, and the intensities of Gtr1-GFP and Gtr2-GFP at vacuolar membranes were decreased, compared with wild-type cells (Fig 8A and 8B).
PMID:26689777	FYPO:0006233	decreased protein localization to vacuolar membrane [assayed_protein] PomBase:SPBC337.13c	In Δlam2 cells, Δnpr2 cells and Δnpr3 cells, vacuoles were smaller, and the intensities of Gtr1-GFP and Gtr2-GFP at vacuolar membranes were decreased, compared with wild-type cells (Fig 8A and 8B).
PMID:26689777	FYPO:0006233	decreased protein localization to vacuolar membrane [assayed_protein] PomBase:SPBC337.13c	In Δlam2 cells, Δnpr2 cells and Δnpr3 cells, vacuoles were smaller, and the intensities of Gtr1-GFP and Gtr2-GFP at vacuolar membranes were decreased, compared with wild-type cells (Fig 8A and 8B).
PMID:26689777	FYPO:0006233	decreased protein localization to vacuolar membrane [assayed_protein] PomBase:SPBC337.13c	In Δlam2 cells, Δnpr2 cells and Δnpr3 cells, vacuoles were smaller, and the intensities of Gtr1-GFP and Gtr2-GFP at vacuolar membranes were decreased, compared with wild-type cells (Fig 8A and 8B).
PMID:26689777	FYPO:0006233	decreased protein localization to vacuolar membrane [assayed_protein] PomBase:SPCC777.05	In Δlam2 cells, Δnpr2 cells and Δnpr3 cells, vacuoles were smaller, and the intensities of Gtr1-GFP and Gtr2-GFP at vacuolar membranes were decreased, compared with wild-type cells (Fig 8A and 8B).
PMID:26689777	FYPO:0006233	decreased protein localization to vacuolar membrane [assayed_protein] PomBase:SPCC777.05	In Δlam2 cells, Δnpr2 cells and Δnpr3 cells, vacuoles were smaller, and the intensities of Gtr1-GFP and Gtr2-GFP at vacuolar membranes were decreased, compared with wild-type cells (Fig 8A and 8B).
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	In Δnpr2 cells and Δnpr3 cells, the increase in cat1+ expression was abol- ished by simultaneous tor2-287 mutation (S4A Fig).
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	In Δnpr2 cells and Δnpr3 cells, the increase in cat1+ expression was abol- ished by simultaneous tor2-287 mutation (S4A Fig).
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	In Δnpr2 cells and Δnpr3 cells, the increase in cat1+ expression was abol- ished by simultaneous tor2-287 mutation (S4A Fig).
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	In Δnpr2 cells and Δnpr3 cells, the increase in cat1+ expression was abol- ished by simultaneous tor2-287 mutation (S4A Fig).
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	In Δnpr2 cells and Δnpr3 cells, the increase in cat1+ expression was abol- ished by simultaneous tor2-287 mutation (S4A Fig).
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	In Δnpr2 cells and Δnpr3 cells, the increase in cat1+ expression was abol- ished by simultaneous tor2-287 mutation (S4A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] medium	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] medium	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] medium	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] medium	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] medium	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	No apparent synthetic effects of these double mutant cells were observed in either canavanine resistance or the rescue of growth defect by TOR inhibitors (Fig 6A and 6B).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Similarly to Δlam2 cells, the growth of npr3::ura4+ cells and npr2::ura4+ cells was partially inhibited on EMM plate, and was completely inhibited on both YES and YPD plates (S2A Fig).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Similarly to Δlam2 cells, the growth of npr3::ura4+ cells and npr2::ura4+ cells was partially inhibited on EMM plate, and was completely inhibited on both YES and YPD plates (S2A Fig).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Similarly to Δlam2 cells, the growth of npr3::ura4+ cells and npr2::ura4+ cells was partially inhibited on EMM plate, and was completely inhibited on both YES and YPD plates (S2A Fig).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Similarly to Δlam2 cells, the growth of npr3::ura4+ cells and npr2::ura4+ cells was partially inhibited on EMM plate, and was completely inhibited on both YES and YPD plates (S2A Fig).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Similarly to Δlam2 cells, the growth of npr3::ura4+ cells and npr2::ura4+ cells was partially inhibited on EMM plate, and was completely inhibited on both YES and YPD plates (S2A Fig).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Similarly to Δlam2 cells, the growth of npr3::ura4+ cells and npr2::ura4+ cells was partially inhibited on EMM plate, and was completely inhibited on both YES and YPD plates (S2A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Similarly, the tor2-287 mutation res- cued the growth defect of these cells (S3B Fig).
PMID:26689777	FYPO:0008372	normal protein localization to cell surface during vegetative growth	TORC1 inhibition by rapamycin and caf- feine abolished the internalization of Cat1 and increases the signal at the cell surface (S4B Fig, Rapamycin + caffeine).
PMID:26689777	FYPO:0008372	normal protein localization to cell surface during vegetative growth	TORC1 inhibition by rapamycin and caf- feine abolished the internalization of Cat1 and increases the signal at the cell surface (S4B Fig, Rapamycin + caffeine).
PMID:26689777	FYPO:0008372	normal protein localization to cell surface during vegetative growth	TORC1 inhibition by rapamycin and caf- feine abolished the internalization of Cat1 and increases the signal at the cell surface (S4B Fig, Rapamycin + caffeine).
PMID:26689777	FYPO:0001545	normal growth on L-canavanine	The canava- nine resistance of Δlam2 cells, Δgtr1 cells and Δgtr2 cells was completely canceled by Torin1 treatment (Fig 3E, canavanine + Torin).
PMID:26689777	FYPO:0001545	normal growth on L-canavanine	The canava- nine resistance of Δlam2 cells, Δgtr1 cells and Δgtr2 cells was completely canceled by Torin1 treatment (Fig 3E, canavanine + Torin).
PMID:26689777	FYPO:0001545	normal growth on L-canavanine	The canava- nine resistance of Δlam2 cells, Δgtr1 cells and Δgtr2 cells was completely canceled by Torin1 treatment (Fig 3E, canavanine + Torin).
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] low	The canavanine resistance of Δlam2 cells, Δgtr1 cells and Δgtr2 cells was partially canceled by rapamycin treatment (Fig 3E, canavanine + Rapamy- cin).
PMID:26689777	FYPO:0001545	normal growth on L-canavanine	The canavanine resistance of Δlam2 cells, Δgtr1 cells and Δgtr2 cells was partially canceled by rapamycin treatment (Fig 3E, canavanine + Rapamy- cin).
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] low	The canavanine resistance of Δlam2 cells, Δgtr1 cells and Δgtr2 cells was partially canceled by rapamycin treatment (Fig 3E, canavanine + Rapamy- cin).
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] medium	The descrease in isp5+ mRNA was abolished in tor2-287Δnpr2 and tor2-287Δnpr3 cells (S6A Fig)
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] low	The descrease in isp5+ mRNA was abolished in tor2-287Δnpr2 and tor2-287Δnpr3 cells (S6A Fig)
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] medium	The descrease in isp5+ mRNA was abolished in tor2-287Δnpr2 and tor2-287Δnpr3 cells (S6A Fig)
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] low	The descrease in isp5+ mRNA was abolished in tor2-287Δnpr2 and tor2-287Δnpr3 cells (S6A Fig)
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	The growth defects of Δgtr2Δgtr1 cells, Δgtr2Δlam2 cells, Δgtr2Δnpr2 cells, Δnpr2Δnpr3 cells and Δnpr2Δlam2 cells on EMM plates were similar to those of the respective single mutant cells (Fig 6A and 6B).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	The growth defects of Δgtr2Δgtr1 cells, Δgtr2Δlam2 cells, Δgtr2Δnpr2 cells, Δnpr2Δnpr3 cells and Δnpr2Δlam2 cells on EMM plates were similar to those of the respective single mutant cells (Fig 6A and 6B).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	The growth defects of Δgtr2Δgtr1 cells, Δgtr2Δlam2 cells, Δgtr2Δnpr2 cells, Δnpr2Δnpr3 cells and Δnpr2Δlam2 cells on EMM plates were similar to those of the respective single mutant cells (Fig 6A and 6B).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	The growth defects of Δgtr2Δgtr1 cells, Δgtr2Δlam2 cells, Δgtr2Δnpr2 cells, Δnpr2Δnpr3 cells and Δnpr2Δlam2 cells on EMM plates were similar to those of the respective single mutant cells (Fig 6A and 6B).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	The growth defects of Δgtr2Δgtr1 cells, Δgtr2Δlam2 cells, Δgtr2Δnpr2 cells, Δnpr2Δnpr3 cells and Δnpr2Δlam2 cells on EMM plates were similar to those of the respective single mutant cells (Fig 6A and 6B).
PMID:26689777	FYPO:0006148	abolished transcription during nitrogen starvation [assayed_transcript] PomBase:SPAC1039.09	The mRNA level of isp5+ (S6A Fig) as well as the basal isp5+ transcriptional activity and its activation induced by nitrogen depletion as measured by Renilla luciferase reporter (S6B Fig) were also decreased in npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells.
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09	The mRNA level of isp5+ (S6A Fig) as well as the basal isp5+ transcriptional activity and its activation induced by nitrogen depletion as measured by Renilla luciferase reporter (S6B Fig) were also decreased in npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells.
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09	The mRNA level of isp5+ (S6A Fig) as well as the basal isp5+ transcriptional activity and its activation induced by nitrogen depletion as measured by Renilla luciferase reporter (S6B Fig) were also decreased in npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells.
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09	The mRNA level of isp5+ (S6A Fig) as well as the basal isp5+ transcriptional activity and its activation induced by nitrogen depletion as measured by Renilla luciferase reporter (S6B Fig) were also decreased in npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells.
PMID:26689777	FYPO:0006148	abolished transcription during nitrogen starvation [assayed_transcript] PomBase:SPAC1039.09	The mRNA level of isp5+ (S6A Fig) as well as the basal isp5+ transcriptional activity and its activation induced by nitrogen depletion as measured by Renilla luciferase reporter (S6B Fig) were also decreased in npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells.
PMID:26689777	FYPO:0006148	abolished transcription during nitrogen starvation [assayed_transcript] PomBase:SPAC1039.09	The mRNA level of isp5+ (S6A Fig) as well as the basal isp5+ transcriptional activity and its activation induced by nitrogen depletion as measured by Renilla luciferase reporter (S6B Fig) were also decreased in npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells.
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	The resultant Δlam2 cells grew slowly on EMM plates, and failed to grow on both YES and YPD plates (Fig 1A).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	The resultant Δlam2 cells grew slowly on EMM plates, and failed to grow on both YES and YPD plates (Fig 1A).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	The resultant Δlam2 cells grew slowly on EMM plates, and failed to grow on both YES and YPD plates (Fig 1A).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	The tor2-287 mutation rescued the growth defect of these cells (Fig 2B).
PMID:26689777	GO:1904262	negative regulation of TORC1 signaling	These findings suggest that Lam2, Gtr1-Gtr2 and Npr2-Npr3 all mediate the above phenotypes through suppressing TORC1 activity.
PMID:26689777	GO:1904262	negative regulation of TORC1 signaling	These findings suggest that Lam2, Gtr1-Gtr2 and Npr2-Npr3 all mediate the above phenotypes through suppressing TORC1 activity.
PMID:26689777	GO:1904262	negative regulation of TORC1 signaling	These findings suggest that Lam2, Gtr1-Gtr2 and Npr2-Npr3 all mediate the above phenotypes through suppressing TORC1 activity.
PMID:26689777	GO:1904262	negative regulation of TORC1 signaling	These findings suggest that Lam2, Gtr1-Gtr2 and Npr2-Npr3 all mediate the above phenotypes through suppressing TORC1 activity.
PMID:26689777	GO:1904262	negative regulation of TORC1 signaling	These findings suggest that Lam2, Gtr1-Gtr2 and Npr2-Npr3 all mediate the above phenotypes through suppressing TORC1 activity.
PMID:26689777	FYPO:0008372	normal protein localization to cell surface during vegetative growth	These intracellular punctate structures were abolished upon TORC1 inhibition by the com- bined treatment of rapamycin and caffeine (Fig 3B, Rapamycin + caffeine)
PMID:26689777	FYPO:0008372	normal protein localization to cell surface during vegetative growth	These intracellular punctate structures were abolished upon TORC1 inhibition by the com- bined treatment of rapamycin and caffeine (Fig 3B, Rapamycin + caffeine)
PMID:26689777	FYPO:0008372	normal protein localization to cell surface during vegetative growth	These intracellular punctate structures were abolished upon TORC1 inhibition by the com- bined treatment of rapamycin and caffeine (Fig 3B, Rapamycin + caffeine)
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] low	This descrease in isp5+ expression was abolished in tor2-287Δlam2, tor2- 287Δgtr2 and tor2-287Δgtr1 cells (Fig 4A)
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] high	This descrease in isp5+ expression was abolished in tor2-287Δlam2, tor2- 287Δgtr2 and tor2-287Δgtr1 cells (Fig 4A)
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] high	This descrease in isp5+ expression was abolished in tor2-287Δlam2, tor2- 287Δgtr2 and tor2-287Δgtr1 cells (Fig 4A)
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] high	This descrease in isp5+ expression was abolished in tor2-287Δlam2, tor2- 287Δgtr2 and tor2-287Δgtr1 cells (Fig 4A)
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] high	This descrease in isp5+ expression was abolished in tor2-287Δlam2, tor2- 287Δgtr2 and tor2-287Δgtr1 cells (Fig 4A)
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	This increase in cat1+ expression was abolished in tor2-287Δlam2 cells, tor2-287Δgtr1 cells and tor2-287Δgtr2 cells (Fig 3A)
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	This increase in cat1+ expression was abolished in tor2-287Δlam2 cells, tor2-287Δgtr1 cells and tor2-287Δgtr2 cells (Fig 3A)
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	This increase in cat1+ expression was abolished in tor2-287Δlam2 cells, tor2-287Δgtr1 cells and tor2-287Δgtr2 cells (Fig 3A)
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	This increase in cat1+ expression was abolished in tor2-287Δlam2 cells, tor2-287Δgtr1 cells and tor2-287Δgtr2 cells (Fig 3A)
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	This increase in cat1+ expression was abolished in tor2-287Δlam2 cells, tor2-287Δgtr1 cells and tor2-287Δgtr2 cells (Fig 3A)
PMID:26689777	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	This increase in cat1+ expression was abolished in tor2-287Δlam2 cells, tor2-287Δgtr1 cells and tor2-287Δgtr2 cells (Fig 3A)
PMID:26689777	FYPO:0004457	decreased protein localization to nucleus during nitrogen starvation [assayed_protein] PomBase:SPCC1902.01	Thus, Δgtr2Δgtr1 cells, Δgtr2Δlam2 cells and Δgtr2Δnpr2 cells showed the lack of nuclear localization of Gaf1-YFP at 30 min after nitrogen depletion (Fig 6C), similarly to the respective single knockout cells
PMID:26689777	FYPO:0004457	decreased protein localization to nucleus during nitrogen starvation [assayed_protein] PomBase:SPCC1902.01	Thus, Δgtr2Δgtr1 cells, Δgtr2Δlam2 cells and Δgtr2Δnpr2 cells showed the lack of nuclear localization of Gaf1-YFP at 30 min after nitrogen depletion (Fig 6C), similarly to the respective single knockout cells
PMID:26689777	FYPO:0004457	decreased protein localization to nucleus during nitrogen starvation [assayed_protein] PomBase:SPCC1902.01	Thus, Δgtr2Δgtr1 cells, Δgtr2Δlam2 cells and Δgtr2Δnpr2 cells showed the lack of nuclear localization of Gaf1-YFP at 30 min after nitrogen depletion (Fig 6C), similarly to the respective single knockout cells
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001357	normal vegetative cell population growth	Treatment with both rapamycin and Torin1 rescued the growth defects of npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells (S3A Fig).
PMID:26689777	FYPO:0001545	normal growth on L-canavanine	Treatment with rapamycin and caffeine partially canceled, and Torin1 treatment fully canceled, cannavanine resistance in Δnpr2 cells and Δnpr3 cells (S4D Fig).
PMID:26689777	FYPO:0001545	normal growth on L-canavanine	Treatment with rapamycin and caffeine partially canceled, and Torin1 treatment fully canceled, cannavanine resistance in Δnpr2 cells and Δnpr3 cells (S4D Fig).
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] low	Treatment with rapamycin and caffeine partially canceled, and Torin1 treatment fully canceled, cannavanine resistance in Δnpr2 cells and Δnpr3 cells (S4D Fig).
PMID:26689777	FYPO:0001545	normal growth on L-canavanine	Treatment with rapamycin and caffeine partially canceled, and Torin1 treatment fully canceled, cannavanine resistance in Δnpr2 cells and Δnpr3 cells (S4D Fig).
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] low	Treatment with rapamycin and caffeine partially canceled, and Torin1 treatment fully canceled, cannavanine resistance in Δnpr2 cells and Δnpr3 cells (S4D Fig).
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] low	Treatment with rapamycin and caffeine partially canceled, and Torin1 treatment fully canceled, cannavanine resistance in Δnpr2 cells and Δnpr3 cells (S4D Fig).
PMID:26689777	FYPO:0004457	decreased protein localization to nucleus during nitrogen starvation [assayed_protein] PomBase:SPCC1902.01	Using npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells, we found that the loss of Npr2 or Npr3 also impairs the nuclear localization of Gaf1-YFP induced by nitrogen depletion (S6C Fig)
PMID:26689777	FYPO:0004457	decreased protein localization to nucleus during nitrogen starvation [assayed_protein] PomBase:SPCC1902.01	Using npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells, we found that the loss of Npr2 or Npr3 also impairs the nuclear localization of Gaf1-YFP induced by nitrogen depletion (S6C Fig)
PMID:26689777	FYPO:0004457	decreased protein localization to nucleus during nitrogen starvation [assayed_protein] PomBase:SPCC1902.01	Using npr3::ura4+ cells, npr2::ura4+ cells and npr2::KanMX4 cells, we found that the loss of Npr2 or Npr3 also impairs the nuclear localization of Gaf1-YFP induced by nitrogen depletion (S6C Fig)
PMID:26689777	FYPO:0010009	decreased protein localization to cell surface, with protein mislocalized to cytoplasm	Using npr3::ura4+ cells, npr2::ura4+ cells, and npr2::KanMX4 cells, we found that the loss of Npr2 or Npr3 also increases mRNA expression of Cat1 (S4A Fig), induces its internalization (S4B Fig, EMM), and causes canavanine resistance (S4C Fig), similarly to the loss of Lam2 as well as Gtr1 and Gtr2.
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] medium	Using npr3::ura4+ cells, npr2::ura4+ cells, and npr2::KanMX4 cells, we found that the loss of Npr2 or Npr3 also increases mRNA expression of Cat1 (S4A Fig), induces its internalization (S4B Fig, EMM), and causes canavanine resistance (S4C Fig), similarly to the loss of Lam2 as well as Gtr1 and Gtr2.
PMID:26689777	FYPO:0010009	decreased protein localization to cell surface, with protein mislocalized to cytoplasm	Using npr3::ura4+ cells, npr2::ura4+ cells, and npr2::KanMX4 cells, we found that the loss of Npr2 or Npr3 also increases mRNA expression of Cat1 (S4A Fig), induces its internalization (S4B Fig, EMM), and causes canavanine resistance (S4C Fig), similarly to the loss of Lam2 as well as Gtr1 and Gtr2.
PMID:26689777	FYPO:0010009	decreased protein localization to cell surface, with protein mislocalized to cytoplasm	Using npr3::ura4+ cells, npr2::ura4+ cells, and npr2::KanMX4 cells, we found that the loss of Npr2 or Npr3 also increases mRNA expression of Cat1 (S4A Fig), induces its internalization (S4B Fig, EMM), and causes canavanine resistance (S4C Fig), similarly to the loss of Lam2 as well as Gtr1 and Gtr2.
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	Using npr3::ura4+ cells, npr2::ura4+ cells, and npr2::KanMX4 cells, we found that the loss of Npr2 or Npr3 also increases mRNA expression of Cat1 (S4A Fig), induces its internalization (S4B Fig, EMM), and causes canavanine resistance (S4C Fig), similarly to the loss of Lam2 as well as Gtr1 and Gtr2.
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] medium	Using npr3::ura4+ cells, npr2::ura4+ cells, and npr2::KanMX4 cells, we found that the loss of Npr2 or Npr3 also increases mRNA expression of Cat1 (S4A Fig), induces its internalization (S4B Fig, EMM), and causes canavanine resistance (S4C Fig), similarly to the loss of Lam2 as well as Gtr1 and Gtr2.
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] medium	Using npr3::ura4+ cells, npr2::ura4+ cells, and npr2::KanMX4 cells, we found that the loss of Npr2 or Npr3 also increases mRNA expression of Cat1 (S4A Fig), induces its internalization (S4B Fig, EMM), and causes canavanine resistance (S4C Fig), similarly to the loss of Lam2 as well as Gtr1 and Gtr2.
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	Using npr3::ura4+ cells, npr2::ura4+ cells, and npr2::KanMX4 cells, we found that the loss of Npr2 or Npr3 also increases mRNA expression of Cat1 (S4A Fig), induces its internalization (S4B Fig, EMM), and causes canavanine resistance (S4C Fig), similarly to the loss of Lam2 as well as Gtr1 and Gtr2.
PMID:26689777	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC869.11	Using npr3::ura4+ cells, npr2::ura4+ cells, and npr2::KanMX4 cells, we found that the loss of Npr2 or Npr3 also increases mRNA expression of Cat1 (S4A Fig), induces its internalization (S4B Fig, EMM), and causes canavanine resistance (S4C Fig), similarly to the loss of Lam2 as well as Gtr1 and Gtr2.
PMID:26689777	FYPO:0010009	decreased protein localization to cell surface, with protein mislocalized to cytoplasm	Whereas Cat1-GFP was present at the cell surface in wild-type cells, it was localized to intracellular punctate structures in Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 3B, EMM).
PMID:26689777	FYPO:0010009	decreased protein localization to cell surface, with protein mislocalized to cytoplasm	Whereas Cat1-GFP was present at the cell surface in wild-type cells, it was localized to intracellular punctate structures in Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 3B, EMM).
PMID:26689777	FYPO:0010009	decreased protein localization to cell surface, with protein mislocalized to cytoplasm	Whereas Cat1-GFP was present at the cell surface in wild-type cells, it was localized to intracellular punctate structures in Δlam2 cells, Δgtr1 cells and Δgtr2 cells (Fig 3B, EMM).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	we generated new strains of Δgtr1 cells and Δgtr2 cells, and found that these mutant cells grew slowly on EMM plates, and failed to grow on both YES and YPD plates, similarly to Δlam2 cells (Fig 1A).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	we generated new strains of Δgtr1 cells and Δgtr2 cells, and found that these mutant cells grew slowly on EMM plates, and failed to grow on both YES and YPD plates, similarly to Δlam2 cells (Fig 1A).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	we generated new strains of Δgtr1 cells and Δgtr2 cells, and found that these mutant cells grew slowly on EMM plates, and failed to grow on both YES and YPD plates, similarly to Δlam2 cells (Fig 1A).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	we generated new strains of Δgtr1 cells and Δgtr2 cells, and found that these mutant cells grew slowly on EMM plates, and failed to grow on both YES and YPD plates, similarly to Δlam2 cells (Fig 1A).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	we generated new strains of Δgtr1 cells and Δgtr2 cells, and found that these mutant cells grew slowly on EMM plates, and failed to grow on both YES and YPD plates, similarly to Δlam2 cells (Fig 1A).
PMID:26689777	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	we generated new strains of Δgtr1 cells and Δgtr2 cells, and found that these mutant cells grew slowly on EMM plates, and failed to grow on both YES and YPD plates, similarly to Δlam2 cells (Fig 1A).
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] medium	Δlam2 cells, tetO7-lam2 cells, Δgtr2 cells, tetO7-gtr2 cells and Δgtr1 cells showed canavanine resistance (Fig 3D).
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] medium	Δlam2 cells, tetO7-lam2 cells, Δgtr2 cells, tetO7-gtr2 cells and Δgtr1 cells showed canavanine resistance (Fig 3D).
PMID:26689777	FYPO:0001029	resistance to canavanine [has_severity] low	Δlam2 cells, tetO7-lam2 cells, Δgtr2 cells, tetO7-gtr2 cells and Δgtr1 cells showed canavanine resistance (Fig 3D).
PMID:26689777	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPAC13G6.07c	Δnpr2 cells and Δnpr3 cells also showed increased Rps6 phosphorylation (S7 Fig), similarly to the loss of Lam2, Gtr1 or Gtr2.
PMID:26689777	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPAPB1E7.12	Δnpr2 cells and Δnpr3 cells also showed increased Rps6 phosphorylation (S7 Fig), similarly to the loss of Lam2, Gtr1 or Gtr2.
PMID:26689777	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPAC13G6.07c	Δnpr2 cells and Δnpr3 cells also showed increased Rps6 phosphorylation (S7 Fig), similarly to the loss of Lam2, Gtr1 or Gtr2.
PMID:26689777	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPAPB1E7.12	Δnpr2 cells and Δnpr3 cells also showed increased Rps6 phosphorylation (S7 Fig), similarly to the loss of Lam2, Gtr1 or Gtr2.
PMID:26697368	FYPO:0004490	increased level of transport gene mRNA during vegetative growth	(comment: CHECK link to GEO dataset- GSE71820)
PMID:26697368	FYPO:0005301	increased level of cell cycle regulated gene mRNA during vegetative growth	(comment: CHECK link to GEO dataset- GSE71820)
PMID:26730850	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 3)
PMID:26730850	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 3)
PMID:26730850	FYPO:0003602	abolished mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 3)
PMID:26730850	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 3)
PMID:26730850	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 3)
PMID:26730850	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 3)
PMID:26730850	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 3)
PMID:26730850	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 3)
PMID:26730850	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 3)
PMID:26730850	FYPO:0003602	abolished mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 3)
PMID:26730850	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 3)
PMID:26730850	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC22G7.08	(Fig. 4)
PMID:26730850	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC22G7.08	(Fig. 4)
PMID:26730850	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC22G7.08	(Fig. 4)
PMID:26730850	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC22G7.08	(Fig. 4)
PMID:26730850	FYPO:0003602	abolished mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC22G7.08	(Fig. 4)
PMID:26730850	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC22G7.08	(Fig. 4)
PMID:26730850	FYPO:0003602	abolished mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC22G7.08	(Fig. 4)
PMID:26730850	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC22G7.08	(Fig. 4)
PMID:26730850	FYPO:0003602	abolished mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 5)
PMID:26730850	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 5)
PMID:26730850	FYPO:0003602	abolished mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 5)
PMID:26730850	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 5)
PMID:26730850	FYPO:0003602	abolished mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 5)
PMID:26730850	FYPO:0003602	abolished mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 5)
PMID:26730850	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 5)
PMID:26730850	FYPO:0003602	abolished mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Fig. 5)
PMID:26730850	FYPO:0000561	normal mitotic G1 phase progression	(Fig. S1)
PMID:26730850	FYPO:0000012	mitotic G2/M phase transition delay	(Figure 1A-C) (comment: transient growth arrest)
PMID:26730850	FYPO:0000333	mitotic G1/S phase transition delay	(Figure 1C) (comment: transient)
PMID:26730850	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC776.01	(Figure 1D)
PMID:26730850	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC22F3.09c	(Figure 1D)
PMID:26730850	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC29E6.08	(Figure 1D) (comment: efficiency/ of introns displaying weak splice sites)
PMID:26730850	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Figure 1D) (comment: efficiency/ of introns displaying weak splice sites)
PMID:26730850	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [has_penetrance] 30	(Figure 1D, 2D) (comment: - examined via RT-PCR) (Figure 2A) (comment: examined via RNA-Seq)
PMID:26730850	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC725.16	(Figure 3, 5) (comment: efficiency/ of introns displaying weak splice sites)
PMID:26730850	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC22G7.08	(Figure 4) (comment: efficiency of introns displaying weak splice sites)
PMID:26730850	GO:1905746	positive regulation of mRNA cis splicing, via spliceosome	(comment: regulation of efficiency at weak donor)
PMID:26744419	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. 1b)
PMID:26744419	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1b)
PMID:26744419	FYPO:0004342	increased LTR-derived RNA level	(Fig. 1c)
PMID:26744419	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 1c)
PMID:26744419	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. 1c)
PMID:26744419	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c [has_severity] medium	(Fig. 1c)
PMID:26744419	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c [has_severity] low	(Fig. 1c)
PMID:26744419	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. 1c)
PMID:26744419	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. 1c)
PMID:26744419	GO:0140464	subnuclear spatial organization of silent mating-type cassette heterochromatin [occurs_at] mating_type_region	(Fig. 1c) (comment: CHECK SHOULD BRE ORGANIZATION)
PMID:26744419	GO:0140698	attachment of telomeric heterochromatin to nuclear envelope	(Fig. 1c, Fig 4e)
PMID:26744419	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPCC1620.07c	(Fig. 1d)
PMID:26744419	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPCC1620.07c	(Fig. 1d)
PMID:26744419	FYPO:0002360	normal chromatin silencing at centromere	(Fig. 1d)
PMID:26744419	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 1d)
PMID:26744419	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c	(Fig. 3)
PMID:26744419	FYPO:0005602	normal subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c	(Fig. 3)
PMID:26744419	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	(Fig. 3)
PMID:26744419	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c	(Fig. 3)
PMID:26744419	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Fig. 3)
PMID:26744419	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c	(Fig. 3)
PMID:26744419	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. 3)
PMID:26744419	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c [has_severity] medium	(Fig. 3b)
PMID:26744419	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c [has_severity] low	(Fig. 3b)
PMID:26744419	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c [has_severity] medium	(Fig. 3b)
PMID:26744419	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c [has_severity] high	(Fig. 3b)
PMID:26744419	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 3c)
PMID:26744419	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] low	(Fig. 3c)
PMID:26744419	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 3c)
PMID:26744419	FYPO:0006429	normal histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth	(Fig. 3d)
PMID:26744419	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase [has_penetrance] 8	(Fig. 4)
PMID:26744419	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase [has_penetrance] 32	(Fig. 4)
PMID:26744419	GO:0072766	centromere clustering at the mitotic interphase nuclear envelope	(Fig. 4b, c)
PMID:26744419	FYPO:0002339	decreased protein localization to nuclear periphery [assayed_using] PomBase:SPAC16A10.07c [has_severity] low	(Fig. 4e)
PMID:26744419	FYPO:0002339	decreased protein localization to nuclear periphery [assayed_using] PomBase:SPAC16A10.07c [has_severity] low	(Fig. 4e)
PMID:26744419	FYPO:0002339	decreased protein localization to nuclear periphery [assayed_using] PomBase:SPAC16A10.07c [has_severity] medium	(Fig. 4e)
PMID:26744419	GO:0005721	pericentric heterochromatin [coincident_with] regional_centromere_central_core	(Fig. 5)
PMID:26744419	GO:0005635	nuclear envelope	(Fig. 5)
PMID:26744419	FYPO:0004886	abolished protein localization to nuclear envelope during vegetative growth [assayed_using] PomBase:SPAC18G6.10	(Fig. 5b)
PMID:26744419	FYPO:0005612	normal protein localization to nuclear envelope [assayed_using] PomBase:SPAC18G6.10	(Fig. 5b)
PMID:26744419	FYPO:0005612	normal protein localization to nuclear envelope [assayed_using] PomBase:SPAC18G6.10	(Fig. 5b)
PMID:26744419	FYPO:0004886	abolished protein localization to nuclear envelope during vegetative growth [assayed_using] PomBase:SPAC18G6.10	(Fig. 5b)
PMID:26744419	FYPO:0006106	abolished chromatin binding at centromere central core [has_severity] high [assayed_using] PomBase:SPAC18G6.10	(Fig. 5c)
PMID:26744419	FYPO:0004879	normal chromatin binding at centromere central core [has_severity] high	(Fig. 5c)
PMID:26744419	GO:0003682	chromatin binding [occurs_at] regional_centromere_central_core	(Fig. 5c)
PMID:26744419	GO:0140449	centromere-nuclear envelope anchor activity [occurs_at] regional_centromere_central_core [part_of] centromere clustering at the mitotic interphase nuclear envelope	(Fig. 5c) (comment: CHECK parent GO:0003682?)
PMID:26744419	GO:0062239	heterochromatin-nuclear membrane anchor activity [occurs_in] chromosome, subtelomeric region [part_of] attachment of telomeric heterochromatin to nuclear envelope	(Fig. 5c) (comment: CHECK parent GO:0003682?)
PMID:26744419	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase [has_severity] medium	(Fig. 6a) (comment: CHECK in combination with csi1∆; phenocopies lem2∆ csi1∆)
PMID:26744419	FYPO:0004790	abnormal telomere-nuclear envelope distance during vegetative growth [has_severity] medium	(Fig. 6c)
PMID:26744419	FYPO:0004924	normal telomere tethering at nuclear periphery during vegetative growth	(Fig. 6c)
PMID:26744419	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. 6d)
PMID:26744419	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. 6d)
PMID:26744419	FYPO:0002360	normal chromatin silencing at centromere	(Fig. 6d)
PMID:26744419	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. 6d)
PMID:26744419	FYPO:0003555	normal chromatin silencing at subtelomere	(Fig. 6e)
PMID:26744419	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. 6e)
PMID:26744419	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. 6e)
PMID:26744419	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. 6e)
PMID:26744419	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. 7)
PMID:26744419	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. 7)
PMID:26744419	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. 7)
PMID:26744419	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c [has_severity] low	(Fig. 7)
PMID:26744419	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c [has_severity] low	(Fig. 7)
PMID:26744419	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c [has_severity] low	(Fig. 7)
PMID:26744419	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	(Fig. 7)
PMID:26744419	FYPO:0005602	normal subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c	(Fig. 7)
PMID:26744419	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. 7)
PMID:26744419	FYPO:0002577	decreased chromatin binding [assayed_using] PomBase:SPBC2D10.17	(Fig. 7b)
PMID:26744419	FYPO:0003010	increased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_using] PomBase:SPCC622.16c	(Fig. 7b)
PMID:26744419	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_using] PomBase:SPBC2D10.17	(Fig. 7b)
PMID:26744419	FYPO:0003009	increased protein localization to centromere outer repeat [assayed_using] PomBase:SPCC622.16c	(Fig. 7b)
PMID:26744419	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_using] PomBase:SPBC2D10.17	(Fig. 7b)
PMID:26744419	FYPO:0002980	increased chromatin binding [assayed_using] PomBase:SPCC622.16c	(Fig. 7b)
PMID:26744419	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. S10)
PMID:26744419	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. S10)
PMID:26744419	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	(Fig. S10)
PMID:26744419	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. S1c)
PMID:26744419	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. S2)
PMID:26744419	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c	(Fig. S2)
PMID:26744419	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. S2)
PMID:26744419	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. S2)
PMID:26744419	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] medium	(Fig. S2)
PMID:26744419	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	(Fig. S2)
PMID:26744419	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. S2)
PMID:26744419	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. S2)
PMID:26744419	FYPO:0002360	normal chromatin silencing at centromere	(Fig. S4)
PMID:26744419	FYPO:0003086	normal chromatin binding [assayed_using] PomBase:SPAC18G6.02c	(Fig. S5A)
PMID:26746798	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1A)
PMID:26746798	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1A)
PMID:26746798	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1A)
PMID:26746798	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1A)
PMID:26746798	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1A)
PMID:26746798	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1A)
PMID:26746798	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1A)
PMID:26746798	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1A)
PMID:26746798	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1A) Defect in Checkpoint Signaling.
PMID:26746798	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 2A)
PMID:26746798	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 2A)
PMID:26746798	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 2A)
PMID:26746798	FYPO:0002898	abolished protein phosphorylation during cellular response to DNA damage [assayed_using] PomBase:SPCC1259.13	(Fig. 2B)
PMID:26746798	FYPO:0002899	normal protein phosphorylation during cellular response to DNA damage [assayed_using] PomBase:SPCC1259.13	(Fig. 2B)
PMID:26746798	FYPO:0002899	normal protein phosphorylation during cellular response to DNA damage [assayed_using] PomBase:SPCC1259.13	(Fig. 2B)
PMID:26746798	FYPO:0002099	normal protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC1259.13	(Fig. 2C)
PMID:26746798	FYPO:0002096	increased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC1259.13	(Fig. 2C)
PMID:26746798	FYPO:0002099	normal protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC1259.13 [has_severity] high	(Fig. 2C)
PMID:26746798	FYPO:0002096	increased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC1259.13	(Fig. 2C)
PMID:26746798	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC1259.13	(Fig. 2C)
PMID:26746798	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c [has_severity] high	(Fig. 3A)
PMID:26746798	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC694.06c [has_severity] high	(Fig. 3A)
PMID:26746798	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC694.06c	(Fig. 3A)
PMID:26746798	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPAC664.07c	(Fig. 3B)
PMID:26746798	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [has_severity] high [assayed_using] PomBase:SPAC664.07c	(Fig. 3B)
PMID:26746798	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [has_severity] high [assayed_using] PomBase:SPAC664.07c	(Fig. 3B)
PMID:26746798	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(Fig. 3C)
PMID:26746798	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(Fig. 3C)
PMID:26746798	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPCC18B5.11c [has_severity] high	(Fig. 3C)
PMID:26746798	FYPO:0004550	abolished protein phosphorylation during cellular response to hydroxyurea [assayed_using] PomBase:SPCC18B5.11c	(Fig. 3C)
PMID:26746798	FYPO:0000963	normal growth on hydroxyurea	(Fig. 6)
PMID:26746798	FYPO:0000963	normal growth on hydroxyurea	(Fig. 6)
PMID:26746798	FYPO:0000963	normal growth on hydroxyurea	(Fig. 6)
PMID:26746798	FYPO:0000963	normal growth on hydroxyurea	(Fig. 6)
PMID:26746798	FYPO:0000229	cut	(Fig. 7A)
PMID:26746798	FYPO:0003165	cut [has_penetrance] high	(Fig. 7B)
PMID:26746798	FYPO:0003165	cut [has_penetrance] 10	(Fig. 7B)
PMID:26749213	GO:0032153	cell division site	(Fig. 1B)
PMID:26749213	GO:0032153	cell division site	(Fig. 1B)
PMID:26749213	GO:0032153	cell division site	(Fig. 1B)
PMID:26749213	GO:0051285	cell cortex of cell tip	(Fig. 1B)
PMID:26749213	GO:0051285	cell cortex of cell tip	(Fig. 1B)
PMID:26749213	GO:0051285	cell cortex of cell tip	(Fig. 1B)
PMID:26749213	FYPO:0003358	sensitive to miconazole [has_severity] low	(Fig. 1c)
PMID:26749213	FYPO:0001235	decreased extent of cell population growth	(Fig. 2D)
PMID:26749213	FYPO:0002061	inviable vegetative cell population	(Fig. 2d)
PMID:26749213	FYPO:0000745	delayed onset of actin cortical patch internalization [has_penetrance] low	(Fig. 3B-D) (Fig. 4A and movies 3 and 4) slow dynamics of actin patch components: Sla1, wsc1, arc5, Crn1
PMID:26749213	FYPO:0000135	abnormal plasma membrane sterol distribution [has_penetrance] low	(Fig. 6D); evidence: filipin staining
PMID:26749213	FYPO:0000079	sensitive to caspofungin [has_severity] low	(Fig. 7b)
PMID:26749213	FYPO:0004247	normal vacuolar morphology during vegetative growth	(Fig. S2A, B)
PMID:26749213	FYPO:0001945	normal protein secretion [assayed_using] PomBase:SPBP4G3.02	(Fig. S2C)
PMID:26749213	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC2G2.06c	(Figure 1a)
PMID:26749213	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC691.03c	(Figure 1a)
PMID:26749213	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC31A2.09c	(Figure 1a)
PMID:26749213	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells [has_penetrance] low	(Supporting Information Fig. S4A)
PMID:26749213	FYPO:0000423	decreased rate of endocytosis during vegetative growth [has_penetrance] 80	(comment: FM4-64 uptake (I made Henars original annotation into a double mutant so the attribution has changed))
PMID:26749213	GO:0072583	clathrin-dependent endocytosis	(comment: moved down drom endocytosis.) Delayed FM4-64 uptake when in combination with a clathrin mutationSlow dynamics of endocytic patch markers
PMID:26749213	FYPO:0005503	abnormally monopolar protein localization to cell tip [has_penetrance] low [assayed_using] PomBase:SPCC1840.02c	(comment: moved down from abnormal protein localization to cell tip (new term))
PMID:26749213	FYPO:0005515	abolished protein localization to cell cortex, with protein mislocalized to vacuole, during vegetative growth [has_penetrance] complete [assayed_using] PomBase:SPBC2G2.06c	(comment: moved down to new term from :protein mislocalized to cytoplasm during vegetative growth)
PMID:26749213	FYPO:0005515	abolished protein localization to cell cortex, with protein mislocalized to vacuole, during vegetative growth [assayed_using] PomBase:SPBC691.03c	(comment: moved down to new term from :protein mislocalized to cytoplasm during vegetative growth)
PMID:26776736	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC22E12.14c [part_of] negative regulation of G2/M transition of mitotic cell cycle [happens_during] cellular response to nutrient	(comment: MOVE EXTENSION DOWN TO NITROGEN) (comment: This can be inferred from all of the proposed EXP and is part of the proposed model we can delete if we can make in a better way)
PMID:26776736	GO:1905287	positive regulation of G2/M transition of mitotic cell cycle involved in cellular response to nitrogen starvation [happens_during] cellular response to nitrogen starvation	(comment: important when growing on poor nitrogen sources)
PMID:26776736	GO:0004674	protein serine/threonine kinase activity [directly_positively_regulates] PomBase:SPAC10F6.16 [part_of] positive regulation of G2/M transition of mitotic cell cycle involved in cellular response to nitrogen starvation	(comment: vw: changed to directly activates and added part_of They are deomstrating that the system is conserved...In Xenopus and mammalian cells, phosphorylation of ENSA by greatwall at serine 67 promotes its binding to and inhibition of PP2A$B55 phosphatase [8, 9]. enough evidence for function by IMP ALSO Our genetic and physiological data is in agreement with published work in budding yeast, Drosophila, Xenopus, and mammalian cells indicating that greatwall phosphorylates endo- sulfine to inhibit PP2A$B55 [8, 9, 27, 28, 35]. To test whether Igo1 is a direct target of Ppk18, we performed Ppk18 in vitro kinase assays using purified recombinant Igo1 and Igo1-S64A, as substrates. Extracts from wild-type (ppk18+) and Myc-tagged (ppk18-13myc) Ppk18 cells, treated for 1 hr with rapamycin in order to activate Ppk18, were immunoprecipitated with anti-c-Myc monoclonal antibodies. Ppk18-13myc immunoprecipitates were able to phosphorylate in vitro wild-type Igo1, but not Igo1-S64A Our genetic and physiological data is in agreement with published work in budding yeast, Drosophila, Xenopus, and mammalian cells indicating that greatwall phosphorylates endo- sulfine to inhibit PP2A$B55 [8, 9, 27, 28, 35]. To test whether Igo1 is a direct target of Ppk18, we performed Ppk18 in vitro kinase assays using purified recombinant Igo1 and Igo1-S64A, as substrates. Extracts from wild-type (ppk18+) and Myc-tagged (ppk18-13myc) Ppk18 cells, treated for 1 hr with rapamycin in order to activate Ppk18, were immunoprecipitated with anti-c-Myc monoclonal antibodies. Ppk18-13myc immunoprecipitates were able to phosphorylate in vitro wild-type Igo1, but not Igo1-S64A Our genetic and physiological data is in agreement with published work in budding yeast, Drosophila, Xenopus, and mammalian cells indicating that greatwall phosphorylates endo- sulfine to inhibit PP2A$B55 [8, 9, 27, 28, 35]. To test whether Igo1 is a direct target of Ppk18, we performed Ppk18 in vitro kinase assays using purified recombinant Igo1 and Igo1-S64A, as substrates. Extracts from wild-type (ppk18+) and Myc-tagged (ppk18-13myc) Ppk18 cells, treated for 1 hr with rapamycin in order to activate Ppk18, were immunoprecipitated with anti-c-Myc monoclonal antibodies. Ppk18-13myc immunoprecipitates were able to phosphorylate in vitro wild-type Igo1 but not Igo1-S64A (Figure S4A), indicating that fission yeast Ppk18 can act as a greatwall kinase.) Phosphorylation of Igo1 was severely impaired in cells deleted for ppk18 or expressing a kinase-dead version of ppk18 (ppk18- K595A or ppk18-KD) but was still present in cek1-deleted cells (Figure 4B), consistent with the idea that Ppk18 is the main greatwall kinase that phosphorylates Igo1 in medium with low nitrogen.
PMID:26776736	GO:0004865	protein serine/threonine phosphatase inhibitor activity [has_input] PomBase:SPBC16H5.07c [part_of] positive regulation of G2/M transition of mitotic cell cycle involved in cellular response to nitrogen starvation	again confirms other systems Endosulfines are small phosphoproteins, highly conserved from yeasts to humans, that specifically bind to and inhibit the PP2A$B55 protein phosphatase subcomplex [8, 9]. PP2A$B55 has been shown to be cell-cycle-regulated in Xenopus, following the opposite pattern of activity to Cdk1$Cyclin B (high in interphase and low in mitosis) [15]. To determine whether Ser64-phosphorylated Igo1 inhibits the PP2A$B55 (PP2A$Pab1 in fission yeast) phosphatase activity, we purified PP2A$Pab1 phosphatase from cells expressing GST- Pab1 using glutathione sepharose beads and assayed them for phosphatase activity. Wild-type Igo1 thiophosphorylated in vitro at Ser64 by Xenopus Greatwall, but not Igo1-S64A, inhibited more than 90% the phosphatase activity of PP2A$Pab1 (B55) (Figures S4B and S4C). This result indicates that Ser64- phosphorylated Igo1 inhibits the activity of PP2A$B55, analogous to the situation in budding yeast [27, 28, 35] and animal cells [8, 9].
PMID:26804021	GO:0000775	chromosome, centromeric region	(Fig. 1a)
PMID:26804021	GO:0099115	chromosome, subtelomeric region [exists_during] mitotic G2 phase	(Fig. 1a, 4) (knob)
PMID:26804021	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPAC15A10.15	(Fig. 3B)
PMID:26804021	FYPO:0005396	abolished protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPAC15A10.15	(Fig. 3B)
PMID:26804021	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPAC15A10.15	(Fig. 3B)
PMID:26804021	FYPO:0005396	abolished protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPAC15A10.15	(Fig. 3D)
PMID:26804021	FYPO:0006260	abolished subtelomeric chromatin knob formation	(Fig. 4)
PMID:26804021	FYPO:0006260	abolished subtelomeric chromatin knob formation	(Fig. 4c)
PMID:26804021	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_using] PomBase:SPAC15A10.15	(Fig. 4c)
PMID:26804021	FYPO:0005225	increased histone H3-K4 dimethylation during vegetative growth [assayed_using] subtelomere	(Fig. 5)
PMID:26804021	FYPO:0006263	increased histone H3-K36 trimethylation during vegetative growth [assayed_using] subtelomere	(Fig. 5)
PMID:26804021	FYPO:0006263	increased histone H3-K36 trimethylation during vegetative growth [assayed_using] subtelomere	(Fig. 5)
PMID:26804021	FYPO:0006263	increased histone H3-K36 trimethylation during vegetative growth [assayed_using] subtelomere	(Fig. 5)
PMID:26804021	FYPO:0005225	increased histone H3-K4 dimethylation during vegetative growth [assayed_using] subtelomere	(Fig. 5)
PMID:26804021	FYPO:0005225	increased histone H3-K4 dimethylation during vegetative growth [assayed_using] subtelomere	(Fig. 5)
PMID:26804021	FYPO:0005917	increased subtelomeric heterochromatin RNA level	(Fig. 5A)
PMID:26804021	FYPO:0005917	increased subtelomeric heterochromatin RNA level	(Fig. 5A)
PMID:26804021	FYPO:0005917	increased subtelomeric heterochromatin RNA level	(Fig. 5A)
PMID:26804021	FYPO:0005917	increased subtelomeric heterochromatin RNA level	(Fig. 5C)
PMID:26804021	FYPO:0005758	abnormal regulation of mitotic DNA replication initiation from late origin	(Fig. 7a)
PMID:26804021	FYPO:0006272	premature mitotic DNA replication initiation from late origin	(Fig. 7b) (comment: CHECK increased occurance?)
PMID:26804021	FYPO:0005918	decreased protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPAC15A10.15 [has_severity] high	(Fig. S6) (comment: CHECK check allele????)
PMID:26804917	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_at] FLEX_element [part_of] cell cycle switching, mitotic to meiotic cell cycle	(Fig. 4)
PMID:26804917	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_at] FLEX_element [part_of] negative regulation of cell cycle switching, mitotic to meiotic cell cycle	(Fig. 4)
PMID:26804917	MOD:00696	phosphorylated residue [added_during] meiosis I cell cycle phase [added_by] PomBase:SPBC11B10.09	(comment: Serine 481 is phosphorylated by Cig2/Cdc2 during meiosis I. Phosphorylation decreases Fkh2 DNA binding affinity)
PMID:2682257	FYPO:0002033	abolished protein phosphorylation during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Fig. 6B) (comment: Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	FYPO:0002085	normal vegetative cell growth	(Fig. 6B) (comment: Cells contain cdc2-F19 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09	(Fig. 6C) (comment: Cells contain cdc2-F19 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(Fig. 6b,C-F) (comment: Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	FYPO:0000670	abnormal mitotic sister chromatid separation [has_penetrance] high	(Fig. 6b,C-F) (comment: Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	FYPO:0001052	cut, small cell [has_penetrance] medium	(Fig. 6b,C-F) (comment: Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	FYPO:0002342	septated vegetative cell [has_penetrance] high	(Fig. 6b,C-F) (comment: Cells contain cdc2-F15 mutant on multi copy LEU2+ plasmid.)
PMID:2682257	MOD:00048	O4'-phospho-L-tyrosine [present_during] mitotic G2 phase	(Figs 1, 2, 3, 4, 5) (comment: cells blocked in late G2 and in mid mitosis)
PMID:2682257	MOD:00048	O4'-phospho-L-tyrosine [absent_during] mitotic M phase	(Figs 1,2,3,4,5) (comment: cells blocked in late G2 and in mid mitosis)
PMID:2682257	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Data not shown, assayed by colony growth on plates
PMID:26832414	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. 3B)
PMID:26832414	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. 3B)
PMID:26832414	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] medium	(Fig. 4A)
PMID:26832414	FYPO:0003096	decreased histone H3-K9 methylation at centromere outer repeat during vegetative growth [has_severity] low	(Fig. 4B)
PMID:26832414	FYPO:0006299	increased chromatin silencing at centromere outer repeat	(Fig. 4C)
PMID:26832414	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPAC18G6.02c [assayed_region] regional_centromere_outer_repeat_region [has_severity] low	(Fig. 4D)
PMID:26832414	FYPO:0000450	decreased protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPBC1105.17 [has_penetrance] 36	(Fig. 4F)
PMID:26869222	FYPO:0005645	resistance to Cutin-1 [has_severity] high	(comment: CONDITION +10µM Cutin-1)
PMID:26869222	FYPO:0000365	small nucleus [has_penetrance] 100	(comment: CONDITION Cells grown at 29°C)
PMID:26869222	FYPO:0005645	resistance to Cutin-1 [has_severity] high	(comment: CONDITION Growth was assayed in presence of 10µM Cutin-1.)
PMID:26869222	FYPO:0003286	decreased mitotic chromosome condensation [has_penetrance] high	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26869222	FYPO:0000029	abnormal chromosome segregation [has_severity] variable severity	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26869222	FYPO:0001513	normal mitotic sister chromatid segregation [has_penetrance] high	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26869222	FYPO:0001513	normal mitotic sister chromatid segregation [has_penetrance] high	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26869222	FYPO:0005645	resistance to Cutin-1 [has_severity] high	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26869222	FYPO:0005645	resistance to Cutin-1 [has_severity] high	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26869222	FYPO:0001127	abnormal cell size [has_severity] variable severity	(comment: CONDITION cells grown at 29°C for 6 hours in 30µM Cutin-1)
PMID:26869222	FYPO:0000344	enlarged nucleus during vegetative growth [has_penetrance] 100	(comment: CONDITION cells grown at 29°C)
PMID:26869222	FYPO:0005645	resistance to Cutin-1 [has_severity] medium	(comment: Cells show partial resistance to 30µM Cutin-1 for 6 hours.)
PMID:26869222	FYPO:0002403	abnormal nucleus [has_severity] variable severity	(comment: The size of the nucleus is not actually abnormal, it is the right size for the cell size but is variable because of the variable cell size at division)
PMID:26869222	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 16.1	(comment: This is in presence of 30µM Cutin-1 for 6 hours. Wild type cells show 36.3% abnormal chromosome segregation in same conditions)
PMID:26869222	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 64.9	(comment: This is in presence of 30µM Cutin-1 for 6 hours. Wild type cells show 36.3% abnormal chromosome segregation in same conditions)
PMID:26869222	FYPO:0005645	resistance to Cutin-1 [has_severity] high	(comment: growth in presence of 10-100µM Cutin-1 for 15 hours at 100µM Cutin-1 reduced to 70% compared to ~10% in wild type; assayed in presence of 30µM Cutin-1 for 6 hours shows no chromosome defects or cell length defects)
PMID:26869222	FYPO:0005645	resistance to Cutin-1 [has_severity] high	(comment: shows no chromosome defects or cell length defects growth in presence of 10-100µM Cutin-1 for 15 hours at 100µM Cutin-1 reduced to 70% compared to ~10% in wild type)
PMID:26869222	FYPO:0005645	resistance to Cutin-1 [has_severity] variable severity	(comment: the resistance to Cutin-1 is dependent on nuclear size. Longer cells have a larger nucleus and are more resistant compared to smaller cells with a smaller nucleus)
PMID:26869222	FYPO:0005712	sensitive to Cutin-1 [has_penetrance] 60	Cells show increased mitotic chromosome segregation defects in presence of Cutin-1
PMID:26877082	FYPO:0000118	multiseptate vegetative cell [has_penetrance] low	(Figure 2)
PMID:26877082	FYPO:0005840	incomplete, asymmetric septum [has_penetrance] low	(Figure 2C)
PMID:26877082	FYPO:0003444	abnormal medial cortical node condensation [has_severity] high	(Figure 2D)
PMID:26877082	FYPO:0003444	abnormal medial cortical node condensation [has_severity] high	(Figure 2D)
PMID:26877082	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_severity] high	(Figure 2D) (comment: CHECK abnormal cable clustering)
PMID:26877082	FYPO:0000134	branched, elongated, multiseptate cell	(Figure 4A)
PMID:26877082	FYPO:0001009	abolished actomyosin contractile ring assembly [has_penetrance] 50	(Figure S4C)
PMID:26877082	FYPO:0000419	decreased rate of cytokinesis	(Figures 1A, S1A, S1B, 1D, S1E)
PMID:26877082	FYPO:0002872	abnormal endoplasmic reticulum localization	(Figures 1A, S1A, S1B, 1D, S1E)
PMID:26882497	MOD:00046	O-phospho-L-serine	(Fig 1)
PMID:26882497	MOD:00046	O-phospho-L-serine	(Fig 1)
PMID:26882497	MOD:00046	O-phospho-L-serine	(Fig 1)
PMID:26882497	MOD:00047	O-phospho-L-threonine	(Fig. 1)
PMID:26882497	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC1795.01c [has_severity] low	(Fig. 2)
PMID:26882497	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC1795.01c [has_severity] high	(Fig. 2)
PMID:26882497	GO:1990948	ubiquitin ligase inhibitor activity [has_input] anaphase-promoting complex [part_of] mitotic spindle assembly checkpoint signaling [happens_during] mitotic metaphase	(Fig. 6) (comment: they incubate with 3 different E2s so can't specify a substrate)
PMID:26882497	GO:0007094	mitotic spindle assembly checkpoint signaling	(Fig. S4A and 2C)
PMID:26882497	GO:0007094	mitotic spindle assembly checkpoint signaling	(Fig. S4A and 2C)
PMID:26882497	FYPO:0004357	decreased protein phosphorylation during mitosis [assayed_using] PomBase:SPCC1795.01c	(Figure 1a) (comment: they don't really show that the modification is phosphorylation, but considering the rest of the data this annotation seems ok)
PMID:26882497	FYPO:0001384	abolished protein kinase activity [assayed_enzyme] PomBase:SPBC106.01 [assayed_substrate] PomBase:SPCC1795.01c	(Figure 1b)
PMID:26882497	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC1795.01c [part_of] mitotic spindle assembly checkpoint signaling [happens_during] mitotic metaphase [occurs_in] outer kinetochore	(Figure 1b)
PMID:26882497	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC106.01 [assayed_substrate] PomBase:SPCC1795.01c [has_severity] high	(Figure 1d)
PMID:26882497	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC106.01 [assayed_substrate] PomBase:SPCC1795.01c [has_severity] low	(Figure 1d)
PMID:26882497	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC106.01 [assayed_substrate] PomBase:SPCC1795.01c [has_severity] medium	(Figure 1d)
PMID:26882497	FYPO:0005779	normal protein localization to kinetochore during mitosis [assayed_using] PomBase:SPCC1795.01c	(Figure 2a) (comment: 20 mins after synchronized released into mitosis. I wouldn't want to guess exactly what stage of mitosis this is)
PMID:26882497	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Figure 2b)
PMID:26882497	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Figure 2b)
PMID:26882497	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_penetrance] medium	(Figure 2b,c)
PMID:26882497	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	(Figure 2b,c)
PMID:26882497	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] low	(Figure 2bc,5)
PMID:26882497	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] low	(Figure 2bc,5)
PMID:26882497	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	(Figure 2bc,5)
PMID:26882497	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] high	(Figure 2bc,5)
PMID:26882497	FYPO:0005784	decreased extent and duration of protein-protein interaction [assayed_using] PomBase:SPAC19G12.01c [assayed_using] PomBase:SPCC1795.01c	(Figure 4a)
PMID:26882497	FYPO:0005784	decreased extent and duration of protein-protein interaction [assayed_using] PomBase:SPAC19G12.01c [assayed_using] PomBase:SPBC20F10.06	(Figure 4a)
PMID:26882497	FYPO:0005785	decreased duration of protein-protein interaction [assayed_using] PomBase:SPAC19G12.01c [assayed_using] PomBase:SPBC20F10.06	(Figure 5a)
PMID:26882497	FYPO:0005785	decreased duration of protein-protein interaction [assayed_using] PomBase:SPAC19G12.01c [assayed_using] PomBase:SPBC20F10.06	(Figure 5a)
PMID:26882497	FYPO:0005785	decreased duration of protein-protein interaction [assayed_using] PomBase:SPAC19G12.01c [assayed_using] PomBase:SPCC1795.01c	(Figure 5a)
PMID:26882497	FYPO:0005784	decreased extent and duration of protein-protein interaction [assayed_using] PomBase:SPAC19G12.01c [assayed_using] PomBase:SPBC20F10.06	(Figure 5a)
PMID:26882497	FYPO:0005785	decreased duration of protein-protein interaction [assayed_using] PomBase:SPAC19G12.01c [assayed_using] PomBase:SPCC1795.01c	(Figure 5a)
PMID:26882497	FYPO:0005784	decreased extent and duration of protein-protein interaction [assayed_using] PomBase:SPAC19G12.01c [assayed_using] PomBase:SPCC1795.01c	(Figure 5a)
PMID:26882497	FYPO:0001687	normal growth on benomyl	(Figure S3)
PMID:26882497	FYPO:0001687	normal growth on benomyl	(Figure S3)
PMID:26882497	FYPO:0000094	sensitive to benomyl	(Figure S3)
PMID:26882497	FYPO:0001687	normal growth on benomyl	(Figure S3)
PMID:26882497	GO:1990757	ubiquitin ligase activator activity	(comment: 3 E2s mixed in the same assay so can't specify a substrate)
PMID:26882497	GO:0007094	mitotic spindle assembly checkpoint signaling	(comment: it looks like it is involved in MAINTAINING the checkpoint) fig S4A and 2C
PMID:26882497	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC106.01 [added_during] mitotic M phase	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC106.01 [added_during] mitotic M phase	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC106.01 [added_during] mitotic M phase	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC106.01 [added_during] mitotic M phase	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC106.01 [added_during] mitotic M phase	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC106.01 [added_during] mitotic M phase	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC106.01	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26882497	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC106.01 [added_during] mitotic M phase	"(comment: they don't show the ""added during"" data so this is a bit anecdotal from the text)"
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000098	sensitive to calcium	(Fig. 1)
PMID:26891792	FYPO:0000021	spheroid vegetative cell	(Fig. 3)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin [has_severity] low	(Fig. 4)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin [has_severity] low	(Fig. 4)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin	(Fig. 4)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin	(Fig. 4)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin	(Fig. 4)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin	(Fig. 4)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin [has_severity] low	(Fig. 4)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin [has_severity] low	(Fig. 4)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin	(Fig. 4)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin [has_severity] medium	(Fig. 5)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin [has_severity] medium	(Fig. 5)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin [has_severity] medium	(Fig. 5)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin [has_severity] high	(Fig. 5)
PMID:26891792	FYPO:0003559	sensitive to doxorubicin [has_severity] high	(Fig. 5)
PMID:26900649	GO:0140483	kinetochore adaptor activity [has_input] PomBase:SPBC106.01	"(comment: chromatin recruiter) Together, we concluded that the primary defects observed in the ndc80-AK01 mutant can be attributed to impaired Mph1 recruitment to kinetochores, which leads to failure in recruitment of the other SAC components and abortive mitotic arrest. (comment: COUld also get 'upstream of/affects SAC"")"
PMID:26912660	GO:0000785	chromatin [exists_during] single-celled organism vegetative growth phase	(comment: exists during veg growth & glucose starv & HU stress)
PMID:26912660	GO:0000785	chromatin [exists_during] cellular response to hydroxyurea	(comment: exists during veg growth & glucose starv & HU stress)
PMID:26912660	GO:0000785	chromatin [exists_during] cellular response to glucose starvation	(comment: exists during veg growth & glucose starv & HU stress)
PMID:26941334	GO:0110085	mitotic actomyosin contractile ring	(comment: localization dependent on actin cytoskeleton)
PMID:26942678	GO:1990251	nuclear exosome focus	(comment: Erh1 localizes with Mmi1 both during mitotic cell cycle and meiosis)
PMID:26942678	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth	(comment: author statement)
PMID:26942678	FYPO:0005858	altered level of translation gene mRNA during vegetative growth	(comment: some up some down)
PMID:26942678	FYPO:0005857	altered antisense RNA level during vegetative growth	(comment: some up some down)
PMID:26960792	GO:0005096	GTPase activator activity [has_input] PomBase:SPAC16.01	(comment: RhoGAP, GTPase activating protein for Cdc42 and Rho2)
PMID:26960792	FYPO:0001120	pear-shaped vegetative cell [has_penetrance] medium	(comment: can't assess viability)
PMID:26960792	FYPO:0000129	spherical vegetative cell [has_penetrance] medium	(comment: can't assess viability)
PMID:26960792	FYPO:0000129	spherical vegetative cell [has_penetrance] medium	(comment: can't assess viability)
PMID:26960792	FYPO:0000129	spherical vegetative cell [has_penetrance] medium	(comment: can't assess viability)
PMID:26960792	FYPO:0000129	spherical vegetative cell [has_penetrance] medium	(comment: can't assess viability)
PMID:26960792	FYPO:0000129	spherical vegetative cell [has_penetrance] medium	(comment: can't assess viability)
PMID:26960792	FYPO:0000129	spherical vegetative cell [has_penetrance] medium	(comment: can't assess viability)
PMID:26960792	FYPO:0000928	abnormal protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPBC354.13	(comment: hard to be more specific when cell shape is also abnormal (Rga6 normally goes to lateral cortex & non-growing tip))
PMID:26960792	FYPO:0002110	viable tapered vegetative cell [has_penetrance] high [has_severity] variable severity	growing tips were longer and thinner than those of wild-type cells. This morphology is similar to the one caused by overexpression of Rga4.
PMID:26990381	FYPO:0005585	decreased cellular triglyceride level during vegetative growth [has_severity] high	As expected, these cells contained negligible amounts of TAG after lysis and TLC analysis (Figure 3K).
PMID:26990381	FYPO:0002061	inviable vegetative cell population	The same cells were not viable when grown in YPO (Figure S2B,C).
PMID:26990381	FYPO:0006054	decreased lipid droplet formation [has_severity] high	There were a negligible number of BODIPY 493/503-stained droplets throughout those elongated double knockout cells compared to positive controls (Figure 1F,G).
PMID:26990381	GO:0097038	perinuclear endoplasmic reticulum	This was especially true in the case of Are1p. mYFP-Are1p and mYFP-Are2p were both localized throughout the nuclear and cortical/peripheral ER (Figure 2A,B). We repeated these experiments in wild-type genetic backgrounds and saw qualitatively similar YFP signal patterns (Figure 2C,D). Thus, the localizations of these two enzymes do not provide evidence to explain polarized lipid droplet formation in either cdc25-22 or wild-type fission yeast cells
PMID:26990381	GO:0097038	perinuclear endoplasmic reticulum	This was especially true in the case of Are1p. mYFP-Are1p and mYFP-Are2p were both localized throughout the nuclear and cortical/peripheral ER (Figure 2A,B). We repeated these experiments in wild-type genetic backgrounds and saw qualitatively similar YFP signal patterns (Figure 2C,D). Thus, the localizations of these two enzymes do not provide evidence to explain polarized lipid droplet formation in either cdc25-22 or wild-type fission yeast cells
PMID:26990381	GO:0032541	cortical endoplasmic reticulum	This was especially true in the case of Are1p. mYFP-Are1p and mYFP-Are2p were both localized throughout the nuclear and cortical/peripheral ER (Figure 2A,B). We repeated these experiments in wild-type genetic backgrounds and saw qualitatively similar YFP signal patterns (Figure 2C,D). Thus, the localizations of these two enzymes do not provide evidence to explain polarized lipid droplet formation in either cdc25-22 or wild-type fission yeast cells
PMID:26990381	GO:0032541	cortical endoplasmic reticulum	This was especially true in the case of Are1p. mYFP-Are1p and mYFP-Are2p were both localized throughout the nuclear and cortical/peripheral ER (Figure 2A,B). We repeated these experiments in wild-type genetic backgrounds and saw qualitatively similar YFP signal patterns (Figure 2C,D). Thus, the localizations of these two enzymes do not provide evidence to explain polarized lipid droplet formation in either cdc25-22 or wild-type fission yeast cells
PMID:26990381	GO:0140042	lipid droplet formation	Thus, plh1Δdga1Δ double knockouts appear to have hampered droplet biogenesis events and it is probable that TAG plays a crucial role in the ER escape hatch mechanism with minimal amounts needed even for SE lipid droplet formation [40].
PMID:26990381	GO:0140042	lipid droplet formation	Thus, plh1Δdga1Δ double knockouts appear to have hampered droplet biogenesis events and it is probable that TAG plays a crucial role in the ER escape hatch mechanism with minimal amounts needed even for SE lipid droplet formation [40].
PMID:26990381	FYPO:0007343	abolished lipid droplet formation	Yeast cells lacking both genes (plh1Δdga1Δ) had no droplets but instead showed vesicle-shaped BODIPY 493/503-stained structures when grown in YE5S (Figure 3J).
PMID:26990381	FYPO:0007342	decreased triglyceride level in lipid droplet	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
PMID:26990381	FYPO:0007342	decreased triglyceride level in lipid droplet	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
PMID:26990381	FYPO:0005585	decreased cellular triglyceride level during vegetative growth	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
PMID:26990381	FYPO:0005585	decreased cellular triglyceride level during vegetative growth	analysis revealed that both strains had reduced whole-cell and lipid droplet TAG levels (Figure 3F,I).
PMID:26990381	GO:0032541	cortical endoplasmic reticulum	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	GO:0097038	perinuclear endoplasmic reticulum	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	GO:0097038	perinuclear endoplasmic reticulum	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	GO:0097038	perinuclear endoplasmic reticulum	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:26990381	GO:0032541	cortical endoplasmic reticulum	mYFP-Dga1p and mYFP-Plh1p were both localized throughout the nuclear and cortical/peripheral ER (Figure 4A,B).
PMID:27023709	GO:0002183	cytoplasmic translational initiation	(Fig. 2H) (comment: cell free system)
PMID:27023709	GO:0002183	cytoplasmic translational initiation	(Fig. 2H) (comment: cell free system)
PMID:27023709	GO:0002183	cytoplasmic translational initiation	(Fig. 2H) (comment: cell free system)
PMID:27023709	GO:0002183	cytoplasmic translational initiation	(Fig. 2H) (comment: cell free system)
PMID:27023709	GO:0002183	cytoplasmic translational initiation	(Fig. 2H) (comment: cell free system)
PMID:27023709	FYPO:0005387	decreased eukaryotic translation initiation factor 2B complex assembly	(Fig. 2i)
PMID:27023709	FYPO:0005387	decreased eukaryotic translation initiation factor 2B complex assembly	(Fig. 2i)
PMID:27023709	FYPO:0005387	decreased eukaryotic translation initiation factor 2B complex assembly	(Fig. 2i)
PMID:27069798	GO:0051015	actin filament binding	(comment: Bundling activity inferred from pull-down experiments as well as from fluorescence microscopy)
PMID:27075176	FYPO:0000061	multinucleate vegetative cell [has_penetrance] 80	(Fig. 6C)
PMID:27075176	FYPO:0001364	abnormal actomyosin contractile ring contraction [has_penetrance] 80	(Fig. 6C)
PMID:27075176	FYPO:0000161	abnormal actomyosin contractile ring assembly [has_penetrance] 80	(Fig. 6C)
PMID:27075176	FYPO:0003338	abnormal actomyosin contractile ring morphology [has_penetrance] 80	(Fig. 6C)
PMID:27075176	FYPO:0001254	multinucleate multiseptate vegetative cell, septa grouped [has_penetrance] 80	(Fig. 6C)
PMID:27075176	FYPO:0000118	multiseptate vegetative cell [has_penetrance] 80	(Fig. 6C)
PMID:27075176	GO:0003786	actin lateral binding [part_of] actin filament bundle assembly	(Figure 1, C and D).
PMID:27075176	GO:0032432	actin filament bundle	(Figure 3A and Supplemental Video 3).
PMID:27075176	GO:0051017	actin filament bundle assembly	(comment: mixed orientations)
PMID:27082518	FYPO:0003440	cell lysis during cytokinesis	(Fig 6AB)
PMID:27082518	GO:0032153	cell division site [exists_during] mitotic M phase	(Fig. 1 C-E)
PMID:27082518	GO:0032153	cell division site [exists_during] mitotic M phase	(Fig. 1 C-E)
PMID:27082518	GO:0032153	cell division site [exists_during] mitotic M phase	(Fig. 1B)
PMID:27082518	FYPO:0002088	exocytic vesicles present in increased numbers at septum during septum assembly	(Fig. 2H, 7A)
PMID:27082518	FYPO:0002089	abnormal exocytosis during vegetative growth [assayed_using] PomBase:SPAC6G9.11 [has_penetrance] 10	(Fig. 3B)
PMID:27082518	FYPO:0002089	abnormal exocytosis during vegetative growth [assayed_using] PomBase:SPAC6G9.11 [has_penetrance] 7	(Fig. 3B)
PMID:27082518	GO:0035838	growing cell tip [exists_during] mitotic interphase	(Fig. 5a)
PMID:27082518	FYPO:0001904	premature actomyosin contractile ring disassembly	(Fig. 6A,B)
PMID:27082518	FYPO:0001368	normal actomyosin contractile ring assembly	(Fig. 6A,B)
PMID:27082518	FYPO:0001364	abnormal actomyosin contractile ring contraction	(Fig. 6A,B)
PMID:27082518	FYPO:0002060	viable vegetative cell population	(Fig. 6E)
PMID:27082518	FYPO:0000223	elongated multiseptate vegetative cell [has_penetrance] high	(Fig. 6E)
PMID:27082518	FYPO:0000134	branched, elongated, multiseptate cell [has_penetrance] low	(Fig. 6E)
PMID:27082518	FYPO:0003440	cell lysis during cytokinesis	(Fig. 6c)
PMID:27082518	FYPO:0002088	exocytic vesicles present in increased numbers at septum during septum assembly	(Fig. 7A)
PMID:27082518	FYPO:0002087	exocytic vesicles present in increased numbers at cell tip during mitotic interphase	(Fig. 7C,D)
PMID:27082518	FYPO:0002088	exocytic vesicles present in increased numbers at septum during septum assembly	(Fig. 7C,D)
PMID:27082518	FYPO:0002086	exocytic vesicles present in increased numbers	(Fig. 7D)
PMID:27082518	FYPO:0005552	decreased protein localization to cleavage furrow rim [assayed_using] PomBase:SPBC19G7.05c	(Fig. 7E)
PMID:27082518	FYPO:0005552	decreased protein localization to cleavage furrow rim [assayed_using] PomBase:SPBC19G7.05c	(Fig. 7E)
PMID:27082518	FYPO:0005551	decreased protein localization to cleavage furrow [assayed_using] PomBase:SPAC821.09	(Fig. 7E)
PMID:27082518	FYPO:0005543	increased duration of actomyosin contractile ring contraction	(Fig. S3B)
PMID:27082518	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPAC6G10.05c	(Fig. S4E)
PMID:27082518	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPCC970.09	(Fig. S4F and S4G)
PMID:27082518	FYPO:0001677	increased protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAC6G10.05c	(Fig. S6 B) (comment: probably due to delayed fusion of TRAPP containing vesicles with PM)
PMID:27082518	FYPO:0001677	increased protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAC6G9.11	(Fig. S6 C) (comment: probably due to delayed fusion of TRAPP containing vesicles with PM)
PMID:27082518	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC18G6.03	(Fig. S6A)
PMID:27082518	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPAC18G6.03	(Fig. S6A)
PMID:27082518	FYPO:0002061	inviable vegetative cell population	(Figure S4D)
PMID:27098497	FYPO:0005606	delayed onset of protein localization to double-strand break site [assayed_using] PomBase:SPBC660.13c	(comment: distal to break point)
PMID:27098497	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(comment: same as rhp6delta alone)
PMID:27098497	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(comment: same as rhp6delta alone)
PMID:27098497	FYPO:0002553	abnormal double-strand break processing	(comment: same as without csn1delta)
PMID:27098497	FYPO:0002553	abnormal double-strand break processing	(comment: same as without csn5delt)
PMID:27098497	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_severity] medium	(comment: same as without exo1+ overexpression)
PMID:27098497	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_severity] medium	(comment: same as without exo1delta)
PMID:27098497	FYPO:0002553	abnormal double-strand break processing	(comment: same as without exo1delta)
PMID:27098497	FYPO:0002474	decreased protein localization to double-strand break site [assayed_using] PomBase:SPBC29A10.05	(comment: same as without htb1-K119R)
PMID:27098497	FYPO:0002553	abnormal double-strand break processing	(comment: worse than without rqh1delta)
PMID:27101289	GO:0042162	telomeric repeat DNA binding [occurs_at] telomeric_repeat	binds with high affinity to diverged S. pombe telomeric repeats)
PMID:27101289	GO:0043565	sequence-specific DNA binding	binds with high affinity to mammalian-type 5'-TTAGGG-3' telomeric repeats, and with very low affinity to diverged S. pombe telomeric repeats
PMID:27146110	FYPO:0006039	incomplete mitotic metaphase chromosome recapture [has_penetrance] 30	(Figure 1, 2)
PMID:27146110	FYPO:0006040	abnormal kinetochore microtubule polymerization during mitotic metaphase chromosome recapture [has_penetrance] 50	(Figure 1, 2)
PMID:27146110	FYPO:0006039	incomplete mitotic metaphase chromosome recapture [has_penetrance] 35	(Figure 1, 2)
PMID:27146110	FYPO:0006039	incomplete mitotic metaphase chromosome recapture [has_penetrance] 40	(Figure 1, 2)
PMID:27146110	FYPO:0006040	abnormal kinetochore microtubule polymerization during mitotic metaphase chromosome recapture [has_penetrance] 20	(Figure 1, 2)
PMID:27146110	FYPO:0006041	decreased rate of mitotic metaphase chromosome recapture	(Figure 2)
PMID:27146110	FYPO:0003779	abnormal nuclear envelope morphology during mitosis	(Figure 2)
PMID:27146110	FYPO:0006041	decreased rate of mitotic metaphase chromosome recapture	(Figure 2)
PMID:27146110	FYPO:0006041	decreased rate of mitotic metaphase chromosome recapture	(Figure 2)
PMID:27146110	FYPO:0005364	decreased rate of kinetochore sliding during chromosome recapture	(Figure 2)
PMID:27146110	FYPO:0005364	decreased rate of kinetochore sliding during chromosome recapture	(Figure 2)
PMID:27146110	FYPO:0006043	increased rate of kinetochore sliding during chromosome recapture	(Figure 2)
PMID:27146110	FYPO:0006040	abnormal kinetochore microtubule polymerization during mitotic metaphase chromosome recapture [has_penetrance] 20	(Figure 3)
PMID:27146110	FYPO:0005960	multipolar mitotic spindle	(Figure 3)
PMID:27146110	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_using] PomBase:SPBC1685.15c	(Figure 4)
PMID:27146110	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_using] PomBase:SPBC2F12.13	(Figure 4)
PMID:27146110	FYPO:0006047	decreased interkinetochore distance before mitotic anaphase	(Figure 5)
PMID:27146110	FYPO:0006045	delayed onset of mitotic sister chromatid biorientation	(Figure 5)
PMID:27146110	FYPO:0006045	delayed onset of mitotic sister chromatid biorientation	(Figure 5)
PMID:27146110	FYPO:0006046	uncentered mitotic chromosome congression	(Figure 5)
PMID:27146110	FYPO:0006049	fluctuating mitotic spindle length	(Figure 6)
PMID:27146110	FYPO:0006049	fluctuating mitotic spindle length	(Figure 6)
PMID:27146110	FYPO:0006049	fluctuating mitotic spindle length	(Figure 6)
PMID:27146110	FYPO:0006049	fluctuating mitotic spindle length	(Figure 6)
PMID:27146110	FYPO:0004705	delayed onset of mitotic sister chromatid separation	(Figure 7)
PMID:27146110	FYPO:0004101	lagging mitotic chromosomes, with complete sister chromatid separation	(Figure 7)
PMID:27146110	FYPO:0004101	lagging mitotic chromosomes, with complete sister chromatid separation	(Figure 7)
PMID:27146110	FYPO:0004101	lagging mitotic chromosomes, with complete sister chromatid separation	(Figure 7)
PMID:27146110	FYPO:0004101	lagging mitotic chromosomes, with complete sister chromatid separation	(Figure 7, 1)
PMID:27146110	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Figure 8)
PMID:27146110	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Figure 8)
PMID:27146110	FYPO:0006044	long mitotic kinetochore microtubules with kinetochore at tip of nuclear envelope protrusion	(Figure 8) (comment: anaphase B)
PMID:27146110	FYPO:0006084	sensitive to cold shock	(Table 1)
PMID:27146110	FYPO:0006084	sensitive to cold shock	(Table 1)
PMID:27146110	FYPO:0006084	sensitive to cold shock	(Table 1)
PMID:27146110	FYPO:0006084	sensitive to cold shock	(Table 1)
PMID:27146110	FYPO:0004021	long polar microtubules	(comment: *****The definition of this term is not right) Figure 2
PMID:27146110	FYPO:0004021	long polar microtubules	(comment: *****The definition of this term is not right) Figure 2
PMID:27146110	FYPO:0004705	delayed onset of mitotic sister chromatid separation	(comment: ***DELAYED) Figure 7
PMID:27146110	FYPO:0004705	delayed onset of mitotic sister chromatid separation	(comment: DELAYED) Figure 7
PMID:27151298	GO:0061578	K63-linked deubiquitinase activity [happens_during] S phase [has_input] PomBase:SPBC16D10.09	(comment: Delete K63-ubiquitin chains from 3 to 8 ubiquitins)
PMID:27151298	MOD:01148	ubiquitinylated lysine [removed_by] PomBase:SPBC713.02c	(comment: K63-diubiquitin chain)
PMID:27151298	MOD:01148	ubiquitinylated lysine [added_by] PomBase:SPAC13G6.01c [added_during] S phase	(comment: K63-diubiquitin chain)
PMID:27151298	MOD:01148	ubiquitinylated lysine [added_by] PomBase:SPAC13G6.01c [added_during] S phase [present_during] cellular response to oxidative stress	(comment: K63-ubiquitin chain from 3 to 8 ubiquitin molecules)
PMID:27151298	MOD:01148	ubiquitinylated lysine [removed_by] PomBase:SPAC328.06	(comment: K63-ubiquitin chain from 3 to 8 ubiquitin molecules)
PMID:27168121	GO:0005515	protein binding	(Fig. 1C)
PMID:27168121	GO:0051286	cell tip [exists_during] mitotic interphase	(Fig. 1b)
PMID:27168121	GO:0032153	cell division site [exists_during] mitotic anaphase B	(Fig. 1b)
PMID:27168121	FYPO:0001492	viable elongated vegetative cell	(Figure 3B)
PMID:27168121	FYPO:0001492	viable elongated vegetative cell	(Figure 3B)
PMID:27168121	FYPO:0001919	fragmented nucleus during vegetative growth	(Figure 3C)
PMID:27168121	FYPO:0000972	increased number of Rad52 foci during vegetative growth	(Figure 3C)
PMID:27168121	FYPO:0001861	increased minichromosome loss upon segregation during vegetative growth	(Figure 3D)
PMID:27168121	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Figure 3E)
PMID:27183912	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c	(comment: can't distinguish tlh1 and tlh2 as identical sequences)
PMID:27183912	FYPO:0005602	normal subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11 [assayed_using] PomBase:SPBCPT2R1.08c	(comment: can't distinguish tlh1 and tlh2 as identical sequences)
PMID:27188733	FYPO:0000614	increased duration of mitotic S phase [has_severity] low	(comment: says increased proportion, which is a synonym)
PMID:27191590	GO:0005737	cytoplasm	(Fig. 1B)
PMID:27191590	FYPO:0001501	sensitive to brefeldin A	(Fig. 1C, 4)
PMID:27191590	FYPO:0001164	normal growth on glucose carbon source	(Fig. 1C, 4)
PMID:27191590	FYPO:0005193	resistance to torin1	(Fig. 1C, 6C, 7C, S5)
PMID:27191590	FYPO:0001501	sensitive to brefeldin A	(Fig. 4D)
PMID:27191590	FYPO:0001501	sensitive to brefeldin A	(Fig. 4E)
PMID:27191590	FYPO:0000123	large vacuoles during vegetative growth	(Fig. 5A)
PMID:27191590	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBP23A10.10	(Fig. 6B)
PMID:27191590	FYPO:0000836	increased protein level [assayed_using] PomBase:SPBP23A10.10	(Fig. 6B)
PMID:27191590	FYPO:0005193	resistance to torin1	(Fig. 6C)
PMID:27191590	FYPO:0001501	sensitive to brefeldin A	(Fig. 6C)
PMID:27191590	FYPO:0001501	sensitive to brefeldin A	(Fig. 6C)
PMID:27191590	FYPO:0005193	resistance to torin1	(Fig. 6C)
PMID:27191590	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC30D10.10c [assayed_using] PomBase:SPBP23A10.10	(Fig. 6D)
PMID:27191590	MOD:00696	phosphorylated residue	(Fig. 6E-G)
PMID:27191590	FYPO:0001501	sensitive to brefeldin A	(Fig. 7C)
PMID:27191590	FYPO:0005193	resistance to torin1	(Fig. 7C)
PMID:27191590	GO:1904262	negative regulation of TORC1 signaling [happens_during] cellular response to stress	happens during cellular resposne to BFA Fig 3A, Fig 4A-B, Fig 5B, Fig S3
PMID:27194449	FYPO:0003347	altered substrate specificity	(comment: CHECK of human pyruvyltransferase activity for the LacNAc-pNP)
PMID:27194449	FYPO:0003347	altered substrate specificity	(comment: CHECK of human pyruvyltransferase activity for the LacNAc-pNP)
PMID:27268234	FYPO:0008219	increased histone H3-K56 acetylation in transcribed regions during mitotic G2/M phase [has_severity] high	(Fig. 3A)
PMID:27268234	FYPO:0008219	increased histone H3-K56 acetylation in transcribed regions during mitotic G2/M phase [has_severity] medium	(Fig. 3A)
PMID:27268234	FYPO:0008220	increased histone H4-K20 monomethylation in transcribed regions during mitotic G2/M phase [has_severity] medium	(Fig. 3B)
PMID:27268234	FYPO:0008220	increased histone H4-K20 monomethylation in transcribed regions during mitotic G2/M phase [has_severity] high	(Fig. 3B)
PMID:27268234	FYPO:0008221	normal histone H3-K56 acetylation during mitotic G2/M phase	(Fig. S5A)
PMID:27268234	FYPO:0008221	normal histone H3-K56 acetylation during mitotic G2/M phase	(Fig. S5A)
PMID:27268234	FYPO:0008224	decreased histone H4-K20 trimethylation during mitotic G2/M phase	(Fig. S5B)
PMID:27268234	FYPO:0008223	normal histone H4-K20 trimethylation during mitotic G2/M phase	(Fig. S5B)
PMID:27268234	FYPO:0008222	normal histone H4-K20 monomethylation during mitotic G2/M phase	(Fig. S5B)
PMID:27268234	FYPO:0008222	normal histone H4-K20 monomethylation during mitotic G2/M phase	(Fig. S5B)
PMID:27268234	FYPO:0003557	increased antisense RNA level	(Fig. S6)
PMID:27268234	FYPO:0007472	abnormal histone exchange	(Fig. S6)
PMID:27268234	FYPO:0003557	increased antisense RNA level	(Fig. S6)
PMID:27268234	FYPO:0007472	abnormal histone exchange	(Fig. S6)
PMID:27325741	FYPO:0002061	inviable vegetative cell population	(comment: temperature permissive for ts cdc17-K42)
PMID:27325741	FYPO:0002061	inviable vegetative cell population	(comment: temperature permissive for ts cdc17-K42)
PMID:27325741	FYPO:0002061	inviable vegetative cell population	(comment: temperature permissive for ts cdc17-K42)
PMID:27327046	GO:0140116	fluoride export across plasma membrane	(Comment: Expression of fex1 from a plasmid in fex1Del/fex2Del double deletion mutant rescues fluoride sensitivity.)
PMID:27327046	FYPO:0002177	viable vegetative cell with normal cell morphology	(Fig. S2, 3)
PMID:27327046	FYPO:0001357	normal vegetative cell population growth	(Fig. S2, 3)
PMID:27327046	FYPO:0003368	resistance to sodium fluoride [has_severity] high	(Fig. S2, 3)
PMID:27327046	FYPO:0001357	normal vegetative cell population growth	(Fig. S2, 3)
PMID:27327046	FYPO:0003369	sensitive to sodium fluoride [has_severity] high	(Figures 2 and 3A, B)
PMID:27327046	GO:0140116	fluoride export across plasma membrane	(comment: Deletion of both homologues fex1 and fex2 make cells highly sensitive to fluoride. Expression of fex1 from a plasmid in fex1Del/fex2Del double deletion mutant rescues fluoride sensitivity.)
PMID:27327046	GO:1903425	fluoride transmembrane transporter activity [part_of] fluoride export across plasma membrane [part_of] cellular detoxification of fluoride	(comment: I changed the evidence from IDA to IMP /AL)
PMID:27327046	GO:1903425	fluoride transmembrane transporter activity [part_of] fluoride export across plasma membrane [part_of] cellular detoxification of fluoride	(comment: I changed the evidence from IDA to IMP /AL)
PMID:27334362	GO:0005637	nuclear inner membrane	(Fig. 1A)
PMID:27334362	GO:0005637	nuclear inner membrane	(Fig. 1a)
PMID:27334362	FYPO:0001234	slow vegetative cell population growth	(Fig. 2B)
PMID:27334362	FYPO:0001357	normal vegetative cell population growth	(Fig. 2C)
PMID:27334362	FYPO:0005371	increased linear minichromosome loss during vegetative growth [has_penetrance] high	(Fig. 2D)
PMID:27334362	FYPO:0005371	increased linear minichromosome loss during vegetative growth	(Fig. 2D)
PMID:27334362	FYPO:0005371	increased linear minichromosome loss during vegetative growth	(Fig. 2D)
PMID:27334362	FYPO:0005371	increased linear minichromosome loss during vegetative growth [has_penetrance] high	(Fig. 2D) (comment: additive)
PMID:27334362	FYPO:0005371	increased linear minichromosome loss during vegetative growth [has_penetrance] 9.7	(Fig. 2a)
PMID:27334362	GO:0061638	CENP-A containing chromatin	(Fig. 3A,B)
PMID:27334362	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_penetrance] high	(Fig. 3C)
PMID:27334362	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 3C)
PMID:27334362	FYPO:0005554	abolished histone H3-K9 dimethylation at centromere inner repeat during vegetative growth	(Fig. 3C)
PMID:27334362	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 3C)
PMID:27334362	FYPO:0005554	abolished histone H3-K9 dimethylation at centromere inner repeat during vegetative growth	(Fig. 3C)
PMID:27334362	FYPO:0004745	abolished histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 3C)
PMID:27334362	FYPO:0005554	abolished histone H3-K9 dimethylation at centromere inner repeat during vegetative growth	(Fig. 3C)
PMID:27334362	FYPO:0000878	decreased histone H3-K9 dimethylation at centromere inner repeat during vegetative growth	(Fig. 3C)
PMID:27334362	FYPO:0004314	normal protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC1105.11c	(Fig. 3D)
PMID:27334362	FYPO:0004314	normal protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPAC1834.04	(Fig. 3D)
PMID:27334362	FYPO:0004314	normal protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPBC8D2.04	(Fig. 3D)
PMID:27334362	FYPO:0001357	normal vegetative cell population growth	(Fig. 6b)
PMID:27334362	FYPO:0000887	increased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 7B)
PMID:27334362	FYPO:0000887	increased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 7B)
PMID:27334362	FYPO:0001839	normal minichromosome loss	(Fig. 8B; Table B)
PMID:27334362	FYPO:0005371	increased linear minichromosome loss during vegetative growth [has_penetrance] 7.4	(Fig. 8B; Table B)
PMID:27334362	FYPO:0005371	increased linear minichromosome loss during vegetative growth [has_penetrance] 13.7	(Fig. 8B; Table B)
PMID:27334362	FYPO:0002430	inviable after spore germination, multiple cell divisions	(Fig. 9A)
PMID:27334362	FYPO:0002060	viable vegetative cell population	(Fig. 9D)
PMID:27334362	FYPO:0002060	viable vegetative cell population	(Fig. 9D)
PMID:27334362	FYPO:0002061	inviable vegetative cell population	(Fig. 9D)
PMID:27334362	FYPO:0002061	inviable vegetative cell population	(Fig. 9D)
PMID:27350684	FYPO:0001387	loss of viability at high temperature	(comment: CHECK conditional synthetic lethal with rna14-11)
PMID:27350684	FYPO:0003602	abolished mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC20F10.06	(comment: splicing of rad21, nda3 and mad2 is also affected)
PMID:27350684	FYPO:0003602	abolished mRNA splicing, via spliceosome [assayed_using] PomBase:SPCC1259.13	(comment: splicing of rad21, nda3 and mad2 is also affected)
PMID:27350684	FYPO:0003602	abolished mRNA splicing, via spliceosome [assayed_using] PomBase:SPCC338.17c	(comment: splicing of rad21, nda3 and mad2 is also affected)
PMID:27350684	FYPO:0003602	abolished mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC26H8.07c	(comment: splicing of rad21, nda3 and mad2 is also affected)
PMID:27365210	FYPO:0008147	decreased mRNA splicing, meiotic genes	Consistent with the meiotic defects, this shift did not occur efficiently in diploid homozygous pfal1 and red1 mutants, reflected by a decreased splicing index (Fig. 3).
PMID:27365210	FYPO:0008147	decreased mRNA splicing, meiotic genes	Consistent with the meiotic defects, this shift did not occur efficiently in diploid homozygous pfal1 and red1 mutants, reflected by a decreased splicing index (Fig. 3).
PMID:27365210	FYPO:0008147	decreased mRNA splicing, meiotic genes	Consistent with the meiotic defects, this shift did not occur efficiently in diploid homozygous pfal1 and red1 mutants, reflected by a decreased splicing index (Fig. 3).
PMID:27365210	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 99	Diploid pfal1Δ−/− cells show a decreased sporulation efficiency compared to wild-type cells (Fig. 2B). Less than 5% of pfal1Δ−/− cells sporulated, and ∼20% form misshapen asci on SPA medium (Fig. 2C), suggesting a meiotic defect.
PMID:27365210	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 95	Diploid red5-2 cells show severe sporulation defects, with <1% of cells producing asci.
PMID:27365210	GO:0030874	nucleolar chromatin	S. pombe, pFal1 localizes to chromatin-containing regions of the nucleus and is not restricted to the nucleolus.
PMID:27365210	GO:0000785	chromatin	S. pombe, pFal1 localizes to chromatin-containing regions of the nucleus and is not restricted to the nucleolus.
PMID:27365210	GO:0071030	nuclear mRNA surveillance of spliceosomal pre-mRNA splicing [happens_during] meiotic cell cycle phase	These results demonstrate that pFal1, Red5, and Red1 are required to generate spliced rec8+ mRNA during starvation-induced meiosis.
PMID:27365210	GO:0071030	nuclear mRNA surveillance of spliceosomal pre-mRNA splicing [happens_during] meiotic cell cycle phase	These results demonstrate that pFal1, Red5, and Red1 are required to generate spliced rec8+ mRNA during starvation-induced meiosis.
PMID:27365210	GO:0071030	nuclear mRNA surveillance of spliceosomal pre-mRNA splicing [happens_during] meiotic cell cycle phase	These results demonstrate that pFal1, Red5, and Red1 are required to generate spliced rec8+ mRNA during starvation-induced meiosis.
PMID:27365210	GO:0071030	nuclear mRNA surveillance of spliceosomal pre-mRNA splicing [happens_during] meiotic cell cycle phase	These results demonstrate that pFal1, Red5, and Red1 are required to generate spliced rec8+ mRNA during starvation-induced meiosis.
PMID:27365210	FYPO:0008147	decreased mRNA splicing, meiotic genes	Using qRT- PCR, we found a reduction in spliced meiotic transcripts of rec8+ in mnhΔ1−/− but not y14Δ−/− or rnps1Δ−/− (Fig. 5A)
PMID:27365210	GO:0035145	exon-exon junction complex	We also observed interactions of pFal1-Myc with Rnps1-GFP and Y14-HA (Fig. 4B,D).
PMID:27365210	GO:0035145	exon-exon junction complex	We also observed interactions of pFal1-Myc with Rnps1-GFP and Y14-HA (Fig. 4B,D).
PMID:27365210	GO:0035145	exon-exon junction complex	We can easily detect interaction between pFal1- Myc and Mnh1-FTP (Fig. 4A).
PMID:27365210	GO:0035145	exon-exon junction complex	We can easily detect interaction between pFal1- Myc and Mnh1-FTP (Fig. 4A).
PMID:27365210	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC27D7.13c [has_severity] medium	We chose to study mei4 + and ssm4 + transcripts because they both contain a DSR region (.........we observed an increase in mei4 + and ssm4 + transcripts during vegetative growth in cells containing red5-2 (Fig. 1D).
PMID:27365210	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC27D7.13c [has_severity] medium	We chose to study mei4 + and ssm4 + transcripts because they both contain a DSR region (.........we observed an increase in mei4 + and ssm4 + transcripts during vegetative growth in cells containing red5-2 (Fig. 1D).
PMID:27365210	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC32H8.11	We chose to study mei4 + and ssm4 + transcripts because they both contain a DSR region (.........we observed an increase in mei4 + and ssm4 + transcripts during vegetative growth in cells containing red5-2 (Fig. 1D).
PMID:27365210	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC27D7.13c [has_severity] low	We chose to study mei4 + and ssm4 + transcripts because they both contain a DSR region (.........we observed an increase in mei4 + and ssm4 + transcripts during vegetative growth in cells containing red5-2 (Fig. 1D).
PMID:27365210	FYPO:0001355	decreased vegetative cell population growth	While viable, pfal1Δ showed a strong growth defect at all three temperatures tested (Fig. 1A).
PMID:27365210	FYPO:0001355	decreased vegetative cell population growth	While viable, pfal1Δ showed a strong growth defect at all three temperatures tested (Fig. 1A).
PMID:27365210	FYPO:0001355	decreased vegetative cell population growth	While viable, pfal1Δ showed a strong growth defect at all three temperatures tested (Fig. 1A).
PMID:27365210	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 96	loss of mnh1 causes severe sporulation defects (Fig. 4F)
PMID:27365210	FYPO:0004937	decreased RNA level during meiosis I [assayed_transcript] PomBase:SPBC29A10.14	qRT-PCR results show a large increase in rec8+ transcript levels during meiosis in wild-type cells, but no increase in pfal1Δ and red5-2 mutants (Fig. 3A).
PMID:27365210	FYPO:0004937	decreased RNA level during meiosis I [assayed_transcript] PomBase:SPBC29A10.14	qRT-PCR results show a large increase in rec8+ transcript levels during meiosis in wild-type cells, but no increase in pfal1Δ and red5-2 mutants (Fig. 3A).
PMID:27385337	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPAC688.07c	(Fig. 3C)
PMID:27385337	FYPO:0001880	abolished protein localization to cell division site [assayed_using] PomBase:SPAC688.07c	(Fig. 3C)
PMID:27385337	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPAC688.07c	(Fig. 3C)
PMID:27385337	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPCC1281.01	(Fig. 5a)
PMID:27385337	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPCC1281.01	(Fig. 5a)
PMID:27385337	FYPO:0000650	increased septation index [has_severity] low	(Figure 1F)
PMID:27385337	FYPO:0002488	cell lysis [has_penetrance] >22	(Figure 3F)
PMID:27385337	FYPO:0002488	cell lysis [has_penetrance] >15	(Figure 3F)
PMID:27385337	FYPO:0002488	cell lysis [has_penetrance] 4	(Figure 3F)
PMID:27385337	FYPO:0002488	cell lysis [has_penetrance] >15	(Figure 3F)
PMID:27385337	FYPO:0002488	cell lysis [has_penetrance] 3	(Figure 3F)
PMID:27385337	FYPO:0002488	cell lysis [has_penetrance] 2	(Figure 3F)
PMID:27385337	FYPO:0002488	cell lysis [has_penetrance] >20	(Figure 3F)
PMID:27385337	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPBC23G7.08c	(Figure 4 G) (comment: localizes as a dot rather than a disk)
PMID:27385337	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPAC688.07c	(Figure 4F)
PMID:27385337	FYPO:0006502	abolished protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPBC23G7.08c	(Figure 4G)
PMID:27385337	FYPO:0002023	abnormal septum morphology during vegetative growth	(Figure 5D, Figure 6)
PMID:27385337	FYPO:0002023	abnormal septum morphology during vegetative growth	(Figure 5D,6)
PMID:27385337	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPAC688.07c	(Table 1)
PMID:27385337	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPAC688.07c	(Table 1)
PMID:27385337	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPAC688.07c	(Table 1)
PMID:27385337	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPAC688.07c [has_severity] low	(Table 1)
PMID:27385337	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPAC688.07c	(Table 1)
PMID:27385337	FYPO:0000836	increased protein level [assayed_using] PomBase:SPAC688.07c	(Table 1)
PMID:27385337	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPAC688.07c	(Table 1)
PMID:27385337	FYPO:0000836	increased protein level [assayed_using] PomBase:SPAC688.07c [has_severity] high	(Table 1)
PMID:27385337	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPAC688.07c	(Table 1)
PMID:27385337	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPAC688.07c [has_severity] low	(Table 1)
PMID:27385337	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPBC23G7.08c	Supplemental Figure S4B
PMID:27385337	FYPO:0000647	vegetative cell lysis [has_penetrance] complete	Supplemental Figure S4F and Table 2
PMID:27385337	FYPO:0001880	abolished protein localization to cell division site [assayed_using] PomBase:SPAC688.07c	Table 1, fig 3 C
PMID:27388936	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 5a)
PMID:27388936	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 5a)
PMID:27388936	FYPO:0005440	swollen elongated cell with enlarged nucleus	(Fig. 5b)
PMID:27388936	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 8a)
PMID:27388936	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 8a)
PMID:27388936	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 8c)
PMID:27388936	FYPO:0004056	decreased protein localization to nucleus, with protein mislocalized to cytoplasm [assayed_using] PomBase:SPAC26A3.08	(Fig. 8c)
PMID:27398807	FYPO:0000963	normal growth on hydroxyurea	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000085	sensitive to camptothecin [has_severity] high	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000088	sensitive to hydroxyurea	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000088	sensitive to hydroxyurea	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000088	sensitive to hydroxyurea	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0001357	normal vegetative cell population growth	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000963	normal growth on hydroxyurea	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0001357	normal vegetative cell population growth	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0001357	normal vegetative cell population growth	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0005629	increased cellular HMW SUMO conjugate level [has_severity] low	(comment: 30 degrees; semi-permissive for slx8-29)
PMID:27398807	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(comment: CONDITION 30 degrees C)
PMID:27398807	FYPO:0005629	increased cellular HMW SUMO conjugate level [has_severity] high	(comment: CONDITION 30 degrees C)
PMID:27398807	FYPO:0005620	increased SUMO chain length [has_severity] high	(comment: CONDITION 30 degrees C)
PMID:27398807	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(comment: CONDITION 30 degrees C)
PMID:27444384	GO:0051536	iron-sulfur cluster binding	(comment: through conserved cysteines)
PMID:27451393	GO:0005515	protein binding	(Fig. 1A)
PMID:27451393	GO:0005515	protein binding	(Fig. 1A)
PMID:27451393	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Fig. 1B, D, E)
PMID:27451393	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Fig. 1B, D, E)
PMID:27451393	GO:0061638	CENP-A containing chromatin	(Fig. 2, F and G)
PMID:27451393	GO:0061638	CENP-A containing chromatin	(Fig. 2B and C, Fig. 2D and E)
PMID:27451393	GO:0033553	rDNA heterochromatin	(Fig. 3A-D)
PMID:27451393	GO:0099115	chromosome, subtelomeric region	(Fig. 3A-D)
PMID:27451393	FYPO:0004604	decreased chromatin silencing at subtelomere	(Fig. 3E)
PMID:27451393	FYPO:0004604	decreased chromatin silencing at subtelomere	(Fig. 3E)
PMID:27451393	FYPO:0004312	abolished protein localization to CENP-A containing chromatin [assayed_using] PomBase:SPAC18G6.10	(Fig. 4A and B)
PMID:27451393	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth	(Fig. 5A)
PMID:27451393	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth	(Fig. 5A)
PMID:27451393	FYPO:0003011	increased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPCC622.16c	(Fig. 5C and D)
PMID:27451393	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPBC2D10.17	(Fig. 5C and D)
PMID:27451393	FYPO:0000091	sensitive to thiabendazole	(Fig. G)
PMID:27451393	FYPO:0000091	sensitive to thiabendazole	(Fig. G)
PMID:27451393	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_using] PomBase:SPAC18G6.10	(comment: DNS)
PMID:27451393	FYPO:0003109	abolished protein localization to telomere during vegetative growth [assayed_using] PomBase:SPAC18G6.10	(comment: DNS)
PMID:27538348	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	(Fig. 1)
PMID:27538348	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. 1)
PMID:27538348	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 1E)
PMID:27538348	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 1E)
PMID:27538348	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1F)
PMID:27538348	FYPO:0004604	decreased chromatin silencing at subtelomere [assayed_transcript] PomBase:SPAC212.11 [has_severity] high	(Fig. 1F)
PMID:27538348	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 1F)
PMID:27538348	FYPO:0004604	decreased chromatin silencing at subtelomere [assayed_transcript] PomBase:SPAC212.11 [has_severity] medium	(Fig. 1F)
PMID:27538348	FYPO:0006111	abolished histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth	(Fig. 1G)
PMID:27538348	FYPO:0004137	decreased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth [has_severity] low	(Fig. 1G)
PMID:27538348	FYPO:0002355	decreased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 1G)
PMID:27538348	FYPO:0006112	abolished histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth	(Fig. 1G)
PMID:27538348	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 2)
PMID:27538348	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 2)
PMID:27538348	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	(Fig. 2)
PMID:27538348	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 2)
PMID:27538348	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 2)
PMID:27538348	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] low	(Fig. 3A)
PMID:27538348	GO:0000792	heterochromatin [coincident_with] PomBase:SPAC5H10.06c	(Fig. 3B and 4B)
PMID:27538348	GO:0000792	heterochromatin [coincident_with] PomBase:SPBC428.08c	(Fig. 3B and 4B)
PMID:27538348	GO:0000792	heterochromatin [coincident_with] PomBase:SPCC11E10.08	(Fig. 3B and 4B)
PMID:27538348	GO:0000792	heterochromatin [coincident_with] PomBase:SPAC1250.04c	(Fig. 3B and 4B)
PMID:27538348	GO:0000792	heterochromatin [coincident_with] PomBase:SPCC1393.10	(Fig. 3B and 4B)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC6F12.09	(Fig. 3C)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPCC1739.03	(Fig. 3C)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPCC663.12	(Fig. 3C)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC13G7.07	(Fig. 3C)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPBC83.03c	(Fig. 3C)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1393.10 [has_severity] high	(Fig. 3C)
PMID:27538348	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC140.03	(Fig. 3C)
PMID:27538348	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC736.11	(Fig. 3C)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC18G6.02c	(Fig. 3C)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPCC188.13c	(Fig. 3C)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC428.08c [has_severity] medium	(Fig. 3C)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC11E10.08 [has_severity] medium	(Fig. 3C)
PMID:27538348	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC613.12c	(Fig. 3C)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPCC970.07c	(Fig. 3C)
PMID:27538348	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC6F12.09	(Fig. 3C)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC3A11.08	(Fig. 3C)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1393.10 [has_severity] high	(Fig. 3C)
PMID:27538348	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1739.03	(Fig. 3C)
PMID:27538348	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC663.12	(Fig. 3C)
PMID:27538348	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC140.03 [has_severity] low	(Fig. 3C)
PMID:27538348	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC13G7.07	(Fig. 3C)
PMID:27538348	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC736.11	(Fig. 3C)
PMID:27538348	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPBC83.03c	(Fig. 3C)
PMID:27538348	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC18G6.02c	(Fig. 3C)
PMID:27538348	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC188.13c	(Fig. 3C)
PMID:27538348	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC428.08c [has_severity] low	(Fig. 3C)
PMID:27538348	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC11E10.08	(Fig. 3C)
PMID:27538348	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC613.12c	(Fig. 3C)
PMID:27538348	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPCC970.07c	(Fig. 3C)
PMID:27538348	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC3A11.08	(Fig. 3C)
PMID:27538348	FYPO:0008245	normal protein localization to chromatin at gene promoter region [assayed_region] PomBase:SPBC428.08c [assayed_protein] PomBase:SPAC22E12.11c	(Fig. 4B)
PMID:27538348	FYPO:0007505	decreased protein localization to chromatin at promoter [assayed_region] PomBase:SPCC1393.10 [assayed_protein] PomBase:SPAC22E12.11c [has_severity] medium	(Fig. 4B)
PMID:27538348	FYPO:0008245	normal protein localization to chromatin at gene promoter region [assayed_region] PomBase:SPCC11E10.08 [assayed_protein] PomBase:SPAC22E12.11c	(Fig. 4B)
PMID:27538348	FYPO:0007505	decreased protein localization to chromatin at promoter [assayed_region] PomBase:SPCC1393.10 [has_severity] medium [assayed_protein] PomBase:SPAC3G9.07c	(Fig. 4C)
PMID:27538348	GO:0000792	heterochromatin [coincident_with] PomBase:SPCC1393.10	(Fig. 4C)
PMID:27538348	GO:0000792	heterochromatin [coincident_with] PomBase:SPBC428.08c	(Fig. 4C)
PMID:27538348	GO:0000792	heterochromatin [coincident_with] PomBase:SPCC11E10.08	(Fig. 4C)
PMID:27538348	FYPO:0007505	decreased protein localization to chromatin at promoter [assayed_region] PomBase:SPCC1393.10 [assayed_protein] PomBase:SPAC22E12.11c [has_severity] medium	(Fig. 4D)
PMID:27538348	FYPO:0008245	normal protein localization to chromatin at gene promoter region [assayed_region] PomBase:SPBC428.08c [assayed_protein] PomBase:SPAC22E12.11c	(Fig. 4D)
PMID:27538348	FYPO:0008245	normal protein localization to chromatin at gene promoter region [assayed_region] PomBase:SPCC11E10.08 [assayed_protein] PomBase:SPAC22E12.11c	(Fig. 4D)
PMID:27538348	FYPO:0007505	decreased protein localization to chromatin at promoter [assayed_region] PomBase:SPCC1393.10 [assayed_protein] PomBase:SPAC22E12.11c [has_severity] medium	(Fig. 4D)
PMID:27538348	FYPO:0007505	decreased protein localization to chromatin at promoter [assayed_region] PomBase:SPBC428.08c [assayed_protein] PomBase:SPAC22E12.11c [has_severity] medium	(Fig. 4D)
PMID:27538348	FYPO:0007505	decreased protein localization to chromatin at promoter [assayed_region] PomBase:SPCC11E10.08 [assayed_protein] PomBase:SPAC22E12.11c [has_severity] medium	(Fig. 4D)
PMID:27538348	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC428.08c	(Fig. 5A)
PMID:27538348	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC11E10.08	(Fig. 5A)
PMID:27538348	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC428.08c [has_severity] medium	(Fig. 5A)
PMID:27538348	FYPO:0001324	decreased protein level during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPCC11E10.08	(Fig. 5A)
PMID:27538348	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 5B and C)
PMID:27538348	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	(Fig. 5B and C)
PMID:27538348	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 5B and C)
PMID:27538348	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 5B and C)
PMID:27538348	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 5B and C)
PMID:27538348	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 5B and C)
PMID:27538348	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 5B and C)
PMID:27538348	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 5D)
PMID:27538348	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 5D)
PMID:27538348	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 5D)
PMID:27538348	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 5D)
PMID:27538348	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 5D)
PMID:27538348	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 5D)
PMID:27538348	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 5D)
PMID:27538348	GO:1990841	promoter-specific chromatin binding [part_of] positive regulation of transcription by RNA polymerase II	Set3 is targeted to the promoters of clr4+ and rik1+, probably through its PHD finger. Set3 promotes transcription of clr4+ and rik1+.
PMID:27548313	FYPO:0000141	abnormal mitotic sister chromatid segregation	(comment: Kenichi comment mitotic defects mitotic defects caused by 343.20 deletion)
PMID:27548313	FYPO:0000141	abnormal mitotic sister chromatid segregation	(comment: Kenichi comment mitotic defects mitotic defects caused by ace2 deletion)
PMID:27548313	FYPO:0000141	abnormal mitotic sister chromatid segregation	(comment: Kenichi comment mitotic defects mitotic defects caused by eng1 deletion)
PMID:27558664	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPCC965.07c	(comment: CHECK affecting gst2)
PMID:27558664	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPCC965.07c	(comment: CHECK affecting gst2)
PMID:27558664	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPCC965.07c	(comment: CHECK affecting gst2)
PMID:27558664	FYPO:0005685	decreased RNA level during cellular response to cadmium ion [assayed_using] PomBase:SPBC27.08c	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	FYPO:0005685	decreased RNA level during cellular response to cadmium ion [assayed_using] PomBase:SPBC27.08c	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	FYPO:0005685	decreased RNA level during cellular response to cadmium ion [assayed_using] PomBase:SPAC1782.11	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	FYPO:0005685	decreased RNA level during cellular response to cadmium ion [assayed_using] PomBase:SPBC36.04	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	FYPO:0005685	decreased RNA level during cellular response to cadmium ion [assayed_using] PomBase:SPBC27.08c	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	FYPO:0005685	decreased RNA level during cellular response to cadmium ion [assayed_using] PomBase:SPAC1782.11	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	FYPO:0005685	decreased RNA level during cellular response to cadmium ion [assayed_using] PomBase:SPBC36.04	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	FYPO:0005685	decreased RNA level during cellular response to cadmium ion [assayed_using] PomBase:SPBC36.04	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	FYPO:0005685	decreased RNA level during cellular response to cadmium ion [assayed_using] PomBase:SPAC1782.11	(comment: CHECK affecting sua1 affecting cys11 affecting met14)
PMID:27558664	GO:0019344	L-cysteine biosynthetic process	Cys2 is a serine O-acetyltransferase required for cysteine biosynthesis Functional profiling revealed that Cys2 is essential for As/Cd tolerance (Table S5). Cys2 has greatest sequence homology to homoserine O-acetyltransferases, predicting that it should be involved with methionine biosynthesis. However, as noted previously, Met6 is also predicted to be a homoserine O-acetyltransferase (Ma et al. 2007). S. cerevisiae homoserine O-acetyltransferase Met2 is significantly more similar to Met6 than Cys2 in S. pombe, suggesting that in S. pombe Met6 is more likely the authentic homoserine O-acetyltransferase (Figure 3). Furthermore, met6D mutants require methionine supplementation for growth on defined minimal medium whereas cys2D cells require cysteine supplementation (Ma et al. 2007). Thus our data showing that cys2D but not met6D cells are highly sensitive to As/Cd toxicity, as well as our data indicating that methionine biosynthesis is not required for cadmium or arsenic resistance, support the notion that Cys2 is actually a serine O-acetyltransferase that is specifically essential for cysteine biosynthesis (Figure 3).
PMID:27558664	GO:0160210	L-serine O-succinyltransferase activity [part_of] L-cysteine biosynthetic process	Cys2 is a serine O-acetyltransferase required for cysteine biosynthesis Functional profiling revealed that Cys2 is essential for As/Cd tolerance (Table S5). Cys2 has greatest sequence homology to homoserine O-acetyltransferases, predicting that it should be involved with methionine biosynthesis. However, as noted previously, Met6 is also predicted to be a homoserine O-acetyltransferase (Ma et al. 2007). S. cerevisiae homoserine O-acetyltransferase Met2 is significantly more similar to Met6 than Cys2 in S. pombe, suggesting that in S. pombe Met6 is more likely the authentic homoserine O-acetyltransferase (Figure 3). Furthermore, met6D mutants require methionine supplementation for growth on defined minimal medium whereas cys2D cells require cysteine supplementation (Ma et al. 2007). Thus our data showing that cys2D but not met6D cells are highly sensitive to As/Cd toxicity, as well as our data indicating that methionine biosynthesis is not required for cadmium or arsenic resistance, support the notion that Cys2 is actually a serine O-acetyltransferase that is specifically essential for cysteine biosynthesis (Figure 3).
PMID:27587357	FYPO:0002061	inviable vegetative cell population	(Fig. 1)
PMID:27587357	FYPO:0002482	inviable spheroid vegetative cell	(Fig. 1d)
PMID:27587357	FYPO:0003333	inviable lemon-shaped cell	(Fig. 1d)
PMID:27587357	FYPO:0003333	inviable lemon-shaped cell	(Fig. 3)
PMID:27587357	FYPO:0003333	inviable lemon-shaped cell	(Fig. 3)
PMID:27587357	FYPO:0002196	abnormal vegetative cell shape [has_penetrance] low	(Fig. 3)
PMID:27587357	FYPO:0002196	abnormal vegetative cell shape	(Fig. 3)
PMID:27587357	FYPO:0002196	abnormal vegetative cell shape	(Fig. 3)
PMID:27587357	FYPO:0002196	abnormal vegetative cell shape	(Fig. 3)
PMID:27587357	FYPO:0005760	increased cell-cell adhesion	(Fig. 3)
PMID:27587357	FYPO:0002196	abnormal vegetative cell shape	(Fig. 3)
PMID:27587357	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:27587357	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:27587357	FYPO:0005760	increased cell-cell adhesion	(Fig. 3)
PMID:27587357	FYPO:0006273	abnormal glycoprotein glycan structure in endoplasmic reticulum lumen	(comment: CHECK see ttps://github.com/pombase/fypo/issues/3152#issuecomment-340506554) A reduced UDP-glucose transport is a decreased transporter activity that produces an abnormal lower level of UDP-glucose in the endoplasmic reticulum lumen
PMID:27587357	GO:0006491	N-glycan processing	(comment: endoplasmic reticulum quality control of glycoprotein folding The quality control of glycoprotein folding is a process that facilitates glycoprotein folding and retains in the endoplasmic reticulum folding intermediates.)
PMID:27587357	GO:0005458	GDP-mannose transmembrane transporter activity	(comment: inferred from cell wall galactomannan defects)
PMID:27587357	GO:0005459	UDP-galactose transmembrane transporter activity [occurs_in] Golgi membrane	(comment: inferred from cell wall galactomannan defects)
PMID:27611590	FYPO:0005766	increased replication fork pausing at nucleosome-depleted regions	(comment: assayed Cdc20 recruitment)
PMID:27611590	FYPO:0005767	increased replication fork pausing at tRNA genes	(comment: assayed Cdc20 recruitment)
PMID:27611590	FYPO:0005768	increased replication fork pausing at rDNA	(comment: assayed Cdc20 recruitment)
PMID:27611590	FYPO:0005765	increased replication fork pausing at highly transcribed RNA polymerase II genes	(comment: assayed Cdc20 recruitment)
PMID:27613427	FYPO:0000271	sensitive to salt stress [has_severity] high	(Comment: condition: AA medium (Rose et al 1990 Methods in Yeast Genetics))
PMID:27613427	FYPO:0000081	sensitive to high osmolarity [has_severity] high	(comment: condition: AA medium (Rose et al 1990 Methods in Yeast Genetics))
PMID:27618268	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPCC1795.01c	((Figure S4C)). (comment: non kinetochore bound)
PMID:27618268	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPCC1322.12c [has_severity] high	(Fig. 1A)
PMID:27618268	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPCC1322.12c [has_severity] high	(Fig. 1A)
PMID:27618268	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPCC1322.12c [has_severity] medium	(Fig. 1A)
PMID:27618268	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPCC1322.12c [has_severity] medium	(Fig. 1A)
PMID:27618268	FYPO:0005300	decreased protein localization to kinetochore during mitotic spindle assembly checkpoint signaling [assayed_using] PomBase:SPCC1322.12c [has_severity] medium	(Fig. 1A)
PMID:27618268	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	(Fig. 1B)
PMID:27618268	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. 1B)
PMID:27618268	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. 1B)
PMID:27618268	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. 1B)
PMID:27618268	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. 1B)
PMID:27618268	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint	(Fig. 1B)
PMID:27618268	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] low	(Fig. 1D)
PMID:27618268	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] low	(Fig. 1D)
PMID:27618268	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] low	(Fig. 2D)
PMID:27618268	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC23H3.08c	(Fig. 2E)
PMID:27618268	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPCC1795.01c	(Fig. 3C)
PMID:27618268	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPBC3D6.04c	(Fig. 3C)
PMID:27618268	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPBC20F10.06	(Fig. 3C)
PMID:27618268	FYPO:0001269	abolished protein localization to kinetochore during vegetative growth [assayed_using] PomBase:SPAC23H3.08c	(Figure 2A)
PMID:27618268	FYPO:0004828	normal protein localization to nucleus during mitosis [assayed_using] PomBase:SPAC23H3.08c	(Figure 2A)
PMID:27618268	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC23H3.08c [assayed_using] PomBase:SPCC1322.12c	(Figure 2B)
PMID:27618268	FYPO:0000168	abnormal mitotic spindle assembly checkpoint	(Figure 2D)
PMID:27618268	FYPO:0000168	abnormal mitotic spindle assembly checkpoint	(Figure 2E) (comment: how is this abnormal? i got confused here)
PMID:27618268	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPBC20F10.06	(Figure S3E)
PMID:27618268	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPCC1795.01c	(Figure S3E)
PMID:27618268	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPBC3D6.04c	(Figure S3E)
PMID:27618268	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPBC3D6.04c	(Figures 4B, S4A)
PMID:27618268	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPBC20F10.06	(Figures 4B, S4A)
PMID:27618268	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPBC20F10.06	(Figures 4C, S4B). (comment: non kinetochore bound)
PMID:27618268	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPBC3D6.04c	(Figures 4C, S4B). (comment: non kinetochore bound)
PMID:27618268	GO:0004722	protein serine/threonine phosphatase activity [has_input] PomBase:SPCC1322.12c [part_of] deactivation of mitotic spindle assembly checkpoint	Together, these data indicate that Mph1 (Mps1) kinase and Dis2 (PP1) phosphatase antagonistically regulate the interaction of Mad1 and Mad2 with Bub1 in fission yeast, most likely through phosphorylation of the conserved central motif of Bub1.
PMID:27618268	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC1322.12c [part_of] mitotic spindle assembly checkpoint signaling [occurs_in] outer kinetochore [happens_during] mitotic metaphase	Together, these data indicate that Mph1 (Mps1) kinase and Dis2 (PP1) phosphatase antagonistically regulate the interaction of Mad1 and Mad2 with Bub1 in fission yeast, most likely through phosphorylation of the conserved central motif of Bub1.
PMID:27627185	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPAC3G9.09c [part_of] positive regulation of cytoplasmic translational initiation	((comment: unphosphorylated form of tif211) inhibited by stress-inducedphosphorylation of Ser51 in the a subunit of eIF2(tif211)
PMID:27627185	GO:0005085	guanyl-nucleotide exchange factor activity [part_of] cytoplasmic translational initiation [has_input] PomBase:SPAC3G9.09c	(comment: unphosphorylated form of tif211)
PMID:27630265	FYPO:0002061	inviable vegetative cell population	(Figure 1)
PMID:27630265	FYPO:0002060	viable vegetative cell population	(Figure 1)
PMID:27630265	FYPO:0001915	abolished prospore membrane formation [has_penetrance] high	(Figure 1, S1)
PMID:27630265	GO:0032120	ascospore-type prospore membrane formation	(Figure 1, S1)
PMID:27630265	GO:0090619	meiotic spindle pole [exists_during] meiotic anaphase I	(Figure 2)
PMID:27630265	GO:0005628	prospore membrane [exists_during] meiosis II cell cycle phase	(Figure 4, 5)
PMID:27630265	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Figure 4, 5, S4)
PMID:27630265	FYPO:0003542	abolished protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC9E9.07c	(Figure 5C, S4B)
PMID:27630265	GO:0090619	meiotic spindle pole [exists_during] meiotic anaphase I	(Figure 6, S6)
PMID:27630265	FYPO:0003542	abolished protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC18G6.03	(Figure 6A, S3)
PMID:27630265	FYPO:0003542	abolished protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC6G9.11	(Figure 6A, S3)
PMID:27630265	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Figure 8, S9)
PMID:27630265	GO:0051285	cell cortex of cell tip	(Figure 8A)
PMID:27630265	GO:0071341	medial cortical node	(Figure 8A)
PMID:27630265	GO:0005628	prospore membrane	(Figure 8A)
PMID:27630265	FYPO:0002557	decreased protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAC23C4.10	(Supplemental Figure S10A)
PMID:27630265	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPAC23C4.10	(Supplemental Figure S10A)
PMID:27630265	FYPO:0002772	decreased protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC23C4.10	(Supplemental Figure S10A)
PMID:27630265	FYPO:0005736	decreased prospore membrane formation [has_penetrance] high	(Supplemental Figure S11)
PMID:27630265	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC6G9.11	(Supplemental Figure S11B)
PMID:27630265	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC6G9.11	(Supplemental Figure S11B)
PMID:27630265	GO:1990896	protein localization to cell cortex of cell tip [has_input] PomBase:SPAC23C4.10	(comment: CHECK in vegetative cells) (Supplemental Figure S10)
PMID:27630265	FYPO:0005737	delayed onset of prospore membrane formation [has_penetrance] 38.2	(comment: CHECK initiation of forespore membrane delayed )(Figure 3, Table 2)
PMID:27630265	GO:0005628	prospore membrane [exists_during] meiotic metaphase II	(comment: from metaphase II to postmeiosis) (Figure 2)
PMID:27630265	GO:0005085	guanyl-nucleotide exchange factor activity	Sec2 interacted with specifically with GTP- bound forms of Ypt3 (Figure 7, Supplemental Figure S8).
PMID:27630265	GO:0090619	meiotic spindle pole [exists_during] meiosis II cell cycle phase	Supplemental Figure S11
PMID:27630265	GO:0032120	ascospore-type prospore membrane formation [happens_during] meiosis II cell cycle phase	Supplemental Figure S11
PMID:27630265	FYPO:0004609	spindle pole bodies present in increased numbers during meiosis	Supplemental Figure S12
PMID:27630265	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC18G6.03	Supplemental Figure S5A
PMID:27630265	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPCC1183.12	Supplemental Figure S5A
PMID:27630265	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC6G9.11	Supplemental Figure S5A
PMID:27648579	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC1105.11c [assayed_using] PomBase:SPBC428.08c	(comment: CHECK not increased (relative to wild type Hht3+/Clr4+) as with hht3-K9M alone)
PMID:27648579	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC1105.11c [assayed_using] PomBase:SPBC428.08c	(comment: CHECK not increased (relative to wild type Hht3+/Clr4+) as with hht3-K9M alone)
PMID:27648579	FYPO:0005848	abolished histone methyltransferase activity (H3-K9 specific) activity [assayed_enzyme] PomBase:SPBC428.08c	(comment: substrate: bulk histone octamers)
PMID:27648579	FYPO:0005847	decreased histone methyltransferase activity (H3-K9 specific) activity [assayed_enzyme] PomBase:SPBC428.08c	(comment: substrate: recombinant mono-nucleosomes)
PMID:27655872	GO:0000139	Golgi membrane	(Fig. 1E)
PMID:27655872	FYPO:0001245	sensitive to cobalt	(Fig. 2A)
PMID:27655872	FYPO:0002060	viable vegetative cell population [has_severity] high	(Fig. 2A)
PMID:27655872	FYPO:0002061	inviable vegetative cell population	(Fig. 2A)
PMID:27655872	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPBC19C2.09	"(Fig. 2B) ""Sre1 cleavage defect under low oxygen"""
PMID:27655872	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPBC19C2.09	"(Fig. 2B) ""Sre1 cleavage defect under low oxygen"""
PMID:27655872	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPBC19C2.09	(Fig. 2B, lanes 5-13)
PMID:27655872	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPBC19C2.09	(Fig. 2C)
PMID:27655872	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPBC19C2.09	(Fig. 2C)
PMID:27655872	FYPO:0001984	protein absent from cell during vegetative growth [assayed_using] PomBase:SPBC354.05c	(Fig. 2D, lane 3)
PMID:27655872	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPBC354.05c	(Fig. 2G, lanes 10- 12)
PMID:27655872	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPBC354.05c	(Fig. 2G, lanes 6-8)
PMID:27655872	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC354.05c [assayed_using] Sre2N	(Fig. 3A, lane 3)
PMID:27655872	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC354.05c [assayed_using] Sre2P	(Fig. 3A, lane 3)
PMID:27655872	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC354.05c [assayed_using] Sre2N	(Fig. 3A, lane 4) (comment: both cleavage products)
PMID:27655872	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC354.05c [assayed_using] Sre2P	(Fig. 3A, lane 4) both cleavage products
PMID:27655872	FYPO:0000836	increased protein level [assayed_using] PomBase:SPBC354.05c [assayed_using] Sre2P	(Fig. 3D)
PMID:27655872	FYPO:0000836	increased protein level [assayed_using] PomBase:SPBC354.05c [assayed_using] Sre2P	(Fig. 3D)
PMID:27655872	FYPO:0000836	increased protein level [assayed_using] PomBase:SPBC354.05c [assayed_using] Sre2P	(Fig. 3D)
PMID:27655872	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC354.05c [assayed_using] Sre2P	(Fig. 3D) compare lanes 3 and 4
PMID:27655872	FYPO:0000836	increased protein level [assayed_using] PomBase:SPBC354.05c [assayed_using] Sre2P	(Fig. 3D, compare lanes 3 and 4)
PMID:27655872	GO:0061630	ubiquitin protein ligase activity [has_input] PomBase:SPBC354.05c	(Fig. 3E, 3D)
PMID:27655872	GO:0061630	ubiquitin protein ligase activity [has_input] PomBase:SPBC19C2.09	(Fig. 3E, 3D)
PMID:27655872	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC354.05c [has_severity] high	(Fig. 5D, 5F) (comment: 4.5 fold) precursor)
PMID:27655872	FYPO:0001669	abolished protein processing during vegetative growth [assayed_substrate] PomBase:SPBC354.05c [assayed_using] Sre2P [assayed_enzyme] PomBase:SPCC790.03	(Fig. 5E and F)
PMID:27655872	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_substrate] PomBase:SPBC354.05c [assayed_enzyme] PomBase:SPBC947.10	(Fig. 5E,F) (comment: precursor)
PMID:27655872	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_substrate] PomBase:SPBC354.05c [assayed_enzyme] PomBase:SPBC947.10	(Fig. 5E,F) (comment: precursor)
PMID:27655872	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_substrate] PomBase:SPBC354.05c [assayed_enzyme] PomBase:SPBC947.10	(Fig. 5E,F) (comment: precursor)
PMID:27655872	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_substrate] PomBase:SPBC354.05c [assayed_enzyme] PomBase:SPBC947.10	(Fig. 5E,F) (comment: precursor)
PMID:27655872	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_substrate] PomBase:SPBC354.05c [assayed_using] Sre2P [assayed_enzyme] PomBase:SPBC947.10	(Fig. 5E,F) (comment: precursor)
PMID:27655872	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_substrate] PomBase:SPBC354.05c [assayed_enzyme] PomBase:SPBC947.10	(Fig. 5E,F) (comment: precursor)
PMID:27655872	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC1565.08 [assayed_using] PomBase:SPCC790.03	(Fig. 6B)
PMID:27655872	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC1565.08 [assayed_using] PomBase:SPCC790.03	(Fig. 6B)
PMID:27655872	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC1565.08 [assayed_using] PomBase:SPCC790.03	(Fig. 6B)
PMID:27655872	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC1565.08 [assayed_using] PomBase:SPCC790.03	(Fig. 6B)
PMID:27655872	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC1565.08 [assayed_using] PomBase:SPCC790.03	(Fig. 7A, lanes 4-6)
PMID:27655872	GO:0005515	protein binding	(Fig. 7A, lanes 4-6)
PMID:27655872	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPBC354.05c [assayed_using] Sre2N	(Fig. 8)
PMID:27655872	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPBC354.05c [assayed_using] Sre2N	(Fig. 8)
PMID:27655872	FYPO:0001245	sensitive to cobalt	(Fig. 8A)
PMID:27655872	FYPO:0001245	sensitive to cobalt	(Fig. 8A)
PMID:27655872	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPBC19C2.09	(Fig. 8C, 8D) Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27655872	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPBC19C2.09	(Fig. 8C, 8D) Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27655872	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPBC19C2.09	(Fig. 8C, 8D) Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27655872	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPBC19C2.09	(Fig. 8C, 8D) Western blot analysis show Sre1 cleavage defect under low oxygen
PMID:27655872	FYPO:0001422	decreased protein processing during vegetative growth	(Fig. 8C, 8D) Western blot analysis show decreased Sre1 cleavage activation under low oxygen
PMID:27655872	FYPO:0000836	increased protein level [assayed_using] PomBase:SPBC19C2.09 [assayed_using] Sre2P	(Fig. 9A)
PMID:27655872	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPBC19C2.09	(Fig. 9A)
PMID:27655872	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPBC19C2.09	(Fig. 9A)
PMID:27655872	FYPO:0001668	normal protein processing during vegetative growth [assayed_using] PomBase:SPBC19C2.09	(Fig. 9A)
PMID:27655872	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC354.05c	(Figure 3E) precursor
PMID:27655872	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_substrate] PomBase:SPBC354.05c [assayed_enzyme] PomBase:SPBC947.10	PRECURSOR Fig 5E and F
PMID:27664110	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1b) severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	FYPO:0002009	decreased oxygen consumption during vegetative growth	(Fig. 1c)
PMID:27664110	FYPO:0003769	decreased cellular mtDNA level [has_severity] high	(Fig. 2)
PMID:27664110	FYPO:0003810	small fragmented mitochondria present in increased numbers	(Fig. 2)
PMID:27664110	FYPO:0000256	mutator	(Fig. 3)
PMID:27664110	FYPO:0000078	abnormal cellular respiration	(Fig. 3)
PMID:27664110	FYPO:0003004	increased cellular reactive oxygen species level during vegetative growth	(Fig. 3)
PMID:27664110	FYPO:0000256	mutator	(comment: text)
PMID:27664110	FYPO:0000256	mutator	(comment: text)
PMID:27664110	FYPO:0000256	mutator	(comment: text)
PMID:27664110	FYPO:0003805	decreased cell population growth on non-fermentable carbon source [has_severity] high	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	FYPO:0000442	decreased cell population growth on glycerol/ethanol carbon source [has_severity] high	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] high	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] high	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	FYPO:0000442	decreased cell population growth on glycerol/ethanol carbon source [has_severity] high	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] high	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664110	FYPO:0000442	decreased cell population growth on glycerol/ethanol carbon source [has_severity] high	severe growth delay on both fermentable (Glucose) and respiratory (Ethanol Glycerol) media at the restrictive temperature, while it behaved like the wild-type at permissive temperature
PMID:27664222	FYPO:0002693	resistance to diamide	(Figure 2A)
PMID:27664222	FYPO:0000763	resistance to cadmium	(Figure 2A)
PMID:27664222	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC926.04c [happens_during] cellular response to oxidative stress	(Figure 3A)
PMID:27664222	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC23D3.12 [happens_during] cellular response to oxidative stress	(Figure 3A)
PMID:27664222	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1347.14c [happens_during] cellular response to oxidative stress	(Figure 3A)
PMID:27664222	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1347.11 [happens_during] cellular response to oxidative stress	(Figure 3A)
PMID:27664222	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC36.02c [happens_during] cellular response to oxidative stress	(Figure 3A)
PMID:27664222	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1B3.03c [happens_during] cellular response to oxidative stress	(Figure 3A)
PMID:27664222	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	(Figure 3A)
PMID:27664222	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC1739.13 [happens_during] cellular response to oxidative stress	(Figure 3A)
PMID:27664222	GO:0005634	nucleus [exists_during] cellular response to diamide	(Figure 5A)
PMID:27664222	GO:0005634	nucleus [exists_during] cellular response to oxidative stress	(Figure 5A)
PMID:27664222	GO:0005737	cytoplasm	(Figure 5A)
PMID:27664222	GO:0034599	cellular response to oxidative stress	(comment: CHECK detoxification of thiol disulphide (in response to disulphide stress))
PMID:27664222	GO:0034599	cellular response to oxidative stress	(comment: CHECK detoxification of thiol disulphide (in response to disulphide stress))
PMID:27664222	FYPO:0006349	abolished protein localization to chromatin at promoter [assayed_using] PomBase:SPAC1783.07c	(comment: diamide-induced promoters)
PMID:27664222	FYPO:0000096	sensitive to cadmium	Supplementary Figure S1B
PMID:27664222	FYPO:0000799	sensitive to diamide	Supplementary Figure S1B
PMID:27664222	FYPO:0000962	normal growth on hydrogen peroxide	Supplementary Figure S3A
PMID:27664222	FYPO:0001037	normal growth during cellular response to salt stress	Supplementary Figure S3A NaCl or KCl)
PMID:27664222	FYPO:0000726	sensitive to oxidative stress	subcategory of oxidative stress known as GSH or disulfide stress (4). Indeed, a lower GSH/GSSG ratio was found after treatment with diamide or Cd (Supplementary Figure S4) in WT and in the SPBC29A10.12Δ strain
PMID:27666591	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC36B7.08c [assayed_using] PomBase:SPBC11B10.10c	(Fig. 7F)
PMID:27666591	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC36B7.08c [assayed_using] PomBase:SPCC1672.10 [has_severity] high	(Fig. 7e)
PMID:27666591	FYPO:0005887	ectopic CENP-A containing chromatin assembly [has_penetrance] 12	(Figure 1A, S1C-S1E)
PMID:27666591	FYPO:0005887	ectopic CENP-A containing chromatin assembly [has_penetrance] 12	(Figure 1B, Figure S1F)
PMID:27666591	FYPO:0005887	ectopic CENP-A containing chromatin assembly	(Figure 1B, Figure S1F)
PMID:27666591	FYPO:0003740	decreased CENP-A containing chromatin assembly [has_penetrance] 76	(Figure 2A)
PMID:27666591	FYPO:0005887	ectopic CENP-A containing chromatin assembly	(Figure 2D)
PMID:27666591	FYPO:0002061	inviable vegetative cell population	(Figure 3A)
PMID:27666591	FYPO:0003744	abolished protein localization to centromeric chromatin during vegetative growth [assayed_using] PomBase:SPBC36B7.08c	(Figure 4C)
PMID:27666591	FYPO:0002574	normal protein localization to centromere during vegetative growth [assayed_using] PomBase:SPCC1672.10	(Figure 4D)
PMID:27666591	FYPO:0005887	ectopic CENP-A containing chromatin assembly [has_penetrance] 14	(Figure 5A)
PMID:27666591	GO:0140898	CENP-A eviction from euchromatin	(Figure 5A)
PMID:27666591	GO:0140713	histone chaperone activity [has_input] PomBase:SPBC11B10.10c	(Figure 5B)
PMID:27666591	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Figure 5C)
PMID:27666591	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Figure 5C)
PMID:27666591	FYPO:0005887	ectopic CENP-A containing chromatin assembly [has_penetrance] 35	(Figure 5C)
PMID:27666591	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC36B7.08c [assayed_using] PomBase:SPBC36B7.08c	(Figure 7B)
PMID:27666591	FYPO:0000091	sensitive to thiabendazole	(Figure 7C)
PMID:27666591	FYPO:0005887	ectopic CENP-A containing chromatin assembly [has_penetrance] 12	(Figure 7D)
PMID:27666591	FYPO:0000091	sensitive to thiabendazole	(Figure S1F)
PMID:27666591	FYPO:0000228	lagging mitotic chromosomes	(Figure S1G)
PMID:27666591	FYPO:0005072	normal protein localization to centromeric chromatin [assayed_using] PomBase:SPBC36B7.08c	(Figure S5B)
PMID:27666591	FYPO:0001234	slow vegetative cell population growth	(Figures 1F and S2B)
PMID:27666591	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Figures 2B and 2C)
PMID:27666591	FYPO:0005888	decreased protein localization to centromeric chromatin, with protein mislocalized to nucleoplasm [assayed_using] PomBase:SPBC1105.17	(Figures 2D and S3B)
PMID:27666591	FYPO:0001870	normal centromere clustering at nuclear periphery during vegetative growth	(Figures S1A and S1B)
PMID:27666591	FYPO:0005887	ectopic CENP-A containing chromatin assembly [has_penetrance] 46	(Figures S2A and S2B)
PMID:27666591	GO:0061638	CENP-A containing chromatin [exists_during] mitotic interphase	(comment: VW: added exists_during..)
PMID:27666591	GO:0140898	CENP-A eviction from euchromatin	(comment: not sure if this is quite right)
PMID:27667686	GO:1902626	assembly of large subunit precursor of preribosome	Using Rbins to acutely inhibit or activate Midasin function, in parallel experiments with inhibitor-sensitive or inhibitor-resistant cells, we uncover Midasin's role in assembling Nsa1 particles, nucleolar precursors of the 60S subunit.
PMID:27687771	GO:0045944	positive regulation of transcription by RNA polymerase II	(comment: target genes: cut6, vht1, bio2)
PMID:27687866	FYPO:0000972	increased number of Rad52 foci during vegetative growth	(comment: CHECK acetaldehyde sensitivity)
PMID:27687866	FYPO:0000972	increased number of Rad52 foci during vegetative growth	(comment: CHECK acetaldehyde sensitivity)
PMID:27687866	FYPO:0000972	increased number of Rad52 foci during vegetative growth	(comment: acetaldehyde absent)
PMID:27697865	FYPO:0004236	thin mitotic spindle midzone	(Fig. 1A)
PMID:27697865	FYPO:0004438	long mitotic spindle during anaphase	(Fig. 4)
PMID:27697865	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Fig. 4E)
PMID:27697865	FYPO:0005976	increased rate of mitotic spindle elongation during anaphase B	(Fig. 5)
PMID:27697865	FYPO:0000274	increased duration of mitotic M phase	(Fig. 5c)
PMID:27697865	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. 5c)
PMID:27697865	FYPO:0006490	decreased duration of mitotic M phase [has_severity] low	(Fig. 6, 7)
PMID:27697865	FYPO:0001355	decreased vegetative cell population growth	(Fig. 6A)
PMID:27697865	FYPO:0001270	complete but unequal mitotic sister chromatid segregation [has_penetrance] 18	(Fig. 6E)
PMID:27697865	FYPO:0000228	lagging mitotic chromosomes	(Fig. 6E)
PMID:27697865	FYPO:0001270	complete but unequal mitotic sister chromatid segregation [has_penetrance] 25	(Fig. 6E)
PMID:27697865	FYPO:0006476	premature mitotic metaphase/anaphase transition	(Fig. S4)
PMID:27697865	FYPO:0001513	normal mitotic sister chromatid segregation	(comment: CHECK Fig.)
PMID:27697865	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(comment: vw: changed to increased activation, and D333A allele)
PMID:27736299	FYPO:0001492	viable elongated vegetative cell [has_severity] high	(Fig. 1) (comment: CHECK 10.81% longer than control mean)
PMID:27736299	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(Fig. 1) (comment: CHECK 10.86% shorter than control mean)
PMID:27736299	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(Fig. 1) (comment: CHECK 11.15% shorter than control mean)
PMID:27736299	FYPO:0001492	viable elongated vegetative cell [has_severity] high	(Fig. 1) (comment: CHECK 11.63% longer than control mean)
PMID:27736299	FYPO:0001492	viable elongated vegetative cell [has_severity] high	(Fig. 1) (comment: CHECK 14.43% longer than control mean)
PMID:27736299	FYPO:0001492	viable elongated vegetative cell [has_severity] high	(Fig. 1) (comment: CHECK 15.55% longer than control mean)
PMID:27736299	FYPO:0001492	viable elongated vegetative cell [has_severity] high	(Fig. 1) (comment: CHECK 15.82% longer than control mean)
PMID:27736299	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(Fig. 1) (comment: CHECK 16.50% shorter than control mean)
PMID:27736299	FYPO:0001492	viable elongated vegetative cell [has_severity] high	(Fig. 1) (comment: CHECK 16.78% longer than control mean)
PMID:27736299	FYPO:0001492	viable elongated vegetative cell [has_severity] high	(Fig. 1) (comment: CHECK 18.92% longer than control mean)
PMID:27736299	FYPO:0001492	viable elongated vegetative cell [has_severity] high	(Fig. 1) (comment: CHECK 19.29% longer than control mean)
PMID:27736299	FYPO:0001492	viable elongated vegetative cell [has_severity] high	(Fig. 1) (comment: CHECK 23.46% longer than control mean)
PMID:27736299	FYPO:0001492	viable elongated vegetative cell [has_penetrance] high	(Fig. 1) (comment: CHECK 31.94% longer than control mean)
PMID:27736299	FYPO:0001492	viable elongated vegetative cell [has_severity] medium	(Fig. 1) (comment: CHECK 8.74% longer than control mean)
PMID:27736299	FYPO:0001492	viable elongated vegetative cell [has_severity] medium	(Fig. 1) (comment: CHECK 8.78% longer than control mean)
PMID:27736299	FYPO:0001492	viable elongated vegetative cell [has_severity] medium	(Fig. 1) (comment: CHECK 8.80% longer than control mean)
PMID:27736299	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] medium	(Fig. 1) (comment: CHECK 9.10% shorter than control mean)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC11B10.09	(Fig. 3) (comment: CHECK Cdc2 level reduced to about 48% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC644.06c	(Fig. 3) (comment: CHECK Cdr1 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC6B12.15	(Fig. 3) (comment: CHECK Cpc2 level reduced to about 55% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC1198.02 [has_severity] medium	(Fig. 3) (comment: CHECK Dea2 level reduced to 50%)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC26A3.15c	(Fig. 3) (comment: CHECK Nsp1 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAP27G11.10c [has_severity] high	(Fig. 3) (comment: CHECK Nup184 level reduced to 30% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC290.03c	(Fig. 3) (comment: CHECK Nup186 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC1486.05	(Fig. 3) (comment: CHECK Nup189 level reduced to ~50% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC1620.11	(Fig. 3) (comment: CHECK Nup97 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC2F7.03c	(Fig. 3) (comment: CHECK Pom1 level reduced to ~55% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC16H5.07c	(Fig. 3) (comment: CHECK Ppa2 reduced to~45% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC1840.03	(Fig. 3) (comment: CHECK Sal3 level reduced to ~48% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC1734.14c	(Fig. 3) (comment: CHECK Suc1 level reduced to ~60% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC18B5.03	(Fig. 3) (comment: CHECK Wee1 level reduced to ~32% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC582.03	(Fig. 3) (comment: CHECK cdc13 level reduced to ~44% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC24H6.05	(Fig. 3) (comment: CHECK cdc25 level reduced to ~48% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27736299	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC22G7.09c	(Fig. 3) (comment: CHECK nup45 level reduced to ~45% decreased protein level in heterozygous diploid cell during vegetative growth)
PMID:27737912	FYPO:0000930	abolished protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPAC6G9.11	(Fig. 6)
PMID:27738016	FYPO:0000944	inviable spore with normal morphology [has_penetrance] 75	(Fig. S13) (comment; evidence: Tetrad dissection)
PMID:27738016	FYPO:0000944	inviable spore with normal morphology [has_penetrance] 75	(Fig. S13) (comment; evidence: Tetrad dissection)
PMID:27738016	FYPO:0000944	inviable spore with normal morphology [has_penetrance] 30	(Fig. S13) (comment; evidence: Tetrad dissection)
PMID:27738016	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. S15)
PMID:27738016	FYPO:0001234	slow vegetative cell population growth [has_severity] low	(Fig. S15)
PMID:27738016	FYPO:0000069	resistance to thiabendazole	(Fig. S6) (comment: condition: 15 ug/ml or 20 ug/ml thiabendazole)
PMID:27738016	FYPO:0000069	resistance to thiabendazole	(Fig. S6) (comment: condition: 15 ug/ml or 20 ug/ml thiabendazole)
PMID:27738016	FYPO:0000069	resistance to thiabendazole	(Fig. S6) (comment: condition: 15 ug/ml or 20 ug/ml thiabendazole)
PMID:27738016	FYPO:0000069	resistance to thiabendazole	(Fig. S6) (comment: condition: 15 ug/ml or 20 ug/ml thiabendazole)
PMID:27738016	FYPO:0000429	delayed G0 to G1 transition	(comment: CHECK G0-exit)
PMID:27738016	FYPO:0004710	increased number of Rad52 foci during G0 to G1 transition [has_penetrance] 50	(comment: CHECK Rad22-YFP, G0-exit)
PMID:27738016	FYPO:0000427	abnormal G1 to G0 transition [has_penetrance] low	(comment: CONDITION 24h G0)
PMID:27738016	FYPO:0006935	viable cell with normal cell morphology during nitrogen starvation	(comment: CONDITION 24h G0)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: CONDITION 24h G0)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: CONDITION 24h G0)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: CONDITION 24h G0)
PMID:27738016	FYPO:0000427	abnormal G1 to G0 transition [has_penetrance] low	(comment: CONDITION 24h G0)
PMID:27738016	FYPO:0000427	abnormal G1 to G0 transition [has_penetrance] low	(comment: CONDITION 24h G0)
PMID:27738016	FYPO:0000427	abnormal G1 to G0 transition [has_penetrance] low	(comment: CONDITION 24h G0)
PMID:27738016	FYPO:0000091	sensitive to thiabendazole	(comment: CONDITION: 15 ug/ml thiabendazole)
PMID:27738016	FYPO:0000091	sensitive to thiabendazole	(comment: CONDITION: 15 ug/ml thiabendazole)
PMID:27738016	FYPO:0000091	sensitive to thiabendazole	(comment: CONDITION: 15 ug/ml thiabendazole)
PMID:27738016	FYPO:0000091	sensitive to thiabendazole	(comment: CONDITION: 15 ug/ml thiabendazole)
PMID:27738016	FYPO:0000964	normal growth on thiabendazole	(comment: CONDITION: 15 ug/ml thiabendazole)
PMID:27738016	FYPO:0006518	loss of viability in G0 [has_severity] low	(comment: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: G0 viability assay)
PMID:27738016	FYPO:0006518	loss of viability in G0 [has_severity] low	(comment: G0 viability assay)
PMID:27738016	FYPO:0006518	loss of viability in G0 [has_severity] low	(comment: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: G0 viability assay)
PMID:27738016	FYPO:0006518	loss of viability in G0	(comment: G0 viability assay)
PMID:27738016	FYPO:0006660	loss of viability upon G0 to G1 transition	(comment: G0 viability assay)
PMID:27738016	FYPO:0006518	loss of viability in G0	(comment: G0 viability assay)
PMID:27738016	FYPO:0006660	loss of viability upon G0 to G1 transition	(comment: G0 viability assay)
PMID:27738016	FYPO:0000091	sensitive to thiabendazole	(comment: condition 15 ug/ml thiabendazole)
PMID:27738016	FYPO:0000091	sensitive to thiabendazole	(comment: condition: 15 ug/ml thiabendazole)
PMID:27738016	FYPO:0000091	sensitive to thiabendazole	(comment: condition: 15 ug/ml thiabendazole)
PMID:27738016	FYPO:0000091	sensitive to thiabendazole	(comment: condition: 15 ug/ml thiabendazole)
PMID:27738016	FYPO:0000091	sensitive to thiabendazole	(comment: condition: 15 ug/ml thiabendazole)
PMID:27738016	FYPO:0000091	sensitive to thiabendazole	(comment: condition: 15 ug/ml thiabendazole)
PMID:27738016	FYPO:0000091	sensitive to thiabendazole	(comment: condition: 15 ug/ml thiabendazole)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: condition: 24h G0)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: condition: 24h G0)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: condition: 24h G0)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: condition: 24h G0)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: condition: 24h G0)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: condition: 24h G0)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: condition: 24h G0)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: condition: 24h G0)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: condition: 24h G0)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: condition: 24h G0)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: condition: 24h G0)
PMID:27738016	FYPO:0007639	increased DNA damage at rDNA during G0	(comment: condition: 48 hours G0)
PMID:27738016	FYPO:0006079	increased chromatin silencing at rDNA [has_severity] high	(comment: condition: 48 hours G0)
PMID:27738016	FYPO:0007639	increased DNA damage at rDNA during G0	(comment: condition: 48 hours G0)
PMID:27738016	FYPO:0007639	increased DNA damage at rDNA during G0	(comment: condition: 48 hours G0)
PMID:27738016	FYPO:0007639	increased DNA damage at rDNA during G0	(comment: condition: 48 hours G0)
PMID:27738016	FYPO:0006079	increased chromatin silencing at rDNA	(comment: condition: 48 hours day G0)
PMID:27738016	FYPO:0006660	loss of viability upon G0 to G1 transition [has_severity] low	(comment: condition: G0 viability assay)
PMID:27738016	FYPO:0006660	loss of viability upon G0 to G1 transition [has_severity] low	(comment: condition: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: condition: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006660	loss of viability upon G0 to G1 transition	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006660	loss of viability upon G0 to G1 transition [has_severity] low	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006660	loss of viability upon G0 to G1 transition [has_severity] low	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006660	loss of viability upon G0 to G1 transition [has_severity] low	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006660	loss of viability upon G0 to G1 transition [has_severity] low	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006518	loss of viability in G0 [has_severity] low	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006518	loss of viability in G0 [has_severity] high	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006518	loss of viability in G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006518	loss of viability in G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006518	loss of viability in G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006660	loss of viability upon G0 to G1 transition [has_severity] low	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006660	loss of viability upon G0 to G1 transition	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006660	loss of viability upon G0 to G1 transition [has_severity] low	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006660	loss of viability upon G0 to G1 transition [has_severity] low	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0006518	loss of viability in G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0007629	normal viability during G0	(comment: evidence: G0 viability assay)
PMID:27738016	FYPO:0004817	decreased rDNA antisense small RNA level	(comment: evidence: small-RNA-seq)
PMID:27738016	FYPO:0002835	centromeric outer repeat transcript-derived siRNA absent	(comment: evidence: small-RNA-seq)
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	24h G0 cell microscopy
PMID:27738016	FYPO:0007553	normal G1 to G0 transition	24h G0 cell microscopy
PMID:27738016	GO:0070317	negative regulation of G0 to G1 transition	mutant defective in maintenance of quiescence
PMID:27738016	GO:0070317	negative regulation of G0 to G1 transition	mutant defective in maintenance of quiescence
PMID:27738016	GO:0070317	negative regulation of G0 to G1 transition	mutant defective in maintenance of quiescence
PMID:27746023	FYPO:0007451	normal protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(Figure 2C)
PMID:27746023	FYPO:0007451	normal protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPAC22H10.07	(Figure 2C)
PMID:27746023	FYPO:0007451	normal protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(Figure 2D)
PMID:27746023	FYPO:0007451	normal protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPAC22H10.07	(Figure S1B)
PMID:27746023	FYPO:0007451	normal protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(Figures 2A, S1A; Movie S1)
PMID:27746023	FYPO:0007451	normal protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(Figures S1C, S1D)
PMID:27746023	FYPO:0007451	normal protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	(Figures S1C, S1D)
PMID:27746023	FYPO:0000998	elongated cell during nitrogen starvation [assayed_using] PomBase:SPAC110.03	(comment: CHECK during nitrogen starvation). Although many mutants in the SAPK pathway have defects in mating and meiosis, this result may help to explain why sty1D and wis1D mutants in particular continue to elongate upon N starvation, unlike other mutants in the pathway
PMID:27746023	FYPO:0000646	swollen vegetative cell	(comment: arrested)
PMID:27746023	FYPO:0007527	increased protein localization to cell tip during nitrogen starvation [assayed_using] PomBase:SPAC110.03	Movie S4. Sty1 activity is critical for maintaining a non-polarized Cdc42 module in N-starved quiescent cells.
PMID:27746023	FYPO:0007451	normal protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03	Movie S4. Sty1 activity is critical for maintaining a non-polarized Cdc42 module in N-starved quiescent cells.
PMID:27746023	FYPO:0006634	increased vegetative cell length	unlike WT cell elongation continued after actin depolymerization, (Figures 2A and 2B; Movie S1) conclusions. 1. the SAPK pathway is required for CRIB dispersal after LatA treatment. 2 the actin cytoskeleton per se is not required for stability of the Cdc42 polarity module at cell tips. 3. cell elongation can occur in the complete absence of the actin cytoskeleton.
PMID:27746023	FYPO:0006634	increased vegetative cell length	unlike WT cell elongation continued after actin depolymerization, (Figures 2A and 2B; Movie S1) conclusions. 1. the SAPK pathway is required for CRIB dispersal after LatA treatment. 2 the actin cytoskeleton per se is not required for stability of the Cdc42 polarity module at cell tips. 3. cell elongation can occur in the complete absence of the actin cytoskeleton.
PMID:27811944	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC3B9.15c [assayed_using] PomBase:SPBC19C2.09	deletion of Sre1 aa 877-900 also destabilized Sre1 and prevented proteolytic activation
PMID:27811944	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC3B9.15c [assayed_using] PomBase:SPBC19C2.09	mutation destabilized Sre1 precursor and prevented Sre1 proteolytic cleavage
PMID:27811944	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC19C2.09 [assayed_using] PomBase:SPBC3B9.15c	mutation destabilized Sre1 precursor and prevented Sre1 proteolytic cleavage
PMID:27851962	GO:0030014	CCR4-NOT complex	(Figure 1)
PMID:27851962	GO:0030014	CCR4-NOT complex	(Figure 1)
PMID:27851962	GO:0030014	CCR4-NOT complex	(Figure 1)
PMID:27851962	GO:0030014	CCR4-NOT complex	(Figure 1)
PMID:27851962	GO:0030014	CCR4-NOT complex	(Figure 1)
PMID:27851962	GO:0030014	CCR4-NOT complex	(Figure 1)
PMID:27851962	GO:0030014	CCR4-NOT complex	(Figure 1)
PMID:27852900	FYPO:0006497	abnormal plasma membrane phosphatidylserine distribution [has_penetrance] high [has_severity] high	(Fig. 4) (comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27852900	FYPO:0006497	abnormal plasma membrane phosphatidylserine distribution [has_penetrance] high [has_severity] low	(Fig. 4) (comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27852900	FYPO:0006497	abnormal plasma membrane phosphatidylserine distribution [has_penetrance] high [has_severity] high	(Fig. 4B) (comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27852900	FYPO:0003771	decreased protein localization to plasma membrane of cell tip during vegetative growth [assayed_using] PomBase:SPAC110.03 [has_penetrance] low	(Fig. 7)
PMID:27852900	FYPO:0003771	decreased protein localization to plasma membrane of cell tip during vegetative growth [has_penetrance] medium [assayed_using] PomBase:SPAC1F7.04	(Fig. 7)
PMID:27852900	FYPO:0002106	viable stubby vegetative cell [has_penetrance] high	(Fig. 8a)
PMID:27852900	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high	(Fig. 8a)
PMID:27852900	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] high	(Fig. 8a)
PMID:27852900	FYPO:0004964	actin cortical patches present in decreased numbers	(Fig. 8d)
PMID:27852900	FYPO:0002297	dispersed actin cortical patch localization during mitotic interphase	(Fig. 8d)
PMID:27852900	FYPO:0006547	abnormal plasma membrane phosphatidylserine distribution resulting in decreased concentration at cell tip	(Figure 3, A and E)
PMID:27852900	FYPO:0006547	abnormal plasma membrane phosphatidylserine distribution resulting in decreased concentration at cell tip	(Figure 3, A and E)
PMID:27852900	FYPO:0004963	normal plasma membrane sterol distribution	(Figure 5D)
PMID:27852900	FYPO:0003150	decreased NETO [has_penetrance] 44	(Figure 8e)
PMID:27852900	FYPO:0006497	abnormal plasma membrane phosphatidylserine distribution [has_penetrance] high [has_severity] medium	(comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27852900	FYPO:0006497	abnormal plasma membrane phosphatidylserine distribution [has_penetrance] high [has_severity] medium	(comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27852900	FYPO:0006497	abnormal plasma membrane phosphatidylserine distribution [has_penetrance] high [has_severity] medium	(comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27852900	FYPO:0006497	abnormal plasma membrane phosphatidylserine distribution [has_penetrance] high [has_severity] low	(comment: GFP-LactC2 probe expressed from pREP3X)
PMID:27871365	GO:0003697	single-stranded DNA binding	(Fig. 3H)
PMID:27871365	GO:0003690	double-stranded DNA binding	(Fig. 3H)
PMID:27871365	GO:0006281	DNA repair	(comment: from later paper: We speculate that SPRTN is able to degrade DPCs to peptide adducts that are sufficiently small for efficient TLS. https://www.sciencedirect.com/science/article/pii/S1097276518309948)
PMID:27872152	GO:0005515	protein binding	(Fig. 2A) (Fig. 2B; Fig. S2B).
PMID:27872152	FYPO:0002061	inviable vegetative cell population	(Fig. 7B,C)
PMID:27872152	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 7D)
PMID:27872152	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 7D)
PMID:27872152	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 7D)
PMID:27872152	FYPO:0005976	increased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Fig. 7E)
PMID:27872152	FYPO:0001859	increased minichromosome loss [has_penetrance] 2	(comment: 2.0% versus <0.1%) (Fig. 7F)
PMID:27872152	GO:0008093	cytoskeletal anchor activity [occurs_in] microtubule plus-end	(comment: CHECK adaptor for dis1-microtubule)
PMID:27886462	FYPO:0000245	loss of viability in stationary phase	(Figure 1A)
PMID:27886462	FYPO:0000245	loss of viability in stationary phase	(Figure 1A)
PMID:27886462	FYPO:0001357	normal vegetative cell population growth	(Figure 1A)
PMID:27886462	FYPO:0001357	normal vegetative cell population growth	(Figure 1A)
PMID:27886462	FYPO:0001357	normal vegetative cell population growth	(Figure 1A)
PMID:27886462	FYPO:0000245	loss of viability in stationary phase	(Figure 1A)
PMID:27886462	FYPO:0000245	loss of viability in stationary phase	(Figure 1A)
PMID:27886462	FYPO:0000245	loss of viability in stationary phase	(Figure 1A)
PMID:27886462	FYPO:0001357	normal vegetative cell population growth	(Figure 1A)
PMID:27886462	FYPO:0005760	increased cell-cell adhesion	(Figure 1B)
PMID:27886462	FYPO:0005760	increased cell-cell adhesion	(Figure 1B)
PMID:27886462	FYPO:0005760	increased cell-cell adhesion	(Figure 1B)
PMID:27886462	FYPO:0005760	increased cell-cell adhesion	(Figure 1B)
PMID:27886462	FYPO:0003730	abolished cell population growth on galactose carbon source	(Figure 1C)
PMID:27886462	FYPO:0003730	abolished cell population growth on galactose carbon source	(Figure 1C)
PMID:27886462	FYPO:0003730	abolished cell population growth on galactose carbon source	(Figure 1C)
PMID:27886462	FYPO:0003730	abolished cell population growth on galactose carbon source	(Figure 1C)
PMID:27886462	FYPO:0003730	abolished cell population growth on galactose carbon source	(Figure 1C)
PMID:27886462	FYPO:0003730	abolished cell population growth on galactose carbon source	(Figure 1C)
PMID:27886462	FYPO:0003730	abolished cell population growth on galactose carbon source	(Figure 1C)
PMID:27886462	FYPO:0003730	abolished cell population growth on galactose carbon source	(Figure 1C)
PMID:27886462	FYPO:0001919	fragmented nucleus during vegetative growth [has_penetrance] high	(Figure 2A)
PMID:27886462	FYPO:0001919	fragmented nucleus during vegetative growth [has_penetrance] high	(Figure 2A)
PMID:27886462	FYPO:0001919	fragmented nucleus during vegetative growth [has_penetrance] high	(Figure 2A)
PMID:27886462	FYPO:0001919	fragmented nucleus during vegetative growth [has_penetrance] high	(Figure 2A)
PMID:27886462	FYPO:0003810	small fragmented mitochondria present in increased numbers [has_penetrance] high	(Figure 3A)
PMID:27886462	FYPO:0003810	small fragmented mitochondria present in increased numbers [has_penetrance] high	(Figure 3A)
PMID:27886462	FYPO:0003810	small fragmented mitochondria present in increased numbers [has_penetrance] high	(Figure 3A)
PMID:27886462	FYPO:0003810	small fragmented mitochondria present in increased numbers [has_penetrance] high	(Figure 3A)
PMID:27886462	FYPO:0003004	increased cellular reactive oxygen species level during vegetative growth	(Figure 3C)
PMID:27886462	FYPO:0003004	increased cellular reactive oxygen species level during vegetative growth	(Figure 3C)
PMID:27886462	FYPO:0003004	increased cellular reactive oxygen species level during vegetative growth [has_severity] high	(Figure 3C)
PMID:27886462	FYPO:0003004	increased cellular reactive oxygen species level during vegetative growth	(Figure 3C)
PMID:27886462	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC1F8.02c	(Figure 4)
PMID:27886462	FYPO:0005505	increased level of cell surface glycoprotein gene mRNA during vegetative growth [assayed_using] PomBase:SPAC977.07c	(Figure 4, Table 3)
PMID:27886462	FYPO:0005505	increased level of cell surface glycoprotein gene mRNA during vegetative growth [assayed_using] PomBase:SPAPB15E9.01c	(Figure 4, Table 3)
PMID:27886462	FYPO:0005505	increased level of cell surface glycoprotein gene mRNA during vegetative growth [assayed_using] PomBase:SPBC359.04c	(Figure 4, Table 3)
PMID:27886462	FYPO:0005505	increased level of cell surface glycoprotein gene mRNA during vegetative growth [assayed_using] PomBase:SPBC947.04	(Figure 4, Table 3)
PMID:27886462	FYPO:0005505	increased level of cell surface glycoprotein gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1F8.06	(Figure 4, Table 3)
PMID:27886462	FYPO:0005505	increased level of cell surface glycoprotein gene mRNA during vegetative growth [assayed_using] PomBase:SPCC1742.01	(Figure 4, Table 3)
PMID:27886462	FYPO:0005505	increased level of cell surface glycoprotein gene mRNA during vegetative growth [assayed_using] PomBase:SPAC186.01	(Figure 4, Table 3)
PMID:27886462	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPBC4F6.09	(Table 2)
PMID:27886462	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPAC23G3.03	(Table 2)
PMID:27886462	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPCC1020.03	(Table 2)
PMID:27886462	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC1683.10c	(Table 2)
PMID:27886462	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPBC947.05c	(Table 2)
PMID:27886462	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1F7.07c	(Table 2)
PMID:27886462	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPBC1683.09c	(Table 2)
PMID:27886462	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1F7.08	(Table 2)
PMID:27886462	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1F8.03c	(Table 2)
PMID:27886462	FYPO:0005826	decreased level of generation of precursor metabolites and energy gene mRNA during vegetative growth [assayed_using] PomBase:SPBP4H10.08	(Table 3)
PMID:27886462	FYPO:0005826	decreased level of generation of precursor metabolites and energy gene mRNA during vegetative growth [assayed_using] PomBase:SPBC16C6.08c	(Table 3)
PMID:27886462	FYPO:0005826	decreased level of generation of precursor metabolites and energy gene mRNA during vegetative growth [assayed_using] PomBase:SPCC1739.09c	(Table 3)
PMID:27886462	FYPO:0005826	decreased level of generation of precursor metabolites and energy gene mRNA during vegetative growth [assayed_using] PomBase:SPCC338.10c	(Table 3)
PMID:27886462	FYPO:0005826	decreased level of generation of precursor metabolites and energy gene mRNA during vegetative growth [assayed_using] PomBase:SPBC16H5.06	(Table 3)
PMID:27886462	FYPO:0005826	decreased level of generation of precursor metabolites and energy gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1B2.04	(Table 3)
PMID:27886462	FYPO:0005826	decreased level of generation of precursor metabolites and energy gene mRNA during vegetative growth [assayed_using] PomBase:SPBC29A3.18	(Table 3)
PMID:27886462	FYPO:0005826	decreased level of generation of precursor metabolites and energy gene mRNA during vegetative growth [assayed_using] PomBase:SPCC737.02c	(Table 3)
PMID:27886462	FYPO:0002664	increased level of stress responsive gene mRNA during vegetative growth [assayed_using] PomBase:SPACUNK4.16c	(Table 4)
PMID:27886462	FYPO:0002664	increased level of stress responsive gene mRNA during vegetative growth [assayed_using] PomBase:SPAC869.07c	(Table 4)
PMID:27886462	FYPO:0002664	increased level of stress responsive gene mRNA during vegetative growth [assayed_using] PomBase:SPBC660.07	(Table 4)
PMID:27886462	FYPO:0002664	increased level of stress responsive gene mRNA during vegetative growth [assayed_using] PomBase:SPAC328.03	(Table 4)
PMID:27886462	FYPO:0002664	increased level of stress responsive gene mRNA during vegetative growth [assayed_using] PomBase:SPAPB24D3.10c	(Table 4)
PMID:27889481	FYPO:0002061	inviable vegetative cell population	(Fig. 2c)
PMID:27889481	FYPO:0001234	slow vegetative cell population growth	(Fig. 2c)
PMID:27889481	FYPO:0002061	inviable vegetative cell population	(Fig. 2c)
PMID:27889481	FYPO:0002060	viable vegetative cell population	(Fig. 2c)
PMID:27889481	FYPO:0004367	normal mitotic spindle assembly [has_penetrance] 100	(Fig. 3D, E)
PMID:27889481	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase [has_penetrance] 80 [has_severity] low	(Fig. 3DE) sad1.2 cells often show extra Mis6-GFP foci unassociated with the SPB, even at permissive temperature
PMID:27889481	FYPO:0004093	normal meiotic telomere clustering [has_penetrance] 100	(Fig. 5C)
PMID:27889481	FYPO:0002060	viable vegetative cell population	(Fig. 6)
PMID:27889481	FYPO:0004367	normal mitotic spindle assembly	(Fig. 6)
PMID:27889481	FYPO:0006363	monopolar spindle during meiosis I	(Figure 1)
PMID:27889481	FYPO:0005736	decreased prospore membrane formation	(Figure 1)
PMID:27889481	FYPO:0007486	monopolar spindle during meiosis II	(Figure 1)
PMID:27889481	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Figure 1B)
PMID:27889481	GO:0035974	meiotic spindle pole body [exists_during] meiosis I cell cycle phase	(Figure 1B)
PMID:27889481	FYPO:0007081	abolished initial meiotic spindle pole body separation in meiosis I [has_penetrance] 24.5	(Figure 1C) In contrast, in the absence of the bouquet, the duplicated SPBs often fail to separate . Indeed, 75.5% of bqt1Δ cells with defective meiosis show problems in SPB separation at MI
PMID:27889481	FYPO:0007081	abolished initial meiotic spindle pole body separation in meiosis I [has_penetrance] 75.5	(Figure 1C) In contrast, in the absence of the bouquet, the duplicated SPBs often fail to separate. Indeed, 75.5% of bqt1Δ cells with defective meiosis show problems in SPB separation at MI
PMID:27889481	FYPO:0007487	abolished new meiotic spindle pole body insertion into nuclear envelope during meiosis II	(Figure 1C, 1F, 1G) We previously observed a tendency for the SPB to dissociate from the NE just prior to meiotic spindle formation in the bqt1Δ setting (Fennell et al., 2015; Tomita and Cooper, 2007); indeed, SPBs showing problems in separation typically appear to dislodge into the cytoplasm (Figure 1C, yellow arrowheads
PMID:27889481	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Figure 1D)
PMID:27889481	GO:0035974	meiotic spindle pole body [exists_during] meiosis I cell cycle phase	(Figure 1D)
PMID:27889481	FYPO:0007482	decreased protein localization to meiotic spindle pole body during meiosis I [assayed_using] PomBase:SPBC365.15 [has_penetrance] 59	(Figure 1E) In contrast, Alp4 localization is defective (ie one or both SPB signals lack any detectable Alp4 colocalization at MI onset) in 59% of bqt1Δ meiocytes (n= 100, p<0.01) from the onset of MI onwards
PMID:27889481	FYPO:0007080	abnormal initial meiotic spindle pole body separation in meiosis I [assayed_using] PomBase:SPBC365.15 [has_penetrance] 59	(Figure 1E) and all (n=50, p<0.01) those SPBs failing to recruit Alp4 show SPB separation problems and failed spindle nucleation (Figure 1E).
PMID:27889481	FYPO:0002772	decreased protein localization to meiotic spindle pole body [assayed_using] PomBase:SPBC12D12.01	(Figure 3A) Sad1.2-GFP remains stably associated with the SPB throughout interphase, in contrast to Sad1.1-GFP, which is destabilized at 36°C
PMID:27889481	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPBC12D12.01	(Figure 3A) Sad1.2-GFP remains stably associated with the SPB throughout interphase, in contrast to Sad1.1-GFP, which is destabilized at 36°C
PMID:27889481	FYPO:0001683	abolished mitotic spindle assembly [has_penetrance] 100	(Figure 3D, E)
PMID:27889481	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase [has_severity] high [has_penetrance] 80	(Figure 3D, E) At restrictive temperature, a population of sad1.2 cells emerges in which all three centromeres are clearly dissociated from the SPB
PMID:27889481	FYPO:0005380	normal mitotic spindle pole body duplication [has_penetrance] 100	(Figure 4B)
PMID:27889481	FYPO:0005640	abnormal meiotic centromere clustering with centromeres dissociated from spindle pole body [has_penetrance] 100	(Figure 5B) (comment: centromeres are also released from LINC in bouquet-defective cells)
PMID:27889481	FYPO:0004160	normal meiotic spindle	(Figure 5C) spindle formation occurs normally at both MI and MII in sad1.2 meiosis
PMID:27889481	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC18G6.10	(Figure S4B)
PMID:27889481	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC14C4.05c	(Figure S4B)
PMID:27889481	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPAC6G9.06c	(Figures 3B-C, S4A)
PMID:27889481	FYPO:0003541	normal protein localization to meiotic spindle pole body [assayed_using] PomBase:SPBC244.01c	(Figures 3B-C, S4A)
PMID:27889481	FYPO:0003569	abnormal mitotic spindle pole body insertion into nuclear envelope, with spindle pole body in cytoplasm [has_penetrance] 100	(Figures 4D-E, S5B, S5D) sad1.2 cells exhibiting total centromere dissociation not only fail to insert but also appear to separate from the NE, dislodging into the cytoplasm
PMID:27889481	FYPO:0000737	abnormal meiotic spindle assembly	(comment: CHECK abolished)
PMID:27889481	FYPO:0007485	abolished meiotic spindle microtubule nucleation from new spindle pole body during meiosis II [has_penetrance] 100	(comment: Figure) In 100% of the bqt1Δ cells that show monopolar spindles (n=11), those spindles are nucleated specifically from the old SPB (Figure S1I). Hence, failed spindle nucleation in the absence of the bouquet is specific to the new SPB.
PMID:27898700	FYPO:0002423	inviable after spore germination, without cell division, septated cells with abnormal cell shape [has_penetrance] complete	(Fig. 1A)
PMID:27898700	FYPO:0005469	inviable after spore germination, without cell division, lysed cell	(Fig. 1A) (comment: CHECK during cytokinesis)
PMID:27898700	FYPO:0002423	inviable after spore germination, without cell division, septated cells with abnormal cell shape	(Fig. 1B) (comment: CHECK swollen multiseptate elongated)
PMID:27898700	FYPO:0002107	inviable stubby vegetative cell [has_penetrance] 50	(Fig. 1C)
PMID:27898700	FYPO:0005869	inviable stubby multiseptate vegetative cell [has_penetrance] 8	(Fig. 1C)
PMID:27898700	FYPO:0002200	inviable stubby septated vegetative cell [has_penetrance] 50	(Fig. 1C)
PMID:27898700	FYPO:0001368	normal actomyosin contractile ring assembly	(Fig. 1F,G)
PMID:27898700	FYPO:0004653	delayed onset of actomyosin contractile ring contraction	(Fig. 1F,G)
PMID:27898700	FYPO:0001365	decreased rate of actomyosin contractile ring contraction	(Fig. 1F,G)
PMID:27898700	FYPO:0001369	mislocalized actomyosin contractile ring	(Fig. 1F,G) slides along axis from midpoint
PMID:27898700	FYPO:0005873	increased secondary cell septum thickness	(Fig. 2 A) (comment: 2x WT)
PMID:27898700	FYPO:0001035	increased cell wall thickness during vegetative growth	(Fig. 2 A) (comment: 3x WT)
PMID:27898700	FYPO:0005872	incomplete septum formed from asymmetrically located sites	(Fig. 2A)
PMID:27898700	FYPO:0005871	thin, incomplete primary cell septum	(Fig. 2A)
PMID:27898700	FYPO:0003205	decreased primary cell septum thickness	(Fig. 2A)
PMID:27898700	FYPO:0001585	abolished protein localization to cell tip during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBP22H7.03	(Fig. 4)
PMID:27898700	FYPO:0002719	decreased protein localization to septum [assayed_using] PomBase:SPBC19G7.05c [has_penetrance] high	(Fig. 4)
PMID:27898700	FYPO:0001585	abolished protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPBC19G7.05c	(Fig. 4)
PMID:27898700	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC19G7.05c	(Fig. 4)
PMID:27898700	FYPO:0001585	abolished protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPBP22H7.03	(Fig. 4)
PMID:27898700	FYPO:0001585	abolished protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPBC19G7.05c	(Fig. 4)
PMID:27898700	FYPO:0002719	decreased protein localization to septum [assayed_using] PomBase:SPBC19G7.05c [has_penetrance] high	(Fig. 4)
PMID:27898700	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPBP22H7.03	(Fig. S3B)
PMID:27898700	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPBP22H7.03	(Fig. S3B)
PMID:27898700	FYPO:0003627	normal protein localization [assayed_using] PomBase:SPBC19G7.05c [has_penetrance] high	(Fig. S4D, S4E)
PMID:27901072	FYPO:0006422	increased level of histone gene mRNA during mitotic S phase [assayed_using] PomBase:SPBC8D2.04	(Fig. 1d)
PMID:27901072	GO:0003712	transcription coregulator activity [has_input] PomBase:SPCC290.04	(Fig. 6)
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC8D2.04	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPCC622.09	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1834.04	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC8D2.03c	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPCC622.08c	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC1105.12	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1834.03c	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC1105.11c	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC8D2.04	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1834.04	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPCC622.09	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPCC622.08c	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC1105.12	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC8D2.03c	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1834.03c	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0004906	decreased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC1105.11c	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPCC622.08c	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPCC622.09	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1834.04	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC8D2.04	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC1105.11c	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1834.03c	(comment: asynchronous) fig 3a
PMID:27901072	FYPO:0006413	increased level of histone gene mRNA during vegetative growth [assayed_using] PomBase:SPBC1105.12	(comment: asynchronous) fig 3a
PMID:27902423	FYPO:0002061	inviable vegetative cell population	(comment: Promoter analysis)
PMID:27902423	FYPO:0001407	decreased cell population growth on glucose carbon source	(comment: Promoter analysis)
PMID:27902423	FYPO:0002061	inviable vegetative cell population	(comment: Promoter analysis)
PMID:27966061	FYPO:0005886	increased transcription from HSE promoter	(comment: indicates Hsf1 activation)
PMID:27984744	FYPO:0007629	normal viability during G0	(Fig. 1A)
PMID:27984744	FYPO:0006518	loss of viability in G0	(Fig. 1A)
PMID:27984744	FYPO:0006518	loss of viability in G0	(Fig. 1A)
PMID:27984744	FYPO:0006518	loss of viability in G0	(Fig. 1A)
PMID:27984744	FYPO:0006518	loss of viability in G0	(Fig. 1A)
PMID:27984744	FYPO:0007629	normal viability during G0	(Fig. 1A)
PMID:27984744	FYPO:0006518	loss of viability in G0	(Fig. 1B)
PMID:27984744	FYPO:0007629	normal viability during G0	(Fig. 1B)
PMID:27984744	FYPO:0006518	loss of viability in G0	(Fig. 1B)
PMID:27984744	FYPO:0007629	normal viability during G0	(Fig. 1B)
PMID:27984744	FYPO:0006518	loss of viability in G0	(Fig. 1B)
PMID:27984744	FYPO:0006518	loss of viability in G0	(Fig. 1B)
PMID:27984744	FYPO:0007468	increased histone H3-K9 dimethylation during G0 [assayed_region] PomBase:SPBC32H8.12c	(Fig. 2A, 2B)
PMID:27984744	FYPO:0007468	increased histone H3-K9 dimethylation during G0 [assayed_region] PomBase:SPBC32H8.12c	(Fig. 2E, 2F)
PMID:27984744	FYPO:0007468	increased histone H3-K9 dimethylation during G0 [assayed_region] PomBase:SPBC32H8.12c	(Fig. 2E, 2F)
PMID:27984744	FYPO:0007468	increased histone H3-K9 dimethylation during G0 [assayed_region] PomBase:SPBC32H8.12c	(Fig. 2E, 2F)
PMID:27984744	FYPO:0006518	loss of viability in G0	(Fig. S2)
PMID:27984744	FYPO:0004276	abnormal negative regulation of transcription during G0	(comment: ChIP-seq); Fig. 1C, 1D
PMID:28011631	GO:0140043	lipid droplet localization to prospore membrane leading edge	(Fig. 1F, Fig. 2C)
PMID:28011631	GO:0140043	lipid droplet localization to prospore membrane leading edge	(Fig. 1H, Fig. 3B)
PMID:28011631	FYPO:0000808	abnormal lipid droplet organization	(Fig. 2C)
PMID:28011631	FYPO:0006053	lipid droplets present in spore cytoplasm in decreased numbers, mislocalized to ascus epiplasm [has_penetrance] 50	(Fig. 2C) (comment: also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	FYPO:0006051	decreased lipid droplet localization to prospore membrane leading edge	(Fig. 2C) (comment: also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	FYPO:0006053	lipid droplets present in spore cytoplasm in decreased numbers, mislocalized to ascus epiplasm	(Fig. 2C) (comment: also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	GO:0140043	lipid droplet localization to prospore membrane leading edge	(Fig. 3B)
PMID:28011631	FYPO:0006053	lipid droplets present in spore cytoplasm in decreased numbers, mislocalized to ascus epiplasm	(Fig. 3B) (comment: also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	FYPO:0006054	decreased lipid droplet formation	(Fig. 3B) (comment: also in lantrunculin treated sceels indicating actin dependeny)
PMID:28011631	FYPO:0006003	normal cellular component organization	(Fig. 3B) normal lipid droplet localization to FSM leading edge
PMID:28011631	FYPO:0004993	normal spore germination frequency	(Fig. 4A)
PMID:28011631	FYPO:0000944	inviable spore with normal morphology [has_penetrance] 80	(Fig. 4A, 4C, and 4D) Using spore colony formation assay and microscopic observation, most of the dga1Δplh1Δ mutant spores failed to form colonies showed no sign of germination.
PMID:28011631	FYPO:0000581	decreased spore germination frequency [has_penetrance] 83	(Fig. 4A,C)
PMID:28011631	GO:0140042	lipid droplet formation	(Fig. 4B)
PMID:28011631	GO:0140042	lipid droplet formation	(Fig. 4B)
PMID:28011631	GO:0019915	lipid storage	(Fig. 4B) The dga1Δplh1Δ mutant possessed few lipid droplets.
PMID:28011631	GO:0019915	lipid storage	(Fig. 4B) The dga1Δplh1Δ mutant possessed few lipid droplets.
PMID:28011631	GO:0030476	ascospore wall assembly	(Fig. 4F) Assembly of Isp3-GFP onto the spore surface was defective in the dga1Δplh1Δ mutant.
PMID:28011631	FYPO:0004925	irregular ascospore wall	(Fig. 4F) Isp3-GFP was improperly assembled in the dga1Δplh1Δ mutant.
PMID:28011631	GO:0005811	lipid droplet [exists_during] meiosis II cell cycle phase	(Figure S2)
PMID:28011631	GO:0005811	lipid droplet [exists_during] meiosis I cell cycle phase	(Figure S2)
PMID:28011631	FYPO:0006051	decreased lipid droplet localization to prospore membrane leading edge	(Figure S3) LP clustering at nucleus
PMID:28017606	FYPO:0007437	constitutive activation of mitotic spindle assembly checkpoint [has_severity] medium	(Figures 1D and 1E) / ectopic. show a very striking result: co-expression of TetR-Spc7-9TE with TetR-D(1-302)Mph1 was sufficient to arrest cells in mitosis.
PMID:28017606	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint [assayed_using] PomBase:SPBC20F10.06	136 amino acids of Mad1 containing a coiled-coil region (CC) were removed, preventing Mad1-Mad2 interaction with Mlps and the nuclear envelope and also removing the Cut7 interaction site. These mad1-DCC cells were also able to arrest efficiently when TetR-Spc7-9TE and TetR-D(1-302)Mph1 were co-expressed (Figure 3E). We conclude that the Mad and Bub proteins do not need to be enriched at kinetochores, spindle poles, or the nuclear periphery for a robust checkpoint arrest to be generated in fission yeast. Most likely a diffuse, soluble pool of Spc7
PMID:28017606	FYPO:0007437	constitutive activation of mitotic spindle assembly checkpoint [has_severity] high	Spc7-wt arrested significantly faster than Spc7-9TE, with $60% mitotic arrest after 12 hr compared to 16 hr for Spc7-9TE.
PMID:28017606	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC20F10.06	Strains co-expressing Spc7 and Mph1 do not accumulate Mad2-GFP at spindle poles in strains containing the mad1-KAKA mutation that disrupts the Mad1-Cut7 kinesin motor interaction.
PMID:28017606	GO:0007094	mitotic spindle assembly checkpoint signaling	This demonstrates that the ‘‘activated’’ Spc7-9TE binding platform is sufficient to recruit these three checkpoint proteins constitutively, and that this works ectopically and thus does not require additional kinetochore factors. and Figure 1C. thus, we believe that this Spc7-Bub-Mad3 complex likely acts as an independent signaling module
PMID:28017606	FYPO:0007438	premature activation of mitotic spindle assembly checkpoint	advance (by ∼4 hr) in the timing of arrest in bub3DΔ cells arresting due to Spc7-9TE cells (although there is no effect with Spc7-wt, see Figure S4C).
PMID:28031482	GO:0000932	P-body	(Fig. 1D)
PMID:28031482	FYPO:0001895	P-bodies present in increased numbers	(Fig. 2B)
PMID:28031482	FYPO:0001896	enlarged P-bodies	(Fig. 4B,4D)
PMID:28031482	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC19G7.10c [assayed_using] PomBase:SPBC19G7.10c	(Fig. 4D)
PMID:28031482	FYPO:0006001	abolished protein localization to P-bodies [assayed_using] PomBase:SPBC19G7.10c	(Fig. 4H, right panel)
PMID:28031482	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC3D6.08c [assayed_using] PomBase:SPBC19G7.10c	(Fig. 5A)
PMID:28031482	FYPO:0000784	protein mislocalized to nucleus during vegetative growth [assayed_using] PomBase:SPBC3D6.08c [has_severity] high	(Fig. 5B)
PMID:28031482	FYPO:0000784	protein mislocalized to nucleus during vegetative growth [assayed_using] PomBase:SPBC3D6.08c	(Fig. 5C)
PMID:28031482	FYPO:0006002	normal protein localization to P-bodies [assayed_using] PomBase:SPBC19G7.10c	(Fig. 5D)
PMID:28031482	GO:0005737	cytoplasm	(Fig. 5G, left panel)
PMID:28031482	FYPO:0000784	protein mislocalized to nucleus during vegetative growth	(Fig. 5G, left panel)
PMID:28031482	FYPO:0000784	protein mislocalized to nucleus during vegetative growth [assayed_using] PomBase:SPBC3D6.08c [has_severity] low	(Fig. 5G, left panel)
PMID:28031482	FYPO:0005995	increased lncRNA level [has_severity] low [assayed_using] PomBase:SPNCRNA.1706	(Fig. 6C)
PMID:28031482	FYPO:0005995	increased lncRNA level [has_severity] low [assayed_using] PomBase:SPNCRNA.1705	(Fig. 6C)
PMID:28031482	FYPO:0005995	increased lncRNA level [has_severity] low [assayed_using] PomBase:SPNCRNA.1703	(Fig. 6C)
PMID:28031482	FYPO:0005995	increased lncRNA level [has_severity] low [assayed_using] PomBase:SPNCRNA.5748	(Fig. 6C)
PMID:28031482	FYPO:0005995	increased lncRNA level [has_severity] low [assayed_using] PomBase:SPNCRNA.1708	(Fig. 6C)
PMID:28031482	FYPO:0005995	increased lncRNA level [has_severity] low [assayed_using] PomBase:SPNCRNA.1702	(Fig. 6C)
PMID:28031482	FYPO:0005995	increased lncRNA level [has_severity] low [assayed_using] PomBase:SPNCRNA.1701	(Fig. 6C)
PMID:28031482	FYPO:0005995	increased lncRNA level [has_severity] low [assayed_using] PomBase:SPNCRNA.1704	(Fig. 6C)
PMID:28031482	FYPO:0002067	slow cell population growth during recovery from stationary phase [has_severity] low	(Fig. 6D)
PMID:28031482	FYPO:0001234	slow vegetative cell population growth [has_severity] low	(Fig. 6D)
PMID:28031482	FYPO:0001234	slow vegetative cell population growth [has_severity] low	(Fig. 6D)
PMID:28031482	FYPO:0001234	slow vegetative cell population growth	(Fig. 6D)
PMID:28031482	FYPO:0001234	slow vegetative cell population growth	(Fig. 6D)
PMID:28031482	FYPO:0001234	slow vegetative cell population growth	(Fig. 6D)
PMID:28031482	FYPO:0002067	slow cell population growth during recovery from stationary phase [has_severity] low	(Fig. 6D)
PMID:28031482	FYPO:0002067	slow cell population growth during recovery from stationary phase [has_severity] low	(Fig. 6D)
PMID:28031482	FYPO:0002067	slow cell population growth during recovery from stationary phase [has_severity] low	(Fig. 6D)
PMID:28031482	FYPO:0002067	slow cell population growth during recovery from stationary phase [has_severity] low	(Fig. 6D)
PMID:28031482	FYPO:0005992	decreased protein localization to P-bodies [assayed_using] PomBase:SPBC19G7.10c	(Figure 1D)
PMID:28031482	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC18E5.11c [assayed_using] PomBase:SPBC19G7.10c	(Figure 1E)
PMID:28031482	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC19A8.12 [assayed_using] PomBase:SPBC19G7.10c	(Figure 1E)
PMID:28031482	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC20G4.08 [assayed_using] PomBase:SPBC19G7.10c	(Figure 1E)
PMID:28031482	FYPO:0002041	abolished deadenylation-independent decapping of nuclear-transcribed mRNA [assayed_using] PomBase:SPAC23C11.02c	(Figure 2B)
PMID:28031482	FYPO:0005994	normal mRNA deadenylation [assayed_using] PomBase:SPAC23C11.02c	(Figure 2D)
PMID:28031482	FYPO:0005993	normal cytoplasmic translation	(Figure 2D)
PMID:28031482	GO:0000932	P-body [exists_during] cellular response to glucose starvation	(Figure 6A)
PMID:28031482	FYPO:0005992	decreased protein localization to P-bodies [assayed_using] PomBase:SPCC31H12.08c	(Figure 6C)
PMID:28031482	FYPO:0005992	decreased protein localization to P-bodies [assayed_using] PomBase:SPCC31H12.08c	(Figure 6C)
PMID:28031482	FYPO:0002061	inviable vegetative cell population	(Figure 7A)
PMID:28031482	GO:0000290	deadenylation-dependent decapping of nuclear-transcribed mRNA	pdc2 is required for mRNA decapping. Fig. 2A 2B
PMID:28103117	MOD:00696	phosphorylated residue [present_during] mitotic G2 phase	(Fig. 2a)
PMID:28103117	MOD:00696	phosphorylated residue [present_during] mitotic M phase	(Fig. 2a)
PMID:28103117	MOD:00696	phosphorylated residue [present_during] mitotic metaphase	(Fig. 2a)
PMID:28103117	MOD:00696	phosphorylated residue [present_during] mitotic anaphase	(Fig. 2a)
PMID:28103117	MOD:00696	phosphorylated residue [present_during] mitotic M phase	(Fig. 2a)
PMID:28103117	MOD:00696	phosphorylated residue [increased_during] mitotic metaphase	(Fig. 2a)
PMID:28103117	MOD:00696	phosphorylated residue [increased_during] mitotic prophase	(Fig. 2a) For example, in the second cell cycle, Wee1 phosphorylation was initiated at the end of G2 (180 minutes) and reached a maximum level at metaphase (200 minutes), just before Cdc13 degradation in anaphase (220 minutes).
PMID:28103117	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC24H6.05	(Fig. 3a) (comment: Cdk1 consensus sites)
PMID:28103117	FYPO:0005955	increased duration of mitotic cell cycle	(comment: The cell cycle was 20 min longer in clp1D cells compared with wild type cells.)
PMID:28103117	FYPO:0005957	decreased protein dephosphorylation during vegetative growth [assayed_using] PomBase:SPAC24H6.05	changes in phosphorylation level Figs. 5A, B and S2)
PMID:28103117	FYPO:0005957	decreased protein dephosphorylation during vegetative growth [assayed_using] PomBase:SPCC18B5.03	changes in phosphorylation level Figs. 5A, B and S2)
PMID:28103117	FYPO:0005957	decreased protein dephosphorylation during vegetative growth [assayed_using] PomBase:SPCC18B5.03	changes in phosphrylation level fig4 Wee1 to remain in the partially phosphorylated form throughout the cell cycle (Fig. S2)
PMID:28103117	FYPO:0005957	decreased protein dephosphorylation during vegetative growth [assayed_using] PomBase:SPAC24H6.05	changes in phosphrylation level fig4 Wee1 to remain in the partially phosphorylated form throughout the cell cycle (Fig. S2)
PMID:28160081	FYPO:0000245	loss of viability in stationary phase	(Fig. 2A)
PMID:28160081	FYPO:0000245	loss of viability in stationary phase	(Fig. 2A)
PMID:28160081	FYPO:0000245	loss of viability in stationary phase	(Fig. 2A)
PMID:28160081	FYPO:0000245	loss of viability in stationary phase	(Fig. 2A)
PMID:28160081	FYPO:0006331	decreased mating efficiency during stationary phase	(Fig. 2B)
PMID:28160081	FYPO:0006333	decreased zinc ion binding	(Fig. 2B)
PMID:28160081	FYPO:0006331	decreased mating efficiency during stationary phase	(Fig. 2B)
PMID:28160081	FYPO:0006331	decreased mating efficiency during stationary phase	(Fig. 2B)
PMID:28160081	FYPO:0006331	decreased mating efficiency during stationary phase	(Fig. 2B)
PMID:28160081	FYPO:0001309	increased viability in stationary phase	(Fig. 4c)
PMID:28160081	FYPO:0000245	loss of viability in stationary phase	(Fig. 5)
PMID:28178520	GO:1990023	mitotic spindle midzone [exists_during] mitotic anaphase B	(Fig. 1)
PMID:28178520	GO:1990023	mitotic spindle midzone [exists_during] mitotic anaphase B	(Fig. 1) (comment: requires Clp1 activity)
PMID:28178520	GO:1990023	mitotic spindle midzone [exists_during] mitotic anaphase B	(Fig. 1) (comment: requires Klp9, Clp1 activity)
PMID:28178520	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B	(Fig. 3)
PMID:28178520	FYPO:0006646	normal duration of mitotic prometaphase	(Fig. 4A)
PMID:28178520	FYPO:0006646	normal duration of mitotic prometaphase	(Fig. 4A)
PMID:28178520	FYPO:0005684	increased duration of mitotic prometaphase	(Fig. 4A)
PMID:28178520	FYPO:0005684	increased duration of mitotic prometaphase	(Fig. 4A)
PMID:28178520	FYPO:0005683	increased duration of mitotic prophase	(Fig. 4A)
PMID:28178520	FYPO:0006257	normal duration of mitotic prophase	(Fig. 4A)
PMID:28178520	FYPO:0006257	normal duration of mitotic prophase	(Fig. 4A)
PMID:28178520	FYPO:0006257	normal duration of mitotic prophase	(Fig. 4A)
PMID:28178520	FYPO:0005684	increased duration of mitotic prometaphase	(Fig. 4A)
PMID:28178520	FYPO:0006646	normal duration of mitotic prometaphase	(Fig. 4A)
PMID:28178520	FYPO:0005684	increased duration of mitotic prometaphase	(Fig. 4A)
PMID:28178520	FYPO:0005684	increased duration of mitotic prometaphase	(Fig. 4D)
PMID:28178520	FYPO:0006646	normal duration of mitotic prometaphase	(Fig. 4D)
PMID:28178520	FYPO:0005683	increased duration of mitotic prophase	(Fig. 4D)
PMID:28178520	FYPO:0004833	decreased protein localization to mitotic spindle midzone during anaphase B	(Fig. 4D)
PMID:28178520	FYPO:0006257	normal duration of mitotic prophase	(Fig. 4D)
PMID:28178520	FYPO:0005683	increased duration of mitotic prophase	(Fig. 4D)
PMID:28178520	FYPO:0005684	increased duration of mitotic prometaphase	(Fig. 4D)
PMID:28178520	FYPO:0005683	increased duration of mitotic prophase	(Fig. 5)
PMID:28178520	FYPO:0005684	increased duration of mitotic prometaphase	(Fig. 5)
PMID:28178520	FYPO:0006646	normal duration of mitotic prometaphase	(Fig. 5)
PMID:28178520	FYPO:0006257	normal duration of mitotic prophase	(Fig. 5)
PMID:28178520	FYPO:0006641	normal protein localization to kinetochore during mitotic metaphase [assayed_using] PomBase:SPCC962.02c	(Figure 1B and S1B,C)
PMID:28178520	FYPO:0004833	decreased protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPBC336.15	(Figure 1B and S1B,C)
PMID:28178520	FYPO:0004833	decreased protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPBC725.12	(Figure 1B and S1B,C)
PMID:28178520	FYPO:0004833	decreased protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPCC962.02c	(Figure 1B and S1B,C)
PMID:28178520	FYPO:0004833	decreased protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPCC320.13c	(Figure 1B and S1B,C)
PMID:28178520	FYPO:0006641	normal protein localization to kinetochore during mitotic metaphase [assayed_using] PomBase:SPCC320.13c	(Figure 1B and S1B,C)
PMID:28178520	FYPO:0006641	normal protein localization to kinetochore during mitotic metaphase [assayed_using] PomBase:SPBC725.12	(Figure 1B and S1B,C)
PMID:28178520	FYPO:0006641	normal protein localization to kinetochore during mitotic metaphase [assayed_using] PomBase:SPBC336.15	(Figure 1B and S1B,C)
PMID:28178520	FYPO:0004833	decreased protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPCC320.13c	(Figure 1B and S1B,C)
PMID:28178520	FYPO:0004833	decreased protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPBC15D4.01c	(Figure 1B and S1B,C)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPAPB1A10.09	(Figure 1B and S1B,C)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPAC3G9.12	(Figure 1B and S1B,C)
PMID:28178520	GO:0005515	protein binding [happens_during] mitotic anaphase B	(Figure 1C)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPAPB1A10.09	(Figure 1D)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPAC3G9.12	(Figure 1D)
PMID:28178520	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC320.13c [assayed_using] PomBase:SPBC15D4.01c	(Figure 1E)
PMID:28178520	FYPO:0004833	decreased protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPCC320.13c	(Figure 1H)
PMID:28178520	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC15D4.01c [assayed_using] PomBase:SPCC320.13c	(Figure 1I)
PMID:28178520	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC15D4.01c [assayed_using] PomBase:SPCC962.02c	(Figure 1I)
PMID:28178520	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] high	(Figure 2A)
PMID:28178520	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Figure 2A; Figure S3A)
PMID:28178520	FYPO:0005684	increased duration of mitotic prometaphase [has_severity] high	(Figure 2A; Figure S3A)
PMID:28178520	FYPO:0001513	normal mitotic sister chromatid segregation [assayed_using] PomBase:SPBC582.03	(Figure 2B)
PMID:28178520	FYPO:0000964	normal growth on thiabendazole [assayed_using] PomBase:SPBC582.03	(Figure 2B)
PMID:28178520	FYPO:0005684	increased duration of mitotic prometaphase	(Figure 4A)
PMID:28178520	FYPO:0006645	normal protein localization to mitotic spindle midzone during metaphase [assayed_using] PomBase:SPCC320.13c	(Figure 4E)
PMID:28178520	FYPO:0003002	decreased protein localization to centromere during mitotic metaphase [assayed_using] PomBase:SPCC320.13c	(Figure 4E)
PMID:28178520	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC821.08c	(Figure 5B)
PMID:28178520	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC821.08c	(Figure 5B)
PMID:28178520	FYPO:0001837	increased duration of protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC582.03	(Figure S3B)
PMID:28178520	FYPO:0006643	mitotic spindle collapse without elongation during metaphase [has_severity] high	(Figure S3B)
PMID:28178520	FYPO:0005728	normal deactivation of mitotic spindle assembly checkpoint [assayed_using] PomBase:SPBC582.03	(Figure S3C,D)
PMID:28178520	FYPO:0006644	decreased protein localization to mitotic spindle midzone, with protein distributed along spindle, during anaphase B [assayed_using] PomBase:SPCC320.13c	(Figure S4C)
PMID:28178520	FYPO:0006644	decreased protein localization to mitotic spindle midzone, with protein distributed along spindle, during anaphase B [assayed_using] PomBase:SPCC962.02c	(Figure S4C)
PMID:28178520	FYPO:0006644	decreased protein localization to mitotic spindle midzone, with protein distributed along spindle, during anaphase B [assayed_using] PomBase:SPBC725.12	(Figure S4C)
PMID:28178520	FYPO:0006644	decreased protein localization to mitotic spindle midzone, with protein distributed along spindle, during anaphase B [assayed_using] PomBase:SPBC336.15	(Figure S4C)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPBC15D4.01c	(Figures 1G and 1I; Figure S1F)
PMID:28178520	FYPO:0006642	decreased protein localization to nucleus during mitotic interphase [assayed_using] PomBase:SPBC15D4.01c	(Figures 1G and 1I; Figure S1F)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPAPB1A10.09	(Figures 1H)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPAC1782.09c	(Figures 1H)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPBC725.12	(Figures 1J)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPCC320.13c	(Figures 1J)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPBC336.15	(Figures 1J)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPBC336.15	(Figures 1J)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPCC320.13c	(Figures 1J)
PMID:28178520	FYPO:0004831	decreased protein localization to mitotic spindle midzone during anaphase [assayed_using] PomBase:SPBC725.12	(Figures 1J)
PMID:28178520	FYPO:0004831	decreased protein localization to mitotic spindle midzone during anaphase [assayed_using] PomBase:SPCC962.02c	(Figures 1J)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPCC962.02c	(Figures 1J)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPBC15D4.01c	(Figures 1J)
PMID:28178520	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPBC15D4.01c	(Figures 1J)
PMID:28178520	FYPO:0004883	abnormal protein localization to mitotic spindle midzone [assayed_using] PomBase:SPCC320.13c	(Figures S1D and S1E)
PMID:28178520	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Figures S2A)
PMID:28178520	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Figures S2A)
PMID:28178520	FYPO:0003268	decreased rate of mitotic spindle elongation [has_severity] low	(Figures S2B)
PMID:28178520	FYPO:0006475	mitotic spindle collapse	(Figures S2B)
PMID:28178520	GO:0000022	mitotic spindle elongation	(comment: requires motor activity)
PMID:28191457	FYPO:0000726	sensitive to oxidative stress [has_severity] high	(comment: Phenotype is inherited in non-Mendelian manner, via protein aggregates (prion-like))
PMID:28191457	FYPO:0004180	increased cellular protein aggregate level [assayed_using] PomBase:SPCC1393.10	(comment: SDS-PAGE followed by western blotting and proteinase K treatment. Dot plots with extracts for pellet, soluble and total cell fractions with and without pre-treatment with 2% SDS. SDD-AGE gels of samples treated at room temperature and at 95°C, both with and without curing with GdnHCl.)
PMID:28193844	GO:0000329	fungal-type vacuole membrane	(Fig. 4)
PMID:28193844	GO:0000324	fungal-type vacuole	(Fig. 4)
PMID:28193844	GO:0015886	heme transport	(Fig. 6)
PMID:28193844	GO:0140357	heme export from vacuole to cytoplasm	(Fig. 6a)
PMID:28193844	FYPO:0004698	decreased heme binding [assayed_using] PomBase:SPBC359.05	(Fig. 8b)
PMID:28193844	FYPO:0006890	decreased heme export from vacuole	(Fig. 9)
PMID:28193844	MOD:00171	N-seryl-glycosylphosphatidylinositolethanolamine	(comment: they show it is GPI anchored, the specified residue is predicted)
PMID:28202541	FYPO:0000847	increased protein degradation during vegetative growth [has_penetrance] low [assayed_using] PomBase:SPBC1734.04	(comment: Anp1-GFP degradation as assayed by appearance of free GFP)
PMID:28202541	FYPO:0003935	decreased protein localization to Golgi apparatus, with protein mislocalized to endoplasmic reticulum [has_penetrance] medium [assayed_using] PomBase:SPBC1734.04	(comment: Anp1-GFP mislocalized from Golgi puncta to ER and vacuole)
PMID:28202541	FYPO:0006068	increased protein localization to endoplasmic reticulum [has_penetrance] low [assayed_using] PomBase:SPAC27F1.07	(comment: Ost1-mCherry increased signal in ER)
PMID:28202541	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC27F1.07	(comment: Ost1-mCherry, mCherry antibody)
PMID:28202541	FYPO:0001215	normal protein complex assembly during vegetative growth [assayed_using] PomBase:SPBC19C2.09 [assayed_using] PomBase:SPBC3B9.15c	(comment: Scp1-13xMyc used for Scp1, pulled on Myc)
PMID:28202541	FYPO:0002448	normal Dsc complex assembly	(comment: pulled on Dsc2)
PMID:28202541	FYPO:0001422	decreased protein processing during vegetative growth [has_penetrance] low [assayed_using] PomBase:SPBC19C2.09	improved relative to WT Sre1
PMID:28218250	FYPO:0005952	normal nucleosome occupancy at highly transcribed RNA polymerase II genes	(comment: ChIP-seq)
PMID:28218250	FYPO:0005948	decreased protein localization to chromatin at highly transcribed RNA polymerase II genes during vegetative growth [has_severity] low [assayed_using] PomBase:SPBC28F2.12	(comment: ChIP-seq)
PMID:28218250	FYPO:0005948	decreased protein localization to chromatin at highly transcribed RNA polymerase II genes during vegetative growth [has_severity] low [assayed_using] PomBase:SPBC28F2.12	(comment: ChIP-seq)
PMID:28218250	FYPO:0005951	decreased nucleosome occupancy at highly transcribed RNA polymerase II genes	(comment: ChIP-seq)
PMID:28218250	FYPO:0005950	increased nucleosome occupancy at highly transcribed RNA polymerase II genes	(comment: ChIP-seq)
PMID:28218250	FYPO:0005950	increased nucleosome occupancy at highly transcribed RNA polymerase II genes	(comment: ChIP-seq)
PMID:28218250	FYPO:0005948	decreased protein localization to chromatin at highly transcribed RNA polymerase II genes during vegetative growth [assayed_using] PomBase:SPBC28F2.12 [has_severity] high	(comment: ChIP-seq)
PMID:28218250	FYPO:0005949	normal protein localization to chromatin at highly transcribed RNA polymerase II genes during vegetative growth [assayed_using] PomBase:SPBC28F2.12	(comment: ChIP-seq)
PMID:28218250	FYPO:0005949	normal protein localization to chromatin at highly transcribed RNA polymerase II genes during vegetative growth [assayed_using] PomBase:SPBC28F2.12	(comment: ChIP-seq)
PMID:28218250	FYPO:0005949	normal protein localization to chromatin at highly transcribed RNA polymerase II genes during vegetative growth [assayed_using] PomBase:SPBC28F2.12	(comment: ChIP-seq)
PMID:28218250	FYPO:0005948	decreased protein localization to chromatin at highly transcribed RNA polymerase II genes during vegetative growth [has_severity] medium [assayed_using] PomBase:SPBC28F2.12	(comment: ChIP-seq)
PMID:28218250	FYPO:0005948	decreased protein localization to chromatin at highly transcribed RNA polymerase II genes during vegetative growth [has_severity] medium [assayed_using] PomBase:SPBC28F2.12	(comment: ChIP-seq)
PMID:28218250	FYPO:0005948	decreased protein localization to chromatin at highly transcribed RNA polymerase II genes during vegetative growth [has_severity] medium [assayed_using] PomBase:SPBC28F2.12	(comment: ChIP-seq)
PMID:28218250	FYPO:0005948	decreased protein localization to chromatin at highly transcribed RNA polymerase II genes during vegetative growth [has_severity] medium [assayed_using] PomBase:SPBC28F2.12	(comment: ChIP-seq)
PMID:28218250	FYPO:0005948	decreased protein localization to chromatin at highly transcribed RNA polymerase II genes during vegetative growth [has_severity] medium [assayed_using] PomBase:SPBC28F2.12	(comment: ChIP-seq)
PMID:28218250	FYPO:0005948	decreased protein localization to chromatin at highly transcribed RNA polymerase II genes during vegetative growth [has_severity] medium [assayed_using] PomBase:SPBC28F2.12	(comment: ChIP-seq)
PMID:28218250	FYPO:0005950	increased nucleosome occupancy at highly transcribed RNA polymerase II genes	(comment: ChIP-seq)
PMID:28218250	FYPO:0005948	decreased protein localization to chromatin at highly transcribed RNA polymerase II genes during vegetative growth [assayed_using] PomBase:SPBC28F2.12 [has_severity] high	(comment: ChIP-seq; same severity as spt16-1 alone)
PMID:28242692	FYPO:0000278	decreased cell population growth following spore germination [has_severity] high	(Fig. 1A)
PMID:28242692	FYPO:0002085	normal vegetative cell growth	(Fig. 1B, supp table S1)
PMID:28242692	FYPO:0002085	normal vegetative cell growth	(Fig. 1B, supp table S1)
PMID:28242692	FYPO:0000278	decreased cell population growth following spore germination [has_severity] low	(Fig. 1C)
PMID:28242692	FYPO:0000278	decreased cell population growth following spore germination [has_severity] low	(Fig. 1C)
PMID:28242692	FYPO:0000278	decreased cell population growth following spore germination [has_severity] low	(Fig. 1C)
PMID:28242692	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 1C)
PMID:28242692	FYPO:0000769	abnormal nuclear envelope morphology during vegetative growth [has_penetrance] 80	(Fig. 1D-F)
PMID:28242692	FYPO:0001733	abnormal mitotic spindle pole body separation	(Fig. 2B)
PMID:28242692	FYPO:0006018	decreased nuclear pore density	(Fig. 4B) asterisk
PMID:28242692	FYPO:0003166	monoseptate vegetative cell with binucleate and anucleate compartments [has_penetrance] 30	(Fig. S1A,B)
PMID:28242692	FYPO:0003166	monoseptate vegetative cell with binucleate and anucleate compartments [has_penetrance] 20	(Fig. S1C)
PMID:28242692	FYPO:0003166	monoseptate vegetative cell with binucleate and anucleate compartments [has_penetrance] 20	(Fig. S1C)
PMID:28242692	FYPO:0001513	normal mitotic sister chromatid segregation	(comment: CHECK rescue)
PMID:28242692	FYPO:0000772	perforated nuclear envelope [has_severity] low	(comment: partial leaking) Fig. 3B, arrow; Fig. 3 C and D, quantification
PMID:28242692	FYPO:0000772	perforated nuclear envelope [has_severity] low	(comment: partial leaking) Fig. 3B, arrow; Fig. 3 C and D, quantification
PMID:28242692	FYPO:0000772	perforated nuclear envelope [has_severity] low	(comment: partial leaking) Fig. 3B, arrow; Fig. 3 C and D, quantification
PMID:28242692	FYPO:0000772	perforated nuclear envelope	(comment: severe leaking) Fig. 3B, arrow; Fig. 3 C and D, quantification, Figure 4 B
PMID:28242692	FYPO:0006019	karmellae present	4B, arrowheads, and Fig. 5B
PMID:28242692	FYPO:0003751	normal nuclear envelope morphology	Remarkably, double-mutant cells displayed WT-like nuclei, although a few examples of probable nuclear fenestrations were observed in lem2Δ single-mutant cells (Fig. 5G).
PMID:28242692	FYPO:0003751	normal nuclear envelope morphology	Remarkably, double-mutant cells displayed WT-like nuclei, although a few examples of probable nuclear fenestrations were observed in lem2Δ single-mutant cells (Fig. 5G).
PMID:28242692	FYPO:0003973	abnormal nuclear pore localization	and the NPCs that were present were localized to regions that were largely free of karmellae and tubulo-vesicular structures (Fig. 4D).
PMID:28242692	FYPO:0000516	normal nuclear import [has_severity] high	cells with abnormal NE morphology at the beginning of the experiment, by contrast, lost nuclear GFP completely over the time course (Fig. S3B). Thus, cytoplasmic GFP resulted from loss of nuclear integrity rather than from defects in nuclear import.
PMID:28264193	GO:0140767	enzyme-substrate adaptor activity [part_of] TORC2 signaling	(Fig. 5) (comment: CHECK fusion mutant not currently capturable)
PMID:28264193	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC24B10.07 [assayed_using] PomBase:SPAPYUG7.02c	(Fig. S2)
PMID:28264193	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC24B10.07 [assayed_using] PomBase:SPAPYUG7.02c	(Fig. S2)
PMID:28264193	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC24B10.07 [assayed_using] PomBase:SPAPYUG7.02c	(Fig. S2)
PMID:28264193	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC24B10.07 [assayed_using] PomBase:SPAPYUG7.02c	(Fig. S2)
PMID:28264193	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC24B10.07 [assayed_using] PomBase:SPAPYUG7.02c	(Fig. S2)
PMID:28264193	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC21B10.05c [assayed_using] PomBase:SPBC30D10.10c	(comment: CHECK Supp)
PMID:2827111	GO:0003917	DNA topoisomerase type I (single strand cut, ATP-independent) activity	(Fig. 7B)
PMID:2827111	FYPO:0001234	slow vegetative cell population growth	(Table 1)
PMID:2827111	FYPO:0002061	inviable vegetative cell population	(Table 1)
PMID:2827111	FYPO:0002061	inviable vegetative cell population	Table1
PMID:2827111	FYPO:0002061	inviable vegetative cell population	Table1
PMID:28281664	FYPO:0000645	small vegetative cell [has_severity] low [has_penetrance] low	(Figure 1)
PMID:28281664	FYPO:0000245	loss of viability in stationary phase [has_severity] medium	(Figure 1B)
PMID:28281664	FYPO:0001309	increased viability in stationary phase [has_severity] medium	(Figure 1D)
PMID:28281664	FYPO:0000245	loss of viability in stationary phase [has_severity] low	(Figure 1D)
PMID:28281664	FYPO:0003824	resistance to caffeine and rapamycin [has_severity] medium	(Figure 1a)
PMID:28281664	FYPO:0001122	elongated vegetative cell	(Figure 1b) divides longer than WT in the same conditions
PMID:28281664	FYPO:0000645	small vegetative cell [has_penetrance] high [has_severity] medium	(Figure 1c, 1d)
PMID:28281664	FYPO:0001942	increased duration of lag phase [has_severity] low	(Figure 1d)
PMID:28281664	FYPO:0003824	resistance to caffeine and rapamycin [has_severity] medium	(Figure 2)
PMID:28281664	FYPO:0001122	elongated vegetative cell [has_penetrance] high [has_severity] medium	(Figure 2)
PMID:28281664	FYPO:0003824	resistance to caffeine and rapamycin [has_severity] low	(Figure 2)
PMID:28281664	FYPO:0003824	resistance to caffeine and rapamycin [has_severity] high	(Figure 2)
PMID:28281664	FYPO:0003824	resistance to caffeine and rapamycin [has_severity] medium	(Figure 2)
PMID:28281664	FYPO:0000245	loss of viability in stationary phase [has_severity] medium	(Figure 2)
PMID:28281664	FYPO:0003824	resistance to caffeine and rapamycin [has_severity] medium	(Figure 2)
PMID:28281664	FYPO:0001309	increased viability in stationary phase [has_severity] low	(Figure 2)
PMID:28281664	FYPO:0003824	resistance to caffeine and rapamycin [has_severity] high	(Figure 2)
PMID:28281664	FYPO:0001103	resistance to hydrogen peroxide [has_severity] low	(Figure 3)
PMID:28281664	FYPO:0001122	elongated vegetative cell [has_penetrance] medium [has_severity] medium	(Figure 3)
PMID:28281664	FYPO:0001122	elongated vegetative cell	(Figure 3)
PMID:28281664	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Figure 3)
PMID:28281664	FYPO:0000245	loss of viability in stationary phase [has_severity] low	(Figure 3)
PMID:28281664	FYPO:0001122	elongated vegetative cell [has_severity] medium [has_penetrance] medium	(Figure 3)
PMID:28281664	FYPO:0000245	loss of viability in stationary phase [has_severity] high	(Figure 3)
PMID:28281664	FYPO:0001103	resistance to hydrogen peroxide [has_severity] medium	(Figure 3)
PMID:28282432	FYPO:0005663	abnormal re-entry into mitotic cell cycle after arrest in response to heat shock	(Fig. 2)
PMID:28282432	FYPO:0005663	abnormal re-entry into mitotic cell cycle after arrest in response to heat shock	(Fig. 2)
PMID:28282432	FYPO:0005585	decreased cellular triglyceride level during vegetative growth [has_severity] low	(Fig. 4)
PMID:28282432	FYPO:0006974	triglyceride absent from cell	(Fig. 4)
PMID:28282432	FYPO:0006974	triglyceride absent from cell	(Fig. 4)
PMID:28282432	FYPO:0006974	triglyceride absent from cell	(Fig. 4)
PMID:28282432	FYPO:0005585	decreased cellular triglyceride level during vegetative growth [has_severity] low	(Fig. 4)
PMID:28282432	FYPO:0005585	decreased cellular triglyceride level during vegetative growth [has_severity] medium	(Fig. 4)
PMID:28282432	FYPO:0005585	decreased cellular triglyceride level during vegetative growth [has_severity] high	(Fig. 4)
PMID:28282432	FYPO:0004695	increased cellular diglyceride level	(Fig. 5)
PMID:28282432	FYPO:0008288	increased cellular ceramide level	(Fig. 5)
PMID:28282432	FYPO:0008288	increased cellular ceramide level	(Fig. 5)
PMID:28282432	FYPO:0004695	increased cellular diglyceride level	(Fig. 5)
PMID:28292899	GO:0106186	cytoplasmic side of plasma membrane, cell tip [exists_during] meiotic prophase I	(Fig. 1A) Inset and Movie S1/ number of Mcp5 molecules per cluster 10 ± 2 ( Fig. 1D)
PMID:28292899	GO:0005546	phosphatidylinositol-4,5-bisphosphate binding	(Fig. 2, 3C)
PMID:28292899	FYPO:0006868	decreased protein localization to cell cortex during meiotic prophase I [assayed_using] PomBase:SPBC216.02	(Fig. 4 D-F)
PMID:28292899	FYPO:0006868	decreased protein localization to cell cortex during meiotic prophase I [assayed_using] PomBase:SPBC216.02	(Fig. 5B)
PMID:28292899	FYPO:0003835	normal horsetail movement	(Fig. 5B)
PMID:28292899	FYPO:0003835	normal horsetail movement	(Fig. 5B)
PMID:28292899	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 5B,A) (comment: ALSO FOR THE myo-1TH3 domain deletion - need genotype description)
PMID:28292899	FYPO:0006868	decreased protein localization to cell cortex during meiotic prophase I [assayed_using] PomBase:SPAC1093.06c	(Fig. 6)
PMID:28292899	FYPO:0000927	abolished horsetail movement	(Fig. 7)
PMID:28292899	FYPO:0000927	abolished horsetail movement	(Fig. 7)
PMID:28334955	FYPO:0000245	loss of viability in stationary phase [has_severity] high	(Fig. 1 E,F)
PMID:28334955	FYPO:0000046	decreased cell population growth [has_severity] low	(Fig. 1A)
PMID:28334955	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] high	(Fig. 1A)
PMID:28334955	FYPO:0000251	decreased cell population growth on galactose carbon source [has_severity] high	(Fig. 1A)
PMID:28334955	FYPO:0000440	sensitive to antimycin A [has_severity] high	(Fig. 1B)
PMID:28334955	FYPO:0001437	normal growth on antimycin A [has_severity] high	(Fig. 1B)
PMID:28334955	FYPO:0000078	abnormal cellular respiration [has_severity] high	(Fig. 1B)
PMID:28334955	FYPO:0000440	sensitive to antimycin A [has_severity] high	(Fig. 1B)
PMID:28334955	FYPO:0000078	abnormal cellular respiration [has_severity] high	(Fig. 1B)
PMID:28334955	FYPO:0000251	decreased cell population growth on galactose carbon source [has_severity] high	(Fig. 1C)
PMID:28334955	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] high	(Fig. 1C)
PMID:28334955	FYPO:0000046	decreased cell population growth [has_severity] low	(Fig. 7A)
PMID:28334955	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] high	(Fig. 7A)
PMID:28334955	FYPO:0000440	sensitive to antimycin A [has_severity] high	(Fig. 7B)
PMID:28334955	FYPO:0000245	loss of viability in stationary phase [has_severity] high	(Fig. 7c)
PMID:28334955	FYPO:0005974	normal mitochondrial protein level [assayed_using] PomBase:SPAPB1E7.11c	(Fig. 9C)
PMID:28334955	FYPO:0003423	decreased mitochondrial RNA level [assayed_using] PomBase:SPMIT.05 [has_severity] high	(Figure 2B)
PMID:28334955	FYPO:0003423	decreased mitochondrial RNA level [assayed_using] PomBase:SPMIT.09 [has_severity] low	(Figure 2B)
PMID:28334955	FYPO:0003423	decreased mitochondrial RNA level [assayed_using] PomBase:SPMIT.01 [has_severity] high	(Figure 2B) (comment: barely detectable level )
PMID:28334955	FYPO:0003423	decreased mitochondrial RNA level [assayed_using] PomBase:SPMIT.10 [has_severity] low	(Figure 2B,8B,8C)
PMID:28334955	FYPO:0002582	normal mature mitochondrial tRNA level	(Figure 2C)
PMID:28334955	GO:0005739	mitochondrion	(Figure 6a)
PMID:28334955	GO:0005739	mitochondrion	(Figure 6a)
PMID:28334955	GO:0005759	mitochondrial matrix	(Figure 6c)
PMID:28334955	GO:0005759	mitochondrial matrix	(Figure 6c)
PMID:28334955	FYPO:0003769	decreased cellular mtDNA level [has_severity] low	(Figure 8A)
PMID:28334955	FYPO:0003423	decreased mitochondrial RNA level [assayed_using] PomBase:SPMIT.05 [has_severity] high	(Figure 8B,8C)
PMID:28334955	FYPO:0003423	decreased mitochondrial RNA level [assayed_using] PomBase:SPMIT.09 [has_severity] low	(Figure 8B,8C)
PMID:28334955	FYPO:0003423	decreased mitochondrial RNA level [assayed_using] PomBase:SPMIT.01 [has_severity] high	(Figure 8B,8C) (comment: barely detectable level )
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.04	(Figure 8D)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.11	(Figure 8D)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.05	(Figure 8D)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.01	(Figure 8D)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.08	(Figure 8D)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.07	(Figure 8D)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPBC106.19	(Figure 9A)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.11	(Figure 9F)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.04	(Figure 9F)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.01	(Figure 9F)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.05	(Figure 9F)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.11	(Figure 9F)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.04	(Figure 9F)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.01	(Figure 9F)
PMID:28334955	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPMIT.05	(Figure 9F)
PMID:28334955	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC106.19	(Figure 9d)
PMID:28334955	FYPO:0004960	normal mitochondrial RNA level [assayed_using] PomBase:SPBC106.19	(Figure Supp S8)
PMID:28334955	GO:0035694	mitochondrial protein catabolic process	(comment: Based on what we know about lon in other species, i think the rescue of mpa1 phenotype is enough to predict a catabolic role)
PMID:28334955	FYPO:0004594	branched, elongated, septated cell [has_penetrance] low	Supp. Figure S3
PMID:28334955	FYPO:0002380	viable spheroid vegetative cell	Supp. Figure S3
PMID:28334955	FYPO:0002106	viable stubby vegetative cell	Supp. Figure S3
PMID:28334955	FYPO:0004153	increased flocculation in stationary phase	Supplementary Figure S3B
PMID:28334955	FYPO:0003335	increased galactose-specific flocculation	Supplementary Figure S3B ((comment: abolished by galactose addition)
PMID:28334955	FYPO:0004153	increased flocculation in stationary phase	Supplementary Figure S7
PMID:28343969	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC23C4.03 [assayed_using] PomBase:SPAC110.02	(Fig. 1B)
PMID:28343969	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPAC23C4.03 [has_penetrance] high	(Fig. 2A,B)
PMID:28343969	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPCC962.02c	(Fig. 2A,B)
PMID:28343969	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPAC23C4.03 [has_penetrance] high	(Fig. 2A,B)
PMID:28343969	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPCC962.02c	(Fig. 2A,B)
PMID:28343969	FYPO:0006598	decreased histone H3-T3 phosphorylation during vegetative growth [assayed_using] PomBase:SPAC23C4.03 [has_penetrance] high	(Fig. 2B)
PMID:28343969	FYPO:0006598	decreased histone H3-T3 phosphorylation during vegetative growth [assayed_using] PomBase:SPAC23C4.03 [has_penetrance] high	(Fig. 2B)
PMID:28343969	FYPO:0006600	decreased protein localization to centromeric chromatin during mitotic metaphase [has_penetrance] high [assayed_using] PomBase:SPCC320.13c	"(Fig. 2C) (comment: this represents Yoshi's suggestion"" An Ark1 reduction can become a reason of merotelic attachment, which is also caused by a defect in kinetochore structures.)"" (comment: CHECK has_penetrance high , assayed_using ark1)"
PMID:28343969	FYPO:0006600	decreased protein localization to centromeric chromatin during mitotic metaphase [has_penetrance] high [assayed_using] PomBase:SPCC320.13c	"(Fig. 2C) (comment: vw: this represents Yoshi's suggestion"" An Ark1 reduction can become a reason of merotelic attachment, which is also caused by a defect in kinetochore structures.)"""
PMID:28343969	FYPO:0004382	meroterically attached lagging mitotic chromosomes [has_penetrance] 15	(Fig. 2C, 2D, 2G)
PMID:28343969	FYPO:0004382	meroterically attached lagging mitotic chromosomes [has_penetrance] medium	(Fig. 2C, 2D, 2G)
PMID:28343969	FYPO:0006601	normal protein localization to centromeric chromatin during mitotic metaphase [assayed_using] PomBase:SPCC320.13c	(Fig. 2E)
PMID:28343969	FYPO:0006601	normal protein localization to centromeric chromatin during mitotic metaphase [assayed_using] PomBase:SPCC320.13c	(Fig. 2E)
PMID:28343969	FYPO:0001513	normal mitotic sister chromatid segregation [has_penetrance] 95	(Fig. 2F)
PMID:28343969	FYPO:0001513	normal mitotic sister chromatid segregation [has_penetrance] 95	(Fig. 2F)
PMID:28343969	FYPO:0004382	meroterically attached lagging mitotic chromosomes [has_penetrance] ~16	(Fig. 2F)
PMID:28343969	FYPO:0002061	inviable vegetative cell population	(Fig. 4C)
PMID:28343969	FYPO:0002061	inviable vegetative cell population	(Fig. 4C)
PMID:28343969	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC110.02 [assayed_using] PomBase:SPBC16A3.11	(Fig. 4E)
PMID:28343969	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC110.02 [assayed_using] PomBase:SPBC16A3.11	(Fig. 4E)
PMID:28343969	FYPO:0000460	decreased mitotic centromeric sister chromatid cohesion [has_severity] medium	(Fig. 4F, 4H)
PMID:28343969	FYPO:0002394	decreased protein acetylation during vegetative growth [assayed_using] PomBase:SPAC10F6.09c	(Fig. 4G)
PMID:28343969	FYPO:0002394	decreased protein acetylation during vegetative growth [assayed_using] PomBase:SPAC10F6.09c	(Fig. 4G)
PMID:28343969	FYPO:0000460	decreased mitotic centromeric sister chromatid cohesion [has_severity] medium	(Fig. 4H)
PMID:28343969	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC428.17c [assayed_using] PomBase:SPAC110.02	(Fig. 4b)
PMID:28343969	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC428.17c [assayed_using] PomBase:SPAC110.02	(Fig. 4b)
PMID:28343969	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 4f)
PMID:28343969	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. 4f)
PMID:28343969	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 4f)
PMID:28343969	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4f)
PMID:28343969	FYPO:0003002	decreased protein localization to centromere during mitotic metaphase [assayed_using] PomBase:SPAC23C4.03	(Fig. S2A, S2C)
PMID:28343969	FYPO:0002060	viable vegetative cell population	(Fig. S4A)
PMID:28343969	FYPO:0002093	decreased meiotic sister chromatid cohesion [has_severity] low	(Fig. S4A)
PMID:28343969	FYPO:0006521	abnormal mitotic sister chromatid cohesion	(Fig. S4A)
PMID:28343969	FYPO:0002093	decreased meiotic sister chromatid cohesion [has_severity] low	(Fig. S4A)
PMID:28343969	FYPO:0002093	decreased meiotic sister chromatid cohesion [has_severity] low	(Fig. S4A)
PMID:28343969	FYPO:0006521	abnormal mitotic sister chromatid cohesion	(Fig. S4A)
PMID:28343969	FYPO:0002061	inviable vegetative cell population	(Fig. S4A)
PMID:28343969	FYPO:0006521	abnormal mitotic sister chromatid cohesion [assayed_using] PomBase:SPCC320.13c	(Fig. S4B)
PMID:28343969	GO:0140463	chromatin-protein adaptor activity [part_of] establishment of mitotic sister chromatid cohesion [has_input] PomBase:SPBC16A3.11 [happens_during] mitotic interphase	(Figures S4D and S4E)
PMID:28343969	GO:0140463	chromatin-protein adaptor activity	(Figures S4D and S4E)
PMID:28343969	GO:0051456	attachment of meiotic spindle microtubules to meiosis II kinetochore	(comment: CHECK specifically, biorientation)
PMID:28343969	GO:0051456	attachment of meiotic spindle microtubules to meiosis II kinetochore	(comment: CHECK specifically, biorientation)
PMID:28343969	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPAC23C4.03 [occurs_in] pericentric heterochromatin [part_of] attachment of meiotic spindle microtubules to meiosis II kinetochore [happens_during] mitotic M phase	Here we identify a conserved Hrk1-interacting motif (HIM) in Pds5 and a Pds5-interacting motif (PIM) in Hrk1 in fission yeast. Mutations in either motif result in the displacement of Hrk1 from centromeres. We also show that the mechanism of Pds5-dependent Hrk1 recruitment is conserved in human cells | (Figure 1 E) Thus, although Eso1, Wpl1, and Hrk1 all bind to the same surface of Pds5, we assume that they do not always compete for binding because of the excess amounts of Pds5 in the cells. Thus, HIM in Pds5 and PIM in Hrk1 are required solely for centromeric Hrk1 localization and its function, at least in the context of targeting the CPC to centromeres.
PMID:28345447	FYPO:0002865	sensitive to polypeptone	(comment: CHECK restored by depletion of ammonium)
PMID:28345447	FYPO:0002865	sensitive to polypeptone	(comment: CHECK restored by depletion of ammonium)
PMID:28345447	FYPO:0002865	sensitive to polypeptone	(comment: CHECK restored by depletion of ammonium)
PMID:28345447	FYPO:0002865	sensitive to polypeptone	(comment: CHECK restored by depletion of ammonium)
PMID:28345447	FYPO:0002865	sensitive to polypeptone	(comment: CHECK restored by depletion of ammonium)
PMID:28366743	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] high	(Fig. 1B)
PMID:28366743	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] high	(Fig. 1B)
PMID:28366743	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1B)
PMID:28366743	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] low	(Fig. 1B)
PMID:28366743	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] high	(Fig. 1B)
PMID:28366743	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPBC20F10.06	(Fig. 1C) (comment: synchronous mitotic cells)
PMID:28366743	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] medium	(Fig. 1b)
PMID:28366743	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] low	(Fig. 2C, D, S2B)
PMID:28366743	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. 2C, D, S2B)
PMID:28366743	FYPO:0007385	increased duration of protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPBC20F10.06	(Fig. 3A, B) (comment: CHECK: present in interphase cells)
PMID:28366743	FYPO:0007385	increased duration of protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC821.08c	(Fig. 3A, B) (comment: CHECK: present in interphase cells)
PMID:28366743	FYPO:0007385	increased duration of protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC821.08c	(Fig. 3B)
PMID:28366743	FYPO:0007385	increased duration of protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPBC20F10.06	(Fig. 3B)
PMID:28366743	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC821.08c	(Fig. 3a)
PMID:28366743	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPBC20F10.06	(Fig. 3a)
PMID:28366743	FYPO:0004367	normal mitotic spindle assembly	(Fig. 4A)
PMID:28366743	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] medium	(Fig. 4A)
PMID:28366743	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC19G12.01c	(Fig. 4C)
PMID:28366743	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC19G12.01c	(Fig. 4C)
PMID:28366743	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC19G12.01c	(Fig. 4C)
PMID:28366743	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC6F12.15c	(Fig. 4D)
PMID:28366743	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] low	(Fig. S1G)
PMID:28366743	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. S1h)
PMID:28366743	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPBC20F10.06 [assayed_using] PomBase:SPAC821.08c	(Fig. S3B)
PMID:28366743	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Figure 1F
PMID:28366743	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPBC20F10.06	(Figure 3A)
PMID:28366743	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC821.08c	(Figure 3A)
PMID:28366743	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC19G12.01c	(Figure 4C) (comment: synchronous mitotic cells)
PMID:28366743	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC6F12.15c	(Figure 4D)
PMID:28366743	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC6F12.15c	(Figure 4D)
PMID:28366743	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC6F12.15c	(Figure 4D)
PMID:28366743	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPAC23H3.08c	(Figure S1e)
PMID:28366743	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPBC20F10.06 [has_severity] high	(Figure S3B)
PMID:28366743	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC20F10.06 [assayed_using] PomBase:SPBC3D6.04c [has_severity] high	(Figure S3B)
PMID:28366743	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPBC20F10.06 [has_severity] high	(Figure S3B)
PMID:28366743	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC1795.01c [assayed_using] PomBase:SPBC20F10.06 [has_severity] high	(Figure S3B)
PMID:28366743	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC821.08c [assayed_using] PomBase:SPBC20F10.06	(Figure S3B)
PMID:28366743	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC821.08c [assayed_using] PomBase:SPBC20F10.06	(Figure S3B)
PMID:28366743	FYPO:0005781	decreased duration of mitotic spindle assembly checkpoint [has_severity] medium	(Figures 1F, S1H)
PMID:28366743	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC821.08c [assayed_using] PomBase:SPCC1795.01c	(comment: synchronous mitotic cells) fig 1c
PMID:28366744	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1A) (comment: checkpoint assay)
PMID:28366744	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1A) (comment: checkpoint assay)
PMID:28366744	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1A) (comment: checkpoint assay)
PMID:28366744	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1A) (comment: checkpoint assay)
PMID:28366744	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Fig. 1A) (comment: checkpoint assay)
PMID:28366744	FYPO:0005783	normal mitotic checkpoint complex assembly	(Fig. 1c)
PMID:28366744	FYPO:0005783	normal mitotic checkpoint complex assembly	(Fig. 1c)
PMID:28366744	FYPO:0007173	decreased mitotic checkpoint complex binding	(Fig. 1c)
PMID:28366744	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPBC20F10.06 [assayed_using] PomBase:SPAC19G12.01c	(Fig. 2a)
PMID:28366744	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC19G12.01c [assayed_using] PomBase:SPCC1795.01c	(Fig. 2a)
PMID:28366744	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC19G12.01c [assayed_using] PomBase:SPCC1795.01c	(Fig. 2a)
PMID:28366744	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC20F10.06 [assayed_using] PomBase:SPAC19G12.01c	(Fig. 2a)
PMID:28366744	FYPO:0001327	increased protein level during vegetative growth [assayed_using] mitotic checkpoint complex	(Fig. S1)
PMID:28366744	FYPO:0000846	decreased protein degradation during vegetative growth [assayed_using] PomBase:SPBC582.03	(Figure 2b)
PMID:28366744	FYPO:0005928	abolished protein polyubiquitination during vegetative growth [assayed_using] PomBase:SPAC821.08c	(Figure 3A)
PMID:28366744	FYPO:0000912	abolished protein ubiquitination during vegetative growth [assayed_using] PomBase:SPAC821.08c	(Figure 3A).
PMID:28366744	FYPO:0000912	abolished protein ubiquitination during vegetative growth [assayed_using] PomBase:SPAC821.08c	(Figure 3A).
PMID:28366744	FYPO:0002082	increased protein ubiquitination during vegetative growth [assayed_using] PomBase:SPAC821.08c	(Figure 3B).
PMID:28366744	FYPO:0004102	decreased protein polyubiquitination during vegetative growth [assayed_using] PomBase:SPAC821.08c	(Figure 3B).
PMID:28366744	FYPO:0002774	increased level of ubiquitinated protein in cell during vegetative growth [assayed_using] PomBase:SPAC821.08c	(Figures 3A, 3B)
PMID:28366744	GO:0031145	anaphase-promoting complex-dependent catabolic process	(comment: Deletion increases levels of mitotic checkpoint complex associated with the anaphase promoting complex in mitosis)
PMID:28366744	GO:0031145	anaphase-promoting complex-dependent catabolic process	(comment: Required for mitotic checkpoint complex binding to the anaphase promoting complex.)
PMID:28366744	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(comment: vw I changed the genotype/) Fig 1A (comment: checkpoint assay)
PMID:28366744	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_using] PomBase:SPAC821.08c	"(comment: vw changed term from ""reduced ubiquitin ligase activity"")"
PMID:28366744	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint	(comment: vw; I changed the genotype here)
PMID:28367989	GO:0099122	RNA polymerase II C-terminal domain binding [has_input] rpb1/Phos(CTD-S2) [part_of] termination of RNA polymerase II transcription	(comment: S2P form)
PMID:28377506	FYPO:0001934	abolished cell population growth on glycerol carbon source	(Fig. 4)
PMID:28377506	FYPO:0001934	abolished cell population growth on glycerol carbon source	(Fig. 4)
PMID:28377506	FYPO:0000726	sensitive to oxidative stress	(Fig. 4D)
PMID:28377506	FYPO:0000963	normal growth on hydroxyurea	"(Fig. 7) ""unlike the hem13-1 mutant, the hem12 and hem14 null mutants of the heme biosynthesis pathway are insensitive to HU"""
PMID:28377506	FYPO:0000963	normal growth on hydroxyurea	"(Fig. 7) ""unlike the hem13-1 mutant, the hem12 and hem14 null mutants of the heme biosynthesis pathway are insensitive to HU"""
PMID:2837764	GO:0005786	signal recognition particle, endoplasmic reticulum targeting	(comment: assayed using mammalian proteins)
PMID:28388826	FYPO:0006566	normal viability upon sulfur starvation	data not shown
PMID:28388826	FYPO:0006566	normal viability upon sulfur starvation	data not shown
PMID:28404620	FYPO:0004604	decreased chromatin silencing at subtelomere [assayed_using] subtelomere [assayed_using] PomBase:SPAC212.11	(comment: also uses Pol ii-RNA immunoprecipitation)
PMID:28404620	FYPO:0004604	decreased chromatin silencing at subtelomere [assayed_using] PomBase:SPAC212.11	(comment: also uses Pol ii-RNA immunoprecipitation)
PMID:28404620	FYPO:0006109	increased subtelomeric transcript-derived siRNA level	(comment: sequencing of Ago1-bound siRNA)
PMID:28404620	FYPO:0006109	increased subtelomeric transcript-derived siRNA level	(comment: sequencing of Ago1-bound siRNA)
PMID:28404620	FYPO:0006109	increased subtelomeric transcript-derived siRNA level	(comment: sequencing of Ago1-bound siRNA)
PMID:28404620	FYPO:0006109	increased subtelomeric transcript-derived siRNA level	(comment: sequencing of Ago1-bound siRNA)
PMID:28404620	FYPO:0006109	increased subtelomeric transcript-derived siRNA level	(comment: sequencing of Ago1-bound siRNA)
PMID:28404620	FYPO:0006110	increased silent mating-type cassette transcript-derived siRNA level	(comment: sequencing of Ago1-bound siRNA)
PMID:28404620	FYPO:0006109	increased subtelomeric transcript-derived siRNA level	(comment: sequencing of Ago1-bound siRNA)
PMID:28404620	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [assayed_using] mating_type_region	(comment: uses Pol ii-RNA immunoprecipitation)
PMID:28404620	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: uses Pol ii-RNA immunoprecipitation)
PMID:28404620	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_using] PomBase:SPAC212.11	(comment: uses histone H3 RNA immunoprecipitation)
PMID:28410370	FYPO:0004806	incomplete cell wall disassembly at cell fusion site	(comment: Strong phenotype in crosses with fus1∆)
PMID:28410370	FYPO:0006503	abnormal protein localization to actin fusion focus [assayed_using] PomBase:SPCC1919.10c	(comment: Wider localization at shmoo tip)
PMID:28410370	FYPO:0000413	abolished cell fusion during mating [has_penetrance] low	(comment: more severe phenotype when crossed to fus1delta)
PMID:28410370	FYPO:0000413	abolished cell fusion during mating [has_penetrance] medium	(comment: more severe phenotype when crossed to fus1∆)
PMID:28410370	FYPO:0000413	abolished cell fusion during mating [has_penetrance] medium	(comment: phenotype more severe when crossed to fus1∆)
PMID:28410370	FYPO:0000413	abolished cell fusion during mating [has_penetrance] medium	(comment: stronger phenotype when crossed to fus1∆)
PMID:28410370	FYPO:0006108	abnormal actin fusion focus assembly	(comment: wider distribution along shmoo tip)
PMID:28410370	FYPO:0006503	abnormal protein localization to actin fusion focus [assayed_using] PomBase:SPAC27F1.02c	(comment: wider localization at the shmoo tip)
PMID:28410370	FYPO:0006503	abnormal protein localization to actin fusion focus [assayed_using] PomBase:SPCC1919.10c	(comment: wider localization)
PMID:28410370	FYPO:0006503	abnormal protein localization to actin fusion focus [assayed_using] PomBase:SPCC1919.10c	(comment: wider localization)
PMID:28410370	FYPO:0006503	abnormal protein localization to actin fusion focus [assayed_using] PomBase:SPCC1919.10c	(comment: wider localization)
PMID:28410370	FYPO:0006503	abnormal protein localization to actin fusion focus [assayed_using] PomBase:SPAC27F1.02c	(comment: wider localization)
PMID:28410370	FYPO:0006503	abnormal protein localization to actin fusion focus [assayed_using] PomBase:SPAC4H3.14c	(comment: wider localization)
PMID:28432181	GO:0106032	snRNA pseudouridine synthase activity [part_of] snRNA pseudouridine synthesis	(comment: snRNA/ complementation of yeast pus1)
PMID:28438891	FYPO:0002061	inviable vegetative cell population	(Fig. 1C)
PMID:28438891	FYPO:0002061	inviable vegetative cell population	(Fig. 1C)
PMID:28438891	FYPO:0000046	decreased cell population growth [has_severity] low	(Fig. 1C)
PMID:28438891	FYPO:0000046	decreased cell population growth [has_severity] low	(Fig. 1C)
PMID:28438891	FYPO:0000046	decreased cell population growth [has_severity] low	(Fig. 1C)
PMID:28438891	FYPO:0000046	decreased cell population growth [has_severity] low	(Fig. 1C)
PMID:28438891	FYPO:0001357	normal vegetative cell population growth	(Fig. 1C)
PMID:28438891	FYPO:0000046	decreased cell population growth [has_severity] low	(Fig. 1C)
PMID:28438891	FYPO:0002061	inviable vegetative cell population	(Fig. 1C)
PMID:28438891	FYPO:0001357	normal vegetative cell population growth	(Fig. 1C)
PMID:28438891	FYPO:0001357	normal vegetative cell population growth	(Fig. 1C)
PMID:28438891	FYPO:0000046	decreased cell population growth [has_severity] low	(Fig. 1C)
PMID:28438891	FYPO:0001357	normal vegetative cell population growth	(Fig. 1D)
PMID:28438891	FYPO:0001357	normal vegetative cell population growth	(Fig. 1D)
PMID:28438891	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPCC338.17c	(Fig. 3C)
PMID:28438891	MOD:00046	O-phospho-L-serine	(Fig. 3C)
PMID:28438891	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPCC338.17c	(Fig. 3C)
PMID:28438891	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPCC338.17c	(Fig. 3C)
PMID:28438891	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Fig. 3C)
PMID:28438891	FYPO:0001357	normal vegetative cell population growth	(Fig. 4)
PMID:28438891	FYPO:0002060	viable vegetative cell population	(Fig. 4E)
PMID:28438891	FYPO:0002060	viable vegetative cell population	(Fig. 5A)
PMID:28438891	GO:0005515	protein binding	(Fig. 7)
PMID:28438891	GO:0000785	chromatin	(Fig. EV5)
PMID:28438891	FYPO:0002061	inviable vegetative cell population	(Figure 5 B) (comment: exacerbates )
PMID:28438891	GO:0045875	negative regulation of sister chromatid cohesion	(comment: MIOTOTIC)
PMID:28438891	GO:0072542	protein phosphatase activator activity [part_of] negative regulation of sister chromatid cohesion [has_input] PomBase:SPBC26H8.05c	(comment: required for Rad21 dephosphorylation)
PMID:28438891	GO:0045875	negative regulation of sister chromatid cohesion	(comment: type 2 cohesion (still bound) MITOTIC)
PMID:28438891	GO:0004722	protein serine/threonine phosphatase activity [part_of] negative regulation of sister chromatid cohesion [has_input] PomBase:SPCC338.17c	(comment: type 2 cohesion (still bound))
PMID:28467824	FYPO:0000826	decreased RNA level	Mutations that are predicted to impair middle module sta- bility also lead to a general decrease in RNA synthesis (Extended Data Fig. 4d), showing that the middle module is globally required for transcription. (comment: used txn rather than RNA level because we know it is transcription)
PMID:28467824	FYPO:0000826	decreased RNA level	Mutations that are predicted to impair middle module sta- bility also lead to a general decrease in RNA synthesis (Extended Data Fig. 4d), showing that the middle module is globally required for transcription. (comment: used txn rather than RNA level because we know it is transcription)
PMID:28469148	FYPO:0002485	decreased intergenic meiotic recombination [assayed_using] PomBase:SPCC1322.13 [assayed_using] PomBase:SPCC777.09c	(comment: CHECK ade6 arg1)
PMID:28469148	FYPO:0002485	decreased intergenic meiotic recombination [assayed_using] PomBase:SPAC227.18 [assayed_using] PomBase:SPAC22G7.06c	(comment: CHECK lys3 ura1)
PMID:28469148	FYPO:0005578	normal intergenic meiotic recombination [assayed_using] PomBase:SPAC227.18 [assayed_using] PomBase:SPAC22G7.06c	(comment: CHECK lys3 ura1)
PMID:28469148	FYPO:0002485	decreased intergenic meiotic recombination [assayed_using] PomBase:SPAC227.18 [assayed_using] PomBase:SPAC22G7.06c	(comment: CHECK lys3 ura1)
PMID:28469148	FYPO:0002485	decreased intergenic meiotic recombination [assayed_using] PomBase:SPAC227.18 [assayed_using] PomBase:SPAC22G7.06c	(comment: CHECK lys3 ura1)
PMID:28469148	FYPO:0002485	decreased intergenic meiotic recombination [assayed_using] PomBase:SPAC227.18 [assayed_using] PomBase:SPAC22G7.06c	(comment: CHECK lys3 ura1)
PMID:28469148	FYPO:0002485	decreased intergenic meiotic recombination [assayed_using] PomBase:SPAC227.18 [assayed_using] PomBase:SPAC22G7.06c	(comment: CHECK lys3 ura1)
PMID:28469148	FYPO:0002485	decreased intergenic meiotic recombination [assayed_using] PomBase:SPAC22G7.06c [assayed_using] PomBase:SPAC56F8.10	(comment: CHECK ura1 met5)
PMID:28469148	FYPO:0002485	decreased intergenic meiotic recombination [assayed_using] PomBase:SPAC22G7.06c [assayed_using] PomBase:SPAC56F8.10	(comment: CHECK ura1 met5)
PMID:28469148	FYPO:0002485	decreased intergenic meiotic recombination [assayed_using] PomBase:SPAC22G7.06c [assayed_using] PomBase:SPAC56F8.10	(comment: CHECK ura1 met5)
PMID:28469148	FYPO:0002485	decreased intergenic meiotic recombination [assayed_using] PomBase:SPAC22G7.06c [assayed_using] PomBase:SPAC56F8.10	(comment: CHECK ura1 met5)
PMID:28469148	FYPO:0002485	decreased intergenic meiotic recombination [assayed_using] PomBase:SPAC22G7.06c [assayed_using] PomBase:SPAC56F8.10	(comment: CHECK ura1 met5)
PMID:28475874	FYPO:0003589	decreased replication slippage during replication fork processing	(comment: in response to a single blocked replisome)
PMID:28475874	FYPO:0006086	increased mitotic sister chromatid bridge formation during replication fork processing	(comment: in response to a single blocked replisome)
PMID:28475874	FYPO:0003589	decreased replication slippage during replication fork processing	(comment: in response to a single blocked replisome)
PMID:28475874	FYPO:0004251	increased DNA resection during replication fork processing	(comment: in response to a single blocked replisome)
PMID:28475874	FYPO:0005236	normal protein localization to chromatin at stalled replication fork	(comment: in response to a single blocked replisome)
PMID:28475874	FYPO:0003589	decreased replication slippage during replication fork processing	(comment: in response to a single blocked replisome)
PMID:28475874	GO:0031297	replication fork processing	In the absence of Rad51, newly replicated strands are extensively resected at dysfunctional replication forks thus generating mitotic sister chromatid bridging
PMID:28475874	GO:0031297	replication fork processing	In the absence of Rad52, newly replicated strands are extensively resected at dysfunctional replication forks thus generating mitotic sister chromatid bridging.
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 2)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 2)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 2)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 2)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 2)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 2)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 2)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 2, 3, 4B)
PMID:28476936	FYPO:0007787	increased transcription during cell cycle arrest at meiotic G2/MI transition	(Fig. 4A, C, E, F) (comment: no supplements added)
PMID:28476936	FYPO:0000836	increased protein level [has_severity] medium	(Fig. 4D) (comment: no supplements added)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0006313	abolished meiotic G2/MI transition [has_penetrance] medium	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. 5) (comment: supplements added)
PMID:28476936	FYPO:0006313	abolished meiotic G2/MI transition [has_penetrance] high	(Fig. S1A, 1)
PMID:28476936	FYPO:0007785	abnormal cell cycle arrest at meiotic G2/MI transition	(Fig. S1A,1B,1C)
PMID:28476936	FYPO:0001235	decreased extent of cell population growth	(Fig. S4A) cell growth at G2/M1 arrest is dependent on transcription. (comment: no supplements added)
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. S5) in this situation Sck1 only causes a small increase in cell length increase compared to Sck2 . This show that Sck2 is the main S6 kinase effector of promoting growth in this situation
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. S5) in this situation gad8 overexpression is unable to promote growth i. This show that Sck2 is the main S6 kinase effector of promoting growth in this situation
PMID:28476936	FYPO:0007786	elongated cell with cell cycle arrest at meiotic G2/MI transition	(Fig. S5) in this situation psk1 only causes a small increase in cell length increase compared to Sck2 . This show that Sck2 is the main S6 kinase effector of promoting growth in this situation
PMID:28479325	FYPO:0001124	normal vegetative cell size	(comment: CHECK normal cell size homeostasis)
PMID:28479325	PomGeneEx:0000013	RNA level unchanged [during] mitotic G2 phase	(comment: relatively constant concentration during G2, as previously observed)
PMID:28479325	PomGeneEx:0000011	RNA level increased [during] mitotic G2 phase	During G2, the concentration of Cdc25 increases about 2 fold (Figure 1A)
PMID:28479325	FYPO:0001317	normal RNA level during vegetative growth	We find that the size dependent expression of Cdc25 does not require the 5′ UTR of its transcript, showing that this mechanism of translational regulation is not necessary for size dependent expression (Figure S3A).
PMID:28479325	GO:0031569	mitotic G2 cell size control checkpoint signaling	We propose that the size-dependent expression of the cdc25 transcript is the mechanism that allows cells to divide at a particular size, but it is not the mechanism which regulates what that size is.
PMID:28481910	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: same as cdc20-M10 alone)
PMID:28497540	FYPO:0004763	abolished protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPBP35G2.03c	(Fig 4B)
PMID:28497540	FYPO:0006423	decreased meiotic sister chromatid cohesion at centromere during meiosis I	(Fig. 1B)
PMID:28497540	GO:1990813	meiotic centromeric cohesion protection in anaphase I	(Fig. 1B)
PMID:28497540	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 20	(Fig. 1B)
PMID:28497540	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] ~10	(Fig. 1B)
PMID:28497540	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 30	(Fig. 1B, 1D)
PMID:28497540	FYPO:0006424	abolished meiotic sister chromatid cohesion at centromere during meiosis I	(Fig. 1C)
PMID:28497540	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 50	(Fig. 1C)
PMID:28497540	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] ~30	(Fig. 1D)
PMID:28497540	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 22-30	(Fig. 1E)
PMID:28497540	GO:1990813	meiotic centromeric cohesion protection in anaphase I	(Fig. 1E,F)
PMID:28497540	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] ~33	(Fig. 1F)
PMID:28497540	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] ~20	(Fig. 1F)
PMID:28497540	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPCC1322.12c	(Fig. 2B)
PMID:28497540	FYPO:0003606	decreased duration of meiotic prophase I	(Fig. 2B)
PMID:28497540	FYPO:0004214	normal protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPCC1322.12c	(Fig. 2B)
PMID:28497540	GO:0000776	kinetochore [exists_during] meiotic metaphase I	(Fig. 2b)
PMID:28497540	GO:0000776	kinetochore [exists_during] meiotic anaphase I	(Fig. 2b)
PMID:28497540	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC1020.02 [part_of] meiotic centromeric cohesion protection in anaphase I [happens_during] meiotic anaphase I	(Fig. 3A,B)
PMID:28497540	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	(Fig. 3C)
PMID:28497540	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	(Fig. 3C)
PMID:28497540	GO:0000776	kinetochore [exists_during] meiotic metaphase I	(Fig. 4A)
PMID:28497540	GO:0000776	kinetochore [exists_during] meiotic prometaphase I	(Fig. 4A)
PMID:28497540	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] ~20	(Fig. 5)
PMID:28497540	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 30	(Fig. 5)
PMID:28497540	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 50	(Fig. 5)
PMID:28497540	FYPO:0006423	decreased meiotic sister chromatid cohesion at centromere during meiosis I [has_severity] low	(Fig. 5C)
PMID:28497540	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 50	(Fig. 5C)
PMID:28497540	FYPO:0006423	decreased meiotic sister chromatid cohesion at centromere during meiosis I [has_severity] high	(Fig. 5C)
PMID:28497540	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC1020.02 [part_of] meiotic centromeric cohesion protection in anaphase I [happens_during] meiotic anaphase I	(Fig. E)
PMID:28497540	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPCC1322.12c	(Fig. S2A)
PMID:28497540	FYPO:0004763	abolished protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPCC1322.12c	(Fig. S4)
PMID:28497540	FYPO:0003606	decreased duration of meiotic prophase I	(Fig. S4)
PMID:28497540	FYPO:0004214	normal protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPBP35G2.03c	(Fig. S5)
PMID:28497540	FYPO:0004214	normal protein localization to kinetochore during meiosis I [assayed_using] PomBase:SPCC1322.12c	(Fig. S5)
PMID:28497540	FYPO:0007174	abnormal protein localization to kinetochore during mitotic interphase [assayed_using] PomBase:SPCC1322.12c	(comment: check during interphase)
PMID:28513584	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Fig. 1)
PMID:28513584	FYPO:0004085	decreased vegetative cell growth	(Fig. 1)
PMID:28513584	FYPO:0004395	short bipolar mitotic spindle during metaphase	(Fig. 2)
PMID:28513584	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. 2)
PMID:28513584	FYPO:0004395	short bipolar mitotic spindle during metaphase	(Fig. 2)
PMID:28513584	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Fig. 2)
PMID:28513584	FYPO:0006174	abolished mitotic spindle elongation during anaphase B	(Fig. 2)
PMID:28513584	FYPO:0000049	inviable cell	(Fig. 2)
PMID:28513584	FYPO:0001053	cut, normal size cell	(Fig. 2) (comment: main text)
PMID:28513584	FYPO:0006475	mitotic spindle collapse [has_penetrance] 15	(Fig. 3)
PMID:28513584	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_penetrance] 25	(Fig. 3)
PMID:28513584	FYPO:0001053	cut, normal size cell [has_penetrance] 80	(Fig. 3)
PMID:28513584	FYPO:0000049	inviable cell	(Fig. 3)
PMID:28513584	FYPO:0000131	abnormal mitotic spindle elongation [has_penetrance] 80	(Fig. 3)
PMID:28513584	FYPO:0000276	monopolar mitotic spindle	(Fig. S1)
PMID:28513584	FYPO:0001574	abnormal bipolar mitotic spindle	(Fig. S1) (comment: Not really abnormal, should be just bipolar)
PMID:28513584	GO:1990498	mitotic spindle microtubule [exists_during] mitotic prophase	(Fig. S3D) and the fact that is required for bipolar spindle formation
PMID:28513584	FYPO:0000049	inviable cell	(Fig. S3E)
PMID:28513584	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B	(Fig. S4)
PMID:28513584	FYPO:0002085	normal vegetative cell growth	(Fig. S4)
PMID:28513584	GO:0061804	mitotic spindle formation (spindle phase one)	(comment: CHECK cut7D pkl1D ase1D lethal)
PMID:28513584	GO:0061804	mitotic spindle formation (spindle phase one)	(comment: CHECK cut7D pkl1D cls1off lethal)
PMID:28513584	GO:0061805	mitotic spindle elongation (spindle phase three)	(comment: CHECK cut7D pkl1D klp9off does not elongate during anaphase B, cut7D pkl1D klp9D lethal, deleting all other kinesins except klp9 did not affect elongation after removing cut7)
PMID:28513584	FYPO:0000049	inviable cell	(comment: Main text (Figure S2 seems wrongly labelled))
PMID:28515144	FYPO:0002289	abolished protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC74.03c	(comment: Abolished ssp2-T189 phosphorylation under osmotic stress)
PMID:28515144	FYPO:0006718	increased duration of protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC74.03c	(comment: Increased duration of ssp2-T189 phosphorylation under osmotic stress)
PMID:28515144	FYPO:0006718	increased duration of protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC74.03c	(comment: Increased duration of ssp2-T189 phosphorylation under osmotic stress)
PMID:28515144	FYPO:0006718	increased duration of protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC74.03c	(comment: Increased duration of ssp2-T189 phosphorylation under osmotic stress)
PMID:28515144	FYPO:0002376	decreased protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC74.03c	(comment: Reduced ssp2-T189 phosphorylation under osmotic stress)
PMID:28515144	FYPO:0002376	decreased protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC74.03c	(comment: Reduced ssp2-T189 phosphorylation under osmotic stress)
PMID:28515144	FYPO:0006718	increased duration of protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC74.03c	(comment:Increased duration of ssp2-T189 phosphorylation under osmotic stress)
PMID:28533364	GO:0170008	mRNA phosphatase activator activity	Second, Dcp1 stabilizes the fold of the Dcp2 RD, especially around the split active site, as revealed by hydrogen deuterium exchange rates (SI Appendix, Fig. S13). Finally, Edc1 enforces the active orientation in Dcp2 (Fig. 1 B-D) through specific interaction between its YAG activation motif and Dcp2. ------ COMMENT: 0927ffeae1602f26 6 920Q9A21F/+7Ic0Fevc8Buw9Caw Second, Dcp1 stabilizes the fold of the Dcp2 RD, especially around the split active site, as revealed by hydrogen deuterium exchange rates (SI Appendix, Fig. S13). Finally, Edc1 enforces the active orientation in Dcp2 (Fig. 1 B-D) through specific interaction between its YAG activation motif and Dcp2.
PMID:28533364	GO:0170008	mRNA phosphatase activator activity	Second, Dcp1 stabilizes the fold of the Dcp2 RD, especially around the split active site, as revealed by hydrogen deuterium exchange rates (SI Appendix, Fig. S13). Finally, Edc1 enforces the active orientation in Dcp2 (Fig. 1 B–D) through specific interaction between its YAG activation motif and Dcp2.
PMID:28541282	GO:0140746	siRNA catabolic process	(Fig. 5d,e) Only in presence of cid14/16 does rrp6 degrade ago1 bound rnas. This mechanism protects the genome from uncontrolled small RNAs
PMID:28541282	GO:0140746	siRNA catabolic process	(comment: CHECK see comment on cid14)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1A, 1B)
PMID:28545058	FYPO:0000769	abnormal nuclear envelope morphology during vegetative growth	(Fig. 1C)
PMID:28545058	FYPO:0000769	abnormal nuclear envelope morphology during vegetative growth	(Fig. 1C)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio	(Fig. 1D)
PMID:28545058	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 2A)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio [has_severity] high	(Fig. 2A)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio [has_severity] high	(Fig. 2A)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio [has_severity] high	(Fig. 2A)
PMID:28545058	FYPO:0001221	normal nucleus:cytoplasm ratio [has_severity] high	(Fig. 2A, 2B)
PMID:28545058	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 2A, 2B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio [has_severity] high	(Fig. 2A, 2B)
PMID:28545058	FYPO:0003286	decreased mitotic chromosome condensation	(Fig. 3A)
PMID:28545058	FYPO:0000836	increased protein level	(Fig. 3A, 3B)
PMID:28545058	FYPO:0000836	increased protein level	(Fig. 3B, Table S4) mass spec used to show that there is bulk accumulation of nuclear localised protein rather than a few specific proteins
PMID:28545058	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 4A)
PMID:28545058	FYPO:0001673	normal nuclear morphology	(Fig. 4A, 4B)
PMID:28545058	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 4A, 4B)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio [has_severity] medium	(Fig. 4C) (comment: cut6-621 partial suppresses the increased NC ratio of rae1-167 so not sure whether increased NC ration is the correct term)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio [has_severity] high	(Fig. 4C, 4D)
PMID:28545058	FYPO:0000769	abnormal nuclear envelope morphology during vegetative growth [has_severity] medium	(Fig. 4D)
PMID:28545058	FYPO:0003751	normal nuclear envelope morphology [has_severity] medium	(Fig. 4D)
PMID:28545058	FYPO:0006926	increased nucleus:cytoplasm ratio [has_severity] medium	(Fig. 4c)
PMID:28545058	FYPO:0000836	increased protein level [has_severity] high [assayed_using] PomBase:SPAC57A7.04c	(Fig. S1C, S1D)
PMID:28545058	FYPO:0000911	increased nuclear RNA level during vegetative growth	Table S5
PMID:28545058	FYPO:0002061	inviable vegetative cell population	data not shown
PMID:28552615	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC23E6.02 [assayed_using] PomBase:SPBC365.06	(Fig. 2h)
PMID:28552615	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC23E6.02 [assayed_using] PomBase:SPBC365.06	(Fig. 2h)
PMID:28552615	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC23E6.02 [assayed_using] PomBase:SPBC365.06	(Fig. 2h)
PMID:28552615	FYPO:0003858	sensitive to etoposide [has_severity] medium	(Fig. 2i)
PMID:28552615	FYPO:0002778	decreased protein sumoylation during vegetative growth [assayed_using] PomBase:SPBC1A4.03c [has_severity] low	(Fig. 3a)
PMID:28552615	GO:0061995	ATP-dependent protein-DNA complex displacement activity	(Fig. 5) (comment: vw, added substrate top2, this term will probably merge into displacement activity)
PMID:28552615	FYPO:0001690	normal growth on camptothecin	(Fig. S1B)
PMID:28552615	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. S1B)
PMID:28552615	FYPO:0000963	normal growth on hydroxyurea	(Fig. S1B)
PMID:28552615	FYPO:0000969	normal growth during cellular response to UV	(Fig. S1B)
PMID:28552615	FYPO:0002775	decreased level of sumoylated protein in cell	(Fig. S1C)
PMID:28552615	FYPO:0002775	decreased level of sumoylated protein in cell	(Fig. S1C)
PMID:28552615	FYPO:0002775	decreased level of sumoylated protein in cell	(Fig. S1C)
PMID:28552615	FYPO:0002775	decreased level of sumoylated protein in cell	(Fig. S1C)
PMID:28552615	FYPO:0002775	decreased level of sumoylated protein in cell	(Fig. S1C)
PMID:28552615	FYPO:0002775	decreased level of sumoylated protein in cell	(Fig. S1C)
PMID:28552615	FYPO:0002775	decreased level of sumoylated protein in cell	(Fig. S1C)
PMID:28552615	FYPO:0002778	decreased protein sumoylation during vegetative growth [has_severity] high [assayed_using] PomBase:SPBC1A4.03c	(Fig. S1C, 3A)
PMID:28552615	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC1A4.03c [assayed_using] PomBase:SPBC23E6.02	(Fig. S1E)
PMID:28552615	GO:0003918	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity	(Figure 3F and G)
PMID:28552615	GO:0005515	protein binding	(Figure S2E)
PMID:28552615	GO:0061630	ubiquitin protein ligase activity [has_input] PomBase:SPBC1A4.03c	(comment: vw edited based on https://github.com/geneontology/go-annotation/issues/5239)
PMID:28552615	GO:0061630	ubiquitin protein ligase activity [has_input] PomBase:SPBC1A4.03c	(comment: vw edited based on https://github.com/geneontology/go-annotation/issues/5239)
PMID:28572514	GO:0005886	plasma membrane	(Fig. 5)
PMID:28572514	GO:0005628	prospore membrane	(Fig. 6)
PMID:28572514	GO:0000329	fungal-type vacuole membrane [exists_during] cellular response to copper ion starvation	(Fig. 6)
PMID:28572514	FYPO:0004931	normal RNA level during sporulation [assayed_enzyme] PomBase:SPAC821.10c	(Fig. 7)
PMID:28572514	FYPO:0004931	normal RNA level during sporulation [assayed_enzyme] PomBase:SPAC821.10c	(Fig. 7)
PMID:28572514	FYPO:0003282	decreased superoxide dismutase activity [assayed_enzyme] PomBase:SPAC821.10c	(Fig. 7)
PMID:28572514	FYPO:0003282	decreased superoxide dismutase activity [assayed_enzyme] PomBase:SPAC821.10c	(Fig. 7)
PMID:28572514	FYPO:0004931	normal RNA level during sporulation [assayed_enzyme] PomBase:SPAC821.10c	(Fig. 7)
PMID:28572514	FYPO:0003360	abolished superoxide dismutase activity [assayed_enzyme] PomBase:SPAC821.10c	(Fig. 9)
PMID:28572514	FYPO:0006210	decreased RNA level during cellular response to copper ion starvation during spore germination [assayed_using] PomBase:SPCC1393.10	(comment: vw: changed to match previous session terms RNA ...from cuf1Δ mutant spores showed loss of copper starvation-dependent induction of ctr4+ and ctr5+ gene expression, indicating that the copper-dependent reg ulation of ctr4+ and ctr5+ mRNAs required Cuf1 during germination and outgrowth.)
PMID:28572514	FYPO:0006210	decreased RNA level during cellular response to copper ion starvation during spore germination [assayed_using] PomBase:SPBC23G7.16	(comment: vw: changed to match previous session terms RNA ...from cuf1Δ mutant spores showed loss of copper starvation-dependent induction of ctr4+ and ctr5+ gene expression, indicating that the copper-dependent reg ulation of ctr4+ and ctr5+ mRNAs required Cuf1 during germination and outgrowth.)
PMID:28572514	FYPO:0006210	decreased RNA level during cellular response to copper ion starvation during spore germination [assayed_using] PomBase:SPAC1142.05	(comment: vw: changed to match previous session terms RNA ...from cuf1Δ mutant spores showed loss of copper starvation-dependent induction of ctr4+ and ctr5+ gene expression, indicating that the copper-dependent reg ulation of ctr4+ and ctr5+ mRNAs required Cuf1 during germination and outgrowth.)
PMID:28586299	FYPO:0006921	decreased gene conversion at mitotic DNA replication fork barriers	(Figure 2) decreased frequency of gene conversions but unaltered frequency of deletions at direct repeat recombination reporter; deletions in a rad51∆ mutant depend on Rad52
PMID:28586299	FYPO:0006920	decreased DNA recombination at mitotic DNA replication fork barriers	(Figure 4A) decreased frequency of deletions and gene conversions at direct repeat recombination reporter
PMID:28586299	FYPO:0006920	decreased DNA recombination at mitotic DNA replication fork barriers	(Figure 4B) decreased frequency of deletions at direct repeat recombination reporter
PMID:28586299	FYPO:0006920	decreased DNA recombination at mitotic DNA replication fork barriers	(Figure 4C) decreased frequency of gene conversions at direct repeat recombination reporter
PMID:28586299	FYPO:0000167	increased DNA recombination at mitotic DNA replication fork barriers	(Figure 4C) increased frequency of deletions at direct repeat recombination reporter
PMID:28600551	FYPO:0005968	resistance to sodium chloride	(Fig. 1)
PMID:28600551	FYPO:0005968	resistance to sodium chloride	(Fig. 1)
PMID:28600551	FYPO:0000852	resistance to salt stress	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	decreased cell population growth during glucose starvation	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	decreased cell population growth during glucose starvation	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	decreased cell population growth during glucose starvation	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	decreased cell population growth during glucose starvation	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	decreased cell population growth during glucose starvation	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	decreased cell population growth during glucose starvation	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0000852	resistance to salt stress	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	decreased cell population growth during glucose starvation [has_severity] low	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0003743	decreased cell population growth during glucose starvation	(Fig. 1) (comment: They say they use YES in methods and fig2)
PMID:28600551	FYPO:0000852	resistance to salt stress	(Fig. 1c)
PMID:28600551	FYPO:0001987	sensitive to high pH	(Fig. 1d)
PMID:28600551	FYPO:0001987	sensitive to high pH	(Fig. 1d)
PMID:28600551	FYPO:0001987	sensitive to high pH	(Fig. 1d)
PMID:28600551	FYPO:0005749	decreased protein phosphorylation during glucose starvation [assayed_using] PomBase:SPCC74.03c	(Fig. 2a)
PMID:28600551	FYPO:0006708	abolished protein phosphorylation during glucose starvation [assayed_using] PomBase:SPCC74.03c	(Fig. 2a)
PMID:28600551	FYPO:0005749	decreased protein phosphorylation during glucose starvation [assayed_using] PomBase:SPCC74.03c	(Fig. 2a)
PMID:28600551	FYPO:0005749	decreased protein phosphorylation during glucose starvation [assayed_using] PomBase:SPCC74.03c	(Fig. 2a)
PMID:28600551	FYPO:0003214	normal protein phosphorylation during cellular response to glucose starvation [assayed_using] PomBase:SPCC74.03c	(Fig. 2a)
PMID:28600551	FYPO:0002446	decreased protein phosphorylation during cellular response to hydrogen peroxide [assayed_using] PomBase:SPCC74.03c	(Fig. 2c)
PMID:28600551	FYPO:0006232	abolished protein phosphorylation during cellular response to hydrogen peroxide [assayed_using] PomBase:SPCC74.03c	(Fig. 2c)
PMID:28600551	FYPO:0006709	abolished protein phosphorylation during cellular response to salt stress [assayed_using] PomBase:SPCC74.03c	(Fig. 2d)
PMID:28600551	FYPO:0001885	decreased protein phosphorylation during salt stress [assayed_using] PomBase:SPCC74.03c	(Fig. 2d)
PMID:28600551	FYPO:0006711	abolished protein phosphorylation during cellular response to alkaline pH [assayed_using] PomBase:SPCC74.03c	(Fig. 2e)
PMID:28600551	FYPO:0006710	decreased protein phosphorylation during cellular response to alkaline pH [assayed_using] PomBase:SPCC74.03c	(Fig. 2e)
PMID:28600551	FYPO:0004765	normal cell population growth during glucose starvation	(Fig. 3c)
PMID:28600551	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPCC622.16c	(Fig. 3d)
PMID:28600551	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPCC622.16c	(Fig. 3d)
PMID:28600551	FYPO:0003743	decreased cell population growth during glucose starvation [has_severity] low	(Fig. 4)
PMID:28600551	FYPO:0005749	decreased protein phosphorylation during glucose starvation [assayed_using] PomBase:SPCC74.03c	(Fig. 4)
PMID:28600551	FYPO:0005749	decreased protein phosphorylation during glucose starvation [assayed_using] PomBase:SPCC74.03c	(Fig. 4)
PMID:28600551	FYPO:0004765	normal cell population growth during glucose starvation	(Fig. 4)
PMID:28600551	FYPO:0004765	normal cell population growth during glucose starvation	(Fig. 4)
PMID:28600551	FYPO:0003743	decreased cell population growth during glucose starvation [has_severity] low	(Fig. 4)
PMID:28600551	FYPO:0003743	decreased cell population growth during glucose starvation [has_severity] low	(Fig. 4)
PMID:28600551	FYPO:0003743	decreased cell population growth during glucose starvation [has_severity] low	(Fig. 4)
PMID:28600551	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPCC74.03c	(Fig. 5)
PMID:28600551	FYPO:0006714	increased cellular free fatty acid level	(Fig. 5)
PMID:28600551	FYPO:0000584	decreased sporulation frequency	(Fig. 5)
PMID:28600551	FYPO:0000584	decreased sporulation frequency	(Fig. 5)
PMID:28600551	FYPO:0000584	decreased sporulation frequency	(Fig. 5)
PMID:28600551	FYPO:0006712	decreased cellular acetyl-CoA level [has_severity] low	(Fig. 5)
PMID:28600551	FYPO:0006712	decreased cellular acetyl-CoA level	(Fig. 5)
PMID:28600551	FYPO:0006712	decreased cellular acetyl-CoA level	(Fig. 5)
PMID:28600551	FYPO:0006713	increased cellular malonyl-CoA level [has_severity] low	(Fig. 5)
PMID:28600551	FYPO:0006713	increased cellular malonyl-CoA level	(Fig. 5)
PMID:28600551	FYPO:0006713	increased cellular malonyl-CoA level	(Fig. 5)
PMID:28600551	FYPO:0006714	increased cellular free fatty acid level	(Fig. 5)
PMID:28600551	FYPO:0006714	increased cellular free fatty acid level	(Fig. 5)
PMID:28600551	FYPO:0000303	decreased conjugation frequency [has_severity] low	(Fig. 5)
PMID:28600551	FYPO:0000303	decreased conjugation frequency	(Fig. 5)
PMID:28600551	FYPO:0000303	decreased conjugation frequency	(Fig. 5)
PMID:28600551	FYPO:0001424	abolished protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPCC74.03c	(Fig. 5)
PMID:28600551	FYPO:0001514	decreased protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPCC74.03c	(Fig. 5)
PMID:28600551	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPCC74.03c	(Fig. 5)
PMID:28600551	FYPO:0005968	resistance to sodium chloride	(comment: I can never remember why e.g. sodium chloride isn't a child to salt stress)
PMID:28619713	FYPO:0005380	normal mitotic spindle pole body duplication [has_penetrance] 38	(Fig. 6C)
PMID:28619713	FYPO:0001791	abnormal mitotic spindle pole body duplication	(Fig. 6C)
PMID:28619713	GO:0061496	half bridge of mitotic spindle pole body	(Fig. S1B)
PMID:28619713	GO:0061496	half bridge of mitotic spindle pole body	(Fig. S1B)
PMID:28619713	GO:0140480	mitotic spindle pole body insertion into the nuclear envelope	(comment: rename CHECK term https://github.com/geneontology/go-ontology/issues/14887) Our data suggest that Sad1 is present at the SPB early to set up structures that will trigger SPB insertion before the cell even enters mitosis.fig6
PMID:28619713	GO:0140480	mitotic spindle pole body insertion into the nuclear envelope	Our data suggest that Sad1 is present at the SPB early to set up structures that will trigger SPB insertion before the cell even enters mitosis.fig6
PMID:28631612	GO:0005737	cytoplasm [part_of] ascospore	"(comment: ""antidote"" product of longer alternative transcript; assayed by expressing S.k. ortholog in S.p.)"
PMID:28631612	GO:0072324	ascus epiplasm	"(comment: ""poison"" product of shorter alternative transcript;assayed by expressing S.k. ortholog in S.p.)"
PMID:28640807	FYPO:0003238	decreased anaerobic cell population growth	(comment: CHECK 2 mM Glutathione restores aerobic growth.)
PMID:28640807	FYPO:0003238	decreased anaerobic cell population growth [has_severity] low	(comment: CHECK 2 mM Glutathione restores aerobic growth.)
PMID:28640807	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: CHECK aerobic conditions)
PMID:28640807	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: CHECK aerobic conditions)
PMID:28640807	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: CHECK aerobic conditions)
PMID:28640807	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: CHECK aerobic conditions)
PMID:28640807	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: CHECK aerobic conditions)
PMID:28640807	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: CHECK aerobic conditions)
PMID:28640807	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: CHECK aerobic conditions)
PMID:28640807	FYPO:0006115	increased protein oxidation during mitotic S phase [assayed_using] PomBase:SPAC1F7.05 [has_severity] high	Increased Cdc22 oxidation attenuated by 2 mM Glutathione. Increased Cdc22 oxidation attenuated by deleting tpx1.
PMID:28640807	FYPO:0006115	increased protein oxidation during mitotic S phase [assayed_using] PomBase:SPAC1F7.05 [has_severity] high	Increased Cdc22 oxidation attenuated by 2 mM Glutathione. Increased Cdc22 oxidation attenuated by deleting tpx1.
PMID:28652406	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPCC757.07c	(comment: CHECK ditto)
PMID:28652406	FYPO:0000087	sensitive to hydrogen peroxide	(comment: CHECK ditto)
PMID:28652406	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAP8A3.04c	(comment: CHECK ditto)
PMID:28652406	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC215.05	(comment: CHECK ditto)
PMID:28652406	FYPO:0004571	increased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAP8A3.04c	(comment: CHECK ditto)
PMID:28652406	FYPO:0007382	normal transcription regulatory region sequence-specific DNA binding [assayed_using] PomBase:SPBC29B5.01	(comment: CHECK ditto)
PMID:28652406	FYPO:0001280	decreased RNA level during cellular response to oxidative stress [assayed_using] PomBase:SPBC106.02c	(comment: CHECK ditto)
PMID:28652406	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC106.02c	(comment: CHECK ditto)
PMID:28652406	FYPO:0000962	normal growth on hydrogen peroxide	(comment: vw, I deleted Caludias annotation by mistake when comparing to the older partially completed session by Laura, so adding back !)
PMID:28652406	FYPO:0002003	abolished RNA polymerase II proximal promoter sequence-specific DNA binding [assayed_using] PomBase:SPBC29B5.01	....whereas it is never recruited to these promoters in cells expressing Pap1.C523D (Fig. 5D).
PMID:28652406	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC106.02c	2A,cells expressing the hypophosphorylation mutant HA-Atf1.10M are not able to fully trigger the ctt1 and srx1 genes after H2O2 stress
PMID:28652406	FYPO:0004052	RNA absent from cell during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC215.05	As shown in Fig. 2B, the capacity of HA-Atf1.10M to activate hsp9 and gpd1 after stress imposition was abolished in the absence of Sty1
PMID:28652406	FYPO:0004052	RNA absent from cell during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAP8A3.04c	As shown in Fig. 2B, the capacity of HA-Atf1.10M to activate hsp9 and gpd1 after stress imposition was abolished in the absence of Sty1
PMID:28652406	FYPO:0005048	increased protein localization to chromatin at RNA polymerase II promoter during vegetative growth [assayed_using] PomBase:SPBC29B5.01	Atf1 is constitutively bound to srx1 and ctt1 in strain Δtrr1....
PMID:28652406	FYPO:0007382	normal transcription regulatory region sequence-specific DNA binding [assayed_using] PomBase:SPBC29B5.01	Atf1.7M-HA are constitutively bound to the gpd1 and hsp9 promoters both before and after stress
PMID:28652406	FYPO:0000962	normal growth on hydrogen peroxide	Concomitantly, although expression of HA-Atf1.10M was not able to suppress the sensitivity to peroxides of strain Δatf1 (supplemental Fig. S1C and Fig. 1G), expression of HAAtf1.10D alleviated this phenotype (Fig. 1G).
PMID:28652406	FYPO:0004571	increased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC215.05	Importantly, expression of the phospho-mimicking HA-Atf1.10D (Fig. 2B) or HA-Atf1.6D (Fig S3, C and D) bypasses the requirement for a MAP kinase in the transcription process, which questions the direct participation of the kinase in Pol II initiation and/or elongation.
PMID:28652406	FYPO:0002003	abolished RNA polymerase II proximal promoter sequence-specific DNA binding [assayed_using] PomBase:SPBC29B5.01	Regarding the role of Pap1 and Atf1 at these genes, ChIP analysis indicates that the stress-dependent recruitment of Atf1 to ctt1 and srx1 promoters is dependent on Pap1 (Fig. 5C).
PMID:28652406	FYPO:0004571	increased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC215.05	Strains expressing wild-type Atf1 or Atf1.7M or Atf1.7D mutants displayed the same patterns of tolerance to peroxides and activation of stress genes as the constitutive amino-terminally tagged versions (supplemental Fig S4, B and C).
PMID:28652406	FYPO:0004571	increased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC215.05	allows stress-dependent activation of ctt1 and srx1 to the same extent as wild-type cells; however, it constitutively induces expression of gpd1 and hsp9 (Fig. 2A).
PMID:28652406	FYPO:0004571	increased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAP8A3.04c	allows stress-dependent activation of ctt1 and srx1 to the same extent as wild-type cells; however, it constitutively induces expression of gpd1 and hsp9 (Fig. 2A).
PMID:28652406	FYPO:0000962	normal growth on hydrogen peroxide	expression of HA-Atf1.10D fully suppressed all stress defects of cells lacking Sty1 (Fig. 2C).
PMID:28652406	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPCC757.07c	expression of the Sty1-independent Atf1.7D-HA mutant cannot bypass the absence of Pcr1, as shown by the lack of transcription of stress genes (Fig. 4C).
PMID:28652406	FYPO:0001280	decreased RNA level during cellular response to oxidative stress [assayed_using] PomBase:SPCC757.07c	that Pap1 is dispensable for the activation of gpd1 and hsp9 but required for ctt1 and srx1 (Fig. 5A)
PMID:28652406	FYPO:0000087	sensitive to hydrogen peroxide	the HA-Atf1.1M mutant was fully able to suppress the sensitivity to peroxides of strain Δatf1, expression of the HA-Atf1.10M and 11M mutants did not alleviate this phenotype (supplemental Fig. S1C).
PMID:28652406	FYPO:0001485	normal cellular response to oxidative stress	the HA-Atf1.1M mutant was fully able to suppress the sensitivity to peroxides of strain Δatf1, expression of the HA-Atf1.10M and 11M mutants did not alleviate this phenotype (supplemental Fig. S1C).
PMID:28652406	FYPO:0000087	sensitive to hydrogen peroxide	the HA-Atf1.1M mutant was fully able to suppress the sensitivity to peroxides of strain Δatf1, expression of the HA-Atf1.10M and 11M mutants did not alleviate this phenotype (supplemental Fig. S1C).
PMID:28652406	FYPO:0004571	increased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC215.05	whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly
PMID:28652406	FYPO:0004571	increased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAP8A3.04c	whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly
PMID:28652406	FYPO:0004571	increased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPCC757.07c	whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly
PMID:28652406	FYPO:0004571	increased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC106.02c	whereas the expression of all stress genes in cells expressing HAAtf1.10D was not altered by sty1 deletion. Concomitantly
PMID:28652406	FYPO:0002003	abolished RNA polymerase II proximal promoter sequence-specific DNA binding [assayed_using] PomBase:SPBC29B5.01	whether Atf1 binding to DNA is dependent on the presence of Pcr1; as shown in Fig. 4D, Atf1-GFP is not recruited to DNA in Δpcr1 cells, with the only exception of srx1
PMID:28652406	FYPO:0000087	sensitive to hydrogen peroxide	Δatf1 expressing the mutant named HA-Atf1.6M, lacking sites 5 to 10 in Atf1, was as sensitive to growth on peroxide-containing plates as cells lacking Atf1.
PMID:28656962	FYPO:0001357	normal vegetative cell population growth	(Figure 5b)
PMID:28656962	FYPO:0001357	normal vegetative cell population growth	(Figure 5b)
PMID:28656962	FYPO:0001357	normal vegetative cell population growth	(Figure 5b)
PMID:28656962	FYPO:0001355	decreased vegetative cell population growth	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	FYPO:0001355	decreased vegetative cell population growth	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	FYPO:0001355	decreased vegetative cell population growth	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	FYPO:0001355	decreased vegetative cell population growth	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	FYPO:0001355	decreased vegetative cell population growth	Strains lacking Ypt7 (ypt7Δ, bhd1Δ ypt7Δ, ypt71Δ ypt7Δ) displayed a significant growth defect in the low amino-acid condition (EMM plates supplemented with low concentration of amino acids) compared to WT strains, or bhd1Δ and ypt71Δ strains (Fig. 5b).
PMID:28656962	GO:1904262	negative regulation of TORC1 signaling [happens_during] cellular response to amino acid starvation	These data suggest that Bhd1 and Ypt71 (but not Ypt7) functionally interact and, in agreement with the mammalian cell data, negatively regulate TORC1 activity in response to amino-acid deprivation.
PMID:28656962	GO:1904262	negative regulation of TORC1 signaling [happens_during] cellular response to amino acid starvation	These data suggest that Bhd1 and Ypt71 (but not Ypt7) functionally interact and, in agreement with the mammalian cell data, negatively regulate TORC1 activity in response to amino-acid deprivation.
PMID:28656962	FYPO:0000077	resistance to rapamycin	To determine whether these proteins are related to TORC1 signalling, we treated bhd1Δ, ypt71Δ, ypt7Δ and double deletion strains with 200 ng ml−1 of rapamycin and found that all of the strains grew better than WT cells (Fig. 5b).
PMID:28656962	FYPO:0000077	resistance to rapamycin	To determine whether these proteins are related to TORC1 signalling, we treated bhd1Δ, ypt71Δ, ypt7Δ and double deletion strains with 200 ng ml−1 of rapamycin and found that all of the strains grew better than WT cells (Fig. 5b).
PMID:28656962	FYPO:0000077	resistance to rapamycin	To determine whether these proteins are related to TORC1 signalling, we treated bhd1Δ, ypt71Δ, ypt7Δ and double deletion strains with 200 ng ml−1 of rapamycin and found that all of the strains grew better than WT cells (Fig. 5b).
PMID:28656962	FYPO:0007907	increased protein phosphorylation during amino acid starvation [assayed_protein] PomBase:SPAC13G6.07c	We observed that loss of Bhd1 and Ypt71, but not Ypt7, resulted in increased TORC1 activity, as determined by an increase in Rps6 and p70 S6K phosphorylation levels when cells were deprived of amino acids (Fig. 5a, compare lanes 1, 3, 5 and 7).
PMID:28656962	FYPO:0007907	increased protein phosphorylation during amino acid starvation [assayed_protein] PomBase:SPAPB1E7.12	We observed that loss of Bhd1 and Ypt71, but not Ypt7, resulted in increased TORC1 activity, as determined by an increase in Rps6 and p70 S6K phosphorylation levels when cells were deprived of amino acids (Fig. 5a, compare lanes 1, 3, 5 and 7).
PMID:28659415	GO:0070941	eisosome assembly	(comment: Pil1p form filaments. Pil1 exchanges rapidly at the ends of these filaments in vivo)
PMID:28659415	GO:0036286	eisosome filament	(comment: Pil1p form filaments. Pil1 exchanges rapidly at the ends of these filaments in vivo)
PMID:28674280	FYPO:0006355	delayed onset of transcription during glucose starvation [assayed_using] PomBase:SPBC1198.14c	(comment: CHECK same as snf22delta alone)
PMID:28674280	FYPO:0006355	delayed onset of transcription during glucose starvation [assayed_using] PomBase:SPBC1198.14c	(comment: CHECK same as snf22delta alone)
PMID:28674280	FYPO:0006355	delayed onset of transcription during glucose starvation [assayed_using] PomBase:SPBC1198.14c	(comment: same as snf22delta alone)
PMID:28682306	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth	Both H3K9me2 and me3 reads mapping specifically to unique sequences at the silent mating-type locus and telomeric DNA regions were drastically reduced (Extended Data Fig. 3a)
PMID:28682306	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth	Both H3K9me2 and me3 reads mapping specifically to unique sequences at the silent mating-type locus and telomeric DNA regions were drastically reduced (Extended Data Fig. 3a)
PMID:28682306	FYPO:0002355	decreased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth	Both H3K9me2 and me3 reads mapping specifically to unique sequences at the silent mating-type locus and telomeric DNA regions were drastically reduced (Extended Data Fig. 3a)
PMID:28682306	FYPO:0002355	decreased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth	Both H3K9me2 and me3 reads mapping specifically to unique sequences at the silent mating-type locus and telomeric DNA regions were drastically reduced (Extended Data Fig. 3a)
PMID:28682306	FYPO:0004137	decreased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth	Both H3K9me2 and me3 reads mapping specifically to unique sequences at the silent mating-type locus and telomeric DNA regions were drastically reduced (Extended Data Fig. 3b-g)
PMID:28682306	FYPO:0004137	decreased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth	Both H3K9me2 and me3 reads mapping specifically to unique sequences at the silent mating-type locus and telomeric DNA regions were drastically reduced (Extended Data Fig. 3b-g)
PMID:28682306	FYPO:0004577	decreased histone H3-K9 trimethylation at subtelomeric heterochromatin during vegetative growth	Both H3K9me2 and me3 reads mapping specifically to unique sequences at the silent mating-type locus and telomeric DNA regions were drastically reduced (Extended Data Fig. 3b-g)
PMID:28682306	FYPO:0004577	decreased histone H3-K9 trimethylation at subtelomeric heterochromatin during vegetative growth	Both H3K9me2 and me3 reads mapping specifically to unique sequences at the silent mating-type locus and telomeric DNA regions were drastically reduced (Extended Data Fig. 3b-g)
PMID:28682306	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPBC428.08c [has_severity] high	ChIP experiments also revealed that in contrast to greatly reduced association of Clr4(W31G) with ­ chromatin, Clr4(F449Y) associated with pericentromeric DNA repeats at levels close to that of wild-type Clr4, demonstrating that Clr4 can bind to H3K9me2 via its chromodomain (Fig. 3i; Extended Data Fig. 9g).
PMID:28682306	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPBC428.08c [has_severity] low	ChIP experiments also revealed that in contrast to greatly reduced association of Clr4(W31G) with ­ chromatin, Clr4(F449Y) associated with pericentromeric DNA repeats at levels close to that of wild-type Clr4, demonstrating that Clr4 can bind to H3K9me2 via its chromodomain (Fig. 3i; Extended Data Fig. 9g).
PMID:28682306	FYPO:0010018	increased histone H3-K36 trimethylation at centromere outer repeat during vegetative growth	ChIP–seq and ChIP–qPCR showed increased levels of transcription-associated H3K4me3, H3K36me3, H3K14 ­ acetylation (H3K14ac), and H4K16ac in clr4F449Y relative to clr4+ cells (Fig. 2d, e; Extended Data Fig. 5e–h).
PMID:28682306	FYPO:0000966	increased histone H3-K14 acetylation at centromere outer repeat during vegetative growth	ChIP–seq and ChIP–qPCR showed increased levels of transcription-associated H3K4me3, H3K36me3, H3K14 ­ acetylation (H3K14ac), and H4K16ac in clr4F449Y relative to clr4+ cells (Fig. 2d, e; Extended Data Fig. 5e–h).
PMID:28682306	FYPO:0010013	increased histone H3-K4 trimethylation at centromere outer repeat during vegetative growth	ChIP–seq and ChIP–qPCR showed increased levels of transcription-associated H3K4me3, H3K36me3, H3K14 ­ acetylation (H3K14ac), and H4K16ac in clr4F449Y relative to clr4+ cells (Fig. 2d, e; Extended Data Fig. 5e–h).
PMID:28682306	FYPO:0007311	increased histone H4-K16 acetylation at centromere outer repeat during vegetative growth	ChIP–seq and ChIP–qPCR showed increased levels of transcription-associated H3K4me3, H3K36me3, H3K14 ­ acetylation (H3K14ac), and H4K16ac in clr4F449Y relative to clr4+ cells (Fig. 2d, e; Extended Data Fig. 5e–h).
PMID:28682306	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] medium [assayed_protein] PomBase:SPBC16C6.10	Chp2 recruitment was also impaired, but to a lesser extent (Fig. 3b; Extended Data Fig. 9c).
PMID:28682306	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC428.08c [assayed_protein] PomBase:SPAC664.01c	Clr4(F449Y) was incorporated into the CLRC methyltransferase complex and inter- acted with Swi6 with efficiency similar to wild-type Clr4 (Extended Data Fig. 1b, c).
PMID:28682306	FYPO:0000874	increased histone H3-K9 dimethylation at centromere during vegetative growth	Furthermore, chromatin immu- noprecipitation followed by high throughput sequencing (ChIP–seq) or quantitative PCR (ChIP–qPCR) showed that while pericentromeric H3K9me2 levels were increased in clr4 mutants relative to clr4+ cells (Fig. 1c; Extended Data Fig. 2a, b)
PMID:28682306	FYPO:0000874	increased histone H3-K9 dimethylation at centromere during vegetative growth	Furthermore, chromatin immu- noprecipitation followed by high throughput sequencing (ChIP–seq) or quantitative PCR (ChIP–qPCR) showed that while pericentromeric H3K9me2 levels were increased in clr4 mutants relative to clr4+ cells (Fig. 1c; Extended Data Fig. 2a, b)
PMID:28682306	FYPO:0000883	decreased histone H3-K9 trimethylation at centromere during vegetative growth	Furthermore, chromatin immu- noprecipitation followed by high throughput sequencing (ChIP–seq) or quantitative PCR (ChIP–qPCR) showed that while pericentromeric H3K9me2 levels were increased in clr4 mutants relative to clr4+ cells (Fig. 1c; Extended Data Fig. 2a, b)H3K9me3 was lost in clr4F449Y cells and reduced in clr4I418P cells (Fig. 1d; Extended Data Fig. 2c).
PMID:28682306	FYPO:0008368	abolished histone H3-K9 trimethylation at centromere during vegetative growth	Furthermore, chromatin immu- noprecipitation followed by high throughput sequencing (ChIP–seq) or quantitative PCR (ChIP–qPCR) showed that while pericentromeric H3K9me2 levels were increased in clr4 mutants relative to clr4+ cells (Fig. 1c; Extended Data Fig. 2a, b)H3K9me3 was lost in clr4F449Y cells and reduced in clr4I418P cells (Fig. 1d; Extended Data Fig. 2c).
PMID:28682306	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	Furthermore, the pericentromeric recruitment of the RITS complex subunits Chp1 was increased in both clr4F449Y and clr4I418P cells, presumably owing to increased H3K9me2 (Fig. 2c; Extended Data Fig. 5a–c)
PMID:28682306	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC18G6.02c	Furthermore, the pericentromeric recruitment of the RITS complex subunits Chp1 was increased in both clr4F449Y and clr4I418P cells, presumably owing to increased H3K9me2 (Fig. 2c; Extended Data Fig. 5a–c)
PMID:28682306	FYPO:0000882	decreased histone H3-K9 trimethylation during vegetative growth	Immunoblotting and quantitative mass spectrometry of an enriched histone fraction showed that H3K9me3 levels were dramatically decreased in clr4F449Y cells, while H3K9me2 levels were increased (Extended Data Fig. 1d, e).
PMID:28682306	FYPO:0000873	increased histone H3-K9 dimethylation during vegetative growth	Immunoblotting and quantitative mass spectrometry of an enriched histone fraction showed that H3K9me3 levels were dramatically decreased in clr4F449Y cells, while H3K9me2 levels were increased (Extended Data Fig. 1d, e).
PMID:28682306	FYPO:0000890	decreased histone H3-K9 trimethylation at centromere outer repeat during vegetative growth [has_severity] high	In cells with stably expressed Clr4 carrying a W31G mutation in its chromodomain (Extended Data Fig. 1a), we observed a ­ drastic loss of H3K9me3, but not H3K9me2, throughout pericentro- meric DNA repeats, demonstrating that the interaction of Clr4 with the RNAi machinery was sufficient for its recruitment and H3K9me2 catalysis (Fig. 3g, h; Extended Data Fig. 9e, f).
PMID:28682306	FYPO:0000887	increased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	In cells with stably expressed Clr4 carrying a W31G mutation in its chromodomain (Extended Data Fig. 1a), we observed a ­ drastic loss of H3K9me3, but not H3K9me2, throughout pericentro- meric DNA repeats, demonstrating that the interaction of Clr4 with the RNAi machinery was sufficient for its recruitment and H3K9me2 catalysis (Fig. 3g, h; Extended Data Fig. 9e, f).
PMID:28682306	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPAC664.01c [has_severity] high	In clr4F449Y cells, Swi6 association with pericentromeric dh repeats was nearly abolished, while its associ- ation with dg repeats was reduced by about threefold (Fig. 3a; Extended Data Fig. 9a).
PMID:28682306	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] medium [assayed_protein] PomBase:SPBC800.03	Moreover, the reduced Swi6 and Chp2 recruit- ment to pericentromeric DNA repeats in clr4F449Y cells was accom- panied by a reduction in Clr3 recruitment (Fig. 3c; Extended Data Fig. 9d).
PMID:28682306	FYPO:0007376	abolished epigenetic heterochromatin inheritance	Notably, replacement of clr4+ with clr4F449Y or clr4I418P abolished the epigenetic inheritance of ade6+ silencing (Fig. 4b, right).
PMID:28682306	FYPO:0007376	abolished epigenetic heterochromatin inheritance	Notably, replacement of clr4+ with clr4F449Y or clr4I418P abolished the epigenetic inheritance of ade6+ silencing (Fig. 4b, right). (Fig. 4c, 4d)
PMID:28682306	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] high	Similar to ∆ clr4 cells, clr4F449Y cells displayed increased growth on plateslacking uracil and grew poorly on FOA plates (Fig. 1e, left) indicatinga loss of otr1R::ura4+ silencing. (Fig. 1f, g)
PMID:28682306	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] medium	Similar to ∆ clr4 cells, clr4F449Y cells displayed increased growth on plateslacking uracil and grew poorly on FOA plates (Fig. 1e, left) indicatinga loss of otr1R::ura4+ silencing. (Fig. 1f, g)
PMID:28682306	FYPO:0007376	abolished epigenetic heterochromatin inheritance	Similarly, consistent with previous results using Clr4 ­ lackingits chromodomain27,28, replacement of clr4+ with clr4W31G abolishedheterochromatin maintenance (Fig. 4b). (Fig. 4c, 4d)
PMID:28682306	FYPO:0010014	increased histone H3-K9 monomethylation during vegetative growth	We also detected high levels of H3K9me1 in both clr4+ and ∆clr4 cells (Extended Data Fig. 6b)
PMID:28682306	FYPO:0004745	abolished histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	We observed a complete loss of H3K9me2 when the clr4I418P mutant was combined with ∆ago1 (Fig. 4e, bottom rows; Extended Data Fig. 10c)
PMID:28682306	FYPO:0004745	abolished histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	We observed a complete loss of H3K9me2 when the clr4I418P mutant was combined with ∆ago1 (Fig. 4e, bottom rows; Extended Data Fig. 10c)
PMID:28682306	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] low	lr4I418P had a milder silencing defect, consistent with partial loss of H3K9me3 in this mutant (Fig. 1d, e). (Fig. 1f, g)
PMID:28765164	FYPO:0002133	abolished protein-RNA interaction [assayed_enzyme] PomBase:SPCC736.12c [assayed_substrate] PomBase:SPNCRNA.1459	(Fig. 2e)
PMID:28765280	FYPO:0002060	viable vegetative cell population	(Fig. 1A)
PMID:28765280	FYPO:0000673	normal septum assembly	(Fig. 1B)
PMID:28765280	FYPO:0002060	viable vegetative cell population	(Fig. 1B)
PMID:28765280	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC17G8.12	(Fig. 1E,F)
PMID:28765280	FYPO:0002060	viable vegetative cell population	(Fig. 2A)
PMID:28765280	FYPO:0002060	viable vegetative cell population	(Fig. 6A)
PMID:28765280	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPAC17G8.12	(Fig. 6C)
PMID:28765280	FYPO:0000673	normal septum assembly	(Fig. 6C)
PMID:28765280	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPAC17G8.12	(Fig. 6G).
PMID:28765280	FYPO:0002060	viable vegetative cell population	(Fig. 7A)
PMID:28765280	GO:0004843	cysteine-type deubiquitinase activity [has_input] PomBase:SPAC17G8.12 [part_of] cytoplasm protein quality control by the ubiquitin-proteasome system	(Fig. 7A)
PMID:28765280	GO:0004843	cysteine-type deubiquitinase activity [has_input] PomBase:SPAC17G8.12 [part_of] cytoplasm protein quality control by the ubiquitin-proteasome system	(Fig. 7A)
PMID:28765280	FYPO:0002060	viable vegetative cell population	(Fig. 7A)
PMID:28765280	FYPO:0002061	inviable vegetative cell population	(Figure 1B)
PMID:28765280	FYPO:0002060	viable vegetative cell population	(Figure 1D)
PMID:28765280	FYPO:0000118	multiseptate vegetative cell [has_penetrance] high	(Figure 2)
PMID:28765280	FYPO:0002086	exocytic vesicles present in increased numbers [has_penetrance] high	(Figure 3b)
PMID:28765280	FYPO:0002086	exocytic vesicles present in increased numbers [has_penetrance] medium	(Figure 3b)
PMID:28765280	GO:0061630	ubiquitin protein ligase activity [part_of] cytoplasm protein quality control by the ubiquitin-proteasome system [has_input] PomBase:SPAC17G8.12	(Figure 6E,F)
PMID:28771613	MOD:00696	phosphorylated residue [added_during] cellular response to leucine starvation	(Figure 1E)
PMID:28771613	FYPO:0002898	abolished protein phosphorylation during cellular response to DNA damage [assayed_using] PomBase:SPAC3G9.09c	(Figure 1E)
PMID:28771613	MOD:00696	phosphorylated residue [added_during] negative regulation of translation [added_by] PomBase:SPBC36B7.09	(Figure 1E)
PMID:28771613	FYPO:0006398	abolished protein phosphorylation during cellular response to leucine starvation [assayed_using] PomBase:SPAC3G9.09c	(Figure 2B)
PMID:28771613	GO:0030295	protein kinase activator activity [has_input] PomBase:SPBC36B7.09 [part_of] negative regulation of cytoplasmic translational initiation in response to stress [happens_during] cellular response to amino acid starvation	(comment: unfortunately no direct binding data, but physical interactions have been shown in other organisms)
PMID:28771613	FYPO:0005179	abnormal mitotic cell cycle regulation during cellular response to UV during mitotic G1 phase [assayed_using] PomBase:SPAC3G9.09c	The preRC- loading delay was abolished in the irradiated gcn1Δ cells (Fig 3C)
PMID:28771613	FYPO:0005179	abnormal mitotic cell cycle regulation during cellular response to UV during mitotic G1 phase [assayed_using] PomBase:SPAC3G9.09c	The preRC- loading delay was abolished in the irradiated gcn1Δ cells (Fig 3C)
PMID:28775153	FYPO:0000229	cut	(Fig. 4B) DAPI staining. (comment: CHECK I have requested a new term and included response to streptonigrin but should it be more general e.g. response to DNA damaging agent (if this is known))
PMID:28775153	FYPO:0006865	normal mitotic DNA damage checkpoint during cellular response to streptonigrin	(Fig. 4C) DAPI staining. (comment: CHECK I have requested a new term and included response to streptonigrin but should it be more general e.g. response to DNA damaging agent (if this is known))
PMID:28775153	FYPO:0000229	cut	(Fig. 4D) DAPI staining. (comment: CHECK I have requested a new term and included response to streptonigrin but should it be more general e.g. response to DNA damaging agent (if this is known))
PMID:28784611	FYPO:0004293	mislocalized septum	(Fig. 1A, 1B)
PMID:28784611	GO:0005886	plasma membrane	(Fig. 1B)
PMID:28784611	FYPO:0005289	actomyosin contractile ring sliding [has_penetrance] 43 [has_severity] high	(Fig. 2A-C)
PMID:28784611	FYPO:0005289	actomyosin contractile ring sliding [has_penetrance] 40	(Fig. 2A-C)
PMID:28784611	FYPO:0005289	actomyosin contractile ring sliding [has_penetrance] 43	(Fig. 2A-C)
PMID:28784611	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPAC2F7.03c	(Fig. 3A) (in table, data not shown)
PMID:28784611	FYPO:0002253	normal septum location	(Fig. 5A)
PMID:28784611	FYPO:0006005	normal actomyosin contractile ring localization	(Fig. 5B) CR sliding events no longer occurred in myo51Δ efr3Δ
PMID:28784611	FYPO:0006005	normal actomyosin contractile ring localization	(Fig. 5B) CR sliding events no longer occurred in myo51Δ efr3Δ
PMID:28784611	FYPO:0002061	inviable vegetative cell population	(Fig. S1C, S1D)
PMID:28784611	FYPO:0002061	inviable vegetative cell population	(Fig. S1C, S1D)
PMID:28784611	FYPO:0002253	normal septum location	(Fig. S2C)
PMID:28784611	FYPO:0002061	inviable vegetative cell population	(Fig. S2D)
PMID:28784611	FYPO:0000339	mislocalized septum during vegetative growth	(Figure 1A)
PMID:28784611	GO:0005886	plasma membrane	(Figure 1B)
PMID:28784611	GO:0005886	plasma membrane	(Figure 1B)
PMID:28784611	FYPO:0002126	abolished protein localization to plasma membrane during vegetative growth [assayed_using] PomBase:SPAC637.04	(Figure 1C)
PMID:28784611	FYPO:0002126	abolished protein localization to plasma membrane during vegetative growth [assayed_using] PomBase:SPBC577.06c	(Figure 1C)
PMID:28784611	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPAC20G8.05c	(Figure 3B)
PMID:28784611	FYPO:0002719	decreased protein localization to septum [assayed_using] PomBase:SPCC645.07	(Figure 3C)
PMID:28784611	FYPO:0002719	decreased protein localization to septum [assayed_using] PomBase:SPAC16E8.09	(Figure 3D)
PMID:28784611	FYPO:0000929	decreased protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPCPB16A4.02c	(Figure 3E)
PMID:28784611	FYPO:0002061	inviable vegetative cell population	(Figure S1C)
PMID:28784611	FYPO:0001489	inviable vegetative cell	(Figure S1D)
PMID:28784611	FYPO:0005020	normal duration of actomyosin contractile ring contraction	(Figure S2A, S2B)
PMID:28784611	FYPO:0005905	normal onset of actomyosin contractile ring assembly	(Figure S2A, S2B)
PMID:28784611	FYPO:0003627	normal protein localization [assayed_using] PomBase:SPBC1289.04c	(Figure S2E)
PMID:28784611	FYPO:0003278	abnormal plasma membrane during vegetative growth	"(comment: CHECK i requested reduced plasma membrane PIP issues/3117 GFP-2xPH(Plc delta)) ""localization The PI(4,5)P2 sensor GFP-2×PH(PLCδ) (Stefan et al., 2002) was reduced at the cell cortex and the division site in efr3Δ compared with WT (Fig. 1 D), indicating that PIP PM abundance is reduced in efr3Δ"""
PMID:28784611	GO:1903475	mitotic actomyosin contractile ring assembly	(comment: naintenence)
PMID:28784611	GO:0007009	plasma membrane organization	(comment: phospholipid biosynthesis?)
PMID:28806726	FYPO:0003923	decreased rate of mitotic DNA replication elongation	(Table S1)
PMID:28806726	FYPO:0006241	abnormal negative regulation of mitotic DNA replication initiation during cellular response to DNA damage	inhibition of origin firing requires intra-S checkpoint (Fig. 5)
PMID:28806726	FYPO:0006241	abnormal negative regulation of mitotic DNA replication initiation during cellular response to DNA damage	inhibition of origin firing requires intra-S checkpoint (Fig. 5)
PMID:28806726	FYPO:0006241	abnormal negative regulation of mitotic DNA replication initiation during cellular response to DNA damage	inhibition of origin firing requires intra-S checkpoint (Fig. 5)
PMID:28806726	FYPO:0006240	decreased rate of mitotic DNA replication elongation during cellular response to DNA damage	replication forks slow independently of intra-S checkpoint (Fig. 6)
PMID:28806726	FYPO:0006242	decreased replication fork stalling during cellular response to DNA damage	replication forks stall with partial dependence on intra-S checkpoint (Fig. 6)
PMID:28806726	FYPO:0006242	decreased replication fork stalling during cellular response to DNA damage	replication forks stall with partial dependence on intra-S checkpoint (Fig. 6)
PMID:28806726	FYPO:0006242	decreased replication fork stalling during cellular response to DNA damage	replication forks stall with partial dependence on intra-S checkpoint (Fig. 6)
PMID:28811350	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [happens_during] cellular response to phosphate starvation [has_input] PomBase:SPBP4G3.02	(comment: consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA)
PMID:28811350	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1271.09	(comment: consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA)
PMID:28811350	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [happens_during] cellular response to phosphate starvation	(comment: consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA)
PMID:28811350	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBP4G3.02	(comment: consensus recognition sequence 5'-TCG(G/C)(A/T)xxTTxAA)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated by MMS mutagenesis)
PMID:28821619	FYPO:0001245	sensitive to cobalt	(comment: generated from MMS mutagenesis)
PMID:28825727	FYPO:0006302	abolished intra-arm chromosome contact change during mitosis	(Fig. 2b) (comment: hi-C difference assay)
PMID:28825727	FYPO:0006302	abolished intra-arm chromosome contact change during mitosis	(Fig. 3) (comment: hi-C)
PMID:28825727	FYPO:0006302	abolished intra-arm chromosome contact change during mitosis	(comment: (vw made more specific) Hi-C) Supplementary Figs. 1b, 1f, 4a-c
PMID:28825727	FYPO:0006302	abolished intra-arm chromosome contact change during mitosis	(comment: Cnd3 depletion following promoter shut-off and auxin-induced degron activation)
PMID:28825727	FYPO:0000214	abnormal mitotic chromosome condensation	(comment: Cnd3 depletion following promoter shut-off and auxin-induced degron activation)
PMID:28825727	FYPO:0000214	abnormal mitotic chromosome condensation	(comment: hi C????? ) Supplementary Figs. 1b, 1f, 4a-c
PMID:28825727	FYPO:0006248	increased centromere clustering at nuclear periphery during mitosis	(comment: hic and) Fig. 3C (comment: pcr ) fig 2d increased mitotic intra centromere connection
PMID:28825727	FYPO:0000214	abnormal mitotic chromosome condensation	Supplementary Figs. 1b, 1f, 4a-c (comment: Cnd3 depletion following promoter shut-off and auxin-induced degron activation)
PMID:28827290	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 70	(Fig. 1B)
PMID:28827290	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 43	(Fig. 1B)
PMID:28827290	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:28827290	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:28827290	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 83	(Fig. 2B)
PMID:28827290	GO:0000775	chromosome, centromeric region	(Fig. 2C)
PMID:28827290	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPCC1672.10	(Fig. 2D)
PMID:28827290	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:28827290	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:28827290	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:28827290	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:28827290	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:28827290	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:28827290	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:28827290	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:28827290	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:28827290	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:28827290	FYPO:0002060	viable vegetative cell population	(Fig. 4)
PMID:28827290	FYPO:0002060	viable vegetative cell population	(Fig. 4)
PMID:28827290	FYPO:0002060	viable vegetative cell population	(Fig. 4)
PMID:28827290	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 85	(Fig. 5)
PMID:28827290	FYPO:0001355	decreased vegetative cell population growth	(Fig. 5)
PMID:28827290	FYPO:0001355	decreased vegetative cell population growth	(Fig. 5)
PMID:28827290	FYPO:0001357	normal vegetative cell population growth	(Fig. 6)
PMID:28827290	FYPO:0001357	normal vegetative cell population growth	(Fig. 6)
PMID:28827290	FYPO:0001357	normal vegetative cell population growth	(Fig. 6)
PMID:28827290	FYPO:0001357	normal vegetative cell population growth	(Fig. 6)
PMID:28827290	FYPO:0001357	normal vegetative cell population growth	(Fig. 6)
PMID:28827290	FYPO:0001357	normal vegetative cell population growth	(Fig. 6)
PMID:28827290	FYPO:0000451	increased protein localization to centromere during vegetative growth [assayed_using] PomBase:SPBP22H7.09c	(Fig. 7)
PMID:28827290	FYPO:0001357	normal vegetative cell population growth	(Fig. 8)
PMID:28827290	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 55	(Figure 2B)
PMID:28827290	FYPO:0000450	decreased protein localization to centromere during vegetative growth [assayed_using] PomBase:SPCC1672.10 [has_penetrance] 42	(comment: CHECK wt 68%) (Fig. 2C)
PMID:28841135	FYPO:0005993	normal cytoplasmic translation [assayed_using] PomBase:SPAC27D7.03c	(comment: mRNA co-immunoprecipitated with ribosomes)
PMID:28882432	FYPO:0001157	increased cell population growth rate at high pH	(Fig. 3)
PMID:28904333	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC1861.01c	(comment: CONDITION 25 degrees)
PMID:28904333	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC1861.01c	(comment: CONDITION 30 degrees)
PMID:28904333	FYPO:0006843	increased histone H3 localization to chromatin	(comment: especially at centromere; also at other regions where Ino80 complex normally binds)
PMID:28904333	FYPO:0006843	increased histone H3 localization to chromatin	(comment: especially at centromere; also at other regions where Ino80 complex normally binds)
PMID:28924043	FYPO:0006723	decreased protein exit from Cdr2 medial cortical node complex during cellular response to osmotic stress [assayed_using] PomBase:SPAC644.06c [has_severity] high	(comment: Cdr1-K41A remains in nodes; Cdr1+ not tagged)
PMID:28924043	FYPO:0002376	decreased protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPAC644.06c	(comment: Cdr1-K41A remains unphosphorylated; Cdr1+ not tagged)
PMID:28924043	GO:0110115	Cdr2 medial cortical node complex [exists_during] cellular hyperosmotic response	(comment: Cdr2 does not exit nodes (unlike Cdr1) upon osmotic stress)
PMID:28924043	GO:0004707	MAP kinase activity [has_input] PomBase:SPAC644.06c [happens_during] cellular hyperosmotic salinity response	(comment: combination of in vitro kinase assay and mutant phenotypes)
PMID:28934464	FYPO:0006754	decreased promoter-enhancer looping during glucose starvation [assayed_using] PomBase:SPBC1198.14c	(Fig. 3B)
PMID:28934464	FYPO:0006754	decreased promoter-enhancer looping during glucose starvation [assayed_using] PomBase:SPBC1198.14c	(Fig. 3B)
PMID:28934464	FYPO:0006755	decreased chromatin binding at promoter element during glucose starvation [assayed_using] PomBase:SPBC29B5.01 [assayed_using] STREP_motif	(Fig. 3C)
PMID:28934464	FYPO:0006755	decreased chromatin binding at promoter element during glucose starvation [assayed_using] PomBase:SPBC29B5.01 [assayed_using] STREP_motif	(Fig. 3C)
PMID:28934464	FYPO:0006755	decreased chromatin binding at promoter element during glucose starvation [assayed_using] CRE [assayed_using] PomBase:SPBC29B5.01	(Fig. 3C)
PMID:28934464	FYPO:0006756	increased chromatin binding at promoter element during glucose starvation [assayed_using] PomBase:SPBC29B5.01 [assayed_using] CRE	(Fig. 3C)
PMID:28934464	FYPO:0006755	decreased chromatin binding at promoter element during glucose starvation [assayed_using] STREP_motif [assayed_using] PomBase:SPAC6F12.02	(Fig. 3D)
PMID:28934464	FYPO:0006756	increased chromatin binding at promoter element during glucose starvation [assayed_using] CRE [assayed_using] PomBase:SPAC6F12.02	(Fig. 3D)
PMID:28934464	FYPO:0006755	decreased chromatin binding at promoter element during glucose starvation [assayed_using] PomBase:SPBC725.11c [assayed_using] CRE	(Fig. 3E)
PMID:28934464	FYPO:0006757	normal chromatin binding at promoter element during glucose starvation [assayed_using] PomBase:SPBC725.11c [assayed_using] STREP_motif	(Fig. 3E)
PMID:28934464	GO:0003714	transcription corepressor activity	(Fig. 5D) (comment: a bit tenuous but we don't have this annotated..)
PMID:28934464	GO:0003714	transcription corepressor activity	(Fig. 5D) (comment: a bit tenuous but we don't have this annotated..)
PMID:28934464	FYPO:0006754	decreased promoter-enhancer looping during glucose starvation [assayed_using] PomBase:SPBC1198.14c	(Fig. S2D)
PMID:28934464	GO:0140585	promoter-enhancer loop anchoring activity	(comment: I replaced GO:0090579 dsDNA loop formation as per https://github.com/geneontology/go-annotation/issues/3610)
PMID:28944093	FYPO:0000271	sensitive to salt stress	(comment: can't disambiguate salt from specific calcium sensitivity in these experiments)
PMID:28944093	FYPO:0000098	sensitive to calcium	(comment: can't disambiguate salt from specific calcium sensitivity in these experiments)
PMID:28944093	FYPO:0000098	sensitive to calcium	(comment: can't disambiguate salt from specific calcium sensitivity in these experiments)
PMID:28944093	FYPO:0000271	sensitive to salt stress	(comment: can't disambiguate salt from specific calcium sensitivity in these experiments)
PMID:28947618	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBCPT2R1.08c	(Fig 7A)
PMID:28947618	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPAC212.06c	(Fig 7A)
PMID:28947618	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPAC212.11	(Fig 7A)
PMID:28947618	FYPO:0001669	abolished protein processing during vegetative growth [assayed_using] PomBase:SPAC31G5.18c	(Fig. 1B)
PMID:28947618	FYPO:0001669	abolished protein processing during vegetative growth [assayed_using] PomBase:SPAC31G5.18c	(Fig. 1B)
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	(Fig. 1D) complements partially sde2Δ
PMID:28947618	FYPO:0001575	abolished vegetative cell population growth	(Fig. 1D) does not complement sde2Δ
PMID:28947618	FYPO:0001669	abolished protein processing during vegetative growth [assayed_using] PomBase:SPAC31G5.18c	(Fig. 2A,B)
PMID:28947618	GO:0004175	endopeptidase activity [has_input] PomBase:SPAC31G5.18c	(Fig. 2D)
PMID:28947618	GO:0004175	endopeptidase activity [has_input] PomBase:SPAC31G5.18c	(Fig. 2D)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific	(Fig. 3C) decreased cell growth, normal processing, protein very stable, complements partially sde2Δ; over expression causes growth defect in hub1-1 strain, defective in telomeric silencing and genome stability
PMID:28947618	FYPO:0000836	increased protein level [assayed_using] PomBase:SPAC31G5.18c	(Fig. 3E) (comment: CHECK N-end rule pathway substrate assayed using LysSde2-C N-end rule substrate pro-obo/term-requests/119/ )
PMID:28947618	GO:0061630	ubiquitin protein ligase activity [has_input] PomBase:SPAC31G5.18c [part_of] ubiquitin-dependent protein catabolic process via the N-end rule pathway	(Fig. 3E) (comment: CHECK N-end rule pathway substrate assayed using LysSde2-C N-end rule substrate pro-obo/term-requests/119/ )
PMID:28947618	GO:0005681	spliceosomal complex	(Fig. 4A)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPCC16C4.12	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPAC212.06c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPAC1420.01c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPAP8A3.09c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPBC25H2.16c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPCC1235.09	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPBC1778.02	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPBC354.07c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPAC227.16c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPBC16E9.15	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPAC16A10.03c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPBC28E12.03	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPBP16F5.02	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPAC1786.01c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPCC1259.15c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPBC1A4.01	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPCC1259.09c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPCC594.07c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPAC17A5.16	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPCC1795.08c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPAC22H10.03c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPBC2G2.13c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPAC17D4.01	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPCC18B5.06	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPBC660.16	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPBC336.13c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPBC428.06c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPAC6F6.15	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPAC4G8.11c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPCC1795.04c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPCC126.02c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPAPB2B4.05	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPBC2A9.09	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPCC1223.10c	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPAC29E6.08	(Fig. 5B,S5A,S5B)
PMID:28947618	FYPO:0006328	decreased protein level in spliceosomal complex [assayed_using] PomBase:SPBC2F12.12c	(Fig. 8B) (comment: CHECK in spliceosome)
PMID:28947618	FYPO:0001357	normal vegetative cell population growth	(Fig. EV2B) normal processing, complements sde2Δ
PMID:28947618	FYPO:0001357	normal vegetative cell population growth	(Fig. EV2B) normal processing, complements sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	(Fig. EV2B) processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	(Fig. EV2B) processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	(Fig. EV2B) processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	(Fig. EV2B) processing defective, does not complement sde2Δ
PMID:28947618	GO:0045292	mRNA cis splicing, via spliceosome	(comment: CHECK Intron-Specific pre-mRNA Splicing)
PMID:28947618	GO:0045292	mRNA cis splicing, via spliceosome	(comment: CHECK Intron-Specific pre-mRNA Splicing)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific	(comment: CHECK assayed_using SPBC1778.02 | assayed_using SPAC227.16C | assayed_using SPBP16F5.02)
PMID:28947618	GO:0005634	nucleus	(comment: CHECK column_17 Sde2UBL)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [has_severity] high	(comment: CHECK decreased cell population growth at high temperature)
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific	(comment: CHECK does not grow at high temperature, defective pre-mRNA splicing, assayed_using SPBC1778.02 | assayed_using SPAC227.16C | assayed_using SPBP16F5.02)
PMID:28947618	FYPO:0000669	abolished peptidase activity [assayed_enzyme] PomBase:SPBC713.02c [assayed_substrate] PomBase:SPAC31G5.18c	(comment: CHECK endo mutant does not cleave Sde2 precursor)
PMID:28947618	FYPO:0000669	abolished peptidase activity [assayed_enzyme] PomBase:SPCC188.08c [assayed_substrate] PomBase:SPAC31G5.18c	(comment: CHECK endo mutant does not cleave Sde2 precursor)
PMID:28947618	FYPO:0001422	decreased protein processing during vegetative growth [assayed_using] PomBase:SPAC31G5.18c	Appendix Fig S2A
PMID:28947618	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific	does not complement sde2Δ, defective in telomeric silencing and genome stability
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, protein stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, protein stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, protein stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, protein unstable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, protein unstable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, protein unstable,complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, protein very stable, complements partially sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	normal processing, protein very stable, does not complement sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001575	abolished vegetative cell population growth	processing defective, does not complement sde2Δ
PMID:28947618	FYPO:0001355	decreased vegetative cell population growth	reduced processing, complements partially sde2Δ
PMID:28974540	FYPO:0003751	normal nuclear envelope morphology [has_penetrance] 40	(Fig. 1)
PMID:28974540	FYPO:0000227	chromosome loss during mitotic chromosome segregation	(Fig. 1)
PMID:28974540	FYPO:0000284	large and small daughter nuclei, with unequal mitotic sister chromatid segregation	(Fig. 1C)
PMID:28974540	GO:0017056	structural constituent of nuclear pore	(Fig. 1a) (comment: + others)
PMID:28974540	FYPO:0002339	decreased protein localization to nuclear periphery [assayed_using] PomBase:SPCC162.08c	(Fig. 1b)
PMID:28974540	FYPO:0002061	inviable vegetative cell population	(Fig. 2E)
PMID:28974540	FYPO:0002061	inviable vegetative cell population	(Fig. 2E)
PMID:28974540	FYPO:0002061	inviable vegetative cell population	(Fig. 2E)
PMID:28974540	FYPO:0002061	inviable vegetative cell population	(Fig. 2E)
PMID:28974540	FYPO:0002061	inviable vegetative cell population	(Fig. 2E)
PMID:28974540	FYPO:0002061	inviable vegetative cell population	(Fig. 2E)
PMID:28974540	FYPO:0002061	inviable vegetative cell population	(Fig. 2E)
PMID:28974540	FYPO:0002061	inviable vegetative cell population	(Fig. 2E)
PMID:28974540	FYPO:0003094	decreased centromeric outer repeat transcript level	(Fig. 3)
PMID:28974540	FYPO:0006353	increased centromere central core transcript level	(Fig. 3)
PMID:28974540	FYPO:0004314	normal protein localization to CENP-A containing chromatin	(Fig. 3G)
PMID:28974540	MOD:01148	ubiquitinylated lysine	(Fig. 4G and see the Ubiquitin pull-down section of Materials and methods).
PMID:28974540	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC1861.01c	(Fig. 4a)
PMID:28974540	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] ~10	(Fig. 4c)
PMID:28974540	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC1861.01c	(Fig. 4e)
PMID:28974540	GO:0005635	nuclear envelope	(Fig. 5A)
PMID:28974540	GO:0005635	nuclear envelope	(Fig. 5A)
PMID:28974540	FYPO:0002339	decreased protein localization to nuclear periphery [assayed_using] PomBase:SPBP19A11.03c	(Fig. 5D-G) (comment: nuclear envelope)
PMID:28974540	FYPO:0002339	decreased protein localization to nuclear periphery [assayed_using] PomBase:SPBC4.07c	(Fig. 5D-G) (comment: nuclear envelope)
PMID:28974540	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC17C9.13c	(Fig. 5b)
PMID:28974540	FYPO:0002339	decreased protein localization to nuclear periphery [assayed_using] PomBase:SPAC17C9.13c	(Fig. 5b) (comment: nuclear envelope)
PMID:28974540	FYPO:0000141	abnormal mitotic sister chromatid segregation [assayed_using] PomBase:SPBC1861.01c [has_severity] medium	(Fig. 6)
PMID:28974540	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC1861.01c	(Fig. 6)
PMID:28974540	FYPO:0000141	abnormal mitotic sister chromatid segregation [assayed_using] PomBase:SPBC1861.01c [has_severity] high	(Fig. 6)
PMID:28974540	FYPO:0004367	normal mitotic spindle assembly [has_penetrance] 40	(Fig. S2)
PMID:28974540	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 31	(Fig. S2A, S1E)
PMID:28974540	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. S2B)
PMID:28974540	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Fig. S3)
PMID:28974540	FYPO:0006583	decreased protein localization to nuclear periphery during mitotic interphase [assayed_using] PomBase:SPBC20F10.06	(Fig. S3C)
PMID:28974540	FYPO:0005779	normal protein localization to kinetochore during mitosis [assayed_using] PomBase:SPBC20F10.06	(Fig. S3E)
PMID:28974540	FYPO:0005779	normal protein localization to kinetochore during mitosis [assayed_using] PomBase:SPCC320.13c	(Fig. S3G, S3H)
PMID:28974540	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] high	(Fig. S3I) (comment: additive, do we know %?)
PMID:28974540	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPAC11E3.03	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC6B1.04	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPAC4F10.12	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC1861.01c	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC1105.17	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC18E5.03c	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC800.13	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPCC576.12c	(comment: added affected genes as extensions) fig 3A-C
PMID:28974540	FYPO:0001317	normal RNA level during vegetative growth [assayed_using] PomBase:SPBC1105.17	(comment: added affected genes as extensions) fig 3E
PMID:28974540	FYPO:0001317	normal RNA level during vegetative growth [assayed_using] PomBase:SPBC1861.01c	(comment: added affected genes as extensions) fig 3E
PMID:28974540	FYPO:0002649	elongated kinetochore during mitosis	(comment: vw: moved down to elongated (update fypo?)) fig 1e
PMID:28976798	GO:0005515	protein binding	(Fig. 1)
PMID:28976798	GO:0005515	protein binding	(Fig. 1)
PMID:28976798	GO:0005515	protein binding	(Fig. 1)
PMID:28976798	GO:0005515	protein binding	(Fig. 1)
PMID:28976798	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC63.08c [assayed_using] PomBase:SPAC4F10.07c	(Fig. 1D)
PMID:28977643	GO:0045003	double-strand break repair via synthesis-dependent strand annealing	(comment: CHECK mhf1-L78R)
PMID:28977649	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_using] glycyl_tRNA	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_using] tryptophanyl_tRNA	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_using] threonyl_tRNA	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_using] asparaginyl_tRNA	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_using] seryl_tRNA	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_using] phenylalanyl_tRNA	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_using] leucyl_tRNA	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_using] isoleucyl_tRNA	(comment: Asn GUU, Gly CCC, Ile AAU, Leu AAG, Leu CAA, Leu CAG, Leu UAG, Phe GAA, Ser AGA, Ser GCU, Thr AGU, Trp CAA)
PMID:28977649	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_using] phenylalanyl_tRNA	(comment: Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU)
PMID:28977649	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_using] leucyl_tRNA	(comment: Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU)
PMID:28977649	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_using] isoleucyl_tRNA	(comment: Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU)
PMID:28977649	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_using] seryl_tRNA	(comment: Ile AAU, Leu UAG, Leu CAG, Phe GAA, Ser GCU)
PMID:28977649	FYPO:0006251	decreased tRNA aminoacylation [assayed_using] seryl_tRNA	(comment: affects tRNA-Ser UGA/CGA; suggests tRNA-Ser UGA/CGA misfolding due to decreased dimethylation of G26, but modification not assayed directly for this tRNA)
PMID:28977649	FYPO:0006251	decreased tRNA aminoacylation [assayed_using] seryl_tRNA	(comment: affects tRNA-Ser UGA/CGA; suggests tRNA-Ser UGA/CGA misfolding due to decreased dimethylation of G26, but modification not assayed directly for this tRNA)
PMID:28977649	FYPO:0006249	normal tRNA aminoacylation [assayed_using] lysyl_tRNA	(comment: tRNA-Ser GCU and tRNA-Ser AGA unaffected)
PMID:28977649	FYPO:0006249	normal tRNA aminoacylation [assayed_using] tryptophanyl_tRNA	(comment: tRNA-Ser GCU and tRNA-Ser AGA unaffected)
PMID:28977649	FYPO:0006249	normal tRNA aminoacylation [assayed_using] leucyl_tRNA	(comment: tRNA-Ser GCU and tRNA-Ser AGA unaffected)
PMID:28977649	FYPO:0006249	normal tRNA aminoacylation [assayed_using] arginyl_tRNA	(comment: tRNA-Ser GCU and tRNA-Ser AGA unaffected)
PMID:28977649	FYPO:0006249	normal tRNA aminoacylation [assayed_using] seryl_tRNA	(comment: tRNA-Ser GCU and tRNA-Ser AGA unaffected)
PMID:28977649	FYPO:0006249	normal tRNA aminoacylation [assayed_using] methionyl_tRNA	(comment: tRNA-Ser GCU and tRNA-Ser AGA unaffected)
PMID:28982178	FYPO:0000249	decreased cell population growth on ammonia nitrogen source	(comment: CHECK 40 fold less)
PMID:29021344	FYPO:0003241	unequal mitotic sister chromatid segregation	(Fig. 3C)
PMID:29021344	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B	(Figure 1F)
PMID:29021344	FYPO:0003969	mislocalized mitotic spindle [has_penetrance] 34	(Figure 2E)
PMID:29021344	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B	(Figure 2G)
PMID:29021344	FYPO:0002061	inviable vegetative cell population	(Figure 4A and Supplemental Figure S4)
PMID:29021344	FYPO:0002061	inviable vegetative cell population	(Figure 4A and Supplemental Figure S4)
PMID:29021344	FYPO:0002061	inviable vegetative cell population	(Figure 4A and Supplemental Figure S4)
PMID:29021344	FYPO:0002061	inviable vegetative cell population	(Figure 4A and Supplemental Figure S4)
PMID:29021344	FYPO:0002061	inviable vegetative cell population	(Figure 4B)
PMID:29021344	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC890.02c	(Figure S5D)
PMID:29021344	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC890.02c	(Figure S5D)
PMID:29021344	FYPO:0002060	viable vegetative cell population	(Supplemental Figure S1A).
PMID:29032152	FYPO:0001234	slow vegetative cell population growth	(Fig. 1)
PMID:29032152	FYPO:0001234	slow vegetative cell population growth [has_severity] low	(Fig. 1, 3b)
PMID:29032152	FYPO:0001926	normal cellular response to hydroxyurea	(Fig. 2)
PMID:29032152	FYPO:0002550	sensitive to UV	(Fig. 2)
PMID:29032152	FYPO:0001689	normal growth on 4-nitroquinoline N-oxide	(Fig. 2)
PMID:29032152	FYPO:0001021	normal growth during cellular response to osmotic stress	(Fig. 2a)
PMID:29032152	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 2b, c)
PMID:29032152	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(Fig. 3b)
PMID:29032152	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(Fig. 3b)
PMID:29032152	FYPO:0001357	normal vegetative cell population growth	(Fig. 3b)
PMID:29032152	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(Fig. 3b)
PMID:29032152	FYPO:0001234	slow vegetative cell population growth [has_severity] low	(Fig. 3b)
PMID:29032152	FYPO:0001689	normal growth on 4-nitroquinoline N-oxide	(Fig. 3e)
PMID:29032152	FYPO:0000969	normal growth during cellular response to UV	(Fig. 3e)
PMID:29032152	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 3e)
PMID:29032152	FYPO:0002876	decreased transcription [has_severity] low	(Fig. 4)
PMID:29032152	FYPO:0002876	decreased transcription [has_severity] low	(Fig. 4)
PMID:29032152	GO:0005515	protein binding	(Fig. 4)
PMID:29032152	FYPO:0002876	decreased transcription [has_severity] low	(Fig. 4)
PMID:29032152	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC1223.10c [assayed_using] PomBase:SPBP23A10.14c	(Table 3)
PMID:29032152	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1223.10c [assayed_using] PomBase:SPBP23A10.14c	(Table 3)
PMID:29032152	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1223.10c [assayed_using] PomBase:SPBP23A10.14c	(Table 3)
PMID:29032152	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1223.10c [assayed_using] PomBase:SPBP23A10.14c	(Table 3)
PMID:29032152	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1223.10c [assayed_using] PomBase:SPBP23A10.14c	(Table 3)
PMID:29032152	GO:0006368	transcription elongation by RNA polymerase II [happens_during] DNA damage response	(comment: inferred from combined experiments)
PMID:29079657	GO:0010515	negative regulation of induction of conjugation with cellular fusion	(Fig. 1)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] cellular response to nitrogen starvation	(Fig. 2 and supp table)
PMID:29079657	GO:0000124	SAGA complex [exists_during] single-celled organism vegetative growth phase	(Fig. 2 and supp table)
PMID:29079657	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC15A10.02 [part_of] positive regulation of transcription by RNA polymerase II [part_of] positive regulation of induction of conjugation with cellular fusion [happens_during] cellular response to starvation	(Fig. 6)
PMID:29079657	GO:1900237	positive regulation of induction of conjugation with cellular fusion	To conclude, upon nutrient starvation, TORC2 functions as both an activator and an inhibitor of sexual differentiation, the latter being mediated by Taf12 phosphorylation.
PMID:2908246	FYPO:0003738	abnormal mitotic cell cycle arrest with condensed chromosomes [has_penetrance] high	(Fig. 3)
PMID:2908246	FYPO:0006101	abnormal interphase microtubules [has_penetrance] high	(Fig. 3)
PMID:2908246	FYPO:0001234	slow vegetative cell population growth	(comment: mild over expression of cdc13+ on multi copy plasmid pYep13 causes slow growth)
PMID:2908246	FYPO:0002085	normal vegetative cell growth [has_penetrance] medium	(comment: mild over expression of cdc13+ on multi copy plasmid pYep13 rescues the cdc13-117 ts phenotype) .
PMID:2908246	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	(comment: mild over expression of cdc2+ on multi copy plasmid rescues the cdc13-117 ts phenotype)
PMID:29084823	FYPO:0000825	increased RNA level during vegetative growth [has_severity] high [assayed_using] PomBase:SPBC19F5.01c	(Fig. 2B, 2C, 6A)
PMID:29084823	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC19F5.01c [has_severity] high	(Fig. 2D, 2E, S2)
PMID:29084823	FYPO:0000708	decreased mating efficiency [has_severity] high	(Fig. 3A)
PMID:29084823	FYPO:0000708	decreased mating efficiency [has_severity] high	(Fig. 3A) deletion of cig1 does not rescue mating efficiency of zfs1 delta
PMID:29084823	FYPO:0000708	decreased mating efficiency [has_severity] high	(Fig. 3A) deletion of cig2 does not rescue mating efficiency zfs1delta
PMID:29084823	FYPO:0001147	normal mating efficiency	(Fig. 3A) deletion of puc1 increases mating efficiency of zfs1 delta to WT
PMID:29084823	FYPO:0000708	decreased mating efficiency [has_severity] high	(Fig. 3B) varying the copy number of pJKpuc1+ leads to varying levels of sporulation efficiency in wild type cells increased puc1 mRNA causes reduced mating efficiency
PMID:29084823	FYPO:0004582	increased cell cycle arrest in mitotic G1 phase in response to nitrogen starvation [has_severity] low	(Fig. 3C)
PMID:29084823	FYPO:0004233	decreased and delayed cell cycle arrest in mitotic G1 phase in response to nitrogen starvation [has_severity] medium	(Fig. 3C)
PMID:29084823	FYPO:0004582	increased cell cycle arrest in mitotic G1 phase in response to nitrogen starvation [has_penetrance] medium	(Fig. 3C, 7A) shows that zfs1delta shows high mating efficiency at nitrogen levels which suppress mating in wild type cells wild type cells
PMID:29084823	MOD:00696	phosphorylated residue [present_during] single-celled organism vegetative growth phase	(Fig. 4A, 4B) (comment: about 10%? of Zfs1 is phosphorylated during vegetative growth)
PMID:29084823	MOD:00696	phosphorylated residue [increased_during] cellular response to nitrogen starvation	(Fig. 4A, 4B) Zfs is hyperphosphorylated in response to nitrogen depletion
PMID:29084823	FYPO:0005034	decreased protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPBC1718.07c [has_severity] high	(Fig. 4D, S3) the hyperphosphoryated zfs1 (3rd band higest). Gad8 is required to hyperphosphorylate zfs1. In Fig4C they also show that TOR inhibition by Torin stimulates hyerphosphorylation of Zfs1
PMID:29084823	FYPO:0005036	abolished protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPBC1718.07c	(Fig. 5B)
PMID:29084823	FYPO:0005034	decreased protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPBC1718.07c [has_severity] medium	(Fig. 5C, 5D)
PMID:29084823	FYPO:0005034	decreased protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPBC1718.07c [has_severity] medium	(Fig. 5C, 5D)
PMID:29084823	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC1718.07c	(Fig. 5E)
PMID:29084823	FYPO:0005034	decreased protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPBC1718.07c	(Fig. 5E)
PMID:29084823	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPBC1718.07c	(Fig. 5E)
PMID:29084823	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC1718.07c	(Fig. 5E)
PMID:29084823	FYPO:0001096	normal RNA level during nitrogen starvation [assayed_using] PomBase:SPBC19F5.01c	(Fig. 6A)
PMID:29084823	FYPO:0001317	normal RNA level during vegetative growth [assayed_using] PomBase:SPBC19F5.01c	(Fig. 6A)
PMID:29084823	FYPO:0001317	normal RNA level during vegetative growth [assayed_using] PomBase:SPBC19F5.01c	(Fig. 6A)
PMID:29084823	FYPO:0001096	normal RNA level during nitrogen starvation [assayed_using] PomBase:SPBC19F5.01c	(Fig. 6A)
PMID:29084823	FYPO:0001096	normal RNA level during nitrogen starvation [assayed_using] PomBase:SPBC19F5.01c	(Fig. 6A)
PMID:29084823	FYPO:0004084	normal protein level during nitrogen starvation [assayed_using] PomBase:SPBC19F5.01c	(Fig. 6A, 6B)
PMID:29084823	FYPO:0004084	normal protein level during nitrogen starvation [assayed_using] PomBase:SPBC19F5.01c [has_severity] medium	(Fig. 6A, 6B)
PMID:29084823	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC19F5.01c [has_severity] medium	(Fig. 6A, 6B)
PMID:29084823	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC19F5.01c [has_severity] high	(Fig. 6A, 6B)
PMID:29084823	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC19F5.01c [has_severity] medium	(Fig. 6A, 6B)
PMID:29084823	FYPO:0004084	normal protein level during nitrogen starvation [assayed_using] PomBase:SPBC19F5.01c	(Fig. 6A, 6B)
PMID:29084823	FYPO:0001043	increased mating efficiency [has_severity] medium	(Fig. 7A) shows that puc1delta shows increased mating efficiency at nitrogen levels which suppress mating in wild type cells
PMID:29084823	GO:0003723	RNA binding [occurs_in] AU_rich_element	(Figure 1A, S1)
PMID:29084823	GO:0003723	RNA binding [occurs_in] five_prime_UTR	(Figure 1C)
PMID:29084823	GO:0003723	RNA binding [occurs_in] three_prime_UTR	(Figure 1C)
PMID:29084823	GO:0140610	RNA sequestering activity [has_input] PomBase:SPBC19F5.01c [part_of] negative regulation of conjugation with cellular fusion	(comment: RNA)
PMID:29084823	FYPO:0001890	increased RNA level	"(comment: jack suggested ""up regulation of protein binding RNAs because normally bound by zfs1"" I'm using this to make the sequestering GO annotation.)"
PMID:29109278	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: mat3M::ura4+)
PMID:29109278	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC16C4.22 [assayed_using] PomBase:SPBC3D6.09	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC16C4.22 [assayed_using] PomBase:SPBC25H2.13c	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(comment: otr1R(SphI)::ura4+)
PMID:29109278	FYPO:0004604	decreased chromatin silencing at subtelomere	(comment: tel2L::ura4+)
PMID:29123917	FYPO:0004094	abnormal protein localization during meiotic cell cycle [assayed_using] PomBase:SPBC582.03	(Fig. 6)
PMID:29123917	FYPO:0006372	incomplete meiotic chromosome segregation, with chromosomal bridge	(Figure S10 E and F)
PMID:29123917	GO:0140445	chromosome, telomeric repeat region [exists_during] meiotic G2 phase	(comment: Later stage of meiotic prophase, observed by co-localisation with Taz1)
PMID:29123917	GO:0140445	chromosome, telomeric repeat region [exists_during] meiotic G2 phase	(comment: Later stage of meiotic prophase, observed by co-localisation with Taz1)
PMID:29134248	GO:0070867	mating projection tip membrane	(comment: CHECK Fusion domain)
PMID:29136238	FYPO:0004542	increased chromatin silencing at subtelomere [has_severity] medium	(Fig. 1)
PMID:29136238	FYPO:0006299	increased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. 1)
PMID:29136238	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. 2)
PMID:29136238	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	(Fig. 2)
PMID:29136238	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] medium	(Fig. 2)
PMID:29136238	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	(Fig. 2)
PMID:29136238	FYPO:0006299	increased chromatin silencing at centromere outer repeat [has_severity] high	(Fig. 2)
PMID:29136238	FYPO:0006395	normal histone H3-K9 acetylation at subtelomeric heterochromatin during vegetative growth	(Fig. 3)
PMID:29136238	FYPO:0003575	normal histone H3-K9 acetylation at centromere outer repeat during vegetative growth	(Fig. 3)
PMID:29136238	FYPO:0006429	normal histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth	(Fig. 3)
PMID:29136238	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 3)
PMID:29136238	FYPO:0003010	increased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_using] PomBase:SPAC664.01c	(Fig. 4)
PMID:29136238	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_using] PomBase:SPAC664.01c	(Fig. 4)
PMID:29136238	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_using] PomBase:SPAC18G6.02c	(Fig. 4, 5)
PMID:29136238	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_using] PomBase:SPAC18G6.02c	(Fig. 4, 5)
PMID:29136238	FYPO:0000088	sensitive to hydroxyurea	(Fig. 7)
PMID:29136238	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC664.01c [assayed_using] PomBase:SPBC8D2.04	and observed a preferential association of Swi6 with Y41F over Y41p peptide, suggesting that phosphorylation of H3Y41 counteracts the interaction of Swi6 with histone H3 (Supplementary Figure S6A).
PMID:29136238	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC664.01c [assayed_using] PomBase:SPBC1105.11c	and observed a preferential association of Swi6 with Y41F over Y41p peptide, suggesting that phosphorylation of H3Y41 counteracts the interaction of Swi6 with histone H3 (Supplementary Figure S6A).
PMID:29136238	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC1834.04 [assayed_using] PomBase:SPAC664.01c	and observed a preferential association of Swi6 with Y41F over Y41p peptide, suggesting that phosphorylation of H3Y41 counteracts the interaction of Swi6 with histone H3 (Supplementary Figure S6A).
PMID:29160296	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC19G12.13c	(Fig. 2C)
PMID:29160296	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC19G12.13c	(Fig. 2C)
PMID:29160296	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC19G12.13c	(Fig. 2C)
PMID:29160296	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC19G12.13c	(Fig. 2C)
PMID:29160296	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC19G12.13c	(Fig. 2C)
PMID:29160296	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC6F6.16c [has_severity] high	(Fig. 3D)
PMID:29160296	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC6F6.16c	(Fig. 3D)
PMID:29160296	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC6F6.16c [has_severity] low	(Fig. 3D)
PMID:29160296	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC6F6.16c [has_severity] medium	(Fig. 3D)
PMID:29160296	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC6F6.16c [has_severity] low	(Fig. 3D)
PMID:29160296	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC6F6.16c	(Fig. 3E)
PMID:29160296	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC6F6.16c	(Fig. 3E)
PMID:29160296	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC6F6.16c	(Fig. 3E)
PMID:29160296	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPAC6F6.16c	(Fig. 3E)
PMID:29160296	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPBC1778.02 [has_severity] high	(Fig. 4F)
PMID:29160296	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPBC1778.02 [has_severity] medium	(Fig. 4F)
PMID:29160296	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPBC1778.02 [has_severity] medium	(Fig. 4F)
PMID:29160296	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPBC1778.02 [has_severity] high	(Fig. 4F)
PMID:29160296	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPBC1778.02 [has_severity] high	(Fig. 4F)
PMID:29160296	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPBC1778.02 [has_severity] high	(Fig. 4F)
PMID:29160296	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPBC1778.02 [has_severity] high	(Fig. 4F)
PMID:29160296	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPBC1778.02 [has_severity] high	(Fig. 4F)
PMID:29160296	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPBC1778.02	(Fig. 4F)
PMID:29160296	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC19G12.13c [assayed_protein] PomBase:SPBC1778.02 [has_severity] high	(Fig. 4F)
PMID:29160296	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] high	(Fig. 5A)
PMID:29160296	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] low	(Fig. 5A)
PMID:29160296	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. 5A)
PMID:29160296	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] high	(Fig. 5A)
PMID:29160296	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] high	(Fig. 5A)
PMID:29160296	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] high	(Fig. 5A)
PMID:29160296	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPAC212.11 [assayed_transcript] PomBase:SPBCPT2R1.08c [has_severity] high	(Fig. 5B)
PMID:29160296	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPAC212.11 [assayed_transcript] PomBase:SPBCPT2R1.08c [has_severity] high	(Fig. 5B)
PMID:29160296	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPAC212.11 [assayed_transcript] PomBase:SPBCPT2R1.08c [has_severity] high	(Fig. 5B)
PMID:29160296	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPAC212.11 [assayed_transcript] PomBase:SPBCPT2R1.08c [has_severity] high	(Fig. 5B)
PMID:29160296	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPAC212.11 [assayed_transcript] PomBase:SPBCPT2R1.08c [has_severity] high	(Fig. 5B)
PMID:29160296	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPAC212.11 [assayed_transcript] PomBase:SPBCPT2R1.08c [has_severity] low	(Fig. 5B)
PMID:29160296	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPAC212.11 [assayed_transcript] PomBase:SPBCPT2R1.08c [has_severity] low	(Fig. 5B)
PMID:29160296	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPAC212.11 [assayed_transcript] PomBase:SPBCPT2R1.08c [has_severity] medium	(Fig. 5B)
PMID:29160296	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPAC212.11 [assayed_transcript] PomBase:SPBCPT2R1.08c [has_severity] high	(Fig. 5B)
PMID:29160296	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] high	(Fig. 5D)
PMID:29160296	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] high	(Fig. 5D)
PMID:29160296	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] high	(Fig. 5D)
PMID:29160296	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] high	(Fig. 5D)
PMID:29160296	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] high	(Fig. 5D)
PMID:29160296	FYPO:0002702	circularized chromosome [has_severity] high	(Fig. 5E)
PMID:29160296	FYPO:0002702	circularized chromosome [has_severity] high	(Fig. 5E)
PMID:29160296	FYPO:0002702	circularized chromosome [has_severity] high	(Fig. 5E)
PMID:29160296	FYPO:0002702	circularized chromosome [has_severity] high	(Fig. 5E)
PMID:29160296	FYPO:0002702	circularized chromosome [has_severity] low	(Fig. 5E)
PMID:29160296	FYPO:0002702	circularized chromosome [has_severity] high	(Fig. 5E)
PMID:29160296	FYPO:0002702	circularized chromosome [has_severity] high	(Fig. 5E)
PMID:29167352	FYPO:0002060	viable vegetative cell population	(Fig. 1C
PMID:29167352	FYPO:0002060	viable vegetative cell population	(Fig. 1C
PMID:29167352	FYPO:0002060	viable vegetative cell population	(Fig. 1C
PMID:29167352	FYPO:0002060	viable vegetative cell population	(Fig. 1C
PMID:29167352	FYPO:0002060	viable vegetative cell population	(Fig. 1C
PMID:29167352	FYPO:0002060	viable vegetative cell population	(Fig. 1C (comment: CONDITION 28 Celcius)
PMID:29167352	GO:1990810	microtubule anchoring at mitotic spindle pole body	(Fig. 4) Klp2 is not required, but acts collaboratively with Pkl1, in anchoring the spindle microtubule to the mitotic SPB
PMID:29167352	FYPO:0001489	inviable vegetative cell	(comment: CONDITION 28 celcius)
PMID:29167352	GO:0072686	mitotic spindle	(comment: often in a punctate manner)
PMID:29167439	FYPO:0006507	increased subtelomeric DNA amplification during G0	(comment: Require for subtelomeric DNA amplification in G0)
PMID:29167439	FYPO:0006507	increased subtelomeric DNA amplification during G0	(comment: increase with telomere shortening and time in quiescence)
PMID:29167439	FYPO:0002945	increased RNA level during G0 [assayed_using] TERRA [has_severity] high	(comment: increase with telomere shortening and time in quiescence)
PMID:29167439	FYPO:0006507	increased subtelomeric DNA amplification during G0 [has_severity] high	(comment: limit subtelomeric DNA amplification in G0)
PMID:29167439	FYPO:0006507	increased subtelomeric DNA amplification during G0	(comment: require for subtelomeric DNA amplification in G0)
PMID:29180432	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC1861.01c [assayed_using] PomBase:SPBC409.04c	(Fig. 2G)
PMID:29180432	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC1861.01c [assayed_using] PomBase:SPBC409.04c [has_severity] high	(Fig. 2G)
PMID:29180432	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC1861.01c [assayed_using] PomBase:SPBC409.04c [has_severity] high	(Fig. 2G)
PMID:29180432	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPCC320.13c [added_during] mitotic prophase	(Fig. 3)
PMID:29180432	FYPO:0005366	abolished protein phosphorylation during mitosis [assayed_protein] PomBase:SPBC1861.01c	(Fig. 3)
PMID:29180432	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC1861.01c [assayed_using] PomBase:SPBC409.04c	(Fig. 4)
PMID:29180432	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 16	(Fig. 5) (measured at 4 um spindle. WT has 6%)
PMID:29180432	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase	(Fig. 5B and D)
PMID:29180432	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Fig. 5f)
PMID:29180432	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPBC1861.01c [assayed_using] PomBase:SPBC409.04c	(Fig. 6)
PMID:29180432	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPCC320.13c [added_during] mitotic prophase	(Fig. 6)
PMID:29180432	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC1861.01c [part_of] repair of mitotic kinetochore microtubule attachment defect [happens_during] mitotic prophase	(Figure 3)
PMID:29180432	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC409.04c [part_of] positive regulation of kinetochore assembly [happens_during] mitotic interphase	(Figure 3)
PMID:29180432	FYPO:0000324	mitotic metaphase/anaphase transition delay [has_penetrance] 6	increased duration of metaphase Fig. 5E
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] ~9	(Fig. 1b, C)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] ~16	(Fig. 1b, C)
PMID:29194511	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 43.8	(Fig. 1b, C)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] ~9	(Fig. 1b, C)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] ~6	(Fig. 1b, C)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] ~13	(Fig. 1b, C)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 6	(Fig. 1b, C)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 13.6	(Fig. 1b, C, 3H)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 15.7	(Fig. 1b, C, 3H)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation	(Fig. 4a)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation	(Fig. 4a)
PMID:29194511	FYPO:0006353	increased centromere central core transcript level	(Fig. 4b)
PMID:29194511	FYPO:0006353	increased centromere central core transcript level	(Fig. 4b)
PMID:29194511	GO:0005515	protein binding	(Fig. 5)
PMID:29194511	FYPO:0001234	slow vegetative cell population growth	(Figure 2A, B, C)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 43	(Figure 2E-F, supplementary Figure 5)
PMID:29194511	FYPO:0000450	decreased protein localization to centromere during vegetative growth [assayed_using] PomBase:SPBC1105.17 [has_severity] high	(Figure 2G, supplementary Figure 4)
PMID:29194511	GO:0003755	peptidyl-prolyl cis-trans isomerase activity [has_input] PomBase:SPBC1105.17	(Figure 3C-D, Supplementary Figure 8A-B)
PMID:29194511	GO:0003755	peptidyl-prolyl cis-trans isomerase activity [has_input] PomBase:SPBC1105.17	(Figure 3E-F, Supplementary Figure 8 C-D)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation	(Figure S1A and B)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation	(Figure S1A and B)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation	(Figure S1A and B)
PMID:29194511	FYPO:0003241	unequal mitotic sister chromatid segregation	(Figure S1A and B)
PMID:29214404	FYPO:0004137	decreased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth	(comment: at telomere 1R)
PMID:29214404	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPAC664.01c	(comment: at telomeres 1L, 1R, 2L, 2R)
PMID:29214404	FYPO:0000873	increased histone H3-K9 dimethylation during vegetative growth	(comment: at telomeres 1L, 2R)
PMID:29214404	FYPO:0005918	decreased protein localization to subtelomeric heterochromatin [assayed_using] PomBase:SPCC622.16c	(comment: greater decrease at telomeres 1R and 2L than at 1L and 2R)
PMID:29215009	FYPO:0003589	decreased replication slippage during replication fork processing	(comment: CHECK same as either single mutant)
PMID:29215009	FYPO:0006318	decreased DNA resection during replication fork processing	(comment: CHECK same as exo1delta alone)
PMID:29215009	FYPO:0006320	normal replication slippage during replication fork processing	(comment: upstream reporter)
PMID:29215009	FYPO:0006320	normal replication slippage during replication fork processing	(comment: upstream reporter)
PMID:29216371	GO:0005515	protein binding [part_of] telomere maintenance via telomerase	(comment: IMP evidence for part_of extension)
PMID:29216371	GO:0005515	protein binding [part_of] telomere maintenance via telomerase	(comment: IMP evidence for part_of extension)
PMID:29249658	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth	(Fig. 1)
PMID:29249658	FYPO:0003150	decreased NETO [has_penetrance] 90	(Fig. 1)
PMID:29249658	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth [has_penetrance] ~32	(Fig. 1)
PMID:29249658	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPBC4F6.06	(Fig. 1B)
PMID:29249658	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPBC4F6.06	(Fig. 1B)
PMID:29249658	FYPO:0003532	increased monopolar index [has_severity] medium	(Fig. 1D, 1E) (comment: CHECK ~55%)
PMID:29249658	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [has_severity] high	(Fig. 2)
PMID:29249658	FYPO:0002679	decreased protein phosphorylation [has_severity] high [assayed_using] PomBase:SPBC4F6.06	(Fig. 2A)
PMID:29249658	FYPO:0000224	lemon-shaped cell	(Fig. 2A)
PMID:29249658	FYPO:0003710	swollen pear-shaped vegetative cell [has_severity] high	(Fig. 2A)
PMID:29249658	FYPO:0003710	swollen pear-shaped vegetative cell [has_severity] high	(Fig. 2A)
PMID:29249658	FYPO:0003710	swollen pear-shaped vegetative cell [has_severity] high	(Fig. 2A)
PMID:29249658	FYPO:0002679	decreased protein phosphorylation [has_severity] high [assayed_using] PomBase:SPBC4F6.06	(Fig. 2A)
PMID:29249658	FYPO:0000223	elongated multiseptate vegetative cell	(Fig. 2A)
PMID:29249658	FYPO:0001315	normal vegetative cell morphology [assayed_using] PomBase:SPBC4F6.06	(Fig. 3)
PMID:29249658	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPBC4F6.06	(Fig. 3)
PMID:29249658	FYPO:0006502	abolished protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPCP1E11.04c	(Fig. 3A)
PMID:29249658	FYPO:0006502	abolished protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPCP1E11.04c	(Fig. 3B)
PMID:29249658	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPBC4F6.06	(Fig. 3D)
PMID:29249658	FYPO:0001585	abolished protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPBC4F6.06	(Fig. 3D)
PMID:29249658	FYPO:0003208	decreased protein localization to cell tip, with protein distributed in plasma membrane or cortex [has_penetrance] 80-90 [assayed_using] PomBase:SPCP1E11.04c	(Fig. 3c)
PMID:29249658	GO:0005515	protein binding	(Fig. 3h)
PMID:29249658	FYPO:0000118	multiseptate vegetative cell	(Fig. 4C, 4D)
PMID:29249658	FYPO:0000013	T-shaped vegetative cell with normal cell length	(Fig. 4C, 4D)
PMID:29249658	FYPO:0001880	abolished protein localization to cell division site [assayed_using] PomBase:SPAC9G1.06c	(Fig. 4F)
PMID:29249658	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC20G8.05c	(Fig. 4F) (comment: lasso)
PMID:29249658	FYPO:0003208	decreased protein localization to cell tip, with protein distributed in plasma membrane or cortex [has_penetrance] 80-90 [assayed_using] PomBase:SPCP1E11.04c	(Fig. S3A)
PMID:29249658	GO:0004674	protein serine/threonine kinase activity [directly_positively_regulates] PomBase:SPBC4F6.06 [part_of] positive regulation of protein localization to cell tip [part_of] cell growth mode switching, monopolar to bipolar	(Figure 1c)
PMID:29249658	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC1706.01	(Figure 2)
PMID:29249658	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC530.04	(Figure 2)
PMID:29249658	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCP1E11.04c [part_of] positive regulation of protein localization to cell tip	(Figure 2)
PMID:29249658	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC4F6.06 [part_of] cell growth mode switching, monopolar to bipolar	(Figure 2D)
PMID:29249658	FYPO:0005501	abolished protein localization to cell cortex, with protein mislocalized to cytoplasm, during vegetative growth [assayed_enzyme] PomBase:SPBC4F6.06	(Figure 3D)
PMID:29249658	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC4F6.06 [assayed_using] PomBase:SPCP1E11.04c	(Figure 3H)
PMID:29249658	FYPO:0001384	abolished protein kinase activity [assayed_enzyme] PomBase:SPBC4F6.06	(Figure S3F)
PMID:29249658	FYPO:0001384	abolished protein kinase activity [assayed_enzyme] PomBase:SPBC4F6.06	(Figure S3F)
PMID:29249658	FYPO:0005501	abolished protein localization to cell cortex, with protein mislocalized to cytoplasm, during vegetative growth [assayed_enzyme] PomBase:SPBC4F6.06	(Figure S3F)
PMID:29249658	FYPO:0005501	abolished protein localization to cell cortex, with protein mislocalized to cytoplasm, during vegetative growth [assayed_using] PomBase:SPCP1E11.04c	(Figure S3F)
PMID:29249658	FYPO:0005501	abolished protein localization to cell cortex, with protein mislocalized to cytoplasm, during vegetative growth [assayed_enzyme] PomBase:SPBC4F6.06	(Figure S3F)
PMID:29249658	FYPO:0005501	abolished protein localization to cell cortex, with protein mislocalized to cytoplasm, during vegetative growth [assayed_using] PomBase:SPCP1E11.04c	(Figure S3F)
PMID:29249658	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC9G1.06c	(Figure S4C)
PMID:29249658	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC20G8.05c	(Figure S4C)
PMID:29249658	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC20G8.05c	(Figure S4C)
PMID:29249658	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC9G1.06c	(Figure S4C)
PMID:29249658	FYPO:0001118	abnormal vegetative cell morphology [has_severity] high	(comment: CHeCK phenotypes)
PMID:29259000	FYPO:0006314	abolished ascus formation	(Fig. 2)
PMID:29259000	FYPO:0000583	abolished sporulation	(Fig. 2) (comment: abolished asci formation)
PMID:29259000	FYPO:0000280	sterile	(Fig. 2A)
PMID:29259000	FYPO:0006313	abolished meiotic G2/MI transition	(Fig. 2A) (comment: CHECK abolished entry into meiosis (at pre meiosis?))
PMID:29259000	FYPO:0006313	abolished meiotic G2/MI transition	(Fig. 2A) (comment: CHECK abolished entry into meiosis (at pre meiosis?))
PMID:29259000	FYPO:0002092	abnormal meiotic sister chromatid cohesion [has_penetrance] 8	(Fig. 3D)
PMID:29259000	FYPO:0002092	abnormal meiotic sister chromatid cohesion [has_penetrance] ~30	(Fig. 3D)
PMID:29259000	FYPO:0002222	long meiosis II spindle [has_penetrance] 20	(Fig. 5)
PMID:29259000	FYPO:0002092	abnormal meiotic sister chromatid cohesion [has_penetrance] 15	(Fig. 5)
PMID:29259000	FYPO:0002222	long meiosis II spindle	(Fig. 5D)
PMID:29259000	FYPO:0006316	spindle pole bodies present in increased numbers during meiosis II	(Fig. 5E)
PMID:29259000	FYPO:0006317	decreased protein localization to meiotic spindle pole body during meiosis II [assayed_using] PomBase:SPAC1F3.06c	(Fig. 7D, E, F)
PMID:29259000	FYPO:0006128	normal duration of meiosis II	(Fig. S5A)
PMID:29259000	FYPO:0000485	decreased meiotic recombination	(Figure 3F)
PMID:29259000	FYPO:0000485	decreased meiotic recombination	(Figure 4)
PMID:29259000	FYPO:0005509	abnormal meiotic sister chromatid segregation [has_penetrance] 40	(Figure 4A and B) (comment: MI NDJ)
PMID:29259000	FYPO:0000678	unequal homologous chromosome segregation [has_penetrance] 50	(Figure 4A and B) (comment: MI NDJ)
PMID:29259000	GO:0035974	meiotic spindle pole body [exists_during] meiosis II cell cycle phase	(Figure 6)
PMID:29259000	GO:0005634	nucleus [exists_during] meiotic interphase	(Figure S3C-E)
PMID:29259000	GO:0005634	nucleus [exists_during] meiotic M phase	(Figure S3C-E)
PMID:29290560	GO:0140268	endoplasmic reticulum-plasma membrane contact site	(Fig. 1)
PMID:29290560	FYPO:0001530	abnormal GTPase activity [assayed_enzyme] PomBase:SPAC110.03	(Fig. 1) ER plasma membrane tethering ER-PM contact removal OR abnormal ER-PM contact formation
PMID:29290560	FYPO:0004730	protein mislocalized to lateral cell cortex [assayed_using] PomBase:SPAC6G9.11	(Fig. 2A)
PMID:29290560	FYPO:0002106	viable stubby vegetative cell [has_penetrance] high	(Fig. 3C)
PMID:29290560	FYPO:0000537	abolished protein secretion during vegetative growth	(Fig. 3D)
PMID:29290560	FYPO:0000539	increased protein secretion during vegetative growth	(Fig. 3D)
PMID:29290560	FYPO:0001945	normal protein secretion	(Fig. 3D)
PMID:29290560	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering	(Figure 1F) ER-PM uncoupling
PMID:29290560	FYPO:0000539	increased protein secretion during vegetative growth [assayed_using] PomBase:SPAC6G9.11	(Figure 2E)
PMID:29290560	FYPO:0002380	viable spheroid vegetative cell [has_penetrance] high	(Figure 3C)
PMID:29290560	FYPO:0002380	viable spheroid vegetative cell [has_penetrance] high	(Figure 3C)
PMID:29290560	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering	(Figures 1C and S1C) ER-PM contact removal
PMID:29290560	FYPO:0004730	protein mislocalized to lateral cell cortex [assayed_using] PomBase:SPCC1235.10c	(Figures 1D and S1F)
PMID:29290560	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering	(Figures 1D and S1F) ER-PM uncoupling (comment: *********lateral PM)
PMID:29292846	GO:0005515	protein binding	(Fig. 1a) (comment: residues 200-307)
PMID:29292846	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC18G6.10 [assayed_using] PomBase:SPBC19C7.10	(Fig. 2)
PMID:29292846	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC18G6.10 [assayed_using] PomBase:SPBC19C7.10	(Fig. 2)
PMID:29292846	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC18G6.10 [assayed_using] PomBase:SPBC19C7.10	(Fig. 2)
PMID:29292846	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC18G6.10 [assayed_using] PomBase:SPBC19C7.10	(Fig. 2)
PMID:29292846	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC18G6.10 [assayed_using] PomBase:SPBC19C7.10	(Fig. 2)
PMID:29292846	FYPO:0000659	abolished DNA binding	(Fig. 3)
PMID:29292846	FYPO:0000655	normal DNA binding	(Fig. 3)
PMID:29292846	FYPO:0000655	normal DNA binding	(Fig. 3)
PMID:29292846	GO:0005635	nuclear envelope	(Fig. 4)
PMID:29292846	GO:0044732	mitotic spindle pole body	(Fig. 4)
PMID:29292846	GO:0005635	nuclear envelope	(Fig. 4)
PMID:29292846	FYPO:0002967	normal protein localization to mitotic spindle pole body	(Fig. 5)
PMID:29292846	FYPO:0002969	increased protein localization to mitotic spindle pole body [has_severity] high [assayed_using] PomBase:SPAC18G6.10	(Fig. 5)
PMID:29292846	FYPO:0002969	increased protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC18G6.10	(Fig. 5)
PMID:29292846	FYPO:0002339	decreased protein localization to nuclear periphery [has_severity] high [assayed_using] PomBase:SPAC18G6.10	(Fig. 5)
PMID:29292846	FYPO:0002563	normal protein localization to nuclear periphery [assayed_using] PomBase:SPAC14C4.05c	(Fig. 5)
PMID:29292846	FYPO:0002568	abolished protein localization to nuclear periphery [assayed_using] PomBase:SPAC18G6.10	(Fig. 5)
PMID:29292846	FYPO:0005612	normal protein localization to nuclear envelope	(Fig. 5)
PMID:29292846	GO:0003690	double-stranded DNA binding	(comment: DNA binding site: 1-60 a.a.)
PMID:29292846	GO:0019237	centromeric DNA binding	(comment: Deletion of LEM domain decreases the association of Lem2 at the centromere)
PMID:29319508	FYPO:0002488	cell lysis [has_penetrance] high	A phenotype in which a cell lyses, i.e. the plasma membrane ruptures and cytoplasm is lost, in presence of higher concentration of 2-deoxyglucose.
PMID:29319508	FYPO:0000064	resistance to 2-deoxyglucose	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of cell
PMID:29319508	FYPO:0000064	resistance to 2-deoxyglucose	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of cell
PMID:29319508	FYPO:0000064	resistance to 2-deoxyglucose	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of cell
PMID:29319508	FYPO:0000064	resistance to 2-deoxyglucose	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of cell
PMID:29319508	FYPO:0000064	resistance to 2-deoxyglucose [has_severity] high	An increased resistance to cell lysis induced by the presence of higher concentration of 2-deoxyglucose in the vegetative growth phase of life cycle of cell
PMID:29330317	FYPO:0004481	abolished cell population growth at high temperature	To identify novel factors involved in the TORC1 pathway, we screened for mutants that showed temperature sensitivity for growth and were derepressed for sexual differentiation at the restrictive temperature, similar to tor2‐ts mutants. We introduced mutations randomly in homothallic wild‐type cells and isolated mutants that could grow at 25°C, but not at 34°C. From these isolated mutants, we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions. We obtained eight mutants and designated them hmt, standing for hypermating and temperature‐sensitive growth.
PMID:29330317	FYPO:0004481	abolished cell population growth at high temperature	To identify novel factors involved in the TORC1 pathway, we screened for mutants that showed temperature sensitivity for growth and were derepressed for sexual differentiation at the restrictive temperature, similar to tor2‐ts mutants. We introduced mutations randomly in homothallic wild‐type cells and isolated mutants that could grow at 25°C, but not at 34°C. From these isolated mutants, we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions. We obtained eight mutants and designated them hmt, standing for hypermating and temperature‐sensitive growth.
PMID:29330317	FYPO:0004481	abolished cell population growth at high temperature	To identify novel factors involved in the TORC1 pathway, we screened for mutants that showed temperature sensitivity for growth and were derepressed for sexual differentiation at the restrictive temperature, similar to tor2‐ts mutants. We introduced mutations randomly in homothallic wild‐type cells and isolated mutants that could grow at 25°C, but not at 34°C. From these isolated mutants, we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions. We obtained eight mutants and designated them hmt, standing for hypermating and temperature‐sensitive growth.
PMID:29330317	FYPO:0004481	abolished cell population growth at high temperature	To identify novel factors involved in the TORC1 pathway, we screened for mutants that showed temperature sensitivity for growth and were derepressed for sexual differentiation at the restrictive temperature, similar to tor2‐ts mutants. We introduced mutations randomly in homothallic wild‐type cells and isolated mutants that could grow at 25°C, but not at 34°C. From these isolated mutants, we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions. We obtained eight mutants and designated them hmt, standing for hypermating and temperature‐sensitive growth.
PMID:29330317	FYPO:0004481	abolished cell population growth at high temperature	To identify novel factors involved in the TORC1 pathway, we screened for mutants that showed temperature sensitivity for growth and were derepressed for sexual differentiation at the restrictive temperature, similar to tor2‐ts mutants. We introduced mutations randomly in homothallic wild‐type cells and isolated mutants that could grow at 25°C, but not at 34°C. From these isolated mutants, we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions. We obtained eight mutants and designated them hmt, standing for hypermating and temperature‐sensitive growth.
PMID:29330317	FYPO:0004481	abolished cell population growth at high temperature	To identify novel factors involved in the TORC1 pathway, we screened for mutants that showed temperature sensitivity for growth and were derepressed for sexual differentiation at the restrictive temperature, similar to tor2‐ts mutants. We introduced mutations randomly in homothallic wild‐type cells and isolated mutants that could grow at 25°C, but not at 34°C. From these isolated mutants, we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions. We obtained eight mutants and designated them hmt, standing for hypermating and temperature‐sensitive growth.
PMID:29330317	FYPO:0004481	abolished cell population growth at high temperature	To identify novel factors involved in the TORC1 pathway, we screened for mutants that showed temperature sensitivity for growth and were derepressed for sexual differentiation at the restrictive temperature, similar to tor2‐ts mutants. We introduced mutations randomly in homothallic wild‐type cells and isolated mutants that could grow at 25°C, but not at 34°C. From these isolated mutants, we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions. We obtained eight mutants and designated them hmt, standing for hypermating and temperature‐sensitive growth.
PMID:29330317	FYPO:0004481	abolished cell population growth at high temperature	To identify novel factors involved in the TORC1 pathway, we screened for mutants that showed temperature sensitivity for growth and were derepressed for sexual differentiation at the restrictive temperature, similar to tor2‐ts mutants. We introduced mutations randomly in homothallic wild‐type cells and isolated mutants that could grow at 25°C, but not at 34°C. From these isolated mutants, we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions. We obtained eight mutants and designated them hmt, standing for hypermating and temperature‐sensitive growth.
PMID:29330317	FYPO:0004481	abolished cell population growth at high temperature	To identify novel factors involved in the TORC1 pathway, we screened for mutants that showed temperature sensitivity for growth and were derepressed for sexual differentiation at the restrictive temperature, similar to tor2‐ts mutants. We introduced mutations randomly in homothallic wild‐type cells and isolated mutants that could grow at 25°C, but not at 34°C. From these isolated mutants, we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions. We obtained eight mutants and designated them hmt, standing for hypermating and temperature‐sensitive growth.
PMID:29330317	FYPO:0004481	abolished cell population growth at high temperature	To identify novel factors involved in the TORC1 pathway, we screened for mutants that showed temperature sensitivity for growth and were derepressed for sexual differentiation at the restrictive temperature, similar to tor2‐ts mutants. We introduced mutations randomly in homothallic wild‐type cells and isolated mutants that could grow at 25°C, but not at 34°C. From these isolated mutants, we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions. We obtained eight mutants and designated them hmt, standing for hypermating and temperature‐sensitive growth.
PMID:29330317	FYPO:0003031	mating without nitrogen starvation	we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions.
PMID:29330317	FYPO:0003031	mating without nitrogen starvation	we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions.
PMID:29330317	FYPO:0003031	mating without nitrogen starvation	we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions.
PMID:29330317	FYPO:0003031	mating without nitrogen starvation	we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions.
PMID:29330317	FYPO:0003031	mating without nitrogen starvation	we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions.
PMID:29330317	FYPO:0003031	mating without nitrogen starvation	we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions.
PMID:29330317	FYPO:0003031	mating without nitrogen starvation	we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions.
PMID:29330317	FYPO:0003031	mating without nitrogen starvation	we picked those that initiated sexual differentiation at 30°C under nutrient‐rich conditions.
PMID:29343550	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPAC1F5.04c [part_of] negative regulation of mitotic actomyosin contractile ring assembly [happens_during] mitotic metaphase	(Figure 1A-B)
PMID:29343550	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPAC1F5.04c	(Figure 1C)
PMID:29343550	FYPO:0002177	viable vegetative cell with normal cell morphology	(Figure 2C)
PMID:29343550	FYPO:0002060	viable vegetative cell population	(Figure 2C)
PMID:29343550	FYPO:0005467	decreased protein localization to actomyosin contractile ring during mitosis [assayed_using] PomBase:SPAC1F5.04c	(Figure 3A)
PMID:29343550	FYPO:0005467	decreased protein localization to actomyosin contractile ring during mitosis [assayed_using] PomBase:SPAC1F5.04c	(Figure 3A)
PMID:29343550	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC20G8.05c	(Figure 4)
PMID:29343550	FYPO:0004737	decreased F-actin level in actomyosin contractile ring during early mitosis	(Figure 4A)
PMID:29343550	FYPO:0004740	normal actomyosin contractile ring	(Figure 4A)
PMID:29343550	FYPO:0004741	normal F-actin level in actomyosin contractile ring during anaphase B	(Figure 4A)
PMID:29343550	FYPO:0004741	normal F-actin level in actomyosin contractile ring during anaphase B	(Figure 4A)
PMID:29343550	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC20G8.05c	(Figure 4C)
PMID:29343550	FYPO:0005467	decreased protein localization to actomyosin contractile ring during mitosis [assayed_using] PomBase:SPAC15A10.08	(Figure 4E)
PMID:29343550	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC15A10.08	(Figure 4E-F)
PMID:29343550	FYPO:0001365	decreased rate of actomyosin contractile ring contraction	(Figure 5)
PMID:29343550	FYPO:0003339	decreased rate of actomyosin contractile ring assembly	(Figure 5)
PMID:29343550	FYPO:0005020	normal duration of actomyosin contractile ring contraction	(Figure 5)
PMID:29343550	FYPO:0003339	decreased rate of actomyosin contractile ring assembly	(Figure 5)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 2)
PMID:29352077	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 2)
PMID:29352077	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 3)
PMID:29352077	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 3)
PMID:29352077	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 3)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 3)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 3)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 3)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 3)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 3)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 3)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 3)
PMID:29352077	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 3)
PMID:29352077	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 3)
PMID:29352077	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 3)
PMID:29352077	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 3)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:29352077	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:29352077	GO:0004843	cysteine-type deubiquitinase activity [has_input] PomBase:SPCC622.09	(Figure 4F)
PMID:29414789	FYPO:0002243	increased acid phosphatase activity	(Fig. 8c)
PMID:29414789	GO:0140256	negative regulation of cellular response to phosphate starvation	(comment: CHECK GONEW: negative regulation of cellular response to phosphate starvation)
PMID:29414789	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPNCRNA.9001	(comment: Northern blot and primer extension analysis)
PMID:29414789	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC8E4.01c	(comment: Northern blot and primer extension analysis)
PMID:29414789	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC8E4.01c	(comment: Northern blot and primer extension analysis)
PMID:29414789	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC8E4.01c	(comment: Northern blot and primer extension analysis)
PMID:29414789	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC8E4.01c	(comment: Northern blot and primer extension analysis)
PMID:29414789	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPNCRNA.1712	(comment: Primer Extension Analysis)
PMID:29414789	FYPO:0003161	RNA absent from cell during vegetative growth [assayed_using] PomBase:SPBP4G3.02	(comment: Primer extension analysis)
PMID:29414789	FYPO:0003161	RNA absent from cell during vegetative growth [assayed_using] PomBase:SPBP4G3.02	(comment: Primer extension analysis)
PMID:29414789	FYPO:0003161	RNA absent from cell during vegetative growth [assayed_using] PomBase:SPBP4G3.02	(comment: Primer extension analysis)
PMID:29414789	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC8E4.01c	(comment: Primer extension analysis)
PMID:29414789	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBP4G3.02	(comment: Primer extension analysis)
PMID:29414789	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC8E4.01c	(comment: Primer extension analysis)
PMID:29414789	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBP4G3.02	(comment: Primer extension analysis)
PMID:29414789	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPNCRNA.1712	(comment: Primer extension analysis)
PMID:29422501	FYPO:0003107	progressively shortening telomeres during vegetative growth [has_severity] high [has_penetrance] high	(Fig. 1a)
PMID:29422501	FYPO:0003106	stable shortened telomeres during vegetative growth [has_severity] high [has_penetrance] high	(Fig. 1c)
PMID:29422501	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium [has_penetrance] medium	(Fig. 1c)
PMID:29422501	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium [has_severity] low	(Fig. 1c)
PMID:29422501	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium [has_severity] low	(Fig. 1c)
PMID:29422501	FYPO:0003107	progressively shortening telomeres during vegetative growth [has_severity] high [has_penetrance] high	(Fig. 2)
PMID:29422501	FYPO:0003107	progressively shortening telomeres during vegetative growth [has_severity] high [has_penetrance] high	(Fig. 2)
PMID:29422501	FYPO:0003107	progressively shortening telomeres during vegetative growth [has_severity] high [has_penetrance] high	(Fig. 2)
PMID:29422501	FYPO:0006466	decreased mature ncRNA level [has_severity] high [has_penetrance] high [assayed_using] telomerase_RNA	(Fig. 3a)
PMID:29422503	GO:0007004	telomere maintenance via telomerase	(Fig. 1)
PMID:29422503	FYPO:0003107	progressively shortening telomeres during vegetative growth	(Fig. 1) Lose telomere signal, much like trt1∆ cells.
PMID:29422503	GO:1904868	telomerase catalytic core complex assembly	(Fig. 1-3)
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPBC29A3.14c [has_severity] medium	(Fig. 1C,D)
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [has_severity] medium [assayed_using] PomBase:SPBC2D10.13	(Fig. 1C,D)
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPBC29A3.14c [has_severity] high	(Fig. 1C,D)
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPAC17G6.17 [has_severity] high	(Fig. 1C,D)
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [has_severity] high [assayed_using] PomBase:SPBC2D10.13	(Fig. 1C,D)
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPAC17G6.17 [has_severity] high	(Fig. 1E)
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPAC17G6.17 [has_severity] high	(Fig. 1E)
PMID:29422503	GO:0140445	chromosome, telomeric repeat region	(Fig. 1e)
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPAC17G6.17	(Fig. 1e) Localization of Pof8 at telomeres is reduced but not eliminated in ccq1∆.
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPAC17G6.17	(Fig. 1e) Localization of Pof8 at telomeres is reduced but not eliminated in est1∆.
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPAC17G6.17	(Fig. 1e) Localization of Pof8 at telomeres is reduced but not eliminated in ter1∆.
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPAC17G6.17	(Fig. 1e) Localization of Pof8 at telomeres is reduced but not eliminated in trt1∆.
PMID:29422503	GO:0070034	telomerase RNA binding [part_of] telomerase catalytic core complex assembly	(Fig. 3a)
PMID:29422503	FYPO:0002357	normal protein-RNA interaction [assayed_using] PomBase:SPAC17G6.17 [assayed_using] telomerase_RNA	(Fig. 3a) Pof8-TER1 interaction is not affected by est1∆.
PMID:29422503	FYPO:0002134	decreased protein-RNA interaction [assayed_using] PomBase:SPAC17G6.17 [assayed_using] telomerase_RNA	(Fig. 3a) Pof8-TER1 interaction is reduced but not eliminated in ccq1∆.
PMID:29422503	FYPO:0002134	decreased protein-RNA interaction [assayed_using] PomBase:SPAC17G6.17 [assayed_using] telomerase_RNA	(Fig. 3a) Pof8-TER1 interaction is reduced but not eliminated in trt1∆ cells.
PMID:29422503	GO:0070034	telomerase RNA binding [part_of] telomerase catalytic core complex assembly	(Fig. 3b)
PMID:29422503	FYPO:0002134	decreased protein-RNA interaction [assayed_using] PomBase:SPNCRNA.214 [assayed_using] PomBase:SPBC29A3.14c	(Fig. 3b)
PMID:29422503	FYPO:0002357	normal protein-RNA interaction [assayed_using] PomBase:SPBC2D10.13 [assayed_using] telomerase_RNA	(Fig. 3c) Interaction between Est1 and TER1 was not affected by pof8∆.
PMID:29422503	FYPO:0000826	decreased RNA level [assayed_using] telomerase_RNA	(Fig. 4a) Expression level of telomerase RNA TER1 is reduced but not eliminated in pof8∆ cells. Expression level for telomerase RNA pre-cursor was not affected by pof8∆.
PMID:29422503	FYPO:0002133	abolished protein-RNA interaction [assayed_using] PomBase:SPBC9B6.05c [assayed_using] telomerase_RNA	(Fig. 4c) Lsm3-TER1 interaction is abolished in pof8∆ cells.
PMID:29422503	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC9B6.05c [assayed_using] PomBase:SPAC17G6.17	(Fig. 4d)
PMID:29422503	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC9B6.05c [assayed_using] PomBase:SPBC29A3.14c	(Fig. 4e)
PMID:29422503	FYPO:0002887	normal protein localization to telomere during vegetative growth [assayed_using] PomBase:SPBC9B6.05c	(Fig. 4f)
PMID:29422503	FYPO:0004656	increased protein localization to telomere during vegetative growth [assayed_using] PomBase:SPBC9B6.05c	(Fig. 4f) Lsm3 binding at telomeres is increased by ter1∆.
PMID:29422503	FYPO:0002887	normal protein localization to telomere during vegetative growth [assayed_using] PomBase:SPBC9B6.05c	(Fig. 4f) Lsm3 binding to telomeres was not affected by est1∆.
PMID:29422503	FYPO:0002887	normal protein localization to telomere during vegetative growth [assayed_using] PomBase:SPBC9B6.05c	(Fig. 4f) Lsm3 binding to telomeres was not affected by trt1∆.
PMID:29422503	FYPO:0002134	decreased protein-RNA interaction [assayed_using] PomBase:SPBC29A3.14c [assayed_using] telomerase_RNA	(Fig. 5)
PMID:29422503	FYPO:0002239	shortened telomeres during vegetative growth	(Fig. 5)
PMID:29422503	FYPO:0002134	decreased protein-RNA interaction [assayed_using] PomBase:SPBC29A3.14c [assayed_using] PomBase:SPNCRNA.214	(Fig. 5)
PMID:29422503	FYPO:0002687	normal telomere length during vegetative growth	(Fig. 5)
PMID:29422503	FYPO:0001890	increased RNA level [assayed_using] telomerase_RNA	(Fig. 5)
PMID:29422503	FYPO:0002133	abolished protein-RNA interaction [assayed_using] telomerase_RNA [assayed_using] PomBase:SPAC17G6.17	(Fig. 6)
PMID:29422503	FYPO:0000826	decreased RNA level [assayed_using] telomerase_RNA	(Fig. 6)
PMID:29422503	FYPO:0003106	stable shortened telomeres during vegetative growth	(Fig. 6) pof8-R343A cells show as short telomere as pof8∆ cells.
PMID:29422503	FYPO:0003106	stable shortened telomeres during vegetative growth	(Fig. 6) pof8-Y330A cells show as short telomere as pof8∆ cells.
PMID:29422503	FYPO:0003106	stable shortened telomeres during vegetative growth	(Fig. 6) pof8-∆[289-402] cells show as short telomere as pof8∆ cells.
PMID:29422503	FYPO:0003106	stable shortened telomeres during vegetative growth	(Fig. 6) pof8-∆[390-402] cells show as short telomere as pof8∆ cells.
PMID:29422503	FYPO:0002133	abolished protein-RNA interaction [assayed_using] telomerase_RNA [assayed_using] PomBase:SPAC17G6.17	(Fig. 6b)
PMID:29422503	FYPO:0003106	stable shortened telomeres during vegetative growth	(Figure 1a)
PMID:29422503	FYPO:0003106	stable shortened telomeres during vegetative growth	(Figure 1a) Telomere shortening is similar to pof8∆ cells.
PMID:29422503	FYPO:0000840	normal RNA level [assayed_using] telomerase_RNA	(Supplementary Fig. 4)
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPBC29A3.14c	Based on ChIP, ter1∆ cause loss of telomerase (Trt1) localization at telomeres.
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPBC2D10.13	Est1 binding to telomeres is reduced to near no binding in ter1∆, based on ChIP assay.
PMID:29422503	FYPO:0004083	normal protein level [assayed_using] PomBase:SPBC2D10.13	Est1 expression level detected by western in ter1∆ cells was similar to Est1 level in ter1+ (wild-type) cells.
PMID:29422503	FYPO:0004083	normal protein level [assayed_using] PomBase:SPBC2D10.13	Est1 showed similar expression level in pof8∆ cells as wild-type cells.
PMID:29422503	FYPO:0002980	increased chromatin binding [assayed_using] PomBase:SPBC9B6.05c [assayed_using] chromosome_arm	Lsm3 binding was detected at ars2004, non-ARS, ade6+ and his1+ loci. In ter1∆ cells, Lsm3 binding to those non-telmeric sites were increased.
PMID:29422503	FYPO:0004083	normal protein level [assayed_using] PomBase:SPBC9B6.05c	Lsm3 protein level was not affected by est1∆.
PMID:29422503	FYPO:0004083	normal protein level [assayed_using] PomBase:SPBC9B6.05c	Lsm3 protein level was not affected by pof8∆.
PMID:29422503	FYPO:0004083	normal protein level [assayed_using] PomBase:SPBC9B6.05c	Lsm3 protein level was not affected by ter1∆.
PMID:29422503	FYPO:0004083	normal protein level [assayed_using] PomBase:SPBC9B6.05c	Lsm3 protein level was not affected by trt1∆.
PMID:29422503	FYPO:0004083	normal protein level [assayed_using] PomBase:SPAC17G6.17	Pof8 expression level is not affected by trt1∆.
PMID:29422503	FYPO:0004083	normal protein level [assayed_using] PomBase:SPAC17G6.17	Pof8 expression level is not affected in ccq1∆.
PMID:29422503	FYPO:0004083	normal protein level [assayed_using] PomBase:SPAC17G6.17	Pof8 expression level was not altered in ter1∆ cells.
PMID:29422503	FYPO:0004083	normal protein level [assayed_using] PomBase:SPAC17G6.17	Pof8 expression was not affected by est1∆.
PMID:29422503	FYPO:0000840	normal RNA level [assayed_using] telomerase_RNA	Supplementary Fig. 4
PMID:29422503	FYPO:0000840	normal RNA level [assayed_using] PomBase:SPNCRNA.214	Supplementary Fig. 4
PMID:29422503	FYPO:0000840	normal RNA level [assayed_using] telomerase_RNA	Supplementary Fig. 4
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPBC2D10.13	Telomere binding of Est1 is reduced in pof8∆ cells.
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPBC29A3.14c	Trt1 binding is reduced to ~58% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%).
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [has_penetrance] 69 [assayed_using] PomBase:SPBC29A3.14c	Trt1 binding is reduced to ~69% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%).
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPBC29A3.14c	Trt1 binding is reduced to ~70% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%).
PMID:29422503	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPBC29A3.14c	Trt1 binding is reduced to ~80% of pof8+ cells, but not as severely reduced as pof8∆ cells (~35%).
PMID:29422503	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPBC29A3.14c	Trt1 expression level detected by western blot is reduced in ter1∆ cells.
PMID:29422503	FYPO:0002134	decreased protein-RNA interaction [assayed_using] PomBase:SPBC29A3.14c [assayed_using] telomerase_RNA	Trt1-TER1 interaction is reduced but not eliminated in pof8-∆[289-4020]. Extent of reduction in Trt1-TER1 is similar to pof8∆ cells.
PMID:29422503	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPBC29A3.14c	moderately reduced less severe thanin ter1∆ cells.
PMID:29422503	FYPO:0003106	stable shortened telomeres during vegetative growth [has_severity] low	pof8∆ poz1∆ cells showed very slightly shortend telomeres, rather than highly elongated telomeres in poz1∆ cells. (This strain showed longer telomere than pof8∆ cells.)
PMID:29422503	FYPO:0003106	stable shortened telomeres during vegetative growth [has_severity] low	pof8∆ rap1∆ cells showed shortened telomeres, more similar to pof8∆, rather than highly elongated telomeres in rap1∆ cells.
PMID:29422503	FYPO:0003106	stable shortened telomeres during vegetative growth	pof8∆ rif1∆ cells showed short telomeres, very similar to pof8∆ cells.
PMID:29422503	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] low	pof8∆ taz1∆ showed much shorter telomere length (almost like wild-type cells) than taz1∆ cells, but showed some rearrangement in sub-telomeres.
PMID:29424342	GO:0006406	mRNA export from nucleus	(Fig. 2)
PMID:29424342	FYPO:0002133	abolished protein-RNA interaction [assayed_enzyme] PomBase:SPCC736.12c [assayed_substrate] PomBase:SPBC32H8.11	(Fig. 4)
PMID:29424342	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC736.12c [assayed_using] PomBase:SPAC1006.03c	(Fig. 4)
PMID:29424342	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC736.12c [assayed_using] PomBase:SPCC736.12c	(Fig. 4)
PMID:29424342	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC736.12c [assayed_using] PomBase:SPCC736.12c	(Fig. 4)
PMID:29424342	FYPO:0000783	protein mislocalized to cytoplasm during vegetative growth [assayed_using] PomBase:SPCC736.12c	(Fig. 4)
PMID:29424342	FYPO:0000838	normal protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPCC736.12c	(Fig. 4B)
PMID:29424342	FYPO:0006862	RNA mislocalized to cytoplasm during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	(Fig. 5)
PMID:29424342	FYPO:0006862	RNA mislocalized to cytoplasm during vegetative growth [assayed_using] PomBase:SPBC32H8.11	(Fig. 5)
PMID:29424342	FYPO:0006862	RNA mislocalized to cytoplasm during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	(Fig. 5)
PMID:29424342	FYPO:0006862	RNA mislocalized to cytoplasm during vegetative growth [assayed_using] PomBase:SPBC32H8.11	(Fig. 5)
PMID:29424342	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC736.12c [assayed_using] PomBase:SPCC736.12c	(Fig. 6)
PMID:29424342	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC736.12c [assayed_using] PomBase:SPAC19G12.17	(Fig. 6)
PMID:29424342	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC736.12c [assayed_using] PomBase:SPAC1006.03c	(Fig. 6)
PMID:29432178	FYPO:0000249	decreased cell population growth on ammonia nitrogen source [has_severity] variable severity [has_severity] high	(Fig. 3A)
PMID:29432178	FYPO:0000249	decreased cell population growth on ammonia nitrogen source [has_severity] low	(Fig. 3A)
PMID:29432178	FYPO:0001357	normal vegetative cell population growth	(Fig. 3A)
PMID:29432178	GO:0045944	positive regulation of transcription by RNA polymerase II [part_of] positive regulation of amino acid biosynthetic process [happens_during] cellular response to amino acid starvation	(Fig. 3B) (comment: CHECK during normal growth)
PMID:29432178	FYPO:0006473	decreased transcription of amino acid biosynthesis genes in response to amino acid starvation	(Fig. 3E)
PMID:29432178	FYPO:0001234	slow vegetative cell population growth	(comment: CHECK Can we say somewhere - overexpresses genes involved by amino acid starvation, or something similar?)
PMID:29432178	FYPO:0006474	abnormal regulation of translation in response to amino acid starvation	Ribosome profiling and matching RNA-seq in gcn2Δ cells treated or untreated with 3-AT revealed that the majority of the translationally induced genes did not respond to amino acid starvation (Fig. 2B)
PMID:29432178	FYPO:0006444	abnormal transcriptional response to amino acid starvation	the expression of most genes induced by amino acid starvation in wild-type cells was not up-regulated, confirming that Gcn2 is the major mediator of this response
PMID:29453312	GO:1990819	mating projection actin fusion focus	(comment: Active Ras1 co-localizes with the actin fusion focus during the process of cell-cell fusion)
PMID:29453312	GO:0051285	cell cortex of cell tip [exists_during] mitotic cell cycle phase	(comment: Active Ras1 is localized to cell poles during mitotic growth)
PMID:29453312	GO:0000935	division septum [exists_during] mitotic cell cycle phase	(comment: Active Ras1 localizes to septa during mitotic growth)
PMID:29453312	GO:1990819	mating projection actin fusion focus	(comment: Ste6 co-localizes with the actin fusion focus during the process of cell-cell fusion)
PMID:29453312	FYPO:0006220	abolished protein localization to septum [assayed_using] ras1/GTP+	In the absence of efc25 Ras1 is not activated at the cell cortex
PMID:29453312	FYPO:0006502	abolished protein localization to cell cortex of cell tip during vegetative growth [assayed_using] ras1/GTP+	In the absence of efc25 Ras1 is not activated at the cell cortex
PMID:29453312	FYPO:0004730	protein mislocalized to lateral cell cortex [assayed_using] ras1/GTP+	In the absence of gap1 Ras activity increases and decorates the entire cortex of vegetative growing cells
PMID:29453312	GO:1902917	positive regulation of mating projection assembly	Ras activity increases during the mating process and is maximum at the fusion site just before the fusion event.
PMID:29453312	FYPO:0006500	premature cell wall disassembly at cell fusion site [has_penetrance] 28	ras1 mutant cells undergo precocious fusion resulting in cell lysis
PMID:29453312	FYPO:0006500	premature cell wall disassembly at cell fusion site [has_penetrance] 26	ras1 mutant cells undergo precocious fusion resulting in cell lysis
PMID:29458562	FYPO:0004085	decreased vegetative cell growth	(Fig. 2)
PMID:29458562	FYPO:0000245	loss of viability in stationary phase	(Fig. 2)
PMID:29458562	FYPO:0002060	viable vegetative cell population	(Fig. 2)
PMID:29458562	FYPO:0004085	decreased vegetative cell growth	(Fig. 2)
PMID:29458562	FYPO:0000562	abolished cellular respiration	(Fig. 2) (comment: likey due to intron encoded maturase)
PMID:29458562	FYPO:0003423	decreased mitochondrial RNA level [has_severity] medium [assayed_using] PomBase:SPMIT.04	(Fig. 3)
PMID:29458562	FYPO:0003423	decreased mitochondrial RNA level [assayed_using] PomBase:SPMIT.05 [has_severity] medium	(Fig. 3)
PMID:29458562	FYPO:0003423	decreased mitochondrial RNA level [has_severity] medium [assayed_using] PomBase:SPMIT.11	(Fig. 3)
PMID:29458562	FYPO:0003423	decreased mitochondrial RNA level [assayed_using] PomBase:SPMIT.01 [has_penetrance] complete	(Fig. 3) (comment: CHECK abolished)
PMID:29458562	FYPO:0003915	decreased mitochondrial protein level [assayed_using] PomBase:SPAC1296.02	(Fig. 4)
PMID:29458562	FYPO:0006446	increased mitochondrial pre-mRNA level [assayed_using] PomBase:SPMIT.05	(Fig. 4)
PMID:29458562	FYPO:0006446	increased mitochondrial pre-mRNA level [assayed_using] PomBase:SPAC1296.02	(Fig. 4)
PMID:29458562	FYPO:0004530	abolished mitochondrial translation [assayed_using] PomBase:SPMIT.01	(Fig. 4)
PMID:29458562	FYPO:0002056	decreased mitochondrial translation [assayed_using] PomBase:SPMIT.11	(Fig. 4)
PMID:29458562	FYPO:0004153	increased flocculation in stationary phase	DNS
PMID:29514920	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC18B5.03 [occurs_in] medial cortical node [happens_during] mitotic G2 phase	(Fig. 1A)
PMID:29514920	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC18B5.03 [part_of] positive regulation of protein localization to medial cortical node [occurs_in] medial cortical node [happens_during] mitotic G2 phase	(Fig. 1A)
PMID:29514920	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC18B5.03	(Fig. 1A)
PMID:29514920	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC644.06c	(Fig. 1A)
PMID:29514920	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC644.06c	(Fig. 1A)
PMID:29514920	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC18B5.03	(Fig. 1A)
PMID:29514920	FYPO:0003919	abolished protein localization to medial cortical node [assayed_using] PomBase:SPAC57A10.02	(Fig. 1B)
PMID:29514920	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC18B5.03	(Fig. 1C)
PMID:29514920	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC18B5.03 [assayed_using] PomBase:SPAC57A10.02	(Fig. 2B)
PMID:29514920	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC18B5.03 [assayed_using] PomBase:SPAC57A10.02	(Fig. 2B)
PMID:29514920	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC18B5.03 [assayed_using] PomBase:SPAC57A10.02	(Fig. 2B)
PMID:29514920	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC18B5.03 [assayed_using] PomBase:SPAC57A10.02	(Fig. 2B)
PMID:29514920	FYPO:0003919	abolished protein localization to medial cortical node [assayed_using] PomBase:SPCC18B5.03	(Fig. 2C) (comment: protein localizes to cytoplasm, nucleus, and spindle-pole body)
PMID:29514920	FYPO:0001492	viable elongated vegetative cell [has_penetrance] medium	(Fig. 2D) (comment: Epistatic to cdr2delta)
PMID:29514920	GO:0110115	Cdr2 medial cortical node complex [exists_during] mitotic interphase	(Fig. 3A, 3B S2, A and B) IN TRANSIENT BURSTS & progressive increase in the number of Wee1 nodes as a function of cell size, ... 20X in Wee1 nodes in large cells versus small cells (Fig. 4 B).
PMID:29514920	FYPO:0001492	viable elongated vegetative cell [has_penetrance] medium	(Figure 2D) (commment: Epistatic to cdr2delta)
PMID:29514920	FYPO:0006326	decreased protein localization to medial cortical node [assayed_using] PomBase:SPCC18B5.03	Fig. 3D
PMID:29514920	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPAC644.06c	Fig. S2, F and G
PMID:29529046	FYPO:0006827	decreased cytosolic zinc level [has_penetrance] high	(Fig. 4B,E)
PMID:29529046	FYPO:0006828	increased cytosolic zinc level [has_severity] high	(Fig. 5A,B) In this paper we used a high affinity zinc-responsive FRET sensor (ZapCY1) to measure zinc ion availability in the cytosol under conditions of zinc deficiency. Thus, in addition to accumulating high levels of total cellular zinc - this manuscript shows that loz1D cells also accumulate higher levels of zinc in the cytosol. This accumulation is also dependent upon Zrt1 as this phenotype is not observed in a loz1 zrt1 double mutant
PMID:29529046	FYPO:0006828	increased cytosolic zinc level [has_severity] medium	(Fig. 6)
PMID:29529046	FYPO:0006334	decreased RNA level during cellular response to zinc ion starvation [assayed_using] PomBase:SPBC16D10.06	(Fig. 8)
PMID:29529046	FYPO:0006829	normal RNA level during cellular response to zinc ion starvation [assayed_using] PomBase:SPAC17D4.03c	(Fig. 8)
PMID:29529046	FYPO:0006830	normal RNA level during cellular response to replete zinc [assayed_using] PomBase:SPAC17D4.03c	(Fig. 8)
PMID:29529046	FYPO:0006830	normal RNA level during cellular response to replete zinc [assayed_using] PomBase:SPBC16E9.14c	(Fig. 8)
PMID:29529046	FYPO:0006829	normal RNA level during cellular response to zinc ion starvation [assayed_using] PomBase:SPBC16E9.14c	(Fig. 8)
PMID:29529046	FYPO:0006830	normal RNA level during cellular response to replete zinc [assayed_using] PomBase:SPAC23C11.14	(Fig. 8)
PMID:29529046	FYPO:0006829	normal RNA level during cellular response to zinc ion starvation [assayed_using] PomBase:SPAC23C11.14	(Fig. 8)
PMID:29529046	FYPO:0006334	decreased RNA level during cellular response to zinc ion starvation [assayed_using] PomBase:SPBC16D10.06	(Fig. 8)
PMID:29529046	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 1) (comment: CHECK EDTA, zinc chelator)
PMID:29529046	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1) (comment: CHECK EDTA, zinc chelator)
PMID:29529046	FYPO:0001534	decreased cellular zinc level	(comment: The experiment performed was to measure total cellular zinc ion levels in a zrt1D strain during a zinc shock) (Figure 4A)
PMID:29529046	FYPO:0006828	increased cytosolic zinc level [has_severity] medium	(comment: The reporter gene was the the ZapCY1 high affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments so the Term name should really be increased cytoplasm, not cellular, zinc level)
PMID:29529046	FYPO:0006828	increased cytosolic zinc level [has_severity] medium	(comment: The reporter gene was the the ZapCY1 high affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments so the Term name should really be increased cytoplasm, not cellular, zinc level)
PMID:29529046	FYPO:0006828	increased cytosolic zinc level [has_penetrance] medium	(comment: The reporter gene was the the ZapCY1 high affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments, so the Term name should really be increased cytoplasm, not cellular, zinc level)
PMID:29529046	FYPO:0006828	increased cytosolic zinc level [has_severity] medium	(comment: The reporter gene was the the ZapCY1 high affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments, so the Term name should really be increased cytoplasm, not cellular, zinc level)
PMID:29529046	FYPO:0006828	increased cytosolic zinc level [has_penetrance] high	(comment: The reporter genes used were the ZapCY1 high affinity and ZapCY2 low affinity zinc-responsive FRET reporter. As this reporter is located in the cytosol and nucleus it measures zinc availability in these compartments so the Term name should really be increased cytoplasm, not cellular, zinc level)
PMID:29529046	GO:0140209	zinc ion import into endoplasmic reticulum [part_of] detoxification of zinc ion	(comment: Zhf1 is required for the rapid transport of zinc ions out of the cytosol during a zinc shock a condition where there is a rapid influx of zinc into a cell)
PMID:29529046	GO:0006882	intracellular zinc ion homeostasis	(comment: Zrg17 also transports zinc out of the cytosol when zinc is available -as well as when it is limiting)
PMID:29549126	GO:0140420	heme import into cell	(Fig. 3B, C)
PMID:29549126	GO:1904334	heme import across plasma membrane	(Fig. 3B, C) We therefore concluded that Shu1 is required for hemin acquisition when hemin is present at very low concentrations (0.075 ΔM), whereas its presence is dispensable under conditions of high hemin concentrations
PMID:29549126	GO:0020037	heme binding	(Fig. 6)
PMID:29549126	GO:0020037	heme binding	(Fig. 6)
PMID:29549126	GO:0016020	membrane	(Fig. 7)
PMID:29549126	GO:0016020	membrane	(Fig. 7)
PMID:29549126	FYPO:0007396	decreased heme import [has_severity] high	(comment: assayed using heme analog ZnMP)
PMID:29549126	FYPO:0007396	decreased heme import [has_severity] low	(comment: assayed using heme analog ZnMP)
PMID:29549126	FYPO:0007397	abolished heme import	(comment: assayed using heme analog ZnMP)
PMID:29596413	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC1105.02c [has_severity] high	(Fig. 7)
PMID:29596413	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPAC56E4.03 [has_severity] high	(Fig. 7)
PMID:29596413	FYPO:0006249	normal tRNA aminoacylation [assayed_using] phenylalanyl_tRNA	(Fig. 7)
PMID:29596413	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC1773.13 [has_severity] high	(Fig. 7)
PMID:29596413	FYPO:0000840	normal RNA level [assayed_using] PomBase:SPBC1105.02c	(Fig. 7C)
PMID:29596413	FYPO:0000840	normal RNA level [assayed_using] PomBase:SPAC56E4.03	(Fig. 7C)
PMID:29596413	FYPO:0001890	increased RNA level [has_severity] medium [assayed_using] PomBase:SPAC56E4.03	(Fig. 7C)
PMID:29596413	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC1105.02c [has_severity] medium	(Fig. 7C)
PMID:29596413	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC1105.02c [has_severity] low	(Fig. 7C) (comment: CHECK supression of trm7-delta)
PMID:29596413	FYPO:0000840	normal RNA level [assayed_using] PomBase:SPBC1105.02c [has_severity] low	(Fig. 7C) (comment: CHECK supression of trm7-delta)
PMID:29596413	FYPO:0000840	normal RNA level [assayed_using] PomBase:SPAC56E4.03 [has_severity] low	(Fig. 7C) (comment: CHECK supression of trm7-delta)
PMID:29596413	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPAC56E4.03 [has_severity] low	(Fig. 7C) (comment: CHECK supression of trm7-delta)
PMID:29596413	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC1105.02c [has_severity] low	(Fig. 7C) (comment: CHECK supression of trm7-delta)
PMID:29596413	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPAC56E4.03 [has_severity] low	(Fig. 7C) (comment: CHECK supression of trm7-delta)
PMID:29610759	GO:0000785	chromatin [coincident_with] mating_type_region	(Fig 1, 4)
PMID:29610759	GO:0000785	chromatin [coincident_with] mating_type_region [part_of] H minus	(Fig. 1)
PMID:29610759	GO:0000785	chromatin [coincident_with] Mat3M [part_of] H minus	(Fig. 1)
PMID:29610759	GO:0000785	chromatin [coincident_with] mating_type_region	(Fig. 1, 4)
PMID:29610759	GO:0000785	chromatin [coincident_with] PomBase:SPAC1142.03c [part_of] H minus	(Fig. 2)
PMID:29610759	GO:1990837	sequence-specific double-stranded DNA binding [occurs_at] mating_type_region [occurs_in] H minus	(Fig. 5)
PMID:29610759	FYPO:0005353	normal replication fork arrest at RTS1 barrier	(comment: at MPS1)
PMID:29610759	GO:0000785	chromatin [coincident_with] mating_type_region	enriched at mat1 right border and cenH left border; Fig. 1
PMID:29618061	FYPO:0007279	increased protein localization to euchromatin [assayed_region] PomBase:SPBP4G3.02 [assayed_protein] PomBase:SPBC28F2.12	(Figure 1D). We found that loss of Clr3 leads to increased Pol II levels upstream of the pho1 promoter and particularly across the gene body.
PMID:29618061	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02 [has_severity] low	. Interestingly, deletion of the H3K4 methyltransferase Set1 leads to derepression of pho1 (Figure 3C). In contrast, deletion of the H3K36 methyltransferase Set2 only had a minor effect on pho1 derepression, suggesting that the mechanism underlying pho1 silencing primarily relies on histone methylation by Set1
PMID:29618061	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	Co-incident with Seb1 loss, tgp1 mRNA levels start to accrue (Supplementary Figure S3A, lane 13)
PMID:29618061	FYPO:0005518	increased histone H3-K14 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPBP4G3.02	H3K14ac levels were also increased in this strain (Figure 2D), similar to that seen in clr3Δ (Figure 1E)
PMID:29618061	FYPO:0007281	normal level of meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC359.06	However, mug14 is not affected in this exosome mutant, suggesting that the gene is likely to be regulated only at the transcriptional level (Figure 5a).
PMID:29618061	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPNCRNA.29	In agreement with a previously demonstrated role for the nuclear exosome complex in the degradation of meiotic transcripts during mitosis, we observe increased levels of meu19 and meu31 in rrp6Δ (Figure 5B and C).
PMID:29618061	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1A6.06c	In agreement with a previously demonstrated role for the nuclear exosome complex in the degradation of meiotic transcripts during mitosis, we observe increased levels of meu19 and meu31 in rrp6Δ (Figure 5B and C).
PMID:29618061	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	In contrast, deletion of TSA- insensitive sir2, which contributes to transcriptional silencing at constitutive heterochromatin, had no effect on pho1 expression (Figure 1B, lane 5).
PMID:29618061	FYPO:0004346	decreased protein localization to chromatin at ncRNA genes [assayed_protein] PomBase:SPCC736.12c	In the case of prt-3Δ, this phenotype is likely a result of lost Mmi1 recruitment since this mutant lacks the DSR motifs we previously mapped ((5,37), Figure 3A, Mmi1 CRAC). We tested Mmi1 recruitment to the prt locus in this mutant and it is indeed defective (data not shown).
PMID:29618061	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	Interestingly, elevated pho1 levels were observed in prt-1Δ, prt-2Δ, and prt-3Δ (Figure 3B, lanes 1- 4) suggesting that element(s) responsible for pho1 silencing are located within the 5′ part of prt.
PMID:29618061	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	Interestingly, elevated pho1 levels were observed in prt-1Δ, prt-2Δ, and prt-3Δ (Figure 3B, lanes 1- 4) suggesting that element(s) responsible for pho1 silencing are located within the 5′ part of prt.
PMID:29618061	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	Interestingly, elevated pho1 levels were observed in prt-1Δ, prt-2Δ, and prt-3Δ (Figure 3B, lanes 1- 4) suggesting that element(s) responsible for pho1 silencing are located within the 5′ part of prt.
PMID:29618061	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	No change in pho1 expression could be detected for either prt-4Δ or prt-5Δ (Figure 3B, lanes 5 and 6).
PMID:29618061	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	No change in pho1 expression could be detected for either prt-4Δ or prt-5Δ (Figure 3B, lanes 5 and 6).
PMID:29618061	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	No detectable increase in either tgp1 or nc-tgp1 was observed in sir2Δ, strains harbouring a clr6 mutation (Supplementary Figure S3A, lanes 6-8)
PMID:29618061	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1698	No detectable increase in either tgp1 or nc-tgp1 was observed in sir2Δ, strains harbouring a clr6 mutation (Supplementary Figure S3A, lanes 6-8)
PMID:29618061	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1698	No detectable increase in either tgp1 or nc-tgp1 was observed in sir2Δ, strains harbouring a clr6 mutation (Supplementary Figure S3A, lanes 6-8)
PMID:29618061	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	No detectable increase in either tgp1 or nc-tgp1 was observed in sir2Δ, strains harbouring a clr6 mutation (Supplementary Figure S3A, lanes 6-8)
PMID:29618061	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02 [has_severity] low	Northern blot (Supplementary Figure S1A). Compared to wild-type pho1 mRNA levels, a slight accumulation was detected for all strains. However, this is less pronounced than in clr3Δ, indicating that Clr3 is unlikely to entirely depend on Clr2 or other components of SHREC for recruitment to pho1.
PMID:29618061	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02 [has_severity] low	Northern blot (Supplementary Figure S1A). Compared to wild-type pho1 mRNA levels, a slight accumulation was detected for all strains. However, this is less pronounced than in clr3Δ, indicating that Clr3 is unlikely to entirely depend on Clr2 or other components of SHREC for recruitment to pho1.
PMID:29618061	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02 [has_severity] low	Northern blot (Supplementary Figure S1A). Compared to wild-type pho1 mRNA levels, a slight accumulation was detected for all strains. However, this is less pronounced than in clr3Δ, indicating that Clr3 is unlikely to entirely depend on Clr2 or other components of SHREC for recruitment to pho1.
PMID:29618061	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02 [has_severity] low	Of the TSA-sensitive HDACs, Clr3 was the only one that had an effect on pho1 expression, with its deletion resulting in increased pho1 mRNA levels (Figure 1B).
PMID:29618061	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4G3.02 [has_severity] high	Remarkably, this mutant showed an additive accumulation of pho1 mRNA levels (Figure 2A) and displayed a slow growth phenotype considerably more severe than either of the single mutants, clr3Δ or clr4Δ (Figure 2B).
PMID:29618061	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4G3.02 [has_severity] high	Remarkably, this mutant showed an additive accumulation of pho1 mRNA levels (Figure 2A) and displayed a slow growth phenotype considerably more severe than either of the single mutants, clr3Δ or clr4Δ (Figure 2B).
PMID:29618061	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4G3.02 [has_severity] high	Remarkably, this mutant showed an additive accumulation of pho1 mRNA levels (Figure 2A) and displayed a slow growth phenotype considerably more severe than either of the single mutants, clr3Δ or clr4Δ (Figure 2B).
PMID:29618061	GO:0000791	euchromatin [coincident_with] PomBase:SPBP4G3.02	This revealed that Clr3 indeed localizes to the gene, particularly at the non-coding region (Figure 1C).
PMID:29618061	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02 [has_severity] low	To directly assess whether this is the case and that the two proteins function as part of the same pathway we performed a Northern blot to compare a double mutant clr3Δset1Δ with the respective single mutants (Figure 3D). We found that the double mutant did not lead to higher pho1 derepression as compared to single set1Δ, indicating that both proteins do indeed function in the same pathway.
PMID:29618061	FYPO:0004346	decreased protein localization to chromatin at ncRNA genes [assayed_protein] PomBase:SPBC800.03	To test whether Clr3 recruitment depends on Set1 we performed ChIP-qPCR. In support of Set1 acting upstream of Clr3 we found the HDAC’s recruitment to the pho1 locus to be compromised in a set1Δ strain (Figure 3E).
PMID:29618061	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	Unlike at pho1, we found that deletion of clr3 has no discernible induction effect on tgp1
PMID:29618061	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	We found accumulation of tgp1 in the seb1-1 mutant compared to wild-type (Supplementary Figure S3A, compare lanes 1 and 2).
PMID:29618061	FYPO:0007505	decreased protein localization to chromatin at promoter [assayed_region] PomBase:SPBP4G3.02 [assayed_protein] PomBase:SPBC800.03	We found that, in the absence of non-coding transcription in a strain lacking the prt promoter (ncproΔ) (5), Clr3 recruitment to pho1 was reduced (Figure 2C).
PMID:29618061	FYPO:0005518	increased histone H3-K14 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPBP4G3.02	an increase in the levels of H3K14ac could be detected by ChIP-qPCR (Figure 1E)
PMID:29618061	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02 [has_severity] low	as expected, northern blot analysis revealed no obvious additive effect compared to the ncproΔ single mutant (Figure 2E).
PMID:29618061	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1698	clr4Δ, or the double mutant clr3Δclr4Δ (Supplementary Figure S3A, lane 4 and 5), also revealed no change in mRNA expression levels. These results indicate that unlike pho1, tgp1 repression
PMID:29618061	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	clr4Δ, or the double mutant clr3Δclr4Δ (Supplementary Figure S3A, lane 4 and 5), also revealed no change in mRNA expression levels. These results indicate that unlike pho1, tgp1 repression
PMID:29618061	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1698	clr4Δ, or the double mutant clr3Δclr4Δ (Supplementary Figure S3A, lane 4 and 5), also revealed no change in mRNA expression levels. These results indicate that unlike pho1, tgp1 repression
PMID:29618061	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	clr4Δ, or the double mutant clr3Δclr4Δ (Supplementary Figure S3A, lane 4 and 5), also revealed no change in mRNA expression levels. These results indicate that unlike pho1, tgp1 repression
PMID:29632066	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [assayed_using] PomBase:SPMTR.01 [has_severity] low	(Fig. S1B)
PMID:29632066	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [assayed_using] PomBase:SPMTR.01 [has_severity] low	(Fig. S1B)
PMID:29632066	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [assayed_using] PomBase:SPMTR.01 [has_severity] low	(Fig. S1B)
PMID:29641590	FYPO:0007064	increased 22S rRNA precursor level	(Fig. 3)
PMID:29641590	FYPO:0001135	increased 35S rRNA precursor level	(Fig. 3)
PMID:29641590	FYPO:0007063	increased 23S rRNA precursor level	(Fig. 3)
PMID:29641590	FYPO:0007065	20S rRNA precursor absent from cell	(Fig. 3)
PMID:29641590	GO:0000472	endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA)	(comment: A1 cleavage)
PMID:29641590	GO:0000447	endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)	(comment: A2 cleavage)
PMID:29689193	FYPO:0003889	decreased cell wall thickness at old end during vegetative growth	(Fig. 3C)
PMID:29689193	FYPO:0006746	decreased cell wall thickness at cell tip during vegetative growth	(Figure 2F)
PMID:29689193	FYPO:0001035	increased cell wall thickness during vegetative growth	(Figure 3B)
PMID:29689193	FYPO:0001035	increased cell wall thickness during vegetative growth	(Figure 3B)
PMID:29689193	GO:1903338	regulation of cell wall organization or biogenesis	(comment: Promotes cell wall thickness hoemostasis)
PMID:29689193	GO:1903338	regulation of cell wall organization or biogenesis	(comment: Promotes cell wall thickness hoemostasis)
PMID:29689193	GO:1903338	regulation of cell wall organization or biogenesis	(comment: Promotes cell wall thickness hoemostasis)
PMID:29689193	FYPO:0006745	abnormal cell wall thickness during vegetative growth	(comment: thicker and thinner, disrupted homeostasis)
PMID:29689193	FYPO:0006745	abnormal cell wall thickness during vegetative growth	(comment: thicker and thinner, disrupted homeostasis)
PMID:29689193	FYPO:0006745	abnormal cell wall thickness during vegetative growth	(comment: thicker and thinner, disrupted homeostasis)
PMID:29697047	FYPO:0005787	normal spatial extent of double-strand break processing	(Fig. 3A)
PMID:29697047	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3D)
PMID:29697047	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 3D)
PMID:29697047	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 3D)
PMID:29697047	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3D)
PMID:29697047	FYPO:0004251	increased DNA resection during replication fork processing [has_severity] high	Applying the live cell resection assay to fission yeast lacking the orthologous Crb2, we observe a strong increases the median rate of resection to (13.9 kb/hr), with some individual cells demonstrating very fast (~40 kb/hr) resection rates (Figure 1F).
PMID:29697047	FYPO:0006319	normal extent of DNA resection during replication fork processing	As Rev7 also functions with Rev3 as part of the polymerase z complex in translesion synthesis, we also confirmed that Rev3 does not affect resection (Figure 2C)
PMID:29697047	FYPO:0006318	decreased DNA resection during replication fork processing [has_severity] high	As expected, cells lacking Exo1 show a persistent LacO/LacI-GFP focus over many hours even after Rad52-mCherry loads (Figure 1C).
PMID:29697047	FYPO:0000085	sensitive to camptothecin [has_severity] low	Con- sistent with these observations, we find that loss of Rev7 is able to rescue the severe growth defect of exo1D cells on rich media plates containing camptothecin, consistent with a derepression of Rqh1-dependent resection in the absence of a functional Exo1 pathway (Figure 3D).
PMID:29697047	FYPO:0000085	sensitive to camptothecin [has_severity] low	Con- sistent with these observations, we find that loss of Rev7 is able to rescue the severe growth defect of exo1D cells on rich media plates containing camptothecin, consistent with a derepression of Rqh1-dependent resection in the absence of a functional Exo1 pathway (Figure 3D).
PMID:29697047	FYPO:0006319	normal extent of DNA resection during replication fork processing	In stark contrast, the rapid rate of resection in a rev7D single mutant is entirely dependent on the presence of Rqh1 (Figure 3A).
PMID:29697047	FYPO:0006319	normal extent of DNA resection during replication fork processing	In stark contrast, the rapid rate of resection in a rev7D single mutant is entirely dependent on the presence of Rqh1 (Figure 3A).
PMID:29697047	FYPO:0004251	increased DNA resection during replication fork processing [has_severity] medium	In the population, the median long-range resection rate for rev7D cells is similar to cells lacking Crb2 (10.4 kb/hr, Figure 2C).
PMID:29697047	FYPO:0004251	increased DNA resection during replication fork processing [has_severity] high	Interestingly, we find that the rapid long-range resection rate observed in crb2D or rev7D cells is entirely Exo1- independent (Figure 3A–C, Figure 3—figure supplement 1).
PMID:29697047	FYPO:0004251	increased DNA resection during replication fork processing [has_severity] medium	Interestingly, we find that the rapid long-range resection rate observed in crb2D or rev7D cells is entirely Exo1- independent (Figure 3A–C, Figure 3—figure supplement 1).
PMID:29697047	FYPO:0004251	increased DNA resection during replication fork processing [has_severity] medium	When consider- ing only precisely determined resection events, the average long-range resection rate in crb2D cells is not statically less than that of crb2Drqh1D cells when correcting for multiple comparisons (p=0.16) (Figure 3A). However, in many crb2Drqh1D cells, resection durations extend beyond the timeframe of data acquisition, suggesting that rapid crb2D resection also requires Rqh1 (Figure 3—figure sup- plement 2).
PMID:29697047	FYPO:0004251	increased DNA resection during replication fork processing [has_severity] medium	When consider- ing only precisely determined resection events, the average long-range resection rate in crb2D cells is not statically less than that of crb2Drqh1D cells when correcting for multiple comparisons (p=0.16) (Figure 3A). However, in many crb2Drqh1D cells, resection durations extend beyond the timeframe of data acquisition, suggesting that rapid crb2D resection also requires Rqh1 (Figure 3—figure sup- plement 2).
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Fig. 4b)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Fig. 4b)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Fig. 4b)
PMID:29735656	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Fig. 4e)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 1A Supp S1A)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 1A Supp S1A)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 1A)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 1A)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 1A)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 1A)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 1A)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 1A)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 1A)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 1A)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 1A)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 1A)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 1A)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 2 AB) (comment: inactive separase, uncleavable kleisin)
PMID:29735656	FYPO:0002061	inviable vegetative cell population	(Figure 2 AB) (comment: inactive separase, uncleavable kleisin)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 2 AB) (comment: inactive separase, uncleavable kleisin)
PMID:29735656	FYPO:0002061	inviable vegetative cell population	(Figure 2 AB) inactive separase, uncleavable kleisin
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0002060	viable vegetative cell population	(Figure 3, Figure S1B)
PMID:29735656	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Figure 3c)
PMID:29735656	FYPO:0000268	sensitive to UV during vegetative growth	(Figure 4d)
PMID:29735656	FYPO:0000088	sensitive to hydroxyurea	(Supp. Figure S4)
PMID:29735656	FYPO:0000085	sensitive to camptothecin	(Supp. Figure. S4)
PMID:29735745	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 1C)
PMID:29735745	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 1C)
PMID:29735745	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 1C)
PMID:29735745	FYPO:0000159	abnormal chromosome condensation	(Fig. 1D)
PMID:29735745	FYPO:0000214	abnormal mitotic chromosome condensation	(Fig. 1D)
PMID:29735745	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 30	(Fig. 1E)
PMID:29735745	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 20	(Fig. 1E)
PMID:29735745	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 10	(Fig. 1E)
PMID:29735745	FYPO:0001513	normal mitotic sister chromatid segregation	(Fig. 2B)
PMID:29735745	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:29735745	GO:0005634	nucleus [exists_during] mitotic interphase	(Fig. 2C)
PMID:29735745	GO:0005634	nucleus [exists_during] mitotic interphase	(Fig. 2C)
PMID:29735745	FYPO:0002061	inviable vegetative cell population	(Fig. 2D)
PMID:29735745	FYPO:0001357	normal vegetative cell population growth	(Fig. 2D)
PMID:29735745	FYPO:0002061	inviable vegetative cell population	(Fig. 2D)
PMID:29735745	FYPO:0001489	inviable vegetative cell [has_penetrance] complete	(Fig. 2D)
PMID:29735745	FYPO:0001235	decreased extent of cell population growth [has_severity] high	(Fig. 2D)
PMID:29735745	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPAC1B9.03c	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPBC1289.04c	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC6G10.04c	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC6G10.04c	(Fig. 3D)
PMID:29735745	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPBC1652.02	(Fig. 3D)
PMID:29735745	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPAC3G9.12	(Fig. 3D)
PMID:29735745	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPAC644.09	(Fig. 3D)
PMID:29735745	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPAC18B11.08c	(Fig. 3D)
PMID:29735745	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPAC17H9.16	(Fig. 3D)
PMID:29735745	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPAC1834.06c	(Fig. 3D)
PMID:29735745	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPBC776.13	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPBC1289.04c	(Fig. 3D)
PMID:29735745	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPAC13G7.10	(Fig. 3D)
PMID:29735745	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPBC1289.04c	(Fig. 3D)
PMID:29735745	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPAC6G10.04c	(Fig. 3D)
PMID:29735745	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPAC11E3.09	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC13G7.10	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPBC1652.02	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPBC1652.02	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC3G9.12	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC3G9.12	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC644.09	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC644.09	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC18B11.08c	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC18B11.08c	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC17H9.16	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC17H9.16	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC1834.06c	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC1834.06c	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC1B9.03c	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC1B9.03c	(Fig. 3D)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPAC13G7.10	(Fig. 3D)
PMID:29735745	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC146.03c	(Fig. 5A)
PMID:29735745	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPCC306.03c	(Fig. 5A)
PMID:29735745	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPCC188.03	(Fig. 5A)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPBC776.13	(Fig. 5A, 5B, 5C; Fig. 7C)
PMID:29735745	GO:0045944	positive regulation of transcription by RNA polymerase II [has_input] PomBase:SPBC776.13	(Fig. 5A, 5B, 5C; Fig. 7C)
PMID:29735745	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC776.13	(Fig. 5A, 5C)
PMID:29735745	FYPO:0001317	normal RNA level during vegetative growth [assayed_using] PomBase:SPBC776.13	(Fig. 5B)
PMID:29735745	FYPO:0001317	normal RNA level during vegetative growth [assayed_using] PomBase:SPCC306.03c	(Fig. 5B)
PMID:29735745	FYPO:0001317	normal RNA level during vegetative growth [assayed_using] PomBase:SPBC776.13	(Fig. 5B)
PMID:29735745	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC776.13	(Fig. 5C)
PMID:29735745	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC776.13	(Fig. 5C)
PMID:29735745	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 5G)
PMID:29735745	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 5G)
PMID:29735745	FYPO:0000214	abnormal mitotic chromosome condensation	(Fig. 5H)
PMID:29735745	FYPO:0002061	inviable vegetative cell population	(Fig. 6B)
PMID:29735745	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001234	slow vegetative cell population growth	(Fig. 6B, 6C)
PMID:29735745	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 6B, 6C)
PMID:29735745	FYPO:0004099	normal mitotic chromosome condensation	(Fig. 6D)
PMID:29735745	FYPO:0001234	slow vegetative cell population growth	(Fig. 7B)
PMID:29735745	FYPO:0002151	inviable spore	(Fig. 7B)
PMID:29735745	FYPO:0001357	normal vegetative cell population growth	(Fig. 7B)
PMID:29735745	FYPO:0000046	decreased cell population growth [has_severity] low	(Fig. 7B)
PMID:29735745	FYPO:0001357	normal vegetative cell population growth	(Fig. 7B)
PMID:29735745	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC776.13	(Fig. 7C)
PMID:29735745	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC776.13	(Fig. 7C)
PMID:29735745	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC776.13	(Fig. 7C)
PMID:29735745	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC776.13	(Fig. 7D)
PMID:29735745	FYPO:0004099	normal mitotic chromosome condensation	(Fig. 7D)
PMID:29735745	FYPO:0004099	normal mitotic chromosome condensation	(Fig. S2D)
PMID:29735745	FYPO:0004099	normal mitotic chromosome condensation	(Fig. S2D)
PMID:29735745	FYPO:0004099	normal mitotic chromosome condensation	(Fig. S2D)
PMID:29735745	FYPO:0004099	normal mitotic chromosome condensation	(Fig. S2D)
PMID:29735745	FYPO:0004099	normal mitotic chromosome condensation	(Fig. S2D)
PMID:29735745	FYPO:0004099	normal mitotic chromosome condensation	(Fig. S2D)
PMID:29735745	FYPO:0004099	normal mitotic chromosome condensation	(Fig. S2D)
PMID:29735745	FYPO:0004099	normal mitotic chromosome condensation	(Fig. S2D)
PMID:29735745	FYPO:0004099	normal mitotic chromosome condensation	(Fig. S2D)
PMID:29735745	GO:0000977	RNA polymerase II transcription regulatory region sequence-specific DNA binding	(comment: binds to the consensus sequence CCCCAY) (Fig. 4)
PMID:29735745	GO:0000977	RNA polymerase II transcription regulatory region sequence-specific DNA binding	(comment: binds to the consensus sequence CCCCAY) (Fig. 4)
PMID:29735745	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific [occurs_at] Zas1_recognition_motif	(comment: binds to the consensus sequence CCCCAY) (Fig. 4)
PMID:29735745	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific [occurs_at] Zas1_recognition_motif	(comment: binds to the consensus sequence CCCCAY) (Fig. 4)
PMID:29735745	GO:0005634	nucleus [exists_during] mitotic M phase	Video S2
PMID:29735745	GO:0005634	nucleus [exists_during] mitotic M phase	Video S2
PMID:29742018	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC3H7.15	(comment: CHECK in vitro)
PMID:29742018	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC3H7.15	(comment: CHECK in vitro)
PMID:29742018	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC3H7.15	(comment: CHECK in vitro)
PMID:29742018	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPAC23C4.12	(comment: CHECK in vitro)
PMID:29742018	FYPO:0002700	increased protein kinase activity [assayed_enzyme] PomBase:SPBC3H7.15	(comment: CHECK in vitro)
PMID:29742018	FYPO:0002700	increased protein kinase activity [assayed_enzyme] PomBase:SPAC23C4.12	(comment: CHECK in vitro)
PMID:29742018	FYPO:0001384	abolished protein kinase activity [assayed_enzyme] PomBase:SPBC3H7.15	(comment: CHECK in vitro)
PMID:29742018	FYPO:0001384	abolished protein kinase activity [assayed_enzyme] PomBase:SPAC23C4.12	(comment: CHECK in vitro)
PMID:29742018	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC23C4.12	(comment: normal with and without spindle checkpoint activation)
PMID:29742018	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC3H7.15	(comment: normal with and without spindle checkpoint activation)
PMID:29742018	FYPO:0002969	increased protein localization to mitotic spindle pole body [assayed_using] PomBase:SPBC3H7.15	Hhp1 accumulates at SPB when spindle checkpoint activated
PMID:29769606	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPCC622.08c [has_severity] low	An acetyl-mimetic H2A-K119Q mutation slightly inhibited Bub1-mediated H2A phosphorylation (Fig. 4B)
PMID:29769606	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPCC622.08c [has_severity] low	An acetyl-mimetic H2A-K119Q mutation slightly inhibited Bub1-mediated H2A phosphorylation (Fig. 4B)
PMID:29769606	FYPO:0003182	sister chromatid nondisjunction at meiosis II	Consistently, sister chromatid non-disjunction at meiosis II was signifcantly increased in the K119D and K119E mutants
PMID:29769606	FYPO:0003182	sister chromatid nondisjunction at meiosis II	Consistently, sister chromatid non-disjunction at meiosis II was signifcantly increased in the K119D and K119E mutants
PMID:29769606	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II	Consistently, sister chromatid non-disjunction at meiosis II was signifcantly increased in the K119D and K119E mutants
PMID:29769606	FYPO:0003182	sister chromatid nondisjunction at meiosis II	Consistently, sister chromatid non-disjunction at meiosis II was signifcantly increased in the K119D and K119E mutants
PMID:29769606	FYPO:0003182	sister chromatid nondisjunction at meiosis II	Consistently, sister chromatid non-disjunction at meiosis II was signifcantly increased in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. S3D).
PMID:29769606	FYPO:0003182	sister chromatid nondisjunction at meiosis II	Consistently, sister chromatid non-disjunction at meiosis II was signifcantly increased in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. S3D).
PMID:29769606	FYPO:0000450	decreased protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAC15A10.15	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_protein] PomBase:SPBP35G2.03c	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0000450	decreased protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAC15A10.15	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0000450	decreased protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAC15A10.15	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_protein] PomBase:SPBP35G2.03c	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_protein] PomBase:SPBP35G2.03c	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_protein] PomBase:SPBP35G2.03c	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_protein] PomBase:SPBP35G2.03c	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [assayed_protein] PomBase:SPBP35G2.03c	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0000450	decreased protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAC15A10.15	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0000450	decreased protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAC15A10.15	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0000450	decreased protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAC15A10.15	Intriguingly, we found that both Sgo2 centromeric localization during mitosis and Sgo1 centromeric localization during meiosis I were dramatically delocalized in the K119D and K119E mutants as well as the H2A-S121A mutant (Fig. 3C-E).
PMID:29769606	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPCC622.08c [has_severity] high	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPCC622.08c [has_severity] high	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPCC622.08c [has_severity] high	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPCC622.08c [has_severity] high	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPCC622.08c [has_severity] high	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC622.08c	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPCC622.08c [has_severity] high	Te recombinant proteins of fssion yeast H2A (SpHta1) were also purifed. An in vitro kinase assay using these recombinant proteins showed that the H2A-K119D and the H2A-K119E mutants, as well as the H2A-S121A mutant, were not signifcantly phosphorylated by Bub1, whereas H2A-K119R mutant proteins were phosphorylated by Bub1 (Fig. 4B).
PMID:29769606	FYPO:0000091	sensitive to thiabendazole	We found that malonyl-mimetic K119D and K119E mutants showed sensitivity to a microtubule depolymerizing agent (TBZ) in the same way the H2A-S121A mutant had (Fig. S3B)
PMID:29769606	FYPO:0000091	sensitive to thiabendazole	We found that malonyl-mimetic K119D and K119E mutants showed sensitivity to a microtubule depolymerizing agent (TBZ) in the same way the H2A-S121A mutant had (Fig. S3B)
PMID:29769606	FYPO:0000091	sensitive to thiabendazole	We found that malonyl-mimetic K119D and K119E mutants showed sensitivity to a microtubule depolymerizing agent (TBZ) in the same way the H2A-S121A mutant had (Fig. S3B)
PMID:29769606	FYPO:0000091	sensitive to thiabendazole	We found that malonyl-mimetic K119D and K119E mutants showed sensitivity to a microtubule depolymerizing agent (TBZ) in the same way the H2A-S121A mutant had (Fig. S3B)
PMID:29774234	FYPO:0000266	sensitive to DNA damaging agents	(comment: CHECK Sensitive to HU, CPT and MMS)
PMID:29774234	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(comment: CHECK same as stn1-226 alone)
PMID:29774234	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(comment: CHECK slightly better growth than stn1-226 alone)
PMID:29774234	FYPO:0005402	increased telomeric 3' overhang length during vegetative growth [has_severity] medium	(comment: Exacerbated at high temperature)
PMID:29774234	FYPO:0000122	abnormal telomere maintenance during vegetative growth	(comment: loss of telomeric and subtelomeric sequences at high temperature)
PMID:29804820	GO:0098654	CENP-A recruiting complex	((comment: The Stoichiometry of the S. pombe Mis18 Holo-ComplexIs (Mis16)2:(Eic1)2:(Mis18)4T)
PMID:29804820	FYPO:0001355	decreased vegetative cell population growth	(Figure 4D)
PMID:29804820	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC1672.10 [assayed_protein] PomBase:SPBC27B12.02	(Figures 6A, 6B).
PMID:29804820	GO:0005515	protein binding	(comment: A Homodimer of the Mis18 C-Terminal Domain Interacts with a Mis16-Eic1 Heterodimer)
PMID:29804820	GO:0098654	CENP-A recruiting complex	(comment: The Stoichiometry of the S. pombe Mis18 Holo-ComplexIs (Mis16)2:(Eic1)2:(Mis18)4T)
PMID:29804820	GO:0098654	CENP-A recruiting complex	(comment: The Stoichiometry of the S. pombe Mis18 Holo-ComplexIs (Mis16)2:(Eic1)2:(Mis18)4T)
PMID:29804820	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC1672.10 [assayed_protein] PomBase:SPAC1834.03c	However, the interaction is significantly diminished when either L32 (Mis16D1-32), or both L32 (Mis16D1-32) and L32/W33 (Mis16D1-33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1-33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29804820	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC1672.10 [assayed_protein] PomBase:SPBC27B12.02	However, the interaction is significantly diminished when either L32 (Mis16D1-32), or both L32 (Mis16D1-32) and L32/W33 (Mis16D1-33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1-33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29804820	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC1672.10 [assayed_protein] PomBase:SPBC8D2.03c	However, the interaction is significantly diminished when either L32 (Mis16D1-32), or both L32 (Mis16D1-32) and L32/W33 (Mis16D1-33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1-33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29804820	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC1672.10 [assayed_protein] PomBase:SPBC27B12.02	However, the interaction is significantly diminished when either L32 (Mis16D1-32), or both L32 (Mis16D1-32) and L32/W33 (Mis16D1-33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1-33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29804820	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC1672.10 [assayed_protein] PomBase:SPBC1105.12	However, the interaction is significantly diminished when either L32 (Mis16D1-32), or both L32 (Mis16D1-32) and L32/W33 (Mis16D1-33), are deleted (Figures 6A and 6B). In contrast, the Mis16-H4a1 interaction was only mildly affected in the context of the Mis16D1-33 truncation. These findings strongly suggest that Mis16 L32 and W33 participate in specific interactions with Eic1 but not histone H4. To verify these observations in vivo, we performed
PMID:29813053	FYPO:0006832	premature primary cell septum biogenesis	(Fig. 2) The start of septation scales with anaphase B progression and cell size in fission yeast and correlates linearly with the cell length.
PMID:29813053	FYPO:0006831	delayed onset of primary cell septum biogenesis	(Fig. 2) The start of septation scales with anaphase B progression and cell size in fission yeast and correlates linearly with the cell length.
PMID:29813053	FYPO:0006831	delayed onset of primary cell septum biogenesis	(Fig. 2) The start of septation scales with anaphase B progression and cell size in fission yeast. and correlates linearly with the cell length.
PMID:29813053	FYPO:0006832	premature primary cell septum biogenesis	(Fig. 2) The start of septation scales with anaphase B progression and correlates linearly with the cell length.
PMID:29813053	FYPO:0003201	decreased rate of primary cell septum biogenesis	(Fig. 3)
PMID:29813053	FYPO:0006834	increased rate of primary cell septum biogenesis	(Fig. 3)
PMID:29813053	GO:1905757	negative regulation of primary cell septum biogenesis	(Fig. 4D, E)
PMID:29813053	FYPO:0006832	premature primary cell septum biogenesis	(Fig. 4E and F) Inactivation of Cdc2 kinase in early mitosis induces a very premature septation onset. ATP-analogue sensitive cdc2-asM17 mutant cells carrying Cdc13-GFP were G2-arrested by growth in the presence of 1 μM1-NP-PP1 for 3.5 h at 32C. Then, the cells were G2-released by transfer to a fresh medium and imaged to detect the entry into mitosis. Cdc2 was inactivated during early mitosis transferring the cells to a fresh medium containing either DMSO or 10 μM1-NP-PP1.
PMID:29813053	GO:1905758	positive regulation of primary cell septum biogenesis	(Fig. 5,6A-D) (comment: also inferred from localization timing)
PMID:29813053	GO:1905758	positive regulation of primary cell septum biogenesis	(Fig. 56E) (comment: also inferred from localization timing)
PMID:29813053	FYPO:0006831	delayed onset of primary cell septum biogenesis	(Fig. 5B) Septation start is delayed when the function of Sid2 is compromised. Cells were grown in YES at 25C shifted to 28C for 4 h and imaged as in Fig 1. The data are developed in Table 1 and Table 3.
PMID:29813053	GO:1905758	positive regulation of primary cell septum biogenesis	(Fig. 5B, Table 1) (comment: also inferred from localization timing)
PMID:29813053	FYPO:0006833	normal onset of primary cell septum biogenesis	(Fig. 5E) Timely activation of septum synthesis does not depend on SIN asymmetry. Defective SIN-Inhibitory Phosphatase (SIP) complex csc2Δ cells were examined. The data of cells of C, D and E are developed in S2 Table.
PMID:29813053	FYPO:0006832	premature primary cell septum biogenesis	(Fig. 6) The levels of Etd1 and Rho1 regulate the timing of septation start. (A) The timing of septum deposition onset correlates with the start of increase of Etd1 in the cell middle. Cells were grown inMMwithout thiamine (GFP-etd1+ induced) at 25ÊC for 24 h and imaged as in Fig 1. (B) The increase of Etd1 in the cell middle and concomitant initiation of septation are delayed in long cells. Cells were analyzed as in A after 3.5 h of cell cycle arrest at 36ÊC. Graphs to the right show the total fluorescence of GFP-Etd1 at the cell poles and middle in the series to the left. A.U., arbitrary units. Arrow, cortical localization of Etd1 in the cell middle. Dashed outlines indicate the ROIs used to measure the total fluorescence of GFP-Etd1 in the corresponding regions of the cell. (C) The timing of septation onset is dependent on the level of etd1+. Cells expressing endogenous etd1+ and 41X-GFP-etd1+ grown at 32ÊC for 24 h either in the absence (ON, high etd1+ level; n = 4, 34 cells) or in the presence of thiamine (OFF, wild-type etd1+ level; n = 2, 11 cells), and cells expressing etd1Δ 81X-etd1+ grown for 15 h with thiamine (OFF, very low etd1+ level; n = 3, 23 cells), just before the emergence of SIN phenotype were analyzed as in A.
PMID:29813053	FYPO:0006831	delayed onset of primary cell septum biogenesis	(Fig. 6) The levels of Etd1 and Rho1 regulate the timing of septation start. (A) The timing of septum deposition onset correlates with the start of increase of Etd1 in the cell middle. Cells were grown inMMwithout thiamine (GFP-etd1+ induced) at 25ÊC for 24 h and imaged as in Fig 1. (B) The increase of Etd1 in the cell middle and concomitant initiation of septation are delayed in long cells. Cells were analyzed as in A after 3.5 h of cell cycle arrest at 36ÊC. Graphs to the right show the total fluorescence of GFP-Etd1 at the cell poles and middle in the series to the left. A.U., arbitrary units. Arrow, cortical localization of Etd1 in the cell middle. Dashed outlines indicate the ROIs used to measure the total fluorescence of GFP-Etd1 in the corresponding regions of the cell. (C) The timing of septation onset is dependent on the level of etd1+. Cells expressing endogenous etd1+ and 41X-GFP-etd1+ grown at 32ÊC for 24 h either in the absence (ON, high etd1+ level; n = 4, 34 cells) or in the presence of thiamine (OFF, wild-type etd1+ level; n = 2, 11 cells), and cells expressing etd1Δ 81X-etd1+ grown for 15 h with thiamine (OFF, very low etd1+ level; n = 3, 23 cells), just before the emergence of SIN phenotype were analyzed as in A.
PMID:29813053	FYPO:0006832	premature primary cell septum biogenesis	(Fig. 6) The levels of Etd1 and Rho1 regulate the timing of septation start. (F) The start of septum deposition is dependent on the level of rho1+. Cells expressing endogenous rho1+ and 3Xrho1+ grown at 32ÊC for 16 h either without (ON, high rho1+ level; n = 2, 14 cells) or with thiamine (OFF, wild-type rho1+ level; n = 2, 16 cells) were analyzed.
PMID:29813053	FYPO:0000639	delayed onset of septum assembly	(Fig. 7) The spindle and the proximity of the nucleus to the division site are required for proper septum synthesis activation in fission yeast. (A) Scheme of the steps required to prevent nuclear separation and to maintain or separate the undivided nucleus from the cell middle and/or from the division site. (A-1 and C) Nucleus and division site are maintained in the cell middle; cells were treated for 90 min and imaged with methyl 2-benzimidazolecarbamate (or carbendazim, MBC, 50 μg ml-1) to avoid spindle assembly and nuclear separation. (A-2 and D) Nucleus and division site are relocated to a cell end; cells were treated for 45 min, centrifuged to displace the nucleus, treated 45 more min and visualized with MBC. (A-3 and E) The nucleus is relocated and separated from the division plane; cells were treated for 90 min, centrifuged and examined with MBC. (B) mad2Δ cells were grown and imaged without MBC as in Fig 1. The mad2Δ cells were used to avoid a delay caused by the activation of the spindle assembly checkpoint. (C-E) The premature and uncoupled septation start caused by the absence of the spindle depends on the position of the nucleus. mad2Δ cells were processed as in A to prevent nuclear separation and to maintain or separate the undivided nucleus from the cell middle and/or the division site. (C) The nucleus and division site are maintained in the cell middle. (F) The nucleus and division site are relocated to a cell end. (E) The nucleus is relocated and separated from the division plane. MBC-treated cells were imaged as in B. Anaphase A onset was considered as time zero. Graphs to the right are as in Fig 4. Dashed lines and arrowheads: green, anaphase A onset; dark blue, septum synthesis start; light blue septum ingression onset. White arrowhead: first CW-stained septum synthesis detection. White arrow: first CW-staining increase showing septum ingression. A.U., arbitrary units. (F) Uncoupled septum synthesis and ingression timing with MBC is restored to wild-type levels when the undivided nucleus is separated from the division site. Table showing the time between anaphase A (green) and septum synthesis start (dark blue) or septum ingression onset (light blue) in the indicated cells. Parenthesis: n, number of experiments and cells; T, delay in septum synthesis and ingression start with respect to control cells with MBC as in C.
PMID:29813053	FYPO:0006832	premature primary cell septum biogenesis	(Fig. 7) The spindle and the proximity of the nucleus to the division site are required for proper septum synthesis activation in fission yeast. (A) Scheme of the steps required to prevent nuclear separation and to maintain or separate the undivided nucleus from the cell middle and/or from the division site. (A-1 and C) Nucleus and division site are maintained in the cell middle; cells were treated for 90 min and imaged with methyl 2-benzimidazolecarbamate (or carbendazim, MBC, 50 μg ml-1) to avoid spindle assembly and nuclear separation. (A-2 and D) Nucleus and division site are relocated to a cell end; cells were treated for 45 min, centrifuged to displace the nucleus, treated 45 more min and visualized with MBC. (A-3 and E) The nucleus is relocated and separated from the division plane; cells were treated for 90 min, centrifuged and examined with MBC. (B) mad2Δ cells were grown and imaged without MBC as in Fig 1. The mad2Δ cells were used to avoid a delay caused by the activation of the spindle assembly checkpoint. (C-E) The premature and uncoupled septation start caused by the absence of the spindle depends on the position of the nucleus. mad2Δ cells were processed as in A to prevent nuclear separation and to maintain or separate the undivided nucleus from the cell middle and/or the division site. (C) The nucleus and division site are maintained in the cell middle. (F) The nucleus and division site are relocated to a cell end. (E) The nucleus is relocated and separated from the division plane. MBC-treated cells were imaged as in B. Anaphase A onset was considered as time zero. Graphs to the right are as in Fig 4. Dashed lines and arrowheads: green, anaphase A onset; dark blue, septum synthesis start; light blue, septum ingression onset. White arrowhead: first CW-stained septum synthesis detection. White arrow: first CW-staining increase showing septum ingression. A.U., arbitrary units. (F) Uncoupled septum synthesis and ingression timing with MBC is restored to wild-type levels when the undivided nucleus is separated from the division site. Table showing the time between anaphase A (green) and septum synthesis start (dark blue) or septum ingression onset (light blue) in the indicated cells. Parenthesis: n, number of experiments and cells; T, delay in septum synthesis and ingression start with respect to control cells with MBC as in C.
PMID:29813053	FYPO:0006831	delayed onset of primary cell septum biogenesis	(Fig. S3D) The timing of septation onset depends on the AR function. The start of septation is delayed when the function of the AR unconventional type II myosin Myp2 is compromised.
PMID:29813053	FYPO:0006831	delayed onset of primary cell septum biogenesis	(Fig. S3E) The timing of septation onset depends on the AR function. The start of septation is delayed when the function of the AR F-BAR protein Cdc15 is compromised.
PMID:29813053	FYPO:0006831	delayed onset of primary cell septum biogenesis	S5 Fig. The establishment of SIN asymmetry and the timely activation of septum synthesis do not depend on each other. (A, B) Early log-phase wild-type and thermosensitive cps1-191 (Bgs1) mutant cells were grown in YES at 25ÊC, shifted to 28ÊC for 1 h (A) or 32ÊC for 30 min (B) to produce a gradual delay in the onset of septum synthesis of cps1-191 mutant, and imaged as in Fig 5C. Anaphase B onset is considered as time zero (T = 0). White arrow: first CWstained detection of septum synthesis. Arrowheads: green, anaphase B onset; blue, septum deposition start (time immediately before septum detection with CW); red, complete asymmetry of SIN Cdc7, being Cdc7-GFP completely lost from one SPB. The data of this figure are developed in S2 Table. (C) The timing of septation onset is not related to the asymmetry of SIN. Early log-phase wild-type cells were grown in YES at 25ÊC, 28ÊC or 32ÊC, imaged as in Fig 5C and the timings of SIN asymmetry and of septation onset were determined with respect to the anaphase B onset (see also the data in S2 Table).
PMID:29844133	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] low	(comment: Beware using aged colonies, cell size recovery observed.)
PMID:29844133	FYPO:0001407	decreased cell population growth on glucose carbon source	(comment: beware using old strains, phenotypic changes observed.)
PMID:29851556	GO:0035861	site of double-strand break	(comment: CHECK in the presence or absence of Nbs1)
PMID:29851556	FYPO:0002475	increased protein localization to double-strand break site [assayed_using] PomBase:SPAC1556.01c	(comment: localization of mutated protein assayed)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] medium	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] medium	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] low	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003659	abnormal mating type switching resulting in duplication or deletion in mating-type region	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] medium	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 3)
PMID:29852001	GO:0007535	donor selection	In summary, our observations suggest that the factors, Clr4, Sir2, Swd1 and Clr3 probably work in the same pathway as Swi6, but Brl2, Pof3, Cbp1 and Swi2 have an effect on donor selection through Swi6-dependent and -independent mechanisms.
PMID:29852001	GO:0007535	donor selection	In summary, our observations suggest that the factors, Clr4, Sir2, Swd1 and Clr3 probably work in the same pathway as Swi6, but Brl2, Pof3, Cbp1 and Swi2 have an effect on donor selection through Swi6-dependent and -independent mechanisms.
PMID:29852001	GO:0007535	donor selection	In summary, our observations suggest that the factors, Clr4, Sir2, Swd1 and Clr3 probably work in the same pathway as Swi6, but Brl2, Pof3, Cbp1 and Swi2 have an effect on donor selection through Swi6-dependent and -independent mechanisms.
PMID:29852001	GO:0007535	donor selection	In summary, our observations suggest that the factors, Clr4, Sir2, Swd1 and Clr3 probably work in the same pathway as Swi6, but Brl2, Pof3, Cbp1 and Swi2 have an effect on donor selection through Swi6-dependent and -independent mechanisms.
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S2
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29852001	FYPO:0000470	decreased mating type switching	Table S3
PMID:29866182	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC736.11	(comment: FLAG-Ago1)
PMID:29866182	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC736.11	(comment: FLAG-Ago1)
PMID:29866182	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC736.11 [assayed_using] PomBase:SPAC140.03	(comment: FLAG-Ago1, Arb1-Myc)
PMID:29866182	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC736.11 [assayed_using] PomBase:SPAC140.03	(comment: FLAG-Ago1, Arb1-Myc)
PMID:29866182	FYPO:0003681	decreased protein level at centromere outer repeat heterochromatin [assayed_using] PomBase:SPCC736.11	(comment: Myc-Ago1)
PMID:29866182	FYPO:0003681	decreased protein level at centromere outer repeat heterochromatin [assayed_using] PomBase:SPCC736.11	(comment: Myc-Ago1)
PMID:29866182	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC83.03c	(comment: Tas3-Myc)
PMID:29898918	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(comment: CHECK Epistatic genetic interaction, same as eme1delta alone)
PMID:29898918	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: CHECK Epistatic genetic interaction, same as eme1delta alone)
PMID:29898918	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(comment: CHECK Epistatic genetic interaction, same as mus81delta alone)
PMID:29898918	FYPO:0000085	sensitive to camptothecin	(comment: CHECK Epistatic genetic interaction, same as mus81delta alone)
PMID:29898918	FYPO:0000085	sensitive to camptothecin	(comment: CHECK Epistatic genetic interaction, same as mus81delta alone)
PMID:29898918	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: CHECK Epistatic genetic interaction,same as mus81delta alone)
PMID:29898918	MOD:00085	N6-methyl-L-lysine	(comment: CHECK Required for cellular resistance to MMS and CPT)
PMID:29898918	MOD:00085	N6-methyl-L-lysine [present_during] mitotic cell cycle	(comment: CHECK present in cycling cells and meiosis I cells. Required for cellular resistance to MMS and CPT.)
PMID:29898918	MOD:00085	N6-methyl-L-lysine [present_during] meiosis I	(comment: CHECK present in cycling cells and meiosis I cells. Required for cellular resistance to MMS and CPT.)
PMID:29898918	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(comment: CHECK slightly worse than srs2delta alone)
PMID:29898918	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(comment: CHECK slightly worse than srs2delta alone)
PMID:29899453	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPAC23C4.19	(Extended Data Fig 2f)
PMID:29899453	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPAC23C4.19	(Extended Data Fig 2f)
PMID:29899453	FYPO:0002577	decreased chromatin binding [assayed_using] PomBase:SPAC23C4.19 [has_severity] medium	(Extended Data Fig 3a, Fig. 2c, Extended Data Fig. 3b-d)
PMID:29899453	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC32H8.10	(Fig. 1B) (comment: vw: corrected back to dis2 not cdk9!)
PMID:29899453	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPBC776.02c	(Fig. 1b)
PMID:29899453	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPBC776.02c	(Fig. 1b)
PMID:29899453	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPBC776.02c [part_of] positive regulation of transcription elongation by RNA polymerase II	(Fig. 1b)
PMID:29899453	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPBC776.02c	(Fig. 1c)
PMID:29899453	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPBC776.02c	(Fig. 1c)
PMID:29899453	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPBC776.02c	(Fig. 1c, Extended Data Fig 2a)
PMID:29899453	FYPO:0001759	normal protein phosphatase activity [assayed_enzyme] PomBase:SPBC776.02c	(Fig. 1d)
PMID:29899453	FYPO:0001757	decreased protein phosphatase activity [assayed_enzyme] PomBase:SPBC776.02c	(Fig. 1d)
PMID:29899453	FYPO:0001757	decreased protein phosphatase activity [assayed_enzyme] PomBase:SPBC776.02c	(Fig. 1d)
PMID:29899453	FYPO:0001757	decreased protein phosphatase activity [assayed_enzyme] PomBase:SPBC776.02c [assayed_substrate] PomBase:SPAC23C4.19	(Fig. 1d, Extended Data Fig. 1d)
PMID:29899453	FYPO:0001757	decreased protein phosphatase activity [assayed_enzyme] PomBase:SPBC776.02c [assayed_substrate] PomBase:SPAC23C4.19	(Fig. 1d, Extended Data Fig. 1d)
PMID:29899453	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPAC23C4.19	(Fig. 2d)
PMID:29899453	FYPO:0003086	normal chromatin binding [assayed_using] PomBase:SPBC776.02c	(Fig. 2e, Extended Data Fig. 4b)
PMID:29899453	FYPO:0003086	normal chromatin binding [assayed_using] PomBase:SPBC776.02c	(Fig. 2e, Extended Data Fig. 4c)
PMID:29899453	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 3e)
PMID:29899453	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 3e)
PMID:29899453	FYPO:0003086	normal chromatin binding [assayed_using] PomBase:SPAC12G12.14c	(Fig. 5c)
PMID:29899453	FYPO:0002980	increased chromatin binding [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPAC23C4.19	(Fig. 6a, b)
PMID:29899453	FYPO:0002980	increased chromatin binding [assayed_using] PomBase:SPBC776.02c [assayed_using] PomBase:SPAC23C4.19	(Fig. 6a, b)
PMID:29899453	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPAC23C4.19	(Fig. S2, Extended Data Fig. 2c)
PMID:29899453	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPBC28F2.12	(Fig. S2, Extended Data Fig. 2d)
PMID:29899453	FYPO:0005260	increased cell population growth at low temperature	(Figure 3d, Extended fig 8d) (comment: (vw: some suppression?))
PMID:29899453	FYPO:0002061	inviable vegetative cell population	(Figure 3e)
PMID:29899453	FYPO:0006614	increased termination of RNA polymerase II transcription	(Figure 3e) Also increased termination index Fig. 4e
PMID:29899453	FYPO:0002680	increased protein phosphorylation [assayed_using] PomBase:SPAC23C4.19	(comment: check this addition) Fig. 2a, Extended Data Fig. 2a
PMID:29899453	FYPO:0002680	increased protein phosphorylation [assayed_using] PomBase:SPBC28F2.12	(comment: vw: I changed the allele to the multi gene genotype to reflect the comment.) Extended Data Fig 2c Fcp1 inactivation stabilizes Rpb1 Ser2 phosphorylation after Lsk1 inhibition. Fission-yeast strains, lsk1as or lsk1as fcp1-452, were grown at 30 °C and shifted to 37 °C (or not shifted), treated for the indicated time with 20 μM 3-MB-PP1, and analysed by immunoblotting for Pol II Ser2 phosphorylation
PMID:29899453	FYPO:0006020	abnormal protein distribution along RNA polymerase II-transcribed genes [assayed_using] PomBase:SPBC28F2.12 [occurs_at] transcription_termination_signal	Extended Data Fig 10
PMID:29899453	FYPO:0006020	abnormal protein distribution along RNA polymerase II-transcribed genes [assayed_using] PomBase:SPBC28F2.12 [occurs_at] transcription_termination_signal	Extended Data Fig 10
PMID:29899453	FYPO:0006020	abnormal protein distribution along RNA polymerase II-transcribed genes [assayed_using] PomBase:SPBC28F2.12 [occurs_at] transcription_termination_signal	Extended Data Fig 10
PMID:29899453	FYPO:0004423	normal protein threonine phosphorylation [assayed_using] PomBase:SPAC23C4.19	Extended Data Fig 2f .(comment: CHECK (cdk9as, cdk9as ssu72C13S, ssu72C13S))
PMID:29899453	FYPO:0006613	decreased termination of RNA polymerase II transcription	Extended Data Fig 3a, Fig. 2c, Extended Data Fig. 3b-d)
PMID:29899453	FYPO:0002980	increased chromatin binding [assayed_using] PomBase:SPBC776.02c	Extended Data Fig 4a Cdk9 inhibition increased chromatin recruitment of Dis2
PMID:29899453	FYPO:0002980	increased chromatin binding [assayed_using] PomBase:SPBC776.02c	Extended Data Fig 4d (comment: (vw: fixed allele))
PMID:29899453	FYPO:0002980	increased chromatin binding [assayed_using] PomBase:SPBC776.02c	Extended Data Fig 4d (comment: Added Dis2 extension)
PMID:29899453	FYPO:0003086	normal chromatin binding [assayed_using] PomBase:SPAC12G12.14c	Extended Data Fig 5a (comment: vw: based on EXP and comment changed allele from psf2 to cdk9 (P.P. Core CPF recruitment to chromatin is unaffected by Cdk9 inhibition). pfs2 pla1 cft1)
PMID:29899453	FYPO:0003086	normal chromatin binding [assayed_using] PomBase:SPBC1709.08	Extended Data Fig 5a (comment: vw: fixed allele and target)
PMID:29899453	FYPO:0003086	normal chromatin binding [assayed_using] PomBase:SPBC646.04	Extended Data Fig 5a (comment: vw: fixed allele and target)
PMID:29899453	FYPO:0002577	decreased chromatin binding [assayed_using] PomBase:SPAC23C4.19	Extended Data Fig 5d .
PMID:29899453	FYPO:0002577	decreased chromatin binding [assayed_using] PomBase:SPAC23C4.19	Extended Data Fig 6a,b ChIP-qPCR analysis at the rps17a+ gene. Comparison of pSpt5:Spt5 ratio in the indicated strains upstream and downstream of the CPS at 30 °C (left) and comparison of the ratio between dis2+ and dis2-11 cells at 18 °C (right). Extended Data Fig 6a,b
PMID:29899453	FYPO:0003086	normal chromatin binding [assayed_using] PomBase:SPCC31H12.05c	Extended Data Fig 6e Cdk9 does not restrict chromatin recruitment of Sds21.
PMID:29899453	GO:1904595	positive regulation of termination of RNA polymerase II transcription	Extended data Figure 9
PMID:29899453	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPBC28F2.12 [occurs_at] transcription_termination_signal	extended data Figure 9 decreased RNA pol2 localization to chromatin (occurs at termination sites)
PMID:29914874	FYPO:0000005	abnormal cell morphology	Supplementary Fig. S3
PMID:29914874	FYPO:0001234	slow vegetative cell population growth	Supplementary Fig. S3
PMID:29914874	FYPO:0001234	slow vegetative cell population growth	Supplementary Fig. S3
PMID:29914874	FYPO:0000017	elongated cell	Supplementary Fig. S3
PMID:29914874	FYPO:0001234	slow vegetative cell population growth	Supplementary Fig. S3
PMID:29914874	FYPO:0001234	slow vegetative cell population growth	Supplementary Fig. S3
PMID:29914874	FYPO:0004750	elongated septated vegetative cell	Supplementary Figure S3
PMID:29914874	FYPO:0001234	slow vegetative cell population growth	Supplementary Table S3
PMID:29930085	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	(Figure 1)
PMID:29930085	GO:0110085	mitotic actomyosin contractile ring	(Figure 1)
PMID:29930085	GO:0005938	cell cortex	(Figure 1)
PMID:29930085	GO:0051285	cell cortex of cell tip [exists_during] mitotic interphase	(Figure 1)
PMID:29930085	GO:0110085	mitotic actomyosin contractile ring	(Figure 1)
PMID:29930085	GO:1902716	cell cortex of growing cell tip [exists_during] mitotic interphase	(Figure 1)
PMID:29930085	GO:0110085	mitotic actomyosin contractile ring	(Figure 1)
PMID:29930085	GO:1902716	cell cortex of growing cell tip	(Figure 1)
PMID:29930085	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPBC32H8.12c	(Figure 1) (comment: CHECK interphase arrest requested during interphase)
PMID:29930085	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPCC1223.06	(Figure 1) (comment: CHECK interphase arrest requested during interphase)
PMID:29930085	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPCC970.09	(Figure 1) (comment: CHECK interphase arrest requested during interphase)
PMID:29930085	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPCC1840.02c	(Figure 1) (comment: CHECK interphase arrest requested during interphase)
PMID:29930085	FYPO:0005465	normal cell polarity	(Figure 1) (comment: CHECK interphase arrest)
PMID:29930085	FYPO:0003329	abolished protein localization to cell tip during mitotic interphase [assayed_using] PomBase:SPBC1604.14c	(Figure 1) (comment: CHECK interphase arrest)
PMID:29930085	FYPO:0003329	abolished protein localization to cell tip during mitotic interphase [assayed_using] PomBase:SPAC110.03 [assayed_using] cdc42/GTP+	(Figure 1) (comment: CHECK interphase arrest)
PMID:29930085	FYPO:0004103	viable spherical vegetative cell [has_penetrance] high	(Figure 2)
PMID:29930085	FYPO:0005465	normal cell polarity	(Figure 2) (comment: CHECK interphase arrest)
PMID:29930085	FYPO:0005465	normal cell polarity	(Figure 2, Movei 1)
PMID:29930085	FYPO:0000930	abolished protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPAC110.03 [assayed_using] cdc42/GTP+	(Figure 3)
PMID:29930085	FYPO:0000930	abolished protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPAC110.03 [assayed_using] cdc42/GTP+	(Figure 3)
PMID:29930085	FYPO:0004103	viable spherical vegetative cell [has_penetrance] high	(Figure 3, Figure 4, Figure S2, Movie 2, Movie 3, Movie 4)
PMID:29930085	FYPO:0004103	viable spherical vegetative cell [has_penetrance] high	(Figure 3, Movie 2)
PMID:29930085	FYPO:0002104	viable vegetative cell with normal cell shape	(Figure 4, Figure S3, Movie 4)
PMID:29930085	FYPO:0002104	viable vegetative cell with normal cell shape	(Figure 4, Movie 4)
PMID:29930085	FYPO:0002104	viable vegetative cell with normal cell shape	(Figure 4, Movie 4)
PMID:29930085	FYPO:0002104	viable vegetative cell with normal cell shape	(Figure 4, Movie 4)
PMID:29930085	FYPO:0003316	normal protein localization to growing cell tip	(Figure 4,AB)
PMID:29930085	GO:0005737	cytoplasm	(Figure 5, Figure S4, Movie 5)
PMID:29930085	GO:0110085	mitotic actomyosin contractile ring	(Figure 5, Figure S4, Movie 5)
PMID:29930085	FYPO:0002060	viable vegetative cell population	(Figure 5B)
PMID:29930085	FYPO:0005465	normal cell polarity	(Figure 5B)
PMID:29930085	FYPO:0004103	viable spherical vegetative cell [has_penetrance] high	(Figure 6, Figure S6, Movie 7)
PMID:29930085	FYPO:0002104	viable vegetative cell with normal cell shape	(Figure 7, Figure S8)
PMID:29930085	FYPO:0002380	viable spheroid vegetative cell [has_penetrance] high	(Figure 7, Figure S8)
PMID:29930085	FYPO:0004103	viable spherical vegetative cell [has_penetrance] high	(Figure 7, Movie 9)
PMID:29930085	FYPO:0006637	decreased protein localization to cell cortex of cell tip, with protein distributed in cortex [assayed_using] PomBase:SPCC1840.02c	(Figure 7, Movie 9) (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29930085	FYPO:0006639	normal vegetative cell diameter	(Figure 7C)
PMID:29930085	FYPO:0001877	viable thin vegetative cell [has_severity] low	(Figure 7D)
PMID:29930085	FYPO:0002106	viable stubby vegetative cell [has_severity] low	(Figure 7D)
PMID:29930085	FYPO:0006617	viable elongated vegetative cell with increased cell diameter	(Figure S1)
PMID:29930085	FYPO:0002150	inviable spore population	(Figure S3)
PMID:29930085	FYPO:0000644	normal protein localization during vegetative growth [assayed_using] PomBase:SPAC24H6.09	(Figure S3)
PMID:29930085	FYPO:0002150	inviable spore population	(Figure S3)
PMID:29930085	FYPO:0004103	viable spherical vegetative cell [has_penetrance] high	(Figure S6, Movie 8)
PMID:29930085	FYPO:0002104	viable vegetative cell with normal cell shape [has_penetrance] high	(Figure S6, Movie 8)
PMID:29930085	FYPO:0006637	decreased protein localization to cell cortex of cell tip, with protein distributed in cortex [assayed_using] PomBase:SPCC1840.02c	(comment: PORTLI GROWTH) (Figs 3B and 4B; Movie 2) (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29930085	FYPO:0006637	decreased protein localization to cell cortex of cell tip, with protein distributed in cortex [assayed_using] PomBase:SPCC1840.02c	(comment: PORTLI GROWTH) (Figs 3B and 4B; Movie 2) (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29930085	FYPO:0006638	decreased protein localization to medial cortex, with protein distributed in cell cortex, during vegetative growth [assayed_using] PomBase:SPBC28E12.03	(comment: PORTLI GROWTH) Figure 6C (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29930085	FYPO:0006637	decreased protein localization to cell cortex of cell tip, with protein distributed in cortex [assayed_using] PomBase:SPAC2F7.03c	(comment: PORTLI GROWTH) Figure S6 (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29930085	FYPO:0006637	decreased protein localization to cell cortex of cell tip, with protein distributed in cortex [assayed_using] PomBase:SPCC1840.02c	(comment: PORTLI GROWTH) Figure S6 (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29930085	FYPO:0006637	decreased protein localization to cell cortex of cell tip, with protein distributed in cortex [assayed_using] PomBase:SPCC1840.02c	(comment: PORTLI GROWTH) fig 2 (comment: CHECK interphase arrest https://github.com/pombase/fypo/issues/3339)
PMID:29930085	FYPO:0006638	decreased protein localization to medial cortex, with protein distributed in cell cortex, during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC28E12.03	(comment: PORTLI Growth) Figure 6, Figure S6, Movie 7 (comment: CHECK https://github.com/pombase/fypo/issues/3339)
PMID:29975113	FYPO:0001876	decreased asymmetric protein localization, with protein localized to both mitotic spindle pole bodies during anaphase [assayed_using] PomBase:SPAC17G8.10c	(DNS) Dma1-I194A constitutively localizes to SPB throughout the cell cycle. Dma1-I194A localizes more intensely at one of the two SPBs for most of mitosis
PMID:29975113	GO:0071341	medial cortical node	(Figure 1B and S1B)
PMID:29975113	GO:0032153	cell division site [exists_during] mitotic M phase	(Figure 1B and S1B) Dma1-mNeonGreen forms a ring at cell division site during early mitosis. Then it leaves and returns to cell division site during mitosis. Dma1 transiently leaves cell division site before Sid2 appears at the cell division site.
PMID:29975113	FYPO:0000836	increased protein level [assayed_using] PomBase:SPAC17G8.10c	(Figure 2B and C)
PMID:29975113	FYPO:0000912	abolished protein ubiquitination during vegetative growth [assayed_using] PomBase:SPAC17G8.10c	(Figure 2D)
PMID:29975113	GO:0061630	ubiquitin protein ligase activity [has_input] PomBase:SPAC17G8.10c [part_of] deactivation of mitotic spindle assembly checkpoint	(Figure 2D) (comment: CHECK in vivo)
PMID:29975113	FYPO:0000912	abolished protein ubiquitination during vegetative growth [assayed_using] PomBase:SPAC17G8.10c	(Figure 2G)
PMID:29975113	FYPO:0002635	normal protein ubiquitination during vegetative growth [assayed_using] PomBase:SPBC244.01c	(Figure S2A)
PMID:29975113	FYPO:0000912	abolished protein ubiquitination during vegetative growth [assayed_using] PomBase:SPBC244.01c	(Figure S2B)
PMID:29975113	FYPO:0002060	viable vegetative cell population	(Figure S2D)
PMID:29975113	FYPO:0001491	viable vegetative cell	(Figure S2D) dma1-GFP sid4-GBP-mCherry cells are very sick, if not die. ppc89-DUB rescued the synthetic sick phenotype of dma1-GFP sid4-GBP-mCherry. The cells have reduced levels of multi-nucleate and kissing nuclei compared with dma1-GFP sid4-GBP-mCherry.
PMID:29975113	GO:0044732	mitotic spindle pole body [exists_during] mitotic metaphase	(Figures 1B and S1A) Dma1-mNeonGreen became enriched at SPBs prior to SPB separation. It appeared to transiently leave SPBs during anaphase B, returning before telophase and then leaving again after cell division. Dma1 SPB transient loss happens before the development of Cdc7 SPB localiztion asymmetry. Dma1 failed to return to SPBs in late anaphase in cdc7-24 cells at restrictive temperature. Dma1 could be detected on majority SPBs in cdc16-116 cells at restrictive temperature, suggesting high SIN activity promote Dma1 SPB re-accumulation at the end of anaphase.
PMID:29975113	FYPO:0002797	decreased protein degradation [assayed_using] PomBase:SPAC17G8.10c	(comment: CHECK These data are consistent with auto-ubiquitination triggering Dma1 destruction.)
PMID:29975113	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPAC17G8.10c	(comment: Vw, because mutants are related to WT, I changed this to 'normal'), Dma1-I194A-mNeonGreen displays transient loss from SPB during anaphase, just like wild-type Dma1.
PMID:29975113	GO:0031030	negative regulation of septation initiation signaling	(comment: [ dma1 unubiquitinated, sid4 phosphorylated]) When Dma1-GFP is permanently tethered to SPBs by Sid4-GBP-mCherry, cells displayed multi-nucleate and kissing nuclei indicative of SIN and cytokinesis failure.
PMID:29975113	FYPO:0003627	normal protein localization [assayed_using] PomBase:SPBC244.01c	(comment: temporal localization pattern) Figure S2B
PMID:29975157	FYPO:0002253	normal septum location	(Fig. 1B)
PMID:29975157	FYPO:0002253	normal septum location	(Fig. 1B)
PMID:29975157	FYPO:0002253	normal septum location	(Fig. 1B)
PMID:29975157	FYPO:0002253	normal septum location	(Fig. 1B)
PMID:29975157	FYPO:0002253	normal septum location	(Fig. 1B)
PMID:29975157	FYPO:0000339	mislocalized septum during vegetative growth	(Fig. 1B)
PMID:29975157	FYPO:0000339	mislocalized septum during vegetative growth [has_severity] medium	(Fig. 1B)
PMID:29975157	FYPO:0002253	normal septum location	(Fig. 1B)
PMID:29975157	FYPO:0002253	normal septum location	(Fig. 1B)
PMID:29975157	FYPO:0000339	mislocalized septum during vegetative growth	(Fig. 1B)
PMID:29975157	FYPO:0002253	normal septum location	(Fig. 1B)
PMID:29975157	FYPO:0000339	mislocalized septum during vegetative growth [has_severity] medium	(Fig. 1B)
PMID:29975157	FYPO:0000339	mislocalized septum during vegetative growth	(Fig. 1B)
PMID:29975157	FYPO:0002253	normal septum location	(Fig. 1B)
PMID:29975157	FYPO:0002253	normal septum location	(Fig. 1B)
PMID:29975157	FYPO:0002253	normal septum location	(Fig. 1B)
PMID:29975157	FYPO:0001369	mislocalized actomyosin contractile ring	(Fig. 2A-C)
PMID:29975157	FYPO:0001369	mislocalized actomyosin contractile ring	(Fig. 2A-C)
PMID:29975157	FYPO:0002071	mislocalized nucleus during vegetative growth	(Fig. 2D)
PMID:29975157	FYPO:0005289	actomyosin contractile ring sliding	(Fig. 3)
PMID:29975157	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPAC20G8.05c	(Fig. 4A)
PMID:29975157	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPCC645.07	(Fig. 4B)
PMID:29975157	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPAC16E8.09	(Fig. 4C)
PMID:29975157	FYPO:0000929	decreased protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPCPB16A4.02c	(Fig. 4D)
PMID:29975157	FYPO:0006628	decreased phosphatidylinositol-4-phosphate level in plasma membrane	(Fig. 5A)
PMID:29975157	FYPO:0006629	normal phosphatidylinositol-4-phosphate level in plasma membrane	(Fig. 5A)
PMID:29975157	FYPO:0006628	decreased phosphatidylinositol-4-phosphate level in plasma membrane	(Fig. 5A)
PMID:29975157	FYPO:0006628	decreased phosphatidylinositol-4-phosphate level in plasma membrane	(Fig. 5A)
PMID:29975157	FYPO:0006628	decreased phosphatidylinositol-4-phosphate level in plasma membrane	(Fig. 5A)
PMID:29975157	FYPO:0006623	decreased phosphatidylinositol-3,4,5-trisphosphate level in plasma membrane	(Fig. 5B)
PMID:29975157	FYPO:0006623	decreased phosphatidylinositol-3,4,5-trisphosphate level in plasma membrane	(Fig. 5B)
PMID:29975157	FYPO:0006624	increased phosphatidylinositol-3,4,5-trisphosphate level in plasma membrane	(Fig. 5B)
PMID:29975157	FYPO:0006623	decreased phosphatidylinositol-3,4,5-trisphosphate level in plasma membrane	(Fig. 5B)
PMID:29975157	FYPO:0006624	increased phosphatidylinositol-3,4,5-trisphosphate level in plasma membrane	(Fig. 5B)
PMID:29975157	FYPO:0006626	increased phosphatidylinositol-4,5-bisphosphate level in plasma membrane	(Fig. 5C)
PMID:29975157	FYPO:0006627	normal phosphatidylinositol-4,5-bisphosphate level in plasma membrane	(Fig. 5C)
PMID:29975157	FYPO:0006625	decreased phosphatidylinositol-4,5-bisphosphate level in plasma membrane	(Fig. 5C)
PMID:29975157	FYPO:0006625	decreased phosphatidylinositol-4,5-bisphosphate level in plasma membrane	(Fig. 5C)
PMID:29975157	FYPO:0002253	normal septum location	(Fig. S1F)
PMID:29975157	FYPO:0002253	normal septum location	(Fig. S1F)
PMID:29975157	FYPO:0002253	normal septum location	(Fig. S1F)
PMID:29975157	FYPO:0000339	mislocalized septum during vegetative growth [has_severity] high	(Fig. S1F)
PMID:29975157	FYPO:0000123	large vacuoles during vegetative growth	(Fig. S2A)
PMID:29975157	FYPO:0000339	mislocalized septum during vegetative growth	(Fig. S2A-D)
PMID:29975157	FYPO:0001369	mislocalized actomyosin contractile ring	(Fig. S2C,D)
PMID:29975157	FYPO:0000339	mislocalized septum during vegetative growth	(Fig. S2E)
PMID:30003614	FYPO:0004695	increased cellular diglyceride level	(Fig. 4)
PMID:30003614	FYPO:0002236	normal cellular sterol ester level	(Fig. 4)
PMID:30003614	FYPO:0006632	normal cellular free fatty acid level	(Fig. 4)
PMID:30003614	FYPO:0002227	increased cellular triglyceride level during vegetative growth	(Fig. 4)
PMID:30003614	FYPO:0002061	inviable vegetative cell population	(Fig. 5) (comment: cerulenin)
PMID:30003614	FYPO:0000808	abnormal lipid droplet organization	(comment: increased number of lipid droplets/cell) (Fig. 3b,c)
PMID:30044717	GO:0051286	cell tip [exists_during] mitotic interphase	(Fig. 1)
PMID:30044717	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] low	(Fig. 2B)
PMID:30044717	FYPO:0002061	inviable vegetative cell population	(Fig. 2a)
PMID:30044717	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] complete	(Fig. 2a) (comment: vw: average survival ~ 7 cell cycles)
PMID:30044717	FYPO:0001355	decreased vegetative cell population growth	(Fig. 2b)
PMID:30044717	FYPO:0006880	increased protein localization to center of cell division site [has_penetrance] complete [assayed_using] PomBase:SPBC19G7.05c	(Fig. 4)
PMID:30044717	FYPO:0004653	delayed onset of actomyosin contractile ring contraction	(Fig. 5)
PMID:30044717	FYPO:0001581	vacuolated	(Fig. 5B)
PMID:30044717	FYPO:0002061	inviable vegetative cell population	(Fig. 5B)
PMID:30044717	FYPO:0002061	inviable vegetative cell population	(Fig. 5B)
PMID:30044717	FYPO:0006880	increased protein localization to center of cell division site [has_penetrance] complete [assayed_using] PomBase:SPAC18G6.03	(Fig. 5C)
PMID:30044717	FYPO:0006880	increased protein localization to center of cell division site [has_penetrance] complete [assayed_using] PomBase:SPAC6G9.11	(Fig. 5C)
PMID:30044717	FYPO:0006883	decreased exocytosis at cell division site [assayed_using] PomBase:SPAC6G9.11	(Fig. 5D and Movie 5)
PMID:30044717	FYPO:0001494	inviable elongated multiseptate vegetative cell	(Fig. 5b)
PMID:30044717	FYPO:0006880	increased protein localization to center of cell division site [has_penetrance] complete [assayed_using] PomBase:SPAC6G10.05c	(Fig. 6A)
PMID:30044717	GO:0032153	cell division site	(Fig. 7E)
PMID:30044717	GO:0035838	growing cell tip	(Fig. 7E)
PMID:30044717	FYPO:0001880	abolished protein localization to cell division site [assayed_using] PomBase:SPAC11E3.02c	(Fig. S1F)
PMID:30044717	FYPO:0001880	abolished protein localization to cell division site [assayed_using] PomBase:SPAC11E3.02c	(Fig. S1G)
PMID:30044717	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC11E3.02c	(Fig. S2)
PMID:30044717	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC11E3.02c	(Fig. S2)
PMID:30044717	FYPO:0006880	increased protein localization to center of cell division site [assayed_using] PomBase:SPAC11E3.02c	(Fig. S2,E)
PMID:30044717	FYPO:0006880	increased protein localization to center of cell division site [assayed_using] PomBase:SPAC11E3.02c	(Fig. S2,E)
PMID:30044717	FYPO:0006880	increased protein localization to center of cell division site [assayed_using] PomBase:SPAC11E3.02c	(Fig. S2C,E)
PMID:30044717	GO:0001786	phosphatidylserine binding	(Fig. S3 DE)
PMID:30044717	GO:0005546	phosphatidylinositol-4,5-bisphosphate binding	(Fig. S3 DE)
PMID:30044717	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] low	(Fig. S4C)
PMID:30044717	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] 55	(Fig. S4C)
PMID:30044717	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] 2	(Fig. S4C)
PMID:30044717	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] high	(Fig. S4C)
PMID:30044717	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPCC1840.02c	(Fig. S4E)
PMID:30044717	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPCC1281.01	(Fig. S4E)
PMID:30044717	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPAC17G8.12	(Fig. S6B)
PMID:30044717	GO:0032153	cell division site [exists_during] mitotic anaphase B	(Figure 1)
PMID:30044717	GO:0090689	cleavage furrow leading edge [exists_during] mitotic anaphase B	(Figure 1)
PMID:30044717	GO:0090689	cleavage furrow leading edge	(Figure 6E)
PMID:30044717	GO:0120207	endocytosis, site selection [happens_during] mitotic cytokinesis	(Figure 7)
PMID:30053106	GO:0160225	G-quadruplex unwinding activity	(comment: requires long flap (binding affinity much higher with 27-nt than 15-nt flap))
PMID:30053106	GO:0160225	G-quadruplex unwinding activity	(comment: requires long flap (binding affinity much higher with 27-nt than 15-nt flap))
PMID:30053106	GO:0070336	flap-structured DNA binding	(comment: requires long flap (binding affinity much higher with 27-nt than 15-nt flap))
PMID:30053106	GO:0070336	flap-structured DNA binding	(comment: requires long flap (binding affinity much higher with 27-nt than 15-nt flap))
PMID:30072377	FYPO:0001309	increased viability in stationary phase [has_severity] low	(Fig. 3B, Fig. 4A,B)
PMID:30072377	FYPO:0001309	increased viability in stationary phase [has_severity] low	(Fig. 3C, D; Fig. 4A,B)
PMID:30072377	FYPO:0001309	increased viability in stationary phase [has_severity] low	(Fig. 4A,B)
PMID:30072377	FYPO:0006779	resistance to spermidine	(Fig. 4C) Resistant to 1 mM spermidine at 37C.
PMID:30072377	FYPO:0006779	resistance to spermidine	(Fig. 4C) Resistant to 1mM spermidine at 37C.
PMID:30072439	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(comment: CHECK Partial suppression of growth defect in the presence of sorbitol)
PMID:30072439	FYPO:0006970	decreased cellular bisphosphoglyceric acid level	(comment: CHECK decreased cellular diphosphoglycerate level)
PMID:30072439	FYPO:0006951	increased cellular N(alpha),N(alpha)-dimethyl-L-histidine level	(comment: CHECK increased cellular dimethyl-histidine level during vegetative growth)
PMID:30072439	FYPO:0003516	increased cellular L-ergothioneine level during vegetative growth	(comment: Drastic changes in antioxidants, sugar derivatives, amino acid derivatives, organic acids, coenzyme A (CoA), and nucleotide derivatives. Most of these compounds are biomarkers for nutritional starvation (low-glucose or nitrogen-starvation).
PMID:30072439	FYPO:0004165	normal glucose consumption	(comment: Normal glucose consumption, but cell division is sensitive to low glucose condition)
PMID:30072439	FYPO:0004860	increased cell wall beta-glucan level [has_severity] medium	(comment: Sorbitol addition partly suppresses beta-glucan accumulation in cwh43-G753R mutant cells)
PMID:30072439	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(comment: Suppression of temperature sensitivity by 1.2M sorbitol)
PMID:30072439	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(comment: Suppression of temperature sensitivity by 1.2M sorbitol)
PMID:30072439	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(comment: Suppression of temperature sensitivity by 1.2M sorbitol)
PMID:30072439	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Partial suppression of growth defect in the presence of sorbitol
PMID:30072439	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	Suppression of temperature sensitivity by 1.2M sorbitol
PMID:30072439	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Synthetic growth defect between cwh43-G753R mutant and dga1Δ plh1Δ double deletion mutant.
PMID:30072439	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	Synthetic growth defect between cwh43-G753R mutant and dga1Δ plh1Δ double deletion mutant.
PMID:30076928	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPCC1259.13	(comment: CHECK RT-PCR)
PMID:30076928	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPCC338.17c	(comment: CHECK RT-PCR)
PMID:30076928	FYPO:0003049	increased transcriptional readthrough [assayed_using] PomBase:SPAC29E6.08	(comment: transcription read through by PCR)
PMID:30076928	FYPO:0004811	abnormal termination of RNA polymerase II transcription [assayed_using] PomBase:SPAC29E6.08	(comment: transcription read through by PCR)
PMID:30089114	MOD:01148	ubiquitinylated lysine	(comment: CHECK polyubiquitylated)
PMID:30089908	FYPO:0000413	abolished cell fusion during mating	(Fig. 1 II)
PMID:30089908	FYPO:0006669	abnormal mating between three cells	(Fig. 1a) type IIIa
PMID:30089908	FYPO:0006672	transient cell fusion during mating followed by meiotic cell cycle entry and sporulation [has_penetrance] high	(Fig. 1a) type IIIb
PMID:30089908	FYPO:0006672	transient cell fusion during mating followed by meiotic cell cycle entry and sporulation [has_penetrance] low	(Fig. 1a) type IIIb
PMID:30089908	FYPO:0000590	normal sporulation [has_penetrance] complete	(Fig. 1g)
PMID:30089908	FYPO:0006014	promiscuous mating	(Fig. 2c) (comment: never ending search for mating partner)
PMID:30089908	FYPO:0006674	abolished protein localization to nucleus during mating [assayed_using] PomBase:SPBC23G7.17c	(Fig. 3d, Supplementary Video 5b)
PMID:30089908	FYPO:0006014	promiscuous mating	(Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b)
PMID:30089908	FYPO:0001147	normal mating efficiency	(Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b)
PMID:30089908	FYPO:0002052	normal sporulation frequency	(Fig. 4a, Extended Data Fig. 4c, Supplementary Video 7b)
PMID:30089908	FYPO:0006673	decreased DNA content in spore	(Figure 1c)
PMID:30089908	FYPO:0006685	abolished protein localization to mating partner nucleus in zygote [assayed_using] PomBase:SPMTR.02	(comment: CHECK *******to nucleus of opposite mating type cell******)
PMID:30089908	FYPO:0001983	protein absent from cell [assayed_using] PomBase:SPBC119.04	(comment: CHECK ******abolished in M cells) Fig. 2a, Supplementary Video 5, Fig. 2b, Supplementary Video 2a Importantly, mei3 was also asymmetrically expressed in WT...zygotes first express the meiotic inducer Mei3 from the P genome.
PMID:30089908	GO:0140538	negative regulation of conjugation with zygote	(comment: CHECK GO:0140538 +name: negative regulation of conjugation with zygote https://github.com/geneontology/go-ontology/issues/16329)
PMID:30089908	GO:0140538	negative regulation of conjugation with zygote	(comment: CHECK GO:0140538 +name: negative regulation of conjugation with zygote https://github.com/geneontology/go-ontology/issues/16329)
PMID:30089908	GO:0005634	nucleus	(comment: CHECK P-cells (rapid) M-cells (delayed))
PMID:30089908	FYPO:0000678	unequal homologous chromosome segregation	(comment: CHECK abolished karyogamy with transient cytogamy -this is a bit like twin haploid meiosis? should be siblings? also looks like karyogamy failure)
PMID:30089908	FYPO:0006672	transient cell fusion during mating followed by meiotic cell cycle entry and sporulation	(comment: CHECK abolished karyogamy with transient cytogamy -this is a bit like twin haploid meiosis? should be siblings? also looks like karyogamy failure)
PMID:30089908	GO:0062071	Pi Mi complex	(comment: CHECK go-ontology/issues/16327)
PMID:30089908	GO:0005737	cytoplasm	(comment: M-cells)
PMID:30089908	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC119.04 [part_of] cell cycle switching, mitotic to meiotic cell cycle	(comment: Regulation of asymmetric gene expression from parental genomes Factor that regulates differential gene expression of homologous parental gene copies)
PMID:30089908	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC119.04 [part_of] cell cycle switching, mitotic to meiotic cell cycle	(comment: Regulation of asymmetric gene expression from parental genomes Factor that regulates differential gene expression of homologous parental gene copies)
PMID:30089908	GO:0005515	protein binding [part_of] cell cycle switching, mitotic to meiotic cell cycle	(comment: Regulation of asymmetric gene expression from parental genomes)
PMID:30089908	GO:0005515	protein binding [part_of] cell cycle switching, mitotic to meiotic cell cycle	(comment: Regulation of asymmetric gene expression from parental genomes)
PMID:30089908	FYPO:0001886	meiotic cell cycle entry and sporulation in haploid	(comment: in M-cell)
PMID:30089908	FYPO:0006014	promiscuous mating	(comment: never ending search for mating partner by P cell)
PMID:30089908	GO:0005634	nucleus	Extended Data Fig. 3b, Supplementary Video 5a
PMID:30089908	FYPO:0006669	abnormal mating between three cells [has_penetrance] 16	Extended Data Fig. 5e, f, Supplementary Video 9; see also ref. 1
PMID:30089908	FYPO:0006669	abnormal mating between three cells [has_penetrance] 10	Extended Data Fig. 5e, f, Supplementary Video 9; see also ref. 1
PMID:30089908	FYPO:0003363	abolished cytogamy [has_penetrance] high	Extended data figure 1F (comment: dominant over shk2 downstream sporulation phenotypes)
PMID:30089908	GO:0000755	cytogamy	Homothalic pak2∆ partners exhibit fusion efficiency decrease of ~20% as compared to wild-type partner fusion. Homothalic pak2∆ cells undergo transient fusion with frequency of ~10%, which is absent in wild-type matings.
PMID:30102332	FYPO:0000650	increased septation index	(Figure 5)
PMID:30102332	FYPO:0000650	increased septation index	(Figure 5)
PMID:30102332	FYPO:0000650	increased septation index	(Figure 5)
PMID:30102332	FYPO:0004903	decreased level of cell separation after cytokinesis gene mRNA during vegetative growth	(Figures 4, 5)
PMID:30102332	FYPO:0004903	decreased level of cell separation after cytokinesis gene mRNA during vegetative growth	(Figures 4, 5)
PMID:30102332	FYPO:0004903	decreased level of cell separation after cytokinesis gene mRNA during vegetative growth	(Figures 4, 5)
PMID:30102332	GO:0006368	transcription elongation by RNA polymerase II	(comment: also inferred from orthology, interactions, and chromatin localization (ChIP))
PMID:30102332	GO:0006368	transcription elongation by RNA polymerase II	(comment: also inferred from orthology, interactions, and chromatin localization (ChIP))
PMID:30102332	GO:0006368	transcription elongation by RNA polymerase II	(comment: also inferred from orthology, interactions, and chromatin localization (ChIP))
PMID:30104346	GO:0045027	DNA end binding [happens_during] replication-born double-strand break repair via sister chromatid exchange	(comment: evidence is combination of ChIP in this paper plus data in other publications showing that Ctp1 binds DNA directly)
PMID:30104346	GO:0045027	DNA end binding [happens_during] replication-born double-strand break repair via sister chromatid exchange	(comment: evidence is combination of ChIP in this paper plus data in other publications showing that Rad50 orthologs (and therefore almost certainly Sc Rad50) binds DNA directl)
PMID:30104346	GO:0003697	single-stranded DNA binding [happens_during] replication-born double-strand break repair via sister chromatid exchange	(comment: evidence is combination of ChIP in this paper plus data in other publications showing that Rad52 binds DNA directly)
PMID:30110338	GO:0062072	histone H3K9me2/3 reader activity [has_input] hht2/Me(K9) [part_of] heterochromatin formation [occurs_at] nucleosome	(comment: CHECK H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331)
PMID:30110338	GO:0062072	histone H3K9me2/3 reader activity [has_input] hht3/Me(K9) [part_of] heterochromatin formation [occurs_at] nucleosome	(comment: CHECK H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331)
PMID:30110338	GO:0062072	histone H3K9me2/3 reader activity [has_input] hht1/Me(K9) [part_of] heterochromatin formation [occurs_at] nucleosome	(comment: CHECK H3 K9me3 https://github.com/geneontology/go-ontology/issues/16331)
PMID:30110338	FYPO:0004232	abolished methylated histone binding [assayed_using] PomBase:SPBC16C6.10 [assayed_using] PomBase:SPAC1834.04	(comment: CHECK H3 K9me3)
PMID:30116786	FYPO:0002552	lipid droplets present in decreased numbers	(Fig. 3)
PMID:30116786	FYPO:0006345	increased duration of protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPAC1952.13	(Fig. 3)
PMID:30116786	FYPO:0006345	increased duration of protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPAC1952.13	(Fig. 3)
PMID:30116786	FYPO:0002552	lipid droplets present in decreased numbers	(Fig. 3)
PMID:30116786	GO:0005634	nucleus [exists_during] cell quiescence following G1 arrest due to nitrogen limitation	(Fig. 3B)
PMID:30116786	GO:0005634	nucleus [exists_during] single-celled organism vegetative growth phase	(Fig. 3B)
PMID:30116786	FYPO:0006667	abnormal nuclear morphology during G0	(Fig. 3C)
PMID:30116786	FYPO:0000238	inviable cell upon G0 to G1 transition	(Fig. 3F) (comment: loss of mitotic competence)
PMID:30116786	FYPO:0006660	loss of viability upon G0 to G1 transition	(Fig. 3F) (comment: loss of mitotic competence)
PMID:30116786	FYPO:0006662	fragmented nucleus during G0 [has_penetrance] ~40	(Fig. 4A,E)
PMID:30116786	FYPO:0002703	increased protein level in autophagosome [assayed_using] PomBase:SPAC664.02c	(Fig. 4C)
PMID:30116786	FYPO:0006664	elongated nucleus during G0 [has_penetrance] ~10	(Fig. 4E)
PMID:30116786	FYPO:0006662	fragmented nucleus during G0 [has_penetrance] ~42	(Fig. 4E)
PMID:30116786	FYPO:0006665	increased nucleophagy during G0 [has_penetrance] ~35	(Fig. 4E)
PMID:30116786	FYPO:0006665	increased nucleophagy during G0 [has_penetrance] ~15	(Fig. 4E)
PMID:30116786	FYPO:0006662	fragmented nucleus during G0 [has_penetrance] ~20	(Fig. 4E)
PMID:30116786	FYPO:0006664	elongated nucleus during G0 [has_penetrance] ~30	(Fig. 4E)
PMID:30116786	FYPO:0006668	normal nuclear morphology during G0 [has_penetrance] ~35	(Fig. 4E)
PMID:30116786	FYPO:0001673	normal nuclear morphology [has_penetrance] ~2	(Fig. 4E)
PMID:30116786	FYPO:0006662	fragmented nucleus during G0 [has_penetrance] ~7	(Fig. 4E)
PMID:30116786	FYPO:0006665	increased nucleophagy during G0 [has_penetrance] ~52	(Fig. 4E)
PMID:30116786	FYPO:0006664	elongated nucleus during G0 [has_penetrance] ~60	(Fig. 4E)
PMID:30116786	FYPO:0006662	fragmented nucleus during G0 [has_penetrance] ~8	(Fig. 4E)
PMID:30116786	FYPO:0006664	elongated nucleus during G0 [has_penetrance] ~6	(Fig. 4E)
PMID:30116786	FYPO:0006664	elongated nucleus during G0 [has_penetrance] ~50	(Fig. 4E)
PMID:30116786	FYPO:0006665	increased nucleophagy during G0 [has_penetrance] ~39	(Fig. 4E)
PMID:30116786	FYPO:0006662	fragmented nucleus during G0	(Fig. S3)
PMID:30134042	FYPO:0005314	decreased protein localization to chromatin at MCB promoters during vegetative growth [assayed_using] PomBase:SPBC336.12c	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	FYPO:0005314	decreased protein localization to chromatin at MCB promoters during vegetative growth [assayed_using] PomBase:SPBC336.12c	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	FYPO:0005314	decreased protein localization to chromatin at MCB promoters during vegetative growth [assayed_using] PomBase:SPBC336.12c	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	FYPO:0005314	decreased protein localization to chromatin at MCB promoters during vegetative growth [assayed_using] PomBase:SPBC336.12c	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	FYPO:0005314	decreased protein localization to chromatin at MCB promoters during vegetative growth [assayed_using] PomBase:SPBC336.12c	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	FYPO:0006739	normal protein localization to chromatin at MCB promoters during vegetative growth [assayed_using] PomBase:SPAC23G3.04	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	FYPO:0005314	decreased protein localization to chromatin at MCB promoters during vegetative growth [assayed_using] PomBase:SPBC336.12c	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	FYPO:0005314	decreased protein localization to chromatin at MCB promoters during vegetative growth [assayed_using] PomBase:SPBC336.12c	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	GO:0000785	chromatin [coincident_with] MCB	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	GO:0000785	chromatin [coincident_with] MCB	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	FYPO:0006740	increased protein localization to chromatin at MCB promoters during vegetative growth [assayed_using] PomBase:SPAC23G3.04	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30134042	FYPO:0006739	normal protein localization to chromatin at MCB promoters during vegetative growth [assayed_using] PomBase:SPAC23G3.04	(comment: CHECK assayed at cdc18 and cdc22)
PMID:30155942	FYPO:0001387	loss of viability at high temperature	(Fig. 2B)
PMID:30155942	FYPO:0001387	loss of viability at high temperature	(Fig. 2B)
PMID:30155942	FYPO:0001387	loss of viability at high temperature	(Fig. 2B)
PMID:30155942	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 2B, Fig. S3A)
PMID:30155942	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 2B, Fig. S3A)
PMID:30155942	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 2B, Fig. S3A)
PMID:30155942	FYPO:0001270	complete but unequal mitotic sister chromatid segregation	(Fig. 3A)
PMID:30155942	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 3B)
PMID:30155942	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 3B)
PMID:30155942	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 3B)
PMID:30155942	FYPO:0005371	increased linear minichromosome loss during vegetative growth [has_severity] medium	(Fig. 3C)
PMID:30155942	FYPO:0005371	increased linear minichromosome loss during vegetative growth [has_severity] low	(Fig. 3C)
PMID:30155942	FYPO:0005371	increased linear minichromosome loss during vegetative growth [has_severity] high	(Fig. 3C)
PMID:30155942	FYPO:0001839	normal minichromosome loss	(Fig. 3C)
PMID:30155942	FYPO:0005371	increased linear minichromosome loss during vegetative growth [has_severity] high	(Fig. 3C)
PMID:30155942	FYPO:0005371	increased linear minichromosome loss during vegetative growth [has_severity] medium	(Fig. 3C)
PMID:30155942	FYPO:0005079	normal protein localization to chromatin at centromere central core [assayed_protein] PomBase:SPCC16A11.14	(Fig. 4B)
PMID:30155942	FYPO:0005080	normal protein localization to heterochromatin at centromere inner repeat [assayed_protein] PomBase:SPCC16A11.14	(Fig. 4B)
PMID:30155942	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_protein] PomBase:SPCC16A11.14 [assayed_region] dg_repeat [assayed_region] dh_repeat	(Fig. 4B)
PMID:30155942	FYPO:0005079	normal protein localization to chromatin at centromere central core [assayed_protein] PomBase:SPCC16A11.14	(Fig. 4C)
PMID:30155942	FYPO:0002842	decreased protein localization to centromere outer repeat [assayed_protein] PomBase:SPCC16A11.14	(Fig. 4C)
PMID:30155942	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_protein] PomBase:SPCC16A11.14 [assayed_region] dg_repeat [assayed_region] dh_repeat	(Fig. 4C)
PMID:30155942	FYPO:0005079	normal protein localization to chromatin at centromere central core [assayed_protein] PomBase:SPCC16A11.14	(Fig. 4C)
PMID:30155942	FYPO:0000863	normal histone H3-K9 dimethylation at centromere inner repeat during vegetative growth	(Fig. 4E)
PMID:30155942	FYPO:0004743	normal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 4E)
PMID:30155942	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPCC338.17c [assayed_region] dg_repeat [assayed_region] dh_repeat [has_severity] medium	(Fig. 4F)
PMID:30155942	FYPO:0004345	decreased protein localization to chromatin at long terminal repeat [assayed_protein] PomBase:SPCC16A11.14 [has_severity] low	(Fig. 5B)
PMID:30155942	FYPO:0005082	normal protein localization to chromatin at long terminal repeat [assayed_protein] PomBase:SPCC16A11.14	(Fig. 5C)
PMID:30155942	FYPO:0004345	decreased protein localization to chromatin at long terminal repeat [has_severity] medium [assayed_protein] PomBase:SPCC16A11.14	(Fig. 5C)
PMID:30155942	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [has_severity] medium [assayed_protein] PomBase:SPCC16A11.14 [assayed_region] PomBase:SPBC32H8.12c	(Fig. 5C)
PMID:30155942	FYPO:0004579	normal transposable element-derived small RNA level [assayed_transcript] long_terminal_repeat_transcript	(Fig. 5D)
PMID:30155942	FYPO:0003105	increased transposable element-derived small RNA level [assayed_transcript] long_terminal_repeat_transcript [has_severity] medium	(Fig. 5D)
PMID:30155942	FYPO:0003105	increased transposable element-derived small RNA level [assayed_transcript] long_terminal_repeat_transcript [has_severity] high	(Fig. 5D)
PMID:30155942	FYPO:0003105	increased transposable element-derived small RNA level [assayed_transcript] long_terminal_repeat_transcript [has_severity] high	(Fig. 5D)
PMID:30155942	FYPO:0005932	decreased nucleosome occupancy at long terminal repeat [assayed_region] five_prime_LTR	(Fig. 5E)
PMID:30155942	FYPO:0005932	decreased nucleosome occupancy at long terminal repeat [assayed_region] five_prime_LTR	(Fig. 5E)
PMID:30155942	FYPO:0008457	normal nucleosome occupancy at long terminal repeat region [assayed_region] five_prime_LTR	(Fig. 5E)
PMID:30155942	FYPO:0003105	increased transposable element-derived small RNA level [assayed_transcript] long_terminal_repeat_transcript [has_severity] high	(Fig. 5F)
PMID:30155942	FYPO:0003105	increased transposable element-derived small RNA level [assayed_transcript] long_terminal_repeat_transcript [has_severity] high	(Fig. 5F)
PMID:30155942	GO:0005634	nucleus	(Fig. S1B)
PMID:30155942	FYPO:0004922	inviable elongated mononucleate aseptate cell with cell cycle arrest at mitotic G2/M phase transition [has_severity] high	(Fig. S2B, Fig. S3C)
PMID:30155942	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. S4A)
PMID:30155942	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. S4A)
PMID:30155942	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. S4A)
PMID:30155942	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. S4A)
PMID:30155942	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. S4A)
PMID:30155942	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. S4A)
PMID:30155942	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. S4B)
PMID:30155942	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] high	(Fig. S4B)
PMID:30155942	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. S4B)
PMID:30155942	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] high	(Fig. S4B)
PMID:30155942	FYPO:0009063	sensitive to X-rays during vegetative growth [has_severity] high	(Fig. S4B)
PMID:30155942	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. S4B)
PMID:30155942	FYPO:0000972	increased number of Rad52 foci during vegetative growth	(Fig. S5)
PMID:30155942	FYPO:0001174	normal growth on sucrose carbon source	(Fig. S6A)
PMID:30155942	FYPO:0001176	decreased cell population growth on sucrose carbon source [has_severity] low	(Fig. S6A)
PMID:30155942	FYPO:0001176	decreased cell population growth on sucrose carbon source [has_severity] high	(Fig. S6A)
PMID:30155942	FYPO:0001162	decreased cell population growth on raffinose carbon source [has_severity] medium	(Fig. S6A)
PMID:30155942	FYPO:0001162	decreased cell population growth on raffinose carbon source [has_severity] medium	(Fig. S6A)
PMID:30155942	FYPO:0001162	decreased cell population growth on raffinose carbon source [has_severity] high	(Fig. S6A)
PMID:30155942	FYPO:0003730	abolished cell population growth on galactose carbon source	(Fig. S6A)
PMID:30155942	FYPO:0003730	abolished cell population growth on galactose carbon source	(Fig. S6A)
PMID:30155942	FYPO:0003730	abolished cell population growth on galactose carbon source	(Fig. S6A)
PMID:30155942	FYPO:0000842	sensitive to ethanol during vegetative growth [has_severity] high	(Fig. S6B)
PMID:30155942	FYPO:0000842	sensitive to ethanol during vegetative growth [has_severity] medium	(Fig. S6B)
PMID:30155942	FYPO:0000785	sensitive to formamide [has_severity] high	(Fig. S6B)
PMID:30155942	FYPO:0000961	normal growth on sorbitol	(Fig. S6B)
PMID:30155942	FYPO:0000785	sensitive to formamide [has_severity] high	(Fig. S6B)
PMID:30155942	FYPO:0000785	sensitive to formamide [has_severity] high	(Fig. S6B)
PMID:30155942	FYPO:0000842	sensitive to ethanol during vegetative growth [has_severity] medium	(Fig. S6B)
PMID:30155942	FYPO:0000961	normal growth on sorbitol	(Fig. S6C)
PMID:30155942	FYPO:0009039	resistance to potassium chloride	(Fig. S6C)
PMID:30155942	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	(Fig. S6C)
PMID:30155942	FYPO:0001214	sensitive to potassium chloride [has_severity] low	(Fig. S6C)
PMID:30155942	FYPO:0000961	normal growth on sorbitol	(Fig. S6C)
PMID:30155942	FYPO:0005889	sensitive to sodium chloride [has_severity] high	(Fig. S6D)
PMID:30155942	FYPO:0005889	sensitive to sodium chloride [has_severity] high	(Fig. S6D)
PMID:30155942	FYPO:0005889	sensitive to sodium chloride [has_severity] high	(Fig. S6D)
PMID:30201262	FYPO:0007200	aggregated actin cortical patches during mitotic interphase	(Fig. 1)
PMID:30201262	FYPO:0007201	decreased rate of actin cortical patch localization to cell division site [has_penetrance] high	(Fig. 6)
PMID:30201262	FYPO:0007201	decreased rate of actin cortical patch localization to cell division site [has_penetrance] low	(Fig. 6)
PMID:30201262	FYPO:0007201	decreased rate of actin cortical patch localization to cell division site	(Fig. 6)
PMID:30201262	FYPO:0001904	premature actomyosin contractile ring disassembly	(comment: Temperature was shifted at anaphase B.)
PMID:30201262	FYPO:0000161	abnormal actomyosin contractile ring assembly	(comment: Temperature was shifted at prophase or metaphase.)
PMID:30201262	FYPO:0002061	inviable vegetative cell population	SFig5
PMID:30212894	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBC27B12.11c	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0001045	decreased acid phosphatase activity	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0001045	decreased acid phosphatase activity	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0002244	abolished acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0006657	abolished acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30212894	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: evidence: correlation with gel shift assays)
PMID:30217891	FYPO:0002484	increased intergenic meiotic recombination [has_severity] high	(Fig. 3)
PMID:30217891	FYPO:0007237	increased meiotic DNA double-strand break formation near existing double-strand break [has_severity] high	(Fig. 3)
PMID:30217891	FYPO:0004602	normal linear element morphology	(Supp Figure S14)
PMID:30228203	FYPO:0007601	decreased protein localization to mitochondrion, with diffuse cytoplasmic protein mislocalization [assayed_protein] PomBase:SPCC613.09	By confocal microscopy, Sen2-mECitrine and Sen54- mECitrine signals were very weak in tom70Δ cells, with the residual signals located in the cytoplasm and some located on mitochondria (Fig. 5A).
PMID:30228203	FYPO:0008394	decreased tRNA splicing	If S. pombe Tom70 is important for function and/or stability of the SEN complex, then deletion of S. pombe TOM70 would be expected to cause defects in pre- tRNA splicing. We used Northern analysis with probes complementary to the 5′ exons or introns of S. pombe tRNALeuCAA and tRNAProCGG. tom70Δ cells accumulate more intron-containing tRNALeuCAA and tRNAProCGG than wild-type cells (Fig. 5C), documenting a role for S. pombe Tom70 in pre-tRNA splicing.
PMID:30228203	FYPO:0008113	increased intron retention	If S. pombe Tom70 is important for function and/or stability of the SEN complex, then deletion of S. pombe TOM70 would be expected to cause defects in pre- tRNA splicing. We used Northern analysis with probes complementary to the 5′ exons or introns of S. pombe tRNALeuCAA and tRNAProCGG. tom70Δ cells accumulate more intron-containing tRNALeuCAA and tRNAProCGG than wild-type cells (Fig. 5C), documenting a role for S. pombe Tom70 in pre-tRNA splicing.
PMID:30228203	GO:0032473	cytoplasmic side of mitochondrial outer membrane	Sen2, Sen34, and Sen54 endogenously tagged at their C termini locate to mitochondria, as indicated by the overlapping signal with the mitochondrion stain MitoView Blue (Fig. 5A). H
PMID:30228203	GO:0032473	cytoplasmic side of mitochondrial outer membrane	Sen2, Sen34, and Sen54 endogenously tagged at their C termini locate to mitochondria, as indicated by the overlapping signal with the mitochondrion stain MitoView Blue (Fig. 5A). H
PMID:30228203	GO:0032473	cytoplasmic side of mitochondrial outer membrane	Sen2, Sen34, and Sen54 endogenously tagged at their C termini locate to mitochondria, as indicated by the overlapping signal with the mitochondrion stain MitoView Blue (Fig. 5A). H
PMID:30228203	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC613.09	the levels of Sen2-mECitrine and Sen54-mECitrine are reduced in tom70Δ cells compared with wild type (Fig. 5B; Supplemental Fig. S9). We interpret these results to support the hypothesis that S. pombe Tom70 functions in the mitochondrial localization of SEN subunits; when mitochondrial localization is not achieved, the SEN subunits become unstable, although it is possible that SEN subunits are poorly expressed in tom70Δ cells.
PMID:30279276	FYPO:0006636	mislocalized protein distributed in cell cortex [assayed_using] PomBase:SPAC110.03	(comment: Cdc42-GTP assayed with CRIB- broad zones of activity)
PMID:30280012	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] medium	(Fig. 6)
PMID:30280012	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] low	(Fig. 6)
PMID:30280012	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] low	(Fig. 6)
PMID:30280012	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] medium	(Fig. 6)
PMID:30280012	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] medium	(Fig. 6)
PMID:30280012	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] medium	(Fig. 6)
PMID:30280012	FYPO:0002177	viable vegetative cell with normal cell morphology	(Fig. S5C, S6)
PMID:30280012	FYPO:0000082	decreased cell population growth at high temperature	(Figure S5A, S5B)
PMID:30282034	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_using] PomBase:SPAC222.09	(comment: CHECK at transcription_termination_signal)
PMID:30282034	FYPO:0006020	abnormal protein distribution along RNA polymerase II-transcribed genes [assayed_using] PomBase:SPBC28F2.12	(comment: CHECK at transcription_termination_signal)
PMID:30282034	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_using] PomBase:SPAC222.09	(comment: CHECK at transcription_termination_signal)
PMID:30282034	FYPO:0007536	normal protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_using] PomBase:SPAC222.09	(comment: CHECK at transcription_termination_signal)
PMID:30332655	MOD:00696	phosphorylated residue [removed_during] mitotic cytokinesis [removed_by] PomBase:SPCC830.06	(comment: inferred from phenotypes and from direct assay using human calcineurin)
PMID:30348841	FYPO:0004909	loss of punctate nuclear protein localization, with protein distributed in nucleus [assayed_using] PomBase:SPBC20F10.04c	(Fig. 1 a) brc1 mutant abolishes Nse4 nuclear foci in HU/MMS treated cells
PMID:30348841	FYPO:0002624	decreased punctate nuclear protein localization [assayed_using] PomBase:SPBC20F10.04c	(Fig. 1) brc1 mutant cells expressing brc1-T672A are deficient in Nse4 foci formation
PMID:30348841	MOD:01149	sumoylated lysine [added_during] DNA damage response	As anticipated, the MMS-induced SUMOylation of Nse4-TAP in wild-type cells was detectable upon immunoprecipitation (IP) of Nse4 without overexpression or initial enrichment of SUMO (Fig. 4A)
PMID:30348841	FYPO:0002775	decreased level of sumoylated protein in cell [assayed_protein] PomBase:SPBC20F10.04c	MMS-induced Nse4 SUMOylation was also reduced in brc1Δ cells but was similar to wild-type in rhp18Δ cells, which support normal Nse4-GFP focus formation (Fig. 4B)
PMID:30348841	FYPO:0006631	decreased protein localization to chromatin [assayed_using] PomBase:SPBC20F10.04c [has_penetrance] high	Notably, however, deletion of either Nse5 or Nse6 strongly reduced Nse4 residence at all binding sites tested, which was most evident under conditions of genotoxic stress that stimulate de novo Smc5-Smc6 loading
PMID:30348841	FYPO:0006631	decreased protein localization to chromatin [assayed_protein] PomBase:SPBC20F10.04c	Notably, however, deletion of either Nse5 or Nse6 strongly reduced Nse4 residence at all binding sites tested, which was most evident under conditions of genotoxic stress that stimulate de novo Smc5-Smc6 loading
PMID:30348841	FYPO:0004909	loss of punctate nuclear protein localization, with protein distributed in nucleus [assayed_using] PomBase:SPBC20F10.04c	Nse4 foci gone in nse6 mutant cells
PMID:30348841	FYPO:0002776	normal level of sumoylated protein in cell [assayed_using] PomBase:SPBC20F10.04c	Nse4 sumoylation at wild type level
PMID:30348841	FYPO:0002775	decreased level of sumoylated protein in cell [assayed_using] PomBase:SPBC20F10.04c	Nse4 sumoylation reduced in brc1Δ
PMID:30348841	FYPO:0002775	decreased level of sumoylated protein in cell [assayed_using] PomBase:SPBC20F10.04c [has_severity] high	Nse4 sumoylation undetectable in nse6Δ
PMID:30348841	FYPO:0005018	decreased double-stranded DNA binding [assayed_using] PomBase:SPBC20F10.04c	deletion of Brc1 significantly reduced Nse4 residence at binding sites tested under normal and genotoxic stress
PMID:30348841	FYPO:0005018	decreased double-stranded DNA binding [assayed_using] PomBase:SPBC20F10.04c	deletion of Nse5 strongly reduced Nse4 residence at binding sites tested under normal and genotoxic stress
PMID:30348841	FYPO:0005018	decreased double-stranded DNA binding [assayed_using] PomBase:SPBC20F10.04c	deletion of Nse6 strongly reduced Nse4 residence at binding sites tested under normal and genotoxic stress
PMID:30348841	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC11E3.08c [assayed_protein] PomBase:SPBC582.05c	mutations in brc1 weaken interaction with nse6
PMID:30348841	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	nse2-SA brc1Δ cells are more sensitive to genotoxins than either single mutant (Fig. 4C).
PMID:30355493	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC3G6.02 [assayed_using] PomBase:SPAC821.06 [has_severity] high	(Fig. 2d)
PMID:30355493	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC3G6.02 [assayed_using] PomBase:SPAC22A12.16	(Fig. 2d)
PMID:30355493	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC3G6.02 [assayed_using] PomBase:SPAC9G1.11c [has_severity] high	(Fig. 2d)
PMID:30355493	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC3G6.02 [assayed_using] PomBase:SPBC1703.07	(Fig. 2d)
PMID:30355493	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC3G6.02 [assayed_using] PomBase:SPCC1739.08c	(Fig. 2d)
PMID:30355493	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC3G6.02 [assayed_using] PomBase:SPBC16A3.01 [has_severity] high	(Fig. 2d)
PMID:30355493	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC3G6.02 [assayed_using] PomBase:SPAC4F10.11 [has_severity] high	(Fig. 2d)
PMID:30355493	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC3G6.02 [assayed_using] PomBase:SPAC22A12.16	(Fig. 2d)
PMID:30355493	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC3G6.02 [assayed_using] PomBase:SPBC1703.07	(Fig. 2d)
PMID:30355493	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC3G6.02 [assayed_using] PomBase:SPAC22A12.16	(Fig. 3c)
PMID:30355493	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC3G6.02 [assayed_using] PomBase:SPBC16A3.01 [has_severity] high	(Fig. 4)
PMID:30355493	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC17G6.12 [assayed_using] PomBase:SPBC12D12.08c	(Fig. S3C)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0003267	normal acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0003267	normal acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0002243	increased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 2A)
PMID:30355770	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 2B)
PMID:30355770	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 2B)
PMID:30355770	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02 [has_severity] high	(Fig. 2B)
PMID:30355770	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] high [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 2B)
PMID:30355770	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 2B)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 4B)
PMID:30355770	FYPO:0002243	increased acid phosphatase activity	(Fig. 4B)
PMID:30355770	FYPO:0002243	increased acid phosphatase activity [has_severity] low	(Fig. 4B)
PMID:30355770	FYPO:0002243	increased acid phosphatase activity [has_severity] low	(Fig. 4B)
PMID:30355770	FYPO:0003267	normal acid phosphatase activity	(Fig. 7D)
PMID:30355770	FYPO:0003267	normal acid phosphatase activity	(Fig. 7D)
PMID:30355770	FYPO:0003267	normal acid phosphatase activity	(Fig. 7D)
PMID:30355770	FYPO:0003267	normal acid phosphatase activity	(Fig. 7D)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 7D)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. 7D)
PMID:30355770	FYPO:0002243	increased acid phosphatase activity [has_severity] high	(Fig. S5)
PMID:30355770	FYPO:0001045	decreased acid phosphatase activity	(Fig. S5)
PMID:30355770	FYPO:0002243	increased acid phosphatase activity	(Fig. S5)
PMID:30355770	FYPO:0002243	increased acid phosphatase activity [has_severity] medium	(Fig. S6)
PMID:30355770	FYPO:0002243	increased acid phosphatase activity [has_severity] medium	(Fig. S6)
PMID:30355770	FYPO:0002243	increased acid phosphatase activity [has_severity] medium	(Fig. S6)
PMID:30355770	FYPO:0002061	inviable vegetative cell population	(Fig. S8)
PMID:30355770	FYPO:0002060	viable vegetative cell population	(Fig. S8)
PMID:30355770	FYPO:0002061	inviable vegetative cell population	(Fig. S8)
PMID:30389790	FYPO:0001035	increased cell wall thickness during vegetative growth	(Fig. 10)
PMID:30389790	FYPO:0006982	normal cell wall morphology during vegetative growth	(Fig. 10)
PMID:30389790	FYPO:0000805	abnormal endoplasmic reticulum organization	(Fig. 10)
PMID:30389790	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2b)
PMID:30389790	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 2b)
PMID:30389790	FYPO:0006980	increased Glc3Man9GlcNAc level	(Fig. 3b)
PMID:30389790	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 5b)
PMID:30389790	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(Fig. 5b)
PMID:30389790	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(Fig. 5b)
PMID:30389790	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(Fig. 5b)
PMID:30389790	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 5b)
PMID:30389790	FYPO:0001211	Glc3Man9GlcNAc absent from cell	(Fig. 6)
PMID:30389790	FYPO:0001211	Glc3Man9GlcNAc absent from cell	(Fig. 6)
PMID:30389790	FYPO:0001211	Glc3Man9GlcNAc absent from cell	(Fig. 6)
PMID:30389790	FYPO:0006981	normal cell wall polysaccharide composition during vegetative growth	(Fig. S4)
PMID:30389790	FYPO:0007030	normal cell wall monosaccharide composition during vegetative growth	(Fig. S4)
PMID:30389790	FYPO:0002060	viable vegetative cell population	(Figure 5 and 11) (comment: no loss of viability )
PMID:30389790	FYPO:0001357	normal vegetative cell population growth	(Figure 5b and S2)
PMID:30389790	FYPO:0001124	normal vegetative cell size	(Figure 5c)
PMID:30389790	FYPO:0000672	normal cell morphology	(Figure 5c)
PMID:30389790	FYPO:0001910	abnormal protein glycosylation during vegetative growth	(Figure 5c) (comment: CHECK hypoglycosylation)
PMID:30389790	GO:0004573	Glc3Man9GlcNAc2 oligosaccharide glucosidase activity [part_of] dolichol-linked oligosaccharide biosynthetic process	(comment: Glucosidase I, a type II membrane protein with a luminal hydrolytic domain, removes the outermost glucose from protein-linked Glc3Man9GlcNAc2 in the endoplasmic reticulum)
PMID:30393157	FYPO:0005823	increased phosphatidylserine externalization	(Fig. 1A)
PMID:30393157	FYPO:0006661	fragmented nucleus [has_penetrance] 40	(Fig. 1C,D)
PMID:30393157	FYPO:0002061	inviable vegetative cell population	(Fig. 2B)
PMID:30393157	FYPO:0002061	inviable vegetative cell population	(Fig. 2B)
PMID:30393157	FYPO:0002061	inviable vegetative cell population	(Fig. 2B)
PMID:30393157	FYPO:0002061	inviable vegetative cell population	(Fig. 2B)
PMID:30393157	FYPO:0005823	increased phosphatidylserine externalization	(Fig. 2C,D)
PMID:30393157	FYPO:0005823	increased phosphatidylserine externalization	(Fig. 2C,D)
PMID:30393157	FYPO:0005823	increased phosphatidylserine externalization	(Fig. 2C,D)
PMID:30393157	FYPO:0005823	increased phosphatidylserine externalization	(Fig. 2C,D)
PMID:30393157	FYPO:0005823	increased phosphatidylserine externalization	(Fig. 2C,D)
PMID:30393157	FYPO:0006661	fragmented nucleus	(Fig. 2E,F)
PMID:30393157	FYPO:0006661	fragmented nucleus	(Fig. 2E,F)
PMID:30393157	FYPO:0006661	fragmented nucleus	(Fig. 2E,F)
PMID:30393157	FYPO:0006661	fragmented nucleus	(Fig. 2E,F)
PMID:30393157	FYPO:0003004	increased cellular reactive oxygen species level during vegetative growth	(Fig. 4)
PMID:30393157	FYPO:0004944	decreased mitochondrial membrane potential	(Fig. 4)
PMID:30393157	FYPO:0003810	small fragmented mitochondria present in increased numbers	(Fig. 4)
PMID:30393157	FYPO:0002006	increased cellular iron level [assayed_using] PomBase:SPAC22A12.11	(Fig. 5A)
PMID:30393157	FYPO:0002006	increased cellular iron level [assayed_using] PomBase:SPBC660.07	(Fig. 5A)
PMID:30393157	FYPO:0002006	increased cellular iron level [assayed_using] PomBase:SPAC977.16c	(Fig. 5A)
PMID:30393157	FYPO:0002006	increased cellular iron level [assayed_using] PomBase:SPAC13F5.03c	(Fig. 5A)
PMID:30393157	FYPO:0002006	increased cellular iron level [assayed_using] PomBase:SPACUNK4.16c	(Fig. 5A)
PMID:30393157	FYPO:0002006	increased cellular iron level [assayed_using] PomBase:SPAC328.03	(Fig. 5A)
PMID:30393157	FYPO:0002006	increased cellular iron level [assayed_using] PomBase:SPCC1223.03c	(Fig. 5A)
PMID:30393157	FYPO:0000375	abolished apoptotic process	(Figure 3D)
PMID:30393157	FYPO:0001673	normal nuclear morphology	(Figure 3D)
PMID:30393157	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPBC947.05c	Table2
PMID:30393157	FYPO:0006783	increased level of carbohydrate metabolism gene mRNA during vegetative growth [assayed_using] PomBase:SPBC660.07	Table2
PMID:30393157	FYPO:0006783	increased level of carbohydrate metabolism gene mRNA during vegetative growth [assayed_using] PomBase:SPACUNK4.16c	Table2
PMID:30393157	FYPO:0006783	increased level of carbohydrate metabolism gene mRNA during vegetative growth [assayed_using] PomBase:SPAC328.03	Table2
PMID:30393157	FYPO:0006783	increased level of carbohydrate metabolism gene mRNA during vegetative growth [assayed_using] PomBase:SPCC1223.03c	Table2
PMID:30393157	FYPO:0006783	increased level of carbohydrate metabolism gene mRNA during vegetative growth [assayed_using] PomBase:SPAC13F5.03c	Table2
PMID:30393157	FYPO:0006783	increased level of carbohydrate metabolism gene mRNA during vegetative growth [assayed_using] PomBase:SPAC977.16c	Table2
PMID:30393157	FYPO:0006783	increased level of carbohydrate metabolism gene mRNA during vegetative growth [assayed_using] PomBase:SPAC22A12.11	Table2
PMID:30393157	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPBC4F6.09	Table2
PMID:30393157	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPAC23G3.03	Table2
PMID:30393157	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1F7.08	Table2
PMID:30393157	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1F7.07c	Table2
PMID:30393157	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPAC8C9.11	Table2
PMID:30393157	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPBC1683.09c	Table2
PMID:30393157	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPBC3D6.03c	Table2
PMID:30393157	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPAC1F8.03c	Table2
PMID:30393157	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPCC61.01c	Table2
PMID:30393157	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth [assayed_using] PomBase:SPAC8C9.12c [assayed_using] PomBase:SPAC1F8.02c	Table2
PMID:3040264	GO:0007076	mitotic chromosome condensation	(Fig. 2B)
PMID:3040264	FYPO:0002071	mislocalized nucleus during vegetative growth	(Fig. 2a)
PMID:3040264	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	(Fig. 2a) (comment: CHECK no spindle rod like chromsomes)
PMID:3040264	FYPO:0001683	abolished mitotic spindle assembly	(Fig. 2a) (comment: CHECK no spindle rod like chromsomes)
PMID:3040264	FYPO:0002018	mitotic spindle absent from cell	(Fig. 2a) (comment: no spindle rod like chromsomes)
PMID:3040264	FYPO:0001683	abolished mitotic spindle assembly	(Fig. 2b)
PMID:3040264	FYPO:0003145	abnormal cell cycle arrest in mitotic prophase	(Fig. 2b) ((comment: CHECK uncondensed chromosomes)
PMID:3040264	FYPO:0000214	abnormal mitotic chromosome condensation [has_penetrance] 80	(Fig. 2b) (comment: CHECK uncondensed chromosomes)
PMID:3040264	FYPO:0001513	normal mitotic sister chromatid segregation [has_penetrance] 75	Table1
PMID:3040264	FYPO:0003757	incomplete mitotic sister chromatid segregation [has_penetrance] 24	Table1
PMID:3040264	FYPO:0004301	normal mitotic sister chromatid separation [has_penetrance] 54	Table1
PMID:30427751	GO:0005515	protein binding	(Fig. 5A) (comment:CHECK recruitment)
PMID:30427751	FYPO:0005558	abnormal microtubule bundle	(Figure 1)
PMID:30427751	FYPO:0000234	abnormal cytoplasmic interphase microtubule nucleation	(Figure 1G,H) (comment: from preexisting microtubules)
PMID:30427751	FYPO:0004090	abnormal protein localization to microtubule cytoskeleton [assayed_using] PomBase:SPCC417.07c	(Figure 2A) (comment:CHECK with increased localization to SPB)
PMID:30427751	FYPO:0004090	abnormal protein localization to microtubule cytoskeleton [assayed_using] PomBase:SPBC365.15	(Figure 2A) (comment:CHECK with increased localization to SPB)
PMID:30427751	FYPO:0004083	normal protein level [assayed_using] PomBase:SPBC365.15	(Figure 2B)
PMID:30427751	FYPO:0004083	normal protein level [assayed_using] PomBase:SPCC417.07c	(Figure 2B)
PMID:30427751	FYPO:0004083	normal protein level [assayed_using] PomBase:SPBC902.06	(Figure 2B)
PMID:30427751	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC11B10.05c [assayed_using] PomBase:SPCC417.07c	(Figure 5A)
PMID:30427751	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC11B10.05c [assayed_using] PomBase:SPCC417.07c	(Figure 5A)
PMID:30427751	FYPO:0004090	abnormal protein localization to microtubule cytoskeleton [assayed_using] PomBase:SPBC11B10.05c [assayed_using] PomBase:SPCC417.07c	(Figure 5G,H)
PMID:30427751	FYPO:0006182	decreased protein localization to interphase microtubule [assayed_using] PomBase:SPBC11B10.05c	(Figure 5I)
PMID:30427751	FYPO:0000935	abnormal protein localization to cortical microtubule cytoskeleton during vegetative growth [assayed_using] PomBase:SPCC417.07c	(Figure 6A,C)
PMID:30427751	FYPO:0005686	microtubule bundles present in decreased numbers during mitotic interphase	(Figure 6A,C)
PMID:30427751	FYPO:0004511	long curved interphase microtubules	(Figure 6D)
PMID:30427751	FYPO:0006182	decreased protein localization to interphase microtubule [assayed_using] PomBase:SPCC417.07c	Therefore, we concluded that Rsp1 is required to prevent excessive accumulation of Mto1
PMID:30427751	FYPO:0006182	decreased protein localization to interphase microtubule [assayed_using] PomBase:SPCC417.07c	Therefore, we concluded that Rsp1 is required to prevent excessive accumulation of Mto1
PMID:30451685	GO:0000329	fungal-type vacuole membrane	(Figure 1) (direct assay for vacuolar membrane) and Figure 1-Figure supplement 1 (sequence feature evidence for transmembrane)
PMID:30451685	GO:0007033	vacuole organization	(Figure 2)
PMID:30451685	GO:0007033	vacuole organization	(Figure 2; Figure S1)
PMID:30451685	FYPO:0003507	normal growth on zinc	(Figure 2D and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0003507	normal growth on zinc	(Figure 2D and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0006786	normal growth on manganese	(Figure 2D and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0006786	normal growth on manganese	(Figure 2D and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0006786	normal growth on manganese	(Figure 2D and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0003507	normal growth on zinc	(Figure 2D and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0000385	normal macroautophagy	(Figure 2—Figure supplement 1A)
PMID:30451685	FYPO:0004247	normal vacuolar morphology during vegetative growth	(Figure 2—Figure supplement 1D)
PMID:30451685	FYPO:0006785	normal growth on cobalt	(Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0006785	normal growth on cobalt	(Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0006785	normal growth on cobalt	(Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0004250	abolished protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 3—Figure supplement 1)
PMID:30451685	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 3—Figure supplement 1A)
PMID:30451685	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_using] PomBase:SPAC30D11.06c	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_using] PomBase:SPAC30D11.06c	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_using] PomBase:SPAC30D11.06c	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_using] PomBase:SPAC30D11.06c	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_using] PomBase:SPAC30D11.06c	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	FYPO:0004250	abolished protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	FYPO:0004250	abolished protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	FYPO:0004250	abolished protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	FYPO:0004250	abolished protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_using] PomBase:SPAC30D11.06c	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	FYPO:0004250	abolished protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 3—Figure supplement 1A, 2B)
PMID:30451685	FYPO:0004247	normal vacuolar morphology during vegetative growth	(Figure 3—Figure supplement 1B)
PMID:30451685	FYPO:0006784	tubular vacuole morphology during vegetative growth	(Figure 3—Figure supplement 1B, 2B)
PMID:30451685	FYPO:0006784	tubular vacuole morphology during vegetative growth	(Figure 3—Figure supplement 1B, 2B)
PMID:30451685	FYPO:0006784	tubular vacuole morphology during vegetative growth	(Figure 3—Figure supplement 1B, 2B)
PMID:30451685	FYPO:0006784	tubular vacuole morphology during vegetative growth	(Figure 3—Figure supplement 1B, 2B)
PMID:30451685	FYPO:0006784	tubular vacuole morphology during vegetative growth	(Figure 3—Figure supplement 1B, 2B)
PMID:30451685	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c	(Figure 3—Figure supplement 2)
PMID:30451685	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c	(Figure 3—Figure supplement 2)
PMID:30451685	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c	(Figure 3—Figure supplement 2)
PMID:30451685	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c	(Figure 3—Figure supplement 2)
PMID:30451685	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c	(Figure 3—Figure supplement 2)
PMID:30451685	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c [has_severity] medium	(Figure 4A)
PMID:30451685	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c [has_severity] high	(Figure 4A)
PMID:30451685	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c [has_severity] low	(Figure 4A)
PMID:30451685	FYPO:0006233	decreased protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 4B)
PMID:30451685	FYPO:0006233	decreased protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 4B)
PMID:30451685	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 4B)
PMID:30451685	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 4B)
PMID:30451685	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 4B)
PMID:30451685	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 4B)
PMID:30451685	FYPO:0004250	abolished protein localization to vacuolar membrane [assayed_using] PomBase:SPBP8B7.24c	(Figure 4B)
PMID:30451685	FYPO:0004247	normal vacuolar morphology during vegetative growth	(Figure 4C,D)
PMID:30451685	FYPO:0004247	normal vacuolar morphology during vegetative growth	(Figure 4C,D)
PMID:30451685	FYPO:0004247	normal vacuolar morphology during vegetative growth	(Figure 4C,D)
PMID:30451685	FYPO:0004247	normal vacuolar morphology during vegetative growth	(Figure 4C,D)
PMID:30451685	FYPO:0004247	normal vacuolar morphology during vegetative growth	(Figure 4C,D)
PMID:30451685	FYPO:0004247	normal vacuolar morphology during vegetative growth	(Figure 4C,D)
PMID:30451685	FYPO:0004247	normal vacuolar morphology during vegetative growth	(Figure 4C,D)
PMID:30451685	FYPO:0001245	sensitive to cobalt	(Figure 4E)
PMID:30451685	FYPO:0000116	sensitive to zinc	(Figure 4E)
PMID:30451685	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c [has_severity] medium	(Figure 4—Figure supplement 1B)
PMID:30451685	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c	(Figure 4—Figure supplement 1B)
PMID:30451685	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c [has_severity] medium	(Figure 4—Figure supplement 1B)
PMID:30451685	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c [has_severity] medium	(Figure 4—Figure supplement 1B)
PMID:30451685	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c [has_severity] medium	(Figure 4—Figure supplement 1B)
PMID:30451685	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBP8B7.24c [assayed_using] PomBase:SPAC30D11.06c [has_severity] low	(Figure 4—Figure supplement 1C)
PMID:30451685	FYPO:0006784	tubular vacuole morphology during vegetative growth [has_penetrance] 60	(Figures 2A and 2B)
PMID:30451685	FYPO:0006784	tubular vacuole morphology during vegetative growth [has_penetrance] 40	(Figures 2A and 2B)
PMID:30451685	FYPO:0006579	sensitive to manganese	(Figures 2C, 2D, and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0006579	sensitive to manganese	(Figures 2C, 2D, and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0000116	sensitive to zinc	(Figures 2C, 2D, and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0000116	sensitive to zinc	(Figures 2C, 2D, and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0001245	sensitive to cobalt	(Figures 2C, 2D, and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0001245	sensitive to cobalt	(Figures 2C, 2D, and Figure 2—Figure supplement 2)
PMID:30451685	FYPO:0006579	sensitive to manganese	(Figures 2C, 2D, and Figure 2—Figure supplement 2) (comment: same as either single mutant)
PMID:30451685	FYPO:0001245	sensitive to cobalt	(Figures 2C, 2D, and Figure 2—Figure supplement 2) (comment: same as either single mutant)
PMID:30451685	FYPO:0000116	sensitive to zinc	(Figures 2C, 2D, and Figure 2—Figure supplement 2) (comment: same as either single mutant)
PMID:30451685	FYPO:0006784	tubular vacuole morphology during vegetative growth	(Figures 4C and 4D)
PMID:30451685	GO:0000329	fungal-type vacuole membrane	when SpHfl1 was overexpressed from a strong nmt1 promoter, the cytosolic signal of mYFP-SpAtg8 disappeared and the vacuole membrane localization of mYFP-SpAtg8 became much more conspicuous (Figure 1F).
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 2C S3A,C)
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 2C S3A,C)
PMID:30462301	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 2C S3A,C)
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 2C,D S3A,C)
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 2C,D S3A,C)
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 2D S3B,C)
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 2D S3B,C)
PMID:30462301	FYPO:0004886	abolished protein localization to nuclear envelope during vegetative growth [assayed_using] PomBase:SPBC1778.02	(Figure 2E and Supplementary Figure S4B)
PMID:30462301	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores	(Figure 3)
PMID:30462301	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores	(Figure 3)
PMID:30462301	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores	(Figure 3)
PMID:30462301	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores	(Figure 3)
PMID:30462301	FYPO:0004791	increased telomere-nuclear envelope distance during mitotic G2 phase	(Figure 3A)
PMID:30462301	FYPO:0004791	increased telomere-nuclear envelope distance during mitotic G2 phase	(Figure 3A)
PMID:30462301	FYPO:0004791	increased telomere-nuclear envelope distance during mitotic G2 phase	(Figure 3A)
PMID:30462301	FYPO:0004791	increased telomere-nuclear envelope distance during mitotic G2 phase	(Figure 3A)
PMID:30462301	FYPO:0006366	abolished meiotic telomere clustering	(Figure 3B and Supplementary Figure S6)
PMID:30462301	FYPO:0000172	abnormal meiotic telomere clustering	(Figure 3B and Supplementary Figure S6)
PMID:30462301	FYPO:0006366	abolished meiotic telomere clustering	(Figure 3B and Supplementary Figure S6)
PMID:30462301	FYPO:0000172	abnormal meiotic telomere clustering	(Figure 3B and Supplementary Figure S6)
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPAC18G6.10	(Figure 4A)
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPAC18G6.10	(Figure 4A)
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPAC18G6.10	(Figure 4A)
PMID:30462301	FYPO:0004083	normal protein level [assayed_using] PomBase:SPAC18G6.10	(Figure 4A)
PMID:30462301	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC12D12.01	(Figure 4F and Supplementary Figure S7F)
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02 [has_severity] medium	(Figure 6B and Supplementary Figure S8B)
PMID:30462301	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 6B and Supplementary Figure S8B)
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02 [has_severity] medium	(Figure 6B and Supplementary Figure S8B)
PMID:30462301	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 6B and Supplementary Figure S8B)
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02 [has_severity] medium	(Figure 6B and Supplementary Figure S8B)
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 6B and Supplementary Figure S8C)
PMID:30462301	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 6B and Supplementary Figure S8C))
PMID:30462301	FYPO:0005612	normal protein localization to nuclear envelope [assayed_using] PomBase:SPBC19C7.10	(Figure S4A)
PMID:30462301	FYPO:0005612	normal protein localization to nuclear envelope [assayed_using] PomBase:SPBC19C7.10	(Figure S4A)
PMID:30462301	FYPO:0004886	abolished protein localization to nuclear envelope during vegetative growth [assayed_using] PomBase:SPBC1778.02	(Supplementary Figure S4A)
PMID:30462301	FYPO:0006515	normal telomere length	(Supplementary Figure S5B)
PMID:30462301	FYPO:0006515	normal telomere length	(Supplementary Figure S5B)
PMID:30462301	FYPO:0006515	normal telomere length	(Supplementary Figure S5B)
PMID:30462301	FYPO:0006515	normal telomere length	(Supplementary Figure S5B)
PMID:30462301	FYPO:0006515	normal telomere length	(Supplementary Figure S5B)
PMID:30462301	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPAC18G6.10	(Supplementary Figure S7A-D)
PMID:30462301	GO:0005515	protein binding	(comment: competatively with lem2)
PMID:30462301	GO:0005515	protein binding	(comment: competatively with sad1)
PMID:30462301	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC1778.02 [assayed_using] PomBase:SPBC19C7.10	(comment: suggested by Junko)
PMID:30462301	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	Supplementary Figure S1A-E
PMID:30462301	FYPO:0005612	normal protein localization to nuclear envelope [assayed_using] PomBase:SPBC19C7.10	Supplementary Figure S4A)
PMID:30462301	FYPO:0004083	normal protein level [assayed_using] PomBase:SPAC18G6.10	Supplementary Figure S7E
PMID:30462301	FYPO:0004083	normal protein level [assayed_using] PomBase:SPAC18G6.10	Supplementary Figure S7E
PMID:30462301	FYPO:0004083	normal protein level [assayed_using] PomBase:SPAC18G6.10	Supplementary Figure S7E
PMID:30463883	FYPO:0006885	decreased protein level at mitotic spindle [assayed_using] PomBase:SPAC664.10	(Figure 2A,B)
PMID:30463883	FYPO:0006885	decreased protein level at mitotic spindle [assayed_using] PomBase:SPAC664.10	(Figure 2A,B)
PMID:30463883	FYPO:0006886	increased protein level at mitotic spindle [assayed_using] PomBase:SPAC664.10	(Figure 2A,B)
PMID:30463883	FYPO:0006885	decreased protein level at mitotic spindle [assayed_using] PomBase:SPAC664.10	(Figure 2A,B)
PMID:30463883	FYPO:0006885	decreased protein level at mitotic spindle [assayed_using] PomBase:SPAC664.10	(Figure 2A,B)
PMID:30463883	FYPO:0002061	inviable vegetative cell population	(Figure 4A)
PMID:30463883	FYPO:0002060	viable vegetative cell population	(comment: CONDITION at 33 degrees Celsius)
PMID:30463883	FYPO:0002060	viable vegetative cell population	(comment: CONDITION at 33 degrees Celsius)
PMID:30463883	FYPO:0002060	viable vegetative cell population	(comment: CONDITION at 33 degrees Celsius)
PMID:30463883	FYPO:0002060	viable vegetative cell population	(comment: CONDITION at 33 degrees Celsius)
PMID:30463883	FYPO:0002060	viable vegetative cell population	(comment: CONDITION at 36 degrees Celsius)
PMID:30463883	FYPO:0002060	viable vegetative cell population	(comment: CONDITION at 36 degrees Celsius)
PMID:30463883	FYPO:0002060	viable vegetative cell population	(comment: CONDITION at 36 degrees Celsius)
PMID:30463883	FYPO:0002060	viable vegetative cell population	(comment: CONDITION at 36 degrees Celsius)
PMID:30463883	FYPO:0002060	viable vegetative cell population	(comment: CONDITION at 36 degrees Celsius)
PMID:30463883	FYPO:0002060	viable vegetative cell population	(comment: at 36 degrees Celsius)
PMID:30463883	FYPO:0006884	thick mitotic spindle during mitotic metaphase	The mitotic spindle has two poles but is thicker than normal.
PMID:30463883	FYPO:0006884	thick mitotic spindle during mitotic metaphase	The mitotic spindle has two poles but is thicker than normal.
PMID:30471998	GO:0034314	Arp2/3 complex-mediated actin nucleation	Dip1 activates Arp2/3 complex to nucleate linear actin filaments analogous to branched actin filaments created by Wsp1-mediated Arp2/3 complex activation. These Dip1-Arp2/3 complex nucleated filaments act as seeds for Wsp1-mediated Arp2/3 complex branching nucleation.
PMID:30475921	FYPO:0006790	meiotic drive suppression	(comment: suppresses wtf13 drive)
PMID:30475921	FYPO:0002151	inviable spore [has_penetrance] high	(comment: when wtf13 antidote not present) (comment: homozygous, wtf13poison/wtf13+, or wtf13poison/wtf13Δ)
PMID:30475921	FYPO:0006793	altered meiotic drive suppression specificity	(comment: wtf13 driver, wtf18 suppressor)
PMID:30475921	FYPO:0006793	altered meiotic drive suppression specificity	(comment: wtf13 driver, wtf18 suppressor)
PMID:30475921	FYPO:0006793	altered meiotic drive suppression specificity	(comment: wtf13 driver, wtf18 suppressor)
PMID:30475921	FYPO:0006793	altered meiotic drive suppression specificity	(comment: wtf13 driver, wtf18 suppressor)
PMID:30475921	GO:0005737	cytoplasm [part_of] ascospore	(comment: wtf18-2 allele assayed)
PMID:30503780	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC1778.02 [assayed_using] PomBase:SPBC19C7.10	((comment: transeferred from Junkos session PMID:30462301)
PMID:30503780	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC1778.02 [assayed_using] PomBase:SPBC19C7.10	((comment: transeferred from Junkos session PMID:30462301)
PMID:30503780	FYPO:0000590	normal sporulation	((comment: transeferred from Junkos session PMID:30462301)
PMID:30503780	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Fig. 2D)
PMID:30503780	FYPO:0000658	decreased DNA binding	(Fig. 4)
PMID:30503780	FYPO:0000658	decreased DNA binding	(Fig. 4)
PMID:30503780	FYPO:0002687	normal telomere length during vegetative growth	(Fig. S5B)
PMID:30503780	FYPO:0005612	normal protein localization to nuclear envelope	(Fig. S5B)
PMID:30503780	FYPO:0005612	normal protein localization to nuclear envelope	(Fig. S5B)
PMID:30503780	FYPO:0004093	normal meiotic telomere clustering	(Fig. S5B)
PMID:30503780	FYPO:0004093	normal meiotic telomere clustering	(Fig. S5B)
PMID:30503780	FYPO:0002687	normal telomere length during vegetative growth	(Fig. S5B)
PMID:30503780	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 2D)
PMID:30503780	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 2D)
PMID:30503780	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC19C7.10 [assayed_using] PomBase:SPBC1778.02	(Figure 2D)
PMID:30503780	GO:0003677	DNA binding	(Figure 3) (comment: incompatible with rap1 binding)
PMID:30503780	FYPO:0004791	increased telomere-nuclear envelope distance during mitotic G2 phase	(Figures 5A and 5B)
PMID:30503780	FYPO:0004791	increased telomere-nuclear envelope distance during mitotic G2 phase	(Figures 5A and 5B)
PMID:30503780	FYPO:0004791	increased telomere-nuclear envelope distance during mitotic G2 phase	(Figures 5A and 5B)
PMID:30503780	FYPO:0004791	increased telomere-nuclear envelope distance during mitotic G2 phase [has_penetrance] 60	(Figures 5C)
PMID:30503780	FYPO:0004791	increased telomere-nuclear envelope distance during mitotic G2 phase [has_penetrance] 50	(Figures 5C)
PMID:30503780	GO:0005515	protein binding	(comment: incompatible with DNA binding)
PMID:30503780	FYPO:0000590	normal sporulation	(comment: transeferred from Junkos session PMID:30462301)
PMID:30528393	GO:0005829	cytosol	(comment: although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA)
PMID:30528393	GO:0005829	cytosol	(comment: although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA)
PMID:30528393	GO:0005739	mitochondrion	(comment: although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA)
PMID:30528393	GO:0005739	mitochondrion	(comment: although this was not assayed it can be deduced from the requirement of both cca1 andd 2 to add CCA)
PMID:30530492	FYPO:0000464	decreased intracellular transport	(comment: CHECK glycosphingolipid transport)
PMID:30530492	GO:0140351	glycosylceramide flippase activity	(comment: glucosylceramide, galactosylceramide)
PMID:30573453	FYPO:0003575	normal histone H3-K9 acetylation at centromere outer repeat during vegetative growth	(Fig. 5)
PMID:30573453	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. 6)
PMID:30573453	FYPO:0002360	normal chromatin silencing at centromere [has_severity] low	(Fig. 6)
PMID:30573453	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Figure 2c)
PMID:30573453	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Figure 2c)
PMID:30573453	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Figure 2c)
PMID:30573453	FYPO:0004237	increased protein localization to heterochromatin at centromere outer repeat region [assayed_using] PomBase:SPCC622.16c	(Figure 2c)
PMID:30573453	FYPO:0000833	normal protein level during vegetative growth	(Figure 2d)
PMID:30573453	FYPO:0000703	normal protein-protein interaction	(Figure 2d)
PMID:30573453	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 3a)
PMID:30573453	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 3a)
PMID:30573453	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Figure 3a)
PMID:30573453	FYPO:0003009	increased protein localization to centromere outer repeat [assayed_using] PomBase:SPAC1952.05	(Figure 4C)
PMID:30573453	FYPO:0002389	normal protein localization to heterochromatin at centromere outer repeat [assayed_using] PomBase:SPAC1952.05	(Figure 4c)
PMID:30573453	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Figure 4d)
PMID:30573453	FYPO:0003575	normal histone H3-K9 acetylation at centromere outer repeat during vegetative growth	(Figure 5)
PMID:30573453	FYPO:0000966	increased histone H3-K14 acetylation at centromere outer repeat during vegetative growth	(Figure 5)
PMID:30573453	FYPO:0006814	increased histone H3-K9 acetylation at centromere outer repeat during vegetative growth	(Figure 5)
PMID:30573453	FYPO:0003574	normal histone H3-K14 acetylation at centromere outer repeat during vegetative growth	(Figure 5)
PMID:30573453	FYPO:0000967	decreased histone H3-K14 acetylation at centromere outer repeat during vegetative growth [has_severity] low	(Figure 5)
PMID:30573453	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Figure 6)
PMID:30573453	FYPO:0002842	decreased protein localization to centromere outer repeat [assayed_using] PomBase:SPAC1952.05	(Figure 6)
PMID:30573453	FYPO:0002842	decreased protein localization to centromere outer repeat [assayed_using] PomBase:SPBC25H2.11c	(Figure 6)
PMID:30573453	FYPO:0003411	decreased chromatin silencing at centromere inner repeat	(Figure 6)
PMID:30573453	FYPO:0000966	increased histone H3-K14 acetylation at centromere outer repeat during vegetative growth	(Figure 6)
PMID:30573453	FYPO:0006814	increased histone H3-K9 acetylation at centromere outer repeat during vegetative growth	(Figure 6)
PMID:30573453	FYPO:0000967	decreased histone H3-K14 acetylation at centromere outer repeat during vegetative growth	(Figure 6)
PMID:30573453	FYPO:0006814	increased histone H3-K9 acetylation at centromere outer repeat during vegetative growth	(Figure 6)
PMID:30573453	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	(Figure S4)
PMID:30573453	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	(Figure S7)
PMID:30573453	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] medium	(Figure S7)
PMID:30573453	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] high	(Figure S7)
PMID:30573453	FYPO:0006814	increased histone H3-K9 acetylation at centromere outer repeat during vegetative growth [has_severity] low	(Figure S8)
PMID:30573453	FYPO:0000966	increased histone H3-K14 acetylation at centromere outer repeat during vegetative growth [has_severity] low	(Figure S8)
PMID:30573453	FYPO:0000966	increased histone H3-K14 acetylation at centromere outer repeat during vegetative growth [has_severity] high	(Figure S8)
PMID:30573453	FYPO:0006814	increased histone H3-K9 acetylation at centromere outer repeat during vegetative growth [has_severity] high	(Figure S8)
PMID:30601114	GO:1905762	CCR4-NOT complex binding	(Figure 1; Figure supplement 1A)
PMID:30601114	GO:1905762	CCR4-NOT complex binding	(Figure 1; Figure supplement 1A)
PMID:30601114	GO:0035925	mRNA 3'-UTR AU-rich region binding [has_input] AU_rich_element [part_of] negative regulation of nuclear-transcribed mRNA poly(A) tail shortening	(Figure 1; Figure supplement 1B,1C)
PMID:30601114	GO:0004535	poly(A)-specific ribonuclease activity [part_of] nuclear-transcribed mRNA poly(A) tail shortening	(Figure 1A and Figure 1-Figure supplement 1D- E)
PMID:30601114	GO:0004535	poly(A)-specific ribonuclease activity [part_of] nuclear-transcribed mRNA poly(A) tail shortening	(Figure 1A and Figure 1-Figure supplement 1D- E)
PMID:30601114	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening [has_penetrance] high	(Figure 2)
PMID:30601114	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening	(Figure 2A and Figure 2-Figure supplement 1B-E)
PMID:30601114	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening	(Figure 2A and Figure 2-Figure supplement 1B-E)
PMID:30601114	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening [has_penetrance] high	(Figure 2B)
PMID:30601114	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening	(Figure 2B)
PMID:30601114	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening [has_penetrance] low	(Figure 2B)
PMID:30601114	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening [has_penetrance] low	(Figure 2B)
PMID:30601114	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening	(Figure 2B)
PMID:30601114	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening	(Figure 2B)
PMID:30601114	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening [has_penetrance] high	(Figure 2B)
PMID:30601114	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening [has_penetrance] high	(Figure 2B)
PMID:30601114	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening [has_penetrance] high	(Figure 2B)
PMID:30601114	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening	(Figure 2B)
PMID:30601114	GO:0062104	pumilio-response element binding	(comment: PRE element) Figure 1-Figure supplement 1B/Figure 1-Figure supplement 1C
PMID:30601114	GO:0044692	exoribonuclease activator activity [part_of] nuclear-transcribed mRNA poly(A) tail shortening	(comment: increases processivity)
PMID:30601114	FYPO:0002134	decreased protein-RNA interaction	ADD DOMAIN WHEN SO TERM AVAILABLE Figure 2A and Figure 2-Figure supplement 1B-E
PMID:30602572	FYPO:0003820	mitochondria present in decreased numbers during vegetative growth	(Fig. 1C) observed that Klp5Δ/Klp6Δ contained only 2.3 + 0.4 (mean + S.E.).
PMID:30602572	FYPO:0000895	mitochondrial aggregation	(Fig. S5B) Furthermore, in Klp4Δ cells, which typically contain several short mitochondria (Fig. 1A), absence of Dnm1 results in a single large, fused mitochondrion
PMID:30602572	FYPO:0006103	short interphase microtubules [has_severity] high [has_penetrance] high	(Figure 1B) the anti-parallel microtubule bundles are only about half the length of wild-type bundles
PMID:30602572	FYPO:0003810	small fragmented mitochondria present in increased numbers [has_penetrance] high [has_severity] high	(Figure 1C, 1D)
PMID:30602572	FYPO:0007197	increased mitochondrial fission [has_penetrance] high [has_severity] high	(Figure 2C) the mitochondria have a fission frequency that is almost double that of wild-type
PMID:30602572	FYPO:0007208	normal microtubule bundle length during mitotic interphase [has_penetrance] high	(Figure 6B)
PMID:30602572	FYPO:0003810	small fragmented mitochondria present in increased numbers [has_penetrance] high [has_severity] high	(Figure 6C, 6D) Increased mitochondrial numbers and decreased mitochondrial sizes with overall mitochondrial volume same as what is observed in wild-type cells
PMID:30602572	FYPO:0007196	decreased mitochondrial fission	Klp5Δ/Klp6Δ cells exhibited a fission frequency that was half that of WT
PMID:30602572	FYPO:0003810	small fragmented mitochondria present in increased numbers	WT cells highly overexpressing Dnm1 had 11.6 + 0.2 mitochondria (mean + S.E.), which is twice that of WT cells
PMID:30602572	FYPO:0003810	small fragmented mitochondria present in increased numbers [has_penetrance] high	We counted 23.3 + 1.4 (mean + S.E.) mitochondria in Klp5Δ/Klp6Δ cells lacking Mmb1Δ (Fig. 6C), which was not significantly different from Mmb1Δ cells
PMID:30626735	FYPO:0000267	sensitive to ionizing radiation during vegetative growth [has_severity] medium	(comment: CHECK 200 Gy; Andres SN et al. (2019))
PMID:30626735	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(comment: CHECK 75 J/m^2; Andres SN et al. (2019))
PMID:30626735	FYPO:0002344	sensitive to phleomycin [has_severity] medium	(comment: CHECK Andres SN et al. (2019))
PMID:30635289	PomGeneEx:0000011	RNA level increased [during] mitotic S phase	Accordingly, the peak of septation matches with the peak of expression of the histone H3 (hht1 gene) as histones are highly expressed during S phase (Figure 1A).
PMID:30635289	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_in] MCB	ChIP analysis showed that Nrm1, Yox1, and Res2 bind to the cnp1 promoter (Figure 4B).
PMID:30635289	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_in] MCB	ChIP analysis showed that Nrm1, Yox1, and Res2 bind to the cnp1 promoter (Figure 4B).
PMID:30635289	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_in] MCB	ChIP analysis showed that Nrm1, Yox1, and Res2 bind to the cnp1 promoter (Figure 4B).
PMID:30635289	PomGeneEx:0000018	protein level increased	Cnp1-GFP protein increases approximately twofold at 165-min postelutriation. This resulindicates that the mRNA increase in G1 results in augmentation of the Cnp1 protein level in S phase.
PMID:30635289	PomGeneEx:0000011	RNA level increased [during] mitotic G1 phase	Consistent with the previous report (Takahashi et al. 2000), cnp1 mRNA peaks before the transcription of histone H3, $120 min after elutriation, showing an approximately twofold increase. This pattern of expression coincides with the expression of cdc18, a well-known cell cycle-regulated gene expressed specifically in G1 phase (Figure 1A).
PMID:30635289	PomGeneEx:0000011	RNA level increased [during] mitotic G1 phase	Consistent with the previous report (Takahashi et al. 2000), cnp1 mRNA peaks before the transcription of histone H3, $120 min after elutriation, showing an approximately twofold increase. This pattern of expression coincides with the expression of cdc18, a well-known cell cycle-regulated gene expressed specifically in G1 phase (Figure 1A).
PMID:30635289	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1105.17	Deletion of nrm1 or yox1 resulted in a $5-6-fold increase in cnp1 mRNA levels, whereas res2 deletion led to a more modest twofold increase (Figure 3A).
PMID:30635289	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1105.17	Deletion of nrm1 or yox1 resulted in a $5-6-fold increase in cnp1 mRNA levels, whereas res2 deletion led to a more modest twofold increase (Figure 3A).
PMID:30635289	FYPO:0002843	protein mislocalized to nucleoplasm [assayed_protein] PomBase:SPBC1105.17	Through the visual screen, we identified that three mutants, nrm1D, yox1D, and res2D, showed abnormal CENP-A distribution patterns (Figure 2A). In these mutants, Cnp1-GFP at centromeres tends to be brighter and also gives a high nucleoplasmic signal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
PMID:30635289	FYPO:0005026	increased protein localization to chromatin at chromosome arms [assayed_protein] PomBase:SPBC1105.17	Through the visual screen, we identified that three mutants, nrm1D, yox1D, and res2D, showed abnormal CENP-A distribution patterns (Figure 2A). In these mutants, Cnp1-GFP at centromeres tends to be brighter and also gives a high nucleoplasmic signal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
PMID:30635289	FYPO:0002843	protein mislocalized to nucleoplasm [assayed_protein] PomBase:SPBC1105.17	Through the visual screen, we identified that three mutants, nrm1D, yox1D, and res2D, showed abnormal CENP-A distribution patterns (Figure 2A). In these mutants, Cnp1-GFP at centromeres tends to be brighter and also gives a high nucleoplasmic signal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
PMID:30635289	FYPO:0002843	protein mislocalized to nucleoplasm [assayed_protein] PomBase:SPBC1105.17	Through the visual screen, we identified that three mutants, nrm1D, yox1D, and res2D, showed abnormal CENP-A distribution patterns (Figure 2A). In these mutants, Cnp1-GFP at centromeres tends to be brighter and also gives a high nucleoplasmic signal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
PMID:30635289	FYPO:0005026	increased protein localization to chromatin at chromosome arms [assayed_protein] PomBase:SPBC1105.17	Through the visual screen, we identified that three mutants, nrm1D, yox1D, and res2D, showed abnormal CENP-A distribution patterns (Figure 2A). In these mutants, Cnp1-GFP at centromeres tends to be brighter and also gives a high nucleoplasmic signal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
PMID:30635289	FYPO:0005026	increased protein localization to chromatin at chromosome arms [assayed_protein] PomBase:SPBC1105.17	Through the visual screen, we identified that three mutants, nrm1D, yox1D, and res2D, showed abnormal CENP-A distribution patterns (Figure 2A). In these mutants, Cnp1-GFP at centromeres tends to be brighter and also gives a high nucleoplasmic signal (Figure 2A), suggesting an increase in Cnp1-GFP levels.
PMID:30635289	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 2	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 6	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 5	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	FYPO:0003970	incomplete mitotic sister chromatid segregation, with chromatin bridge [has_penetrance] 13	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 24	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	FYPO:0003970	incomplete mitotic sister chromatid segregation, with chromatin bridge [has_penetrance] 20	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	FYPO:0003970	incomplete mitotic sister chromatid segregation, with chromatin bridge [has_penetrance] 3	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 3	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] ~6	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635289	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] 24	Using DAPI staining, we observed that the MBF repressor mutant cells displayed lagging chromosomes, chromosome bridges, and also unequal nuclei segregation during mitosis (Figure 2C and Figure S4).
PMID:30635402	FYPO:0000228	lagging mitotic chromosomes	(comment: ICRF-193, a bisdioxopiperazine derivative [meso-4,4-(2,3-butanediyl)-bis (2,6-piperazinedione)], is a catalytic topo II inhibitor)
PMID:30635402	FYPO:0005739	complete but unequal mitotic sister chromatid segregation with unseparated chromosomes	(comment: This phenotype is observed in the presence of ICRF-193, a bisdioxopiperazine derivative [meso-4,4-(2,3-butanediyl)-bis (2,6-piperazinedione)], a catalytic topo II inhibitor.)
PMID:30635402	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC1A4.03c	(comment: also assayed directly using human CKII)
PMID:30635402	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC23C11.11 [present_during] mitotic cell cycle	These phosphorylation sites were identified by the phos-tag analysis, phospho-specific antibodies, and in vitro phosphorylation assay
PMID:30639107	FYPO:0006616	viable vegetative cell with increased cell diameter	(Fig. 1B)
PMID:30639107	FYPO:0001877	viable thin vegetative cell	(Fig. 1B)
PMID:30639107	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Fig. 1C)
PMID:30639107	FYPO:0008308	increased cell volume at division [has_severity] low	(Fig. 1C)
PMID:30639107	FYPO:0001879	thin cell [has_severity] medium	(Fig. 1C)
PMID:30639107	FYPO:0004085	decreased vegetative cell growth [has_severity] medium	(Fig. 1C)
PMID:30639107	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	(Fig. 1E)
PMID:30639107	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high	(Fig. 1E)
PMID:30639107	FYPO:0004085	decreased vegetative cell growth [has_severity] low	(Fig. 1E)
PMID:30639107	FYPO:0008308	increased cell volume at division [has_severity] high	(Fig. 1E)
PMID:30639107	FYPO:0008308	increased cell volume at division [has_severity] high	(Fig. 1E)
PMID:30639107	FYPO:0008308	increased cell volume at division [has_severity] high	(Fig. 1E)
PMID:30639107	FYPO:0008308	increased cell volume at division [has_severity] high	(Fig. 1E)
PMID:30639107	FYPO:0008309	increased cell surface area at division [has_severity] medium	(Fig. 1E)
PMID:30639107	FYPO:0008309	increased cell surface area at division [has_severity] high	(Fig. 1E)
PMID:30639107	FYPO:0008309	increased cell surface area at division [has_severity] low	(Fig. 1E)
PMID:30639107	FYPO:0001392	abnormal regulation of cell growth	(Fig. 3)
PMID:30640914	FYPO:0004610	increased duration of meiotic prophase I	(Fig. 8)
PMID:30640914	FYPO:0004610	increased duration of meiotic prophase I	(Fig. 8)
PMID:30640914	FYPO:0005650	normal onset of premeiotic DNA replication	(Fig. S4)
PMID:30640914	FYPO:0004993	normal spore germination frequency	(Figure S1)
PMID:30640914	FYPO:0000581	decreased spore germination frequency	(Figure S1A)
PMID:30640914	FYPO:0004993	normal spore germination frequency	(Figure S1A)
PMID:30640914	FYPO:0004993	normal spore germination frequency	(Figure S1A)
PMID:30640914	FYPO:0004993	normal spore germination frequency	(Figure S1A)
PMID:30640914	FYPO:0005650	normal onset of premeiotic DNA replication	(Figure S2)
PMID:30640914	FYPO:0006841	increased duration of meiotic S phase	(Figure S2)
PMID:30640914	FYPO:0004628	delayed onset of premeiotic DNA replication	(Figure S2)
PMID:30640914	FYPO:0004628	delayed onset of premeiotic DNA replication	(Figure S2)
PMID:30640914	FYPO:0005650	normal onset of premeiotic DNA replication	(Figure S4)
PMID:30640914	FYPO:0001370	abnormal protein localization [assayed_using] PomBase:SPAC17A5.18c	(comment: Cellular fractionation; affecting Rec25)
PMID:30640914	FYPO:0001370	abnormal protein localization [assayed_using] PomBase:SPAC17A5.18c	(comment: Cellular fractionation; affecting Rec25)
PMID:30640914	FYPO:0001370	abnormal protein localization [assayed_using] PomBase:SPAC17A5.18c	(comment: Cellular fractionation; affecting Rec25)
PMID:30640914	FYPO:0006838	abnormal linear element maturation	(comment: Rec25 visualization)
PMID:30640914	FYPO:0006838	abnormal linear element maturation	(comment: Rec25 visualization)
PMID:30640914	FYPO:0006838	abnormal linear element maturation	(comment: Rec25 visualization)
PMID:30640914	FYPO:0003891	normal intragenic meiotic recombination [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] low [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] low [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003891	normal intragenic meiotic recombination [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] low [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] low [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003891	normal intragenic meiotic recombination [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003891	normal intragenic meiotic recombination [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] medium [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] medium [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] medium [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] medium [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] medium [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003891	normal intragenic meiotic recombination [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0003891	normal intragenic meiotic recombination [assayed_using] PomBase:SPCC1322.13	(comment: Recombination assay; assayed region: ade6 gene)
PMID:30640914	FYPO:0005578	normal intergenic meiotic recombination [assayed_using] PomBase:SPBC1A4.02c [assayed_using] PomBase:SPBC21H7.07c	(comment: Recombination assay; assayed region: leu1-his5 interval)
PMID:30640914	FYPO:0002484	increased intergenic meiotic recombination [assayed_using] PomBase:SPBC1A4.02c [assayed_using] PomBase:SPBC21H7.07c	(comment: Recombination assay; assayed region: leu1-his5 interval)
PMID:30640914	FYPO:0002485	decreased intergenic meiotic recombination [has_severity] medium [assayed_using] PomBase:SPBC1A4.02c [assayed_using] PomBase:SPBC21H7.07c	(comment: Recombination assay; assayed region: leu1-his5 interval)
PMID:30640914	FYPO:0002485	decreased intergenic meiotic recombination [has_severity] medium [assayed_using] PomBase:SPBC1A4.02c [assayed_using] PomBase:SPBC21H7.07c	(comment: Recombination assay; assayed region: leu1-his5 interval)
PMID:30640914	FYPO:0003615	decreased meiotic DNA double-strand break formation [has_severity] high	(comment: mbs1 hotspot quantification
PMID:30640914	FYPO:0003615	decreased meiotic DNA double-strand break formation [has_severity] high	(comment: mbs1 hotspot quantification)
PMID:30640914	FYPO:0003615	decreased meiotic DNA double-strand break formation [has_severity] low	(comment: mbs1 hotspot quantification)
PMID:30640914	FYPO:0003615	decreased meiotic DNA double-strand break formation [has_severity] medium	(comment: mbs1 hotspot quantification)
PMID:30640914	FYPO:0003615	decreased meiotic DNA double-strand break formation [has_severity] low	(comment: mbs1 hotspot quantification)
PMID:30640914	FYPO:0003615	decreased meiotic DNA double-strand break formation [has_severity] high	(comment: mbs1 hotspot quantification)
PMID:30640914	FYPO:0003615	decreased meiotic DNA double-strand break formation [has_severity] low	(comment: mbs1 hotspot quantification)
PMID:30646830	FYPO:0001766	abnormal tRNA methylation [has_severity] high	Abolished tRNA cytosine-5 methylation of C49 and C50 (comment: tRNA bisulphite sequencing)
PMID:30646830	FYPO:0001766	abnormal tRNA methylation [has_severity] high	abolished tRNA C34, C48 methylation (comment: trna bisulphite sequencing)
PMID:30646830	GO:0016428	tRNA (cytidine-N5)-methyltransferase activity	trm401 (Trm4a) methylates C34 of tRNA-Leu (CAA) and tRNA-Pro (CGG) as well as all C48 tRNA methylation sites. Methylates C34 only on intron-containing tRNA.
PMID:30646830	GO:0016428	tRNA (cytidine-N5)-methyltransferase activity	trm402 (Trm4b) methylates C49 and C50 of tRNAs
PMID:30649994	FYPO:0006895	decreased protein localization to cell tip during meiosis [assayed_using] PomBase:SPBC216.02	(Fig. 3E)
PMID:30649994	FYPO:0006895	decreased protein localization to cell tip during meiosis [assayed_using] PomBase:SPBC216.02	(Fig. 3E)
PMID:30649994	FYPO:0006896	decreased mitochondrion localization to cell tip during meiosis	(Fig. 3E)
PMID:30649994	FYPO:0006896	decreased mitochondrion localization to cell tip during meiosis	(Fig. 3E)
PMID:30649994	GO:0005938	cell cortex [exists_during] meiotic prophase I	(Fig. 4b)
PMID:30649994	FYPO:0003790	normal protein localization during meiosis [assayed_using] PomBase:SPBC216.02	(Fig. S3)
PMID:30649994	GO:1901612	cardiolipin binding	Supplemental Figure S2
PMID:30649994	GO:0070300	phosphatidic acid binding	Supplemental Figure S2
PMID:30652128	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001840	increased minichromosome loss during vegetative growth [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006810	decreased gross chromosomal rearrangement	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001840	increased minichromosome loss during vegetative growth [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001840	increased minichromosome loss during vegetative growth [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001840	increased minichromosome loss during vegetative growth [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001840	increased minichromosome loss during vegetative growth [has_severity] medium	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001840	increased minichromosome loss during vegetative growth [has_severity] high	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001840	increased minichromosome loss during vegetative growth [has_severity] low	(comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001742	increased isochromosome formation	(comment: Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001742	increased isochromosome formation	(comment: Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001742	increased isochromosome formation	(comment: Pulse-field gel electrophoresis (PFGE), Polymerase chain reaction (PCR), Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0001740	increased gross chromosomal rearrangement	rpd1-S7A increased the rate of gross chromosomal rearrangement in the otherwise wild-type background. (comment: Monitoring an extra-chromosome ChL)
PMID:30652128	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] medium	rpd1-S7A reduced centromere noncoding RNA in the clr4∆ strain. (comment: Northern blot assay)
PMID:30652128	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] medium	tfs1∆ reduced centromere noncoding RNA in the clr4∆ strain. (comment: Northern blot assay)
PMID:30658998	FYPO:0006911	normal growth on hexestrol	(Fig. 1B)
PMID:30658998	FYPO:0006914	normal growth on terconazole	(Fig. 1B)
PMID:30658998	FYPO:0006913	normal growth on ketoconazole	(Fig. 1B)
PMID:30658998	FYPO:0006910	normal growth on vanoxerine	(Fig. 1B)
PMID:30658998	FYPO:0002061	inviable vegetative cell population	(Fig. 1B)
PMID:30658998	FYPO:0001355	decreased vegetative cell population growth	(Fig. 1B)
PMID:30658998	FYPO:0003810	small fragmented mitochondria present in increased numbers	(Fig. 1C)
PMID:30658998	FYPO:0003810	small fragmented mitochondria present in increased numbers	(Fig. 1C) (comment: supressed by hexestrol)
PMID:30658998	FYPO:0003769	decreased cellular mtDNA level	(Fig. 1D)
PMID:30658998	FYPO:0003769	decreased cellular mtDNA level	(Fig. 1D) (comment: supressed by hexestrol or clomifene)
PMID:30658998	FYPO:0006034	normal mitochondrion	(comment: supressed dna fragmentation)
PMID:30658998	FYPO:0006034	normal mitochondrion	(comment: supressed dna fragmentation)
PMID:30659798	GO:0008017	microtubule binding	(Fig. 2)
PMID:30659798	GO:0003777	microtubule motor activity	(Fig. 2f)
PMID:30667359	FYPO:0007005	decreased DNA recombination downstream of mitotic DNA replication fork barriers	(Figure 2B)
PMID:30667359	FYPO:0007005	decreased DNA recombination downstream of mitotic DNA replication fork barriers	(Figure 2B)
PMID:30667359	FYPO:0006920	decreased DNA recombination at mitotic DNA replication fork barriers	(Figure 2B)
PMID:30667359	FYPO:0000167	increased DNA recombination at mitotic DNA replication fork barriers	(Figure 2B)
PMID:30667359	FYPO:0006920	decreased DNA recombination at mitotic DNA replication fork barriers	(Figure 6B)
PMID:30667359	FYPO:0006920	decreased DNA recombination at mitotic DNA replication fork barriers	(Figure 6B)
PMID:30667359	FYPO:0007005	decreased DNA recombination downstream of mitotic DNA replication fork barriers	(Figure 6C)
PMID:30667359	FYPO:0007005	decreased DNA recombination downstream of mitotic DNA replication fork barriers	(Figure 6C)
PMID:30667359	FYPO:0007006	increased DNA recombination downstream of mitotic DNA replication fork barriers	(Figure 6C)
PMID:30667359	FYPO:0007007	normal DNA recombination frequency downstream of mitotic DNA replication fork barriers	(Figure 6C)
PMID:30667359	FYPO:0007006	increased DNA recombination downstream of mitotic DNA replication fork barriers	(Figure 6C)
PMID:30667359	FYPO:0007006	increased DNA recombination downstream of mitotic DNA replication fork barriers	(Figure 6C)
PMID:30667359	FYPO:0007007	normal DNA recombination frequency downstream of mitotic DNA replication fork barriers	(Figure 6c)
PMID:30715423	FYPO:0003124	abnormal cytoplasmic translation [has_severity] low	(comment: No queuosine-mediated reduction of translational errors at GGC (Gly) and UGC (Tyr) codons)
PMID:30715423	GO:1990145	maintenance of translational fidelity	... Q-modification in tRNAs is to improve translation ofC-ending codons relative to U-ending codons in S. pombe.
PMID:30715423	FYPO:0002056	decreased mitochondrial translation [assayed_protein] PomBase:SPMIT.05	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	FYPO:0007317	decreased cytoplasmic translation [assayed_protein] PomBase:SPBC16C6.08c	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	FYPO:0007317	decreased cytoplasmic translation [assayed_protein] PomBase:SPAC24C9.16c	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	FYPO:0002056	decreased mitochondrial translation [assayed_protein] PomBase:SPMIT.11	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	FYPO:0002056	decreased mitochondrial translation [assayed_protein] PomBase:SPMIT.01	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30715423	FYPO:0007317	decreased cytoplasmic translation [assayed_protein] PomBase:SPBC29A10.13	Reduced translation of transcripts with a mitochondrial function that is mediated by queuosine-modified tRNAs is abrogated in pmt1∆.
PMID:30726745	FYPO:0004105	abolished polar cell growth [has_penetrance] high	(Figure 1)
PMID:30726745	FYPO:0004572	decreased exocytosis during vegetative growth [has_penetrance] high	(Figure 2, Figure 3)
PMID:30726745	FYPO:0004572	decreased exocytosis during vegetative growth [has_penetrance] high	(Figure 2, Figure 3)
PMID:30726745	GO:1902716	cell cortex of growing cell tip	(Figure 6)
PMID:30726745	FYPO:0003267	normal acid phosphatase activity	(Figure 7A)
PMID:30726745	FYPO:0001045	decreased acid phosphatase activity	(Figure 7A)
PMID:30726745	FYPO:0001045	decreased acid phosphatase activity	(Figure 7A)
PMID:30726745	FYPO:0001045	decreased acid phosphatase activity	(Figure 7A)
PMID:30726745	FYPO:0001903	normal septation index	(Figure 7C, 7D)
PMID:30726745	FYPO:0001903	normal septation index	(Figure 7C, 7D)
PMID:30726745	FYPO:0001903	normal septation index	(Figure 7C, 7D)
PMID:30726745	FYPO:0001252	multinucleate multiseptate vegetative cell [has_penetrance] ~80	(Figure 7C, 7D)
PMID:30726745	FYPO:0001252	multinucleate multiseptate vegetative cell [has_penetrance] ~80	(Figure S5)
PMID:30759079	FYPO:0006927	decreased nucleus:cytoplasm ratio	(Fig. 6) The nuclear envelope is marked with Cut11-GFP
PMID:30759079	FYPO:0006927	decreased nucleus:cytoplasm ratio	(Fig. 6) The nuclear envelope is marked with Cut11-GFP
PMID:30759079	FYPO:0006927	decreased nucleus:cytoplasm ratio	(Fig. 6) The nuclear envelope is marked with Cut11-GFP
PMID:30759079	FYPO:0006927	decreased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006926	increased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	decreased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	decreased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	decreased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	decreased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	decreased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	decreased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0006927	decreased nucleus:cytoplasm ratio	Table 1 The nuclear envelope for all the mutants analysed is marked with Ish1-yEGFP integrated in the gene deletion locus. The the NC ratio of the control is reduced from 0.08 to 0.05.
PMID:30759079	FYPO:0002256	abnormal nuclear morphology	data not shown
PMID:30759079	FYPO:0002256	abnormal nuclear morphology	data not shown
PMID:30759079	FYPO:0002256	abnormal nuclear morphology	data not shown
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] low	(Fig. 3B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] high	(Fig. 3B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] high	(Fig. 3B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] complete	(Fig. 3B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] medium	(Fig. 3B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] medium	(Fig. 3B)
PMID:30759238	FYPO:0003353	normal DNA double-strand break formation at mating-type locus	(Fig. 3C)
PMID:30759238	FYPO:0003353	normal DNA double-strand break formation at mating-type locus	(Fig. 3C)
PMID:30759238	FYPO:0003353	normal DNA double-strand break formation at mating-type locus	(Fig. 3C)
PMID:30759238	FYPO:0003353	normal DNA double-strand break formation at mating-type locus	(Fig. 3C)
PMID:30759238	FYPO:0003353	normal DNA double-strand break formation at mating-type locus	(Fig. 3C)
PMID:30759238	FYPO:0003353	normal DNA double-strand break formation at mating-type locus	(Fig. 3C)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] low	(Fig. 4B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] complete	(Fig. 4B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] complete	(Fig. 4B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] high	(Fig. 4B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] complete	(Fig. 4B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] low	(Fig. 4B)
PMID:30759238	FYPO:0003353	normal DNA double-strand break formation at mating-type locus	(Fig. 4D)
PMID:30759238	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 4D)
PMID:30759238	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 4D)
PMID:30759238	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 4D)
PMID:30759238	FYPO:0003352	decreased DNA double-strand break formation at mating-type locus [has_severity] high	(Fig. 4D)
PMID:30759238	FYPO:0003353	normal DNA double-strand break formation at mating-type locus	(Fig. 4D)
PMID:30759238	GO:0003899	DNA-directed RNA polymerase activity [part_of] mating-type locus imprinting	(Fig. 5)
PMID:30759238	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1347.10 [assayed_protein] PomBase:SPAC3H5.06c [has_severity] medium	(Fig. 6)
PMID:30759238	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1347.10 [assayed_protein] PomBase:SPAC3H5.06c [has_severity] high	(Fig. 6)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] complete	(Fig. S6B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] complete	(Fig. S6B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] high	(Fig. S6B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] complete	(Fig. S6B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] complete	(Fig. S6B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] medium	(Fig. S6B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] high	(Fig. S6B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] high	(Fig. S6B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] high	(Fig. S6B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] complete	(Fig. S6B)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6C)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6C)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6C)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6C)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6C)
PMID:30759238	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S6C)
PMID:30759238	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S6C)
PMID:30759238	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S6D)
PMID:30759238	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S6D)
PMID:30759238	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S6D)
PMID:30759238	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S6D)
PMID:30759238	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S6D)
PMID:30759238	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S6D)
PMID:30759238	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S6D)
PMID:30759238	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S6D)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6D)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6D)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6D)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6D)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6D)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6D)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6D)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6D)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6D)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6D)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6D)
PMID:30759238	FYPO:0001357	normal vegetative cell population growth	(Fig. S6D)
PMID:30759238	FYPO:0000472	normal mating type switching	(Fig. S9B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] medium	(Fig. S9B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] low	(Fig. S9B)
PMID:30759238	FYPO:0000470	decreased mating type switching [has_penetrance] low	(Fig. S9B)
PMID:30773398	GO:0005737	cytoplasm	(Fig. 1a)
PMID:30773398	GO:0005634	nucleus	(Fig. 1a)
PMID:30773398	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 35	(Fig. 3)
PMID:30773398	GO:0062122	histone H3K37 methyltransferase activity [has_input] PomBase:SPAC1834.04	(Figs 1B, 1D, 1F, S1, S2)
PMID:30773398	GO:0062122	histone H3K37 methyltransferase activity [has_input] PomBase:SPBC1105.11c	(Figs 1B, 1D, 1F, S1, S2)
PMID:30773398	GO:0062122	histone H3K37 methyltransferase activity [has_input] PomBase:SPBC8D2.04	(Figs 1B, 1D, 1F, S1, S2)
PMID:30773398	FYPO:0002919	abolished histone H3-K36 methylation during vegetative growth	(Figure 1E)
PMID:30773398	FYPO:0006857	decreased histone H3-K37 methylation	(Figure 1E)
PMID:30773398	FYPO:0006857	decreased histone H3-K37 methylation	(Figure 1E)
PMID:30773398	FYPO:0002919	abolished histone H3-K36 methylation during vegetative growth	(Figure 1E)
PMID:30773398	FYPO:0006858	abolished histone H3-K37 methylation	(Figure S2)
PMID:30773398	FYPO:0006858	abolished histone H3-K37 methylation	(Figure S2)
PMID:30773398	FYPO:0006858	abolished histone H3-K37 methylation	(Figure S2)
PMID:30773398	FYPO:0006858	abolished histone H3-K37 methylation	(Figure S2)
PMID:30773398	FYPO:0006858	abolished histone H3-K37 methylation	(Figure S2)
PMID:30773398	FYPO:0006858	abolished histone H3-K37 methylation	(Figure S2)
PMID:30773398	GO:0005515	protein binding	(comment: CHECK homodimer)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. 1)
PMID:30796050	FYPO:0003107	progressively shortening telomeres during vegetative growth [has_severity] medium	(Fig. 1)
PMID:30796050	FYPO:0004656	increased protein localization to telomere during vegetative growth [assayed_using] PomBase:SPBC29A3.14c	(Fig. 1)
PMID:30796050	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC188.07	(Fig. 1)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. 1)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] low	(Fig. 1)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] high	(Fig. 1)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] high	(Fig. 2)
PMID:30796050	FYPO:0004656	increased protein localization to telomere during vegetative growth [assayed_using] PomBase:SPBC660.13c	(Fig. 2)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. 2)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. 2)
PMID:30796050	FYPO:0005402	increased telomeric 3' overhang length during vegetative growth	(Fig. 2, S2)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. 3)
PMID:30796050	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPBC409.12c	(Fig. 3)
PMID:30796050	FYPO:0003803	decreased protein localization to telomere [has_severity] high [assayed_using] PomBase:SPBC409.12c	(Fig. 3)
PMID:30796050	FYPO:0006859	decreased mitotic DNA replication at telomere	(Fig. 3) (comment: less intense Y arc in 2D gel)
PMID:30796050	FYPO:0006860	decreased mitotic DNA replication at rDNA	(Fig. 3) (comment: less intense Y arc in 2D gel)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. 4)
PMID:30796050	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC409.12c [assayed_using] PomBase:SPCC1393.14	(Fig. 4)
PMID:30796050	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC409.12c [assayed_using] PomBase:SPAC3H5.06c	(Fig. 4)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] low	(Fig. 4)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. 4)
PMID:30796050	FYPO:0003107	progressively shortening telomeres during vegetative growth [has_severity] medium	(Fig. EV2)
PMID:30796050	FYPO:0003803	decreased protein localization to telomere [has_severity] low [assayed_using] PomBase:SPBC409.12c	(Fig. EV3)
PMID:30796050	FYPO:0003803	decreased protein localization to telomere [has_severity] high [assayed_using] PomBase:SPBC409.12c	(Fig. EV3)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] low	(Fig. EV3) restrictive temperature for cdc2-M68
PMID:30796050	FYPO:0003107	progressively shortening telomeres during vegetative growth [has_severity] medium	(Fig. S1)
PMID:30796050	FYPO:0003107	progressively shortening telomeres during vegetative growth [has_severity] medium	(Fig. S1)
PMID:30796050	FYPO:0003107	progressively shortening telomeres during vegetative growth [has_severity] medium	(Fig. S2)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. S2)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. S2)
PMID:30796050	FYPO:0003107	progressively shortening telomeres during vegetative growth [has_severity] medium	(Fig. S2)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. S3)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. S3)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. S3)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. S3)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. S3)
PMID:30796050	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	(Fig. S3)
PMID:30796050	GO:0004722	protein serine/threonine phosphatase activity [has_input] PomBase:SPBC409.12c	(comment: also inferred from orthology and various genetic interactions)
PMID:30806623	FYPO:0001492	viable elongated vegetative cell	(Fig. 1)
PMID:30806623	FYPO:0004310	normal duration of mitotic M phase	(Fig. 1)
PMID:30806623	FYPO:0004310	normal duration of mitotic M phase	(Fig. 1)
PMID:30806623	FYPO:0000648	viable small vegetative cell	(Fig. 1)
PMID:30806623	FYPO:0007958	increased rate of mitotic spindle elongation	(Fig. 1)
PMID:30806623	FYPO:0003268	decreased rate of mitotic spindle elongation	(Fig. 1)
PMID:30806623	FYPO:0005706	increased duration of mitotic anaphase B	(Fig. 3)
PMID:30806623	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B	(Fig. 3)
PMID:30806623	FYPO:0007958	increased rate of mitotic spindle elongation	(Fig. 5)
PMID:30806623	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B	(Fig. 6)
PMID:30806623	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Fig. 6)
PMID:30806623	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Fig. 6)
PMID:30806623	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Fig. 6)
PMID:30806623	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Fig. 6)
PMID:30810475	FYPO:0002141	normal cell population growth at low temperature	(Fig. 1)
PMID:30810475	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 1)
PMID:30810475	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1)
PMID:30810475	FYPO:0002061	inviable vegetative cell population	(Fig. 1)
PMID:30810475	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 1)
PMID:30810475	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 1)
PMID:30810475	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 1)
PMID:30810475	FYPO:0001357	normal vegetative cell population growth	(Fig. 1)
PMID:30810475	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC26H8.07c	(Fig. 1b)
PMID:30810475	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC119.18	(Fig. 1b)
PMID:30810475	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC29E6.08	(Fig. 1b)
PMID:30810475	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC29E6.08	(Fig. 1b)
PMID:30810475	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC26H8.07c	(Fig. 1b) for dga1 normal splicing of inton 3, abnormal intron 2, Fig. S4
PMID:30810475	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC144.06	(Fig. 1b) for dga1 normal splicing of inton 3, abnormal intron 2, Fig. S4
PMID:30810475	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC222.09 [assayed_using] PomBase:SPCC1235.15 [assayed_using] PomBase:SPBC19G7.17	(Fig. 1b) for dga1 normal splicing of inton 3, abnormal intron 2, Fig. S4
PMID:30810475	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC29E6.08	(Fig. 1b) for dga1 normal splicing of inton 3, abnormal intron 2, Fig. S4
PMID:30810475	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC119.18	(Fig. 1b) for dga1 normal splicing of inton 3, abnormal intron 2, Fig. S4
PMID:30810475	FYPO:0001355	decreased vegetative cell population growth	(Fig. 4)
PMID:30810475	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC29E6.08	(Fig. 4)
PMID:30810475	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC29E6.08	(Fig. 4)
PMID:30810475	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC29E6.08	(Fig. 4)
PMID:30810475	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC29E6.08 [has_severity] low	(Fig. 4)
PMID:30810475	FYPO:0006943	normal 3'-5' RNA helicase activity [assayed_enzyme] PomBase:SPBC1711.17	(Fig. 6)
PMID:30810475	FYPO:0004300	normal ATPase activity [assayed_enzyme] PomBase:SPBC1711.17	(Fig. 6)
PMID:30810475	FYPO:0000220	increased centromeric outer repeat transcript level [assayed_using] PomBase:SPNCRNA.232	(Fig. 7)
PMID:30810475	FYPO:0000229	cut	(Fig. 7)
PMID:30810475	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Fig. 7)
PMID:30810475	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 7)
PMID:30810475	FYPO:0001917	inviable elongated mononucleate monoseptate vegetative cell	(Fig. 7)
PMID:30810475	FYPO:0000091	sensitive to thiabendazole	(Fig. 7)
PMID:30810475	FYPO:0000220	increased centromeric outer repeat transcript level [assayed_using] PomBase:SPNCRNA.362	(Fig. 7)
PMID:30810475	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Fig. 7)
PMID:30810475	FYPO:0001919	fragmented nucleus during vegetative growth	(Fig. 7) (comment: CHECK they say fragmented nucleus but they stained chromosomes, not nuclear envelope)
PMID:30810475	FYPO:0000220	increased centromeric outer repeat transcript level [assayed_using] PomBase:SPNCRNA.230	(Fig. S6, 7)
PMID:30810475	FYPO:0000220	increased centromeric outer repeat transcript level [assayed_using] PomBase:SPNCRNA.362	(Fig. S6, 7)
PMID:30810475	FYPO:0000220	increased centromeric outer repeat transcript level [assayed_using] PomBase:SPNCRNA.232	(Fig. S6, 7)
PMID:30810475	FYPO:0000220	increased centromeric outer repeat transcript level [assayed_using] PomBase:SPNCRNA.231	(Fig. S6, 7)
PMID:30810475	GO:0000384	first spliceosomal transesterification activity [part_of] mRNA cis splicing, via spliceosome	(comment: Required for splicing of introns with strong 5' splice site - U6 snRNA and branch site - U2 snRNA interactions)
PMID:30810475	GO:0016887	ATP hydrolysis activity	In vitro RNA helicase activity using recombinant protein encoded by the helicase domain of Prp16
PMID:30810475	GO:0034458	3'-5' RNA helicase activity	In vitro RNA helicase activity using recombinant protein encoded by the helicase domain of Prp16
PMID:30810475	GO:0045292	mRNA cis splicing, via spliceosome	Required for the splicing of several genome-wide transcripts. Inferred from transcriptome sequencing of the mutant strain prp16F528S. Splicing defects in transcripts validated by RT-PCR assays.
PMID:30840879	FYPO:0001880	abolished protein localization to cell division site [assayed_using] PomBase:SPBC23G7.08c	(Fig. 1B)
PMID:30840879	FYPO:0001880	abolished protein localization to cell division site [assayed_using] PomBase:SPBC23G7.08c	(Fig. 1B)
PMID:30840879	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC23G7.08c [assayed_using] PomBase:SPAC688.07c	(Fig. 1F)
PMID:30840879	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPBC23G7.08c	(Fig. 2A, Figure 2A)
PMID:30840879	FYPO:0005307	decreased phospholipid binding [assayed_using] PomBase:SPAC688.07c	(Fig. 2b)
PMID:30840879	FYPO:0006942	normal lipid binding [assayed_using] PomBase:SPBC23G7.08c	(Fig. 2b) (comment: CHECK normal lipid binding)
PMID:30840879	FYPO:0005307	decreased phospholipid binding [assayed_using] PomBase:SPBC23G7.08c	(Fig. 3c)
PMID:30840879	FYPO:0005307	decreased phospholipid binding [has_severity] high	(Fig. 3c)
PMID:30840879	FYPO:0005307	decreased phospholipid binding [has_severity] high	(Fig. 3c)
PMID:30840879	FYPO:0001880	abolished protein localization to cell division site [assayed_using] PomBase:SPBC23G7.08c	(Fig. 3e)
PMID:30840879	FYPO:0001880	abolished protein localization to cell division site [assayed_using] PomBase:SPBC23G7.08c	(Fig. 3e)
PMID:30840879	FYPO:0002869	decreased protein localization to cell division site [assayed_using] PomBase:SPBC23G7.08c	(Fig. 3e)
PMID:30840879	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] 12	(Fig. 4)
PMID:30840879	FYPO:0002442	normal protein localization to cell division site [assayed_using] PomBase:SPBC23G7.08c	(Figure 2A)
PMID:30840879	FYPO:0006937	abolished lipid binding [assayed_using] PomBase:SPBC23G7.08c	(Figure 2A)
PMID:30840879	GO:0008093	cytoskeletal anchor activity [has_input] PomBase:SPBC23G7.08c [part_of] mitotic division septum assembly [occurs_in] cell division site [happens_during] mitotic M phase	(comment: CHECK F-BAR/BAR domain adaptors) Rng10(751-950) interacts directly with the Rga7 F-BAR domain
PMID:30840879	GO:0070273	phosphatidylinositol-4-phosphate binding	(comment: CHECK MEMBRANE LIPID BINDING) Rga7 F-BAR preferred membranes rich in PI(4)P and PI(4,5)P2 (Figure 3D)
PMID:30840879	GO:0005546	phosphatidylinositol-4,5-bisphosphate binding	(comment: CHECK MEMBRANE LIPID BINDING) Rga7 F-BAR preferred membranes rich in PI(4)P and PI(4,5)P2 (Figure 3D)
PMID:30840879	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC23G7.08c [assayed_using] PomBase:SPAC688.07c	Defining the Rga7-binding motif within Rng10 further, we found that Rng10(751-950) bound Rga7(1-320) with a similar Kd of 0.69 μM (Figures 1F, 1G, and S2B)
PMID:30840879	FYPO:0006936	abolished protein localization to plasma membrane at cell division site during vegetative growth [assayed_using] PomBase:SPBC23G7.08c	GFP-Rga7(277-695) alone, lacking the majority of the F-BAR domain, could not localize to the PM, resulting in massive cell lysis
PMID:30840879	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC23G7.08c [assayed_using] PomBase:SPAC688.07c	To test for a direct interaction, we performed in vitro binding assays using recombinant Rng10 C terminus and the Rga7 F-BAR (Figures 1D and S2A). GST- Rng10(751-1,038) efficiently bound His6-Rga7(1-320) with a dissociation constant (Kd) of 0.43 μM (Figures 1D, 1E, and S2B).
PMID:30853434	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic metaphase	(Fig. 1D)
PMID:30853434	GO:0071341	medial cortical node [exists_during] mitotic interphase	(Fig. 1D)
PMID:30853434	GO:0005634	nucleus [exists_during] mitotic interphase	(Fig. 1D)
PMID:30853434	GO:0061608	nuclear import signal receptor activity [has_input] PomBase:SPCC4B3.15	(Fig. 2E, 2F)
PMID:30853434	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC4B3.15	(Figure 1C)
PMID:30853434	FYPO:0001677	increased protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC4B3.15	(Figure 1D-G) (comment: live cell imaging)
PMID:30853434	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPCC4B3.15	(Figure 1H, 1I) (comment: live cell imaging)
PMID:30853434	FYPO:0001402	normal protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPCC4B3.15	(Figure 1H, 1I) (comment: live cell imaging)
PMID:30853434	FYPO:0006853	increased protein localization to medial cortex during mitotic telophase [assayed_using] PomBase:SPCC4B3.15	(Figure 2A, 2B) (comment: live cell imaging)
PMID:30853434	FYPO:0003189	decreased protein import into nucleus [assayed_using] PomBase:SPCC4B3.15	(Figure 2E, 2F) (comment: live cell imaging)
PMID:30853434	FYPO:0005905	normal onset of actomyosin contractile ring assembly	(Figure 3A, 3B) (comment: Live-cell time-lapse imaging)
PMID:30853434	FYPO:0001365	decreased rate of actomyosin contractile ring contraction	(Figure 3A, 3B) (comment: Live-cell time-lapse imaging)
PMID:30853434	FYPO:0002874	premature protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAC926.03	(Figure 3A, 3B) (comment: Live-cell time-lapse imaging)
PMID:30853434	FYPO:0003210	mislocalized, misoriented septum	(Figure 3C, 3D) (comment: live cell DIC)
PMID:30853434	FYPO:0002873	normal septum orientation	(Figure 3C,D)
PMID:30853434	FYPO:0002873	normal septum orientation	(Figure 3D) (comment: live cell DIC)
PMID:30853434	FYPO:0004854	increased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC57A10.02	(Figure 4A, 4B) (comment: live cell imaging)
PMID:30853434	FYPO:0007474	variable cell size at division	(Figure 4E) (comment: moved from wee) (comment: skewed towards small, low severity)
PMID:30853434	FYPO:0001223	binucleate multiseptate vegetative cell	(Figure 4G) (comment: live cell DIC)
PMID:30853434	FYPO:0003210	mislocalized, misoriented septum	(Figure 4G) (comment: live cell DIC)
PMID:30853434	FYPO:0003210	mislocalized, misoriented septum	(Figure 4G) (comment: live cell DIC)
PMID:30853434	FYPO:0003439	branched septum	(Figure 4G) (comment: live cell DIC)
PMID:30853434	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Figure 4H) (comment: live cell DIC)
PMID:30853434	FYPO:0003210	mislocalized, misoriented septum	(Figure 4I) (comment: Live-cell time-lapse imaging)
PMID:30853434	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC24B11.11c [added_during] mitotic M phase	(Figure S1)
PMID:30853434	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC24B11.11c [added_during] mitotic M phase	(Figure S1)
PMID:30853434	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC24B11.11c [added_during] mitotic M phase	(Figure S1)
PMID:30853434	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC24B11.11c [added_during] mitotic M phase	(Figure S1)
PMID:30853434	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC24B11.11c [added_during] mitotic M phase	(Figure S1)
PMID:30853434	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC24B11.11c [added_during] mitotic M phase	(Figure S1)
PMID:30853434	FYPO:0002874	premature protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC645.05c	(Figure S2A, S2B) (comment: live cell imaging)
PMID:30853434	FYPO:0006008	normal onset of protein localization to cell division site [assayed_using] PomBase:SPAC1F5.04c	(Figure S2A, S2B) (comment: live cell imaging)
PMID:30853434	FYPO:0002874	premature protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAC4F8.13c	(Figure S2A, S2B) (comment: live cell imaging)
PMID:30853434	FYPO:0002874	premature protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPAC20G8.05c	(Figure S2A, S2B) (comment: vw: changed from FYPO:0001677 to FYPO:0002874 to match rlc1) (comment: live cell imaging))
PMID:30853434	FYPO:0006008	normal onset of protein localization to cell division site [assayed_using] PomBase:SPAC23C11.16	(Figure S2C) (comment: live cell imaging)
PMID:30853434	FYPO:0003919	abolished protein localization to medial cortical node [assayed_using] PomBase:SPCC4B3.15	(Figure S3A) (comment: live cell imaging)
PMID:30853434	FYPO:0000929	decreased protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPCC4B3.15	(Figure S3A) (comment: live cell imaging)
PMID:30853434	FYPO:0004780	decreased protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_using] PomBase:SPCC4B3.15	(Figure S3C, S3D) (comment: live cell imaging)
PMID:30853434	FYPO:0000929	decreased protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPCC4B3.15	(Figure S3C, S3D) (comment: live cell imaging)
PMID:30853434	FYPO:0006326	decreased protein localization to medial cortical node [assayed_using] PomBase:SPCC4B3.15	(Figure S4A)
PMID:30853434	FYPO:0001402	normal protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPCC4B3.15	(Figure S4A) (comment: live cell imaging)
PMID:30853434	FYPO:0001402	normal protein localization to cell cortex during vegetative growth [assayed_using] PomBase:SPCC4B3.15	(Figure S4A) (comment: live cell imaging)
PMID:30853434	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPCC4B3.15 [assayed_using] PomBase:SPAC57A10.02	(Figure S4C, S4D)
PMID:30853434	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Figure S4F, S4G) (comment: vw: move to FYPO:0006822 and requested parentage fix in FYPO) (comment: live cell DIC)
PMID:30853434	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Figure S4F, S4G) (comment: vw: moved to FYPO:0006822 and requested parentage fix in FYPO) (comment: live cell DIC)
PMID:30853434	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(Figure S4F, S4H) (comment: live cell DIC)
PMID:30853434	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(Figure S4F, S4H) (comment: live cell DIC)
PMID:30853434	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Figure S4G) (comment: live cell DIC)
PMID:30853434	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPAC57A10.02 [assayed_using] PomBase:SPCC4B3.15	(comment: increased binding by about 2 fold from) (Figure 4C, 4D)
PMID:30862564	FYPO:0003125	decreased cytoplasmic translational initiation	(comment: converted from bp by cc)
PMID:30862564	FYPO:0003125	decreased cytoplasmic translational initiation	(comment: converted from bp by cc)
PMID:30967422	FYPO:0000284	large and small daughter nuclei, with unequal mitotic sister chromatid segregation [has_penetrance] 18	(Figure 2b)
PMID:30967422	FYPO:0000284	large and small daughter nuclei, with unequal mitotic sister chromatid segregation [has_penetrance] 25	(Figure 2b)
PMID:30967422	FYPO:0000284	large and small daughter nuclei, with unequal mitotic sister chromatid segregation [has_penetrance] 20	(Figure 2b)
PMID:30967422	FYPO:0000284	large and small daughter nuclei, with unequal mitotic sister chromatid segregation [has_penetrance] 30	(Figure 2b)
PMID:30973898	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1D)
PMID:30973898	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1D)
PMID:30973898	FYPO:0000964	normal growth on thiabendazole	(Figure 1A)
PMID:30973898	FYPO:0003809	normal growth on latrunculin A	(Figure 1A)
PMID:30973898	FYPO:0001214	sensitive to potassium chloride	(Figure 1A)
PMID:30973898	FYPO:0000107	sensitive to latrunculin A	(Figure 1A)
PMID:30973898	FYPO:0003840	sensitive to carbendazim [has_severity] medium	(Figure 1A)
PMID:30973898	FYPO:0001686	normal growth on carbendazim	(Figure 1A)
PMID:30973898	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Figure 1A)
PMID:30973898	FYPO:0005947	normal growth on potassium chloride	(Figure 1A)
PMID:30973898	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Figure 1B)
PMID:30973898	FYPO:0000964	normal growth on thiabendazole	(Figure 1B)
PMID:30973898	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC18G6.15 [assayed_using] PomBase:SPAC18G6.15	(Figure 2B) (comment: (two hybrid))
PMID:30973898	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC18G6.15 [assayed_using] PomBase:SPAC18G6.15	(Figure 2B) (comment: (two hybrid))
PMID:30973898	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC18G6.15 [assayed_using] PomBase:SPAC18G6.15	(Figure 2B) (comment: (two hybrid))
PMID:30973898	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC18G6.15 [assayed_using] PomBase:SPAC18G6.15	(Figure 2B) (comment: (two hybrid))
PMID:30973898	FYPO:0000069	resistance to thiabendazole [has_severity] high	(Figure 2C)
PMID:30973898	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Figure 2C)
PMID:30973898	FYPO:0002061	inviable vegetative cell population	(Figure 2C)
PMID:30973898	FYPO:0000069	resistance to thiabendazole [has_severity] high	(Figure 2C)
PMID:30973898	FYPO:0002966	normal protein localization to mitotic spindle [assayed_using] PomBase:SPAC18G6.15	(Figure 2D)
PMID:30973898	FYPO:0005441	abolished protein localization to microtubule during mitotic interphase [assayed_using] PomBase:SPAC18G6.15	(Figure 2D)
PMID:30973898	GO:0005881	cytoplasmic microtubule [exists_during] mitotic interphase	(Figure 2D)
PMID:30973898	GO:0005880	nuclear microtubule [exists_during] mitotic M phase	(Figure 2D)
PMID:30973898	FYPO:0000069	resistance to thiabendazole [has_severity] high	(Figure 3A)
PMID:30973898	FYPO:0000069	resistance to thiabendazole [has_severity] high	(Figure 3A)
PMID:30973898	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Figure 3A)
PMID:30973898	FYPO:0002059	inviable cell population	(Figure 3A)
PMID:30973898	FYPO:0002061	inviable vegetative cell population	(Figure 3A)
PMID:30973898	FYPO:0000229	cut	(Figure 4) DAPI staining
PMID:30973898	FYPO:0001007	normal mitosis [has_severity] medium	(Figure 4C)
PMID:30973898	FYPO:0001007	normal mitosis [has_severity] medium	(Figure 4C)
PMID:30973898	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] ~40	(Figure 4C) mini-chromosome Ch16 loss assay
PMID:30973898	FYPO:0000069	resistance to thiabendazole [has_severity] high	(Figure 5A)
PMID:30973898	FYPO:0000069	resistance to thiabendazole [has_severity] high	(Figure 5A)
PMID:30973898	FYPO:0000069	resistance to thiabendazole [has_severity] high	(Figure 5A)
PMID:30973898	FYPO:0000069	resistance to thiabendazole [has_severity] high	(Figure 5A)
PMID:30973898	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Figure 5A)
PMID:30973898	FYPO:0000069	resistance to thiabendazole [has_severity] high	(Figure 5A)
PMID:30973898	FYPO:0004083	normal protein level [assayed_using] PomBase:SPAC18G6.15	(Figure S2A)
PMID:30973898	FYPO:0004083	normal protein level [assayed_using] PomBase:SPAC18G6.15	(Figure S2A)
PMID:30973898	FYPO:0003627	normal protein localization [assayed_using] PomBase:SPAC18G6.15	(Figure S2B)
PMID:30973898	FYPO:0003627	normal protein localization [assayed_using] PomBase:SPAC18G6.15	(Figure S2B)
PMID:30973898	FYPO:0003241	unequal mitotic sister chromatid segregation [has_severity] high	(comment: evidence: mini-chromosome Ch16 loss assay)
PMID:30975915	FYPO:0002061	inviable vegetative cell population	(Fig. 2B)
PMID:30975915	FYPO:0001839	normal minichromosome loss	(Fig. 4)
PMID:30975915	FYPO:0002360	normal chromatin silencing at centromere	(Fig. 4)
PMID:30975915	FYPO:0001234	slow vegetative cell population growth	(Fig. 4A)
PMID:30975915	FYPO:0000963	normal growth on hydroxyurea	(Fig. 4B)
PMID:30975915	FYPO:0000088	sensitive to hydroxyurea	(Fig. 4B)
PMID:30975915	FYPO:0000088	sensitive to hydroxyurea	(Fig. 4B)
PMID:30975915	FYPO:0002061	inviable vegetative cell population	(Figure 1)
PMID:30975915	FYPO:0002061	inviable vegetative cell population	(Figure 1)
PMID:30975915	FYPO:0001357	normal vegetative cell population growth	(Figure 1)
PMID:30975915	FYPO:0002061	inviable vegetative cell population	(Figure 1)
PMID:30975915	FYPO:0002061	inviable vegetative cell population	(Figure 1A)
PMID:30975915	FYPO:0002061	inviable vegetative cell population	(Figure 3)
PMID:30975915	FYPO:0002061	inviable vegetative cell population	(Figure 3)
PMID:30975915	FYPO:0002061	inviable vegetative cell population	(Figure 3)
PMID:30992049	FYPO:0000085	sensitive to camptothecin	(comment: 25 degrees; same as mst1-L344S alone)
PMID:30992049	FYPO:0000085	sensitive to camptothecin [has_severity] low	(comment: CHECK same as nmt81-vid21 alone)
PMID:30992049	FYPO:0000085	sensitive to camptothecin [has_severity] high	(comment: grows normally at 25 degrees but not at 30 degrees)
PMID:30992049	FYPO:0000085	sensitive to camptothecin	(comment: grows normally at 25 degrees but not at 30 degrees)
PMID:30992049	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(comment: grows normally at 25 degrees but not at 30 degrees)
PMID:30992049	FYPO:0001355	decreased vegetative cell population growth	(comment: grows normally at 25 degrees but not at 30 degrees)
PMID:30992049	FYPO:0000085	sensitive to camptothecin [has_severity] low	(comment: hhf1 and hhf3 are wild-type. Only hhf2 is mutated)
PMID:30992049	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(comment: hhf1 and hhf3 are wild-type. Only hhf2 is mutated)
PMID:30992049	FYPO:0002550	sensitive to UV	(comment: hhf1 and hhf3 are wild-type. Only hhf2 is mutated)
PMID:30992049	FYPO:0000095	sensitive to bleomycin	(comment: hhf1 and hhf3 are wild-type. Only hhf2 is mutated)
PMID:30992049	FYPO:0000085	sensitive to camptothecin [has_severity] low	(comment: hhf2 and hhf3 are wild-type. Only hhf2 is mutated)
PMID:30992049	FYPO:0000085	sensitive to camptothecin [has_severity] low	(comment: hhf2 and hhf3 are wild-type. Only hhf2 is mutated)
PMID:30992049	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(comment: same as swi1delta alone)
PMID:30996236	FYPO:0001357	normal vegetative cell population growth	(Fig. 2)
PMID:30996236	FYPO:0001357	normal vegetative cell population growth	(Fig. 2)
PMID:30996236	FYPO:0001234	slow vegetative cell population growth	(Fig. 2)
PMID:30996236	FYPO:0001357	normal vegetative cell population growth	(Fig. 2)
PMID:30996236	FYPO:0001357	normal vegetative cell population growth	(Fig. 2)
PMID:30996236	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(Fig. 2)
PMID:30996236	FYPO:0001234	slow vegetative cell population growth [has_severity] low	(Fig. 2)
PMID:30996236	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 2)
PMID:30996236	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 2)
PMID:30996236	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 2)
PMID:30996236	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 2)
PMID:30996236	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 2)
PMID:30996236	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 2)
PMID:30996236	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 2)
PMID:30996236	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(Fig. 2)
PMID:30996236	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 3)
PMID:30996236	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 3)
PMID:30996236	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 3)
PMID:30996236	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 3)
PMID:30996236	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 3)
PMID:30996236	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 3)
PMID:30996236	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 3)
PMID:30996236	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 3)
PMID:30996236	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 3)
PMID:30996236	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 3)
PMID:30996236	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 3)
PMID:30996236	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 3)
PMID:30996236	FYPO:0002674	normal protein localization to plasma membrane	(Fig. 3)
PMID:31000521	FYPO:0007304	short bipolar mitotic spindle during anaphase [has_severity] medium	(Fig. 2A) (comment: Spindle pole-to-pole distance was measured based on the distance of duplicated SPBs revealed by Sad1-DsRed.)
PMID:31000521	FYPO:0007304	short bipolar mitotic spindle during anaphase [has_severity] high	(Fig. 2A) (comment: Spindle pole-to-pole distance was measured based on the distance of duplicated SPBs revealed by Sad1-DsRed.)
PMID:31000521	FYPO:0000274	increased duration of mitotic M phase [has_severity] medium	(Fig. 2C)
PMID:31000521	FYPO:0000274	increased duration of mitotic M phase [has_severity] high	(Fig. 2C)
PMID:31000521	FYPO:0000274	increased duration of mitotic M phase [has_severity] low	(Fig. 2C)
PMID:31000521	FYPO:0001513	normal mitotic sister chromatid segregation [has_penetrance] 1.3	(Fig. 3B)
PMID:31000521	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Fig. 5B)
PMID:31000521	FYPO:0000634	abolished protein localization to centromere during vegetative growth	(Fig. 5B) (comment: CHECK abolish Swi6 protein localization to centromere during vegetative growth)
PMID:31000521	FYPO:0002574	normal protein localization to centromere during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Fig. 5C)
PMID:31000521	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Fig. 5E)
PMID:31000521	FYPO:0006811	normal gross chromosomal rearrangement frequency	(Fig. 7) (comment: using minichromosome)
PMID:31000521	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(Fig. 7) (comment: using minichromosome)
PMID:31000521	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(Fig. 7) (comment: using minichromosome)
PMID:31000521	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(Fig. 7) (comment: using minichromosome)
PMID:31000521	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 7B)
PMID:31000521	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Fig. 7B)
PMID:31000521	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Fig. 7B)
PMID:31000521	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 7B)
PMID:31000521	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Fig. 7B)
PMID:31000521	FYPO:0000091	sensitive to thiabendazole	(Fig. S1)
PMID:31000521	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 12.5	(Figure 3B)
PMID:31000521	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 18.6	(Figure 3B)
PMID:31000521	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 16.8	(Figure 3B)
PMID:31000521	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 5.8	(Figure 3B)
PMID:31000521	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 13.5	(Figure 3B) (comment: vw changed more specific to lagging chromosmes) Increase the frequency of mitotic cells showing lagging chromosomes. Rad21 fails to accumulate at centromere in the absence of Swi6.
PMID:31000521	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 3B) Chp1 fails to accumulate at noncentromeric location in the absence of Chp2 and Swi6.
PMID:31000521	FYPO:0004310	normal duration of mitotic M phase	(comment: (VW changed to multi allele)) The delay of m-to-G1/S phase transition in swi6∆ and dfp1-3A was abolished after deleting mad2.
PMID:31000521	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 3.4	(comment: (vw 3B? changed from normal to lagging, added penetrance)) dfp1-CFP-2CD rescues minichromosome loss in the absence of Swi6.
PMID:31000521	FYPO:0001007	normal mitosis	(comment: (vw: changed genotype to add swi6 delt)) dfp1-CFP-2CD restores lagging chromosomes in the absence of Swi6. Rad21 locates to centromere in dfp1-CFP-2CD mutants.
PMID:31000521	FYPO:0004310	normal duration of mitotic M phase	Rad21 locates to centromere in dfp1-3A mutants.
PMID:31000521	FYPO:0002574	normal protein localization to centromere during vegetative growth [assayed_using] PomBase:SPCC338.17c	Rad21-GFP enrichment at the centromere is unaffected in swi6-sm1 (Figure S4C)
PMID:31000521	FYPO:0001513	normal mitotic sister chromatid segregation	The swi6-sm1 allele disrupts silencing without lagging chromosomes (Yamagishi et al. 2008) (Figure S4, A and B). We observed a similar frequency of lagging chromosomes in wild-type (1%) and swi6-sm1 mutants (1.03%).
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 1 supp data)
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 1 supp data)
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 1 supp data)
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 1 supp data)
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 1 supp data)
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 1 supp data)
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 1)
PMID:31015410	FYPO:0006926	increased nucleus:cytoplasm ratio [has_severity] medium	(Fig. 1)
PMID:31015410	FYPO:0002891	normal chromatin organization during vegetative growth [has_severity] high	(Fig. 1) (comment: normal compaction)
PMID:31015410	FYPO:0006926	increased nucleus:cytoplasm ratio [has_severity] medium	(Fig. 1a) shows the lem2 chromatin binding domain is not required to restrict enhancement of the NC ratio of rae1-167
PMID:31015410	FYPO:0006926	increased nucleus:cytoplasm ratio [has_severity] medium	(Fig. 1a,b,c)
PMID:31015410	FYPO:0006927	decreased nucleus:cytoplasm ratio [has_severity] medium	(Fig. 2a,b,c)
PMID:31015410	FYPO:0006928	nuclear membrane blebbing [has_severity] medium	(Fig. 2d,e,f,g,h, S6B)
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 3a,b)
PMID:31015410	FYPO:0000062	abnormal nuclear morphology during vegetative growth [has_penetrance] high	(Fig. 3c)
PMID:31015410	FYPO:0001380	normal nuclear morphology during vegetative growth	(Fig. 3c)
PMID:31015410	FYPO:0006926	increased nucleus:cytoplasm ratio [has_severity] medium	(Fig. 3c)
PMID:31015410	FYPO:0001380	normal nuclear morphology during vegetative growth	(Fig. 3c)
PMID:31015410	FYPO:0006926	increased nucleus:cytoplasm ratio [has_penetrance] low	(Fig. 3c,d)
PMID:31015410	FYPO:0006926	increased nucleus:cytoplasm ratio [has_penetrance] low	(Fig. 3c,d)
PMID:31015410	FYPO:0006926	increased nucleus:cytoplasm ratio [has_penetrance] medium	(Fig. 3d)
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 3d)
PMID:31015410	FYPO:0001380	normal nuclear morphology during vegetative growth [has_penetrance] high	(Fig. 3e)
PMID:31015410	FYPO:0001380	normal nuclear morphology during vegetative growth [has_penetrance] high	(Fig. 3e)
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio [has_penetrance] medium	(Fig. 3e)
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio [has_penetrance] medium	(Fig. 3e)
PMID:31015410	FYPO:0006927	decreased nucleus:cytoplasm ratio [has_penetrance] low	(Fig. 3f)
PMID:31015410	FYPO:0006927	decreased nucleus:cytoplasm ratio [has_penetrance] low	(Fig. 3f)
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 4a,c)
PMID:31015410	FYPO:0006926	increased nucleus:cytoplasm ratio [has_penetrance] high	(Fig. 4a,c)
PMID:31015410	FYPO:0006926	increased nucleus:cytoplasm ratio [has_penetrance] high	(Fig. 4a,c)
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. 4a,c)
PMID:31015410	FYPO:0006926	increased nucleus:cytoplasm ratio [has_severity] high	(Fig. 4b,c) (comment: CHECK ENHANCER OF N/C ratio of lem2/rae1)
PMID:31015410	GO:0031965	nuclear membrane	Supp Fig6
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio [has_severity] high	supp Fig 7
PMID:31015410	FYPO:0001221	normal nucleus:cytoplasm ratio [has_severity] high	supp Fig 7
PMID:31015410	FYPO:0003627	normal protein localization [assayed_using] PomBase:SPAC18G6.10	supp Fig6a
PMID:31015410	FYPO:0006926	increased nucleus:cytoplasm ratio [has_severity] medium	supp data Fig 1b,c
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level	(Fig. 6)
PMID:31030285	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC19G12.12	(Fig. 7)
PMID:31030285	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPCC162.05	(Fig. 7)
PMID:31030285	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC2D10.18	(Fig. 7)
PMID:31030285	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPCC4G3.04c	(Fig. 7)
PMID:31030285	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPCC4G3.04c	(Fig. 7)
PMID:31030285	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC19G12.12	(Fig. 7)
PMID:31030285	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPCC162.05	(Fig. 7)
PMID:31030285	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC2D10.18	(Fig. 7)
PMID:31030285	FYPO:0001420	normal vegetative cell population growth rate	(Fig. 8)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	(Fig. S1)
PMID:31030285	FYPO:0006979	increased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] low	(Fig. S1)
PMID:31030285	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC1687.12c	Coq4 protein is decreased but Dlp1, Coq3, Coq5 and Coq8 are not
PMID:31030285	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPAC1687.12c	Coq4 protein is increased but Dlp1, Coq3, Coq5, and Coq8 are not
PMID:31030285	FYPO:0004167	increased cell population growth on glycerol carbon source	cell growth is faster than wild type in glycerol and ethanol medium
PMID:31030285	FYPO:0000442	decreased cell population growth on glycerol/ethanol carbon source	cell growth is slower than wild type in glycerol and ethanol medium
PMID:31030285	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPAC13F5.03c	data not shown
PMID:31041892	FYPO:0001492	viable elongated vegetative cell [has_penetrance] low	(Fig. 1)
PMID:31041892	FYPO:0001492	viable elongated vegetative cell [has_penetrance] low	(Fig. 1)
PMID:31041892	FYPO:0001492	viable elongated vegetative cell [has_penetrance] low	(Fig. 1)
PMID:31041892	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC24B11.11c [has_severity] low	(Figure 2)
PMID:31041892	FYPO:0002562	delayed onset of protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC24B11.11c [has_severity] low	(Figure 2)
PMID:31041892	FYPO:0002562	delayed onset of protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC24B11.11c [has_severity] low	(Figure 2)
PMID:31041892	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC24B11.11c [has_severity] low	(Figure 2)
PMID:31041892	FYPO:0002562	delayed onset of protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC24B11.11c [has_severity] low	(Figure 2) (comment: blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants)
PMID:31041892	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC24B11.11c [has_severity] low	(Figure 2) blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	FYPO:0002562	delayed onset of protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC428.13c	(Figure 3)
PMID:31041892	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC428.13c	(Figure 3)
PMID:31041892	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC428.13c	(Figure 3)
PMID:31041892	FYPO:0002562	delayed onset of protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC428.13c	(Figure 3)
PMID:31041892	FYPO:0002562	delayed onset of protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC428.13c [has_severity] low	(Figure 3) (comment: blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants)
PMID:31041892	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC428.13c [has_severity] low	(Figure 3) blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants
PMID:31041892	FYPO:0004653	delayed onset of actomyosin contractile ring contraction [has_severity] low	(Figure 4)
PMID:31041892	FYPO:0004653	delayed onset of actomyosin contractile ring contraction [has_severity] low	(Figure 4)
PMID:31041892	FYPO:0005905	normal onset of actomyosin contractile ring assembly	(Figure 4) (comment: blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants)
PMID:31041892	FYPO:0005905	normal onset of actomyosin contractile ring assembly	(Figure 4) (comment: blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants)
PMID:31041892	FYPO:0004653	delayed onset of actomyosin contractile ring contraction [has_severity] low	(Figure 4) (comment: blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants)
PMID:31041892	FYPO:0005905	normal onset of actomyosin contractile ring assembly	(Figure 4) blt1∆/gef2∆ (comment: phenotype equivalent to blt1∆ or gef2∆ single mutants)
PMID:31041892	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC1A4.05	(Figure 5)
PMID:31041892	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC31A2.16	(Figure 5)
PMID:31041892	FYPO:0004646	normal duration of mitotic anaphase	(comment: blt1∆/gef2∆ phenotype equivalent to blt1∆ or gef2∆ single mutants)
PMID:31053915	GO:0010340	carboxyl-O-methyltransferase activity	(comment: catechol O-methyltransferase activity (Vw I kept this as o-methytransferase since no report of catachols in fission yeast))
PMID:31053915	GO:0008171	O-methyltransferase activity	(comment: catechol O-methyltransferase activity)
PMID:31053915	GO:1990748	cellular detoxification	(comment: detoxification)
PMID:31053915	GO:1990748	cellular detoxification	(comment: detoxification)
PMID:31072933	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC338.17c	((comment: Rescued to WT level) Rad21 phosphorylation level in cohesin hinge cs mutants is rescued by Δwpl1, while the loss of the Rad21 protein level in cohesin hinge ts mutants cannot be rescued by Δwpl1
PMID:31072933	FYPO:0001355	decreased vegetative cell population growth	(Fig. 3B)
PMID:31072933	FYPO:0001355	decreased vegetative cell population growth	(Fig. 3B)
PMID:31072933	FYPO:0001355	decreased vegetative cell population growth	(Fig. 3B)
PMID:31072933	FYPO:0001355	decreased vegetative cell population growth	(Figure 1C)
PMID:31072933	MOD:01149	sumoylated lysine [present_during] mitotic metaphase	(Figure 1G)
PMID:31072933	GO:0061665	SUMO ligase activity [has_input] PomBase:SPCC306.03c	(Figure 1G)
PMID:31072933	GO:0061665	SUMO ligase activity [has_input] PomBase:SPBC146.03c	(Figure 1G)
PMID:31072933	GO:0061665	SUMO ligase activity [has_input] PomBase:SPCC188.03	(Figure 1G)
PMID:31072933	MOD:01149	sumoylated lysine [present_during] mitotic metaphase	(Figure 1G)
PMID:31072933	MOD:01149	sumoylated lysine [present_during] mitotic metaphase	(Figure 1G, Figure 2)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002061	inviable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002061	inviable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002061	inviable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002061	inviable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002061	inviable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1e)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1e)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 1e)
PMID:31072933	FYPO:0005934	abolished protein sumoylation during vegetative growth [assayed_using] PomBase:SPCC306.03c	(Figure 2)
PMID:31072933	FYPO:0005934	abolished protein sumoylation during vegetative growth [assayed_using] PomBase:SPCC188.03	(Figure 2)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 2C)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 3A)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 3A)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 3A)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 3A)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 3A)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 3A)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 3A)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 3A)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 3F)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 4A,B)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 4A,B)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 4A,B)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 4A,B)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 4A,B)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 4D-H)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 4D-H)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure 4D-H)
PMID:31072933	FYPO:0001355	decreased vegetative cell population growth	(Figure 5C)
PMID:31072933	FYPO:0002061	inviable vegetative cell population	(Figure 5C)
PMID:31072933	FYPO:0001355	decreased vegetative cell population growth	(Figure 5C)
PMID:31072933	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Figure 6c)
PMID:31072933	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Figure 6c)
PMID:31072933	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Figure 6c)
PMID:31072933	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Figure 6c)
PMID:31072933	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Figure 6c)
PMID:31072933	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Figure 6c)
PMID:31072933	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Figure 6c)
PMID:31072933	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Figure 6c)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S3)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S4)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S4)
PMID:31072933	FYPO:0002060	viable vegetative cell population	(Figure S4)
PMID:31072933	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Figure S7A)
PMID:31072933	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Figure S7A)
PMID:31072933	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Figure S7A)
PMID:31072933	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC338.17c	(Figure S7A)
PMID:31072933	FYPO:0002061	inviable vegetative cell population	(Figure S8)
PMID:31072933	FYPO:0002061	inviable vegetative cell population	(Figure S8)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Fig. 2A top)
PMID:31089172	FYPO:0006644	decreased protein localization to mitotic spindle midzone, with protein distributed along spindle, during anaphase B [assayed_using] PomBase:SPBC15D4.01c	(Fig. 2A, B)
PMID:31089172	FYPO:0006644	decreased protein localization to mitotic spindle midzone, with protein distributed along spindle, during anaphase B [assayed_using] PomBase:SPBC15D4.01c	(Fig. 2A, B)
PMID:31089172	FYPO:0003268	decreased rate of mitotic spindle elongation	(Fig. 2C, D)
PMID:31089172	FYPO:0003268	decreased rate of mitotic spindle elongation	(Fig. 2C, D)
PMID:31089172	FYPO:0003268	decreased rate of mitotic spindle elongation	(Fig. 2C, D)
PMID:31089172	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Fig. 2E)
PMID:31089172	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 2E)
PMID:31089172	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 2E)
PMID:31089172	FYPO:0002060	viable vegetative cell population	(Fig. 3)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:31089172	FYPO:0002060	viable vegetative cell population	(Fig. 3)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:31089172	FYPO:0004692	normal protein localization to mitotic spindle midzone [assayed_using] PomBase:SPBC15D4.01c	(Fig. 4)
PMID:31089172	FYPO:0004753	abolished protein localization to nucleus during mitotic interphase [assayed_using] PomBase:SPBC15D4.01c	(Fig. 4)
PMID:31089172	FYPO:0004833	decreased protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPBC15D4.01c	(Fig. 4)
PMID:31089172	FYPO:0002060	viable vegetative cell population	(Fig. 4A)
PMID:31089172	GO:1990023	mitotic spindle midzone [exists_during] mitotic anaphase	(Fig. 4A)
PMID:31089172	GO:0005654	nucleoplasm [exists_during] mitotic metaphase	(Fig. 4A)
PMID:31089172	GO:0005654	nucleoplasm [exists_during] mitotic interphase	(Fig. 4A)
PMID:31089172	FYPO:0006919	normal protein localization to nucleus during mitotic interphase [assayed_using] PomBase:SPBC15D4.01c	(Fig. 5B, C)
PMID:31089172	FYPO:0003350	abolished protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPBC15D4.01c	(Fig. 5B, C)
PMID:31089172	FYPO:0003350	abolished protein localization to mitotic spindle midzone during anaphase B [assayed_using] PomBase:SPBC15D4.01c	(Fig. 5B, C)
PMID:31089172	FYPO:0006919	normal protein localization to nucleus during mitotic interphase [assayed_using] PomBase:SPBC15D4.01c	(Fig. 5B, C)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Fig. 5D and Supplementary Fig. S2A,C)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Fig. 5D and Supplementary Fig. S2A,C)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Fig. 5D and Supplementary Fig. S2A,C)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Fig. 5D and Supplementary Fig. S2A,C)
PMID:31089172	FYPO:0006917	normal onset of mitotic metaphase/anaphase transition	(Fig. 6)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Fig. 6)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Fig. 6)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Fig. 6)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Figure 4A)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Figure 4A)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Figure 4A)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Figure 4A)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Figure 4A)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Figure 4A)
PMID:31089172	FYPO:0002061	inviable vegetative cell population	(Figure 4A)
PMID:31089172	FYPO:0004753	abolished protein localization to nucleus during mitotic interphase [assayed_using] PomBase:SPBC15D4.01c	(Figure 4A, B)
PMID:31089172	FYPO:0004833	decreased protein localization to mitotic spindle midzone during anaphase B	(Figure 4A, B)
PMID:31089172	FYPO:0006918	abolished protein localization to nucleoplasm during mitotic interphase	(Figure 4A, B)
PMID:31089172	FYPO:0004753	abolished protein localization to nucleus during mitotic interphase [assayed_using] PomBase:SPBC15D4.01c	(Figure 4A, B)
PMID:31089172	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Figure 4A, B)
PMID:31089172	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Figure 4A, B)
PMID:31089172	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Figure 4A, B)
PMID:31089172	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Figure 4A, B)
PMID:31089172	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Figure 4A, B)
PMID:31089172	FYPO:0004753	abolished protein localization to nucleus during mitotic interphase [assayed_using] PomBase:SPAC25G10.07c	(Figure 4A, B)
PMID:31089172	FYPO:0004753	abolished protein localization to nucleus during mitotic interphase [assayed_using] PomBase:SPBC15D4.01c	(Figure 4A, B)
PMID:31089172	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Figure 5E)
PMID:31089172	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Figure 5E)
PMID:31089172	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Figure 5E)
PMID:31089172	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Figure 5E)
PMID:31089172	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Figure 6C-E)
PMID:31089172	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] high	(Figure 6C-E)
PMID:31116668	GO:0031520	plasma membrane of cell tip	(Fig. 1d) (comment: vw: localized by the secretory pathway)
PMID:31116668	FYPO:0006447	abolished protein localization to cleavage furrow during vegetative growth [assayed_using] PomBase:SPAC1F7.03	(Fig. 1e)
PMID:31116668	FYPO:0006005	normal actomyosin contractile ring localization	(Fig. 4)
PMID:31116668	GO:0009992	intracellular water homeostasis	(Fig. 5)
PMID:31116668	FYPO:0006899	asymmetric cell separation after cytokinesis	(Fig. 5c)
PMID:31131414	FYPO:0002019	elongated telomeres during vegetative growth	(comment: CONDITION Southern blot) (comment: same as rap1-7A single mutant)
PMID:31149897	FYPO:0006923	normal DNA recombination frequency at mitotic DNA replication fork barriers	(Fig. 3)
PMID:31149897	FYPO:0000167	increased DNA recombination at mitotic DNA replication fork barriers	(Fig. 4)
PMID:31149897	FYPO:0006921	decreased gene conversion at mitotic DNA replication fork barriers [has_severity] low	(Fig. 4)
PMID:31149897	FYPO:0000167	increased DNA recombination at mitotic DNA replication fork barriers	(Fig. 4)
PMID:31149897	FYPO:0000167	increased DNA recombination at mitotic DNA replication fork barriers	(Fig. 4) (comment: very small difference from fbh1delta alone)
PMID:31149897	FYPO:0006925	decreased number of Rad51 foci at mitotic DNA replication fork barriers	(Fig. 5)
PMID:31149897	FYPO:0006924	decreased number of Rad52 foci at mitotic DNA replication fork barriers	(Fig. 5)
PMID:31149897	FYPO:0006921	decreased gene conversion at mitotic DNA replication fork barriers	(Fig. 6)
PMID:31149897	FYPO:0006921	decreased gene conversion at mitotic DNA replication fork barriers	(Fig. 6)
PMID:31149897	FYPO:0000473	increased mitotic recombination	(Figure 3A) (comment: CHECK increased spontaneous direct repeat recombination)
PMID:31149897	FYPO:0006922	abnormal DNA clamp unloading	PCNA foci persist longer than normal, and form large bright patches before disappearing (Fig 2).
PMID:31149897	FYPO:0006920	decreased DNA recombination at mitotic DNA replication fork barriers	elg1∆ exhibits reduced direct repeat recombination associated with replication fork collapse at the RTS1 replication fork barrier
PMID:31178220	GO:1901612	cardiolipin binding	SpTam41 interacts strongly with cardiolipin
PMID:31201205	GO:0005783	endoplasmic reticulum	(Fig. 2)
PMID:31201205	GO:0005635	nuclear envelope	(Fig. 2)
PMID:31201205	GO:0005783	endoplasmic reticulum	(Fig. 2)
PMID:31201205	GO:0005886	plasma membrane	(Fig. 2)
PMID:31201205	GO:0005886	plasma membrane	(Fig. 2)
PMID:31201205	GO:0005635	nuclear envelope	(Fig. 2)
PMID:31201205	FYPO:0002061	inviable vegetative cell population	(Fig. 2B,C)
PMID:31201205	FYPO:0002061	inviable vegetative cell population	(Fig. 2B,C)
PMID:31201205	FYPO:0002061	inviable vegetative cell population	(Fig. 2B,C)
PMID:31201205	FYPO:0002061	inviable vegetative cell population	(Fig. 2B,C)
PMID:31201205	FYPO:0002061	inviable vegetative cell population	(Fig. 2B,C)
PMID:31201205	FYPO:0006579	sensitive to manganese [has_severity] low	(Figure 4)
PMID:31201205	FYPO:0001020	normal growth on calcium [has_severity] high	(Figure 4)
PMID:31201205	FYPO:0006579	sensitive to manganese [has_severity] high	(Figure 4)
PMID:31201205	FYPO:0001020	normal growth on calcium [has_severity] high	(Figure 4)
PMID:31201205	FYPO:0006579	sensitive to manganese [has_severity] high	(Figure 4)
PMID:31201205	FYPO:0006579	sensitive to manganese [has_severity] low	(Figure 4)
PMID:31201205	FYPO:0006579	sensitive to manganese [has_severity] low	(Figure 4)
PMID:31201205	FYPO:0002251	inviable swollen elongated vegetative cell	(Figure 5)
PMID:31201205	FYPO:0002903	viable pear-shaped vegetative cell	(Figure 5) (vw: changed to pear, descendent of spherical)
PMID:31201205	FYPO:0004533	normal cell wall beta-glucan level [has_severity] high	(Figure 6)
PMID:31201205	FYPO:0004860	increased cell wall beta-glucan level [has_severity] high	(Figure 6)
PMID:31201205	FYPO:0004860	increased cell wall beta-glucan level [has_severity] medium	(Figure 6)
PMID:31201205	FYPO:0002060	viable vegetative cell population	(Figure 7)
PMID:31201205	FYPO:0006660	loss of viability upon G0 to G1 transition	(Figure 7B)
PMID:31201205	FYPO:0006660	loss of viability upon G0 to G1 transition	(Figure 7B)
PMID:31201205	FYPO:0002048	normal cell morphology during nitrogen starvation	(Figure 7B) small viable
PMID:31201205	FYPO:0006935	viable cell with normal cell morphology during nitrogen starvation	(Figure 7B) small, viable
PMID:31201205	FYPO:0002903	viable pear-shaped vegetative cell	(comment: CHECK small viable)
PMID:31201205	FYPO:0001234	slow vegetative cell population growth	The resulting cwh43 pdt1Δ 201 double mutant partly recovered colony formation capacity at 36°C, compared to that of the 202 cwh43 single mutant (Fig. 2D).
PMID:31206516	FYPO:0007477	abnormal epigenetic heterochromatin inheritance [has_penetrance] 38.3	(comment: vw: variegated population) These results suggested that the white phenotype of W70 was not linked to otr1R::ade6+. The re-appearance of red colonies from epe1Δ W70 cells (Fig 1C) suggested that the white phenotype was due to epigenetic rather than genetic alterations.
PMID:31206516	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPCC622.16c [has_severity] high	FLAG ChIP analysis revealed that H297A reduced appreciably Epe1 enrichment on centromeric dg repeats and IRC3 (Fig 4G), a centromeric boundary sequence where Epe1 accumulates to a high level [12, 14
PMID:31206516	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC622.16c [assayed_protein] PomBase:SPAC664.01c	However, consistent with the previous report [13], the C-terminal half of Epe1 (487-948 amino acids region) interacted with Swi6 in the yeast two-hybrid system, but the N-terminal half (1-486) did not (S4I Fig).
PMID:31206516	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC622.16c [assayed_protein] PomBase:SPAC664.01c	However, consistent with the previous report [13], the C-terminal half of Epe1 (487-948 amino acids region) interacted with Swi6 in the yeast two-hybrid system, but the N-terminal half (1-486) did not (S4I Fig).
PMID:31206516	FYPO:0007479	normal epigenetic heterochromatin inheritance	However, how Epe1 finds target sites to prevent ectopic heterochromatin formation is unknown. Since Epe1 physically interacts with the bromodomain protein Bdf2, which is required for heterochromatin-euchromatin boundary formation [14], we predicted that Bdf2 would recruit Epe1 to the target sites. However, bdf2Δ cells showed an almost uniform red phenotype in the ade6-m210 background (S4H Fig), suggesting that Bdf2 was not related to suppression of variegation and ectopic heterochromatin formation.
PMID:31206516	FYPO:0007479	normal epigenetic heterochromatin inheritance	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0007479	normal epigenetic heterochromatin inheritance	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0007479	normal epigenetic heterochromatin inheritance	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0007479	normal epigenetic heterochromatin inheritance	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0007479	normal epigenetic heterochromatin inheritance	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0007479	normal epigenetic heterochromatin inheritance	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0007479	normal epigenetic heterochromatin inheritance	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0007479	normal epigenetic heterochromatin inheritance	Loss of Clr4 abolished red-white variegation in the epe1Δ ade6-m210 background, indicating a requirement for the H3K9 methyltransferase Clr4. clr3 and sir2, which encode histone deacetylases, are required for self-propagation of heterochromatin [30-34]. The introduction of clr3Δ or sir2Δ into the epe1Δ background also induced a uniform red phenotype. Similarly, loss of Swi6 suppressed variegation.
PMID:31206516	FYPO:0004749	increased spatial extent of subtelomeric heterochromatin assembly [has_severity] variable severity	Since loss of Epe1 increases H3K9me levels at subtel1L and 2L [23, 24], we hypothesized that the ade5 gene was silenced by ectopically deposited H3K9me, which arrested red pigment formation.
PMID:31206516	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC664.01c [assayed_protein] PomBase:SPCC622.16c [has_severity] low	The H297A substitution slightly impaired the interaction (S4G Fig), which was confirmed by the results of a bait-prey exchange experiment. We performed co-immunoprecipitation analysis of Swi6 with Epe1H297A. Consistent with the results of yeast two-hybrid assay, the Epe1H297A mutant interacted with Swi6 with a slightly lower efficiency than wild-type Epe1 (Fig 4H).
PMID:31206516	GO:0033696	heterochromatin boundary formation	Thus, we concluded that ectopic heterochromatin-mediated repression of ade5 caused the white phenotype of the epe1Δ W70 strain.
PMID:31206516	FYPO:0007477	abnormal epigenetic heterochromatin inheritance [has_penetrance] 3.8	Unlike loss of Epe1, the H297A mutation generated few pink/white colonies in the ade6-m210 background (Fig 4A); indeed, 96.2% of Epe1H297A cells formed WT-like red colonies, while 61.7% of epe1Δ cells did.
PMID:31206516	FYPO:0002876	decreased transcription	We found that deletion of the N-terminal 171 amino acids (Epe1ΔN) abolished transcriptional activation by Epe1 and the N-terminal 208 amino acids (Epe1N208) activated transcription of the HIS3 reporter independently of JmjC (Fig 4I), suggesting that the N-terminal 171 amino acids region is required for the transcriptional activation activity.
PMID:31206516	FYPO:0007477	abnormal epigenetic heterochromatin inheritance [has_penetrance] 20	We introduced Epe1ΔN into ade6-m210 cells to examine the effect of the ΔN mutation on the suppression of ectopic heterochromatin formation. Epe1ΔN cells formed pink/white colonies with a slightly lower frequency than epe1Δ cells (Fig 4K), indicating that the NTA domain contributed to the suppression of ectopic heterochromatin-mediated variegation.
PMID:31206516	FYPO:0007477	abnormal epigenetic heterochromatin inheritance [has_severity] variable severity	We next examined the requirement for Ago1 and Taz1 for epe1Δ-induced variegation, because both factors are involved in subtelomeric constitutive heterochromatin formation [5]. epe1Δ ago1Δ, epe1Δ taz1Δ, and epe1Δ ago1Δ taz1Δ strains displayed red-white variegated phenotypes (S2A and S2B Fig), indicating that neither RNAi nor Taz1 was essential for epe1Δ- induced variegation.
PMID:31206516	FYPO:0007477	abnormal epigenetic heterochromatin inheritance [has_severity] variable severity	We next examined the requirement for Ago1 and Taz1 for epe1Δ-induced variegation, because both factors are involved in subtelomeric constitutive heterochromatin formation [5]. epe1Δ ago1Δ, epe1Δ taz1Δ, and epe1Δ ago1Δ taz1Δ strains displayed red-white variegated phenotypes (S2A and S2B Fig), indicating that neither RNAi nor Taz1 was essential for epe1Δ- induced variegation.
PMID:31206516	FYPO:0007477	abnormal epigenetic heterochromatin inheritance [has_severity] variable severity	We next examined the requirement for Ago1 and Taz1 for epe1Δ-induced variegation, because both factors are involved in subtelomeric constitutive heterochromatin formation [5]. epe1Δ ago1Δ, epe1Δ taz1Δ, and epe1Δ ago1Δ taz1Δ strains displayed red-white variegated phenotypes (S2A and S2B Fig), indicating that neither RNAi nor Taz1 was essential for epe1Δ- induced variegation.
PMID:31217286	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] 85	(Fig. 1)
PMID:31217286	FYPO:0007677	abnormal sterol distribution	(Fig. 1C)
PMID:31217286	FYPO:0002318	increased cellular ergosterol level [has_penetrance] high	(Fig. 1D)
PMID:31217286	FYPO:0000231	abnormal actomyosin contractile ring myosin filament organization [has_penetrance] 76	(Fig. 2)
PMID:31217286	FYPO:0002560	abnormal protein localization to actomyosin contractile ring [has_penetrance] 75 [assayed_protein] PomBase:SPBC1A4.05	(Fig. 2)
PMID:31217286	FYPO:0002032	abnormal actin cable morphology during mitosis [has_penetrance] 75	(Fig. 3)
PMID:31217286	FYPO:0002560	abnormal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPCC4B3.15	(Fig. 4A)
PMID:31217286	FYPO:0002560	abnormal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPAC4F8.13c	(Fig. 4B)
PMID:31217286	FYPO:0002560	abnormal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPAC20G8.05c	(Fig. 4C)
PMID:31217286	FYPO:0002560	abnormal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPAC1F5.04c	(Fig. 5A)
PMID:31217286	FYPO:0008169	normal actin cable morphology during mitotic interphase	(Fig. 6A, 6B)
PMID:31217286	FYPO:0004738	abnormal actomyosin contractile ring organization [has_penetrance] 70	(Fig. 6C)
PMID:31217286	FYPO:0004738	abnormal actomyosin contractile ring organization [has_penetrance] 45	(Fig. 6C)
PMID:31217286	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] 75	(Fig. 6D)
PMID:31217286	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] 10	(Fig. 6D)
PMID:31217286	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] 40	(Fig. S1C)
PMID:31217286	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] 40	(Fig. S1C)
PMID:31217286	GO:0005783	endoplasmic reticulum	(Fig. S1D)
PMID:31217286	FYPO:0000805	abnormal endoplasmic reticulum organization [has_penetrance] 80 [assayed_protein] PomBase:SPAC630.08c	(Fig. S1E, S1F)
PMID:31217286	FYPO:0002318	increased cellular ergosterol level [has_penetrance] high	(Fig. S6)
PMID:31217286	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] 10	Phenotype of Erg25 overexpression is suppressed by Erg11 inhibition. Fig. 1E
PMID:31239353	FYPO:0007044	decreased alkaline phosphatase activity during stress response to zinc ion	(Fig. 1)
PMID:31239353	FYPO:0007045	decreased alkaline phosphatase activity during cellular response to zinc ion starvation	(Fig. 1)
PMID:31239353	FYPO:0007044	decreased alkaline phosphatase activity during stress response to zinc ion	(Fig. 1)
PMID:31239353	FYPO:0007045	decreased alkaline phosphatase activity during cellular response to zinc ion starvation [has_severity] high	(Fig. 1) (comment: CHECK abolished?)
PMID:31239353	GO:0004035	alkaline phosphatase activity	(Figure 1A)
PMID:31239353	FYPO:0007049	decreased RNA level during stress response to zinc ion [assayed_using] PomBase:SPBC14F5.13c	(Figure 1B and 1C)
PMID:31239353	FYPO:0006334	decreased RNA level during cellular response to zinc ion starvation [assayed_using] PomBase:SPBC14F5.13c	(Figure 1B and 1C)
PMID:31239353	FYPO:0007067	decreased protein level during stress response to zinc ion [assayed_using] PomBase:SPBC14F5.13c	(Figure 2B)
PMID:31239353	FYPO:0001422	decreased protein processing during vegetative growth [has_severity] high [assayed_using] PomBase:SPBC14F5.13c	(Figure 4) ....although processing of Pho8 is dependent upon the growth phase of cells, zinc is the major factor that limits Pho8 activity in vivo
PMID:31239353	FYPO:0001422	decreased protein processing during vegetative growth [has_severity] high [assayed_using] PomBase:SPBC14F5.13c	(Figure 4) hat although processing of Pho8 is dependent upon the growth phase of cells, zinc is the major factor that limits Pho8 activity in vivo
PMID:31239353	FYPO:0007043	abolished alkaline phosphatase activity	(Figure 5B)
PMID:31239353	FYPO:0007043	abolished alkaline phosphatase activity	(Figure 5B)
PMID:31239353	FYPO:0007054	normal protein level during cellular response to zinc ion starvation [assayed_using] PomBase:SPBC14F5.13c	(Figure 5D)
PMID:31239353	FYPO:0007053	decreased protein level during cellular response to zinc ion starvation [assayed_using] PomBase:SPBC14F5.13c [has_severity] low	(Figure 5D)
PMID:31239353	FYPO:0007048	normal alkaline phosphatase activity during stress response to zinc ion	(Figure 7)
PMID:31239353	FYPO:0007047	normal alkaline phosphatase activity	(Figure 7)
PMID:31239353	FYPO:0007048	normal alkaline phosphatase activity during stress response to zinc ion	(Figure 7)
PMID:31239353	FYPO:0007041	increased alkaline phosphatase activity	(Figure 8)
PMID:31239353	GO:0106219	zinc ion sensor activity	(comment: CHECK DIRECTLY_ACTIVATES pho8 GO:0004035) As zinc did not affect Pho8 stability, processing, or dimerization, we hypothesized that the activity of Pho8 is directly affected by cellular zinc status. .. .....Taken together these results are consistent with yeast maintaining an inactive 5 Zinc-dependent alkaline phosphatase activity pool of Pho8 in low zinc, which can be rapidly activated as soon as zinc is available.
PMID:31239353	GO:0004035	alkaline phosphatase activity	(comment: CHECK Figure 1A Zinc-dependent)
PMID:31239353	FYPO:0007045	decreased alkaline phosphatase activity during cellular response to zinc ion starvation [has_severity] high	(comment: CHECK abolished ?)
PMID:31239353	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [has_input] PomBase:SPBC14F5.13c [part_of] negative regulation of transcription initiation by RNA polymerase II [part_of] cellular response to zinc ion	(comment: pho8 transcript and protein levels are increased in high zinc BUT ZINC DEPENDENT CHAnges are independent of transcript levels)
PMID:31239353	FYPO:0007052	increased protein level during stress response to zinc ion [assayed_using] PomBase:SPBC14F5.13c	Pho8 abundance is increased in high zinc in a loz1 deletion strain (Figure 2B and 2C)
PMID:31239353	FYPO:0007050	increased RNA level during stress response to zinc ion [assayed_using] PomBase:SPBC14F5.13c	consistent with Loz1 facilitating the repression of pho8 gene expression in high zinc (Figure 2A)
PMID:31239353	FYPO:0007044	decreased alkaline phosphatase activity during stress response to zinc ion	reduced alkaline phosphatase activity and Pho8 dimerization (Figures 6C and 6D)
PMID:31239353	FYPO:0007044	decreased alkaline phosphatase activity during stress response to zinc ion	reduced alkaline phosphatase activity and Pho8 dimerization (Figures 6C and 6D)
PMID:31239353	FYPO:0007042	decreased alkaline phosphatase activity	reduced during conditions of zinc shock (Figure 8 and Figure 9). (comment: as Pho8 binds its zinc cofactors inside of the secretory pathway, it activity is dependent upon zinc transporters that supply zinc ions to the secretory pathway)
PMID:31257143	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint [has_penetrance] 80	(Figure 2B) (comment: demonstrates robust arrest 3b 80% 12 hours)
PMID:31257143	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Figure 2B) (comment: demonstrates robust arrest)
PMID:31257143	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Figure 2D)
PMID:31257143	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Figure 2d)
PMID:31257143	FYPO:0004318	abolished mitotic spindle assembly checkpoint	(Figure 2d)
PMID:31257143	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPCC1795.01c	(Figure S4)
PMID:31257143	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC1322.12c [assayed_using] PomBase:SPCC1795.01c	(Figure S4)
PMID:31257143	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Figures S3B and S3C)
PMID:31257143	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Figures S3B and S3D)
PMID:31257143	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint [has_penetrance] 80	3b (comment: 80% 12 hours)
PMID:31260531	GO:0062070	SAGA complex binding [part_of] SAGA complex localization to transcription regulatory region	(comment: Rep2 locates SAGA complex at MBF-regulated promoters.)
PMID:31260531	GO:0000785	chromatin [coincident_with] MCB [exists_during] mitotic G1 phase	(comment: chromatin association at MCBs is part of positive regulation of G1/S transition of mitotic cell cycle)
PMID:31262821	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 3A)
PMID:31262821	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 3A)
PMID:31262821	FYPO:0001690	normal growth on camptothecin	(Fig. 3A)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 3A)
PMID:31262821	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 3A)
PMID:31262821	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 3A)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 3A)
PMID:31262821	FYPO:0000963	normal growth on hydroxyurea	(Fig. 3A)
PMID:31262821	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 3A)
PMID:31262821	FYPO:0007814	increased rate of mitotic DNA replication elongation during cellular response to hydroxyurea	(Fig. 3C)
PMID:31262821	FYPO:0010016	increased replication fork stalling during cellular response to DNA damage	(Fig. 3E)
PMID:31262821	GO:0120292	positive regulation of mitotic recombination-dependent replication fork processing [happens_during] mitotic S phase	(Fig. 4)
PMID:31262821	FYPO:0010012	increased histone H2B-K33 acetylation during vegetative growth [has_severity] low	(Fig. 4A)
PMID:31262821	FYPO:0010012	increased histone H2B-K33 acetylation during vegetative growth [has_severity] medium	(Fig. 4A)
PMID:31262821	FYPO:0010017	normal histone H2B-K33 acetylation during vegetative growth	(Fig. 4A)
PMID:31262821	FYPO:0010012	increased histone H2B-K33 acetylation during vegetative growth [has_severity] high	(Fig. 4A)
PMID:31262821	FYPO:0010017	normal histone H2B-K33 acetylation during vegetative growth	(Fig. 4A)
PMID:31262821	FYPO:0010017	normal histone H2B-K33 acetylation during vegetative growth	(Fig. 4A)
PMID:31262821	FYPO:0010017	normal histone H2B-K33 acetylation during vegetative growth	(Fig. 4A)
PMID:31262821	GO:0004407	histone deacetylase activity [has_input] PomBase:SPCC622.09 [part_of] positive regulation of mitotic recombination-dependent replication fork processing	(Fig. 4B)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 4B)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 4B)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 4B)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 4B)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 4C)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 4C)
PMID:31262821	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 4C)
PMID:31262821	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 4C)
PMID:31262821	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 4C)
PMID:31262821	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 4C)
PMID:31262821	FYPO:0000963	normal growth on hydroxyurea	(Fig. 4C)
PMID:31262821	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 4C)
PMID:31262821	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 4C)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 4C)
PMID:31262821	FYPO:0010016	increased replication fork stalling during cellular response to DNA damage [has_severity] low	(Fig. 4D)
PMID:31262821	FYPO:0010016	increased replication fork stalling during cellular response to DNA damage [has_severity] low	(Fig. 4D)
PMID:31262821	FYPO:0010016	increased replication fork stalling during cellular response to DNA damage [has_severity] high	(Fig. 4D)
PMID:31262821	FYPO:0001903	normal septation index	(Fig. 5A)
PMID:31262821	FYPO:0001128	decreased septation index	(Fig. 5A)
PMID:31262821	FYPO:0001903	normal septation index	(Fig. 5A)
PMID:31262821	FYPO:0001903	normal septation index	(Fig. 5A)
PMID:31262821	FYPO:0002095	increased protein phosphorylation during cellular response to DNA damage [assayed_protein] PomBase:SPCC18B5.11c	(Fig. 5B)
PMID:31262821	FYPO:0010017	normal histone H2B-K33 acetylation during vegetative growth	(Fig. 5C)
PMID:31262821	FYPO:0010017	normal histone H2B-K33 acetylation during vegetative growth	(Fig. 5C)
PMID:31262821	FYPO:0010017	normal histone H2B-K33 acetylation during vegetative growth	(Fig. 5C)
PMID:31262821	FYPO:0010017	normal histone H2B-K33 acetylation during vegetative growth	(Fig. 5C)
PMID:31262821	FYPO:0010017	normal histone H2B-K33 acetylation during vegetative growth	(Fig. 5C)
PMID:31262821	FYPO:0010017	normal histone H2B-K33 acetylation during vegetative growth	(Fig. 5C)
PMID:31262821	FYPO:0010017	normal histone H2B-K33 acetylation during vegetative growth	(Fig. 5C)
PMID:31262821	FYPO:0010017	normal histone H2B-K33 acetylation during vegetative growth	(Fig. 5C)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 5F)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 5F)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 5F)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 5F)
PMID:31262821	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 5G)
PMID:31262821	FYPO:0010011	increased DNA damage at rDNA during vegetative growth	(Fig. 6D)
PMID:31262821	FYPO:0006321	decreased protein localization to chromatin at stalled replication fork [assayed_protein] PomBase:SPAC17D4.02 [has_severity] medium	(Fig. 7B)
PMID:31262821	FYPO:0006321	decreased protein localization to chromatin at stalled replication fork [has_severity] low [assayed_protein] PomBase:SPBC25D12.03c	(Fig. 7B)
PMID:31262821	FYPO:0006321	decreased protein localization to chromatin at stalled replication fork [has_severity] low [assayed_protein] PomBase:SPAC17D4.02	(Fig. 7B)
PMID:31262821	FYPO:0005236	normal protein localization to chromatin at stalled replication fork [assayed_protein] PomBase:SPBC25D12.03c	(Fig. 7B)
PMID:31262821	FYPO:0005236	normal protein localization to chromatin at stalled replication fork [assayed_protein] PomBase:SPAC17D4.02	(Fig. 7B)
PMID:31262821	FYPO:0006321	decreased protein localization to chromatin at stalled replication fork [assayed_protein] PomBase:SPBC25D12.03c [has_severity] medium	(Fig. 7B)
PMID:31262821	FYPO:0006321	decreased protein localization to chromatin at stalled replication fork [assayed_protein] PomBase:SPBC25D12.03c [has_severity] medium	(Fig. 7C)
PMID:31262821	FYPO:0006321	decreased protein localization to chromatin at stalled replication fork [has_severity] low [assayed_protein] PomBase:SPBC25D12.03c	(Fig. 7C)
PMID:31262821	FYPO:0006321	decreased protein localization to chromatin at stalled replication fork [has_severity] low [assayed_protein] PomBase:SPAC17D4.02	(Fig. 7C)
PMID:31262821	FYPO:0006321	decreased protein localization to chromatin at stalled replication fork [assayed_protein] PomBase:SPAC17D4.02 [has_severity] medium	(Fig. 7C)
PMID:31269446	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0000080	decreased cell population growth at low temperature	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0000080	decreased cell population growth at low temperature	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0000080	decreased cell population growth at low temperature	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0007213	decreased histone H3-K9 dimethylation at heterochromatin island during vegetative growth	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0002664	increased level of stress responsive gene mRNA during vegetative growth	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0003049	increased transcriptional readthrough	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0003049	increased transcriptional readthrough	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0007213	decreased histone H3-K9 dimethylation at heterochromatin island during vegetative growth	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0002664	increased level of stress responsive gene mRNA during vegetative growth	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0003049	increased transcriptional readthrough	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0003049	increased transcriptional readthrough	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0002664	increased level of stress responsive gene mRNA during vegetative growth	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0007213	decreased histone H3-K9 dimethylation at heterochromatin island during vegetative growth	(comment: CONDITION 18 °C)
PMID:31269446	FYPO:0006612	decreased protein localization to chromatin at transcription termination site [assayed_using] rpb1/Phos(CTD-S2)	(comment: non-canonical termination sites)
PMID:31269446	FYPO:0006612	decreased protein localization to chromatin at transcription termination site [assayed_using] rpb1/Phos(CTD-S2)	(comment: non-canonical termination sites)
PMID:31269446	FYPO:0006612	decreased protein localization to chromatin at transcription termination site [assayed_using] rpb1/Phos(CTD-S2)	(comment: non-canonical termination sites)
PMID:31269446	GO:0090052	regulation of pericentric heterochromatin formation	(comment: si independent pericentric heterochromatin formation CPF and RNAi Act in Parallel to Assemble Centromeric Heterochromatin)
PMID:31269446	GO:0090052	regulation of pericentric heterochromatin formation	(comment: si independent pericentric heterochromatin formation CPF and RNAi Act in Parallel to Assemble Centromeric Heterochromatin)
PMID:31276301	FYPO:0007175	abolished protein localization to plasma membrane at cell division site during mitotic interphase [assayed_using] PomBase:SPAC144.14	(Fig. 4a)
PMID:31276301	FYPO:0007176	abolished protein localization to plasma membrane at cell division site during mitosis [assayed_using] PomBase:SPAC144.14	(Fig. 4a)
PMID:31276301	FYPO:0007181	normal protein localization to cell division site during mitotic anaphase [assayed_using] PomBase:SPAC144.14	(Fig. 4b)
PMID:31276301	FYPO:0006636	mislocalized protein distributed in cell cortex [assayed_using] PomBase:SPAC144.14	(Fig. 4d)
PMID:31276301	FYPO:0007178	abolished protein localization to medial cortex during mitosis [assayed_using] PomBase:SPAC144.14	(Fig. 4e)
PMID:31276301	FYPO:0007179	mislocalized protein distributed in cell cortex during mitotic interphase [assayed_using] PomBase:SPBC1A4.05	(Fig. 4e)
PMID:31276301	FYPO:0007177	abolished protein localization to medial cortex during mitotic interphase [assayed_using] PomBase:SPAC144.14	(Fig. 4e)
PMID:31276301	FYPO:0002215	viable curved elongated vegetative cell	(Fig. 6)
PMID:31276301	FYPO:0005880	long interphase microtubules curved around cell end	(Fig. 6)
PMID:31276301	FYPO:0004622	abolished mitotic spindle disassembly	(Figure 7b)
PMID:31276301	FYPO:0004097	normal actomyosin contractile ring contraction	(Figure S1a)
PMID:31276301	FYPO:0002060	viable vegetative cell population	(Figure S1a)
PMID:31276301	FYPO:0003702	normal microtubule cytoskeleton morphology during vegetative growth	(Figure S1a)
PMID:31276301	FYPO:0003717	normal actin cytoskeleton morphology during vegetative growth	(Figure S1a)
PMID:31276301	FYPO:0004652	normal actomyosin contractile ring morphology	(Figure S1a)
PMID:31276301	FYPO:0007182	decreased cytoplasmic microtubule depolymerization at plus end at cell tip	(Table 3)
PMID:31276301	FYPO:0003190	decreased rate of cytoplasmic microtubule depolymerization during vegetative growth	(Table 3)
PMID:31276301	FYPO:0000733	long mitotic spindle	Furthermore, abnormally elongated cytoplasmic and spindle MTs were frequently observed in these cells (Figure 6).
PMID:31276301	FYPO:0004429	normal rate of mitotic spindle elongation	Furthermore, abnormally elongated cytoplasmic and spindle MTs were frequently observed in these cells (Figure 6).
PMID:31276301	FYPO:0005706	increased duration of mitotic anaphase B	Table 2 Figures 5a-d and S2)
PMID:31276588	FYPO:0000047	normal cell population growth	(Figure 1B)
PMID:31276588	FYPO:0000080	decreased cell population growth at low temperature	(Figure 1B)
PMID:31276588	FYPO:0000080	decreased cell population growth at low temperature	(Figure 1B)
PMID:31276588	FYPO:0000047	normal cell population growth	(Figure 1B)
PMID:31276588	FYPO:0002244	abolished acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 1C)
PMID:31276588	FYPO:0002244	abolished acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 1C)
PMID:31276588	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 1C)
PMID:31276588	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 1C)
PMID:31276588	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1271.09	(Figure 1D)
PMID:31276588	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Figure 1D)
PMID:31276588	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Figure 1D)
PMID:31276588	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Figure 1D)
PMID:31276588	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Figure 1D)
PMID:31276588	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1271.09	(Figure 1D)
PMID:31276588	FYPO:0002059	inviable cell population	(Figure 1E)
PMID:31276588	FYPO:0002059	inviable cell population	(Figure 1E)
PMID:31276588	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 1F)
PMID:31276588	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 1F)
PMID:31276588	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 2A)
PMID:31276588	FYPO:0002061	inviable vegetative cell population	(Figure 2C)
PMID:31276588	FYPO:0002061	inviable vegetative cell population	(Figure 2C)
PMID:31276588	FYPO:0000080	decreased cell population growth at low temperature	(Figure 2C)
PMID:31276588	FYPO:0002061	inviable vegetative cell population	(Figure 2C)
PMID:31276588	FYPO:0002061	inviable vegetative cell population	(Figure 2C)
PMID:31276588	FYPO:0002061	inviable vegetative cell population	(Figure 2C)
PMID:31276588	FYPO:0002061	inviable vegetative cell population	(Figure 2C)
PMID:31276588	FYPO:0002061	inviable vegetative cell population	(Figure 2C)
PMID:31276588	FYPO:0000080	decreased cell population growth at low temperature	(Figure 2C)
PMID:31276588	FYPO:0002061	inviable vegetative cell population	(Figure 2C)
PMID:31276588	GO:0140463	chromatin-protein adaptor activity [part_of] positive regulation of transcription initiation by RNA polymerase II [part_of] intracellular phosphate ion homeostasis	(comment: CHECK target genes pho1, pho84, and tgp1)
PMID:31276588	GO:0140463	chromatin-protein adaptor activity [part_of] co-transcriptional lncRNA 3' end processing, cleavage and polyadenylation pathway [part_of] intracellular phosphate ion homeostasis	(comment: CHECK target genes repressing lncRNA)
PMID:31276588	GO:0052745	inositol phosphate phosphatase activity [part_of] intracellular phosphate ion homeostasis	Octo phosphatase IP8 is a relevant substrate for the Aps1 pyrophosphatase with respect to phosphate homeostasis.
PMID:31276588	GO:0180034	co-transcriptional lncRNA 3' end processing, cleavage and polyadenylation pathway	lncRNA. Specifically, it is hypothesized that loss of the Ser7-PO4 or Ser5-PO4 marks leads to precocious termination of prt lncRNA transcription prior to the pho1 promoter and loss of the Thr4-PO4 mark reduces termination and hence increases transcription across the pho1 promoter (8) (Figure 1A).
PMID:31278118	FYPO:0006670	meiotic cell cycle entry in haploid cell [has_penetrance] 24	(Fig. 1D, 1E)
PMID:31278118	FYPO:0006670	meiotic cell cycle entry in haploid cell [has_penetrance] 7	(Fig. 1D, 1E)
PMID:31278118	FYPO:0006670	meiotic cell cycle entry in haploid cell [has_penetrance] 15	(Fig. 1D, 1E)
PMID:31278118	FYPO:0006670	meiotic cell cycle entry in haploid cell [has_penetrance] 34	(Fig. 1d)
PMID:31278118	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_penetrance] medium	(Fig. 2B) (Figure S1B and Table S2). This variegated staining pattern is a characteristic of mutants that are known to be defective in the maintenance of heterochromatin and that show a reduction, but not loss, of H3K9me levels (Taneja et al. 2017). Indeed, ChIP analyses of H3K9 di- and trimethylation (H3K9me2/3) showed a reduction in heterochromatic H3K9 marks at or near mat2P in pds5D (Figure 2B).
PMID:31278118	FYPO:0003074	abolished protein localization to pericentric heterochromatin during vegetative growth [assayed_using] PomBase:SPAC110.02	(Fig. 5B) (comment: vw: moved pds5 to assayed target)
PMID:31278118	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 7)
PMID:31278118	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 7)
PMID:31278118	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Figure 4A) (comment: CHECK https://github.com/pombase/fypo/issues/3693)
PMID:31278118	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 6A)
PMID:31278118	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 6B)
PMID:31278118	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 6B)
PMID:31278118	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 6B)
PMID:31278118	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(Figure S5)
PMID:31278118	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(Figure S5) Moreover, when we deleted pds5 in cells lacking Eso1 and/or Wpl1, the levels of haploid meiosis displayed by double or triple mutants were comparable to that of single-mutant pds5D
PMID:31278118	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] medium	(Table 1)
PMID:31278118	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	Compared to the single ago1D or pds5D deletion mutants, the ago1D pds5D double mutant showed severe loss-of-silencing of Kint2::ura4+ (Figure S2C).
PMID:31278118	FYPO:0007278	normal protein localization to euchromatin [assayed_using] PomBase:SPAC110.02	However, the localization of Pds5 to euchromatic locations was unaffected in heterochromatin-deficient cells (Figure 5E)
PMID:31278118	FYPO:0007278	normal protein localization to euchromatin [assayed_using] PomBase:SPAC110.02	However, the localization of Pds5 to euchromatic locations was unaffected in heterochromatin-deficient cells (Figure 5E)
PMID:31278118	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] medium	Table1
PMID:31278118	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth [has_penetrance] medium	cells revealed that H3K9me2 was notably decreased at centromeres and telomeres in pds5D (Figure 3, A and B).
PMID:31278118	FYPO:0004137	decreased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth [has_penetrance] medium	cells revealed that H3K9me2 was notably decreased at centromeres and telomeres in pds5D (Figure 3, A and B).
PMID:31278118	FYPO:0006670	meiotic cell cycle entry in haploid cell [has_penetrance] medium	ue to their antagonistic roles in cohesion establishment, the lethality of eso1D can be suppressed by deletion of wpl1 (Feytout et al. 2011; Kagami et al. 2011). Whereas wpl1D did not show defects in heterochromatic silencing, the eso1D wpl1D double mutant showed derepression of mat2P::ura4+ and haploid meiosis similar to pds5D cells (Figure 6A)
PMID:31278118	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] medium	ue to their antagonistic roles in cohesion establishment, the lethality of eso1D can be suppressed by deletion of wpl1 (Feytout et al. 2011; Kagami et al. 2011). Whereas wpl1D did not show defects in heterochromatic silencing, the eso1D wpl1D double mutant showed derepression of mat2P::ura4+ and haploid meiosis similar to pds5D cells (Figure 6A)
PMID:31285271	GO:0016282	eukaryotic 43S preinitiation complex	(Fig. 2) (comment: Asc1 associates with polysomes.)
PMID:31285271	FYPO:0003125	decreased cytoplasmic translational initiation	(Fig. 4)
PMID:31285271	FYPO:0000046	decreased cell population growth	(Fig. 4h)
PMID:31285271	FYPO:0001234	slow vegetative cell population growth	(Fig. 4h)
PMID:31285271	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to heat	(Fig. 5) Asc1 colocalized with stress granule proteins in response to heat shock.
PMID:31285271	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC17A5.15c [assayed_using] PomBase:SPBC17A3.04c [has_severity] high	(Figure 1d)
PMID:31285271	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC17A5.15c [has_severity] high [assayed_using] PomBase:SPAC30C2.04	(Figure 1e)
PMID:31285271	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC17A5.15c	(Figure 2d)
PMID:31285271	FYPO:0007029	decreased protein localization to polysome [assayed_using] PomBase:SPAC30C2.04	(Figure 2d)
PMID:31285271	FYPO:0007029	decreased protein localization to polysome [assayed_using] PomBase:SPAC17A5.15c	(Figure 2d)
PMID:31285271	FYPO:0007029	decreased protein localization to polysome [assayed_using] PomBase:SPBC17A3.04c	(Figure 2d)
PMID:31285271	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC17A3.04c	(Figure 2d)
PMID:31285271	FYPO:0001645	decreased protein-protein interaction [has_severity] high [assayed_using] PomBase:SPAC30C2.04 [assayed_using] PomBase:SPBC17D11.05	(Figure 3a)
PMID:31285271	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC30C2.04 [assayed_using] PomBase:SPBC685.06 [has_severity] medium	(Figure 3a)
PMID:31285271	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC685.06 [has_severity] medium [assayed_using] PomBase:SPBC17D11.05	(Figure 3e)
PMID:31285271	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC685.06 [has_severity] medium [assayed_using] PomBase:SPAC17C9.03	(Figure 3e)
PMID:31285271	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC3G9.09c	(comment: 312c8af6293e302e 41 MB+WxZqtLoWkmNqZLfwtd2DBEh8) (Fig. 6)
PMID:31285271	GO:0001731	formation of translation preinitiation complex	(comment: CHECK cytoplasmic translation is a parent to this term)
PMID:31285271	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC30C2.04 [assayed_using] PomBase:SPAC3G9.09c	(commnet: 312c8af6293e302e 41 MB+WxZqtLoWkmNqZLfwtd2DBEh8) (Fig. 6f)
PMID:31289327	FYPO:0003803	decreased protein localization to telomere [assayed_using] PomBase:SPAC6F6.17	(Fig. 4a)
PMID:31289327	FYPO:0000012	mitotic G2/M phase transition delay	(Fig. 5)
PMID:31289327	FYPO:0000012	mitotic G2/M phase transition delay	(Fig. 5)
PMID:31289327	FYPO:0002019	elongated telomeres during vegetative growth	(Fig. S2)
PMID:31289327	FYPO:0002019	elongated telomeres during vegetative growth	(Fig. S2)
PMID:31289327	FYPO:0002019	elongated telomeres during vegetative growth	(Fig. S2)
PMID:31289327	FYPO:0002019	elongated telomeres during vegetative growth	(Fig. S2)
PMID:31294478	GO:0000785	chromatin [coincident_with] tRNA_gene	(Fig. 1A and F)
PMID:31294478	GO:0000785	chromatin [coincident_with] PomBase:SPSNRNA.06	(Fig. 1b) We have shown using ChIP-seq experiments that Sen1 associates with all types of RNA polymerase III-transcribed genes. This includes tRNA_genes, 5S rRNA_genes, snu6 and srp7 but not the TFIIIC-bound COC sites.
PMID:31294478	FYPO:0007013	normal mature 5S rRNA level	(Fig. 2b)
PMID:31294478	FYPO:0007014	normal mature 5.8S rRNA level	(Fig. 2b)
PMID:31294478	FYPO:0007013	normal mature 5S rRNA level	(Fig. 2b)
PMID:31294478	FYPO:0001134	normal mature 18S rRNA level	(Fig. 2b)
PMID:31294478	FYPO:0007012	normal mature 28S rRNA level	(Fig. 2b)
PMID:31294478	FYPO:0007013	normal mature 5S rRNA level	(Fig. 2b)
PMID:31294478	FYPO:0001134	normal mature 18S rRNA level	(Fig. 2b)
PMID:31294478	FYPO:0007012	normal mature 28S rRNA level	(Fig. 2b)
PMID:31294478	FYPO:0006748	decreased pre-tRNA level during vegetative growth [assayed_using] PomBase:SPATRNAPRO.02	(Fig. 2c, 5d)
PMID:31294478	FYPO:0006748	decreased pre-tRNA level during vegetative growth [assayed_using] PomBase:SPCTRNAARG.10	(Fig. 2c, 5d)
PMID:31294478	FYPO:0006748	decreased pre-tRNA level during vegetative growth [assayed_using] PomBase:SPBTRNATYR.04	(Fig. 2c, 5d)
PMID:31294478	FYPO:0006748	decreased pre-tRNA level during vegetative growth [assayed_using] PomBase:SPBTRNAARG.05	(Fig. 2c, 5d)
PMID:31294478	FYPO:0004032	increased protein localization to chromatin at rDNA [assayed_using] PomBase:SPBC2G5.07c	(Fig. 3)
PMID:31294478	FYPO:0004033	increased protein localization to chromatin at tRNA genes [assayed_using] PomBase:SPBC2G5.07c	(Fig. 3)
PMID:31294478	FYPO:0007016	increased protein localization to chromatin at 3' end of rRNA genes [assayed_using] PomBase:SPBC651.08c	(Fig. 4)
PMID:31294478	FYPO:0007016	increased protein localization to chromatin at 3' end of rRNA genes [assayed_using] PomBase:SPAC4G9.08c	(Fig. 4)
PMID:31294478	FYPO:0007015	increased protein localization to chromatin at 3' end of tRNA genes [assayed_using] PomBase:SPBC651.08c	(Fig. 4)
PMID:31294478	FYPO:0007015	increased protein localization to chromatin at 3' end of tRNA genes [assayed_using] PomBase:SPAC4G9.08c	(Fig. 4)
PMID:31294478	FYPO:0002061	inviable vegetative cell population	(Figure 5B)
PMID:31294478	GO:0000785	chromatin [coincident_with] rRNA_gene	(comment: CHECK COINCIDENT WITH 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472)
PMID:31294478	GO:0000785	chromatin [coincident_with] rRNA_gene	(comment: CHECK coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472)
PMID:31294478	GO:0000785	chromatin [coincident_with] rRNA_gene	(comment: CHECK coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472)
PMID:31294478	GO:0000785	chromatin [coincident_with] rRNA_gene	(comment: CHECK coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472)
PMID:31294478	GO:0000785	chromatin [coincident_with] rRNA_gene	(comment: CHECK coincident with 5S_rRNA_gene NTR https://github.com/The-Sequence-Ontology/SO-Ontologies/issues/472)
PMID:31294478	FYPO:0006984	increased transcriptional readthrough at RNA polymerase III-transcribed genes [assayed_using] PomBase:SPCTRNAARG.10	AL fig 4. (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	FYPO:0006984	increased transcriptional readthrough at RNA polymerase III-transcribed genes [assayed_using] PomBase:SPATRNAPRO.02	AL fig 4. (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	FYPO:0006984	increased transcriptional readthrough at RNA polymerase III-transcribed genes [assayed_using] PomBase:SPBTRNATYR.04	AL fig 4. (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	FYPO:0006984	increased transcriptional readthrough at RNA polymerase III-transcribed genes [assayed_using] PomBase:SPCTRNAARG.10	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	FYPO:0006984	increased transcriptional readthrough at RNA polymerase III-transcribed genes [assayed_using] PomBase:SPCTRNASER.09	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	FYPO:0006984	increased transcriptional readthrough at RNA polymerase III-transcribed genes [assayed_using] PomBase:SPBTRNATYR.04	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	FYPO:0006984	increased transcriptional readthrough at RNA polymerase III-transcribed genes [assayed_using] PomBase:SPATRNAPRO.02	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	FYPO:0006984	increased transcriptional readthrough at RNA polymerase III-transcribed genes [assayed_using] PomBase:SPNCRNA.98	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	FYPO:0006984	increased transcriptional readthrough at RNA polymerase III-transcribed genes [assayed_using] PomBase:SPRRNA.37	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	FYPO:0006984	increased transcriptional readthrough at RNA polymerase III-transcribed genes [assayed_using] PomBase:SPCTRNATHR.10	AL fig 4. and 5c (comment: vincent: We have assayed the presence of read-through transcripts at SPATRNAPRO.02, SPCTRNAARG.10, SPBTRNATYR.04, SPBTRNAARG.05, SPCTRNASER.09, SPCTRNATHR.10 using strand-specific RT-qPCR. We also used Northern blots and 3' RACE to confirm the presence of read-through transcripts at SPATRNAPRO.02.)
PMID:31294478	GO:0030874	nucleolar chromatin	ChIP-qPCR of Dbl8 indicates that Dbl8 is enriched at the rDNA and at highly-expressed RNAPII-transcribed genes
PMID:31294800	GO:0035925	mRNA 3'-UTR AU-rich region binding	(comment: UAAU motif)
PMID:31315658	FYPO:0006518	loss of viability in G0	(Fig. 1c)
PMID:31315658	FYPO:0006518	loss of viability in G0	Additional file 1: Fig. S1b, c
PMID:31315658	FYPO:0006518	loss of viability in G0	Additional file 1: Fig. S1b, c
PMID:31315658	FYPO:0006518	loss of viability in G0	Additional file 1: Fig. S1b, c
PMID:31315658	FYPO:0007471	abnormal heterochromatin organization during G0	In sharp contrast, the H3K9me2 levels remained constant in leo1∆ cells throughout G0 phase (Fig. 2; Additional file 2: Fig. S2
PMID:31332096	FYPO:0003814	abolished response to S-phase DNA damage checkpoint signaling [has_penetrance] high	(comment: elimination of Rad3-specific phosphorylation)|
PMID:31332096	FYPO:0004372	decreased response to mitotic G2 DNA damage checkpoint signaling	(comment: reduced chk1 phosphorylation)
PMID:31341193	GO:0006895	Golgi to endosome transport [has_input] PomBase:SPBC16C6.06 [has_input] PomBase:SPAC24C9.08	(Fig. 1)
PMID:31341193	GO:0006895	Golgi to endosome transport [has_input] PomBase:SPBC16C6.06 [has_input] PomBase:SPAC24C9.08	(Fig. 1)
PMID:31341193	GO:0006895	Golgi to endosome transport [has_input] PomBase:SPBC16C6.06 [has_input] PomBase:SPAC24C9.08	(Fig. 1)
PMID:31341193	GO:0042147	retrograde transport, endosome to Golgi [has_input] PomBase:SPBC16C6.06	(Fig. 1)
PMID:31341193	GO:0042147	retrograde transport, endosome to Golgi [has_input] PomBase:SPBC16C6.06	(Fig. 1)
PMID:31341193	GO:0005770	late endosome	(Fig. 1) (comment: major)
PMID:31341193	GO:0005802	trans-Golgi network	(Fig. 1) (comment: minor)
PMID:31341193	FYPO:0007056	abnormal post-Golgi vesicle-mediated transport [has_penetrance] medium [assayed_using] PomBase:SPBC16C6.06	(Fig. 1) Increased colocalization with Cfr1
PMID:31341193	FYPO:0003658	normal protein localization to Golgi membrane [has_penetrance] high [assayed_using] PomBase:SPBC16C6.06	(Fig. 1a-c)
PMID:31341193	FYPO:0005114	normal protein localization to endosome [has_penetrance] high [assayed_using] PomBase:SPBC16C6.06	(Fig. 1a-c)
PMID:31341193	FYPO:0005114	normal protein localization to endosome [has_penetrance] high [assayed_using] PomBase:SPBC16C6.06	(Fig. 1d)
PMID:31341193	FYPO:0007056	abnormal post-Golgi vesicle-mediated transport [assayed_using] PomBase:SPBC16C6.06 [has_penetrance] medium	(Fig. 3) Increased co-localization with Cfr1
PMID:31341193	FYPO:0004248	normal protein localization to vacuolar membrane [has_penetrance] high [assayed_using] PomBase:SPAC16E8.07c	(Fig. 5)
PMID:31341193	FYPO:0004248	normal protein localization to vacuolar membrane [has_penetrance] high [assayed_using] PomBase:SPAC16E8.07c	(Fig. 5)
PMID:31341193	FYPO:0000353	abnormal endomembrane system morphology [has_penetrance] high	(Fig. 7)
PMID:31341193	FYPO:0007057	abnormal recycling endosome to Golgi transport [has_penetrance] high [assayed_using] PomBase:SPAC6G9.11	(Fig. 7) Syb1 co-localizes with late endosome markers
PMID:31341193	FYPO:0005947	normal growth on potassium chloride	(comment: CONDITION 28ºC)
PMID:31341193	FYPO:0000674	normal cell population growth at high temperature	(comment: CONDITION 37ºC)
PMID:31341193	GO:0005802	trans-Golgi network	(comment: Co-localization with TGN marker)
PMID:31341193	FYPO:0005397	normal intracellular protein transport during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPAC19G12.10c	(comment: Dot-Blot assay)
PMID:31341193	FYPO:0000539	increased protein secretion during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPAC19G12.10c	(comment: Dot-Blot test)
PMID:31341193	FYPO:0007055	normal endosome organization	(comment: Evaluated by measuring the size of Vps10-GFP foci)
PMID:31341193	FYPO:0007056	abnormal post-Golgi vesicle-mediated transport [has_penetrance] medium [assayed_using] PomBase:SPBC16C6.06	(comment: Increased co-localization with Cfr1)
PMID:31341193	FYPO:0007056	abnormal post-Golgi vesicle-mediated transport [has_penetrance] medium [assayed_using] PomBase:SPAC24C9.08	(comment: Increased co-localization with Cfr1)
PMID:31341193	GO:0000328	fungal-type vacuole lumen	(comment: Microscopy)
PMID:31341193	GO:0032588	trans-Golgi network membrane	(comment: Microscopy)
PMID:31341193	GO:0031906	late endosome lumen	(comment: Microscopy)
PMID:31341193	FYPO:0000171	abnormal late endosome to vacuole transport [has_penetrance] high [assayed_using] PomBase:SPBC16C6.06	(comment: Reduced co-localization with the PI3P probe Cherry-FYVE)
PMID:31341193	FYPO:0000179	abnormal protein targeting via MVB pathway [has_penetrance] medium [assayed_using] PomBase:SPBC16C6.06	(comment: Reduced co-localization with the PI3P probe Cherry-FYVE)
PMID:31341193	FYPO:0000171	abnormal late endosome to vacuole transport [assayed_using] PomBase:SPBC16C6.06 [has_penetrance] low	(comment: Reduced co-localization with the PI3P probe Cherry-FYVE)
PMID:31341193	FYPO:0001355	decreased vegetative cell population growth	(comment: Reduced growth at 37ºC on YES agar plates)
PMID:31341193	FYPO:0001355	decreased vegetative cell population growth	(comment: Reduced growth on 0.6M KCl plates)
PMID:31341193	GO:0008233	peptidase activity [has_input] PomBase:SPBC16C6.06	(comment: this is in a mutant but I guess it occurs physiologicall?)
PMID:31341193	FYPO:0001668	normal protein processing during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC16C6.06	isp6 delta suppresses Vps10 abnormal processing observed in ent3 delta gga22 delta strain
PMID:31341193	FYPO:0001668	normal protein processing during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC16C6.06	isp6 delta supresses the abnormal Vps10 processing detected in ent3 delta gga21 delta gga22 delta strain
PMID:31341193	FYPO:0001668	normal protein processing during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC16C6.06	isp6 delta supresses the abnormal Vps10 processing detected in vps35 delta strain
PMID:31341193	FYPO:0001668	normal protein processing during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC16C6.06	isp6 delta supresses the abnormal Vps10 proessing detected in gga21 delta gga22 delta strain
PMID:31350787	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] low	(Fig. 1)
PMID:31350787	FYPO:0001164	normal growth on glucose carbon source	(Fig. 1)
PMID:31350787	FYPO:0001164	normal growth on glucose carbon source	(Fig. 1)
PMID:31350787	FYPO:0007121	normal growth on iron	(Fig. 1)
PMID:31350787	FYPO:0000962	normal growth on hydrogen peroxide	(Fig. 1)
PMID:31350787	FYPO:0001409	normal growth on glycerol carbon source	(Fig. 1)
PMID:31350787	FYPO:0001409	normal growth on glycerol carbon source	(Fig. 1)
PMID:31350787	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] high	(Fig. 1A)
PMID:31350787	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Fig. 1A)
PMID:31350787	FYPO:0001934	abolished cell population growth on glycerol carbon source [has_severity] high	(Fig. 1A)
PMID:31350787	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] medium	"(Fig. 1A) (comment: they say it is dramatically reduced....between med/low severity... ""dramatically reduced on glycerol medium, which requires high mitochondrial respiratory activity at 30 °C"")"
PMID:31350787	FYPO:0001934	abolished cell population growth on glycerol carbon source	(Fig. 2A) The Dmti2 mutant was not able to grow at all on medium containing glycerol at the restrictive temperature of 37 °C
PMID:31350787	GO:0005759	mitochondrial matrix	(Fig. 3)
PMID:31350787	GO:0005759	mitochondrial matrix	(Fig. 3)
PMID:31350787	FYPO:0003769	decreased cellular mtDNA level [has_penetrance] 45	(Fig. 4B)
PMID:31350787	FYPO:0004529	normal mitochondrial translation	(Fig. 5)
PMID:31350787	FYPO:0002056	decreased mitochondrial translation	(Fig. 5)
PMID:31350787	FYPO:0007122	decreased mitochondrial respiratory chain complex assembly	(Fig. 6)
PMID:31366733	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC1861.01c [assayed_using] PomBase:SPAC15E1.07c	(Fig. 7)
PMID:31366733	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC1861.01c [assayed_using] PomBase:SPAC15E1.07c	(Fig. 7)
PMID:31366733	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC1861.01c [assayed_using] PomBase:SPAC15E1.07c	(Fig. 7)
PMID:31366733	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC1861.01c [assayed_using] PomBase:SPAC15E1.07c	(Fig. 7)
PMID:31366733	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC1861.01c [assayed_using] PomBase:SPAC15E1.07c	(Fig. 7)
PMID:31371524	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC1672.10 [assayed_using] PomBase:SPBC27B12.02	(Figure 2)
PMID:31371524	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPCC1672.10 [assayed_using] PomBase:SPBC27B12.02	(Figure 2)
PMID:31371524	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1672.10 [assayed_using] PomBase:SPBC27B12.02	(Figure 2)
PMID:31371524	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC1672.10 [assayed_using] PomBase:SPBC27B12.02	(Figure 4)
PMID:31371524	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC27B12.02 [assayed_using] PomBase:SPCC970.12	(Figure 6)
PMID:31371524	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC27B12.02 [assayed_using] PomBase:SPCC970.12 [has_severity] low	(Figure 6)
PMID:31371524	GO:0005515	protein binding	(comment: inhibits hhf4 binding)
PMID:31427431	FYPO:0002059	inviable cell population	(Figure 1)
PMID:31427431	FYPO:0000080	decreased cell population growth at low temperature	(Figure 1b)
PMID:31427431	FYPO:0002141	normal cell population growth at low temperature	(Figure 1b)
PMID:31427431	FYPO:0001357	normal vegetative cell population growth	(Figure 1b)
PMID:31427431	FYPO:0001357	normal vegetative cell population growth	(Figure 1b)
PMID:31427431	FYPO:0000674	normal cell population growth at high temperature	(Figure 1b)
PMID:31427431	FYPO:0001357	normal vegetative cell population growth	(Figure 1b)
PMID:31427431	FYPO:0000674	normal cell population growth at high temperature	(Figure 1b)
PMID:31427431	FYPO:0001357	normal vegetative cell population growth	(Figure 1b)
PMID:31427431	FYPO:0000082	decreased cell population growth at high temperature	(Figure 1b)
PMID:31427431	FYPO:0000080	decreased cell population growth at low temperature	(Figure 1b)
PMID:31427431	FYPO:0000674	normal cell population growth at high temperature	(Figure 1b)
PMID:31427431	FYPO:0002141	normal cell population growth at low temperature	(Figure 1b)
PMID:31427431	FYPO:0000069	resistance to thiabendazole	(Figure 1e)
PMID:31427431	FYPO:0000069	resistance to thiabendazole	(Figure 1e)
PMID:31427431	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC2F12.13 [assayed_using] PomBase:SPBC1685.15c	(Figure 1f)
PMID:31427431	FYPO:0000030	abnormal mitotic chromosome congression	(Figure 2)
PMID:31427431	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Figure 2)
PMID:31427431	FYPO:0000030	abnormal mitotic chromosome congression	(Figure 2)
PMID:31427431	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Figure 2)
PMID:31427431	FYPO:0000228	lagging mitotic chromosomes	(Figure 2)
PMID:31427431	FYPO:0000228	lagging mitotic chromosomes	(Figure 2)
PMID:31427431	FYPO:0000069	resistance to thiabendazole	(Figure 2f)
PMID:31427431	FYPO:0000069	resistance to thiabendazole	(Figure 2f)
PMID:31427431	FYPO:0000069	resistance to thiabendazole	(Figure 2f)
PMID:31427431	FYPO:0000069	resistance to thiabendazole	(Figure 2f)
PMID:31427431	FYPO:0001943	abnormal microtubule binding	(Figure 4)
PMID:31427431	FYPO:0000324	mitotic metaphase/anaphase transition delay	(Figure 5)
PMID:31427431	FYPO:0000141	abnormal mitotic sister chromatid segregation	(Figure 5)
PMID:31427431	FYPO:0000733	long mitotic spindle	(Figure 5)
PMID:31427431	FYPO:0007071	increased rate of mitotic spindle elongation during anaphase A	(Figure 6)
PMID:31427431	FYPO:0001846	increased duration of mitotic anaphase A	(Figure 6)
PMID:31427431	FYPO:0001846	increased duration of mitotic anaphase A	(Figure 6)
PMID:31427431	FYPO:0001846	increased duration of mitotic anaphase A	(Figure 6)
PMID:31427431	FYPO:0000228	lagging mitotic chromosomes	(Figure 6)
PMID:31427431	FYPO:0000228	lagging mitotic chromosomes [has_severity] low	(Figure 6)
PMID:31427431	FYPO:0000228	lagging mitotic chromosomes	(Figure 6)
PMID:31427431	FYPO:0007071	increased rate of mitotic spindle elongation during anaphase A	(Figure 6)
PMID:31427431	FYPO:0007071	increased rate of mitotic spindle elongation during anaphase A	(Figure 6)
PMID:31427431	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B [has_severity] low	(Figure 7)
PMID:31427431	FYPO:0007072	decreased duration of mitotic anaphase B [has_severity] low	(Figure 7)
PMID:31427431	FYPO:0007072	decreased duration of mitotic anaphase B [has_severity] low	(Figure 7)
PMID:31427431	FYPO:0007072	decreased duration of mitotic anaphase B [has_severity] low	(Figure 7)
PMID:31427431	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Figure 7)
PMID:31427431	FYPO:0005342	normal rate of mitotic spindle elongation during anaphase B	(Figure 7)
PMID:31427431	FYPO:0003165	cut [has_penetrance] medium	(Figure 7) (comment: type II cells)
PMID:31427431	FYPO:0001357	normal vegetative cell population growth	(Figure S1)
PMID:31427431	FYPO:0000733	long mitotic spindle	(Figure S2)
PMID:31427431	FYPO:0000733	long mitotic spindle	(Figure S2)
PMID:31468675	FYPO:0004085	decreased vegetative cell growth [has_severity] high	(comment: evidence: measured by cell growth spot assay)
PMID:31468675	FYPO:0006993	decreased chromatin silencing at centromere otr1R	(comment: evidence: measured by cell growth spot assay)
PMID:31468675	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: evidence: measured by cell growth spot assay)
PMID:31468675	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: evidence: measured by cell growth spot assay)
PMID:31468675	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: partial derepression of marker gene at silent mating-type cassette; measured by cell growth spot assay)
PMID:31477575	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAPYUG7.02c [assayed_using] PomBase:SPAC24B11.06c	(Fig. 1)
PMID:31477575	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAPYUG7.02c [assayed_using] PomBase:SPAC24B11.06c	(Fig. 1)
PMID:31477575	GO:0005515	protein binding	(Fig. 1)
PMID:31477575	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAPYUG7.02c [assayed_using] PomBase:SPAC24B11.06c	(Fig. 1)
PMID:31477575	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC12C2.02c	(Fig. 2b)
PMID:31477575	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC12C2.02c	(Fig. 2b)
PMID:31477575	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC777.08c	(Fig. 2b)
PMID:31477575	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC30D10.10c	(Fig. 2b)
PMID:31477575	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC21B10.05c	(Fig. 2b)
PMID:31477575	GO:0005829	cytosol	(Fig. 3c)
PMID:31477575	GO:0005938	cell cortex	(Fig. 3c)
PMID:31477575	FYPO:0002290	normal protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC24B10.07	(Fig. S1)
PMID:31477575	FYPO:0002290	normal protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC24B10.07	(Fig. S1)
PMID:31477575	FYPO:0002290	normal protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC24B10.07	(Fig. S1)
PMID:31477575	FYPO:0002290	normal protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC24B10.07	(Fig. S1)
PMID:31477575	FYPO:0002290	normal protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC24B10.07	(Fig. S1)
PMID:31477575	FYPO:0002290	normal protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC24B10.07	(Fig. S1)
PMID:31477575	FYPO:0002290	normal protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC24B10.07	(Fig. S1)
PMID:31477575	FYPO:0002290	normal protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC24B10.07	(Fig. S1)
PMID:31477575	FYPO:0002290	normal protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC24B10.07	(Fig. S1)
PMID:31477575	FYPO:0002376	decreased protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC24B10.07 [has_severity] high	(Fig. S3B)
PMID:31477575	FYPO:0002290	normal protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC24B10.07	(Fig. S3B)
PMID:31477575	FYPO:0002290	normal protein phosphorylation during cellular response to osmotic stress [assayed_using] PomBase:SPCC24B10.07	(Fig. S3B)
PMID:31483748	FYPO:0007192	abolished spindle pole body-led chromosome movement during mitotic interphase	(Fig. 1B-G)
PMID:31483748	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 2)
PMID:31483748	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 2)
PMID:31483748	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 2)
PMID:31483748	FYPO:0000085	sensitive to camptothecin	(Fig. 2)
PMID:31483748	FYPO:0000267	sensitive to ionizing radiation during vegetative growth	(Fig. 2)
PMID:31483748	FYPO:0000963	normal growth on hydroxyurea	(Fig. 2)
PMID:31483748	FYPO:0000969	normal growth during cellular response to UV	(Fig. 2)
PMID:31483748	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 2)
PMID:31483748	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 2)
PMID:31483748	FYPO:0000089	sensitive to methyl methanesulfonate	(Figure 2A)
PMID:31483748	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Figure 2C)
PMID:31483748	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Figure 2C)
PMID:31483748	FYPO:0000089	sensitive to methyl methanesulfonate	(Figure 2C) No increase in severity to mto1 delete
PMID:31483748	FYPO:0007191	increased duration of Rad52 focus presence during vegetative growth	(Figure 3A, 3B)
PMID:31483748	FYPO:0000972	increased number of Rad52 foci during vegetative growth	(Figure 3A, 3B) (comment: number and intensity)
PMID:31483748	FYPO:0000089	sensitive to methyl methanesulfonate	(Figure S1A)
PMID:31483748	FYPO:0000089	sensitive to methyl methanesulfonate	(Figure S1A)
PMID:31483748	FYPO:0007209	decreased sister chromatid cohesion along chromosome arms during mitotic interphase	(comment: CHECK issues/3588 decreased)
PMID:31483748	FYPO:0007209	decreased sister chromatid cohesion along chromosome arms during mitotic interphase	(comment: CHECK issues/3588) Figure 5A-E
PMID:31483748	FYPO:0000185	decreased gene conversion during vegetative growth	Recombination rates were decreased by 10-fold in mto1∆ strains in both recombination substrates (Figure 4B)
PMID:31483748	FYPO:0006921	decreased gene conversion at mitotic DNA replication fork barriers	Recombination rates were decreased by 10-fold in mto1∆ strains in both recombination substrates (Figure 4B)
PMID:31483748	FYPO:0005386	decreased protein localization to chromatin at chromosome arms [assayed_using] PomBase:SPCC338.17c	Reduced Rad21 binding to chromosome arms
PMID:31495586	FYPO:0007094	increased duration of cell fusion during mating [has_severity] low	(Figure 1)
PMID:31495586	FYPO:0007094	increased duration of cell fusion during mating [has_severity] low	(Figure 1)
PMID:31495586	FYPO:0007094	increased duration of cell fusion during mating [has_severity] high	(Figure 1)
PMID:31495586	FYPO:0007095	increased protein localization to actin fusion focus [assayed_using] PomBase:SPAC27F1.02c [has_severity] low	(Figure 2)
PMID:31495586	FYPO:0000413	abolished cell fusion during mating	(Figure 2)
PMID:31495586	FYPO:0000413	abolished cell fusion during mating [has_penetrance] low	(Figure 2)
PMID:31495586	FYPO:0000413	abolished cell fusion during mating [has_penetrance] medium	(Figure 2)
PMID:31495586	FYPO:0000413	abolished cell fusion during mating [has_penetrance] medium	(Figure 2)
PMID:31495586	FYPO:0000413	abolished cell fusion during mating [has_penetrance] low	(Figure 2)
PMID:31495586	FYPO:0000413	abolished cell fusion during mating [has_penetrance] high	(Figure 2)
PMID:31495586	FYPO:0000413	abolished cell fusion during mating [has_penetrance] high	(Figure 2)
PMID:31495586	FYPO:0000413	abolished cell fusion during mating	(Figure 2)
PMID:31495586	FYPO:0007095	increased protein localization to actin fusion focus	(Figure 2) (comment: Increased 1.5-fold, assayed using CHD)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPAC23D3.10c	(Figure 3)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPCC1919.10c	(Figure 3)
PMID:31495586	FYPO:0006108	abnormal actin fusion focus assembly	(Figure 3)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPBC646.06c	(Figure 3)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPBC106.20	(Figure 3)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPAC6F12.08c	(Figure 3)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPAC18G6.03	(Figure 3)
PMID:31495586	FYPO:0007097	ectopic actin fusion focus assembly [has_severity] high	(Figure 3) (comment: assayed using Myo52)
PMID:31495586	FYPO:0007097	ectopic actin fusion focus assembly [has_severity] medium	(Figure 3) (comment: assayed using Myo52)
PMID:31495586	FYPO:0007097	ectopic actin fusion focus assembly [has_severity] low	(Figure 3, S4) (comment: assayed using Myo52 and Fus1)
PMID:31495586	FYPO:0002445	protein mislocalized to actin cortical patch [assayed_using] PomBase:SPAC1F5.04c	(Figure 4 and 6)
PMID:31495586	FYPO:0006081	increased protein localization to actin cortical patch [assayed_using] PomBase:SPBC2D10.14c	(Figure 4 and 6)
PMID:31495586	FYPO:0006120	decreased protein localization to actin cortical patch [assayed_using] PomBase:SPAC12B10.07	(Figure 4 and 6)
PMID:31495586	FYPO:0006081	increased protein localization to actin cortical patch [assayed_using] PomBase:SPCC1919.10c	(Figure 4 and 6)
PMID:31495586	FYPO:0000742	abnormal protein localization to actin cortical patch [assayed_using] PomBase:SPBC106.20	(Figure 4)
PMID:31495586	FYPO:0000742	abnormal protein localization to actin cortical patch [assayed_using] PomBase:SPAC20G4.02c	(Figure 4)
PMID:31495586	FYPO:0006120	decreased protein localization to actin cortical patch [assayed_using] PomBase:SPAC631.01c	(Figure 5)
PMID:31495586	FYPO:0007094	increased duration of cell fusion during mating [has_severity] low	(Figure 5)
PMID:31495586	FYPO:0006120	decreased protein localization to actin cortical patch [assayed_using] PomBase:SPAC631.01c	(Figure 5)
PMID:31495586	FYPO:0007097	ectopic actin fusion focus assembly [has_severity] medium	(Figure 5) (comment: assayed using Myo52)
PMID:31495586	FYPO:0007097	ectopic actin fusion focus assembly [has_severity] low	(Figure 5) (comment: assayed using Myo52)
PMID:31495586	FYPO:0007097	ectopic actin fusion focus assembly [has_severity] low	(Figure 5) (comment: assayed using Myo52)
PMID:31495586	FYPO:0000744	normal protein localization to actin cortical patch [assayed_using] PomBase:SPBC1778.06c	(Figure 6)
PMID:31495586	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPCC895.05	(Figure 6)
PMID:31495586	FYPO:0000742	abnormal protein localization to actin cortical patch [assayed_using] PomBase:SPAC27F1.02c	(Figure 6)
PMID:31495586	FYPO:0002445	protein mislocalized to actin cortical patch [assayed_using] PomBase:SPCC895.05	(Figure 6)
PMID:31495586	FYPO:0002030	abnormal actin cable organization	(Figure 6)
PMID:31495586	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth	(Figure 6)
PMID:31495586	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPCC895.05	(Figure 6)
PMID:31495586	FYPO:0001584	abnormal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPBC1778.06c	(Figure 6)
PMID:31495586	FYPO:0007095	increased protein localization to actin fusion focus	(Figure S1) (comment: assayed using CHD)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPBC106.20	(Figure S3)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPCC1919.10c	(Figure S3)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPAC6F12.08c	(Figure S3)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPAC6F12.08c	(Figure S3)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPBC106.20	(Figure S3)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPAC18G6.03	(Figure S3)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPCC1919.10c	(Figure S3)
PMID:31495586	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_using] PomBase:SPAC18G6.03	(Figure S3)
PMID:31495586	FYPO:0006081	increased protein localization to actin cortical patch [has_severity] medium	(Figure S5) (comment: assayed using LifeAct)
PMID:31495586	FYPO:0006081	increased protein localization to actin cortical patch	(Figure S5) (comment: assayed using LifeAct)
PMID:31495586	FYPO:0006081	increased protein localization to actin cortical patch	(Figure S5) (comment: assayed using LifeAct)
PMID:31495586	FYPO:0000742	abnormal protein localization to actin cortical patch [assayed_using] PomBase:SPAC27F1.02c	(Figure S6)
PMID:31495586	FYPO:0000742	abnormal protein localization to actin cortical patch [assayed_using] PomBase:SPAC27F1.02c	(Figure S6)
PMID:31495586	FYPO:0000742	abnormal protein localization to actin cortical patch [assayed_using] PomBase:SPAC27F1.02c	(Figure S6)
PMID:31495586	FYPO:0006876	normal protein localization to cell cortex of cell tip [assayed_using] PomBase:SPCC895.05	(Figure S6)
PMID:31495586	FYPO:0006081	increased protein localization to actin cortical patch [assayed_using] PomBase:SPAC631.01c	(comment: 1.1 fold,) Figure S2
PMID:31495586	FYPO:0007095	increased protein localization to actin fusion focus [assayed_using] PomBase:SPAC20G4.02c	(comment: Increased 4-fold,) Figure2
PMID:31495586	FYPO:0007095	increased protein localization to actin fusion focus [assayed_using] PomBase:SPAC20G4.02c	(comment: Increased 4-fold,) Figure2
PMID:31495586	FYPO:0007095	increased protein localization to actin fusion focus [assayed_using] PomBase:SPAC20G4.02c	(comment: Increased 4-fold,) FigureS1
PMID:31495586	FYPO:0007095	increased protein localization to actin fusion focus	(comment: assayed using CHD,) FigureS1
PMID:31509478	FYPO:0002059	inviable cell population	(Fig. 1)
PMID:31509478	FYPO:0002060	viable vegetative cell population	(Fig. 1)
PMID:31509478	FYPO:0002059	inviable cell population	(Fig. 2)
PMID:31509478	FYPO:0000650	increased septation index	(Fig. 3)
PMID:31509478	FYPO:0000650	increased septation index	(Fig. 3)
PMID:31509478	FYPO:0003343	elongated multinucleate multiseptate cell, single septa between nuclei	(Fig. 3)
PMID:31509478	FYPO:0003343	elongated multinucleate multiseptate cell, single septa between nuclei	(Fig. 3)
PMID:31509478	FYPO:0002177	viable vegetative cell with normal cell morphology	(Fig. 3)
PMID:31509478	FYPO:0005840	incomplete, asymmetric septum	(Fig. 3F)
PMID:31509478	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC4F6.12	(Fig. 6)
PMID:31509478	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPAC20G8.05c	(Fig. S3C)
PMID:31509478	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPAC20G8.05c	(Fig. S3C)
PMID:31509478	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPAC20G8.05c	(Fig. S3C)
PMID:31509478	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPAC20G8.05c	(Fig. S3C)
PMID:31509478	FYPO:0002059	inviable cell population	(Figure 1)
PMID:31509478	FYPO:0005543	increased duration of actomyosin contractile ring contraction	(Figure 3E)
PMID:31509478	FYPO:0005543	increased duration of actomyosin contractile ring contraction	(Figure 3E)
PMID:31509478	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBP4H10.04 [has_severity] high	(Figure 6A)
PMID:31509478	FYPO:0001904	premature actomyosin contractile ring disassembly	(comment: synonym =ring collapse) fig3F
PMID:31515876	GO:0043565	sequence-specific DNA binding [happens_during] cellular response to zinc ion	(comment: CHECK ADD SO TERM WHEN AVAILABLE ) Mutagenesis of 3 Loz1 response elements in the SPBC1348.06c promoter resulted in the promoter no longer being repressed in high zinc in a manner that is dependent upon Loz1 (see Figure 4). The minimal Loz1 DNA binding domain (amino acids 426-522) also binds to this motif in vitro (supplemental Fig 2), and multiple copies of this element are able to confer Loz1-mediated gene repression in a minimal reporter system - see Figure 6)
PMID:31515876	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [has_input] PomBase:SPAC2E1P3.05c [happens_during] cellular response to zinc ion [part_of] negative regulation of transcription by RNA polymerase II	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [has_input] PomBase:SPBC16D10.06 [happens_during] cellular response to zinc ion [part_of] negative regulation of transcription by RNA polymerase II	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [has_input] PomBase:SPCC576.03c [happens_during] cellular response to zinc ion [part_of] negative regulation of transcription by RNA polymerase II	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [has_input] PomBase:SPAC977.16c [happens_during] cellular response to zinc ion [part_of] negative regulation of transcription by RNA polymerase II	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [has_input] PomBase:SPAC1F12.10c [happens_during] cellular response to zinc ion [part_of] negative regulation of transcription by RNA polymerase II	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [has_input] PomBase:SPCC569.05c [happens_during] cellular response to zinc ion [part_of] negative regulation of transcription by RNA polymerase II	ChIP-seq, RNA-seq and northern blot analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 3B and 3C)
PMID:31515876	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [has_input] PomBase:SPBC1348.06c [happens_during] cellular response to zinc ion [part_of] negative regulation of transcription by RNA polymerase II	ChIP-seq, RNA-seq and reporter gene analysis demonstrate that this transcript is repressed in high zinc in a manner that is dependent upon Loz1 (Table 1, Figure 4)
PMID:31515876	FYPO:0007091	increased negative regulation of transcription by zinc [assayed_using] PomBase:SPBC16D10.06	Loz1 represses gene expression when zinc is in excess and growth in zinc deficient media leads to de-repression of its target genes. Expression from the pgk1DTATA promoter leads to higher levels of Loz1 accumulating inside of cells, which in turn leads to higher levels of gene repression under low zinc conditions (Figure 1B)
PMID:31515876	FYPO:0007092	increased DNA binding during cellular response to zinc ion [assayed_using] PomBase:SPAC5H10.06c	When Loz1 is expressed at a constant level inside of cells, it binds to the adh4 promoter in high zinc conditions and not in low zinc conditions (consistent with its role in gene repression in high zinc conditions
PMID:31515876	FYPO:0007092	increased DNA binding during cellular response to zinc ion [assayed_using] PomBase:SPBC16D10.06	When Loz1 is expressed at a constant level inside of cells, it binds to the zrt1 promoter in high zinc conditions and not in low zinc conditions (comment: consistent with its role in gene repression in high zinc conditions)
PMID:31515876	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [has_input] PomBase:SPBPB2B2.15 [happens_during] cellular response to zinc ion [part_of] negative regulation of transcription by RNA polymerase II	deletion of loz1 leads to increased expression of this transcript in high zinc growth conditions (inferred from RNA seq analysis - see Table 1).
PMID:31515876	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [has_input] PomBase:SPNCRNA.1710 [happens_during] cellular response to zinc ion [part_of] negative regulation of transcription by RNA polymerase II	deletion of loz1 leads to increased expression of this transcript in high zinc growth conditions (inferred from RNA seq analysis - see Table 1).
PMID:31515876	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [has_input] PomBase:SPAC5H10.06c [happens_during] cellular response to zinc ion [part_of] negative regulation of transcription by RNA polymerase II	deletion of loz1 leads to increased expression of this transcript in high zinc growth conditions (inferred from RNA seq analysis - see Table 1).
PMID:31532702	FYPO:0004159	abnormal homologous chromosome segregation	(Figure 1B)
PMID:31532702	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] ~99	(Figure 1B)
PMID:31532702	FYPO:0004510	abnormal spindle assembly during meiosis II [has_penetrance] 80	(Figure 1B, D)
PMID:31532702	FYPO:0007079	normal initial meiotic spindle pole body separation in meiosis II [has_penetrance] 85	(Figure 1D)(comment: E . monopolar?)
PMID:31532702	FYPO:0007099	normal spindle elongation in meiosis I [has_penetrance] 40	(Figure 2A)
PMID:31532702	FYPO:0000590	normal sporulation [has_penetrance] 40	(Figure 2A)
PMID:31532702	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Figure 5B)
PMID:31532702	FYPO:0001734	abolished mitotic spindle pole body separation [has_severity] high	(Figure 5C, D)
PMID:31532702	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Figure 5E)
PMID:31532702	FYPO:0000732	short bipolar mitotic spindle	(Figure 5E)
PMID:31532702	FYPO:0003566	delayed onset of mitotic spindle pole body separation	(Figure 5G) (comment: this term referes to initial)
PMID:31532702	FYPO:0002060	viable vegetative cell population	(Figure 5H)
PMID:31532702	FYPO:0002060	viable vegetative cell population	(Figure 5I)
PMID:31532702	FYPO:0003566	delayed onset of mitotic spindle pole body separation	(Figure 6A)
PMID:31532702	FYPO:0007080	abnormal initial meiotic spindle pole body separation in meiosis I	(Figure 6D, E)
PMID:31532702	FYPO:0007081	abolished initial meiotic spindle pole body separation in meiosis I	(Figure S3B, C) (comment: pentrance, frequently like quadruple)
PMID:31532702	FYPO:0004668	premature homologous chromosome segregation	(Figure S5)
PMID:31532702	FYPO:0000732	short bipolar mitotic spindle	(Figure S6)
PMID:31532702	FYPO:0002060	viable vegetative cell population	(comment: I didn't check the supp, but probably can only make this annotation?)
PMID:31532702	FYPO:0001734	abolished mitotic spindle pole body separation [has_penetrance] 48	(comment: meiosis I inital ) Figure 3B, C
PMID:31532702	FYPO:0004077	abnormal sporulation resulting in formation of ascus with single large spore [has_penetrance] 90	(comment: single nucleus)
PMID:31532702	FYPO:0007083	meiotic spindle collapse	28 ~ 32 min, Figure 3B; and 24 ~ 28 min, Figure S3B)
PMID:31532702	FYPO:0006475	mitotic spindle collapse	28 ~ 32 min, Figure 3B; and 24 ~ 28 min, Figure S3B)
PMID:31532702	GO:0000073	initial mitotic spindle pole body separation	The Nuf2-containing kinetochore complex serves as a physical fulcrum for microtubule-dependent SPB separation
PMID:31532702	GO:0140456	initial meiotic spindle pole body separation [happens_during] meiosis I cell cycle phase	meiotic . The Nuf2-containing kinetochore complex serves as a physical fulcrum for microtubule-dependent SPB separation
PMID:31532702	FYPO:0007081	abolished initial meiotic spindle pole body separation in meiosis I [has_penetrance] 90	top, Figure 3B, C)
PMID:31538680	FYPO:0000006	abnormal mitotic DNA damage checkpoint	Mutant proliferates faster and with shorter lag than wild-type in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin
PMID:31538680	FYPO:0005094	decreased duration of S-phase DNA damage checkpoint during cellular response to hydroxyurea [has_severity] medium	Mutant proliferates faster and with shorter lag than wild-type in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin
PMID:31538680	FYPO:0000006	abnormal mitotic DNA damage checkpoint	Mutant proliferates faster and with shorter lag than wild-type in sublethal concentrations of hydroxyurea, phleomycin or doxorubicin
PMID:31562247	FYPO:0000056	mitochondria fused	(Fig. 3a)
PMID:31562247	FYPO:0007197	increased mitochondrial fission [assayed_enzyme] PomBase:SPBC106.10	(Figure 4a, b)
PMID:31562247	FYPO:0007197	increased mitochondrial fission [assayed_enzyme] PomBase:SPBC106.10	(Figure 4a, b)
PMID:31562247	FYPO:0002700	increased protein kinase activity [assayed_enzyme] PomBase:SPBC106.10	(Figure 4c)
PMID:31562247	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC106.10	(Figure 4c)
PMID:31562247	FYPO:0007611	small fragmented mitochondria present in decreased numbers	(comment: CHECK (with decreased total volume -. new term requested)) Throughout the period of glucose starvation, mitochondria in dnm1􏰇 cells did not appear to fragment but shrunk over time (Fig. 3A). mitochondrion numbers remained largely unchanged during glucose starvation (Fig. 3B)
PMID:31562247	FYPO:0003896	normal mitochondrial morphology	As shown in Fig. 5A, the changes in mitochondrial morphology were similar within 40 min of glucose starvation in the three mutant and WT cells
PMID:31562247	FYPO:0002780	decreased cellular reactive oxygen species level during vegetative growth	As shown in Fig. 6, A and B, ROS production under glucose starvation was reduced, but not abolished, in the absence of Dnm1 because only 􏰆25% of dnm1􏰇 cells were DCDHF-DA- positive after glucose starvation.
PMID:31562247	FYPO:0003896	normal mitochondrial morphology	Indeed, no noticeable change in mitochondrial morphology or altered mitochondrion numbers were found in the three mutant cells cultured in glucose-rich EMM (Fig. 5, C and D).
PMID:31563844	FYPO:0003164	abolished nuclease activity [assayed_enzyme] PomBase:SPBC685.02	Consistent with these studies, mutation of either of the analogous active site aspartates to alanines (D176A, D207A), abrogated the nuclease activity of spExo5 (Supplementary Fig. S2A).
PMID:31563844	FYPO:0003164	abolished nuclease activity [assayed_enzyme] PomBase:SPBC685.02	Consistent with these studies, mutation of either of the analogous active site aspartates to alanines (D176A, D207A), abrogated the nuclease activity of spExo5 (Supplementary Fig. S2A).
PMID:31563844	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high [has_severity] high	Examination of the cell morphology revealed that the cells were elongated, indicative of checkpoint activation [17] (Fig. 4B
PMID:31563844	FYPO:0001122	elongated vegetative cell [has_penetrance] high [has_severity] high	Examination of the cell morphology revealed that the cells were elongated, indicative of checkpoint activation [17] (Fig. 4B
PMID:31563844	FYPO:0000102	sensitive to cisplatin [has_severity] high	Exo5Δ and pli1Δ show synergistic interactions indicating that they operate in different, competing pathways (Fig. 5F).
PMID:31563844	FYPO:0000102	sensitive to cisplatin [has_severity] high	Exo5Δ and pli1Δ show synergistic interactions indicating that they operate in different, competing pathways (Fig. 5F).
PMID:31563844	FYPO:0000102	sensitive to cisplatin	Exo5Δ and pli1Δ show synergistic interactions indicating that they operate in different, competing pathways (Fig. 5F).
PMID:31563844	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	Fission yeast Exo1 exonuclease is involved in Okazaki fragment maturation, double-strand break repair, mismatch repair, and interstrand crosslink repair [27-29]. While the single exo1Δ and exo5Δ mutants showed a comparable sensitivity to UV, MMS and ICL agents, the double mutant exo1Δ exo5Δ showed an increased sensitivity to these agents, indicating that Exo1 and Exo5 repair these damages with partial redundancy (Fig. 5A, Supplementary Fig. S4E).
PMID:31563844	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	Fission yeast Exo1 exonuclease is involved in Okazaki fragment maturation, double-strand break repair, mismatch repair, and interstrand crosslink repair [27-29]. While the single exo1Δ and exo5Δ mutants showed a comparable sensitivity to UV, MMS and ICL agents, the double mutant exo1Δ exo5Δ showed an increased sensitivity to these agents, indicating that Exo1 and Exo5 repair these damages with partial redundancy (Fig. 5A, Supplementary Fig. S4E).
PMID:31563844	FYPO:0000102	sensitive to cisplatin	Furthermore, the deletion is particularly hypersensitive to interstrand crosslinking (ICL) agents such as 8-methoxypsoralen (Fig. 5B) and cis-platin (Fig. 5C). 8- methoxypsoralen intercalates into the DNA and forms interstrand crosslinks upon irradiation with visible light [23].
PMID:31563844	FYPO:0000102	sensitive to cisplatin [has_severity] medium	Furthermore, the deletion is particularly hypersensitive to interstrand crosslinking (ICL) agents such as 8-methoxypsoralen (Fig. 5B) and cis-platin (Fig. 5C). 8- methoxypsoralen intercalates into the DNA and forms interstrand crosslinks upon irradiation with visible light [23].
PMID:31563844	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	However, the exo5Δ mutant is more sensitive than isogenic wild-type to UV-irradiation and alkylating agents (Fig. 5A).
PMID:31563844	FYPO:0003503	normal vegetative cell length	However, while overexpression of exo5-D207A in a rad3Δ background eliminated the cell elongation phenotype, it did not suppress lethality (Fig. 4A,B)
PMID:31563844	FYPO:0002061	inviable vegetative cell population	However, while overexpression of exo5-D207A in a rad3Δ background eliminated the cell elongation phenotype, it did not suppress lethality (Fig. 4A,B)
PMID:31563844	FYPO:0003503	normal vegetative cell length	However, while overexpression of exo5-D207A in a rad3Δ background eliminated the cell elongation phenotype, it did not suppress lethality (Fig. 4A,B)
PMID:31563844	FYPO:0002061	inviable vegetative cell population	Interestingly, while neither the single exo5Δ nor rad2Δ mutant is associated with a detectable mitochondrial growth phenotype, the double mutant exo5Δ rad2Δ showed a failure to grow on media lacking a fermentable carbon source (Fig. 2B).
PMID:31563844	FYPO:0002060	viable vegetative cell population	S. pombe exo5Δ strains are viable, indicating that spExo5 is not essential for mitochondrial genome stability (Fig. 2B).
PMID:31563844	GO:0036298	recombinational interstrand cross-link repair	The Fanconi branch of ICL repair is represented by fml1+ and fan1+. Exo5+ is epistatic with fml1+, i.e. the double mutant is not more sensitive than the single mutants (Fig. 5E). Likewise, the exo5Δfan1Δ double mutant is not more sensitive than the single mutants (Supplementary Fig. S5A). These data suggest that Exo5 functions in the Fanconi pathway of ICL repair.
PMID:31563844	GO:0036298	recombinational interstrand cross-link repair	The Fanconi branch of ICL repair is represented by fml1+ and fan1+. Exo5+ is epistatic with fml1+, i.e. the double mutant is not more sensitive than the single mutants (Fig. 5E). Likewise, the exo5Δfan1Δ double mutant is not more sensitive than the single mutants (Supplementary Fig. S5A). These data suggest that Exo5 functions in the Fanconi pathway of ICL repair.
PMID:31563844	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	The UV sensitivity of a rad13Δ mutant, the 3’-endonuclease that functions in nucleotide excision repair (ortholog of human XPG) is increased in the double mutant with exo5Δ, suggesting that Exo5 does not have a function in nucleotide excision repair.
PMID:31563844	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	The UV sensitivity of a rad13Δ mutant, the 3’-endonuclease that functions in nucleotide excision repair (ortholog of human XPG) is increased in the double mutant with exo5Δ, suggesting that Exo5 does not have a function in nucleotide excision repair.
PMID:31563844	GO:0005634	nucleus	The affinity-purified wild-type Exo5-FLAG protein showed two prominent species by immunoblot blot analysis (Fig. 2A). The upper band is consistent with the predicted molecular weight of spExo5-3XFLAG protein (~50 kDa), while the lower band is consistent with that of a protein starting at Met58, followed by loss of a small signal peptide upon mitochondrial entry (~43 kDa). Importantly, the M58A mutant lacked the lower band, as one would expect if translation of the mitochondrial species started at Met58 with the M58A mutation eliminating this initiation. Conversely, the Δ(1-57) mutant showed only the lower band, further supporting our model.
PMID:31563844	GO:0005739	mitochondrion	The affinity-purified wild-type Exo5-FLAG protein showed two prominent species by immunoblot blot analysis (Fig. 2A). The upper band is consistent with the predicted molecular weight of spExo5-3XFLAG protein (~50 kDa), while the lower band is consistent with that of a protein starting at Met58, followed by loss of a small signal peptide upon mitochondrial entry (~43 kDa). Importantly, the M58A mutant lacked the lower band, as one would expect if translation of the mitochondrial species started at Met58 with the M58A mutation eliminating this initiation. Conversely, the Δ(1-57) mutant showed only the lower band, further supporting our model.
PMID:31563844	FYPO:0000102	sensitive to cisplatin [has_severity] high	The crosslink sensitivity of pso2Δ is substantially higher than that of exo5Δ (Fig. 5B, C), while the double mutant exo5Δ pso2Δ shows an increased sensitivity to cis-platin (Fig. 5C, Supplementary Fig. S5B
PMID:31563844	FYPO:0000102	sensitive to cisplatin [has_severity] high	The crosslink sensitivity of pso2Δ is substantially higher than that of exo5Δ (Fig. 5B, C), while the double mutant exo5Δ pso2Δ shows an increased sensitivity to cis-platin (Fig. 5C, Supplementary Fig. S5B
PMID:31563844	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	The double mutant also showed a minor growth defect on rich media containing glucose (Fig. 5D)
PMID:31563844	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	The double mutant also showed a minor growth defect on rich media containing glucose (Fig. 5D)
PMID:31563844	GO:0051539	4 iron, 4 sulfur cluster binding	The purified enzyme shows an absorption at 410 nm, characteristic of a [4Fe-4S] iron-sulfur cluster (Fig. 1B,C).
PMID:31563844	GO:0051539	4 iron, 4 sulfur cluster binding	The purified enzyme shows an absorption at 410 nm, characteristic of a [4Fe-4S] iron-sulfur cluster (Fig. 1B,C).
PMID:31563844	GO:0032042	mitochondrial DNA metabolic process	The results from these experiments establish a redundant function in mitochondria for Exo5 and FEN1, presumably operating during the final steps of DNA replication in order to generate ligatable nicks.
PMID:31563844	GO:0032042	mitochondrial DNA metabolic process	The results from these experiments establish a redundant function in mitochondria for Exo5 and FEN1, presumably operating during the final steps of DNA replication in order to generate ligatable nicks.
PMID:31563844	FYPO:0002061	inviable vegetative cell population	This lethality was not due to the nuclease activity of the protein, since overexpression of the nuclease-deficient mutant (exo5-D207A) showed similar lethality.
PMID:31563844	FYPO:0002061	inviable vegetative cell population	Under these highly inducing conditions, Exo5-FLAG levels were increased dramatically, and cells carrying the Exo5+ plasmid showed a negative growth phenotype (Supplementary Fig. S3B).
PMID:31563844	FYPO:0000490	abnormal mitochondrial genome maintenance [has_severity] high	We observed a severe loss of mitochondrial DNA from the exo5Δ rad2Δ strain compared to the wild-type and single mutants, suggesting that Exo5 and FEN1 are redundantly required for mitochondrial DNA maintenance (Fig. 2C).
PMID:31563844	FYPO:0000490	abnormal mitochondrial genome maintenance [has_severity] high	We observed a severe loss of mitochondrial DNA from the exo5Δ rad2Δ strain compared to the wild-type and single mutants, suggesting that Exo5 and FEN1 are redundantly required for mitochondrial DNA maintenance (Fig. 2C).
PMID:31563844	GO:0005634	nucleus	Wild-type Exo5+ showed diffuse cytoplasmic fluorescence and both nuclear and punctate mitochondrial fluorescence. The Exo5-M58A mutant showed diffuse cytoplasmic/nuclear fluorescence, but lacked punctate fluorescence suggesting its exclusion from the mitochondria. The Δ(1-57) mutant showed only punctate staining suggesting that this truncated form of Exo5 is solely localized to the mitochondria (Supplementary Table 2). Therefore, both sets of data are consistent with a model in which mitochondrial localization of spExo5 proceeds through translational initiation at Met58, whereas initiation at Met1 yields predominantly the cytoplasmic and nuclear forms.
PMID:31563844	GO:0005739	mitochondrion	Wild-type Exo5+ showed diffuse cytoplasmic fluorescence and both nuclear and punctate mitochondrial fluorescence. The Exo5-M58A mutant showed diffuse cytoplasmic/nuclear fluorescence, but lacked punctate fluorescence suggesting its exclusion from the mitochondria. The Δ(1-57) mutant showed only punctate staining suggesting that this truncated form of Exo5 is solely localized to the mitochondria (Supplementary Table 2). Therefore, both sets of data are consistent with a model in which mitochondrial localization of spExo5 proceeds through translational initiation at Met58, whereas initiation at Met1 yields predominantly the cytoplasmic and nuclear forms.
PMID:31563844	GO:0045145	single-stranded DNA 5'-3' DNA exonuclease activity [occurs_in] nucleus [part_of] recombinational interstrand cross-link repair	spExo5 showed activity on either substrate, with a preference for the 5’-ended substrate (Supplementary Fig. S2B).
PMID:31563844	GO:0045145	single-stranded DNA 5'-3' DNA exonuclease activity [occurs_in] mitochondrion [part_of] mitochondrial DNA metabolic process	spExo5 showed activity on either substrate, with a preference for the 5’-ended substrate (Supplementary Fig. S2B).
PMID:31575705	FYPO:0006686	decreased DNA double-strand break processing	(Fig. 1)
PMID:31575705	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 1A) growth inhibited by 0.005% MMS after 4 days
PMID:31575705	FYPO:0006318	decreased DNA resection during replication fork processing	(Fig. 2C) (comment: RTS1-RFB assay)
PMID:31575705	FYPO:0000957	normal growth on methyl methanesulfonate	(Figure 1A)
PMID:31575705	FYPO:0000957	normal growth on methyl methanesulfonate	(Figure 1A)
PMID:31575705	FYPO:0006318	decreased DNA resection during replication fork processing	(comment: RTS1-RFB assay)
PMID:31575705	GO:0000785	chromatin	(comment: constitutive)
PMID:31575705	FYPO:0000089	sensitive to methyl methanesulfonate	The fft3-K418R-myc strain exhibited similar sensitivity to CPT and MMS than fft3Δ cells, indicating that the ATPase activity is required to promote cell resistance to replication stress.
PMID:31575705	FYPO:0003586	abnormal replication fork processing	decreased replciation restart fig1 indicating that only one-third of forks arrested at the RTS1-RFB are efficiently restarted in the absence of Fft3.
PMID:31575705	FYPO:0007254	normal replication fork processing	normal replciation restart/ HR-mediated fork restart RTS1-RFB assay. urprisingly, the induction of downstream RS in fft3-K418R-myc strain was similar to the one observed in wild-type cells (Fig 4D, bottom panel). This finding indicates that the lack of the ATPase activity does not impact the efficiency of HR-mediated fork restart.
PMID:31582398	FYPO:0007275	abnormal mitochondrion inheritance during meiotic cell cycle [has_penetrance] ~31	"""in the absence of Mcp5 in rho+ parental strain (strain PHP4xVA074; see Table S1), only 31.3% of the tetrads dissected (n = 16 tetrads) exhibited mtDNA segregation similar to that observed in Fig. 6 D."""
PMID:31582398	FYPO:0007275	abnormal mitochondrion inheritance during meiotic cell cycle [has_severity] high [has_penetrance] high	(Figure. 3C, D, E, F and Video 5)
PMID:31582398	FYPO:0007275	abnormal mitochondrion inheritance during meiotic cell cycle [has_severity] high [has_penetrance] high	(Figure. 3C, D, E, F and Video 5)
PMID:31582398	FYPO:0007276	normal mitochondrion inheritance during meiotic cell cycle [has_penetrance] high [has_severity] high	(Figure. 5C, D) normal (comment: CHECK increased mitochondrial segregation during meiosis)
PMID:31582398	FYPO:0007276	normal mitochondrion inheritance during meiotic cell cycle	To verify that the attachment to microtubules was not necessary for segregation during meiosis, we employed parental cells lacking the microtubule-mitochondrial linker protein Mmb1 (Fu et al., 2011). Additionally, one of the parental cells had its mitochondria fluorescently labeled. In zygotes and asci resulting from this cross, we observed that parental mitochondria continued to remain segregated (Fig. S2, C and D).
PMID:31584934	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2)
PMID:31584934	FYPO:0007160	abnormal DNA replication-dependent nucleosome assembly	(Fig. 3)
PMID:31584934	FYPO:0007160	abnormal DNA replication-dependent nucleosome assembly	(Fig. 3)
PMID:31584934	GO:0006335	DNA replication-dependent chromatin assembly	(Fig. 3,4)
PMID:31584934	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC8D2.04 [assayed_using] PomBase:SPCC663.05c	(Fig. 3c)
PMID:31584934	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 6)
PMID:31584934	FYPO:0000085	sensitive to camptothecin	(Fig. 6)
PMID:31584934	FYPO:0001690	normal growth on camptothecin	(Fig. 6)
PMID:31584934	FYPO:0001690	normal growth on camptothecin	(Fig. 6)
PMID:31584934	FYPO:0000085	sensitive to camptothecin	(Fig. 6)
PMID:31584934	FYPO:0000085	sensitive to camptothecin	(Fig. 6)
PMID:31584934	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 6)
PMID:31584934	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 6)
PMID:31584934	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 6)
PMID:31584934	FYPO:0003906	normal growth on bleomycin	(Fig. 6)
PMID:31584934	FYPO:0003906	normal growth on bleomycin	(Fig. 6)
PMID:31584934	FYPO:0000095	sensitive to bleomycin	(Fig. 6)
PMID:31584934	FYPO:0000473	increased mitotic recombination	(Fig. 7)
PMID:31584934	FYPO:0007158	decreased histone H3 binding [assayed_using] PomBase:SPBC8D2.04 [has_severity] high	"(comment: changed to decreased from abolished based on ""H3-FLAG association with H3-H113D-HA was severely reduced)"
PMID:31584934	FYPO:0002151	inviable spore	(comment: consistent with this, we found that the deletion of pcf1 is synthetic lethal with the deletion of hip1, the gene encoding one subunit of the fission yeast HIRA complex (S4A Fig)
PMID:31584934	FYPO:0007159	decreased histone H4 binding [assayed_using] PomBase:SPBC8D2.04 [has_severity] high	(commnet: Reciprocally, H3-H113D-HA association with wt H3 and H4 were severely reduced)
PMID:31615333	FYPO:0003165	cut with abnormal chromosome segregation	(Figure 1c)
PMID:31615333	FYPO:0006613	decreased termination of RNA polymerase II transcription [assayed_using] PomBase:SPAC1705.03c [assayed_using] PomBase:SPAC19B12.02c	(Figure 2 and 3)
PMID:31615333	FYPO:0006613	decreased termination of RNA polymerase II transcription [assayed_using] PomBase:SPAC1705.03c [assayed_using] PomBase:SPAC19B12.02c	(Figure 2 and 3)
PMID:31615333	FYPO:0006279	normal termination of RNA polymerase II transcription [assayed_using] PomBase:SPAC1705.03c [assayed_using] PomBase:SPAC19B12.02c	(Figure 2 and S3)
PMID:31615333	FYPO:0006279	normal termination of RNA polymerase II transcription [assayed_using] PomBase:SPAC1705.03c [assayed_using] PomBase:SPAC19B12.02c	(Figure 2 and S3)
PMID:31615333	FYPO:0006279	normal termination of RNA polymerase II transcription [assayed_using] PomBase:SPAC1705.03c [assayed_using] PomBase:SPAC19B12.02c	(Figure 2 and S3)
PMID:31615333	FYPO:0005740	normal transcription during cellular response to heat [assayed_using] PomBase:SPAC13G7.02c [assayed_using] PomBase:SPAC926.04c	(Figure 2) (comment: detected by northern blot analysis)
PMID:31615333	FYPO:0005740	normal transcription during cellular response to heat [assayed_using] PomBase:SPAC13G7.02c [assayed_using] PomBase:SPAC926.04c	(Figure S1)
PMID:31615333	FYPO:0006613	decreased termination of RNA polymerase II transcription	(Figure S3)
PMID:31615333	FYPO:0006613	decreased termination of RNA polymerase II transcription	(Figure S3)
PMID:31615333	FYPO:0006613	decreased termination of RNA polymerase II transcription	(Figure S3)
PMID:31615768	FYPO:0005722	mitotic spindle collapse during anaphase B elongation	(Fig. 1C)
PMID:31615768	FYPO:0007126	abnormal microtubule bundle formation during mitotic spindle assembly	(Fig. 1C)
PMID:31615768	FYPO:0003307	increased mitotic index	(Fig. 3)
PMID:31615768	FYPO:0005411	increased number of unattached kinetochores [has_penetrance] 33	(Fig. 3)
PMID:31615768	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	(Fig. 3)
PMID:31615768	FYPO:0002061	inviable vegetative cell population	(Fig. 3I)
PMID:31615768	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 85	(Fig. 3a) (comment: by cen2-GFP observation)
PMID:31615768	FYPO:0004412	abolished protein localization to mitotic spindle midzone during anaphase [assayed_using] PomBase:SPAC3G9.12	(Fig. 4)
PMID:31615768	FYPO:0007124	normal protein localization to mitotic spindle midzone during prophase [assayed_using] PomBase:SPAC3G9.12	(Fig. 4)
PMID:31615768	FYPO:0006174	abolished mitotic spindle elongation during anaphase B	(Figure 1A)
PMID:31615768	FYPO:0007106	normal mitotic spindle morphology [has_penetrance] high	(Figure 1E) (comment: unbundled microtubules seen in early mitosis)
PMID:31615768	FYPO:0007123	unbundled spindle during mitotic prophase [has_penetrance] high	(Figure 1E) (comment: unbundled microtubules seen in early mitosis)
PMID:31615768	FYPO:0002061	inviable vegetative cell population	(Figure S1)
PMID:31615768	FYPO:0003186	abolished protein localization to mitotic spindle [assayed_using] PomBase:SPAC3G9.12	(Figure S2)
PMID:31615768	GO:0072686	mitotic spindle [exists_during] mitotic prophase	(Figure S2A/4)
PMID:31615768	GO:1990023	mitotic spindle midzone [exists_during] mitotic anaphase	(Figure S2A/4)
PMID:31615768	GO:0001578	microtubule bundle formation [happens_during] mitotic prophase	(Figure S4)
PMID:31618856	FYPO:0002061	inviable vegetative cell population	(Fig. 1)
PMID:31618856	FYPO:0004315	abnormal microtubule cytoskeleton during vegetative growth	(Fig. 3)
PMID:31618856	FYPO:0000131	abnormal mitotic spindle elongation	(Fig. 4)
PMID:31618856	FYPO:0006475	mitotic spindle collapse	(Fig. 4)
PMID:31618856	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 30	(Fig. 4)
PMID:31618856	FYPO:0005694	decreased interphase microtubule nucleation	(Figure 2D)
PMID:31618856	FYPO:0005681	decreased microtubule polymerization	(comment: CHECK defective in microtubule growth during both interphase and mitosis)
PMID:31618856	FYPO:0005699	normal interphase microtubule nucleation from spindle pole body	appears to retain normal microtubule nucleation activity
PMID:31641022	FYPO:0002060	viable vegetative cell population	(Fig. 2)
PMID:31644361	FYPO:0001124	normal vegetative cell size	(Fig. 1) In contrast, Cdr2 overexpression induced hyperphosphorylation of Wee1 but no change in Cdk1-pY15
PMID:31644361	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPBC11B10.09	(Fig. 1B) Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity
PMID:31644361	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPBC11B10.09	(Fig. 1B) Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity
PMID:31644361	FYPO:0002680	increased protein phosphorylation [assayed_using] PomBase:SPCC18B5.03 [has_severity] high	(Fig. 1B) Cdr1 overexpression induced hyperphosphorylation of Wee1 and loss of Cdk1-pY15, indicating inhibition of Wee1 kinase activity
PMID:31644361	FYPO:0002680	increased protein phosphorylation [assayed_using] PomBase:SPCC18B5.03 [has_severity] high	(Fig. 1B) In contrast, Cdr2 overexpression induced hyperphosphorylation of Wee1 but no change in Cdk1-pY15
PMID:31644361	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(Fig. 1C) overexpression of Cdr1 but not of Cdr2 resulted in reduced cell size in cdr1∆cdr2∆ cells (Figure 1C
PMID:31644361	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPCC18B5.03	(Figure 1D) Phosphorylation of Wee1 in fission yeast cells was reduced in the catalytically inactive mutant cdr1(K41A)
PMID:31644361	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPCC18B5.03	(Figure 1H) (in vitro) Cdr1 directly phosphorylated Wee1, but Cdr1(K41A) did not ().
PMID:31644361	FYPO:0004083	normal protein level [assayed_using] PomBase:SPCC18B5.03	(Figure 3, A and D) We confirmed that wee1(4A) protein level does not increase and still localizes to cortical nodes
PMID:31644361	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPCC18B5.03	(Figure 3A) Consistent with this model, wee1(4A) phosphorylation was reduced when compared with wild type, and its phosphorylation was not altered by cdr1∆ or cdr2∆ (
PMID:31644361	FYPO:0001122	elongated vegetative cell [has_penetrance] high	(Figure 3B)
PMID:31644361	FYPO:0002061	inviable vegetative cell population	(Figure 3C) Both wee1(4A) and cdr1∆ were synthetically lethal with cdc25-dD
PMID:31644361	FYPO:0002061	inviable vegetative cell population	(Figure 3C) Both wee1(4A) and cdr1∆ were synthetically lethal with cdc25-dD
PMID:31644361	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPCC18B5.03	(Figure 4A) We confirmed that S. pombe Cdk1- asM17 directly thiophosphorylates Wee1 and Wee1(K596L)
PMID:31644361	FYPO:0002999	normal protein localization to medial cortical node [assayed_using] PomBase:SPAC644.06c	(Figure 5B) We tested the effects of artificially recruiting mEGFP-cdr1(∆460-482) back to nodes using cdr2-GFPbinding peptide (GBP)-mCherry, which contains the GBP. In this system, mEGFP-cdr1(∆460-482) colocalized with cdr2-GBP-mCherry at nodes.
PMID:31644361	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] low	Accordingly, the size of wee1(4A) cells was largely (but not entirely) insensitive to Cdr1 overexpression (Figure 3G).
PMID:31644361	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] medium	Along with enhanced Wee1 hyperphosphorylation, these cells divided at a smaller size than wild-type cells. These results show that Cdr1 localization to nodes is a limiting factor for phosphorylation of Wee1 and cell size at division
PMID:31644361	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC18B5.03 [occurs_in] Cdr2 medial cortical node complex	Cdr1 directly phosphorylated Wee1, but Cdr1(K41A) did not (Figure 1H).
PMID:31644361	FYPO:0001122	elongated vegetative cell [has_penetrance] high	Indeed, cdr1∆ wee1(4A) cells divided at the same size as cdr1∆ cells
PMID:31657618	PomGeneEx:0000012	RNA level decreased [in_presence_of] wortmannin	(Fig. 3)
PMID:31657618	PomGeneEx:0000012	RNA level decreased [in_presence_of] wortmannin	(Fig. 3)
PMID:31657618	PomGeneEx:0000012	RNA level decreased [in_presence_of] wortmannin	(Fig. 3)
PMID:31657618	PomGeneEx:0000012	RNA level decreased [in_presence_of] wortmannin	(Fig. 3)
PMID:31657618	PomGeneEx:0000012	RNA level decreased [in_presence_of] wortmannin	(Fig. 3)
PMID:31657618	PomGeneEx:0000012	RNA level decreased [in_presence_of] wortmannin	(Fig. 3)
PMID:31657618	FYPO:0001122	elongated vegetative cell	(Fig. 4)
PMID:31657618	FYPO:0001122	elongated vegetative cell	(Fig. 4)
PMID:31657618	FYPO:0001122	elongated vegetative cell	(Fig. 4)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	(comment: CHECK Table ?) ----- COMMENT: 61b5b08d53bec31b 11 BCT25wJvpLwsSnBDCDQXMVETx5s (comment: CHECK Table ?)
PMID:31657618	FYPO:0009060	resistance to wortmannin	Table
PMID:31712578	FYPO:0004993	normal spore germination frequency	Table S3
PMID:31712578	FYPO:0004993	normal spore germination frequency	Table S3
PMID:31712578	FYPO:0004993	normal spore germination frequency	Table S3
PMID:31712578	FYPO:0004993	normal spore germination frequency	Table S3
PMID:31712578	FYPO:0004993	normal spore germination frequency	Table S3
PMID:31712578	FYPO:0003612	viable spore population	Table S3
PMID:31712578	FYPO:0004993	normal spore germination frequency	Table S3
PMID:31712578	FYPO:0003612	viable spore population	Table S3; spore viability lower than wild type (~50% of wild-type viability)
PMID:31712578	FYPO:0003612	viable spore population	Table S3; spore viability similar to wild type
PMID:31712578	FYPO:0003612	viable spore population	Table S3; spore viability similar to wild type
PMID:31712578	FYPO:0003612	viable spore population	Table S3; spore viability similar to wild type
PMID:31712578	FYPO:0003612	viable spore population	Table S3; spore viability similar to wild type
PMID:31712578	FYPO:0003612	viable spore population	Table S3; spore viability similar to wild type
PMID:31712578	FYPO:0003612	viable spore population	Table S3; spore viability similar to wild type
PMID:31719112	FYPO:0005338	decreased protein localization to nucleus during cellular response to hydroxyurea [assayed_using] PomBase:SPAP14E8.02	(comment: temperature permissive for mcm4/cdc21-M68)
PMID:31719112	FYPO:0005338	decreased protein localization to nucleus during cellular response to hydroxyurea [assayed_using] PomBase:SPAP14E8.02	(comment: temperature restrictive for cdc22-M45)
PMID:31719163	GO:0032153	cell division site [exists_during] mitotic M phase	localizes to division site after Gef1 and Scd2, but before contractile ring constriction begins
PMID:31719163	GO:0032153	cell division site [exists_during] mitotic M phase	localizes to division site before Scd1, and before contractile ring constriction begins
PMID:31719163	GO:0032153	cell division site [exists_during] mitotic M phase	localizes to division site before Scd1, and before contractile ring constriction begins
PMID:31748520	FYPO:0002577	decreased chromatin binding [assayed_protein] PomBase:SPBP16F5.03c	(Fig. 2e, 1f) (comment: CHECK spt7/tra1 pho84 and mei2 promoters. and spt7/tras ssa2 promoter)
PMID:31748520	FYPO:0002577	decreased chromatin binding [assayed_protein] PomBase:SPBC25H2.11c	(Fig. 2e, 1f) (comment: CHECK spt7/tra1 pho84 and mei2 promoters. and spt7/tras ssa2 promoter)
PMID:31748520	FYPO:0002577	decreased chromatin binding [assayed_protein] PomBase:SPAC1F5.11c	(Fig. 2e, 1f) (comment: CHECK spt7/tra1 pho84 and mei2 promoters. and spt7/tras ssa2 promoter)
PMID:31748520	FYPO:0000097	sensitive to caffeine during vegetative growth [has_severity] high	(Fig. 5d)
PMID:31748520	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 5d) Phenotypic analyses of tra1-Sptra2 and tra1-Sctra1 strains showed that tra1-Sptra2 mutants are sensitive to HU and caffeine, similar to tra1Δ mutants
PMID:31748520	FYPO:0000781	decreased transcription during vegetative growth [has_severity] low	(comment: RNA-seq)
PMID:31748520	FYPO:0002876	decreased transcription [has_severity] medium	(comment: RNA-seq)
PMID:31748520	FYPO:0002876	decreased transcription [has_severity] medium	(comment: RNA-seq)
PMID:31748520	FYPO:0001855	normal transcription during vegetative growth	(comment: RNA-seq)
PMID:31748520	FYPO:0000781	decreased transcription during vegetative growth [has_severity] low	(comment: RNA-seq)
PMID:31748520	FYPO:0000781	decreased transcription during vegetative growth [has_severity] medium	(comment: RNA-seq)
PMID:31748520	FYPO:0000781	decreased transcription during vegetative growth [has_severity] high	(comment: RNA-seq)
PMID:31748520	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPAC1F5.11c	. Similarly, we observed about a twofold reduction of Tra2 levels from NuA4 (Fig. 2b).
PMID:31748520	FYPO:0008120	decreased protein level in SAGA complex [assayed_protein] PomBase:SPBP16F5.03c [has_penetrance] complete	Abolished Tra1 interaction with SAGA complex spt20Δ mutants, without any other visible changes in its overall migration profile (Fig. 6a). Spt20 is therefore essential for Tra1 incorporation into SAGA.
PMID:31748520	FYPO:0008120	decreased protein level in SAGA complex [has_severity] high [assayed_protein] PomBase:SPBP16F5.03c	Decreased levels of Tra1 and Tra2 in SAGA and NuA4 complexes, respectively (Figure 2)
PMID:31748520	FYPO:0008121	decreased protein level in NuA4 complex [has_severity] high [assayed_protein] PomBase:SPAC1F5.11c	Decreased levels of Tra1 and Tra2 in SAGA and NuA4 complexes, respectively (Figure 2)
PMID:31748520	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1604.17c [assayed_protein] PomBase:SPBP16F5.03c	Importantly, quantitative MS analyses show that both Tra1-SpTra2 and Tra1-ScTra1 hybrid mutant proteins efficiently copurify with Tti2 (Supplementary Fig. 9b).
PMID:31748520	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPBP16F5.03c	MS analyses revealed a tenfold reduction of Tra1 from SAGA when Tti2 is depleted, as compared with control conditions (Fig. 2a). Similarly, we observed about a twofold reduction of Tra2 levels from NuA4 (Fig. 2b). Both approaches showed decreased interaction between newly synthesised Tra1 and affinity purified Spt7 in cells partially depleted of Tel2. These results demonstrate that TTT contributes to the de novo incorporation of Tra1 into the SAGA complex.
PMID:31748520	FYPO:0008117	abnormal de novo SAGA complex assembly	See Figure 3a, 3b Describes the biogenesis of a multisubunit complex from nascent proteins. (comment: Could be linked to pombase ID of one or several components of the complex)
PMID:31748520	FYPO:0008117	abnormal de novo SAGA complex assembly	See Figure 3c, 3d
PMID:31748520	FYPO:0008121	decreased protein level in NuA4 complex	See Figure 4
PMID:31748520	GO:0140662	ATP-dependent protein folding chaperone [has_input] PomBase:SPBP16F5.03c	Silver staining analysis showed that Hsp90 inactivation causes a specific decrease of Tra1 in Spt7 purification eluates (Supplementary Fig. 6). effect is modest in this hypomorphic mutant, this observation supports the conclusion that Hsp90, like TTT, contributes to the de novo assembly of Tra1 into SAGA.
PMID:31748520	GO:0140463	chromatin-protein adaptor activity	Such distinct architectural roles provide a functional validation of the recent structural studies of yeast SAGA and NuA4, which showed that Tra1 occupies a peripheral position within SAGA
PMID:31748520	GO:0005198	structural molecule activity	Tra2 contributes to the scaffolding and stabilisation of the entire NuA4 complex.
PMID:31748520	FYPO:0001522	normal growth on caffeine	whereas tra1-Sctra1 strains show no growth defects, as compared with wild-type cells (Fig. 5d).
PMID:31748520	FYPO:0000963	normal growth on hydroxyurea	whereas tra1-Sctra1 strains show no growth defects, as compared with wild-type cells (Fig. 5d).
PMID:31777937	GO:0140432	5'-hydroxyl dinucleotide hydrolase activity	Our nuclease assays confirm this prediction and demonstrate that this 5′-hydroxyl dinucleotide hydrolase (HDH) activity for DXO is higher than the subsequent 5′-3′ exoribonuclease activity for selected substrates.
PMID:31811152	FYPO:0007357	Smp focus absent from cell [assayed_using] PomBase:SPNCRNA.130	(Fig. 2)
PMID:31811152	FYPO:0007357	Smp focus absent from cell [assayed_using] PomBase:SPNCRNA.130	(Fig. 2)
PMID:31811152	FYPO:0007350	decreased homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 2 [has_severity] high [assayed_using] PomBase:SPNCRNA.103	(Figure 1b) (comment: live cell observation)
PMID:31811152	FYPO:0007353	normal homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 2 [has_penetrance] complete [assayed_using] PomBase:SPNCRNA.103	(Figure 1b) (comment: live cell observation)
PMID:31811152	FYPO:0007350	decreased homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 2 [has_severity] medium [assayed_using] PomBase:SPNCRNA.103	(Figure 1b) (comment: live cell observation)
PMID:31811152	FYPO:0007353	normal homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 2 [has_penetrance] complete [assayed_using] PomBase:SPNCRNA.103	(Figure 1b) (comment: live cell observation)
PMID:31811152	FYPO:0007350	decreased homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 2 [has_severity] high [assayed_using] PomBase:SPNCRNA.103	(Figure 1b) (comment: live cell observation)
PMID:31811152	FYPO:0007350	decreased homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 2 [has_severity] high [assayed_using] PomBase:SPNCRNA.103	(Figure 1b) (comment: live cell observation)
PMID:31811152	FYPO:0007350	decreased homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 2 [has_severity] low [assayed_using] PomBase:SPNCRNA.103	(Figure 1b) (comment: live cell observation)
PMID:31811152	FYPO:0007353	normal homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 2 [has_penetrance] high [assayed_using] PomBase:SPNCRNA.103	(Figure 1b) (comment: live cell observation)
PMID:31811152	FYPO:0007350	decreased homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 2 [has_severity] high [assayed_using] PomBase:SPNCRNA.103	(Figure 1b,4b) (comment: live cell observation)
PMID:31811152	FYPO:0007355	increased number of Smp foci [has_severity] high [assayed_using] PomBase:SPNCRNA.103	(Figure 1c)
PMID:31811152	FYPO:0007355	increased number of Smp foci [has_severity] high [assayed_using] PomBase:SPNCRNA.103	(Figure 1c)
PMID:31811152	FYPO:0007349	decreased homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 1 [assayed_using] PomBase:SPNCRNA.130	(Figure 4A)
PMID:31811152	FYPO:0007354	normal homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 3 [has_penetrance] complete [assayed_using] PomBase:SPNCRNA.584	(Figure 4a) (comment: homologous pairing examined at C24 locus)
PMID:31811152	FYPO:0007351	decreased homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 3 [assayed_using] PomBase:SPNCRNA.584	(Figure 4b)
PMID:31811152	FYPO:0007349	decreased homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 1 [has_severity] high [assayed_using] PomBase:SPNCRNA.130	(Figure 4b) (comment: live cell observation)
PMID:31811152	FYPO:0007351	decreased homologous chromosome pairing at cis-acting homologous chromosome pairing region on chromosome 3 [has_severity] high [assayed_using] PomBase:SPNCRNA.584	(Figure 4b) (comment: live cell observation)
PMID:31811152	FYPO:0007357	Smp focus absent from cell [assayed_using] PomBase:SPNCRNA.584	(comment: C24 locus) fig2
PMID:31811152	FYPO:0007356	normal Smp focus formation [assayed_using] PomBase:SPNCRNA.584	(comment: C24 locus) fig2
PMID:31833215	FYPO:0000245	loss of viability in stationary phase	(comment: same as maf1delta alone)
PMID:31837996	FYPO:0005917	increased subtelomeric heterochromatin RNA level	(comment: RNA-seq)
PMID:31837996	FYPO:0005917	increased subtelomeric heterochromatin RNA level	(comment: RNA-seq)
PMID:31837996	FYPO:0002913	increased antisense RNA transcription [has_severity] high	(comment: RNA-seq)
PMID:31837996	FYPO:0002913	increased antisense RNA transcription [has_severity] high	(comment: RNA-seq)
PMID:31837996	FYPO:0002913	increased antisense RNA transcription [has_severity] high	(comment: RNA-seq)
PMID:31837996	FYPO:0007835	increased histone binding [assayed_using] PomBase:SPBP8B7.19	(comment: assayed using bulk histones)
PMID:31837996	FYPO:0007835	increased histone binding [assayed_using] PomBase:SPBC609.05	(comment: assayed using bulk histones)
PMID:31837996	FYPO:0000854	abnormal nucleosome positioning in euchromatin	(comment: similar to pob3delta alone)
PMID:31837996	FYPO:0005528	decreased subtelomeric chromatin knob formation [has_severity] high	(comment: similar to pob3delta alone)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1B)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium [assayed_transcript] PomBase:SPMTR.01	(Fig. 1C)
PMID:31883795	GO:0034399	nuclear periphery	(Fig. 1E and F)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium [assayed_transcript] PomBase:SPMTR.01	(Fig. 2G)
PMID:31883795	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [has_severity] high [assayed_protein] PomBase:SPCC4G3.18	(Fig. 3C and D)
PMID:31883795	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [has_severity] high [assayed_protein] PomBase:SPCC4G3.18	(Fig. 3C and D)
PMID:31883795	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [has_severity] high [assayed_protein] PomBase:SPBC16C6.12c	(Fig. 3C and D)
PMID:31883795	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [has_severity] high [assayed_protein] PomBase:SPBC16C6.12c	(Fig. 3C and D)
PMID:31883795	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC4G3.18 [has_severity] high	(Fig. 3C and D)
PMID:31883795	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC4G3.18 [has_severity] high	(Fig. 3C and D)
PMID:31883795	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [has_severity] high [assayed_protein] PomBase:SPBC16C6.12c	(Fig. 3C and D)
PMID:31883795	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [has_severity] high [assayed_protein] PomBase:SPBC16C6.12c	(Fig. 3C and D)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 3F)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 3F)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low [assayed_transcript] PomBase:SPMTR.01	(Fig. 3G)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high [assayed_transcript] PomBase:SPMTR.01	(Fig. 3H)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high [assayed_transcript] PomBase:SPMTR.01	(Fig. 3H)
PMID:31883795	FYPO:0008369	decreased silent mating type cassette heterochromatin tethering to nuclear periphery during vegetative growth	(Fig. 4C and D)
PMID:31883795	FYPO:0008369	decreased silent mating type cassette heterochromatin tethering to nuclear periphery during vegetative growth	(Fig. 4C and D)
PMID:31883795	FYPO:0008369	decreased silent mating type cassette heterochromatin tethering to nuclear periphery during vegetative growth	(Fig. 4C and D)
PMID:31883795	FYPO:0008368	abolished histone H3-K9 trimethylation at centromere during vegetative growth	(Fig. 5A and B)
PMID:31883795	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 5A and B)
PMID:31883795	FYPO:0008364	normal histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth	(Fig. 5A and B)
PMID:31883795	FYPO:0000883	decreased histone H3-K9 trimethylation at centromere during vegetative growth [has_severity] medium	(Fig. 5A and B)
PMID:31883795	FYPO:0000883	decreased histone H3-K9 trimethylation at centromere during vegetative growth [has_severity] medium	(Fig. 5A and B)
PMID:31883795	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 5A and B)
PMID:31883795	FYPO:0000883	decreased histone H3-K9 trimethylation at centromere during vegetative growth [has_severity] medium	(Fig. 5A and B)
PMID:31883795	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 5A and B)
PMID:31883795	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 5A and B)
PMID:31883795	FYPO:0008368	abolished histone H3-K9 trimethylation at centromere during vegetative growth	(Fig. 5A and B)
PMID:31883795	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 5A and B)
PMID:31883795	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 5A and B)
PMID:31883795	FYPO:0008368	abolished histone H3-K9 trimethylation at centromere during vegetative growth	(Fig. 5A and B)
PMID:31883795	FYPO:0008368	abolished histone H3-K9 trimethylation at centromere during vegetative growth	(Fig. 5A and B)
PMID:31883795	FYPO:0008367	decreased duration of heterochromatin maintenance involved in chromatin silencing at silent mating type cassette	(Fig. 5D)
PMID:31883795	FYPO:0008367	decreased duration of heterochromatin maintenance involved in chromatin silencing at silent mating type cassette	(Fig. 5D)
PMID:31883795	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 6A and Fig. S6B)
PMID:31883795	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 6A and Fig. S6B)
PMID:31883795	FYPO:0008368	abolished histone H3-K9 trimethylation at centromere during vegetative growth	(Fig. 6A and Fig. S6B)
PMID:31883795	FYPO:0008368	abolished histone H3-K9 trimethylation at centromere during vegetative growth	(Fig. 6A and Fig. S6B)
PMID:31883795	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 6A and Fig. S6B)
PMID:31883795	FYPO:0000883	decreased histone H3-K9 trimethylation at centromere during vegetative growth [has_severity] low	(Fig. 6A and Fig. S6B)
PMID:31883795	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC609.05 [assayed_protein] PomBase:SPAC664.01c	(Fig. 6C)
PMID:31883795	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC609.05	(Fig. 6D)
PMID:31883795	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] high	(Fig. 6G)
PMID:31883795	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] high	(Fig. 6G)
PMID:31883795	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] high	(Fig. 6G)
PMID:31883795	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] medium	(Fig. 6G)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 7A)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 7A)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 7A)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 7A)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1B)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1B)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1E)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1E)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1E)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1E)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1E)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1E)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1E)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S2D)
PMID:31883795	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. S2D)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. S2D)
PMID:31883795	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. S2D)
PMID:31883795	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. S2D)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S7C)
PMID:31883795	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S7C)
PMID:31883795	GO:0140464	subnuclear spatial organization of silent mating-type cassette heterochromatin	Our analyses show that RIXC bound to the H3K9me-Swi6 platform tethers heterochromatic regions to Amo1 at the nuclear periphery, which in turn stabilizes heterochromatin through suppression of histone turnover (Figure 7D).
PMID:31883795	GO:0062239	heterochromatin-nuclear membrane anchor activity [part_of] subnuclear spatial organization of silent mating-type cassette heterochromatin	Our analyses show that RIXC bound to the H3K9me-Swi6 platform tethers heterochromatic regions to Amo1 at the nuclear periphery, which in turn stabilizes heterochromatin through suppression of histone turnover (Figure 7D).
PMID:31895039	FYPO:0002060	viable vegetative cell population	(Fig. 1) (comment: CONDITION 36.5°C)
PMID:31895039	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 17	(Fig. 1c)
PMID:31895039	FYPO:0002394	decreased protein acetylation during vegetative growth [assayed_using] PomBase:SPAC10F6.09c	(Fig. 2 supp1)
PMID:31895039	FYPO:0007499	increased chromatin binding at cohesin associated regions [assayed_using] PomBase:SPAC31A2.05c	(Fig. 2)
PMID:31895039	FYPO:0007499	increased chromatin binding at cohesin associated regions [has_severity] high [assayed_using] PomBase:SPAC31A2.05c	(Fig. 2)
PMID:31895039	FYPO:0007198	normal mitotic centromeric sister chromatid cohesion [has_penetrance] 80	(Fig. 2)
PMID:31895039	FYPO:0000674	normal cell population growth at high temperature	(Fig. 2)
PMID:31895039	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:31895039	FYPO:0002060	viable vegetative cell population	(Fig. 2)
PMID:31895039	FYPO:0002060	viable vegetative cell population	(Fig. 2)
PMID:31895039	FYPO:0002060	viable vegetative cell population	(Fig. 2)
PMID:31895039	FYPO:0002060	viable vegetative cell population	(Fig. 2)
PMID:31895039	FYPO:0001838	decreased protein phosphorylation during vegetative growth [has_severity] high [assayed_using] PomBase:SPCC338.17c	(Fig. 2)
PMID:31895039	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 40	(Fig. 2)
PMID:31895039	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 0.1	(Fig. 2)
PMID:31895039	FYPO:0007499	increased chromatin binding at cohesin associated regions [has_severity] high [assayed_using] PomBase:SPCC338.17c	(Fig. 2)
PMID:31895039	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 10	(Fig. 2)
PMID:31895039	FYPO:0000460	decreased mitotic centromeric sister chromatid cohesion [has_penetrance] 65	(Fig. 2)
PMID:31895039	FYPO:0002060	viable vegetative cell population	(Fig. 2)
PMID:31895039	FYPO:0002060	viable vegetative cell population	(Fig. 2)
PMID:31895039	FYPO:0000674	normal cell population growth at high temperature	(Fig. 2)
PMID:31895039	FYPO:0007499	increased chromatin binding at cohesin associated regions [has_severity] high [assayed_using] PomBase:SPCC338.17c	(Fig. 2)
PMID:31895039	FYPO:0007499	increased chromatin binding at cohesin associated regions [assayed_using] PomBase:SPCC338.17c	(Fig. 2)
PMID:31895039	FYPO:0007499	increased chromatin binding at cohesin associated regions [has_severity] high [assayed_using] PomBase:SPAC31A2.05c	(Fig. 2)
PMID:31895039	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 70	(Fig. 2)
PMID:31895039	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 60	(Fig. 2)
PMID:31895039	FYPO:0007498	decreased chromatin binding at cohesin associated regions [assayed_using] PomBase:SPCC338.17c	(Fig. 2) (comment: CHECK Phenotype suppressed by the deletion of the pef1 gene)
PMID:31895039	FYPO:0007498	decreased chromatin binding at cohesin associated regions [assayed_using] PomBase:SPAC31A2.05c	(Fig. 2) (comment: CHECK Phenotype suppressed by the deletion of the pef1 gene)
PMID:31895039	FYPO:0002060	viable vegetative cell population	(Fig. 2) (comment: CONDITION 34°C)
PMID:31895039	FYPO:0002060	viable vegetative cell population	(Fig. 2) (comment: CONDITION 36.5°C)
PMID:31895039	FYPO:0007498	decreased chromatin binding at cohesin associated regions [has_severity] high [assayed_using] PomBase:SPAC31A2.05c	(Fig. 2) Phenotype suppressed by the deletion of pef1
PMID:31895039	FYPO:0007498	decreased chromatin binding at cohesin associated regions [has_severity] high [assayed_using] PomBase:SPCC338.17c	(Fig. 2) Phenotype suppressed by the deletion of pef1
PMID:31895039	FYPO:0002061	inviable vegetative cell population	(Fig. 2b)
PMID:31895039	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPCC338.17c	(Fig. 5g)
PMID:31895039	FYPO:0007499	increased chromatin binding at cohesin associated regions [has_severity] high [assayed_using] PomBase:SPAC31A2.05c	(Fig. 7) The phenotype is exacerbated by pph3 deletion and rescued by pef1 deletion
PMID:31895039	FYPO:0002060	viable vegetative cell population	(Figure 1—Figure supplement 1)
PMID:31895039	FYPO:0002061	inviable vegetative cell population	(Figure 1—Figure supplement 1)
PMID:31895039	FYPO:0001234	slow vegetative cell population growth	"(Figure 1—Figure supplement 1) ""although colonies were tiny and grew very slowly"""
PMID:31895039	FYPO:0007498	decreased chromatin binding at cohesin associated regions [has_penetrance] high [assayed_using] PomBase:SPCC338.17c	(Figure 2, S1)
PMID:31895039	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPCC338.17c	"(Figure 5D) ""In vitro Rad21 phosphorylation was abolished when Pef1 was purified from psl1 deleted cells"""
PMID:31895039	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPCC338.17c	(Figure 5E, Figure 5—Figure supplement 1). Replacement of T262 by an alanine abolished in vitro Rad21 phosphorylation by Pef1-GFP
PMID:31895039	FYPO:0002060	viable vegetative cell population	(comment: CONDITION 34°C), Fig. 2
PMID:31895039	FYPO:0002061	inviable vegetative cell population	(comment: CONDITION 34°C), Fig. 2
PMID:31895039	FYPO:0002060	viable vegetative cell population	(comment: CONDITION 36.5°C)
PMID:31895039	GO:0045876	positive regulation of sister chromatid cohesion [happens_during] mitotic G1 phase	(comment: antagonises pef1)
PMID:31895039	GO:0045875	negative regulation of sister chromatid cohesion [happens_during] mitotic G1 phase	Pef1 ablation or chemical inactivation of its kinase activity stimulates Rad21 and Mis4 binding to their cognates sites on chromosomes. The effect in most prominent in the G1 phase of the mitotic cycle.
PMID:31895039	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPCC338.17c [part_of] negative regulation of sister chromatid cohesion	Phosphorylates Rad21 on threonine 262. Fig. 2
PMID:31895039	GO:0005634	nucleus	Psm1 and Mis4 are found in Pef1 immunoprecipitates (Fig. 5AB)
PMID:31911490	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(Fig. 1B)
PMID:31911490	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(Fig. 1B)
PMID:31911490	FYPO:0003214	normal protein phosphorylation during cellular response to glucose starvation [assayed_using] PomBase:SPCC757.09c	(Fig. 1B)
PMID:31911490	FYPO:0001122	elongated vegetative cell	(Fig. 1B)
PMID:31911490	FYPO:0003214	normal protein phosphorylation during cellular response to glucose starvation [assayed_using] PomBase:SPCC757.09c	(Fig. 1B) cell length at division either of pmk1􏰂 cells or in a mutant strain lacking the dual-specificity phosphatase Pmp1 that dephosphorylates and inactivates Pmk1 in vivo (14), ... was similar to that of wild-type cells (Fig. 1B)
PMID:31911490	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(Fig. 1B,1C) (14.04+0.25 versus 11.98+0.29μm, respectively)
PMID:31911490	FYPO:0002700	increased protein kinase activity [assayed_enzyme] PomBase:SPAC24B11.06c	(Fig. 1D). In addition, basal Sty1 activity was significantly higher in exponentially growing rnc1􏰂 cells expressing a genomic C-terminal hemagglutinin (HA)-tagged version of the MAP kinase, compared to wild-type cells or a pmk1􏰂 mutant
PMID:31911490	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC887.10	(Fig. 2)
PMID:31911490	FYPO:0000836	increased protein level [assayed_using] PomBase:SPBC409.07c	(Fig. 2B)
PMID:31911490	FYPO:0002680	increased protein phosphorylation [assayed_using] PomBase:SPAC24B11.06c [has_severity] high	(Fig. 2C)
PMID:31911490	FYPO:0001885	decreased protein phosphorylation during salt stress [assayed_using] PomBase:SPBC119.08	(Fig. 3f)
PMID:31911490	GO:0005515	protein binding [part_of] negative regulation of p38MAPK cascade [happens_during] cellular response to stress	(Fig. 4B)
PMID:31911490	FYPO:0005749	decreased protein phosphorylation during glucose starvation [assayed_using] PomBase:SPCC757.09c	(Fig. 4h)
PMID:31911490	FYPO:0003552	decreased RNA catabolic process [assayed_using] PomBase:SPAC9G1.02	(Fig. 5B)
PMID:31911490	FYPO:0002700	increased protein kinase activity [assayed_using] PomBase:SPAC24B11.06c [assayed_enzyme] PomBase:SPAC24B11.06c	(Fig. 5C)
PMID:31911490	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(Fig. 5e)
PMID:31911490	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(comment:12.13 + 0.1)
PMID:31911490	FYPO:0002134	decreased protein-RNA interaction [assayed_using] PomBase:SPAC19D5.01	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1Δ, wis1Δ , atf1Δ , pyp1Δ , and pyp2Δ mRNAs in vitro (Fig. 5A)
PMID:31911490	FYPO:0002134	decreased protein-RNA interaction [assayed_using] PomBase:SPBC409.07c	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1Δ, wis1Δ , atf1Δ , pyp1Δ , and pyp2Δ mRNAs in vitro (Fig. 5A)
PMID:31911490	FYPO:0002134	decreased protein-RNA interaction [assayed_using] PomBase:SPBC29B5.01	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1Δ, wis1Δ , atf1Δ , pyp1Δ , and pyp2Δ mRNAs in vitro (Fig. 5A)
PMID:31911490	FYPO:0002134	decreased protein-RNA interaction [assayed_using] PomBase:SPAC26F1.10c	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1Δ, wis1Δ , atf1Δ , pyp1Δ , and pyp2Δ mRNAs in vitro (Fig. 5A)
PMID:31911490	FYPO:0002134	decreased protein-RNA interaction [assayed_using] PomBase:SPAC9G1.02	A nonphosphorylatable GST-Rnc1 fusion [GST-Rnc1(S/T6A)] expressed in fission yeast was several times less effective than the wild type (GST-Rnc1) in binding wak1Δ, wis1Δ , atf1Δ , pyp1Δ , and pyp2Δ mRNAs in vitro (Fig. 5A)
PMID:31911490	FYPO:0000836	increased protein level [assayed_using] PomBase:SPAC19D5.01 [has_severity] low	Pyp2 protein levels increased +2 times in the mutant background (Fig. 5C), but they were of a lower magnitude than that in rnc1􏰂 versus wild-type cells (+8 to 9 times) (Fig. 2C
PMID:31911490	GO:0004707	MAP kinase activity [has_input] PomBase:SPCC757.09c	These results suggest that while T50 is a main phosphorylation site for Sty1 within Rnc1, other phosphosites are likely targeted by this kinase in vivo.
PMID:31911490	FYPO:0000836	increased protein level [assayed_using] PomBase:SPBC409.07c	and enhanced expression of Wak1, Wis1, and Pyp1 proteins during unperturbed growth (Fig. 5C)
PMID:31932483	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPBC409.07c [assayed_substrate] PomBase:SPAC24B11.06c	(Fig. 2)
PMID:31932483	MOD:00210	L-cysteine sulfenic acid	(Fig. 3)
PMID:31932483	FYPO:0004333	increased protein phosphorylation during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC24B11.06c	(Fig. 4A)
PMID:31932483	FYPO:0000087	sensitive to hydrogen peroxide	(Fig. 4B) (comment: CONDITION 0.5 mM H2O2 in agar)
PMID:31932483	FYPO:0005947	normal growth on potassium chloride	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	FYPO:0005947	normal growth on potassium chloride	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	FYPO:0001214	sensitive to potassium chloride	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	FYPO:0005947	normal growth on potassium chloride	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	FYPO:0005947	normal growth on potassium chloride	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	FYPO:0005947	normal growth on potassium chloride	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	FYPO:0005947	normal growth on potassium chloride	(Fig. 4B) (comment: CONDITION 1M KCl in agar)
PMID:31932483	FYPO:0000962	normal growth on hydrogen peroxide	(Fig. 4B) (comment: CONDITION0.5 mM H2O2 in agar)
PMID:31932483	FYPO:0000962	normal growth on hydrogen peroxide	(Fig. 4B) (comment: CONDITION0.5 mM H2O2 in agar)
PMID:31932483	FYPO:0000962	normal growth on hydrogen peroxide	(Fig. 4B) (comment: CONDITION0.5 mM H2O2 in agar)
PMID:31932483	FYPO:0000087	sensitive to hydrogen peroxide	(Fig. 4B) (comment: CONDITION0.5 mM H2O2 in agar)
PMID:31932483	FYPO:0000087	sensitive to hydrogen peroxide	(Fig. 4B) (comment: CONDITION0.5 mM H2O2 in agar)
PMID:31932483	FYPO:0000962	normal growth on hydrogen peroxide	(Fig. 4B) (comment: CONDITION0.5 mM H2O2 in agar)
PMID:31932483	FYPO:0007481	attenuated increase in transcription during cellular response to stress in presence of small molecule [assayed_using] PomBase:SPBC106.02c	(Fig. 6E)
PMID:31932483	FYPO:0007332	abolished increase in protein phosphorylation during cellular response to stress in presence of small molecule	(Fig. 6F)
PMID:31932483	FYPO:0007332	abolished increase in protein phosphorylation during cellular response to stress in presence of small molecule [assayed_using] PomBase:SPAC24B11.06c	(Fig. 7E)
PMID:31941401	FYPO:0006295	abolished macroautophagy during nitrogen starvation	(Fig. S2)
PMID:31941401	FYPO:0006266	normal vacuole size during vegetative growth	(Fig. S2)
PMID:31941401	FYPO:0000674	normal cell population growth at high temperature	(Fig. S2)
PMID:31941401	FYPO:0006295	abolished macroautophagy during nitrogen starvation	(Figure 1B)
PMID:31941401	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC660.08 [assayed_using] PomBase:SPBP8B7.24c	(Figure 1E)
PMID:31941401	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC660.08 [assayed_using] PomBase:SPBP8B7.24c	(Figure 1F)
PMID:31941401	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC660.08 [assayed_using] PomBase:SPBP8B7.24c	(Figure 1G)
PMID:31941401	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC660.08 [assayed_using] PomBase:SPBP8B7.24c	(Figure 1G)
PMID:31941401	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC660.08 [assayed_using] PomBase:SPBP8B7.24c	(Figure 1G)
PMID:31941401	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC660.08 [assayed_using] PomBase:SPBP8B7.24c	(Figure 1G)
PMID:31941401	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC660.08 [assayed_using] PomBase:SPBP8B7.24c	(Figure 1G)
PMID:31941401	FYPO:0006295	abolished macroautophagy during nitrogen starvation	(Figure 2A) (comment: Pho8Δ60 autophagy assay)
PMID:31941401	FYPO:0002615	decreased protein localization to pre-autophagosomal structure [has_severity] medium [assayed_using] PomBase:SPBP8B7.24c	(Figure 3A, B)
PMID:31941401	FYPO:0002615	decreased protein localization to pre-autophagosomal structure [has_severity] medium [assayed_using] PomBase:SPBC1711.11	(Figure 3A,B) but reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	FYPO:0002615	decreased protein localization to pre-autophagosomal structure [has_severity] medium [assayed_using] PomBase:SPAC25A8.02	(Figure 3A,B) but reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	FYPO:0002615	decreased protein localization to pre-autophagosomal structure [has_severity] medium [assayed_using] PomBase:SPBC405.05	(Figure 3A,B) but reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	FYPO:0002615	decreased protein localization to pre-autophagosomal structure [has_severity] medium [assayed_using] PomBase:SPBC4B4.10c	(Figure 3A,B) but reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	FYPO:0002615	decreased protein localization to pre-autophagosomal structure [has_severity] medium [assayed_using] PomBase:SPBC31E1.01c	(Figure 3A,B) but reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	FYPO:0002615	decreased protein localization to pre-autophagosomal structure [has_severity] medium [assayed_using] PomBase:SPAC823.16c	(Figure 3A,B) but reduced the PAS accumulation of the ...t Atg14, ...s Atg18b and Atg24b, Atg2, Atg5, Atg16, and Atg8
PMID:31941401	FYPO:0000381	decreased macroautophagy [has_severity] medium	(comment: Pho8Δ60 assay) (Fig. S3A).
PMID:31941401	FYPO:0000381	decreased macroautophagy [has_severity] medium	(comment: Pho8Δ60 assay) (Fig. S3A).
PMID:31941401	FYPO:0000381	decreased macroautophagy [has_severity] medium	In contrast, Pho8Δ60 activity was only restored to about half of the wild-type level when expressing Atg38[AIM mut]. AND Tdh1-YFP processing assay
PMID:31980821	FYPO:0007414	subtelomere expansion during G0	(Fig. 2B)
PMID:31980821	FYPO:0007419	decreased telomere tethering at nuclear periphery during G0	(Fig. 2D) althouh also the percentage of cells that contain a unique telomeric cluster in G0 after streaks 3 and 4 (Figure 2D). We found that telomere attrition observed in the absence of telomerase did not significantly impair telomere hyperclusterization in quiescence. However, telomere clusterization did not reach WT level in ter1Δ cells after 3 days in G0.
PMID:31980821	FYPO:0007419	decreased telomere tethering at nuclear periphery during G0	(Fig. 3D) We confirmed that telomere foci moved from nuclear periphery to a more central area (zone 1 to zone 2 or 3) in bqt4Δ Vg cells
PMID:31980821	FYPO:0006516	normal telomere length during G0	(Fig. 5A) bqt4delta/ telomerase + cells exhibited wild-type telomeres that were stable in post-mitotic cells
PMID:31980821	FYPO:0007269	normal interphase mitotic telomere clustering during vegetative growth	(Figure 2D) We found that telomere attrition observed in the absence of telomerase did not significantly impair telomere hyperclusterization in quiescence. However, telomere clusterization did not reach WT level in ter1Δ cells after 3 days in G0.
PMID:31980821	FYPO:0002955	abnormal G0 to G1 transition	As previously shown, we observed that telomere erosion and STEEx formation in ter1Δ cells correlates with defects to exit properly from G0 (22)
PMID:31980821	FYPO:0004085	decreased vegetative cell growth [has_penetrance] high	In contrast to ter1Δ cells in which the loss of growth capacity was progressive, the growth of bqt4Δ ter1Δ cells was severely impaired (Figure 4A and Supplementary Figure S2).
PMID:31980821	FYPO:0002955	abnormal G0 to G1 transition [has_severity] high	Indeed, in bqt4Δ ter1Δ cells the percentage of cells that are unable to form a colony increased in correlation with the massive accumulation of STEEx at D1 and D3 of senescence
PMID:31980821	FYPO:0007414	subtelomere expansion during G0 [has_severity] high	STEEx were readily detected as two bands at 1500 and 900 bp, the highest one being prevalent (Figure 5A, right panel). Strikingly, we observed a massive accumulation of STEEx in quiescent bqt4Δ ter1Δ cells at early time points of quiescence (Figure 5A).
PMID:31980821	FYPO:0007421	increased transcription at telomere during G0 [assayed_using] TERRA [has_severity] high	TERRA level was higher in bqt4Δ than WT in vegetative cells and this difference was substantially intensified after 48H in quiescence (Figure 6A)
PMID:31980821	FYPO:0002908	increased transcription at telomere during vegetative growth [assayed_using] TERRA	TERRA level was higher in bqt4Δ than WT in vegetative cells and this difference was substantially intensified after 48H in quiescence (Figure 6A)
PMID:31980821	FYPO:0007421	increased transcription at telomere during G0 [has_severity] high	When ter1+ gene was deleted in bqt4Δ cells, we observed that the combination of telomere erosion and NE dissociation provokes a massive accumulation of TERRA in Vg cells and this robust increase in transcription is even stronger after 48H in quiescence
PMID:31980821	FYPO:0002908	increased transcription at telomere during vegetative growth [has_severity] high	When ter1+ gene was deleted in bqt4Δ cells, we observed that the combination of telomere erosion and NE dissociation provokes a massive accumulation of TERRA in Vg cells and this robust increase in transcription is even stronger after 48H in quiescence
PMID:31980821	FYPO:0007421	increased transcription at telomere during G0 [assayed_using] TERRA	accumulation of TERRA depends on Cid14, a RNA poly adenyl-transferase, (Supplementary Figure S5)
PMID:31980821	FYPO:0007419	decreased telomere tethering at nuclear periphery during G0	zoning of telomere foci within the nuclear envelope was severely impaired in bqt4Δ ter1Δ for vegetative and quiescent cells (Supplementary Figure S3D and E).
PMID:31980821	FYPO:0007419	decreased telomere tethering at nuclear periphery during G0	zoning of telomere foci within the nuclear envelope was severely impaired in bqt4Δ ter1Δ for vegetative and quiescent cells (Supplementary Figure S3D and E).
PMID:32012158	FYPO:0007280	decreased protein localization to nuclear exosome focus [assayed_using] PomBase:SPAC2F7.14c	(Figure 1A)
PMID:32012158	FYPO:0006080	normal protein localization to nuclear exosome focus during vegetative growth [assayed_protein] PomBase:SPBC16E9.12c	(Figure 1A)
PMID:32012158	FYPO:0007280	decreased protein localization to nuclear exosome focus [assayed_using] PomBase:SPAC1F3.01	(Figure 1A)
PMID:32012158	FYPO:0007280	decreased protein localization to nuclear exosome focus [has_severity] low [assayed_using] PomBase:SPAC1F3.01	(Figure 1A)
PMID:32012158	FYPO:0007280	decreased protein localization to nuclear exosome focus [assayed_using] PomBase:SPBC26H8.10	(Figure 1A)
PMID:32012158	FYPO:0006080	normal protein localization to nuclear exosome focus during vegetative growth [assayed_using] PomBase:SPAC1F3.01	(Figure 1A)
PMID:32012158	FYPO:0003042	abolished protein localization to nuclear exosome focus [assayed_using] PomBase:SPAC1F3.01	(Figure 2)
PMID:32012158	FYPO:0006080	normal protein localization to nuclear exosome focus during vegetative growth [assayed_using] PomBase:SPAC1006.03c	(Figure 2)
PMID:32012158	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC736.12c [assayed_using] PomBase:SPAC1F3.01	(Figure 3A)
PMID:32012158	FYPO:0003042	abolished protein localization to nuclear exosome focus [assayed_using] PomBase:SPAC2F7.14c	(Figure 5A)
PMID:32012158	FYPO:0003042	abolished protein localization to nuclear exosome focus [assayed_using] PomBase:SPBC26H8.10	(Figure 5A)
PMID:32012158	FYPO:0006080	normal protein localization to nuclear exosome focus during vegetative growth [assayed_using] PomBase:SPAC1006.03c	(Figure 5B)
PMID:32012158	FYPO:0006080	normal protein localization to nuclear exosome focus during vegetative growth [assayed_using] PomBase:SPCC736.12c	(Figure 5B)
PMID:32012158	FYPO:0007280	decreased protein localization to nuclear exosome focus [assayed_using] PomBase:SPAC1F3.01 [has_severity] low	(Figure 6A)
PMID:32012158	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC29A10.14	(Figure S3A)
PMID:32012158	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	(Figure S3A)
PMID:32012158	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC32H8.11	(Figure S3A)
PMID:32012158	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC29A10.14	(Figure S3A)
PMID:32012158	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	(Figure S3A)
PMID:32012158	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC32H8.11	(Figure S3A)
PMID:32012158	FYPO:0006821	slow vegetative cell growth	(Figure S3A)
PMID:32012158	FYPO:0002085	normal vegetative cell growth	(Figure S3A)
PMID:32012158	FYPO:0003557	increased antisense RNA level [assayed_using] PomBase:SPNCRNA.1365	(Figure S3A) COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED
PMID:32012158	FYPO:0003557	increased antisense RNA level [assayed_using] PomBase:SPNCRNA.1365	(Figure S3A) COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED
PMID:32012158	FYPO:0006996	normal antisense RNA level [assayed_using] PomBase:SPNCRNA.1365	(Figure S3A) COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED
PMID:32012158	FYPO:0003557	increased antisense RNA level [assayed_using] PomBase:SPNCRNA.1365	(Figure S3A) COULD ALSO ADD TO ANTISENS RPL402, BUT NOT ANNOTATED IN GENOME
PMID:32012158	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPAC1F3.01 [part_of] nuclear mRNA surveillance of meiosis-specific transcripts	The interaction between these proteins was abolished in the absence of red1 (Fig 3A), suggesting that Red1 physically links Mmi1 with the exosome. and Fig 4B The direct binding of Red1 with Rrp6 was also observed (Fig 4B).
PMID:32023460	FYPO:0007273	increased cortical endoplasmic reticulum remodeling	(Fig. 2) increased cortical ER remodeling dynamics
PMID:32023460	FYPO:0007273	increased cortical endoplasmic reticulum remodeling	(Fig. 2) increased cortical ER remodeling dynamics
PMID:32023460	FYPO:0007273	increased cortical endoplasmic reticulum remodeling	(Fig. 2) the cortical tubular ER pattern changes faster than wild type
PMID:32023460	FYPO:0007268	decreased cortical endoplasmic reticulum remodeling	(Figure 3A) decreased cortical ER remodeling dynamics the cortical tubular ER pattern changes slower than wild type
PMID:32023460	FYPO:0007268	decreased cortical endoplasmic reticulum remodeling	(Figure 3A) the cortical tubular ER pattern changes slower than wild type
PMID:32023460	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering	(Figure 4, S4B).
PMID:32023460	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC736.15 [assayed_using] PomBase:SPBC16G5.05c	(Figure 4, S4B).
PMID:32023460	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering	(Figure 4, S4B).
PMID:32023460	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering	(Figure 4, S4B).
PMID:32023460	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering	(Figure 4, S4B).
PMID:32023460	FYPO:0007265	long eisosome filaments present in decreased numbers	(Figure S1F). Pil1 mis-assembled into fewer and longer filaments
PMID:32023460	FYPO:0002680	increased protein phosphorylation [assayed_using] PomBase:SPCC736.15	(Figure S1F). increased Pil1 phosphorylation was detected in these cells
PMID:32023460	FYPO:0007268	decreased cortical endoplasmic reticulum remodeling	(Figure S3C). the cortical tubular ER pattern changes slower than wild type
PMID:32023460	FYPO:0007268	decreased cortical endoplasmic reticulum remodeling	(Figure S3D)
PMID:32023460	FYPO:0007273	increased cortical endoplasmic reticulum remodeling	(Figure S5G). the cortical tubular ER pattern changes faster than wild type
PMID:32023460	FYPO:0002872	abnormal endoplasmic reticulum localization	(Figures 1A, 1B) (EM) data also confirmed that eisosomes/MCC associated with the cER, especially with curved cER rims, over the lateral cell cortex in WT (Figures 1C and S1A). Such an association was abolished in scs2Dscs22D cells lacking ER-PM contacts.(comment: the Exp says more but I don't know how to capture that)
PMID:32023460	FYPO:0007263	eisosomes present in decreased numbers	(comment: PMID:32023460) Of note, the PM coverage of eisosomes was also reduced in scs2Dscs22D cells (Figure S1B), implicating VAPs in the regulation of eisosome assembly.
PMID:32023460	GO:0007029	endoplasmic reticulum organization	(comment: cortical)
PMID:32023460	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC16G5.05c [assayed_using] PomBase:SPCC736.15	Pil1 lacking the C terminus failed to interact with Scs2 (Figure S5F
PMID:32023460	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPCC736.15	decreased Pil1 protein abundance Figure S1F
PMID:32023460	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPCC736.15	decreased Pil1 protein abundance Figure S1F
PMID:32023460	FYPO:0007273	increased cortical endoplasmic reticulum remodeling	increased cortical ER remodeling dynamics
PMID:32023460	FYPO:0007273	increased cortical endoplasmic reticulum remodeling	increased cortical ER remodeling dynamics
PMID:32023460	FYPO:0007273	increased cortical endoplasmic reticulum remodeling	increased cortical ER remodeling dynamics the cortical tubular ER pattern changes faster than wild type
PMID:32023460	FYPO:0007263	eisosomes present in decreased numbers	resulting in the formation of fewer punctate eisosomes (Figure S1B).
PMID:32023460	FYPO:0007268	decreased cortical endoplasmic reticulum remodeling	the cortical tubular ER pattern changes slower than wild type
PMID:32023460	FYPO:0007268	decreased cortical endoplasmic reticulum remodeling	the cortical tubular ER pattern changes slower than wild type
PMID:32023460	FYPO:0007268	decreased cortical endoplasmic reticulum remodeling	the cortical tubular ER pattern changes slower than wild type
PMID:32032353	FYPO:0000590	normal sporulation	(comment: Both wtf21 alleles were found at equal frequency in the viable spores.)
PMID:32032353	GO:0005737	cytoplasm [part_of] ascospore	(comment: S.p. wtf13 assayed; doesn't specify which isoform (or if it's both))
PMID:32032353	GO:0005737	cytoplasm [part_of] ascospore	(comment: S.p. wtf13 assayed; doesn't specify which isoform (or if it's both))
PMID:32032353	GO:0005737	cytoplasm [part_of] ascospore	(comment: assayed by expressing S.k. ortholog in S.p.)
PMID:32032353	GO:0005783	endoplasmic reticulum	(comment: assayed by expressing S.k. ortholog in S.p.)
PMID:32032353	GO:0005737	cytoplasm [part_of] ascospore	(comment: assayed by expressing S.k. ortholog in S.p.)
PMID:32032353	GO:0110134	meiotic drive	(comment: inferred from crosses involving hemizygous diploids)
PMID:32032353	GO:0110134	meiotic drive	(comment: inferred from crosses involving hemizygous diploids)
PMID:32047038	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAPB17E12.04c [assayed_using] PomBase:SPAC17G6.12	(Fig. 5G) The IP6-binding pocket formed between CSN2 and Rbx1 is remarkably conserved from yeasts to plants and humans (Figs. 2D and 3D). Deleting ipk1, the yeast IP6 synthase, abolishes Csn2 interaction with Cul1 in Schizosaccharomyces pombe
PMID:32047038	FYPO:0000268	sensitive to UV during vegetative growth	(Fig. 5H) This defect in UV-resistance can be rescued by wild-type SpCsn2, but not its IP6 binding-deficient K70E mutant .
PMID:32047038	FYPO:0000268	sensitive to UV during vegetative growth	(Fig. 5H) This defect in UV-resistance can be rescued by wild-type SpCsn2, but not its IP6 binding-deficient K70E mutant .
PMID:32047038	FYPO:0000969	normal growth during cellular response to UV	(Fig. 5H) This defect in UV-resistance can be rescued by wild-type SpCsn2, but not its IP6 binding-deficient K70E mutant .
PMID:32053662	FYPO:0004455	decreased protein localization to nucleus [has_severity] high [assayed_using] PomBase:SPBC19C2.09	(Fig. 6b, c)
PMID:32053662	FYPO:0004455	decreased protein localization to nucleus [has_severity] high [assayed_using] PomBase:SPBC19C2.09	(Fig. 6b, c)
PMID:32053662	FYPO:0004455	decreased protein localization to nucleus [has_severity] high [assayed_using] PomBase:SPBC19C2.09	(Fig. 6b, c)
PMID:32053662	FYPO:0004455	decreased protein localization to nucleus [has_severity] high [assayed_using] PomBase:SPBC19C2.09	(Fig. 6b, c)
PMID:32053662	FYPO:0004455	decreased protein localization to nucleus [has_severity] high [assayed_using] PomBase:SPBC19C2.09	(Fig. 6b, c)
PMID:32053662	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high	(Fig. 6d)
PMID:32053662	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPBC19C2.09 [has_severity] low	(Fig. 6d)
PMID:32053662	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high	(Fig. 6d)
PMID:32053662	FYPO:0003251	decreased transcription from SRE promoter [has_severity] medium	(Figure 5a-c)
PMID:32053662	FYPO:0003251	decreased transcription from SRE promoter [has_severity] high	(Figure 5a-c)
PMID:32053662	FYPO:0003251	decreased transcription from SRE promoter [has_severity] high	(Figure 5a-c)
PMID:32053662	FYPO:0003251	decreased transcription from SRE promoter [has_severity] medium	(Figure 5a-c)
PMID:32053662	FYPO:0003251	decreased transcription from SRE promoter [has_severity] medium	(Figure 5a-c)
PMID:32053662	FYPO:0003251	decreased transcription from SRE promoter [has_severity] medium	(Figure 5a-c)
PMID:32053662	FYPO:0003251	decreased transcription from SRE promoter [has_severity] medium	(Figure 5a-c)
PMID:32053662	FYPO:0003251	decreased transcription from SRE promoter [has_severity] medium	(Figure 5a-c)
PMID:32062975	FYPO:0003736	normal mitotic index	(Figure 6A)
PMID:32062975	FYPO:0000141	abnormal mitotic sister chromatid segregation	(Figure 6A)
PMID:32062975	FYPO:0001903	normal septation index	(Figure 6A)
PMID:32062975	FYPO:0000091	sensitive to thiabendazole	(Figure 6B)
PMID:32071154	FYPO:0004024	normal protein localization to cytoplasmic stress granule [assayed_using] PomBase:SPAC24B11.06c	(Fig. 2B)
PMID:32071154	FYPO:0007321	decreased stress granule assembly during vegetative growth	(Fig. 4)
PMID:32071154	FYPO:0007323	normal stress granule assembly during cellular response to heat	(Fig. 4)
PMID:32071154	FYPO:0007323	normal stress granule assembly during cellular response to heat	(Fig. 4)
PMID:32071154	FYPO:0007321	decreased stress granule assembly during vegetative growth	(Fig. 4)
PMID:32071154	FYPO:0007321	decreased stress granule assembly during vegetative growth	(Fig. 4)
PMID:32071154	FYPO:0007321	decreased stress granule assembly during vegetative growth	(Fig. 4)
PMID:32071154	FYPO:0007323	normal stress granule assembly during cellular response to heat	(Fig. 4)
PMID:32071154	FYPO:0007319	decreased stress granule assembly during glucose starvation	(Fig. 5C)
PMID:32071154	FYPO:0007319	decreased stress granule assembly during glucose starvation	(Fig. 5C)
PMID:32071154	FYPO:0002348	abolished stress granule assembly during vegetative growth	(Fig. 5C)
PMID:32071154	FYPO:0007319	decreased stress granule assembly during glucose starvation	(Fig. 5C)
PMID:32071154	FYPO:0001896	enlarged P-bodies	(Fig. 6a)
PMID:32071154	FYPO:0001896	enlarged P-bodies	(Fig. 6a)
PMID:32071154	FYPO:0001896	enlarged P-bodies	(Fig. 6a)
PMID:32071154	FYPO:0001896	enlarged P-bodies	(Fig. 6a)
PMID:32071154	FYPO:0002061	inviable vegetative cell population	(Fig. 7)
PMID:32071154	FYPO:0002061	inviable vegetative cell population	(Fig. 7)
PMID:32071154	FYPO:0002061	inviable vegetative cell population	(Fig. 7)
PMID:32071154	FYPO:0002061	inviable vegetative cell population	(Fig. 7)
PMID:32071154	FYPO:0002061	inviable vegetative cell population	(Fig. 7B)
PMID:32071154	FYPO:0002061	inviable vegetative cell population	(Fig. 7B)
PMID:32071154	FYPO:0001357	normal vegetative cell population growth	(Fig. 7B)
PMID:32071154	FYPO:0002061	inviable vegetative cell population	(Fig. 7B)
PMID:32071154	FYPO:0002350	normal stress granule assembly during vegetative growth	(Figure 2C)
PMID:32071154	FYPO:0001897	P-bodies present in decreased numbers during vegetative growth	(Figure 6E)
PMID:32071154	FYPO:0001897	P-bodies present in decreased numbers during vegetative growth	(Figure 6E)
PMID:32071154	FYPO:0006002	normal protein localization to P-bodies [assayed_using] PomBase:SPAC57A7.04c	(Figure 6F)
PMID:32071154	FYPO:0006002	normal protein localization to P-bodies [assayed_using] PomBase:SPAC57A7.04c	(Figure 6F)
PMID:32071154	FYPO:0007317	decreased cytoplasmic translation	(comment: polysome profile)
PMID:32071154	FYPO:0002061	inviable vegetative cell population	(comment: polysome profile)
PMID:32075773	FYPO:0007300	abolished protein aggregate center formation	(Fig. 2B, S2B-D)
PMID:32075773	FYPO:0007299	decreased protein aggregate center formation	(Fig. 2B, S2B-D)
PMID:32075773	FYPO:0007299	decreased protein aggregate center formation	(Fig. 2B, S2B-D)
PMID:32075773	FYPO:0007299	decreased protein aggregate center formation	(Fig. 2B, S2B-D)
PMID:32075773	FYPO:0007299	decreased protein aggregate center formation	(Fig. 2B, S2B-D)
PMID:32075773	FYPO:0007299	decreased protein aggregate center formation	(Fig. 2B, S2B-D)
PMID:32075773	FYPO:0007299	decreased protein aggregate center formation	(Fig. 2B, S2B-D)
PMID:32075773	FYPO:0002348	abolished stress granule assembly during vegetative growth	(Fig. 3D) Lack of Mas5 abolishes both PAC formation and the assembly of stress granules.
PMID:32075773	FYPO:0007302	protein absent from cell during heat shock [assayed_using] PomBase:SPAC1F7.04	(Fig. 4D)
PMID:32075773	FYPO:0007302	protein absent from cell during heat shock [assayed_using] PomBase:SPAC1F7.04	(Fig. 4D)
PMID:32075773	FYPO:0007301	normal protein aggregate center formation	(Fig. S2)
PMID:32075773	FYPO:0007301	normal protein aggregate center formation	(Fig. S2)
PMID:32075773	FYPO:0007301	normal protein aggregate center formation	(Fig. S2)
PMID:32075773	FYPO:0007301	normal protein aggregate center formation	(Fig. S2)
PMID:32075773	FYPO:0007301	normal protein aggregate center formation	(Fig. S2A)
PMID:32075773	FYPO:0002674	normal protein localization to plasma membrane [assayed_using] PomBase:SPAC1F7.04	(Figure 1B)
PMID:32075773	FYPO:0003151	decreased protein level during cellular response to heat [assayed_using] PomBase:SPAC1F7.04	(Figure 1B)
PMID:32075773	FYPO:0001408	sensitive to heat shock [has_severity] high	37C is a moderate heat shock for fission yeast, which does not slow growth nor exerts toxicity to wild-type cultures, but significantly affects the viability of cells lacking stress signaling components, such as the MAP kinase Sty1 (Figures 1E and S1B).
PMID:32084401	FYPO:0003246	normal mitotic S phase progression [has_penetrance] high	(Fig. 1B) cells blocked in G1 by nitrogen starvation and released in presence of nitrogen into S phase with cdc13+ switched off
PMID:32084401	FYPO:0000446	cell cycle arrest at mitotic G2/M phase transition [has_penetrance] high	(Fig. 2A) cells are unable to enter mitosis in absence of cdc13+ expression-no septated cells
PMID:32084401	FYPO:0002061	inviable vegetative cell population	(Fig. 2A) cells expressing only cdc13HPM are unable to form colonies
PMID:32084401	FYPO:0007475	delayed onset of protein localization to mitotic spindle pole body [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPBC582.03	(Fig. 2B-D) Endogenous untagged nmt 41cdc13+ is expressed to allow cells to proceed into mitosis tagged exogenous cdc13HPM or cdc13+ control can be seen at SPB
PMID:32084401	FYPO:0006824	premature protein localization to mitotic spindle pole body [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 2G) when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	FYPO:0006824	premature protein localization to mitotic spindle pole body [has_penetrance] high [assayed_using] PomBase:SPAC23C11.16	(Fig. 2G) when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	FYPO:0006824	premature protein localization to mitotic spindle pole body [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 2G) when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	FYPO:0006824	premature protein localization to mitotic spindle pole body [has_penetrance] high [assayed_using] PomBase:SPAC23C11.16	(Fig. 2G) when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	FYPO:0006824	premature protein localization to mitotic spindle pole body [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 2G) when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	FYPO:0006824	premature protein localization to mitotic spindle pole body [has_penetrance] high [assayed_using] PomBase:SPAC23C11.16	(Fig. 2G) when plo1 is advanced on to the spindle pole body cdc13HPM is also advanced
PMID:32084401	FYPO:0002822	decreased protein localization to mitotic spindle pole body during mitosis [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 2H) cdc13HPM localisation to SPB in mitosis is dependent on plo1 activity
PMID:32084401	FYPO:0002822	decreased protein localization to mitotic spindle pole body during mitosis [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 2H) cdc13HPM localisation to SPB in mitosis is dependent on plo1 activity
PMID:32084401	FYPO:0007567	premature protein localization to mitotic spindle pole body during metaphase [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 2H) when plo1 kinase is inactivated at the restrictive temperature the HPM mutant does not bind to the SPB after release into mitosis
PMID:32084401	FYPO:0002516	premature mitotic G2/M phase transition [has_penetrance] high [has_severity] medium	(Fig. 3A) when an integrated copy of cdc13HPM (at leu1 locus) is expressed from the cdc13 promoter the endogenous cdc13+ cells are advanced into mitosis. This suggests cdc13HPM can do some of events required for mitotic entry. This is independent of the G1/S cyclins
PMID:32084401	FYPO:0000776	normal protein phosphorylation during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Fig. S1-E) cdc2 Y15 phosphorylation same in cdc13+ control and cdc13HPM strain endogenous cdc13+ is completely degraded so does not contribute in the HPM mutant
PMID:32084401	FYPO:0001357	normal vegetative cell population growth	(Fig. S1A, S1C) cells arrested G1 in low nitrogen then released into S phase at restrictive temperature cells the tested for viability at 25°C after S phase with only ccdc13hpm
PMID:32084401	FYPO:0003246	normal mitotic S phase progression [has_penetrance] high	(Fig. S1D) cdc13+ and cdc13HPM are not differentially sensitive to rum1. S phase same in both strains in absence of rum1
PMID:32084401	FYPO:0000776	normal protein phosphorylation during vegetative growth	(Figure S1E) Wee1-dependent CDK-Y15 phosphorylation was similar between Cdc13HPM-CDK and Cdc13WT-CDK
PMID:32084401	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	cdc13HPM mutant can localise to SPB in mitosis
PMID:32084401	GO:0044732	mitotic spindle pole body [exists_during] mitotic interphase	cdc13HPM mutant fails to localise to the SPB during G2
PMID:32101481	FYPO:0007393	septum mislocalized to cell tip [has_penetrance] 95-100 [has_severity] high	(Figure 1A and 1B)
PMID:32101481	FYPO:0007393	septum mislocalized to cell tip	(Figure 2, C)
PMID:32101481	FYPO:0007393	septum mislocalized to cell tip [has_penetrance] 45-50	(Figure 2D)
PMID:32101481	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC20G8.05c [assayed_using] PomBase:SPBC83.18c	(Figure 6, A and B)
PMID:32101481	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC20G8.05c [assayed_using] PomBase:SPBC4F6.12	(Figure 6, A and B)
PMID:32101481	FYPO:0007393	septum mislocalized to cell tip [has_penetrance] 50	(Figure 6D) Indeed, deleting components of the CR scaffolded by Cdc15 (e.g., pxl1 or fic1) suppressed tip septation in mid1Δ pom1as1cells to a similar degree as cdc15-22D (Figure 6, D and E).
PMID:32101481	FYPO:0007393	septum mislocalized to cell tip [has_penetrance] 45-50	(Figure 6E)
PMID:32101481	FYPO:0007405	abnormal protein localization to medial cortex, with protein distributed in cell cortex, during vegetative growth [assayed_using] PomBase:SPAC20G8.05c	(comment: CHECK 4B?)
PMID:32101481	FYPO:0007393	septum mislocalized to cell tip [has_penetrance] 50	Indeed, the percentage of tip septa was significantly reduced in mid1Δ pom1as1 cdc15-22D cells (Figure 4G).
PMID:32101481	FYPO:0006897	increased rate of actomyosin contractile ring contraction [has_severity] medium	Though the length of CR formation (node appearance to complete ring) was similar in wild type, cdc15-22A, and cdc15-22D, the periods of maturation (interval between CR formation and constriction initiation) and constriction (start to end of CR diameter decrease) were shorter in cdc15-22A and longer in cdc15-22D (Figure 4F).
PMID:32101481	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC20G8.05c [part_of] negative regulation of mitotic actomyosin contractile ring assembly	the slow-migrating, phosphorylated forms of Cdc15 were reduced in pom1Δ cells (Figure 3B), and recombinant Pom1 efficiently phosphorylated recombinant N-terminal (Cdc15N; amino acids [aa]1-460) ||||||. later....We conclude that Cdc15 is a key substrate in the Pom1-mediated tip occlusion pathway.
PMID:32101745	FYPO:0005420	increased level of iron assimilation gene mRNA during vegetative growth	(Fig. 4e) The 73 genes with increased expression in the iss1-DC mutant were evaluated for common functions and were strongly enriched for factors important for iron assimilation GO:0033212.
PMID:32101745	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC32H8.11	(Fig. 4g,S4, Figure 5A)
PMID:32101745	FYPO:0002173	increased level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	(Fig. 4g,S4, Figure 5A)
PMID:32101745	FYPO:0001357	normal vegetative cell population growth	(Figure 3A)
PMID:32101745	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Figure 3A,B)
PMID:32101745	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Figure 3E)
PMID:32101745	FYPO:0004170	abolished histone H3-K9 dimethylation at centromere during vegetative growth	(Figure 3F)
PMID:32101745	FYPO:0003049	increased transcriptional readthrough [has_severity] low	(Figure 4C,S3) Although the percentage of total reads was relatively small, the iss1-DC mutation caused a reproducible and statistically significant extension of the 30 end of transcripts by about 200 nt.
PMID:32101745	FYPO:0007213	decreased histone H3-K9 dimethylation at heterochromatin island during vegetative growth [assayed_using] PomBase:SPBC32H8.11	(Figure 5B) the iss1-DC mutation significantly reduced H3K9me2 at both ssm4 and mei4).
PMID:32101745	FYPO:0007213	decreased histone H3-K9 dimethylation at heterochromatin island during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	(Figure 5B) the iss1-DC mutation significantly reduced H3K9me2 at both ssm4 and mei4).
PMID:32101745	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC22G7.10 [assayed_using] PomBase:SPCC736.12c	(Figure 5F) the iss1-DC truncation did disrupt its interaction with Mmi1.
PMID:32101745	GO:1990251	nuclear exosome focus	(Figure 5H) We found that Iss1 assembles into nuclear dots, and these co-localized with Pla1, indicating that Iss1 also assembles in vivo with RNA elimination factors
PMID:32101745	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC22G7.10 [assayed_using] PomBase:SPAC1F3.01	(Figure S5) However, the truncation did not reduce Iss1 interaction with Rrp6
PMID:32168916	FYPO:0004085	decreased vegetative cell growth	(Fig. 3)
PMID:32168916	FYPO:0004085	decreased vegetative cell growth	(Fig. 3)
PMID:32168916	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPAC664.06	(Figure 3,S4) (comment: ALSO TFIIH but not sure which sunbunit)
PMID:32168916	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC26H8.07c	(Figure 3,S4) (comment: ALSO TFIIH but not sure which sunbunit)
PMID:32168916	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPAC664.06	(Figure 4) (comment: ALSO TFIIH but not sure which sunbunit)
PMID:32168916	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC26H8.07c	(Figure 4) (comment: ALSO TFIIH but not sure which sunbunit)
PMID:32168916	FYPO:0003619	normal mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC26H8.07c	(Figure 4) (comment: CHECK SAP155K700E restored splicing to prp10-1)
PMID:32168916	FYPO:0002060	viable vegetative cell population	(Figure S4)
PMID:32168916	FYPO:0002060	viable vegetative cell population	(Figure S4)
PMID:32168916	FYPO:0002060	viable vegetative cell population	(Figure S4)
PMID:32168916	FYPO:0002060	viable vegetative cell population	(Figure S4)
PMID:32204793	FYPO:0000265	sensitive to DNA damage [has_severity] high	(Figure 1; Figure supplement 1A)
PMID:32204793	FYPO:0000265	sensitive to DNA damage [has_severity] high	(Figure 1; Figure supplement 1A)
PMID:32204793	FYPO:0000265	sensitive to DNA damage [has_severity] high	(Figure 1; Figure supplement 1A; Figure 7C,D; Figure 7—Figure supplement 1A)
PMID:32204793	FYPO:0000265	sensitive to DNA damage	(Figure 1D; Figure 1—Figure supplement 1)
PMID:32204793	FYPO:0000265	sensitive to DNA damage	(Figure 1D; Figure 1—Figure supplement 1)
PMID:32204793	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC644.14c [assayed_using] PomBase:SPBC28F2.07	(Figure 5B) Figure 5—Figure supplement 1C
PMID:32204793	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC644.14c [assayed_using] PomBase:SPBC28F2.07	(Figure 5B; Figure 5—Figure supplement 1C)
PMID:32204793	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC644.14c [assayed_using] PomBase:SPBC28F2.07	(Figure 5B; Figure 5—Figure supplement 1C)
PMID:32204793	FYPO:0000658	decreased DNA binding [assayed_using] PomBase:SPBC28F2.07	(Figure 5B; Figure 5—Figure supplement 1C)
PMID:32204793	FYPO:0000658	decreased DNA binding [assayed_using] PomBase:SPBC28F2.07	(Figure 6—Figure supplement 1)
PMID:32204793	FYPO:0000659	abolished DNA binding [assayed_using] PomBase:SPBC28F2.07	(Figure 6—Figure supplement 1)
PMID:32204793	FYPO:0000265	sensitive to DNA damage [has_severity] medium	(Figure 7; Figure supplement 1B)
PMID:32204793	FYPO:0000265	sensitive to DNA damage [has_severity] high	(Figure 7; Figure supplement 1B)
PMID:32204793	FYPO:0000265	sensitive to DNA damage [has_severity] medium	(Figure 7; Figure supplement 1B)
PMID:32204793	FYPO:0007346	normal growth during cellular response to DNA damage	(Figure 7A,B)
PMID:32204793	FYPO:0007346	normal growth during cellular response to DNA damage	(Figure 7A,B)
PMID:32204793	FYPO:0007346	normal growth during cellular response to DNA damage	(Figure 7A,B)
PMID:32204793	FYPO:0000265	sensitive to DNA damage [has_severity] high	(Figure 7C,D)
PMID:32204793	FYPO:0000265	sensitive to DNA damage [has_severity] medium	(Figure 7C,D)
PMID:32204793	FYPO:0000265	sensitive to DNA damage [has_severity] medium	(Figure 7C,D)
PMID:32204793	GO:0001671	ATPase activator activity [has_input] PomBase:SPAC644.14c	(comment: in complex with Sfr1) Figure 6
PMID:32204793	GO:0001671	ATPase activator activity [has_input] PomBase:SPAC644.14c	(comment: in complex with Swi5) Figure 6
PMID:32204793	GO:0042148	DNA strand invasion [part_of] double-strand break repair via homologous recombination	inferred from combination of in vitro assay and phenotypes; Figures 1 & 5, including supplements
PMID:32204793	GO:0042148	DNA strand invasion [part_of] double-strand break repair via homologous recombination	inferred from combination of in vitro assay and phenotypes; Figures 1 & 5, including supplements
PMID:32269268	FYPO:0001489	inviable vegetative cell [has_penetrance] 13	(Fig. 1)
PMID:32269268	FYPO:0001489	inviable vegetative cell [has_penetrance] 23	(Fig. 1)
PMID:32269268	FYPO:0001489	inviable vegetative cell [has_penetrance] 9	(Fig. 1)
PMID:32269268	FYPO:0001489	inviable vegetative cell [has_penetrance] 34	(Fig. 1)
PMID:32269268	FYPO:0001489	inviable vegetative cell [has_penetrance] 6	(Fig. 1)
PMID:32269268	FYPO:0001489	inviable vegetative cell [has_penetrance] 3	(Fig. 1)
PMID:32269268	FYPO:0001489	inviable vegetative cell [has_penetrance] 26	(Fig. 1)
PMID:32269268	FYPO:0001489	inviable vegetative cell [has_penetrance] 3	(Fig. 1)
PMID:32269268	FYPO:0001489	inviable vegetative cell [has_penetrance] 2	(Fig. 1)
PMID:32269268	FYPO:0004137	decreased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth	(Fig. 2)
PMID:32269268	FYPO:0004573	increased telomeric transcript level	(Fig. 2, S1)
PMID:32269268	FYPO:0000220	increased centromeric outer repeat transcript level	(Fig. 4)
PMID:32269268	FYPO:0004573	increased telomeric transcript level	(Fig. 4)
PMID:32269268	FYPO:0007226	normal chromatin silencing at heterochromatin island	(Fig. 5)
PMID:32269268	FYPO:0007653	decreased histone H3-K9 trimethylation at heterochromatin island at meiotic gene during vegetative growth	(Fig. 5)
PMID:32269268	FYPO:0007531	decreased histone H3-K9 dimethylation at heterochromatin island at meiotic gene during vegetative growth	(Fig. 5)
PMID:32269268	FYPO:0007654	decreased protein localization to heterochromatin island at meiotic gene during vegetative growth	(Fig. 5)
PMID:32269268	FYPO:0000220	increased centromeric outer repeat transcript level	(Fig. S2)
PMID:32269268	FYPO:0001489	inviable vegetative cell [has_penetrance] 10	"(comment: 25 degrees C; using ""low temperature"" to distinguish from 30 degrees C;) Fig 1"
PMID:32269268	FYPO:0001489	inviable vegetative cell [has_penetrance] 7	"(comment: 25 degrees C; using ""low temperature"" to distinguish from 30 degrees C;) Fig 1"
PMID:32269268	FYPO:0001489	inviable vegetative cell [has_penetrance] 7	"(comment: 25 degrees C; using ""low temperature"" to distinguish from 30 degrees C;) Fig 1"
PMID:32269268	FYPO:0001489	inviable vegetative cell [has_penetrance] 13	"(comment: 25 degrees C; using ""low temperature"" to distinguish from 30 degrees C;) Fig 1"
PMID:32269268	GO:0140720	subtelomeric heterochromatin	(comment: [vw added to cover missing EXP annotation based on localization phenotype below])
PMID:32277274	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPAC1687.18c [part_of] mitotic sister chromatid cohesion	(Fig. 2)
PMID:32277274	FYPO:0000460	decreased mitotic centromeric sister chromatid cohesion	(Fig. a)
PMID:32277274	FYPO:0007209	decreased sister chromatid cohesion along chromosome arms during mitotic interphase	(Fig. b)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 1)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 1)
PMID:32282918	FYPO:0000080	decreased cell population growth at low temperature	(Figure 1)
PMID:32282918	FYPO:0000082	decreased cell population growth at high temperature	(Figure 1)
PMID:32282918	FYPO:0000082	decreased cell population growth at high temperature	(Figure 1)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure 1)
PMID:32282918	FYPO:0000082	decreased cell population growth at high temperature	(Figure 1)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure 1)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure 1)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure 1)
PMID:32282918	FYPO:0002085	normal vegetative cell growth	(Figure 1)
PMID:32282918	FYPO:0000080	decreased cell population growth at low temperature	(Figure 1)
PMID:32282918	FYPO:0000080	decreased cell population growth at low temperature	(Figure 1)
PMID:32282918	FYPO:0002085	normal vegetative cell growth	(Figure 1)
PMID:32282918	FYPO:0000082	decreased cell population growth at high temperature	(Figure 1)
PMID:32282918	FYPO:0000082	decreased cell population growth at high temperature	(Figure 1)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 1)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC29B5.02c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP23A10.15c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC27D7.14c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC513.03	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC2G2.15c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC1565.04c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC18G6.12c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC1399.02	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC622.12c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC29A3.18	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC530.10c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC32C12.02	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC1223.03c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC70.02c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC56F8.15	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPACUNK4.17	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1861.02	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC23E6.03c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC70.08c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC83.13	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC1782.07	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1685.17	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1703.13c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC3A11.07	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC31G5.09c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC15E1.02c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1709.13c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC713.05	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC2H10.01	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC977.16c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC11C11.06c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.12c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC11E3.06	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC186.01	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC725.10	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC794.04c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1709.14	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC645.02	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC27D7.03c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC1B3.04c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAPJ695.02	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP23A10.15c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC27D7.14c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC513.03	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC688.06c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC2G2.15c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC1565.04c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC12D12.02c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC19C7.04c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC18G6.12c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC1399.02	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC622.12c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC29A3.18	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC428.07	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC530.10c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC794.01c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC32C12.02	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC1223.03c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC70.02c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC56F8.15	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPACUNK4.17	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1861.02	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC23E6.03c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC70.08c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC83.13	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC1782.07	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC11H11.04	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1685.17	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1703.13c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC3A11.07	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC16A3.13	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC343.12	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC31G5.09c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC336.05c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC15E1.02c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1709.13c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC713.05	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC2H10.01	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBPB2B2.01	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC977.16c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBPB8B6.04c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC11C11.06c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.12c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC11E3.06	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC354.12	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC186.01	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC725.10	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC794.04c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1709.14	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC645.02	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC27D7.03c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC1B3.04c	(Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAPJ695.02	(Figure 10)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1F7.08	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC794.03	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC1020.09	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1F7.08	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC18B5.01c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC25B8.12c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC106.02c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC11D3.01c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC9E9.09c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1039.02	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC23H3.15c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC4F6.09	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC750.01	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC186.05c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC569.09	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC13G7.13c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC947.04	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1683.09c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC27D7.09c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC1020.09	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC18B5.01c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC25B8.12c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC106.02c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC11D3.01c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC9E9.09c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1039.02	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC23H3.15c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC4F6.09	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC750.01	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC186.05c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1F7.07c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC13A11.06	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC27D7.11c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC13D6.01	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC794.03	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC569.09	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC13G7.13c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC947.04	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1683.09c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC27D7.09c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1F7.07c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC13A11.06	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC27D7.11c	(Figure 11)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC13D6.01	(Figure 11)
PMID:32282918	FYPO:0000080	decreased cell population growth at low temperature	(Figure 2)
PMID:32282918	FYPO:0000080	decreased cell population growth at low temperature	(Figure 2)
PMID:32282918	FYPO:0001355	decreased vegetative cell population growth	(Figure 2)
PMID:32282918	FYPO:0000080	decreased cell population growth at low temperature	(Figure 2)
PMID:32282918	FYPO:0000080	decreased cell population growth at low temperature	(Figure 2)
PMID:32282918	FYPO:0000080	decreased cell population growth at low temperature	(Figure 2)
PMID:32282918	FYPO:0001355	decreased vegetative cell population growth	(Figure 2)
PMID:32282918	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 3A)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 3A)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 3A, 9C)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1271.09	(Figure 3B)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1271.09	(Figure 3B)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Figure 3B)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1271.09	(Figure 3B)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Figure 3B)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Figure 3B)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Figure 3B, Figure 10)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Figure 3B, Figure 10)
PMID:32282918	FYPO:0000082	decreased cell population growth at high temperature	(Figure 5A)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure 5A)
PMID:32282918	FYPO:0000080	decreased cell population growth at low temperature	(Figure 5A)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure 5A)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure 5A)
PMID:32282918	FYPO:0000082	decreased cell population growth at high temperature	(Figure 5A)
PMID:32282918	FYPO:0000082	decreased cell population growth at high temperature	(Figure 5A)
PMID:32282918	FYPO:0000082	decreased cell population growth at high temperature	(Figure 5A)
PMID:32282918	FYPO:0000082	decreased cell population growth at high temperature	(Figure 5A)
PMID:32282918	FYPO:0000082	decreased cell population growth at high temperature	(Figure 5A)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure 5A)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 5B)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 5B)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 5B)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 5B)
PMID:32282918	FYPO:0001355	decreased vegetative cell population growth	(Figure 5B)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 5C)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 6A)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 6A)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 6A)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 6A)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 6A)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 6B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 6B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 6B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 6B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 6B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 6B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 6B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 6B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 6B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 6B)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure 7A)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 7A)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 7A)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 7A)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure 7A)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure 7A)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure 7A)
PMID:32282918	FYPO:0000080	decreased cell population growth at low temperature	(Figure 7A) pin∆ rescues the lethality of aps1∆ asp1-H397A
PMID:32282918	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 7B)
PMID:32282918	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 7B)
PMID:32282918	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 7B, 8B)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 8A)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 8A)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 8A)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 8A)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 8A)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 8B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 8B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 8B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 8B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 8B)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 8B)
PMID:32282918	FYPO:0001355	decreased vegetative cell population growth	(Figure 9B)
PMID:32282918	FYPO:0000082	decreased cell population growth at high temperature	(Figure 9B)
PMID:32282918	FYPO:0000080	decreased cell population growth at low temperature	(Figure 9B)
PMID:32282918	FYPO:0000080	decreased cell population growth at low temperature	(Figure 9B)
PMID:32282918	FYPO:0001355	decreased vegetative cell population growth	(Figure 9B)
PMID:32282918	FYPO:0001355	decreased vegetative cell population growth	(Figure 9B)
PMID:32282918	FYPO:0001355	decreased vegetative cell population growth	(Figure 9B)
PMID:32282918	FYPO:0001355	decreased vegetative cell population growth	(Figure 9B)
PMID:32282918	FYPO:0001355	decreased vegetative cell population growth	(Figure 9B)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 9B)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure 9B)
PMID:32282918	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 9C)
PMID:32282918	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 9C)
PMID:32282918	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 9C)
PMID:32282918	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 9C)
PMID:32282918	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC23C4.19	(Figure S1)
PMID:32282918	FYPO:0007535	normal phosphorylation of RNA polymerase II C-terminal domain serine 2 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure S1)
PMID:32282918	FYPO:0007539	normal phosphorylation of RNA polymerase II C-terminal domain threonine 4 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure S1)
PMID:32282918	FYPO:0005061	normal phosphorylation of RNA polymerase II C-terminal domain serine 5 residues during vegetative growth [assayed_protein] PomBase:SPBC28F2.12	(Figure S1)
PMID:32282918	FYPO:0008034	normal phosphorylation of RNA polymerase II C-terminal domain serine 7 residues during vegetative growth	(Figure S1)
PMID:32282918	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC16C4.03	(Figure S2)
PMID:32282918	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC16C4.03	(Figure S2)
PMID:32282918	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC23C4.19	(Figure S2)
PMID:32282918	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC23C4.19	(Figure S2)
PMID:32282918	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC23C4.19	(Figure S2)
PMID:32282918	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC23C4.19	(Figure S2)
PMID:32282918	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC23C4.19	(Figure S2)
PMID:32282918	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC16C4.03	(Figure S2)
PMID:32282918	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC16C4.03	(Figure S2)
PMID:32282918	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC16C4.03	(Figure S2)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure S3)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure S3)
PMID:32282918	FYPO:0001357	normal vegetative cell population growth	(Figure S3)
PMID:32282918	FYPO:0001355	decreased vegetative cell population growth	(Figure S3)
PMID:32282918	FYPO:0001355	decreased vegetative cell population growth	(Figure S3)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure S3)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure S3)
PMID:32282918	FYPO:0001355	decreased vegetative cell population growth	(Figure S3)
PMID:32282918	FYPO:0001355	decreased vegetative cell population growth	(Figure S3)
PMID:32282918	FYPO:0002059	inviable cell population	(Figure S3)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC569.09	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC27D7.03c	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC725.10	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC794.03	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1F7.07c	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC13D6.01	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC25B8.12c	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC18B5.01c	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1F7.08	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC1020.09	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC27D7.09c	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1683.09c	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAPJ695.02	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC11E3.06	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.12c	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBPB8B6.04c	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC977.16c	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC2H10.01	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC29B5.02c	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC713.05	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC31G5.09c	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC3A11.07	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC11H11.04	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1861.02	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC56F8.15	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC32C12.02	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC530.10c	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC18G6.12c	(Figure S7)
PMID:32282918	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC513.03	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC750.01	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC4F6.09	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC23H3.15c	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC11D3.01c	(Figure S7)
PMID:32282918	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC106.02c	(Figure S7)
PMID:32295063	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [assayed_using] PomBase:SPCC1322.13 [has_severity] variable severity [has_penetrance] high	( comment: KΔ::ade6+ monitored by qRT-PCR)
PMID:32295063	GO:0031509	subtelomeric heterochromatin formation	(Fig. 4C)
PMID:32295063	GO:0031509	subtelomeric heterochromatin formation	(Fig. 4C)
PMID:32295063	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(comment: CHECK compared to Lsd1-ao single mutant)
PMID:32295063	FYPO:0007339	increased cen-dg RNA level	(comment: CHECK compared to lsd1-ao single mutant)
PMID:32295063	FYPO:0002336	normal chromatin silencing at silent mating-type cassette [has_penetrance] medium	(comment: KΔ::ade6+ monitored by qRT-PCR)
PMID:32295063	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high [has_penetrance] high	(comment: KΔ::ade6+ monitored by qRT-PCR)
PMID:32295063	GO:0031508	pericentric heterochromatin formation	At all constitutive heterochromatic domains, lsd C-terminal mutants showed strong cumulative genetic interactions with clr3∆ and sir2∆, indicating that they play overlapping functions in epigenetic silencing. In particular, lsd2-∆C sir2∆ double mutants show the strongest silencing defects at centromeric regions and sub-telomeric regions, while lsd1-∆HMG clr3∆ double mutants have the most robust effect at the mating-type locus (Figure 7D).
PMID:32295063	GO:0030466	silent mating-type cassette heterochromatin formation	At all constitutive heterochromatic domains, lsd C-terminal mutants showed strong cumulative genetic interactions with clr3∆ and sir2∆, indicating that they play overlapping functions in epigenetic silencing. In particular, lsd2-∆C sir2∆ double mutants show the strongest silencing defects at centromeric regions and sub-telomeric regions, while lsd1-∆HMG clr3∆ double mutants have the most robust effect at the mating-type locus (Figure 7D).
PMID:32295063	GO:0031509	subtelomeric heterochromatin formation	At all constitutive heterochromatic domains, lsd C-terminal mutants showed strong cumulative genetic interactions with clr3∆ and sir2∆, indicating that they play overlapping functions in epigenetic silencing. In particular, lsd2-∆C sir2∆ double mutants show the strongest silencing defects at centromeric regions and sub-telomeric regions, while lsd1-∆HMG clr3∆ double mutants have the most robust effect at the mating-type locus (Figure 7D).
PMID:32319721	FYPO:0001309	increased viability in stationary phase [has_severity] medium	(comment: CFU counts)
PMID:32320462	FYPO:0007439	abnormal eisosome morphology	(comment: Eisosomes protruding towards cell interior)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007677	abnormal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007677	abnormal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007677	abnormal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007676	normal intracellular sterol transport	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007676	normal intracellular sterol transport	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0004963	normal plasma membrane sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007676	normal intracellular sterol transport	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007676	normal intracellular sterol transport	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007678	normal sterol distribution	(comment: Evaluated with D4H sterol sensor)
PMID:32320462	FYPO:0007677	abnormal sterol distribution	(comment: Evaluated with D4H sterol sensor; internal structures)
PMID:32320462	FYPO:0007440	abnormal intracellular sterol transport	(comment: Sterols do not accumulate in endosomes after treatement with CK-666)
PMID:32320462	FYPO:0007440	abnormal intracellular sterol transport	(comment: Sterols do not accumulate in endosomes after treatement with CK-666)
PMID:32320462	FYPO:0007440	abnormal intracellular sterol transport	(comment: Sterols do not accumulate in endosomes)
PMID:32320462	FYPO:0007440	abnormal intracellular sterol transport	Sterols accumulate in endosomes
PMID:32327557	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 60	(Fig. 2)
PMID:32327557	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] 22	(Fig. 2)
PMID:32327557	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 80	(Fig. 2)
PMID:32327557	FYPO:0006363	monopolar spindle during meiosis I [has_penetrance] 74	(Fig. 2)
PMID:32327557	FYPO:0007987	decreased rate of spindle elongation during meiotic anaphase B	(Fig. 2)
PMID:32327557	FYPO:0006315	abolished homologous chromosome segregation [has_penetrance] 45	(Fig. 2)
PMID:32327557	GO:0090619	meiotic spindle pole [exists_during] meiosis I cell cycle phase	(Fig. 3)
PMID:32327557	GO:0090619	meiotic spindle pole [exists_during] meiosis I cell cycle phase	(Fig. 3)
PMID:32327557	GO:0005827	polar microtubule [exists_during] meiosis I cell cycle phase	(Fig. 3)
PMID:32327557	GO:0097431	mitotic spindle pole [exists_during] mitotic M phase	(Fig. 3)
PMID:32327557	GO:1990537	mitotic spindle polar microtubule [exists_during] mitotic M phase	(Fig. 3)
PMID:32327557	GO:0005827	polar microtubule [exists_during] meiosis I cell cycle phase	(Fig. 3)
PMID:32327557	GO:0090619	meiotic spindle pole [exists_during] meiosis I cell cycle phase	(Fig. 3)
PMID:32327557	FYPO:0007988	long spindle microtubules protruding beyond spindle pole body during meiosis I [has_penetrance] complete	(Fig. 3)
PMID:32327557	FYPO:0003787	long mitotic spindle microtubules protruding beyond spindle pole body [has_penetrance] 13	(Fig. 3)
PMID:32327557	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 9	(Fig. 3)
PMID:32327557	FYPO:0007103	spindle collapse during meiosis I [has_penetrance] 11	(Fig. 3)
PMID:32327557	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 98	(Fig. 4)
PMID:32327557	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 55	(Fig. 4)
PMID:32327557	FYPO:0001894	abnormal sporulation resulting in formation of ascus with more or fewer than four spores [has_penetrance] 90	(Fig. 4)
PMID:32327557	FYPO:0006363	monopolar spindle during meiosis I [has_penetrance] 20	(comment: CONDITION 5ug/mL)
PMID:32327557	GO:0090306	meiotic spindle assembly [happens_during] meiosis I cell cycle phase	(comment: Small rescue of cut7D pkl1D)
PMID:32341083	FYPO:0001270	complete but unequal mitotic sister chromatid segregation [has_penetrance] 13	(comment: HU absent)
PMID:32341083	FYPO:0003165	cut [has_penetrance] 8	(comment: HU absent)
PMID:32341083	FYPO:0001513	normal mitotic sister chromatid segregation	(comment: HU absent)
PMID:32341083	FYPO:0003165	cut [has_penetrance] 4	(comment: HU absent)
PMID:32355220	FYPO:0006810	decreased gross chromosomal rearrangement	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007423	decreased isochromosome formation	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007423	decreased isochromosome formation	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007423	decreased isochromosome formation	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0001742	increased isochromosome formation	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0001742	increased isochromosome formation	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006810	decreased gross chromosomal rearrangement	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006810	decreased gross chromosomal rearrangement	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007423	decreased isochromosome formation	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0001742	increased isochromosome formation	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0001859	increased minichromosome loss	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007423	decreased isochromosome formation	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007424	increased chromosomal truncation	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007424	increased chromosomal truncation	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0007423	decreased isochromosome formation	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006810	decreased gross chromosomal rearrangement	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006810	decreased gross chromosomal rearrangement	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0006811	normal gross chromosomal rearrangement frequency	(comment: An extrachromosome ChLC)
PMID:32355220	FYPO:0000185	decreased gene conversion during vegetative growth [has_penetrance] high	(comment: CHECK BACKGROUND ade6B/ade6X at the ura4 locus)
PMID:32355220	FYPO:0000185	decreased gene conversion during vegetative growth [has_penetrance] high [assayed_using] regional_centromere	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0000185	decreased gene conversion during vegetative growth [has_penetrance] high [assayed_using] regional_centromere	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0005788	increased gene conversion during vegetative growth [assayed_using] regional_centromere	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0007425	normal gene conversion [assayed_using] regional_centromere	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0007425	normal gene conversion [assayed_using] regional_centromere	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0005788	increased gene conversion during vegetative growth [assayed_using] regional_centromere	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0005788	increased gene conversion during vegetative growth [assayed_using] regional_centromere	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0005788	increased gene conversion during vegetative growth [assayed_using] regional_centromere	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0007425	normal gene conversion [assayed_using] regional_centromere	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0000185	decreased gene conversion during vegetative growth [has_penetrance] high [assayed_using] regional_centromere	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0005788	increased gene conversion during vegetative growth [assayed_using] regional_centromere	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0005788	increased gene conversion during vegetative growth	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0007425	normal gene conversion [assayed_using] regional_centromere	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0000185	decreased gene conversion during vegetative growth [assayed_using] regional_centromere	(comment: ade6B/ade6X at cen1)
PMID:32355220	FYPO:0007425	normal gene conversion	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	FYPO:0000185	decreased gene conversion during vegetative growth [has_penetrance] medium	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	FYPO:0007425	normal gene conversion	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	FYPO:0007425	normal gene conversion	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	FYPO:0000185	decreased gene conversion during vegetative growth	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	FYPO:0000185	decreased gene conversion during vegetative growth [has_penetrance] medium	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	FYPO:0000185	decreased gene conversion during vegetative growth	(comment: ade6B/ade6X at the ura4 locus)
PMID:32355220	FYPO:0007425	normal gene conversion [assayed_using] regional_centromere	a(comment: de6B/ade6X at cen1)
PMID:32361273	FYPO:0000708	decreased mating efficiency [has_severity] medium	(Fig. 1)
PMID:32361273	FYPO:0001043	increased mating efficiency [has_severity] low	(Fig. 1)
PMID:32361273	FYPO:0001043	increased mating efficiency	(Fig. 1)
PMID:32361273	FYPO:0000708	decreased mating efficiency	(Fig. 1)
PMID:32361273	FYPO:0005035	normal protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPCC24B10.07	(Fig. 1C) (comment: i.e normal TOR signalloing)
PMID:32361273	FYPO:0003345	abolished cell cycle arrest in mitotic G1 phase in response to nitrogen starvation	(Fig. 1D) The cells also presented a defect in the degradation of the cyclin Cdc13 and a delay in the dephosphorylation of Ste9
PMID:32361273	FYPO:0002798	decreased protein degradation during nitrogen starvation [assayed_using] PomBase:SPBC582.03 [has_severity] high	(Fig. 2)
PMID:32361273	FYPO:0002277	increased protein degradation during nitrogen starvation [assayed_using] PomBase:SPBC32F12.09	(Fig. 2)
PMID:32361273	FYPO:0004084	normal protein level during nitrogen starvation [assayed_using] PomBase:SPAPB2B4.03	(Fig. 2)
PMID:32361273	FYPO:0002681	increased protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPBC11B10.09	(Fig. 2) This conserved inhibitory phosphorylation occurs as the Cdc2-Cdc13 complex is being formed to prevent its premature activation during G2 phase
PMID:32361273	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] low	(Fig. 2D) length is 10.299 micron cf WT 12.7 in same conditions
PMID:32361273	FYPO:0000998	elongated cell during nitrogen starvation [has_severity] low	(Fig. 2D) length is 7.5 micron cf WT 6.2 in same conditions
PMID:32361273	FYPO:0002798	decreased protein degradation during nitrogen starvation [assayed_using] PomBase:SPBC582.03 [has_severity] medium	(Fig. 2E, S2A)
PMID:32361273	FYPO:0002798	decreased protein degradation during nitrogen starvation [assayed_using] PomBase:SPBC582.03 [has_severity] medium	(Fig. 2F)
PMID:32361273	FYPO:0002277	increased protein degradation during nitrogen starvation [assayed_using] PomBase:SPBC582.03 [has_severity] medium	(Fig. 2F)
PMID:32361273	FYPO:0007476	decreased duration of cell cycle arrest in mitotic G1 phase	(Fig. 2G) the use of cdc10 mutant backgrounds is common for checking the ability of cells to arrest in G1
PMID:32361273	FYPO:0001000	normal cell cycle arrest in mitotic G1 phase during nitrogen starvation	(Fig. 3)
PMID:32361273	FYPO:0002277	increased protein degradation during nitrogen starvation [assayed_using] PomBase:SPBC582.03 [has_severity] high	(Fig. 3)
PMID:32361273	FYPO:0001043	increased mating efficiency	(Fig. 3)
PMID:32361273	FYPO:0001043	increased mating efficiency	(Fig. 3b)
PMID:32361273	FYPO:0002801	normal protein degradation during nitrogen starvation [assayed_using] PomBase:SPBC32F12.09	(Fig. 4) Notably, loss of cig1 and cig2 utterly overrode these defects
PMID:32361273	FYPO:0002801	normal protein degradation during nitrogen starvation [assayed_using] PomBase:SPBC582.03	(Fig. 7)
PMID:32361273	FYPO:0000708	decreased mating efficiency	(Fig. 7A)
PMID:32361273	FYPO:0005034	decreased protein phosphorylation during nitrogen starvation [assayed_using] PomBase:SPAC31G5.09c	(Fig. S1A)
PMID:32361273	FYPO:0001152	decreased RNA level during nitrogen starvation [assayed_using] PomBase:SPAC27D7.03c	(Fig. S1A)
PMID:32361273	FYPO:0002798	decreased protein degradation during nitrogen starvation [assayed_using] PomBase:SPBC582.03 [has_severity] medium	(Fig. S2B)
PMID:32361273	MOD:00696	phosphorylated residue [present_during] mitotic G2 phase	(Figure S4D)
PMID:32361273	MOD:00696	phosphorylated residue [present_during] mitotic S phase	(Figure S4D)
PMID:32361273	MOD:00696	phosphorylated residue [present_during] mitotic M phase	(Figure S4D)
PMID:32361273	MOD:00696	phosphorylated residue [removed_during] cellular response to nitrogen starvation	(Figure S4D)
PMID:32361273	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC188.02 [assayed_using] PomBase:SPBC32F12.09	(TAP-Par1F314Q), this interaction was reduced (Figure 6C)
PMID:32361273	FYPO:0004233	decreased and delayed cell cycle arrest in mitotic G1 phase in response to nitrogen starvation	(comment: Delay in the dephosphoryaltion of Ste9 and defect in the degradation of the cyclin Cdc13 in nitrogen starvation)
PMID:32361273	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPBC32F12.09 [part_of] mitotic G1 cell size control checkpoint signaling	(comment: protein phophatase substrate adaptor)
PMID:32361273	FYPO:0001387	loss of viability at high temperature	Deletion of par1 also affected the survival of the wee1-50 mutant (Figure 4C), and this worsening of the phenotype correlated with the inability of the double wee1-50 par1D mutant to accumulate Rum1 (Figure 4D).
PMID:32361273	FYPO:0001283	decreased protein level during cellular response to nitrogen starvation [assayed_using] PomBase:SPBC32F12.09	Deletion of par1 also affected the survival of the wee1-50 mutant (Figure 4C), and this worsening of the phenotype correlated with the inability of the double wee1-50 par1D mutant to accumulate Rum1 (Figure 4D).
PMID:32361273	FYPO:0002798	decreased protein degradation during nitrogen starvation [assayed_using] PomBase:SPBC582.03 [has_severity] high	deletion mutants of either ste9 or rum1 fail to degrade Cdc13 (Figures S4A and S4B).
PMID:32361273	FYPO:0002798	decreased protein degradation during nitrogen starvation [assayed_using] PomBase:SPBC582.03 [has_severity] high	deletion mutants of either ste9 or rum1 fail to degrade Cdc13 (Figures S4A and S4B).
PMID:32414915	GO:0120230	recombinase activator activity [happens_during] meiotic prophase I [part_of] reciprocal meiotic recombination	The Meu13-Mcp7 complex activates the initiation step of DNA strand exchange by Dmc1. The Meu13-Mcp7 complex also stimulates Rad51-driven strand exchange to a much less extent in the presence of the Swi5-Sfr1 complex.
PMID:32414915	GO:0120230	recombinase activator activity [happens_during] meiotic prophase I [part_of] reciprocal meiotic recombination	The Meu13-Mcp7 complex activates the initiation step of DNA strand exchange by Dmc1. The Meu13-Mcp7 complex also stimulates Rad51-driven strand exchange to a much less extent in the presence of the Swi5-Sfr1 complex.
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBP4G3.02	(Fig. 1b), similar to the effect observed upon deletion of the lncRNA (Supplementary Fig. 1b)6,7,11.
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBP4G3.02	(Fig. 1b), similar to the effect observed upon deletion of the lncRNA (Supplementary Fig. 1b)6,7,11.
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBC1D7.05	(Fig. 1b), similar to the effect observed upon deletion of the lncRNA (Supplementary Fig. 1b)6,7,11.
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBC1D7.05	(Fig. 1b), similar to the effect observed upon deletion of the lncRNA (Supplementary Fig. 1b)6,7,11.
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBC1D7.05	A significant increase in the level of both pho1 and byr2 mRNAs in cwf10-1 as compared to WT confirmed that the splicing machinery indeed affects the expression of genes repressed by lncRNAs (Fig. 2c)
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBP4G3.02	A significant increase in the level of both pho1 and byr2 mRNAs in cwf10-1 as compared to WT confirmed that the splicing machinery indeed affects the expression of genes repressed by lncRNAs (Fig. 2c)
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBP4G3.02	Cells lacking Ago1 showed a considerable increase in pho1 transcript levels as determined by northern blot analysis (Fig. 4e), but the observed effect was weaker than in pir2-1 or cwf10-1, suggesting that additional factors likely cooperate with Pir2- splicing machinery.
PMID:32415063	GO:0000785	chromatin [coincident_with] sense_overlap_lncRNA_gene	Chromatin immunoprecipitation followed by sequencing (ChIP-seq) confirmed Pir2 enrichment at lncRNAs, including prt and nam1 (Fig. 1c and Supplementary Fig. 1c)
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBP4G3.02 [has_severity] high	However, the ago1Δ clr3Δ double mutant showed cumulative de-repression of pho1 (Fig. 5d).
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBP4G3.02 [has_severity] high	However, the ago1Δ clr3Δ double mutant showed cumulative de-repression of pho1 (Fig. 5d).
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBP4G3.02 [has_severity] high	However, the ago1Δ clr3Δ double mutant showed cumulative de-repression of pho1 (Fig. 5d).
PMID:32415063	FYPO:0002052	normal sporulation frequency	Importantly, cwf10-1 rescued the sporulation defect observed in rrp6Δ caused by the silencing of the byr2 gene by nam1 lncRNA (Fig. 2e), similar to pir2-1 (Fig. 1f).
PMID:32415063	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC725.08 [assayed_protein] PomBase:SPCC1739.03	Interestingly, this interaction was impaired in the cwf10- 1 mutant, indicating that splicing factors are required for association of Pir2 with Hrr1 (Fig. 4b)
PMID:32415063	FYPO:0008155	abnormal regulatory lncRNA 3'-end processing [assayed_transcript] PomBase:SPNCRNA.1459	Loss of the MTREC subunit Red1 resulted in the accumulation of longer readthrough transcripts (referred to as prt-L and nam1-L) (Fig. 1a), as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)6,7,11.
PMID:32415063	FYPO:0008155	abnormal regulatory lncRNA 3'-end processing [assayed_transcript] PomBase:SPNCRNA.1712	Loss of the MTREC subunit Red1 resulted in the accumulation of longer readthrough transcripts (referred to as prt-L and nam1-L) (Fig. 1a), as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)6,7,11.
PMID:32415063	GO:0106222	lncRNA binding	Moreover, RNA immunoprecipitation sequencing analysis (RIP-seq) showed that Pir2 binds to the lncRNAs (Fig. 1d and Supplementary Fig. 1d)
PMID:32415063	FYPO:0006631	decreased protein localization to chromatin [assayed_region] PomBase:SPNCRNA.1712 [assayed_protein] PomBase:SPBC800.03	Moreover, quantitative ChIP analyses showed enrichment of Clr3 and Pob3 at prt-pho1 in WT cells and a reduced localization in pir2-1 cells (Fig. 5e).
PMID:32415063	FYPO:0006631	decreased protein localization to chromatin [assayed_region] PomBase:SPNCRNA.1712 [assayed_protein] PomBase:SPBC1289.04c	Moreover, quantitative ChIP analyses showed enrichment of Clr3 and Pob3 at prt-pho1 in WT cells and a reduced localization in pir2-1 cells (Fig. 5e).
PMID:32415063	FYPO:0002052	normal sporulation frequency	Remarkably, entry into meiosis and sporulation efficiency were restored in pir2-1 rrp6Δ cells (Fig. 1f).
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBP4G3.02	Remarkably, strains carrying splice site mutations showed significant upregulation of the pho1 transcript (Fig. 3c), similar to the effect observed in pir2-1, cwf10- 1 and prtΔ (Figs. 1b, 2c and Supplementary Fig. 1b)
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBP4G3.02	Remarkably, strains carrying splice site mutations showed significant upregulation of the pho1 transcript (Fig. 3c), similar to the effect observed in pir2-1, cwf10- 1 and prtΔ (Figs. 1b, 2c and Supplementary Fig. 1b)
PMID:32415063	GO:0031047	regulatory ncRNA-mediated gene silencing	Supporting the function of Pir2 and lncRNA in the same pathway, we found no additive effect on pho1 expression in the pir2-1 prtΔ double mutant when compared to the effect in the single mutants (Fig. 1e).
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBP4G3.02	Surprisingly, pir2-1 showed a drastic upregulation of pho1 and byr2 genes as compared to wild-type (WT) (Fig. 1b)
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBC1D7.05	Surprisingly, pir2-1 showed a drastic upregulation of pho1 and byr2 genes as compared to wild-type (WT) (Fig. 1b)
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBP4G3.02	The lncRNA-mediated repression of pho1 was impaired in cbc1-1 cells (Supplementary Fig. 1e)
PMID:32415063	FYPO:0008155	abnormal regulatory lncRNA 3'-end processing [assayed_transcript] PomBase:SPNCRNA.1712	The lncRNA-mediated repression of pho1 was impaired in cbc1-1 cells (Supplementary Fig. 1e), sug-
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBP4G3.02	The loss of Clr3 or Pob3 caused an increase in pho1 transcript levels, consistent with their involvement in repression by lncRNA8,38, but the extent of upregulation was less than in pir2-1 (Fig. 5c).
PMID:32415063	FYPO:0006548	increased gene expression [assayed_using] PomBase:SPBP4G3.02	The loss of Clr3 or Pob3 caused an increase in pho1 transcript levels, consistent with their involvement in repression by lncRNA8,38, but the extent of upregulation was less than in pir2-1 (Fig. 5c).
PMID:32415063	GO:0031047	regulatory ncRNA-mediated gene silencing	The requirement for Pir2 in mediating the repressive effects of lncRNAs is a highly significant finding.
PMID:32415063	GO:0031047	regulatory ncRNA-mediated gene silencing	These results confirm the biological significance of Pir2 association with splicing machinery and show that these factors collaborate to promote gene repression by lncRNAs.
PMID:32415063	FYPO:0000121	abnormal sporulation [has_penetrance] 94	We asked if Pir2 is also required for the repression of byr2 that is observed upon the accumulation of nam1 lncRNA in cells lacking Rrp6. Since byr2 is required for meiotic induction, cells lacking Rrp6 are defective in sporulation (Fig. 1f)11.
PMID:32415063	FYPO:0006076	siRNA absent from cell [assayed_transcript] PomBase:SPNCRNA.1712	We next wondered whether cryptic introns are required for Pir2- dependent generation of siRNAs. Mutations of the pho1 cryptic intron splice sites in rrp6Δ cells abolished the production of siRNAs mapping to the entire prt lncRNA, including the region upstream of pho1 (Fig. 4d). This result suggests that the cryptic intron acts as part of the prt lncRNA to engage RNAi machinery. Importantly, siRNAs mapping to other loci were not affected (Fig. 4d and Supplementary Fig. 5)
PMID:32415063	FYPO:0006076	siRNA absent from cell	We then analyzed the role of Pir2 in siRNA production in cells lacking Rrp6, which show accumulation of lncRNAs and robust repression of their target loci. We found that siRNAs, which ranged in size from 20-24 nt and mapped to lncRNAs targeting pho1 and byr2, were abolished in both pir2-1 and cwf10-1 mutant backgrounds (Fig. 4c and Supplementary Fig. 4a, b).
PMID:32415063	FYPO:0006076	siRNA absent from cell	We then analyzed the role of Pir2 in siRNA production in cells lacking Rrp6, which show accumulation of lncRNAs and robust repression of their target loci. We found that siRNAs, which ranged in size from 20-24 nt and mapped to lncRNAs targeting pho1 and byr2, were abolished in both pir2-1 and cwf10-1 mutant backgrounds (Fig. 4c and Supplementary Fig. 4a, b). Pir2 was also required for siRNA production at Tf2 elements, pericentromeric repeats, and other loci (Fig. 4c, Supplementary Fig. 5 and Supplementary Data 2).
PMID:32415063	FYPO:0008155	abnormal regulatory lncRNA 3'-end processing [assayed_transcript] PomBase:SPNCRNA.1712	as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)
PMID:32415063	FYPO:0008155	abnormal regulatory lncRNA 3'-end processing [assayed_transcript] PomBase:SPNCRNA.1459	as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)
PMID:32415063	FYPO:0008155	abnormal regulatory lncRNA 3'-end processing [assayed_transcript] PomBase:SPNCRNA.1712	as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)
PMID:32415063	FYPO:0008155	abnormal regulatory lncRNA 3'-end processing [assayed_transcript] PomBase:SPNCRNA.1459	as was also observed in mmi1Δ and rrp6Δ cells (Fig. 1a and Supplementary Fig. 1a)
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 1, 2 and 4) Supplementary Fig S1, S3 and S5
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 1, 2 and 4) Supplementary Fig S1, S3 and S5
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 1, 2 and 4) Supplementary Fig S1, S3 and S5
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 2)
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 2)
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 2)
PMID:32496538	FYPO:0006996	normal antisense RNA level	(Figure 2)
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 2)
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 2)
PMID:32496538	FYPO:0006996	normal antisense RNA level	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0006996	normal antisense RNA level	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0002913	increased antisense RNA transcription	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0006996	normal antisense RNA level	(Figure 4 and Supplementary Fig S5)
PMID:32496538	FYPO:0006020	abnormal protein distribution along RNA polymerase II-transcribed genes [assayed_using] PomBase:SPBC28F2.12	(Figure 5)
PMID:32496538	FYPO:0006020	abnormal protein distribution along RNA polymerase II-transcribed genes [assayed_using] PomBase:SPAC23C11.15	(Figure 5)
PMID:32496538	FYPO:0006020	abnormal protein distribution along RNA polymerase II-transcribed genes [assayed_using] PomBase:SPAC23C11.15	(Figure 5) rbp1 also Figure 7
PMID:32496538	FYPO:0006020	abnormal protein distribution along RNA polymerase II-transcribed genes [assayed_using] PomBase:SPBC28F2.12	(Figure 5) rbp1 also Figure 7
PMID:32496538	FYPO:0006020	abnormal protein distribution along RNA polymerase II-transcribed genes [assayed_using] PomBase:SPAC23C11.15	(Figure 5) rbp1 also Figure 7
PMID:32496538	FYPO:0006020	abnormal protein distribution along RNA polymerase II-transcribed genes [assayed_using] PomBase:SPBC28F2.12	(Figure 5) rbp1 also Figure 7
PMID:32496538	FYPO:0004347	increased histone H3-K9 acetylation at protein coding gene during vegetative growth	(Figure 6 and Supplementary Fig S8)
PMID:32496538	FYPO:0005516	decreased nucleosome occupancy in euchromatin	(Figure 6 and Supplementary Fig S8)
PMID:32496538	FYPO:0005518	increased histone H3-K14 acetylation at protein coding gene during vegetative growth	(Figure 6 and Supplementary Fig S8)
PMID:32496538	FYPO:0007347	normal histone H3-K36 trimethylation during vegetative growth	(Supplementary Fig S7)
PMID:32496538	FYPO:0007347	normal histone H3-K36 trimethylation during vegetative growth	(Supplementary Fig S7)
PMID:32496538	FYPO:0001509	normal protein localization to chromatin during vegetative growth [assayed_using] PomBase:SPAC29B12.02c	(Supplementary Fig S7)
PMID:32496538	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_using] PomBase:SPAC29B12.02c	(Supplementary Fig S7)
PMID:32496538	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_using] PomBase:SPAC29B12.02c	(Supplementary Fig S7)
PMID:32496538	FYPO:0007347	normal histone H3-K36 trimethylation during vegetative growth	(Supplementary Fig S7)
PMID:32496538	FYPO:0005518	increased histone H3-K14 acetylation at protein coding gene during vegetative growth	(Supplementary Fig S8)
PMID:32496538	FYPO:0005518	increased histone H3-K14 acetylation at protein coding gene during vegetative growth	(Supplementary Fig S8)
PMID:32496538	FYPO:0005518	increased histone H3-K14 acetylation at protein coding gene during vegetative growth	(Supplementary Fig S8)
PMID:32499400	FYPO:0004066	increased protein localization to chromatin at protein coding gene [assayed_using] PomBase:SPBC27B12.11c	(comment: CHECK at tgp1 promoter)
PMID:32499400	FYPO:0003670	sensitive to mycophenolic acid [has_severity] low	(comment: CONDITION 100 ug/mL MPA)
PMID:32499400	FYPO:0000084	sensitive to 6-azauracil [has_severity] medium	(comment: CONDITION EMM -U agar plates, supplemented with 6AU concentration ranging from 3.6 to 150 ug/mL)
PMID:32499400	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_using] PomBase:SPNCRNA.1698	(comment: also assayed genome-wide)
PMID:32499400	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_using] PomBase:SPNCRNA.1698	(comment: also assayed genome-wide)
PMID:32499400	FYPO:0007411	abnormal distribution of RNA polymerase II C-terminal domain residue phosphorylation during vegetative growth	(comment: at different lncRNA polyadenylation sites)
PMID:32499400	FYPO:0007408	abnormal protein localization to chromatin at polyadenylation site [assayed_using] PomBase:SPAC222.09	(comment: at lncRNAs upstream of PHO regulon genes (nc-tgp1, nc-pho1, prt1))
PMID:32499400	FYPO:0007408	abnormal protein localization to chromatin at polyadenylation site [assayed_using] PomBase:SPAC6F12.17	(comment: at lncRNAs upstream of PHO regulon genes (nc-tgp1, nc-pho1, prt1))
PMID:32499408	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPAC25A8.01c [has_severity] high	(Fig. 5e)
PMID:32499408	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] low	(Figure 1B-E, S1B
PMID:32499408	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Figure 1B-E, S1B)
PMID:32499408	FYPO:0002834	decreased chromatin silencing at centromere [has_severity] high	(Figure 1B-E, S1B)
PMID:32499408	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Figure 1B-E, S1B)
PMID:32499408	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	(Figure 1B-E, S1B)
PMID:32499408	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Figure 1B-E, S1B)
PMID:32499408	FYPO:0003216	decreased chromatin silencing at rDNA [has_severity] low	(Figure 1B-E, S1B)
PMID:32499408	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Figure 2E)
PMID:32499408	FYPO:0005867	decreased histone H3-K9 dimethylation at rDNA during vegetative growth [has_severity] high	(Figure 3)
PMID:32499408	FYPO:0000877	decreased histone H3-K9 dimethylation at centromere during vegetative growth [has_severity] high	(Figure 3)
PMID:32499408	FYPO:0004083	normal protein level [assayed_using] PomBase:SPCC736.11	(Figure 4B)
PMID:32499408	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPAC19G12.13c [has_severity] high	(Figure 7A)
PMID:32499408	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPAC140.03	It is noteworthy that the amount of Arb1 was also drastically decreased in hsp90-G84C cells at high temperatures (Figure 4E)
PMID:32499408	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC736.11 [assayed_using] PomBase:SPBC83.03c	We then examined how the altered protein level of Tas3 affects the RITS complex formation in vivo. Notably, the low level of Tas3 in hsp90-G84C cells could only recruit minimal amount of Ago1 detected by co-immunoprecipitation assay at elevated temperatures (Figure 4C). (Figure 4B)
PMID:32499408	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC736.11 [assayed_using] PomBase:SPAC140.03	even at 25 °C, Arb1-associated Ago1 in the immunoprecipitates from hsp90-G84C cells was much reduced compared to wild-type samples (Figure 4E)
PMID:32499408	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPBC83.03c	that the amount of Tas3 but not Ago1 was significantly reduced once the hsp90-G84C cells were shifted to restrictive temperature of 37 °C for 4 hours (Figure 4B)
PMID:32502403	GO:1990023	mitotic spindle midzone [exists_during] mitotic anaphase B	(Figure 1A)
PMID:32502403	GO:0140515	mitotic nuclear bridge organization	(comment: CHECK causally upstreasm of?)
PMID:32502403	FYPO:0007546	abolished nuclear envelope division [has_penetrance] 20	A failed mitotic nuclear division is a cell phenotype observed at the end of mitosis during the vegetative life cycle in which the nuclear division does not occur and the two DNA masses remain linked by the internuclear membrane bridge. This can result in the coalescence of both DNA masses into one nucleus.
PMID:32502403	FYPO:0007546	abolished nuclear envelope division [has_penetrance] 94	A failed mitotic nuclear division is a cell phenotype observed at the end of mitosis during the vegetative life cycle in which the nuclear division does not occur and the two DNA masses remain linked by the internuclear membrane bridge. This can result in the coalescence of both DNA masses into one nucleus.
PMID:32502403	FYPO:0007546	abolished nuclear envelope division [has_penetrance] complete	A failed mitotic nuclear envelope division is a cell phenotype observed at the end of mitosis during the vegetative life cycle in which the nuclear division does not occur and the two DNA masses remain linked by the internuclear membrane bridge. This can result in the coalescence of both DNA masses into one nucleus. We found that wild-type cells showed timed NE division in the absence of actomyosin ring (Figures 4A and 4B), demonstrating that NE division is independent of cell division. However, 100% of imp1D cells (n = 126) completely failed to undergo NE division, resulting in cells with two nuclei linked by a long NE bridge (Figures 4A and 4B; Video S4). This result demonstrates that Imp1 is required for NE division.
PMID:32502403	GO:0097038	perinuclear endoplasmic reticulum [exists_during] mitotic anaphase B	Apq12 localized in tubules connected to or in close proximity to the MMD and at spindle pole regions, mirroring ER tubules marked with Yop1-GFP, Rtn1- GFP, or the artificial ER luminal marker mCherry-ADEL
PMID:32502403	GO:0140599	mitotic nuclear bridge midzone membrane domain [exists_during] mitotic anaphase B	Apq12 localized in tubules connected to or in close proximity to the MMD and at spindle pole regions, mirroring ER tubules marked with Yop1-GFP, Rtn1- GFP, or the artificial ER luminal marker mCherry-ADEL
PMID:32502403	FYPO:0006716	large and small daughter nuclei, with unequal nuclear envelope distribution [has_penetrance] high	Consistently, these cells showed a higher frequency of asymmetric NE divisions (Figure S2C)
PMID:32502403	FYPO:0007549	coalescence of partially separated nuclei [has_penetrance] complete	The coalescence of daughter nuclei was also observed in apq12D cells that failed to undergo nuclear division (Figure 4F).
PMID:32502403	FYPO:0007545	increased duration of protein localization to mitotic nuclear bridge [has_penetrance] high [assayed_using] PomBase:SPAC1786.03	We found that, in imp1D cells, NPCs were detected at the MMD and the peripheral NPC component Nup60 was removed from this domain (Figure 4C); however, the removal of structural components such as Nup107 and the membrane nucleoporin Cut11 was not observed (Figures 4C, S3A, and S3B).
PMID:32502403	FYPO:0007549	coalescence of partially separated nuclei [has_penetrance] complete	When these cells were left in this condition, daughter nuclei began to move closer to each other until they finally merged into one single nucleus (Figure 4E). This phenotype can be promoted if spindles are forced to disassemble by treating the cells with 30 mg/mL MBC, resulting in 35% (n = 34) of nuclear coalescence events.
PMID:32502403	FYPO:0007548	abnormal mitotic nuclear bridge midzone membrane domain organization [has_penetrance] high	ase1D cells that elongated the spindle, the MMD was not properly formed, and the number of NPCs was variable (Figure S2B
PMID:32502403	FYPO:0007547	abnormal nuclear pore localization to mitotic nuclear bridge midzone membrane [has_penetrance] high	ase1D cells that elongated the spindle, the MMD was not properly formed, and the number of NPCs was variable (Figure S2B
PMID:32518066	GO:0035613	RNA stem-loop binding	Lsm1Δ56C-7 can only bind tightly to the RNA with a 5′ stem-loop and single stranded 3′ end (Kd = 70 and 32 nM, respectively) (Fig. 5C).
PMID:32518066	GO:0008266	poly(U) RNA binding	These data indicate that high affinity binding sites for the Lsm1-7 complex must be at the 3′ termini of RNA.
PMID:32518066	GO:0035925	mRNA 3'-UTR AU-rich region binding	We conclude that the carboxy-terminal 12 amino acids of Lsm1 are important for the binding specificity of Lsm1-7.
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure 2)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure 2)
PMID:32546512	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 2) (comment: vw changed from decreased to normal (compared to WT))
PMID:32546512	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 2) (comment: vw changed from decreased to normal (compared to WT))
PMID:32546512	FYPO:0001234	slow vegetative cell population growth	(Figure 2) We obtained viable erh1Figure 2A Δ asp1-D333A haploids after mating and sporulation; the doublemutant was slow-growing on YES agar and cold-sensitive: he de-repression of Pho1 activity by erh1Δ was erased in the asp1-D333A background
PMID:32546512	FYPO:0001234	slow vegetative cell population growth	(Figure 2) We obtained viable erh1Figure 2A Δ asp1-D333A haploids after mating and sporulation; the doublemutant was slow-growing on YES agar and cold-sensitive: he de-repression of Pho1 activity by erh1Δ was erased in the asp1-D333A background
PMID:32546512	FYPO:0005369	abolished cell population growth at low temperature	(Figure 2A)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure 2A)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure 2A)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 2B)
PMID:32546512	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 2B)
PMID:32546512	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] medium	(Figure 2C)
PMID:32546512	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 2C)
PMID:32546512	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] high	(Figure 2C) the fivefold de-repression of Pho1 in the aps1Δ strain was enhanced additively to 12- fold in the erh1Δ aps1Δ background
PMID:32546512	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] high	(Figure 2C) the fivefold de-repression of Pho1 in the aps1Δ strain was enhanced additively to 12- fold in the erh1Δ aps1Δ background
PMID:32546512	FYPO:0003267	normal acid phosphatase activity	(Figure 4)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure 4)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure 4)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure 4)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 4)
PMID:32546512	FYPO:0000082	decreased cell population growth at high temperature	(Figure 4)
PMID:32546512	FYPO:0003267	normal acid phosphatase activity	(Figure 4)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure 4)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 4)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 4)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 4)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 4)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 4)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity	(Figure 4B)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity	(Figure 4B)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity	(Figure 4B)
PMID:32546512	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPAC19G12.17	(Figure 4B)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity	(Figure 4B)
PMID:32546512	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPAC19G12.17	(Figure 4B)
PMID:32546512	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 5)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure 5)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure 5)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure 5)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 5)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 5)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure 5)
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 5)
PMID:32546512	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] high	(Figure 5)
PMID:32546512	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] high	(Figure 5)
PMID:32546512	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] high	(Figure 5)
PMID:32546512	FYPO:0001357	normal vegetative cell population growth	(Figure 8)
PMID:32546512	FYPO:0001357	normal vegetative cell population growth	(Figure 8)
PMID:32546512	FYPO:0001357	normal vegetative cell population growth	(Figure 8)
PMID:32546512	FYPO:0001357	normal vegetative cell population growth	(Figure 8)
PMID:32546512	FYPO:0006821	slow vegetative cell growth	(Figure 8)
PMID:32546512	FYPO:0002061	inviable vegetative cell population	(Figure S1)
PMID:32546512	FYPO:0002085	normal vegetative cell growth	(Figure S1)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure S1)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure S1)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure S1)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure S1)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure S1)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure S1)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure S1)
PMID:32546512	FYPO:0000080	decreased cell population growth at low temperature	(Figure S1)
PMID:32546512	FYPO:0000082	decreased cell population growth at high temperature	(Figure S1)
PMID:32546512	FYPO:0004481	abolished cell population growth at high temperature	(Figure S1)
PMID:32546512	FYPO:0000082	decreased cell population growth at high temperature	(Figure S1)
PMID:32546512	FYPO:0001234	slow vegetative cell population growth	(Figure S1)
PMID:32546512	FYPO:0001234	slow vegetative cell population growth	(Figure S1)
PMID:32546512	FYPO:0002061	inviable vegetative cell population	(Figure S1)
PMID:32546512	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: (Normal compared to WT)) The instructive findings were that the de-repression of Pho1 by erh1Δ was effaced in rhn1Δ, ssu72-C13S, ctf1Δ, ppn1Δ, and swd22Δ cells and was attenuated in dis2Δ cells (Fig. 4B
PMID:32546512	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: (Normal compared to WT)) The instructive findings were that the de-repression of Pho1 by erh1Δ was effaced in rhn1Δ, ssu72-C13S, ctf1Δ, ppn1Δ, and swd22Δ cells and was attenuated in dis2Δ cells (Fig. 4B
PMID:32546512	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	In addition, using the prt-pho1 reporter plasmid to gauge Pho1 acid phosphatase expression, we found that Pho1 activity was lower in mmi1Δ cells than in wild-type cells (Fig. 6C)
PMID:32546512	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02 [has_severity] low	Northern blotting and primer extension, Figure 6
PMID:32546512	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4G3.02	Northern blotting, Figure 6
PMID:32546512	GO:0043628	regulatory ncRNA 3'-end processing	a scenario in which Erh1 acts as a brake on Mmi1’s ability to promote CPF-dependent termination during prt lncRNA synthesis.
PMID:32546512	GO:0043628	regulatory ncRNA 3'-end processing	suggest ... Erh1 acts as a brake on Mmi1’s ability to promote CPF-dependent termination during prt lncRNA synthesis.
PMID:32546830	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC20F10.04c [assayed_using] PomBase:SPCC5E4.06	(Figure 2)
PMID:32546830	FYPO:0002150	inviable spore population	(Figure 2E) (comment: tetrad analysis)
PMID:32546830	GO:0005515	protein binding	(comment: linker)
PMID:32571823	FYPO:0005253	resistance to tamoxifen	(Fig 4) (comment: Ccr1 is a molecular target of TAM.)
PMID:32571823	FYPO:0002716	normal vacuole fusion during vegetative growth	(Fig. 5)
PMID:32571823	FYPO:0002060	viable vegetative cell population	(Figure 1)
PMID:32571823	FYPO:0002640	sensitive to clotrimazole [has_severity] high	(Figure 1)
PMID:32571823	FYPO:0002640	sensitive to clotrimazole [has_severity] high	(Figure 1)
PMID:32571823	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Figure 2)
PMID:32571823	FYPO:0003853	sensitive to fluconazole [has_severity] medium	(Figure 2)
PMID:32571823	FYPO:0003358	sensitive to miconazole [has_severity] medium	(Figure 2)
PMID:32571823	FYPO:0002641	sensitive to micafungin [has_severity] low	(Figure 2)
PMID:32571823	FYPO:0006581	sensitive to fenpropimorph [has_severity] low	(Figure 2)
PMID:32571823	FYPO:0000086	sensitive to tacrolimus [has_severity] low	(Figure 2)
PMID:32571823	FYPO:0005252	sensitive to tamoxifen [has_severity] low	(Figure 2)
PMID:32571823	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Figure 2)
PMID:32571823	FYPO:0005252	sensitive to tamoxifen [has_severity] medium	(Figure 2)
PMID:32571823	FYPO:0000086	sensitive to tacrolimus [has_severity] medium	(Figure 2)
PMID:32571823	FYPO:0006581	sensitive to fenpropimorph [has_severity] medium	(Figure 2)
PMID:32571823	FYPO:0002641	sensitive to micafungin [has_severity] medium	(Figure 2)
PMID:32571823	FYPO:0002328	sensitive to terbinafine [has_severity] medium	(Figure 2)
PMID:32571823	FYPO:0003358	sensitive to miconazole [has_severity] high	(Figure 2)
PMID:32571823	FYPO:0003853	sensitive to fluconazole [has_severity] high	(Figure 2)
PMID:32571823	FYPO:0000647	vegetative cell lysis [has_severity] medium	(Figure 2b)
PMID:32571823	FYPO:0000647	vegetative cell lysis [has_severity] medium	(Figure 2b)
PMID:32571823	FYPO:0002792	small vacuoles present in increased numbers during cellular hypotonic response	(Figure 2c)
PMID:32571823	FYPO:0005252	sensitive to tamoxifen [has_severity] medium	(Figure 2d)
PMID:32571823	FYPO:0002641	sensitive to micafungin [has_severity] low	(Figure 2d)
PMID:32571823	FYPO:0002641	sensitive to micafungin [has_severity] medium	(Figure 2d)
PMID:32571823	FYPO:0002640	sensitive to clotrimazole [has_severity] high	(Figure 2d)
PMID:32571823	FYPO:0005254	normal growth on tamoxifen	(Figure 2d)
PMID:32571823	FYPO:0001470	normal growth on tacrolimus	(Figure 2d)
PMID:32571823	FYPO:0002328	sensitive to terbinafine	(Figure 2d)
PMID:32571823	FYPO:0000086	sensitive to tacrolimus	(Figure 2d)
PMID:32571823	FYPO:0002643	normal growth on clotrimazole	(Figure 2d)
PMID:32571823	FYPO:0002343	normal growth on terbinafine	(Figure 2d)
PMID:32571823	FYPO:0001758	increased protein phosphatase activity [assayed_enzyme] PomBase:SPBP4H10.04	(Figure 3A) (comment: increased cacineurin signalling)
PMID:32571823	FYPO:0001198	increased cellular calcium level	(Figure 3B)
PMID:32571823	FYPO:0000098	sensitive to calcium	(Figure 3C)
PMID:32571823	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_using] PomBase:SPBP4H10.04	(Figure 3D)
PMID:32594847	FYPO:0001125	normal vegetative cell shape	DNS
PMID:32594847	FYPO:0001124	normal vegetative cell size	DNS
PMID:32594847	FYPO:0000047	normal cell population growth	DNS
PMID:32650974	GO:0006487	protein N-linked glycosylation	(Figure 1,2,4) These results suggested that the elongation of mannan takes place sequentially by the actions of the a-mannosyltransferases in the order of SpOch1p, SpMnn9p and SpAnp1p.
PMID:32650974	GO:0006487	protein N-linked glycosylation	(Figure 1,2,4) These results suggested that the elongation of mannan takes place sequentially by the actions of the a-mannosyltransferases in the order of SpOch1p, SpMnn9p and SpAnp1p.
PMID:32650974	GO:0006487	protein N-linked glycosylation	(Figure 4) These results suggested that the elongation of mannan takes place sequentially by the actions of the a-mannosyltransferases in the order of SpOch1p, SpMnn9p and SpAnp1p.
PMID:32650974	GO:0140497	mannan polymerase II complex	(comment: CHECK M-Pol I complex)
PMID:32650974	GO:0140497	mannan polymerase II complex	(comment: CHECK M-Pol I complex)
PMID:32650974	FYPO:0007436	swollen elongated multiseptate vegetative cell	(comment: CHECK swollen)
PMID:32650974	GO:0005515	protein binding	(comment: split YFP and affinity capture)
PMID:32692737	GO:2000779	regulation of double-strand break repair	(comment: regulates pathway choice)
PMID:32723864	FYPO:0007749	decreased protein localization to meiotic spindle during meiosis I [assayed_using] PomBase:SPAPB1A10.09	(Fig. 3F) The results show that the absence of Klp2 affects the localization of Ase1-GFP to the meiotic spindles and leads to a decrease of the Ase1-GFP intensity on the meiotic spindles.
PMID:32723864	FYPO:0004395	short bipolar mitotic spindle during metaphase [has_penetrance] ~18	(Figure 5)
PMID:32723864	FYPO:0007753	multiple spindles during meiosis I [has_penetrance] ~28	(Figure 5)
PMID:32723864	FYPO:0004395	short bipolar mitotic spindle during metaphase [has_penetrance] ~82	(Figure 5)
PMID:32723864	FYPO:0007752	spindle regression during meiosis I	(Figure 5) Three typical types of plots are shown: (I) WTlike metaphase spindle length (maintenance), (II) spindle regression (regression), and (III) continuous spindle elongation (lacking metaphase).
PMID:32723864	FYPO:0004395	short bipolar mitotic spindle during metaphase [has_penetrance] ~74	(Figure 6)
PMID:32723864	FYPO:0004395	short bipolar mitotic spindle during metaphase [has_penetrance] ~26	(Figure 6)
PMID:32723864	FYPO:0007755	short meiotic spindle during metaphase I [has_penetrance] 71	(Figure 6)
PMID:32723864	FYPO:0007756	abnormal homologous chromosome segregation with collapsed spindle	(Figure 7)
PMID:32723864	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_penetrance] ~20	(Figure 7)
PMID:32723864	FYPO:0007756	abnormal homologous chromosome segregation with collapsed spindle	(Figure 7)
PMID:32723864	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 7)
PMID:32723864	FYPO:0007756	abnormal homologous chromosome segregation with collapsed spindle	(Figure 7)
PMID:32723864	FYPO:0007746	normal spindle elongation during meiotic metaphase I	(Figure S1)
PMID:32723864	FYPO:0007745	abnormal spindle assembly during meiosis I [has_severity] high	(Figure S1)
PMID:32723864	FYPO:0007746	normal spindle elongation during meiotic metaphase I	(Figure S1)
PMID:32723864	FYPO:0007744	spindle collapse during meiotic prophase I	(Figure S1) In contrast, 50% of the spindles in klp2D cells underwent abrupt collapse during metaphase I (Fig. 2, A, C, and E, 3A)
PMID:32723864	FYPO:0007751	spindle collapse during meiotic prometaphase I	(Figure S1) In contrast, 50% of the spindles in klp2D cells underwent abrupt collapse during metaphase I (Fig. 2, A, C, and E, 3A)
PMID:32723864	GO:0140642	meiotic spindle formation (spindle phase two)	Ase1 is required for promoting spindle elongation during mitotic prophase but synergizes with Klp2 to maintain spindle stability during metaphase I.
PMID:32723864	GO:0061804	mitotic spindle formation (spindle phase one)	Ase1 is required for promoting spindle elongation during mitotic prophase but synergizes with Klp2 to maintain spindle stability during metaphase I.
PMID:32723864	GO:0140642	meiotic spindle formation (spindle phase two)	Ase1 is required for promoting spindle elongation during mitotic prophase but synergizes with Klp2 to maintain spindle stability during metaphase I.
PMID:32723864	FYPO:0007748	increased duration of spindle assembly during meiosis I	In both mitotic and meiotic cells, the absence of Klp2 slightly but significantly prolonged the duration of preanaphase (Fig. 2, F and G).
PMID:32723864	FYPO:0007747	normal meiotic spindle length during prophase I	absence of Klp2 did not significantly affect spindle elongation during prophase I and only slightly lengthened the maximal spindle length during metaphase I (Fig. 2G).
PMID:32735772	FYPO:0007446	decreased reticulophagy during cellular response to endoplasmic reticulum stress	(Fig. 3)
PMID:32735772	FYPO:0005264	resistance to dithiothreitol	(Fig. 6b)
PMID:32735772	FYPO:0005264	resistance to dithiothreitol	(Fig. 6b)
PMID:32735772	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S1B)
PMID:32735772	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S1B)
PMID:32735772	FYPO:0001357	normal vegetative cell population growth	(Fig. S1B)
PMID:32735772	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC6B12.08 [assayed_using] PomBase:SPBP8B7.24c	(Figure 1C)
PMID:32735772	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC6B12.08 [assayed_using] PomBase:SPBP8B7.24c	(Figure 1C)
PMID:32735772	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC6B12.08 [assayed_using] PomBase:SPBP8B7.24c	(Figure 1C)
PMID:32735772	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC6B12.08 [assayed_using] PomBase:SPBC16G5.05c	(Figure 1C) AIM-mutated Epr1- C was pulled down as efficiently as wild-type Epr1-C by Scs2 but did not support the pull-down of Atg8 PLUS more experiments We hypothesized that the main role of Epr1 in ER-phagy is to mediate a connection between Atg8 and VAPs. requirement of Epr1 in ER-phagy can be by-passed by an artificial soluble tether that bridges an Atg8-VAP connection.Figure 4D).
PMID:32735772	FYPO:0007446	decreased reticulophagy during cellular response to endoplasmic reticulum stress	(Figure 2B, 2G, 2H)
PMID:32735772	GO:0000407	phagophore assembly site	(Figure 2a)
PMID:32735772	GO:0005783	endoplasmic reticulum	(Figure 2a)
PMID:32735772	GO:0005515	protein binding	(Figure 3C) Epr1 interacted with both Scs2 and Scs22 in the Y2H assay
PMID:32735772	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC6B12.08 [assayed_using] PomBase:SPBC16G5.05c	(Figure 3C) The 42-amino-acid Epr1-C region (residues 339-380), which is capable of Atg8 binding and contains the predicted FFAT motif, is sufficient for interacting with VAPs
PMID:32735772	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC6B12.08 [assayed_using] PomBase:SPAC17C9.12	(Figure 3C) The 42-amino-acid Epr1-C region (residues 339-380), which is capable of Atg8 binding and contains the predicted FFAT motif, is sufficient for interacting with VAPs
PMID:32735772	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC16G5.05c [assayed_using] PomBase:SPAC6B12.08	(Figure 3C) The 42-amino-acid Epr1-C region (residues 339-380), which is capable of Atg8 binding and contains the predicted FFAT motif, is sufficient for interacting with VAPs
PMID:32735772	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC6B12.08 [assayed_using] PomBase:SPAC17C9.12	(Figure 3C) The 42-amino-acid Epr1-C region (residues 339-380), which is capable of Atg8 binding and contains the predicted FFAT motif, is sufficient for interacting with VAPs
PMID:32735772	FYPO:0007449	abolished protein localization to endoplasmic reticulum, with protein mislocalized to cytoplasm	(Figure 3D)
PMID:32735772	FYPO:0007449	abolished protein localization to endoplasmic reticulum, with protein mislocalized to cytoplasm [assayed_using] PomBase:SPAC6B12.08	(Figure 3D) (comment: CHECK ******check with DAN, is this an overexpression allele?)
PMID:32735772	FYPO:0007449	abolished protein localization to endoplasmic reticulum, with protein mislocalized to cytoplasm [assayed_using] PomBase:SPAC6B12.08	(Figure 3D) As expected, in cells lacking both Scs2 and Scs22, Epr1 became diffusely distributed in the cytoplasm
PMID:32735772	FYPO:0007447	abolished reticulophagy during cellular response to endoplasmic reticulum stress	(Figure 5A) reduced in scs2D and abolished in scs2D scs22D
PMID:32735772	FYPO:0007446	decreased reticulophagy during cellular response to endoplasmic reticulum stress	(Figure 5A) reduced in scs2D and abolished in scs2D scs22D
PMID:32735772	FYPO:0000843	sensitive to dithiothreitol	(Figure 6A)
PMID:32735772	FYPO:0000843	sensitive to dithiothreitol	(Figure 6A)
PMID:32735772	FYPO:0000843	sensitive to dithiothreitol	(Figure 6A)
PMID:32735772	FYPO:0000843	sensitive to dithiothreitol	(Figure 6A)
PMID:32735772	FYPO:0000843	sensitive to dithiothreitol	(Figure 6A)
PMID:32735772	FYPO:0000843	sensitive to dithiothreitol	(Figure 6A)
PMID:32735772	FYPO:0000843	sensitive to dithiothreitol	(Figure 6A)
PMID:32735772	FYPO:0005910	decreased protein level during cellular response to endoplasmic reticulum stress [assayed_using] PomBase:SPAC6B12.08	(Figure 7B) We found that DTT-induced increase of Epr1 was severely diminished in ire1D (Figure 7B), indicating that Epr1 upregulation requires Ire1.
PMID:32735772	FYPO:0007446	decreased reticulophagy during cellular response to endoplasmic reticulum stress [has_severity] low	(Figure 7E) the ER-phagy defect of ire1D was largely rescued (Figure 7E).
PMID:32735772	FYPO:0006294	normal macroautophagy during nitrogen starvation	(Figure S1E)
PMID:32735772	FYPO:0006294	normal macroautophagy during nitrogen starvation	(Figure S1E) nitrogen starvation-induced ER-phagy appeared to be normal in epr1D
PMID:32735772	FYPO:0007447	abolished reticulophagy during cellular response to endoplasmic reticulum stress	(Figure S6B), indicating that Ire1 is dispensable for DTT-induced bulk autophagy but is essential for DTT-induced ER-phagy.
PMID:32735772	GO:0005515	protein binding	(Figures 1B and S1C)
PMID:32735772	GO:0005515	protein binding	(Figures 1B and S1C)
PMID:32735772	GO:0061709	reticulophagy [happens_during] response to endoplasmic reticulum stress	(Figures 2G and 2H)
PMID:32735772	FYPO:0007449	abolished protein localization to endoplasmic reticulum, with protein mislocalized to cytoplasm	(Figures S3B and S3D) Epr1-C showed ER localization in vegetatively growing cells, whereas Epr1-N was diffusely distributed in the cytoplasm and the nucleus
PMID:32735772	FYPO:0006378	normal protein localization to endoplasmic reticulum during vegetative growth	(Figures S3B and S3D) Epr1-C showed ER localization in vegetatively growing cells, whereas Epr1-N was diffusely distributed in the cytoplasm and the nucleus
PMID:32735772	GO:0044804	nucleophagy	(comment: CHECK check with Dan ****) Thus, Epr1 is an ER-phagy receptor required for ER stress-induced selective autophagy of both the nuclear envelope and the peripheral ER.
PMID:32735772	FYPO:0007444	normal macroautophagy during cellular response to endoplasmic reticulum stress	Mutating the FFAT motif or the AIM abolished the ability of Epr1-C to rescue epr1D (Figures 4A, 4B, and S3D).
PMID:32735772	FYPO:0007444	normal macroautophagy during cellular response to endoplasmic reticulum stress	Mutating the FFAT motif or the AIM abolished the ability of Epr1-C to rescue epr1D (Figures 4A, 4B, and S3D).
PMID:32735772	FYPO:0007444	normal macroautophagy during cellular response to endoplasmic reticulum stress	Remarkably, Epr1-C, but not Epr1-N, could completely rescue the defects of epr1D in DTT-induced ER- phagy
PMID:32790622	FYPO:0002052	normal sporulation frequency	(comment: evidence: viable spore yield assay)
PMID:32790622	FYPO:0002151	inviable spore [has_penetrance] 84	(comment: evidence: viable spore yield assay)
PMID:32790622	FYPO:0002151	inviable spore [has_penetrance] 75	(comment: evidence: viable spore yield assay)
PMID:32790622	FYPO:0002151	inviable spore [has_penetrance] 96	(comment: evidence: viable spore yield assay)
PMID:32790622	FYPO:0002151	inviable spore [has_penetrance] 67	(comment: evidence: viable spore yield assay) 16% of the surviving spores had inherited two copies of chromosome 3 and were thus aneuploid/diploid.
PMID:32790622	FYPO:0002151	inviable spore [has_penetrance] 19	(comment: evidence: viable spore yield assay) 20% of the surviving spores had inherited the two centromere 3-linked markers suggesting they are aneuploid/diploid.
PMID:32790622	FYPO:0002151	inviable spore [has_penetrance] 83	(comment: evidence: viable spore yield assay) 30% of the surviving spores had inherited the two centromere 3-linked markers suggesting they are aneuploid/diploid.
PMID:32817556	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] low	(comment: Phenotype is greatly enhanced by mutation of the IR-R boundary element)
PMID:32841241	FYPO:0002580	normal mature tRNA level [assayed_using] threonyl_tRNA	(comment: CHECK ACU codon/AGU anticodon tRNA)
PMID:32841241	FYPO:0002583	decreased mature tRNA level during vegetative growth [has_severity] low [assayed_using] prolyl_tRNA	(comment: CHECK CCU codon/AGG anticodon tRNA)
PMID:32841241	FYPO:0002583	decreased mature tRNA level during vegetative growth [has_severity] high [assayed_using] prolyl_tRNA	(comment: CHECK CCU codon/AGG anticodon tRNA)
PMID:32841241	FYPO:0002583	decreased mature tRNA level during vegetative growth [has_severity] medium [assayed_using] prolyl_tRNA	(comment: CHECK CCU codon/AGG anticodon tRNA)
PMID:32841241	FYPO:0002583	decreased mature tRNA level during vegetative growth [has_severity] medium [assayed_using] prolyl_tRNA	(comment: CHECK CCU codon/AGG anticodon tRNA)
PMID:32841241	FYPO:0002583	decreased mature tRNA level during vegetative growth [has_severity] medium [assayed_using] prolyl_tRNA	(comment: CHECK CCU codon/AGG anticodon tRNA)
PMID:32841241	FYPO:0002583	decreased mature tRNA level during vegetative growth [has_severity] low [assayed_using] prolyl_tRNA	(comment: CHECK CCU codon/AGG anticodon tRNA)
PMID:32841241	FYPO:0002583	decreased mature tRNA level during vegetative growth [has_severity] medium [assayed_using] tyrosyl_tRNA	(comment: CHECK UAC codon/GUA anticodon tRNA)
PMID:32841241	FYPO:0002583	decreased mature tRNA level during vegetative growth [has_severity] low [assayed_using] tyrosyl_tRNA	(comment: CHECK UAC codon/GUA anticodon tRNA)
PMID:32841241	FYPO:0002583	decreased mature tRNA level during vegetative growth [has_severity] medium [assayed_using] tyrosyl_tRNA	(comment: CHECK UAC codon/GUA anticodon tRNA)
PMID:32841241	FYPO:0002583	decreased mature tRNA level during vegetative growth [has_severity] high [assayed_using] tyrosyl_tRNA	(comment: CHECK UAC codon/GUA anticodon tRNA)
PMID:32841241	FYPO:0002583	decreased mature tRNA level during vegetative growth [has_severity] low [assayed_using] tyrosyl_tRNA	(comment: CHECK UAC codon/GUA anticodon tRNA)
PMID:32841241	FYPO:0002583	decreased mature tRNA level during vegetative growth [has_severity] medium [assayed_using] tyrosyl_tRNA	(comment: CHECK UAC codon/GUA anticodon tRNA)
PMID:32848252	GO:0044615	nuclear pore nuclear basket [exists_during] mitotic interphase	(Fig. 3a) Extended Data Fig. 4a-c Removed from nuclear basket in bridge midzone during nuclear division
PMID:32848252	GO:0044615	nuclear pore nuclear basket [exists_during] mitotic interphase	(Fig. 3a) Extended Data Fig. 4a-c Removed from nuclear basket in bridge midzone during nuclear division
PMID:32848252	GO:0140512	mitotic nuclear bridge midzone	(Fig. 3b)
PMID:32848252	FYPO:0003783	abnormal nuclear pore localization during mitosis [has_penetrance] complete [has_severity] high [assayed_using] PomBase:SPAC1786.03	(Fig. 3g)
PMID:32848252	FYPO:0007458	abolished nuclear pore localization to mitotic nuclear bridge [has_severity] high [assayed_using] PomBase:SPCC285.13c [has_penetrance] complete	(Fig. 4) Extended Data Fig. 7
PMID:32848252	FYPO:0001556	excess nuclear envelope present [has_penetrance] complete [has_severity] high	(Fig. 4, 6)
PMID:32848252	FYPO:0004725	nuclear envelope protrusion present during mitotic interphase [has_penetrance] high [has_severity] high	(Fig. 4,6)
PMID:32848252	FYPO:0000772	perforated nuclear envelope [has_penetrance] medium [has_severity] medium	(Fig. 4a, b) Daughter nuclei in the les1Δ strain also suffered transient leakages at the time of maximum spindle elongation, as measured by loss of nuclear NLS-GFP
PMID:32848252	GO:0140516	mitotic nuclear pore complex disassembly [happens_during] mitotic anaphase B	(comment: causally upstream?)
PMID:32848252	GO:0007084	mitotic nuclear membrane reassembly	(comment: lem2 (which encodes Lem2, the binding partner of Cmp7) is also SL with les1)
PMID:32848252	FYPO:0003783	abnormal nuclear pore localization during mitosis [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC1786.03	Extended Data Fig. 4
PMID:32848252	FYPO:0000337	abnormal mitosis [has_penetrance] complete [has_severity] high	Extended Data Fig. 6 c,d
PMID:32848252	GO:0005637	nuclear inner membrane	Extended Data Figure 2 (comment: nucleoplasmic side)
PMID:32848252	FYPO:0003783	abnormal nuclear pore localization during mitosis [has_penetrance] high [has_severity] medium [assayed_using] PomBase:SPAC1786.03	Extended Data Figure 8
PMID:32848252	GO:0007084	mitotic nuclear membrane reassembly	Instead, the repair process was associated with recruitment of the ESCRTIII protein Cmp7 (Fig. 4d) to sites of local NEB20 (Fig. 4d, Extended Data Fig. 8b, c).
PMID:32848252	GO:1905557	regulation of mitotic nuclear envelope disassembly [happens_during] mitotic anaphase B	Les1 stalks functionally isolate daughter nuclei from the process of Imp1-dependent local NEB at the centre of the bridge probably acts to create a seal by gathering the inner nuclear envelope tightly around the spindle
PMID:32878942	GO:2000099	regulation of establishment or maintenance of bipolar cell polarity	(Fig. 3D)
PMID:32878942	GO:0061245	establishment or maintenance of bipolar cell polarity	(Fig. 3D)
PMID:32878942	GO:2000099	regulation of establishment or maintenance of bipolar cell polarity	(Fig. 3D)
PMID:32878942	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPBC83.18c	(Fig. 4)
PMID:32878942	FYPO:0003532	increased monopolar index [has_severity] high	(Fig. 4D,E,F)
PMID:32878942	FYPO:0003776	increased pseudohyphal growth [has_severity] medium	(Fig. 4H,I and S3F,G)
PMID:32878942	FYPO:0003776	increased pseudohyphal growth [has_severity] medium	(Fig. 4H,I and S3F,G)
PMID:32878942	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC83.18c [assayed_using] PomBase:SPAC20G8.05c	(Fig. S3A)
PMID:32878942	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC83.18c [assayed_using] PomBase:SPBC11C11.02	(Fig. S3A)
PMID:32878942	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC83.18c [assayed_using] PomBase:SPBC11C11.02	(Fig. S3A)
PMID:32878942	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC83.18c [assayed_using] PomBase:SPAC20G8.05c	(Fig. S3A)
PMID:32878942	FYPO:0003532	increased monopolar index	(Fig. S3B,C)
PMID:32878942	FYPO:0003532	increased monopolar index	(Fig. S3B,C)
PMID:32878942	FYPO:0003532	increased monopolar index	(Fig. S3B,C,D)
PMID:32878942	FYPO:0000674	normal cell population growth at high temperature	(Fig. S3E)
PMID:32878942	FYPO:0000674	normal cell population growth at high temperature	(Fig. S3E)
PMID:32878942	FYPO:0000674	normal cell population growth at high temperature	(Fig. S3E)
PMID:32878942	FYPO:0000674	normal cell population growth at high temperature	(Fig. S3E)
PMID:32878942	FYPO:0003776	increased pseudohyphal growth [has_severity] medium	(Fig. S3F)
PMID:32878942	FYPO:0003776	increased pseudohyphal growth [has_severity] high	(Fig. S3F,G)
PMID:32878942	FYPO:0002871	decreased protein localization to growing cell tip [assayed_using] PomBase:SPBC83.18c	(Figure 2D,E)
PMID:32878942	FYPO:0001396	normal NETO	(Figure 2F-H)
PMID:32878942	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPBC83.18c	(Figure 2I)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000011	RNA level increased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000011	RNA level increased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000011	RNA level increased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000011	RNA level increased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000011	RNA level increased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	PomGeneEx:0000012	RNA level decreased [in_presence_of] arginine	(comment: CHECK EMM media with arginine)
PMID:32896087	FYPO:0007560	sensitive to arginine [has_severity] high	(comment: Data from screening of prototroph deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] medium	(comment: Liquid media growth assay. Mutant isolated from deletion collection.)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] medium	(comment: Liquid media growth assay. Mutant isolated from deletion collection.)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: Liquid media growth assay. Mutant isolated from deletion collection.)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] medium	(comment: Liquid media growth assay. Mutant isolated from deletion collection.)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] medium	(comment: Liquid media growth assay. Mutant isolated from deletion collection.)
PMID:32896087	GO:0005739	mitochondrion	(comment: arg3-GFP fusion localisation in minimal media (EMM))
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: solid media screen using prototroph deletion library.)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] medium	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] medium	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] medium	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] high	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] medium	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] medium	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] high	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] high	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] high	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] high	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] high	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] high	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] high	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] medium	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] high	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] medium	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] medium	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] medium	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	FYPO:0000035	growth auxotrophic for arginine [has_severity] low	(comment: solid media screen using prototrophic deletion library)
PMID:32896087	GO:0006526	L-arginine biosynthetic process	genes detected in screen Figure EV2
PMID:32896087	GO:0006526	L-arginine biosynthetic process	genes detected in screen Figure EV2
PMID:32896087	GO:0006526	L-arginine biosynthetic process	genes detected in screen Figure EV2
PMID:32896087	GO:0006526	L-arginine biosynthetic process	genes detected in screen Figure EV2
PMID:32896087	GO:0006526	L-arginine biosynthetic process	genes detected in screen Figure EV2
PMID:32896087	GO:0006526	L-arginine biosynthetic process	genes detected in screen Figure EV2
PMID:32896087	GO:0006526	L-arginine biosynthetic process	genes detected in screen Figure EV2
PMID:32896087	GO:0006526	L-arginine biosynthetic process	genes detected in screen Figure EV2
PMID:32896087	GO:0006526	L-arginine biosynthetic process	genes detected in screen Figure EV2
PMID:32908306	GO:0005739	mitochondrion	(comment: Cup1-GFP immunofluorescence)
PMID:32909946	FYPO:0006295	abolished macroautophagy during nitrogen starvation	(Fig. 1a)
PMID:32909946	FYPO:0006295	abolished macroautophagy during nitrogen starvation	(Fig. 1a)
PMID:32909946	FYPO:0001384	abolished protein kinase activity [assayed_enzyme] PomBase:SPCC63.08c	(Figure 1C) Such a band was not observed for D193A and T208A mutants, confirming that they are indeed kinase dead
PMID:32909946	FYPO:0001384	abolished protein kinase activity [assayed_enzyme] PomBase:SPCC63.08c	in vitro autophosphorylation activity of Atg1 from atg11D mutant was almost undetectable (Figure 1D
PMID:32909946	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPCC63.08c	we found that in S. pombe, Atg1 from atg13D, atg17D, or atg101D mutant exhibited autophosphorylation activities similar to that of Atg1 from wild type
PMID:32915139	FYPO:0000107	sensitive to latrunculin A [has_severity] high	(Fig. 1 S5)
PMID:32915139	FYPO:0000107	sensitive to latrunculin A [has_severity] medium	(Fig. 1 SF)
PMID:32915139	FYPO:0000107	sensitive to latrunculin A [has_severity] medium	(Fig. 1 SF)
PMID:32915139	FYPO:0000107	sensitive to latrunculin A [has_severity] high	(Fig. 1)
PMID:32915139	FYPO:0004513	resistance to latrunculin A	(Fig. 1F)
PMID:32915139	FYPO:0001317	normal RNA level during vegetative growth [assayed_using] PomBase:SPBC32H8.12c	(Fig. 2)
PMID:32915139	FYPO:0000107	sensitive to latrunculin A [has_severity] high	(Fig. 3a)
PMID:32915139	FYPO:0000107	sensitive to latrunculin A [has_severity] high	(Fig. 3a)
PMID:32915139	FYPO:0002998	abolished actomyosin contractile ring assembly, clumped medial cortical nodes [has_penetrance] 77	(Fig. 3b)
PMID:32915139	FYPO:0002998	abolished actomyosin contractile ring assembly, clumped medial cortical nodes [has_penetrance] 77	(Fig. 3c)
PMID:32915139	FYPO:0001368	normal actomyosin contractile ring assembly [has_penetrance] 80	(Fig. 4d)
PMID:32915139	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC895.05	(Fig. 5b)
PMID:32915139	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC895.05	(Fig. 5b)
PMID:32915139	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPCC895.05	(Fig. 5c)
PMID:32915139	MOD:00696	phosphorylated residue [present_during] cellular response to actin cytoskeletal stress	(Figure 1C)
PMID:32915139	MOD:00696	phosphorylated residue [present_during] cellular response to actin cytoskeletal stress	(Figure 1C)
PMID:32915139	MOD:00696	phosphorylated residue [present_during] cellular response to actin cytoskeletal stress	(Figure 1C)
PMID:32915139	FYPO:0007151	long actin cables	(Figure 2A, C) (comment: CHECK check, has synonym increased stability (better than increased length?))
PMID:32915139	FYPO:0001368	normal actomyosin contractile ring assembly	(Figure 2—Figure supplement 5). ngs formed and constricted correctly in >85% of sty1D cells (Figure 2D).
PMID:32915139	FYPO:0002082	increased protein ubiquitination during vegetative growth [assayed_using] PomBase:SPCC895.05	(Figure 5; Figure supplement 4)
PMID:32915139	MOD:01148	ubiquitinylated lysine [present_during] cellular response to actin cytoskeletal stress	(Figure 5; Figure supplement 4)
PMID:32915139	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPCC895.05	(Figure 5B)
PMID:32915139	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPCC895.05	(comment: CHECK 25%)
PMID:32915139	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPCC895.05	(comment: CHECK 50%)
PMID:32915139	FYPO:0004513	resistance to latrunculin A	(comment: CHECK Overexpression under the control of B-estradiol promoter (vw: I added an allele synonym, later these will be searchable and visible))
PMID:32915139	PomGeneEx:0000019	protein level decreased [during] cellular response to actin cytoskeletal stress	(comment: CHECK replaces wt annotation)
PMID:32915139	PomGeneEx:0000019	protein level decreased [during] cellular response to actin cytoskeletal stress	(comment: CHECK replaces wt annotation)
PMID:32915139	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPAC24B11.06c	Cells expressing a mutant allele Mcs4(D512N) that does not activate the SAPK pathway upon stimulation with hydro- gen peroxide (Shieh et al., 1997), displayed Sty1 activation during LatA treatment
PMID:32915139	PomGeneEx:0000019	protein level decreased [during] cellular response to heat	We found that total For3 levels also decline in S. pombe wild-type cells in response to stimuli that activate Sty1, like heat shock (40 ̊C), osmotic saline (0.6 M KCl), and oxidative stress (1 mM H2O2) (Pe ́rez and Cansado, 2010) in a MAPK-dependent manner (Figure 5—Figure supplement 3).
PMID:32915139	PomGeneEx:0000019	protein level decreased [during] cellular response to oxidative stress	We found that total For3 levels also decline in S. pombe wild-type cells in response to stimuli that activate Sty1, like heat shock (40 ̊C), osmotic saline (0.6 M KCl), and oxidative stress (1 mM H2O2) (Pe ́rez and Cansado, 2010) in a MAPK-dependent manner (Figure 5—Figure supplement 3).
PMID:32915139	PomGeneEx:0000019	protein level decreased [during] cellular hyperosmotic salinity response	We found that total For3 levels also decline in S. pombe wild-type cells in response to stimuli that activate Sty1, like heat shock (40 ̊C), osmotic saline (0.6 M KCl), and oxidative stress (1 mM H2O2) (Pe ́rez and Cansado, 2010) in a MAPK-dependent manner (Figure 5—Figure supplement 3).
PMID:32915139	FYPO:0004513	resistance to latrunculin A [has_severity] high	cells lacking Sty1 grew in these low LatA concentrations (Figure 1B).
PMID:32915139	FYPO:0001365	decreased rate of actomyosin contractile ring contraction	explicit delay in ring constriction and disassembly (21 ± 0.6 min in wild-type cells vs 36 ± 1.6 min in for3D cells; Figure 2—Figure supplement 5
PMID:32915139	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPAC24B11.06c	upstream elements of this signaling cascade shared this phenotype... Mcs4, the redundant MAPKKK´s Wak1 and Win1, and MAPKK Wis1 (Figure 1A, Figure 1—Figure supplement 1
PMID:32915139	FYPO:0004513	resistance to latrunculin A	upstream elements of this signaling cascade shared this phenotype... Mcs4, the redundant MAPKKK´s Wak1 and Win1, and MAPKK Wis1 (Figure 1A, Figure 1—Figure supplement 1
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1, Fig. 8)
PMID:33010152	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4)
PMID:33010152	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 4)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 4)
PMID:33010152	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 4)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 4)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 4)
PMID:33010152	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 4)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 4)
PMID:33010152	FYPO:0001355	decreased vegetative cell population growth	(Fig. 4)
PMID:33010152	FYPO:0001355	decreased vegetative cell population growth	(Fig. 4)
PMID:33010152	FYPO:0001355	decreased vegetative cell population growth	(Fig. 4)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 5)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 5)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 5)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 5)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0001357	normal vegetative cell population growth	(Fig. 5)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 8)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 8)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 8)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 8)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 8)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 8)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 8)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 8)
PMID:33010152	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 8)
PMID:33010152	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 8)
PMID:33049028	FYPO:0001934	abolished cell population growth on glycerol carbon source	(Fig. 4)
PMID:33049028	FYPO:0003040	decreased RNA splicing, via splicosome [assayed_using] PomBase:SPMIT.05	Further analysis revealed that the levels of intron-retaining cox1 and cob1 transcripts were increased in Δppr10 cells in the intron-containing background (Fig. 1A-C)
PMID:33049028	FYPO:0003040	decreased RNA splicing, via splicosome [assayed_using] PomBase:SPMIT.01	Further analysis revealed that the levels of intron-retaining cox1 and cob1 transcripts were increased in Δppr10 cells in the intron-containing background (Fig. 1A-C)
PMID:33049028	FYPO:0000840	normal RNA level [assayed_using] PomBase:SPMIT.01	The results showed that in the intronless background, the cox1 and cob1 mRNAs were detected at similar levels in WT[Δi] and Δppr10[Δi] cells (Fig. 1E-G
PMID:33049028	FYPO:0000840	normal RNA level [assayed_using] PomBase:SPMIT.05	The results showed that in the intronless background, the cox1 and cob1 mRNAs were detected at similar levels in WT[Δi] and Δppr10[Δi] cells (Fig. 1E-G
PMID:33108274	GO:0000324	fungal-type vacuole [part_of] ascospore	The wtf4 poison proteins is distributed throughout asci and spores in the absence of the wtf4antidote. The antidote assembles with the poison and then both proteins are localized to the vacuole in spores.
PMID:33108274	GO:0000324	fungal-type vacuole [part_of] ascospore	The wtf4 poison proteins is distributed throughout asci and spores in the absence of the wtf4antidote. The antidote assembles with the poison and then both proteins are localized to the vacuole in spores.
PMID:33109728	FYPO:0001355	decreased vegetative cell population growth	(Fig. 4B)
PMID:33109728	FYPO:0002061	inviable vegetative cell population	(Fig. 4B)
PMID:33109728	FYPO:0002061	inviable vegetative cell population	(Fig. 4B)
PMID:33109728	FYPO:0002061	inviable vegetative cell population	(Fig. 4B)
PMID:33109728	FYPO:0001357	normal vegetative cell population growth	(Fig. 4B)
PMID:33109728	FYPO:0001357	normal vegetative cell population growth	(Fig. 4B)
PMID:33109728	FYPO:0001355	decreased vegetative cell population growth	(Fig. 4B)
PMID:33109728	FYPO:0001357	normal vegetative cell population growth	(Fig. 4B)
PMID:33109728	FYPO:0001355	decreased vegetative cell population growth	(Fig. 4B)
PMID:33109728	FYPO:0001357	normal vegetative cell population growth	(Fig. 4B)
PMID:33125111	FYPO:0000056	mitochondria fused	(Fig. 1A).
PMID:33125111	FYPO:0001234	slow vegetative cell population growth	(Fig. 1B). (comment: decreasing slows after 6 hours)
PMID:33125111	FYPO:0007208	normal microtubule bundle length during mitotic interphase	(Fig. 1C).
PMID:33125111	FYPO:0002401	microtubule bundles present in increased numbers	(Fig. 1C).
PMID:33125111	FYPO:0000177	abnormal mitotic spindle assembly	(Fig. 3).
PMID:33125111	FYPO:0000141	abnormal mitotic sister chromatid segregation	(Fig. 3).
PMID:33131769	FYPO:0006940	asymmetric protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC4F8.13c	(comment: CHECK *****(abnormal distribution in...)) inhomogeneous contractile Rng2 ring An inhomogeneous contractile Rng2 ring is an abnormal actomyosin contractile ring that show an uneven distribution of 2mYFP-Rng2-12A over the ring.
PMID:33131769	FYPO:0001904	premature actomyosin contractile ring disassembly	An fragile actomyosin contractile ring is an abnormal actomyosin contractile ring that disassemble by treatment with a low dose of Latrunculin A, an actin depolymerizing agent.
PMID:33131769	FYPO:0001904	premature actomyosin contractile ring disassembly	An fragile actomyosin contractile ring is an abnormal actomyosin contractile ring that disassemble by treatment with a low dose of Latrunculin A, an actin depolymerizing agent.
PMID:33137119	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1c)
PMID:33137119	FYPO:0001021	normal growth during cellular response to osmotic stress	(Fig. 1c)
PMID:33137119	FYPO:0004765	normal cell population growth during glucose starvation	(Fig. 2)
PMID:33137119	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPBC16G5.15c	(Fig. 3A) (comment: affecting substrate Fkh2 in vitro)
PMID:33137119	FYPO:0001266	normal protein phosphorylation during cellular response to salt stress [assayed_using] PomBase:SPBC16G5.15c	(Fig. 3A) (comment: affecting substrate Fkh2 in vitro)
PMID:33137119	FYPO:0001266	normal protein phosphorylation during cellular response to salt stress [assayed_using] PomBase:SPCC24B10.07	(Fig. 3A) Gad8-K263C was also phosphorylated at S546 under conditions that compromise Tor1 activity, such as osmotic or low glucose stress (S3A Fig), further supporting Tor1-independent phosphorylation of Gad8-K263C by an as yet unknown kinase.
PMID:33137119	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPCC24B10.07	(Fig. 3A) To our surprise, Gad8-K263C was phosphorylated at S546 in wild type cells, as well as in Δtor1 cells (S546-P, Fig 3A).This finding suggests that the Gad8-K263C mutant is phosphorylated by a kinase that normally does not recognize Gad8 as a substrate.
PMID:33137119	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPBC16G5.15c	(Fig. 3A) affecting substrate Fkh2 in vitro
PMID:33137119	FYPO:0000674	normal cell population growth at high temperature	(Fig. 3B)
PMID:33137119	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPCC24B10.07	(Fig. 3C) The wild type Gad8 is not phosphorylated at T387 in the absence of Tor1 and is only weakly phosphorylated under low-glucose conditions (Fig 3C).
PMID:33137119	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPCC24B10.07	(Fig. 3C) we found that Gad8-K263C is phosphorylated at T387 in Δtor1 cells under normal or low-glucose growth conditions.
PMID:33137119	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPCC24B10.07	(Fig. 3C) we found that Gad8-K263C is phosphorylated at T387 in Δtor1 cells under normal or low-glucose growth conditions.
PMID:33137119	FYPO:0005947	normal growth on potassium chloride	(Fig. 3b)
PMID:33137119	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 3b)
PMID:33137119	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 6C,D)
PMID:33137119	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 6b)
PMID:33137119	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 6b)
PMID:33137119	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 6c) (comment: dominent negative effect)
PMID:33137119	FYPO:0002830	delayed onset of protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC1259.13	(Fig. 7B)
PMID:33137119	FYPO:0000271	sensitive to salt stress [has_severity] high	(Figure 3d)
PMID:33137119	FYPO:0000088	sensitive to hydroxyurea	(S5A Fig)
PMID:33137119	FYPO:0001021	normal growth during cellular response to osmotic stress	(comment: CHECK pREP81-gad8-K263C)
PMID:33137119	FYPO:0000674	normal cell population growth at high temperature	(comment: CHECK pREP81-gad8-K263C) Figure 2
PMID:33137119	FYPO:0004765	normal cell population growth during glucose starvation	(comment: CHECK pREP81-gad8-T260C) Figure 2
PMID:33137119	FYPO:0001021	normal growth during cellular response to osmotic stress	(comment: CHECK pREP81-gad8-T260C) fig 1a
PMID:33137119	FYPO:0000674	normal cell population growth at high temperature	(comment: CHECK pREP81-gad8-T260C) fig 1a
PMID:33137119	FYPO:0002680	increased protein phosphorylation [assayed_using] PomBase:SPCC1259.13 [has_severity] low	(comment: Following release from campthotecin)
PMID:33137119	FYPO:0002680	increased protein phosphorylation [assayed_substrate] PomBase:SPCC24B10.07	(comment: affecting Gad8-S546 phosphorylation)
PMID:33137119	FYPO:0002680	increased protein phosphorylation [assayed_substrate] PomBase:SPCC24B10.07	(comment: affecting Gad8-S546 phosphorylation)
PMID:33137119	FYPO:0002680	increased protein phosphorylation [assayed_substrate] PomBase:SPCC24B10.07	(comment: affecting Gad8-S546 phosphorylation)
PMID:33137119	FYPO:0002700	increased protein kinase activity [assayed_enzyme] PomBase:SPCC24B10.07 [assayed_substrate] PomBase:SPBC16G5.15c	(comment: affecting substrate Fkh2 in vitro)
PMID:33137119	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPCC24B10.07 [assayed_substrate] PomBase:SPBC16G5.15c	(comment: affecting substrate Fkh2 in vitro)
PMID:33137119	FYPO:0002700	increased protein kinase activity [assayed_enzyme] PomBase:SPCC24B10.07 [assayed_substrate] PomBase:SPBC16G5.15c	(comment: affecting substrate Fkh2 in vitro)
PMID:33137119	FYPO:0002700	increased protein kinase activity [assayed_enzyme] PomBase:SPCC24B10.07 [assayed_substrate] PomBase:SPBC16G5.15c	(comment: affecting substrate Fkh2 in vitro)
PMID:33137119	FYPO:0004765	normal cell population growth during glucose starvation	(comment: pREP81-gad8-K263C)
PMID:33137119	FYPO:0000708	decreased mating efficiency [has_severity] low	(comment: pREP81-gad8-K263C)
PMID:33137119	FYPO:0001032	resistance to camptothecin	(comment: pREP81-gad8-Q298L)
PMID:33137119	FYPO:0000708	decreased mating efficiency [has_severity] low	(comment: pREP81-gad8-Q298L) fig 5a
PMID:33137119	FYPO:0002578	resistance to hydroxyurea	(comment: pREP81-gad8-Q298L) fig6D
PMID:33137119	FYPO:0000708	decreased mating efficiency [has_severity] low	(comment: pREP81-gad8-T260C) fig 2B
PMID:33137119	FYPO:0000708	decreased mating efficiency [has_severity] medium	(comment: pREP81-gad8-T260C) fig 2B
PMID:33137119	FYPO:0000088	sensitive to hydroxyurea	Additionally, the phosphorylation sites of Gad8 are required for genotoxic stress, since gad8-S527A/S546A mutant alleles are also sensitive to DNA damage and DNA replication stress (S5B Fig).
PMID:33137119	FYPO:0000082	decreased cell population growth at high temperature	As previously described [33], mutating both Tor1-dependent phosphorylation sites, S546 and S527, to alanine, abolished the ability of cells to grow at high temperature or in the presence of osmotic stress (Fig 3B)
PMID:33137119	FYPO:0000088	sensitive to hydroxyurea	The only conditions under which we did not detect phosphorylation of Gad8-K263C were in Δtor1 cells in the presence of hydroxyurea or camptothecin (S3B Fig), a finding that may suggest that the activity of the kinase responsible for Gad8-K263C phosphorylation is inhibited under genotoxic stress conditions.
PMID:33138913	FYPO:0007448	normal reticulophagy during nitrogen starvation	(Figure 1)
PMID:33138913	FYPO:0007448	normal reticulophagy during nitrogen starvation	(Figure 1)
PMID:33138913	FYPO:0007594	abolished mitophagy during nitrogen starvation	(Figure 1)
PMID:33138913	FYPO:0007596	decreased mitophagy during nitrogen starvation	(Figure 1A)
PMID:33138913	FYPO:0007594	abolished mitophagy during nitrogen starvation	(Figure 1D)
PMID:33138913	FYPO:0000501	increased mitophagy [assayed_using] PomBase:SPAC14C4.01c	(Figure 2)
PMID:33138913	PomGeneEx:0000018	protein level increased [during] cellular response to nitrogen starvation	(Figure 2A)
PMID:33138913	GO:0005741	mitochondrial outer membrane	(Figure 2F, 2G, 2H)
PMID:33138913	FYPO:0003768	normal protein localization to mitochondrion	(Figure 3 Supp 1B&C)
PMID:33138913	FYPO:0007592	normal mitophagy during nitrogen starvation	(Figure 3B)
PMID:33138913	FYPO:0007594	abolished mitophagy during nitrogen starvation	(Figure 3B,4B)
PMID:33138913	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC14C4.01c [assayed_using] PomBase:SPBP8B7.24c	(Figure 3D)
PMID:33138913	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC14C4.01c [assayed_using] PomBase:SPBP8B7.24c	(Figure 3D)
PMID:33138913	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC14C4.01c [assayed_using] PomBase:SPBP8B7.24c	(Figure 3D)
PMID:33138913	FYPO:0007592	normal mitophagy during nitrogen starvation	(Figure 3H)
PMID:33138913	FYPO:0007592	normal mitophagy during nitrogen starvation	(Figure 3H)
PMID:33138913	FYPO:0007592	normal mitophagy during nitrogen starvation	(Figure 3H)
PMID:33138913	FYPO:0001357	normal vegetative cell population growth	(Figure 3I)
PMID:33138913	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Figure 3I)
PMID:33138913	FYPO:0003768	normal protein localization to mitochondrion [assayed_using] PomBase:SPAC14C4.01c	(Figure 3K)
PMID:33138913	FYPO:0007592	normal mitophagy during nitrogen starvation	(Figure 4B)
PMID:33138913	FYPO:0007596	decreased mitophagy during nitrogen starvation [assayed_using] PomBase:SPAC14C4.01c	(Figure 4B) Atg43 lacking the 20 C-terminal aa exhibited only a partial defect in mitophagy
PMID:33138913	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Figure 4C)
PMID:33138913	FYPO:0007601	decreased protein localization to mitochondrion, with diffuse cytoplasmic protein mislocalization [assayed_using] PomBase:SPAC14C4.01c	(Figure 4D)
PMID:33138913	FYPO:0003768	normal protein localization to mitochondrion [assayed_using] PomBase:SPAC14C4.01c	(Figure 4D)
PMID:33138913	FYPO:0003768	normal protein localization to mitochondrion [assayed_using] PomBase:SPAC14C4.01c	(Figure 4G)
PMID:33138913	FYPO:0001355	decreased vegetative cell population growth	(Figure 5, Figure supplement 1F)
PMID:33138913	FYPO:0001355	decreased vegetative cell population growth	(Figure 5, Figure supplement 1F)
PMID:33138913	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC14C4.01c [assayed_using] PomBase:SPBC409.23	(Figure 6B)
PMID:33138913	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC14C4.01c [assayed_using] PomBase:SPBC409.23	(Figure 6B)
PMID:33138913	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC14C4.01c [assayed_using] PomBase:SPBC409.23	(Figure 6B,D)
PMID:33138913	FYPO:0007594	abolished mitophagy during nitrogen starvation	(comment: CHECK check genotype******)Figure 3C
PMID:33138913	FYPO:0003768	normal protein localization to mitochondrion [assayed_using] PomBase:SPAC14C4.01c	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	FYPO:0003768	normal protein localization to mitochondrion [assayed_using] PomBase:SPBC409.23	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	FYPO:0003768	normal protein localization to mitochondrion [assayed_using] PomBase:SPAC6B12.12	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	FYPO:0003768	normal protein localization to mitochondrion [assayed_using] PomBase:SPBC713.08	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	FYPO:0003768	normal protein localization to mitochondrion [assayed_using] PomBase:SPBC713.08	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	FYPO:0003768	normal protein localization to mitochondrion [assayed_using] PomBase:SPBC409.23	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	FYPO:0003768	normal protein localization to mitochondrion [assayed_using] PomBase:SPAC14C4.01c	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	FYPO:0003768	normal protein localization to mitochondrion [assayed_using] PomBase:SPAC14C4.01c	Atg43 was observed on mitochondria in the absence of Tom70 (Figure 5E) and vice versa (Figure 5—Figure supplement 1I)
PMID:33138913	FYPO:0007602	decreased cellular superoxide level during nitrogen starvation	By contrast, the atg7D and atg43DAIM mutants did not exhibit such an increased in superoxide (Figure 7D)
PMID:33138913	FYPO:0007602	decreased cellular superoxide level during nitrogen starvation	By contrast, the atg7D and atg43DAIM mutants did not exhibit such an increased in superoxide (Figure 7D)
PMID:33138913	FYPO:0007596	decreased mitophagy during nitrogen starvation	Consistent with this, mitophagy was impaired in the mim1D and mim2D mutants (Figure 5D)
PMID:33138913	FYPO:0007596	decreased mitophagy during nitrogen starvation	Consistent with this, mitophagy was impaired in the mim1D and mim2D mutants (Figure 5D)
PMID:33138913	FYPO:0007038	decreased protein localization to mitochondrion [assayed_using] PomBase:SPAC14C4.01c	In the absence of Mim1 or Mim2, the GFP-Atg43 signal at the mitochondria was severely decreased (Figure 5C)
PMID:33138913	FYPO:0007038	decreased protein localization to mitochondrion [assayed_using] PomBase:SPAC14C4.01c	In the absence of Mim1 or Mim2, the GFP-Atg43 signal at the mitochondria was severely decreased (Figure 5C)
PMID:33138913	GO:0005515	protein binding [part_of] mitophagy	The interaction between full-length Atg43 and Mim2 was confirmed using reciprocal immunoprecipitation experiments (Figure 5A and Figure 5—Figure supplement 1B).
PMID:33138913	GO:0140580	mitochondrion autophagosome adaptor activity [has_input] PomBase:SPBP8B7.24c [part_of] mitophagy	Therefore, we propose that a major role of Atg43 in the mitophagy process is to tether Atg8 to mitochondria through direct interaction with Atg8 via the AIM region.
PMID:33138913	GO:0032977	membrane insertase activity [has_input] PomBase:SPAC6B12.12 [part_of] protein insertion into mitochondrial outer membrane	This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization.
PMID:33138913	GO:0032977	membrane insertase activity [has_input] PomBase:SPAC14C4.01c [part_of] protein insertion into mitochondrial outer membrane	This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization.
PMID:33138913	GO:0032977	membrane insertase activity [has_input] PomBase:SPAC14C4.01c [part_of] protein insertion into mitochondrial outer membrane	This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization.
PMID:33138913	GO:0032977	membrane insertase activity [has_input] PomBase:SPAC6B12.12 [part_of] protein insertion into mitochondrial outer membrane	This raises the possibility that the MIM complex assists Atg43 through facilitating its mitochondrial localization.
PMID:33138913	FYPO:0007038	decreased protein localization to mitochondrion [assayed_using] PomBase:SPAC6B12.12	We confirmed that Mim1 and Mim2 are required for stable localization of Tom70 on mitochondria in fission yeast (Figure 5—Figure supplement 1H
PMID:33138913	FYPO:0007038	decreased protein localization to mitochondrion [assayed_using] PomBase:SPAC6B12.12	We confirmed that Mim1 and Mim2 are required for stable localization of Tom70 on mitochondria in fission yeast (Figure 5—Figure supplement 1H
PMID:33138913	FYPO:0007594	abolished mitophagy during nitrogen starvation	whereas Atg43 with a truncation of the 60 C-terminal aa was defective in mitophagy (Figure 4B)
PMID:33153481	FYPO:0007517	increased chromatin mobility	(Fig. 2, S5) (comment: CHECK G2 arrested cells by cdc2-asM17)
PMID:33153481	FYPO:0001352	abnormal chromatin organization during vegetative growth	(Fig. 2,3, S4)(comment: CHECK Hi-C, G2 arrested cells by cdc2-asM17)
PMID:33153481	FYPO:0007516	decreased DNA volume	(Fig. 2a,d,e,f, S3, 3D) quantification of DAPI stained DNA, G2 arrested cells by cdc2-asM17, Shortened the distance between genomic loci
PMID:33153481	FYPO:0007519	normal DNA volume	(Fig. 2e) 3D quantification of DAPI stained DNA, G2 arrested cells by cdc2-asM17)
PMID:33153481	FYPO:0007328	normal number of Rad52 foci during vegetative growth	(Fig. 6b-d) (comment: CHECK Rad52 foci quantification, G2 arrested cells by cdc2-asM17, + Thiolutin)
PMID:33153481	FYPO:0007518	increased transcription-induced DNA damage	(Fig. 6b-d) Rad52 foci quantification, G2 arrested cells by cdc2-asM17, + Thiolutin
PMID:33153481	FYPO:0000972	increased number of Rad52 foci during vegetative growth	(Fig. 6b-d); (comment: CHECK Rad52 foci PMID:33153481, G2 arrested cells by cdc2-asM17)
PMID:33153481	FYPO:0001221	normal nucleus:cytoplasm ratio	(Fig. S2) (comment: CHECK -background? G2 arrested cells by cdc2-asM17)
PMID:33159083	GO:1990426	mitotic recombination-dependent replication fork processing	(comment: CHECK pmt3-D81R pmt3-KallR)
PMID:33159083	FYPO:0000204	abnormal mRNA export from nucleus [has_severity] low	(comment: same as nup132delta alone)
PMID:33172987	GO:0005546	phosphatidylinositol-4,5-bisphosphate binding	(Fig. 1D-E)
PMID:33172987	FYPO:0002126	abolished protein localization to plasma membrane during vegetative growth [assayed_using] PomBase:SPCPB16A4.02c	(Fig. 1F-G
PMID:33172987	FYPO:0002674	normal protein localization to plasma membrane [assayed_using] PomBase:SPAC19G12.14	(Fig. S2B)
PMID:33172987	FYPO:0007253	abolished membrane lipid binding [assayed_using] PomBase:SPCPB16A4.02c	(Figure 1C)
PMID:33172987	FYPO:0007528	normal membrane lipid binding [assayed_using] PomBase:SPCPB16A4.02c	(Figure 1C) (comment: CHECK requested normal membrane lipid binding)
PMID:33172987	GO:0005543	phospholipid binding	(Figure 3)
PMID:33172987	FYPO:0002674	normal protein localization to plasma membrane [assayed_using] PomBase:SPAC19G12.14	(Figure 3A)
PMID:33172987	FYPO:0000339	mislocalized septum during vegetative growth	(Figure 4E-F)
PMID:33172987	FYPO:0002126	abolished protein localization to plasma membrane during vegetative growth [assayed_using] PomBase:SPCPB16A4.02c	(Figure S1)
PMID:33172987	FYPO:0002126	abolished protein localization to plasma membrane during vegetative growth [assayed_using] PomBase:SPCPB16A4.02c	(Figure S1)
PMID:33172987	FYPO:0002126	abolished protein localization to plasma membrane during vegetative growth [assayed_using] PomBase:SPCPB16A4.02c	(Figure S1)
PMID:33172987	FYPO:0002126	abolished protein localization to plasma membrane during vegetative growth [assayed_using] PomBase:SPCPB16A4.02c	(Figure S1)
PMID:33172987	FYPO:0001357	normal vegetative cell population growth	(Figure S2)
PMID:33172987	FYPO:0001357	normal vegetative cell population growth	(Figure S2)
PMID:33172987	FYPO:0001357	normal vegetative cell population growth	(Figure S2)
PMID:33172987	FYPO:0001357	normal vegetative cell population growth	(Figure S2)
PMID:33172987	FYPO:0001357	normal vegetative cell population growth	(Figure S2)
PMID:33172987	FYPO:0001357	normal vegetative cell population growth	(Figure S2)
PMID:33172987	FYPO:0001357	normal vegetative cell population growth	(Figure S2)
PMID:33172987	FYPO:0001357	normal vegetative cell population growth	(Figure S2)
PMID:33172987	FYPO:0001357	normal vegetative cell population growth	(Figure S2)
PMID:33172987	FYPO:0001357	normal vegetative cell population growth	(Figure S2)
PMID:33172987	FYPO:0002674	normal protein localization to plasma membrane [assayed_using] PomBase:SPBC577.06c	(Figure S2)
PMID:33172987	FYPO:0001355	decreased vegetative cell population growth	(Figure S3)
PMID:33172987	FYPO:0001355	decreased vegetative cell population growth	(Figure S3)
PMID:33172987	FYPO:0002127	increased protein localization to plasma membrane during vegetative growth [assayed_using] PomBase:SPCPB16A4.02c	(Figure S3)
PMID:33172987	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(comment: CHECK THIS IS A GUESS I COULD NOT ACCESS THE SUPP SO ANNOTATED TO THE Snider ITS3-1 growth phenotype)
PMID:33172987	GO:0005543	phospholipid binding	(comment: Opy1 PH1 (aa1-128) can directly bind phospholipids in vitro) (Figure 1)
PMID:33172987	GO:0005515	protein binding	(comment: PH1 domain) Fig. 2A, Table S2
PMID:33176147	FYPO:0007544	normal cohesin complex binding	(Fig. 1E)
PMID:33176147	FYPO:0007544	normal cohesin complex binding	(Fig. 1E)
PMID:33176147	FYPO:0007544	normal cohesin complex binding	(Fig. 1E)
PMID:33176147	FYPO:0005018	decreased double-stranded DNA binding	(Fig. 1F)
PMID:33176147	FYPO:0005018	decreased double-stranded DNA binding	(Fig. 1F)
PMID:33176147	FYPO:0007543	abolished double-stranded DNA binding	(Fig. 1F)
PMID:33176147	FYPO:0007542	normal double-stranded DNA binding	(Fig. 1F,S2A)
PMID:33176147	FYPO:0001387	loss of viability at high temperature [has_severity] medium	(Fig. 2A)
PMID:33176147	FYPO:0001387	loss of viability at high temperature [has_severity] high	(Fig. 2A)
PMID:33176147	FYPO:0007542	normal double-stranded DNA binding	(Fig. S2A)
PMID:33176147	FYPO:0005555	decreased mitotic cohesin loading	(Figure 2c,3B and S3B Figures 4C and 4D)
PMID:33176147	FYPO:0005555	decreased mitotic cohesin loading	(Figure 2c,3B and S3B Figures 4C and 4D)
PMID:33176147	FYPO:0005555	decreased mitotic cohesin loading [has_penetrance] medium	(Figures 4E and 4F)
PMID:33176147	FYPO:0005555	decreased mitotic cohesin loading [has_penetrance] medium	(Figures 4E and 4F)
PMID:33176147	FYPO:0005555	decreased mitotic cohesin loading [has_penetrance] medium [has_severity] high	(Figures 4E and 4F)
PMID:33202882	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPAC1610.03c	(comment: intron 2)
PMID:33225241	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: same as mas5delta alone)
PMID:33225241	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: same as mas5delta alone)
PMID:33357436	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPAC1F5.04c [assayed_using] PomBase:SPAC20G8.05c	(Fig. 2B) (comment: in vitro binding assay with Cdc15 F-BAR domain and Cdc12 peptide aa20-40)
PMID:33357436	FYPO:0005467	decreased protein localization to actomyosin contractile ring during mitosis [assayed_using] PomBase:SPAC1F5.04c	(Figure 3A)
PMID:33357436	GO:0004721	phosphoprotein phosphatase activity [has_input] PomBase:SPAC20G8.05c [part_of] positive regulation of cytokinesis, actomyosin contractile ring assembly	(Figure 4F)
PMID:33357436	FYPO:0005221	normal protein oligomerization	(Figure S2B) of purified Cdc15 F-BAR domain
PMID:33357436	FYPO:0007528	normal membrane lipid binding	(Figure S2C)
PMID:33357436	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_using] PomBase:SPAC20G8.05c	(Figure S2E)
PMID:33357436	FYPO:0001365	decreased rate of actomyosin contractile ring contraction	(Figures 3C, 3D)
PMID:33357436	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC4F6.12 [assayed_using] PomBase:SPAC20G8.05c	(comment: In vitro binding assay with Cdc15 F-BAR domain and full length Pxl1)
PMID:33357436	FYPO:0004594	branched, elongated, septated cell	(comment: additional cewlll. poles)
PMID:33357436	FYPO:0005289	actomyosin contractile ring sliding [has_penetrance] 51	(comment: moved down from abnormal localization)
PMID:33357436	GO:0106006	cytoskeletal protein-membrane anchor activity [has_input] PomBase:SPAC1F5.04c [part_of] mitotic actomyosin contractile ring assembly [happens_during] mitotic M phase [occurs_in] medial cortex	These results indicate that the Cdc15 F-BAR domain can position Cdc12 directly at the PM by binding membrane and Cdc12 simultaneously.
PMID:33378674	GO:0006335	DNA replication-dependent chromatin assembly	(comment: at pericentromeric regions)
PMID:33378677	FYPO:0007884	abolished Lsm2-8 complex binding [assayed_protein] PomBase:SPAC17G6.17 [assayed_protein] PomBase:SPCC1840.10	(comment: inferred from abolished interaction between Pof8 and Lsm subunits)
PMID:33378677	FYPO:0007885	decreased Lsm2-8 complex binding [assayed_protein] PomBase:SPCC1840.10 [assayed_protein] PomBase:SPAC17G6.17	(comment: inferred from abolished interaction between Pof8 and Lsm subunits)
PMID:33378677	FYPO:0007884	abolished Lsm2-8 complex binding [assayed_protein] PomBase:SPCC1840.10 [assayed_protein] PomBase:SPAC17G6.17	(comment: inferred from abolished interaction between Pof8 and Lsm subunits)
PMID:33400299	GO:0005829	cytosol [exists_during] cellular response to glucose stimulus	(Fig. 3a) glucose r excess
PMID:33400299	GO:0005634	nucleus [exists_during] cellular response to glucose starvation	(Fig. 3a) glucose starve
PMID:33400299	GO:0005634	nucleus [exists_during] cellular response to nitric oxide	(Fig. 3a) glucose starve
PMID:33400299	FYPO:0007612	increased transcription from STREP promoter [assayed_using] PomBase:SPAC6F12.02	(Figure 1m)
PMID:33400299	FYPO:0007613	decreased transcription from STREP promoter [assayed_using] PomBase:SPAC6F12.02	(Figure 1m)
PMID:33400299	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [happens_during] cellular response to nitric oxide	(Figure 2k-m).
PMID:33400299	FYPO:0007615	increased transcription from STREP promoter during cellular response to nitric oxide [assayed_using] PomBase:SPAC6F12.02 [has_severity] high	(Figure 2n)
PMID:33400299	FYPO:0007615	increased transcription from STREP promoter during cellular response to nitric oxide [assayed_using] PomBase:SPAC6F12.02 [has_severity] medium	(Figure 2n)
PMID:33400299	FYPO:0007615	increased transcription from STREP promoter during cellular response to nitric oxide [assayed_using] PomBase:SPAC6F12.02 [has_severity] medium	(Figure 2n)
PMID:33400299	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 4b)
PMID:33400299	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 4b)
PMID:33400299	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 4b)
PMID:33400299	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 4b)
PMID:33400299	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 4b)
PMID:33400299	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 4b)
PMID:33400299	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 4b)
PMID:33400299	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 4b)
PMID:33400299	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 4b)
PMID:33400299	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 4b)
PMID:33400299	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 4b)
PMID:33400299	FYPO:0006141	abolished cell population growth on gluconate carbon source	(Figure 4b)
PMID:33400299	FYPO:0000440	sensitive to antimycin A	Table1
PMID:33400299	FYPO:0000440	sensitive to antimycin A	Table1
PMID:33400299	FYPO:0007617	sensitive to sodium azide	Table1
PMID:33400299	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [happens_during] response to reactive oxygen species	To further examine whether ROS and NO mediated increased Rst2 transcriptional activity caused by mitochondrial complex III/IV inhibitors, we examined the effect of antioxidant N-acetyl-L-cysteine (NAC) which aids in ROS detoxification and 2-(4-Carboxyphenyl)-4,4,5,5-tetramethy-limidazo-line-1-oxyl-3- oxide (Carboxy-PTIO), a NO-specific scavenger on the Rst2 transcriptional activity stimulated by mitochondrial complex III/IV inhibitors. The results showed that NAC and Carboxy-PTIO significantly inhibited mitochondrial complex III/IV inhibitors-induced activation of Rst2 in a dose-dependent manner (Figure 2e-j) suggesting that ROS and NO were involved in mitochondrial respiratory chain complex III/IV inhibitors-induced activation of Rst2. To further prove this result, we also examined the effect of a mammalian NO synthesis (NOS) inhibitor, N G-nitro-l-arginine methyl ester (NAME) on the Rst2 transcriptional activity stimulated by mitochondrial complex III/IV inhibitors, since it was reported that NAME treatment can reduce NO formation by more than 60% in yeast cells (Astuti et al., 2016a). As expected, NAME dose-dependently decreased mitochondrial complex III/IV inhibitors- induced Rst2 activation (Figure 2k-m).
PMID:33400299	FYPO:0007612	increased transcription from STREP promoter [assayed_using] PomBase:SPAC6F12.02	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	FYPO:0007612	increased transcription from STREP promoter [assayed_using] PomBase:SPAC6F12.02	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	FYPO:0007612	increased transcription from STREP promoter [assayed_using] PomBase:SPAC6F12.02	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	FYPO:0007612	increased transcription from STREP promoter [assayed_using] PomBase:SPAC6F12.02	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	FYPO:0007612	increased transcription from STREP promoter [assayed_using] PomBase:SPAC6F12.02	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	FYPO:0007612	increased transcription from STREP promoter [assayed_using] PomBase:SPAC6F12.02	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	FYPO:0007612	increased transcription from STREP promoter [assayed_using] PomBase:SPAC6F12.02	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	FYPO:0007612	increased transcription from STREP promoter [assayed_using] PomBase:SPAC6F12.02	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	FYPO:0007612	increased transcription from STREP promoter [assayed_using] PomBase:SPAC6F12.02	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	FYPO:0007612	increased transcription from STREP promoter [assayed_using] PomBase:SPAC6F12.02	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33400299	FYPO:0007612	increased transcription from STREP promoter [assayed_using] PomBase:SPAC6F12.02	transcriptional activity was dramatically increased in these 11 mitochondrial mutant strains (Figure 1i,j).
PMID:33410907	FYPO:0004333	increased protein phosphorylation during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC24B11.06c	(Fig. 2a)
PMID:33410907	PomGeneEx:0000011	RNA level increased [during] cellular response to hydroperoxide	(Figure 1)
PMID:33410907	PomGeneEx:0000011	RNA level increased [during] cellular response to hydroperoxide	(Figure 1)
PMID:33410907	PomGeneEx:0000011	RNA level increased [during] cellular response to hydroperoxide	(Figure 1)
PMID:33410907	FYPO:0000087	sensitive to hydrogen peroxide	(Figure 1)
PMID:33410907	FYPO:0006819	normal vegetative cell growth rate	(Figure 1)
PMID:33410907	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPCC757.07c	(Figure 1C)
PMID:33410907	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAP8A3.04c	(Figure 1C)
PMID:33410907	FYPO:0001116	decreased RNA level during cellular response to hydrogen peroxide [assayed_using] PomBase:SPBC215.05	(Figure 1C)
PMID:33410907	GO:0000785	chromatin [coincident_with] PomBase:SPCC757.07c [exists_during] cellular response to oxidative stress	(Figure 2B)
PMID:33410907	GO:0000785	chromatin [coincident_with] PomBase:SPAP8A3.04c [exists_during] cellular response to oxidative stress	(Figure 2B)
PMID:33410907	GO:0000785	chromatin [coincident_with] PomBase:SPBC215.05 [exists_during] cellular response to oxidative stress	(Figure 2B)
PMID:33410907	FYPO:0007619	normal protein localization to chromatin during cellular response to oxidative stress [assayed_using] PomBase:SPBC29B5.01	(Figure 2c) (comment: CHECK this replaces the sty1 WT annotation Should this be normal? i.e. normal for the conditions? )
PMID:33410907	FYPO:0007619	normal protein localization to chromatin during cellular response to oxidative stress [assayed_using] PomBase:SPAC24B11.06c	(Figure 2c) (comment: CHECK this replaces the sty1 WT annotation Should this be normal? i.e. normal for the conditions? )
PMID:33410907	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC24B11.06c	(Figure 4) (comment: Sty1 interacted and phosphorylated Rpb1-CTD at Ser5)
PMID:33410907	MOD:00046	O-phospho-L-serine [removed_by] PomBase:SPAC3G9.04	(Figure 4) (comment: Sty1 interacted and phosphorylated Rpb1-CTD at Ser5)
PMID:33410907	GO:0008353	RNA polymerase II CTD heptapeptide repeat kinase activity [has_input] PomBase:SPBC28F2.12	(Figure 4) (comment: Sty1 interacted and phosphorylated Rpb1-CTD at Ser5)
PMID:33410907	FYPO:0000087	sensitive to hydrogen peroxide	(Figure 5)
PMID:33410907	FYPO:0001103	resistance to hydrogen peroxide	(Figure 5)
PMID:33410907	GO:0005515	protein binding [part_of] cellular response to oxidative stress [part_of] positive regulation of transcription initiation by RNA polymerase II [happens_during] cellular response to oxidative stress	(Figure 5D)
PMID:33410907	FYPO:0005889	sensitive to sodium chloride	(Figure 5e)
PMID:33410907	GO:0180007	RNA polymerase II CTD heptapeptide repeat S5 phosphatase activity [has_input] PomBase:SPBC28F2.12	(Figure 6c) (comment: The anti-myc, anti-Rpb1 CTD (8WG16) and anti-pS5-Rpb1 CTD (H14) antibodies were used for immunoprecipitation.)
PMID:33410907	FYPO:0003004	increased cellular reactive oxygen species level during vegetative growth	(comment: CHECK is this +H2o2) the intracellular level of ROS was elevated in pin1 and ssu72 mutants (Figure 6H)
PMID:33410907	FYPO:0003004	increased cellular reactive oxygen species level during vegetative growth	(comment: CHECK is this +h2o2) the intracellular level of ROS was elevated in pin1 and ssu72 mutants (Figure 6H)
PMID:33410907	GO:0000785	chromatin [exists_during] cellular response to oxidative stress [coincident_with] PomBase:SPBC215.05	As shown in Figure 3C and D, upon H2O2 stress, Rpb1 was recruited to the promoter and extensively phosphorylated at Ser5.
PMID:33410907	GO:0000785	chromatin [coincident_with] PomBase:SPAP8A3.04c [exists_during] cellular response to oxidative stress	As shown in Figure 3C and D, upon H2O2 stress, Rpb1 was recruited to the promoter and extensively phosphorylated at Ser5.
PMID:33410907	FYPO:0007620	decreased protein phosphorylation during cellular response to oxidative stress [assayed_using] PomBase:SPBC28F2.12	In line with these results, Ser2 phosphorylation of Rpb1-CTD, which facilitated transcription elongation, was reduced in pin1 mutant as a secondary effect derived from defect in transcription initiation to elongation (Figure 3A and B).
PMID:33410907	GO:0060261	positive regulation of transcription initiation by RNA polymerase II [occurs_at] STREP_motif [happens_during] cellular response to oxidative stress	In line with these results, Ser2 phosphorylation of Rpb1-CTD, which facilitated transcription elongation, was reduced in pin1 mutant as a secondary effect derived from defect in transcription initiation to elongation (Figure 3A and B).
PMID:33410907	FYPO:0007619	normal protein localization to chromatin during cellular response to oxidative stress [assayed_using] PomBase:SPBC28F2.12	In the absence of Pin1, Ser5 phosphorylated Rpb1 was associated and accumulated at the promoter region following H2O2 stress but was defective in entering elongation to generate transcripts of the corresponding genes (Figure 1C)
PMID:33410907	FYPO:0007621	increased protein-protein interaction during cellular response to oxidative stress [assayed_using] PomBase:SPBC28F2.12 [assayed_using] PomBase:SPAC24B11.06c	Intriguingly, upon oxidative stress, the association between Rpb1 and Sty1 was decreased in wild type cells and up regulated in the pin1 mutant with reduced phosphorylation of Ser2 (Figure 4B).
PMID:33410907	GO:0140463	chromatin-protein adaptor activity [part_of] positive regulation of transcription initiation by RNA polymerase II [happens_during] cellular response to oxidative stress	Ssu72, but not with the GST control in the pull down experiment. These results suggested that Pin1 directly interacted with and recruited Ssu72 for pSer5 dephosphorylation to facilitate progression of transcription important for cellular response to oxidative stress
PMID:33410907	GO:0003755	peptidyl-prolyl cis-trans isomerase activity [part_of] positive regulation of transcription initiation by RNA polymerase II [happens_during] cellular response to oxidative stress	These results suggested that, in addition to the binding to theRpb1-CTD, the isomerization activity was also required for the fu
PMID:33410907	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPBC28F2.12 [assayed_using] PomBase:SPCC16C4.03	fig? (comment: under calf alkaline phosphatase treated)
PMID:33419777	FYPO:0007474	variable cell size at division	(Fig S1) delayed septation, Cellular phenotype where cells initiate growth before septation has taken place, resulting in variable cell size at division.
PMID:33419777	FYPO:0000118	multiseptate vegetative cell [has_penetrance] medium	(Fig. 1A)
PMID:33419777	FYPO:0007474	variable cell size at division	(Fig. 1B, C Table 1)
PMID:33419777	FYPO:0007474	variable cell size at division	(Fig. 1B, C Table 1)
PMID:33419777	FYPO:0007474	variable cell size at division	(Fig. 1B, C Table 1)
PMID:33419777	FYPO:0007474	variable cell size at division	(Fig. 1B, C Table 1)
PMID:33419777	FYPO:0007474	variable cell size at division	(Fig. 1B, C Table 1)
PMID:33419777	FYPO:0007660	variable cell size at division with subsequent division at abnormal size	(Fig. 2, Table 2)
PMID:33419777	FYPO:0007660	variable cell size at division with subsequent division at abnormal size	(Fig. 2, Table 2)
PMID:33419777	FYPO:0007660	variable cell size at division with subsequent division at abnormal size	(Fig. 3A-F) (comment: same result in Wild type background)
PMID:33419777	FYPO:0007660	variable cell size at division with subsequent division at abnormal size	(Fig. 3A-F) (comment: same result in wild type background)
PMID:33419777	FYPO:0007474	variable cell size at division	(Fig. 3H) (comment: same in wild type background)
PMID:33419777	FYPO:0007474	variable cell size at division	(Fig. 3I) (comment: same in wild type background)
PMID:33419777	FYPO:0003751	normal nuclear envelope morphology [has_penetrance] high	(Fig. 4A)
PMID:33419777	FYPO:0001556	excess nuclear envelope present [has_penetrance] high	(Fig. 4A)
PMID:33419777	FYPO:0000133	elongated multinucleate vegetative cell [has_penetrance] medium	(Fig. 4B,C,D) A cellular phenotype found in multinucleated cells where nuclear division is no longer synchronous and cells with an odd number of nuclei are observed
PMID:33419777	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC582.03	(Fig. 5A)
PMID:33419777	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC11B10.09	(Fig. 5A)
PMID:33419777	FYPO:0004422	normal protein phosphorylation [assayed_using] PomBase:SPBC11B10.09	(Fig. 5A)
PMID:33419777	FYPO:0007474	variable cell size at division	(Fig. 5C Table 3)
PMID:33419777	FYPO:0007474	variable cell size at division [has_severity] high	(Fig. 5C) compare 4 and 6 the variability of cdc2cdc13 fusion protein is increased in mga2 delta. I don't quite know how to annotate this or whether I leave it as 'variable size at division and do a genetic interaction and Im not sure that the term I have suggested is right
PMID:33419777	FYPO:0007474	variable cell size at division [has_severity] high	(Fig. 5C) compare 7 and 9 When cdc2 is not tyrosine phosphorylation mga2 delta does not increase the cell size variability any further.
PMID:33419777	FYPO:0007474	variable cell size at division [has_severity] high	(Fig. 5C) compare16 and 17 Table 3 I don't quite know how to annotate this or whether I leave it as 'variable size at division and do a genetic interaction and Im not sure that the term I have suggested is right
PMID:33419777	FYPO:0000443	abnormal protein localization during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 5E,F) abnormal protein localisation in multinucleated cells
PMID:33419777	FYPO:0007474	variable cell size at division [has_severity] high	cellular phenotype of variable cell size at division may be further increased in the absence of another cellular protein Fig5 compare 14 and 15 Table 3 I don't quite know how to annotate this or whether I leave it as 'variable size at division and do a genetic interaction and Im not sure that the term I have suggested is right
PMID:33434270	FYPO:0007517	increased chromatin mobility [assayed_using] chromosome_arm	(Figure 5A)
PMID:33434270	FYPO:0007638	decreased anisotropic motion of mitotic chromatin [assayed_using] chromosome_arm	(Figure 6A)
PMID:33437930	FYPO:0000726	sensitive to oxidative stress	The spotting assay revealed the enhanced pyrogallol sensitivity of wat1/pop3 delete cells as compared to wild type cells (Fig. 1A)
PMID:33468217	GO:0031445	regulation of heterochromatin formation	(comment: inferred from silencing and H3-K9 methylation phenotypes)
PMID:33483504	FYPO:0000895	mitochondrial aggregation	(Fig. 1) (comment: cox4-GFP to label Mt)
PMID:33483504	FYPO:0007611	small fragmented mitochondria present in decreased numbers	(Fig. 1a)
PMID:33483504	FYPO:0001234	slow vegetative cell population growth	(Fig. 1b) (comment: n=344)
PMID:33483504	FYPO:0007712	mitochondria absent from cell [has_penetrance] 19.2	(Fig. 1b) (comment: n=344)
PMID:33483504	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 1c)
PMID:33483504	FYPO:0000906	abnormal mitochondrion inheritance during vegetative growth [has_severity] high	(Fig. 1d) Despite the multiple types of abnormalities observed in emr1Δ cells, mitochondria of emr1Δ cells were still able to undergo fission and fusion (Fig. 1d), but improperly segregated into daughter cells after mitosis (Fig. 1e). This phenotype of defective mitochondrial segregation is consistent with the previous finding that spherical/giant mitochondria in mutant cells compromise mitochondrial movements, inheritance, and segregation7,8,2
PMID:33483504	FYPO:0007611	small fragmented mitochondria present in decreased numbers	(Fig. 3b)
PMID:33483504	FYPO:0001234	slow vegetative cell population growth	(Fig. 3d)
PMID:33483504	FYPO:0007713	large ERMES foci present in decreased numbers [assayed_using] PomBase:SPBC28F2.06c	(Fig. 4) significantly decreased the number of Mdm12 (a constitutive component of the ERMES complex) foci
PMID:33483504	FYPO:0007724	normal ERMES foci [assayed_using] PomBase:SPBC28F2.06c	(Fig. 4d) (comment: though the expression levels of Mdm12 were comparable in WT and emr1Δ Cells)
PMID:33483504	FYPO:0007713	large ERMES foci present in decreased numbers [assayed_using] PomBase:SPBC27B12.01c	(Fig. 5)
PMID:33483504	FYPO:0003768	normal protein localization to mitochondrion [assayed_using] PomBase:SPAC8C9.19	(Figure 3a)
PMID:33483504	FYPO:0003768	normal protein localization to mitochondrion [assayed_using] PomBase:SPAC8C9.19	(Figure 3a)
PMID:33483504	FYPO:0003896	normal mitochondrial morphology [assayed_using] PomBase:SPAC8C9.19	(Figure 3b)
PMID:33483504	GO:0120010	intermembrane phospholipid transfer	(comment: er to mitochondria)
PMID:33483504	GO:0032473	cytoplasmic side of mitochondrial outer membrane	(comment: integral) Fig. 2a, 2b, 2c, 2d
PMID:33483504	FYPO:0007713	large ERMES foci present in decreased numbers [assayed_using] PomBase:SPBC28F2.06c	As shown in Fig. 6b, c, Emr1-FL and Emr1-ΔN, but not Emr1-ΔC, restored the normal number of Mdm12 foci, confirming that the C-terminus of Emr1 is required for regulating the number of ERMES foci.
PMID:33496728	FYPO:0007831	narrow protein radial density distribution in medial cortical node during mitotic anaphase B [assayed_protein] PomBase:SPAC1F5.04c	(Fig. 4 C). Cdc12p distributed in a smaller zone in the R-nodes of Δmid1 cells...node dimensions in the R-nodes of constricting contractile rings.....
PMID:33496728	FYPO:0001365	decreased rate of actomyosin contractile ring contraction [has_penetrance] high [has_severity] high	(Figure 1)
PMID:33496728	FYPO:0001365	decreased rate of actomyosin contractile ring contraction [has_penetrance] high	(Figure 1)
PMID:33496728	FYPO:0000161	abnormal actomyosin contractile ring assembly	(Figure 1A, B)
PMID:33496728	FYPO:0006897	increased rate of actomyosin contractile ring contraction [has_penetrance] high	(Figure 1E, F)
PMID:33496728	FYPO:0001365	decreased rate of actomyosin contractile ring contraction [has_penetrance] high	(Figure 1E, F) We generated Δmid1 Δmyp2 double-mutant cells and found that the distribution of constriction rates of their contractile rings is still bimodal, albeit with both populations constricting 25-50% more slowly than the Δmid1 populations, consistent with Myp2p being responsible for ∼50% of the constriction rate
PMID:33496728	FYPO:0001365	decreased rate of actomyosin contractile ring contraction [has_penetrance] low	(Figure 1E,F) (comment: VW instead of abnormal, I did increased and decreased rate with low penetrance i.e the rate is variable within the population someincreased and some decrreased, although there see to be 2 distinct sub-populations we can't capture this effectively)
PMID:33496728	FYPO:0006897	increased rate of actomyosin contractile ring contraction [has_penetrance] low	(Figure 1E,F) The average constriction rate of Δmid1 contractile rings is 0.27 μm/min (Saha and Pollard, 2012a), but the distribution of constriction rates appears bimodal with fast and slow subpopulations. The type of strand that builds the contractile ring strongly correlates with its constriction rate, with contractile rings made from nascent strands constricting faster (0.32 μm/min) and contractile rings made from enduring strands constricting more slowly (0.20 μm/min; Fig. 1 E).
PMID:33496728	FYPO:0002999	normal protein localization to medial cortical node [has_penetrance] 100 [assayed_protein] PomBase:SPCC645.05c	(Figure 2) (Figure 3) (Figure 4) (Figure S2)
PMID:33496728	FYPO:0007830	narrow protein radial density distribution in medial cortical node during mitotic interphase	(Figure 3) (Figure 4) (Figure S2)
PMID:33496728	FYPO:0003946	delayed onset of protein localization to cell division site	(Figure 5)
PMID:33496728	FYPO:0003946	delayed onset of protein localization to cell division site [has_penetrance] high [assayed_protein] PomBase:SPAC4F8.13c	(Figure 5)
PMID:33496728	FYPO:0007832	delayed onset of protein localization to medial cortical node	(Figure 5)
PMID:33496728	FYPO:0000161	abnormal actomyosin contractile ring assembly	(Figure 5) (comment: vw: changed severity from high to low as this seems to partially rescue mid1-delta?)
PMID:33496728	FYPO:0000161	abnormal actomyosin contractile ring assembly	(Figure 6)
PMID:33496728	FYPO:0000161	abnormal actomyosin contractile ring assembly	(Figure S1)
PMID:33496728	FYPO:0001368	normal actomyosin contractile ring assembly	(Figure S1)
PMID:33496728	FYPO:0000161	abnormal actomyosin contractile ring assembly	(Figure S1)
PMID:33496728	FYPO:0001364	abnormal actomyosin contractile ring contraction	(Figure S1)
PMID:33496728	FYPO:0003946	delayed onset of protein localization to cell division site	(Figure S3)
PMID:33496728	FYPO:0003946	delayed onset of protein localization to cell division site	(Figure S3)
PMID:33496728	FYPO:0003946	delayed onset of protein localization to cell division site	(Figure S3)
PMID:33496728	FYPO:0003946	delayed onset of protein localization to cell division site [has_penetrance] high [assayed_protein] PomBase:SPCC645.05c	(Figures 1,5) +5 min, a 15-min delay compared with wild-type cells
PMID:33506191	FYPO:0006339	mononucleate vegetative cell with mislocalized nucleus [has_penetrance] 60-70	(Fig. 1)
PMID:33506191	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 30-40	(Fig. 1)
PMID:33506191	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 30-40	(Fig. 1)
PMID:33506191	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 30-40	(Fig. 1)
PMID:33506191	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 30-40	(Fig. 1)
PMID:33506191	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 30-40	(Fig. 1)
PMID:33506191	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 30-40	(Fig. 1)
PMID:33506191	FYPO:0006339	mononucleate vegetative cell with mislocalized nucleus [has_penetrance] 60-70	(Fig. 1)
PMID:33506191	FYPO:0006339	mononucleate vegetative cell with mislocalized nucleus [has_penetrance] 60-70	(Fig. 1)
PMID:33506191	FYPO:0006339	mononucleate vegetative cell with mislocalized nucleus [has_penetrance] 60-70	(Fig. 1)
PMID:33506191	FYPO:0006339	mononucleate vegetative cell with mislocalized nucleus [has_penetrance] 60-70	(Fig. 1)
PMID:33506191	FYPO:0006339	mononucleate vegetative cell with mislocalized nucleus [has_penetrance] 60-70	(Fig. 1)
PMID:33506191	FYPO:0006339	mononucleate vegetative cell with mislocalized nucleus [has_penetrance] 60-70	(Fig. 1)
PMID:33506191	FYPO:0006339	mononucleate vegetative cell with mislocalized nucleus [has_penetrance] 47.5	(Fig. 2) (comment: live cell imaging)
PMID:33506191	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] 52.5	(Fig. 2) (comment: live cell imaging)
PMID:33506191	FYPO:0007966	abolished nuclear displacement from cell division site after abolished mitotic sister chromatid separation [has_penetrance] >95	(Fig. 4)
PMID:33506191	FYPO:0007966	abolished nuclear displacement from cell division site after abolished mitotic sister chromatid separation [has_penetrance] >95	(Fig. 4)
PMID:33506191	FYPO:0007966	abolished nuclear displacement from cell division site after abolished mitotic sister chromatid separation [has_penetrance] >95	"(Fig. 4) (comment: If possible, please add the following comment - “The nucleus is retained in the center of the cell during mitosis."")"
PMID:33506191	FYPO:0007966	abolished nuclear displacement from cell division site after abolished mitotic sister chromatid separation [has_penetrance] >95	(Fig. 6)
PMID:33506191	FYPO:0000252	increased spontaneous diploidization [has_penetrance] ~25	(Fig. 7)
PMID:33506191	FYPO:0000252	increased spontaneous diploidization [has_penetrance] ~10	(Fig. 7) These results indicate that first, the main reason for lethality of cut7 is derived from the cut phenotype; second, some cells could escape from cut by displacing the nucleus from the middle of the cell axis; and finally, these cut7 survivors could resume cell division as diploid progenies at the permissive temperature.
PMID:33511417	FYPO:0000674	normal cell population growth at high temperature	(Fig. 5)
PMID:33511417	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 5)
PMID:33511417	FYPO:0000674	normal cell population growth at high temperature	(Fig. 5)
PMID:33511417	FYPO:0004491	decreased nucleosome occupancy	(comment: genome-wide average)
PMID:33511417	FYPO:0007656	increased nucleosome occupancy at transcription start site	(comment: genome-wide average; slightly increased amplitudes of the -2, -1, +1 nucleosome peaks relative to NDR)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPAC25G10.04c	(Figure 2)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPAC25G10.04c	(Figure 2)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPAC17A5.18c	(Figure 2)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPBC36B7.06c	(Figure 2)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPBC577.05c	(Figure 2)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPAC17A5.18c	(Figure 2)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPAC17A5.18c	(Figure 2)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPAC17A5.18c	(Figure 2)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPAC17A5.18c	(Figure 2)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPAC17A5.18c	(Figure 2)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPAC25G10.04c	(Figure 2)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPAC25G10.04c	(Figure 2)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPAC25G10.04c	(Figure 2)
PMID:33526714	FYPO:0007146	abolished protein localization to nucleus, with protein mislocalized to cytoplasm, during meiotic cell cycle [assayed_protein] PomBase:SPAC25G10.04c	(Figure 2)
PMID:33529549	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 34-40	(Figure 1) Decreased equational segregation in the sgo1∆ rec12∆ background or the haploid sgo1∆ background.
PMID:33529549	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] ~65	(Figure 1) Increased equational segregation in sgo1∆ background.
PMID:33529549	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 2-4	(Figure 1) Increased equational segregation in sgo1∆ background.
PMID:33529549	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] ~25	(Figure 1) Increased equational segregation in the sgo1∆ background.
PMID:33529549	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 9-12	(Figure 1) These results indicate that the error correction mechanism decreases bi-oriented attachment of sister chromatids in the presence of chiasmata, but conversely increases bi-oriented attachment (thereby decreasing mono-oriented attachment) in the absence of chiasmata. In our previous study, the equational segregation frequencies of cen1 were somewhat higher in the rec12Δ background [28], although the reason for this is unknown. However, the mad2Δ mutation similarly decreased equational segregation, being consistent with our current results.
PMID:33529549	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I	***** increased bi-oriented attachment of sister chromatids in meiosis I*****The frequencies of sister centromere splitting varied (electronic supplementary material, Figure S2A), but the mean splitting frequencies per centromere obtained by the bootstrap method were significantly higher in rec12Δ cells than in rec12+ cells (the difference was also significant in the usual t-test, p < 0.01; Figure 2d, +). The elevated frequency of sister centromere splitting in chiasma-lacking cells confirms that chiasmata prevent bi-oriented attachment of sister chromatids.
PMID:33529549	FYPO:0008099	abolished homologous chromosome movement at anaphase A	Anaphase A chromosome movement is completely abolished and only anaphase B chromosome movement occurs.
PMID:33529549	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] ~18	Decreased equational segregation in the diploid sgo1∆ rec12∆ background or the haploid sgo1∆ background.
PMID:33529549	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] ~12	Furthermore, the dam1Δ mutation increased equational segregation of sister chromatids in rec12+ cells (Figure 5b, left) but it decreased equational segregation in sgo1Δ rec12Δ or haploid meiotic sgo1Δ cells (Figure 5b,c)
PMID:33529549	FYPO:0000678	unequal homologous chromosome segregation [has_severity] low	Importantly, the dam1Δ mutation impaired disjunction of homologous chromosomes (Figure 5a), as seen in mad2Δ and ark1-so mutants [25,52].
PMID:33529549	GO:0031619	homologous chromosome orientation in meiotic metaphase I	The elevated frequency of sister centromere splitting in chiasma-lacking cells confirms that chiasmata prevent bi-oriented attachment of sister chromatids.
PMID:33533152	FYPO:0007220	normal histone H3-K9 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPAC821.09	(Fig. 10A)
PMID:33533152	FYPO:0007217	decreased histone H3-K9 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPAPJ760.03c [has_severity] high	(Fig. 10A)
PMID:33533152	FYPO:0007217	decreased histone H3-K9 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPAC821.09 [has_severity] high	(Fig. 10A)
PMID:33533152	FYPO:0007220	normal histone H3-K9 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPAPJ760.03c	(Fig. 10A)
PMID:33533152	FYPO:0007220	normal histone H3-K9 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPAPJ760.03c	(Fig. 10A)
PMID:33533152	FYPO:0007220	normal histone H3-K9 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPAC821.09	(Fig. 10A)
PMID:33533152	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 10B)
PMID:33533152	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 10B)
PMID:33533152	FYPO:0001689	normal growth on 4-nitroquinoline N-oxide	(Fig. 10B)
PMID:33533152	FYPO:0001689	normal growth on 4-nitroquinoline N-oxide	(Fig. 10B)
PMID:33533152	FYPO:0000969	normal growth during cellular response to UV	(Fig. 10B)
PMID:33533152	FYPO:0000969	normal growth during cellular response to UV	(Fig. 10B)
PMID:33533152	FYPO:0007217	decreased histone H3-K9 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPAC821.09 [has_severity] high	(Fig. 10C)
PMID:33533152	FYPO:0007217	decreased histone H3-K9 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPAPJ760.03c [has_severity] high	(Fig. 10C)
PMID:33533152	FYPO:0007220	normal histone H3-K9 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPAPJ760.03c	(Fig. 10C)
PMID:33533152	FYPO:0007220	normal histone H3-K9 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPAPJ760.03c	(Fig. 10C)
PMID:33533152	FYPO:0007220	normal histone H3-K9 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPAC821.09	(Fig. 10C)
PMID:33533152	FYPO:0007220	normal histone H3-K9 acetylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPAC821.09	(Fig. 10C)
PMID:33533152	FYPO:0001098	sensitive to 4-nitroquinoline N-oxide [has_severity] high	(Fig. 2A)
PMID:33533152	FYPO:0001689	normal growth on 4-nitroquinoline N-oxide	(Fig. 2A, 3A)
PMID:33533152	FYPO:0001689	normal growth on 4-nitroquinoline N-oxide	(Fig. 2A, 3A)
PMID:33533152	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 2C)
PMID:33533152	FYPO:0002550	sensitive to UV [has_severity] high	(Fig. 2C)
PMID:33533152	FYPO:0000969	normal growth during cellular response to UV	(Fig. 2C, 3A)
PMID:33533152	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 2C, 3A)
PMID:33533152	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 2C, 3A)
PMID:33533152	FYPO:0000969	normal growth during cellular response to UV	(Fig. 2C, 3A)
PMID:33533152	FYPO:0001689	normal growth on 4-nitroquinoline N-oxide	(Fig. 3D)
PMID:33533152	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 3D)
PMID:33533152	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 3D)
PMID:33533152	FYPO:0000969	normal growth during cellular response to UV	(Fig. 3D)
PMID:33533152	FYPO:0002550	sensitive to UV [has_severity] medium	(Fig. 3D)
PMID:33533152	FYPO:0000969	normal growth during cellular response to UV	(Fig. 3D)
PMID:33533152	FYPO:0001098	sensitive to 4-nitroquinoline N-oxide [has_severity] high	(Fig. 3D)
PMID:33533152	FYPO:0001689	normal growth on 4-nitroquinoline N-oxide	(Fig. 3D)
PMID:33533152	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3D)
PMID:33533152	FYPO:0003503	normal vegetative cell length	(Fig. 4C)
PMID:33533152	FYPO:0003503	normal vegetative cell length	(Fig. 4C)
PMID:33533152	FYPO:0001492	viable elongated vegetative cell [has_penetrance] 25	(Fig. 4C)
PMID:33533152	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC622.16c	(Fig. 5)
PMID:33533152	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 6A)
PMID:33533152	FYPO:0003670	sensitive to mycophenolic acid [has_severity] high	(Fig. 6A)
PMID:33533152	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 6A)
PMID:33533152	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPJ760.03c [has_severity] high	(Fig. 6B)
PMID:33533152	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAPJ760.03c	(Fig. 6B)
PMID:33533152	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09	(Fig. 6B)
PMID:33533152	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09	(Fig. 6B)
PMID:33533152	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAPJ760.03c	(Fig. 6B)
PMID:33533152	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] high [assayed_transcript] PomBase:SPAC821.09	(Fig. 6B)
PMID:33533152	FYPO:0001689	normal growth on 4-nitroquinoline N-oxide	(Fig. 8B)
PMID:33533152	FYPO:0000969	normal growth during cellular response to UV	(Fig. 8B)
PMID:33533152	FYPO:0000969	normal growth during cellular response to UV	(Fig. 8B)
PMID:33533152	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 8B)
PMID:33533152	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 8B)
PMID:33533152	FYPO:0001689	normal growth on 4-nitroquinoline N-oxide	(Fig. 8B)
PMID:33533152	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 8B)
PMID:33533152	FYPO:0002550	sensitive to UV [has_severity] high	(Fig. 8B)
PMID:33533152	FYPO:0001098	sensitive to 4-nitroquinoline N-oxide [has_severity] high	(Fig. 8B)
PMID:33533152	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 9A)
PMID:33533152	FYPO:0003670	sensitive to mycophenolic acid [has_severity] high	(Fig. 9A)
PMID:33533152	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 9A)
PMID:33533152	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09	(Fig. 9B)
PMID:33533152	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09	(Fig. 9B)
PMID:33533152	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAPJ760.03c	(Fig. 9B)
PMID:33533152	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAPJ760.03c	(Fig. 9B)
PMID:33533152	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] high [assayed_transcript] PomBase:SPAC821.09	(Fig. 9B)
PMID:33533152	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPJ760.03c [has_severity] high	(Fig. 9B)
PMID:33534698	GO:0010508	positive regulation of autophagy [happens_during] cellular response to nitrogen starvation	(Fig. 4a)
PMID:33534698	GO:0010508	positive regulation of autophagy [happens_during] cellular response to nitrogen starvation	(Fig. 4a) Though much less than that in wild-type cells, autophagy was still detectable in the tsc2D iml1D double mutant, indicating that, in addition to the GATOR1 and TSC complexes, there must be an additional mechanism to attenuate TORC1 upon nitrogen starvation for autophagy induction.
PMID:33534698	FYPO:0007803	abolished macroautophagy during leucine starvation	(Fig. 4e) In order to test whether the Gcn2 kinase induces autophagy through phosphorylation of eIF2a, we constructed a strain that expresses eIF2a with its phosphorylation site Ser52 substituted by alanine (eIF2a-S52A).
PMID:33534698	GO:0061700	GATOR2 complex	(Figure 1)
PMID:33534698	GO:0061700	GATOR2 complex	(Figure 1)
PMID:33534698	GO:0035859	Seh1-associated complex	(Figure 1)
PMID:33534698	GO:1990130	GATOR1 complex	(Figure 1)
PMID:33534698	GO:0061700	GATOR2 complex	(Figure 1)
PMID:33534698	GO:0061700	GATOR2 complex	(Figure 1)
PMID:33534698	GO:0061700	GATOR2 complex	(Figure 1)
PMID:33534698	GO:0005774	vacuolar membrane	(Figure 1, Supp 1)
PMID:33534698	GO:0005774	vacuolar membrane	(Figure 1, Supp 1)
PMID:33534698	GO:0005774	vacuolar membrane	(Figure 1, Supp 1)
PMID:33534698	GO:0005774	vacuolar membrane	(Figure 1, Supp 1)
PMID:33534698	GO:0005774	vacuolar membrane	(Figure 1, Supp 1)
PMID:33534698	GO:0005774	vacuolar membrane	(Figure 1, Supp 1)
PMID:33534698	GO:0005774	vacuolar membrane	(Figure 1, Supp 1)
PMID:33534698	FYPO:0001357	normal vegetative cell population growth	(Figure 2a)
PMID:33534698	FYPO:0001357	normal vegetative cell population growth	(Figure 2a)
PMID:33534698	FYPO:0001357	normal vegetative cell population growth	(Figure 2a)
PMID:33534698	FYPO:0001355	decreased vegetative cell population growth	(Figure 2a)
PMID:33534698	FYPO:0001357	normal vegetative cell population growth	(Figure 2a)
PMID:33534698	FYPO:0001357	normal vegetative cell population growth	(Figure 2a)
PMID:33534698	FYPO:0001357	normal vegetative cell population growth	(Figure 2a)
PMID:33534698	FYPO:0001357	normal vegetative cell population growth	(Figure 2a)
PMID:33534698	FYPO:0001355	decreased vegetative cell population growth	(Figure 2a)
PMID:33534698	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Figure 2b)
PMID:33534698	FYPO:0001357	normal vegetative cell population growth	(Figure 2b) (comment: any1 rescues)
PMID:33534698	FYPO:0001357	normal vegetative cell population growth	(Figure 2b) (comment: any1 rescues)
PMID:33534698	FYPO:0001357	normal vegetative cell population growth	(Figure 2e) (comment: sea3 rescued by gtr1 GDP-locked)
PMID:33534698	FYPO:0001357	normal vegetative cell population growth	(Figure 2e) (comment:sea3 rescued by gtr1 GDP-locked)
PMID:33534698	FYPO:0006345	increased duration of protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPCC4G3.08	(Figure 2f)
PMID:33534698	FYPO:0006345	increased duration of protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPCC4G3.08 [has_severity] high	(Figure 2g)
PMID:33534698	FYPO:0004250	abolished protein localization to vacuolar membrane [assayed_protein] PomBase:SPAC12G12.01c	(Figure 3 Figure supplement 1C-E).
PMID:33534698	FYPO:0004250	abolished protein localization to vacuolar membrane [assayed_protein] PomBase:SPAC15F9.02	(Figure 3 Figure supplement 1C-E).
PMID:33534698	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_protein] PomBase:SPBC543.04	(Figure 3 Figure supplement 2E,F and G)
PMID:33534698	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_protein] PomBase:SPBC26H8.04c	(Figure 3 Figure supplement 2E,F and G)
PMID:33534698	FYPO:0001357	normal vegetative cell population growth	(Figure 3—Figure supplement 3A), indicating that Arg854 of S. pombe Iml1 is not essential for the GATOR1 function.
PMID:33534698	GO:0004694	eukaryotic translation initiation factor 2alpha kinase activity [part_of] GCN2-mediated signaling [happens_during] cellular response to amino acid starvation [has_input] PomBase:SPCC11E10.07c	(comment: CONDITION Arginine starvation) Similarly, in cells of arginine auxotrophy, Gcn2-dependent autophagy was detectable after incubation in the growth medium without arginine (Figure 4—Figure supplement 1C).
PMID:33534698	GO:0140469	GCN2-mediated signaling [happens_during] cellular response to amino acid starvation	(comment: vw I edited to make the response the extension to GCN2 mediated signalling, but I hope to improve these GO terms.)
PMID:33534698	FYPO:0004250	abolished protein localization to vacuolar membrane [assayed_protein] PomBase:SPAC11E3.05	Consistently, in the absence of intact GATOR1, the vacuolar localization of Sea3 (Figure 1E) was lost and the protein diffused throughout the cytosol (Figure 3I, Figure 3—Figure supplement 1A)
PMID:33534698	FYPO:0004250	abolished protein localization to vacuolar membrane [assayed_protein] PomBase:SPAC4F8.11	Furthermore, consi tent with the essential role of Sea3 in the interaction between GATOR1 and the other GATOR2 subunits, the vacuolar localization of Sea2, Sea4, and Seh1 ( was abrogated in the sea3D background (Figure 3—Figure supplement 1C-E).
PMID:33534698	GO:0010508	positive regulation of autophagy [happens_during] cellular response to amino acid starvation	Gcn2-dependent induction of autophagy was also observed in cells treated by 3-amino-1,2,4-triazole (3-AT) or methionine sulfoximine (MSX), inhibitors of histidine and glutamine biosynthesis, respectively (Figure 4—Figure supplement 1D,E).
PMID:33534698	GO:0004694	eukaryotic translation initiation factor 2alpha kinase activity [part_of] GCN2-mediated signaling [happens_during] cellular response to leucine starvation [has_input] PomBase:SPCC11E10.07c	However, no GFP accumulation was detected in gcn2D cells under leucine starvation (Figure 4C), demonstrating that the autophagy induced by leucine starvation is dependent on the Gcn2 kinase.
PMID:33534698	FYPO:0006398	abolished protein phosphorylation during cellular response to leucine starvation [assayed_protein] PomBase:SPCC4G3.08	In contrast, Psk1 remained phosphorylated even after the starvation in the gcn2D, eIF2a-S52A, and fil1D mutant strains (Figure 5A), suggesting that TORC1 inactivation in leucine-starved cells is mediated by the Gcn2-eIF2a-Fil1 pathway.
PMID:33534698	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_protein] PomBase:SPAC23H3.03c	In the case of the sea3D mutant, Iml1, Npr2, and Npr3 were all detectable on vacuoles (Figure 3—Figure supplement 2E,F and G)
PMID:33534698	FYPO:0006295	abolished macroautophagy during nitrogen starvation	In the gnc2D iml1D tsc2D triple mutant, a trace of released GFP was detected only after 14 hr of nitrogen starvation (Figure 6C) while autophagy takes place within 2 hr in wild-type cells after the starvation (Figure 4B).
PMID:33534698	PomGeneEx:0000018	protein level increased [during] cellular response to leucine starvation	Indeed, we observed that, after leucine starvation, the Fil1 protein increased, which was dependent on Gcn2 and the phosphorylation of eIF2a (Figure 4—Figure supplement 1H).
PMID:33534698	FYPO:0007803	abolished macroautophagy during leucine starvation	Moreover, S. pombe cells lacking Gcn3 (Figure 4D) or Fil1 (Figure 4F) displayed autophagy defects during leucine starvation.
PMID:33534698	FYPO:0007803	abolished macroautophagy during leucine starvation	Moreover, the autophagy defect of the gcn2D mutant was complemented by TORC1 inactivation by the TORC1 inhibitors, rapamycin and caffeine (Figure 5B).
PMID:33534698	GO:0035591	signaling adaptor activity [has_input] PomBase:SPBC26H8.04c	On the other hand, Iml1 and Sea3 were co-immunoprecipitated even in the absence of Seh1, Sea2, and Sea4 (Figure 3E), implying that Sea3 directly binds to GATOR1 and anchors the other GATOR2 components to GATOR1.
PMID:33534698	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC26H8.04c [assayed_protein] PomBase:SPBC337.13c	On the other hand, immunoprecipitation of the GATOR1 subunit Iml1 found that the physical interaction between GATOR1 and the Gtr1 GTPase was reduced in the sea3D mutant (Figure 3M).
PMID:33534698	GO:0005096	GTPase activator activity [occurs_in] vacuolar membrane [happens_during] cellular response to nitrogen starvation [has_input] PomBase:SPBC337.13c [part_of] negative regulation of autophagy	Recently, another conserved arginine residue in mammalian GATOR1, Arg78 of the Nprl2 subunit,was proposed to serve as an arginine finger that promotes GTP hydrolysis by RagA/B (Shen et al.,2019, Figure 3—Figure supplement 3B). To assess the role of the equivalent residue in the S.pombe GATOR1, Arg98 in Npr2 was substituted with alanine to construct an npr2R98A mutantstrain. The mutant cells exhibited a compromised growth phenotype that was rescued by rapamycinor the gtr1SN mutation, an indicative of compromised GAP activity of GATOR1 (Figure 3—Figure supplement 3C). Though the npr2R98A phenotype was not as severe as that of the npr2 nullmutant, these observations are in line with the model that the conserved Arg residue in Npr2, butnot the one in Iml1, acts as an arginine finger of GATOR1 also in fission yeast.
PMID:33534698	GO:0005096	GTPase activator activity [has_input] PomBase:SPBC337.13c [occurs_in] vacuolar membrane [happens_during] cellular response to nitrogen starvation [part_of] negative regulation of autophagy	Recently, another conserved arginine residue in mammalian GATOR1, Arg78 of the Nprl2 subunit,was proposed to serve as an arginine finger that promotes GTP hydrolysis by RagA/B (Shen et al.,2019, Figure 3—Figure supplement 3B). To assess the role of the equivalent residue in the S.pombe GATOR1, Arg98 in Npr2 was substituted with alanine to construct an npr2R98A mutantstrain. The mutant cells exhibited a compromised growth phenotype that was rescued by rapamycinor the gtr1SN mutation, an indicative of compromised GAP activity of GATOR1 (Figure 3—Figuresupplement 3C). Though the npr2R98A phenotype was not as severe as that of the npr2 nullmutant, these observations are in line with the model that the conserved Arg residue in Npr2, butnot the one in Iml1, acts as an arginine finger of GATOR1 also in fission yeast.
PMID:33534698	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC11E3.05 [assayed_protein] PomBase:SPBC26H8.04c	The binding of Sea3 to GATOR1 is dependent on the integrity of the GATOR1 complex, and the absence of any one of the GATOR1 subunits disrupted the Sea3-GATOR1 association (Figure 3F,G and H).
PMID:33534698	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC11E3.05 [assayed_protein] PomBase:SPBC26H8.04c	The binding of Sea3 to GATOR1 is dependent on the integrity of the GATOR1 complex, and the absence of any one of the GATOR1 subunits disrupted the Sea3-GATOR1 association (Figure 3F,G and H).
PMID:33534698	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC11E3.05 [assayed_protein] PomBase:SPBC26H8.04c	The binding of Sea3 to GATOR1 is dependent on the integrity of the GATOR1 complex, and the absence of any one of the GATOR1 subunits disrupted the Sea3-GATOR1 association (Figure 3F,G and H).
PMID:33534698	GO:0010508	positive regulation of autophagy [happens_during] cellular response to leucine starvation	We found that autophagy after leucine starvation was severely impaired in cells lacking Cpc2 and in those overexpressing a fission yeast ortholog of Yih1/IMPACT (Figure 4—Figure supplement 1G), confirming the essential role of the Gcn2 activity in autophagy induction upon amino acid starvation.
PMID:33536395	FYPO:0001911	decreased protein glycosylation during vegetative growth [assayed_protein] PomBase:SPCC191.11	(Fig. 3B)
PMID:33536395	FYPO:0007288	normal protein galactosylation during vegetative growth	(Fig. 3C)
PMID:33536395	GO:0006890	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum	(comment: changed from protein retention in ER lumen)
PMID:33536395	GO:0005794	Golgi apparatus	As expected, Och1-EGFP expressed in the wild type strain showed strong fluorescence as a typical Golgi-like dots, but faint fluorescent dots were confirmed in gmn2∆ cells (Fig. 4A).
PMID:33536395	FYPO:0004786	decreased protein localization to Golgi apparatus [assayed_protein] PomBase:SPAC1006.05c	As expected, Och1-EGFP expressed in the wild type strain showed strong fluorescence as a typical Golgi-like dots, but faint fluorescent dots were confirmed in gmn2∆ cells (Fig. 4A).
PMID:33536395	FYPO:0007800	abolished protein localization to endoplasmic reticulum, with protein mislocalized to cell surface	In contrast, gmn2∆ cells missorted and secreted a significant amount of BiP to the cell surface. These results indicate that Gmn2p is required for normal retention of a luminal ER protein in S. pombe cells.
PMID:33536395	FYPO:0007800	abolished protein localization to endoplasmic reticulum, with protein mislocalized to cell surface	In contrast, gmn2∆ cells missorted and secreted a significant amount of BiP to the cell surface. These results indicate that Gmn2p is required for normal retention of a luminal ER protein in S. pombe cells.
PMID:33536395	GO:0000139	Golgi membrane	The Gmn2-EGFP protein was recycled back into the ER just as Gms1-EGFP, indicating that Gmn2-EGFP localized mostly to the Golgi membranes (Fig. 6B).
PMID:33536395	FYPO:0001234	slow vegetative cell population growth [has_severity] low	The gmn2∆ cells were found to be viable despite growing slightly slower than the wild type (Fig. 3A MM (leu-)) and exhibited the same phenotypes as those of the original gmn2 mutant.
PMID:33536395	FYPO:0000106	sensitive to hygromycin B [has_severity] high	The gmn2∆ cells were highly sensitive to hygromycin B, being unable to grow on YES plates containing 25 μg/ml of the drug (Fig. 3A)
PMID:33536434	FYPO:0001327	increased protein level during vegetative growth [assayed_transcript] PomBase:SPAC27D7.03c	(comment: GI Redundancy)
PMID:33536435	GO:0003899	DNA-directed RNA polymerase activity	In an independent experiment, we established an Sp Pol I elongation complex (EC) in vitro similar to its Sc counterpart
PMID:33536435	GO:0003899	DNA-directed RNA polymerase activity	In an independent experiment, we established an Sp Pol I elongation complex (EC) in vitro similar to its Sc counterpart
PMID:33536435	GO:0003899	DNA-directed RNA polymerase activity	In an independent experiment, we established an Sp Pol I elongation complex (EC) in vitro similar to its Sc counterpart
PMID:33536435	GO:0003899	DNA-directed RNA polymerase activity	In an independent experiment, we established an Sp Pol I elongation complex (EC) in vitro similar to its Sc counterpart
PMID:33536435	GO:0003899	DNA-directed RNA polymerase activity	In an independent experiment, we established an Sp Pol I elongation complex (EC) in vitro similar to its Sc counterpart
PMID:33536435	GO:0003899	DNA-directed RNA polymerase activity	In an independent experiment, we established an Sp Pol I elongation complex (EC) in vitro similar to its Sc counterpart
PMID:33536435	GO:0003899	DNA-directed RNA polymerase activity	In an independent experiment, we established an Sp Pol I elongation complex (EC) in vitro similar to its Sc counterpart
PMID:33536435	GO:0003899	DNA-directed RNA polymerase activity	In an independent experiment, we established an Sp Pol I elongation complex (EC) in vitro similar to its Sc counterpart
PMID:33536435	GO:0003899	DNA-directed RNA polymerase activity	In an independent experiment, we established an Sp Pol I elongation complex (EC) in vitro similar to its Sc counterpart
PMID:33536435	GO:0003899	DNA-directed RNA polymerase activity	In an independent experiment, we established an Sp Pol I elongation complex (EC) in vitro similar to its Sc counterpart
PMID:33536435	GO:0003899	DNA-directed RNA polymerase activity	In an independent experiment, we established an Sp Pol I elongation complex (EC) in vitro similar to its Sc counterpart
PMID:33536435	GO:0003899	DNA-directed RNA polymerase activity	In an independent experiment, we established an Sp Pol I elongation complex (EC) in vitro similar to its Sc counterpart
PMID:33568651	FYPO:0007681	abnormal RNA-DNA hybrid ribonuclease activity	Rnh201-RED mutant, based on the S. cerevsiae equivalent, is unable to remove single rNMPs from DNA but, buy genetic analysis, is able to remove runs of rNMPs.
PMID:33568651	FYPO:0007254	normal replication fork processing	replication dynamic analysis demonstrates that the priming strand is stable in the absence of Ku (previous work has shown resection is increased behind the arrested fork). Replication restart is slightly delayed, confirming previous work. Assayed by polymerase usage sequencing
PMID:33574613	FYPO:0003230	decreased histone H3-K9 methylation at heterochromatin island during vegetative growth [assayed_using] PomBase:SPAC27D7.13c [has_severity] high	(Fig. 1a)
PMID:33574613	FYPO:0003230	decreased histone H3-K9 methylation at heterochromatin island during vegetative growth [assayed_using] PomBase:SPBC32H8.11 [has_severity] high	(Fig. 1a)
PMID:33574613	FYPO:0003230	decreased histone H3-K9 methylation at heterochromatin island during vegetative growth [assayed_using] PomBase:SPBC32H8.11 [has_severity] high	(Fig. 1a)
PMID:33574613	FYPO:0003230	decreased histone H3-K9 methylation at heterochromatin island during vegetative growth [assayed_using] PomBase:SPAC27D7.13c [has_severity] high	(Fig. 1a)
PMID:33574613	FYPO:0003746	increased histone H3-K9 methylation at heterochromatin island during vegetative growth [has_severity] low	(Fig. 1b) (comment: CHECK (1.5x) (me2))
PMID:33574613	FYPO:0007213	decreased histone H3-K9 dimethylation at heterochromatin island during vegetative growth [assayed_using] PomBase:SPBC32H8.11 [has_severity] high	(Fig. 1b) (comment: CHECK me2)
PMID:33574613	FYPO:0007213	decreased histone H3-K9 dimethylation at heterochromatin island during vegetative growth [assayed_using] PomBase:SPAC27D7.13c [has_severity] high	(Fig. 1b) (comment: CHECK me2)
PMID:33574613	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC7D4.14c	(Fig. 1f, g)
PMID:33574613	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC17H9.02	(Figure 1c)
PMID:33574613	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC7D4.14c [has_severity] high	(Figure 1e)
PMID:33574613	MOD:01148	ubiquitinylated lysine	(Figure 1h)
PMID:33574613	FYPO:0005121	decreased level of early meiotic gene mRNA during meiotic cell cycle [assayed_using] PomBase:SPAC17A5.18c	(Figure 6B) DSBs; for example, rec25, rec27 and mug20), which are critical for recombination and proper chromosome segregation during meiosis-I4
PMID:33574613	FYPO:0005121	decreased level of early meiotic gene mRNA during meiotic cell cycle [assayed_using] PomBase:SPBC577.05c	(Figure 6B) DSBs; for example, rec25, rec27 and mug20), which are critical for recombination and proper chromosome segregation during meiosis-I4
PMID:33574613	FYPO:0005121	decreased level of early meiotic gene mRNA during meiotic cell cycle [assayed_using] PomBase:SPBC36B7.06c	(Figure 6B) DSBs; for example, rec25, rec27 and mug20), which are critical for recombination and proper chromosome segregation during meiosis-I4
PMID:33574613	GO:0080008	Cul4-RING E3 ubiquitin ligase complex	(comment: which?)
PMID:33574613	GO:0080008	Cul4-RING E3 ubiquitin ligase complex	(comment: which?)
PMID:33574613	FYPO:0000485	decreased meiotic recombination [assayed_using] PomBase:SPBC36B7.06c	Compared with the WT, cells expressing Pir1-SD showed a marked decrease in recombination frequency (Fig. 6f).
PMID:33574613	FYPO:0000485	decreased meiotic recombination [assayed_using] PomBase:SPBC577.05c	Compared with the WT, cells expressing Pir1-SD showed a marked decrease in recombination frequency (Fig. 6f).
PMID:33574613	FYPO:0000485	decreased meiotic recombination [assayed_using] PomBase:SPAC17A5.18c	Compared with the WT, cells expressing Pir1-SD showed a marked decrease in recombination frequency (Fig. 6f).
PMID:33574613	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_using] PomBase:SPAC7D4.14c	Consistently, ubiquitination of Pir1-SD in the tor2-ts6 mts2-1 mutant was reduced (Fig. 2e).
PMID:33574613	FYPO:0000581	decreased spore germination frequency	Defective chromosome segregation and reduced spore viability were also noted (Fig. 7a and Supplementary Videos 1-3)
PMID:33574613	FYPO:0004159	abnormal homologous chromosome segregation	Defective chromosome segregation and reduced spore viability were also noted (Fig. 7a and Supplementary Videos 1-3)
PMID:33574613	FYPO:0002033	abolished protein phosphorylation during vegetative growth	Extended Data Fig. 2a, c
PMID:33574613	FYPO:0003235	normal histone H3-K9 methylation at centromere outer repeat during vegetative growth	Extended data Fig 1b, c (comment: also at MTREC independent islands)
PMID:33574613	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC1006.03c	Interestingly, the expression of Pir1-SD in tor2-ts6 cells restored the levels of Red1 (Extended Data Fig. 2e), suggesting that the reduction in Red1 in the tor2 mutant cells (Fig. 1c) is linked to the degradation of its interaction partner Pir1
PMID:33574613	FYPO:0007685	increased vegetative cell population growth during nutrient starvation	Intriguingly, cells expressing Pir1-SD, but not Pir1-WT or Pir1-SA, continued to divide on nutrient-limiting medium at a low temperature (Fig. 4a), suggesting that stabilized Pir1 supports cell proliferation under suboptimal growth conditions.
PMID:33574613	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC7D4.14c	Moreover, loss of the ubiquitin ligase-associated Cullin-RING finger family protein Cul4, a component of ClrC35,36 that interacts with MTREC15, also stabilized Pir1 in both tor2-ts6 and nitrogen-starved cells (Fig. 3c
PMID:33574613	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC7D4.14c	Moreover, loss of the ubiquitin ligase-associated Cullin-RING finger family protein Cul4, a component of ClrC35,36 that interacts with MTREC15, also stabilized Pir1 in both tor2-ts6 and nitrogen-starved cells (Fig. 3c
PMID:33574613	FYPO:0002082	increased protein ubiquitination during vegetative growth [assayed_using] PomBase:SPAC7D4.14c	Moreover, ubiquitination of Pir1 was detected in tor2-ts6 cells and increased in the tor2-ts6 mts2-1 mutant (Fig. 1h)
PMID:33574613	PomGeneEx:0000019	protein level decreased [during] meiosis I cell cycle phase	Notably, Pir1 was depleted during early meiosis (Fig. 5a) but gradually recovered by middle meiosis.
PMID:33574613	FYPO:0007281	normal level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPAC27D7.13c [has_severity] high	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g).
PMID:33574613	FYPO:0007281	normal level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC32H8.11 [has_severity] high	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g).
PMID:33574613	FYPO:0007281	normal level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPAC27D7.13c [has_severity] high	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g).
PMID:33574613	FYPO:0007281	normal level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC32H8.11 [has_severity] high	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g).
PMID:33574613	FYPO:0007281	normal level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPAC27D7.13c	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g). and Fig. 4g).
PMID:33574613	FYPO:0007281	normal level of meiotic gene mRNA during vegetative growth [assayed_using] PomBase:SPBC32H8.11	Remarkably, the loss of Ubi4, Cul4 or Ddb1 in tor2-ts6 cells restored the silencing of gametogenic genes genome-wide (Fig. 3h and Extended Data Fig. 3g). and Fig. 4g).
PMID:33574613	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC7D4.14c	Replacement of the 12 phospho-serine residues with the phospho-mimic aspartic acid residue (Pir1-12SD) indeed conferred stability in tor2-ts6 cells (Extended Data Fig. 2d)
PMID:33574613	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPAC7D4.14c	Replacement of the 12 phospho-serine residues with the phospho-mimic aspartic acid residue (Pir1-12SD) indeed conferred stability in tor2-ts6 cells (Extended Data Fig. 2d); Deletion of ubi4 in tor2-ts6 cells cells indeed stabilized Pir1 (Fig. 3b)
PMID:33574613	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Similar to pir1∆, tor2-ts6 cells showed a severe growth defect at a semi-permissive temperature (29°C) on minimal medium but not on rich medium (Fig. 4d).
PMID:33574613	FYPO:0001357	normal vegetative cell population growth	Similar to pir1∆, tor2-ts6 cells showed a severe growth defect at a semi-permissive temperature (29°C) on minimal medium but not on rich medium (Fig. 4d).
PMID:33574613	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_using] PomBase:SPAC7D4.14c	The addition of ubi4∆, cul4∆ or ddb1∆ dramatically reduced Pir1 ubiquitination in tor2-ts6 mts2-1 cells (Fig. 3f).
PMID:33574613	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_using] PomBase:SPAC7D4.14c	The addition of ubi4∆, cul4∆ or ddb1∆ dramatically reduced Pir1 ubiquitination in tor2-ts6 mts2-1 cells (Fig. 3f).
PMID:33574613	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_using] PomBase:SPAC7D4.14c	The addition of ubi4∆, cul4∆ or ddb1∆ dramatically reduced Pir1 ubiquitination in tor2-ts6 mts2-1 cells (Fig. 3f).
PMID:33574613	FYPO:0007212	decreased chromatin silencing at heterochromatin island	The restoration of silencing required Pir1, as a loss of Ubi4 failed to silence ade6-DSR in pir1∆ cells (Fig. 3g).
PMID:33574613	FYPO:0007212	decreased chromatin silencing at heterochromatin island	The restoration of silencing required Pir1, as a loss of Ubi4 failed to silence ade6-DSR in pir1∆ cells (Fig. 3g).
PMID:33574613	FYPO:0001357	normal vegetative cell population growth	We indeed observed that pir1∆ cells exhibited a growth defect on minimal medium
PMID:33574613	FYPO:0001355	decreased vegetative cell population growth	We indeed observed that pir1∆ cells exhibited a growth defect on minimal medium
PMID:33574613	FYPO:0007686	increased number of nuclear exosome foci	Whereas Pir1-WT disappeared, Pir1-SD persisted during meiosis as multiple nuclear foci coinciding with Mmi1 and Erh1 foci (Fig. 5b,c).
PMID:33574613	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores	abnormal asci containing fewer than four, or no, spores were frequently generated (Fig. 7c).
PMID:33574613	FYPO:0004966	increased duration of horsetail movement	cells showed impaired oscillation of chromosomes and a prolonged horsetail stage (approximately 160min compared with approximately 120min; Fig. 7a,b).
PMID:33574613	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC7D4.14c [part_of] positive regulation of nuclear mRNA surveillance of meiosis-specific transcripts	he Tor2-containing TORC1 complex phosphorylated Pir1 in vitro and mutation of the 12 serine residues to alanine attenuated Pir1 phosphorylation (Extended Data Fig. 2a,c).
PMID:33574613	FYPO:0007687	normal protein localization to nuclear exosome focus during meiosis [assayed_using] PomBase:SPCC736.12c	restores the MTREC and Rrp6 association with Mmi1 and Erh1 during meiosis (Fig. 5d).
PMID:33574613	FYPO:0007687	normal protein localization to nuclear exosome focus during meiosis [assayed_using] PomBase:SPAC19G12.17	restores the MTREC and Rrp6 association with Mmi1 and Erh1 during meiosis (Fig. 5d).
PMID:33574613	FYPO:0007226	normal chromatin silencing at heterochromatin island	the deletion of ubi4, ddb1 or cul4 restored ade6-DSR silencing (Fig. 3g and Extended Data Fig. 3d).
PMID:33574613	FYPO:0007226	normal chromatin silencing at heterochromatin island	the deletion of ubi4, ddb1 or cul4 restored ade6-DSR silencing (Fig. 3g and Extended Data Fig. 3d).
PMID:33574613	FYPO:0007226	normal chromatin silencing at heterochromatin island	the deletion of ubi4, ddb1 or cul4 restored ade6-DSR silencing (Fig. 3g and Extended Data Fig. 3d).
PMID:33574613	FYPO:0006542	increased RNA level during mitosis [assayed_using] PomBase:SPBC337.08c	ubi4 gene, which encodes polyubiquitin implicated in sexual development34, was upregulate in tor2-ts6 cells (Fig. 3a).
PMID:33579781	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 2)
PMID:33579781	FYPO:0002141	normal cell population growth at low temperature	(Fig. 2) However, S. pombe is viable when Pro3 or Pro6 is changed to alanine in every other heptad, including the rump, in the context of the full-length CTD (Fig. 2), signifying that reduced proline content is tolerated and that Pro3 and Pro6 need not be present in consecutive heptads
PMID:33579781	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 2) However, S. pombe is viable when Pro3 or Pro6 is changed to alanine in every other heptad, including the rump, in the context of the full-length CTD (Fig. 2), signifying that reduced proline content is tolerated and that Pro3 and Pro6 need not be present in consecutive heptads
PMID:33579781	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC4F6.09 [assayed_transcript] PomBase:SPBC106.02c [assayed_transcript] PomBase:SPAC1F7.07c [assayed_transcript] PomBase:SPAC1F7.08 [assayed_transcript] PomBase:SPBC1271.09	(Fig. 4A)
PMID:33579781	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC4F6.09 [assayed_transcript] PomBase:SPBC106.02c [assayed_transcript] PomBase:SPAC1F7.07c [assayed_transcript] PomBase:SPAC1F7.08	(Fig. 4A)
PMID:33579781	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC4F6.09 [assayed_transcript] PomBase:SPBC106.02c [assayed_transcript] PomBase:SPAC1F7.07c [assayed_transcript] PomBase:SPAC1F7.08	(Fig. 4A)
PMID:33579781	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC23G3.02c [assayed_transcript] PomBase:SPAC23G3.03	(Fig. 4A)
PMID:33579781	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1271.09 [assayed_transcript] PomBase:SPBP4G3.02 [assayed_transcript] PomBase:SPBC8E4.01c [assayed_transcript] PomBase:SPBC4F6.09 [assayed_transcript] PomBase:SPBC106.02c [assayed_transcript] PomBase:SPAC1F8.03c [assayed_transcript] PomBase:SPAC1F7.07c [assayed_transcript] PomBase:SPAC1F7.08	(Fig. 4A)
PMID:33579781	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC23G3.02c [assayed_transcript] PomBase:SPAC23G3.03 [assayed_transcript] PomBase:SPBC1683.09c	(Fig. 4A)
PMID:33579781	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1271.09 [assayed_transcript] PomBase:SPBP4G3.02 [assayed_transcript] PomBase:SPBC8E4.01c [assayed_transcript] PomBase:SPBC4F6.09 [assayed_transcript] PomBase:SPBC106.02c	(Fig. 4A)
PMID:33579781	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC23G3.02c [assayed_transcript] PomBase:SPAC23G3.03	(Fig. 4A)
PMID:33579781	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1271.09 [assayed_transcript] PomBase:SPBC4F6.09 [assayed_transcript] PomBase:SPBC106.02c	(Fig. 4A)
PMID:33579781	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 4A)
PMID:33579781	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1271.09 [assayed_transcript] PomBase:SPBC4F6.09	(Fig. 4A)
PMID:33579781	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC23G3.02c [assayed_transcript] PomBase:SPAC23G3.03 [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 4A)
PMID:33579781	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 4A)
PMID:33579781	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC4F6.09 [assayed_transcript] PomBase:SPBC106.02c [assayed_transcript] PomBase:SPAC1F7.07c [assayed_transcript] PomBase:SPAC1F7.08 [assayed_transcript] PomBase:SPBC1271.09 [assayed_transcript] PomBase:SPBP4G3.02 [assayed_transcript] PomBase:SPBC1683.09c [assayed_transcript] PomBase:SPAC1F8.03c [assayed_transcript] PomBase:SPAC1F8.02c	(Fig. 4A)
PMID:33579781	FYPO:0001355	decreased vegetative cell population growth	(Fig. 5A)
PMID:33579781	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:33579781	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:33579781	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:33579781	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:33579781	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:33579781	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:33579781	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:33579781	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:33579781	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:33579781	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:33579781	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:33579781	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:33579781	GO:0006369	termination of RNA polymerase II transcription	(comment: CHECK Need to add modified version)
PMID:33683349	FYPO:0007700	inviable small vegetative cell with premature mitotic G2/M phase transition [has_penetrance] high	"(Fig. 1, 2) (comment: Nick suggested ""mitotic catastrophe""We would make this a related synonym?)"
PMID:33683349	FYPO:0000648	viable small vegetative cell [has_penetrance] medium	(Fig. 2) (comment: CONDITION 30 degrees) wee1-50ts mik1D cells divide at a smaller size than wee1-50ts mik1D cig2D cells
PMID:33683349	FYPO:0002176	viable vegetative cell with normal cell size [has_penetrance] high	(Fig. 3)
PMID:33683349	FYPO:0006823	viable small vegetative cell with slow cell growth [has_penetrance] high	(Fig. 3)
PMID:33683349	FYPO:0002176	viable vegetative cell with normal cell size [has_penetrance] high	(Fig. 3)
PMID:33683349	FYPO:0000648	viable small vegetative cell [has_penetrance] high	(Fig. 3) (comment: i.e wee?)
PMID:33683349	FYPO:0002516	premature mitotic G2/M phase transition	(Fig. 5)
PMID:33683349	FYPO:0001387	loss of viability at high temperature [has_severity] high	(Fig. 5a)
PMID:33683349	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 5b) (comment: (I only curated the red line temp inc at tome zero, becase it would be difficult to specify at 60 mins, I could not think of a way to do this). I'm assuming these cells do not enter mitosis, is that correct)
PMID:33683349	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	(Fig. 6a)
PMID:33683349	FYPO:0001387	loss of viability at high temperature [has_severity] high	(Figure 4)
PMID:33683349	FYPO:0001490	inviable elongated vegetative cell [has_severity] high	(Figure 4)
PMID:33683349	FYPO:0002060	viable vegetative cell population	(Figure 6b)
PMID:33683349	FYPO:0000082	decreased cell population growth at high temperature	(comment: High temp - 30 degrees. (VW I changed this from a cell phenotype term to a population phenotype term) ) fig1 We interpret this suppression to indicate that the lethal mitoses, which occur in the smallest cells, require Cig2/CDK activity instead of, or in addition to, Cdc13/CDK activity.
PMID:33711009	FYPO:0005369	abolished cell population growth at low temperature	(comment: CONDITION 20°)
PMID:33711009	FYPO:0005369	abolished cell population growth at low temperature	(comment: CONDITION 20°)
PMID:33711009	FYPO:0005369	abolished cell population growth at low temperature	(comment: CONDITION 20°)
PMID:33711009	FYPO:0005369	abolished cell population growth at low temperature	(comment: CONDITION 20°)
PMID:33711009	FYPO:0005369	abolished cell population growth at low temperature	(comment: CONDITION 20°)
PMID:33711009	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC74.02c [assayed_protein] PomBase:SPBC776.02c	Neither the N-terminal segment from aa 1-496 nor the C-terminal fragment from 578-710 was able to bind to Dis2 or Swd22 in the 2-hybrid format (Fig 11A)
PMID:33711009	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC74.02c [assayed_protein] PomBase:SPAC824.04	Neither the N-terminal segment from aa 1-496 nor the C-terminal fragment from 578-710 was able to bind to Dis2 or Swd22 in the 2-hybrid format (Fig 11A)
PMID:33723569	FYPO:0003503	normal vegetative cell length	(comment: 25ºC, live-cell imaging, cell length at septation)
PMID:33723569	FYPO:0003503	normal vegetative cell length	(comment: 25ºC, live-cell imaging, cell length at septation)
PMID:33723569	FYPO:0002553	abnormal double-strand break processing	(comment: CONDITION 25ºC)
PMID:33723569	FYPO:0002344	sensitive to phleomycin [has_severity] low	(comment: CONDITION 25ºC)
PMID:33723569	FYPO:0000095	sensitive to bleomycin [has_severity] low	(comment: CONDITION 25ºC)
PMID:33723569	FYPO:0000095	sensitive to bleomycin [has_severity] low	(comment: CONDITION 25ºC)
PMID:33723569	FYPO:0000095	sensitive to bleomycin [has_severity] low	(comment: CONDITION 25ºC)
PMID:33723569	FYPO:0003906	normal growth on bleomycin	(comment: CONDITION 25ºC)
PMID:33723569	FYPO:0002601	normal histone H2A phosphorylation during vegetative growth	(comment: CONDITION 25ºC)
PMID:33723569	FYPO:0000095	sensitive to bleomycin [has_severity] low	(comment: CONDITION 25ºC)
PMID:33723569	FYPO:0000095	sensitive to bleomycin [has_severity] low	(comment: CONDITION 25ºC)
PMID:33723569	FYPO:0000085	sensitive to camptothecin	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0000088	sensitive to hydroxyurea	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0000268	sensitive to UV during vegetative growth	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0000268	sensitive to UV during vegetative growth	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0001355	decreased vegetative cell population growth	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0000089	sensitive to methyl methanesulfonate	(comment: CONDITION 32ºC)
PMID:33723569	FYPO:0007710	decreased number of Ssb1 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007711	normal number of Ssb1 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0004516	decreased number of Rad52 foci during vegetative growth	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0004516	decreased number of Rad52 foci during vegetative growth	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007328	normal number of Rad52 foci during vegetative growth	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007328	normal number of Rad52 foci during vegetative growth	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0004516	decreased number of Rad52 foci during vegetative growth	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0004516	decreased number of Rad52 foci during vegetative growth	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007328	normal number of Rad52 foci during vegetative growth	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0002573	increased number of Ssb1 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0004709	increased number of Rad52 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0006686	decreased DNA double-strand break processing	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0006686	decreased DNA double-strand break processing	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0002573	increased number of Ssb1 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0000972	increased number of Rad52 foci during vegetative growth	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007710	decreased number of Ssb1 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007710	decreased number of Ssb1 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007710	decreased number of Ssb1 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007711	normal number of Ssb1 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007711	normal number of Ssb1 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007710	decreased number of Ssb1 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0006687	decreased DNA double-strand break processing during double-strand break repair via homologous recombination	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0004466	increased number of Rad52 foci during cellular response to camptothecin	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0002573	increased number of Ssb1 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0007328	normal number of Rad52 foci during vegetative growth	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0000972	increased number of Rad52 foci during vegetative growth	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0002573	increased number of Ssb1 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0004516	decreased number of Rad52 foci during vegetative growth	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0002573	increased number of Ssb1 foci	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0006686	decreased DNA double-strand break processing	(comment: live-cell imaging, 25ºC)
PMID:33723569	FYPO:0006686	decreased DNA double-strand break processing	(comment: live-cell imaging, 25ºC)
PMID:33754639	FYPO:0002061	inviable vegetative cell population	(comment: temperature sensitive 37°)
PMID:33771877	FYPO:0007730	normal protein distribution along RNA polymerase II-transcribed genes during mitotic metaphase [assayed_using] PomBase:SPBC28F2.12 [assayed_region] PomBase:SPBC1105.05	(Fig. 1)
PMID:33771877	FYPO:0007738	normal protein localization to chromatin at 3' end of RNA polymerase II-transcribed genes during mitotic metaphase	(Fig. 1)
PMID:33771877	FYPO:0007735	increased protein localization to chromatin at 3' end of RNA polymerase III-transcribed genes during mitotic metaphase [assayed_using] PomBase:SPCC330.13	(Fig. 2)
PMID:33771877	FYPO:0007735	increased protein localization to chromatin at 3' end of RNA polymerase III-transcribed genes during mitotic metaphase [assayed_using] PomBase:SPCC306.03c	(Fig. 2)
PMID:33771877	FYPO:0007732	normal protein localization to chromatin at 3' end of RNA polymerase III-transcribed genes during mitotic metaphase [assayed_using] PomBase:SPAC29E6.08	(Fig. 2b)
PMID:33771877	FYPO:0007732	normal protein localization to chromatin at 3' end of RNA polymerase III-transcribed genes during mitotic metaphase [assayed_using] PomBase:SPBC21H7.05	(Fig. 2b) Importantly, the accumulation of condensin in sen1Δ cells could not be caused by an accumulation of either TFIIIC or Tbp1 because their levels on chromatin remained largely unaffected in the absence of Sen1, as shown by ChIP with a GFP-tagged version of Tbp1 and a myc-tagged version of the TFIIIC component Sfc6 (Figs 2B and S1).
PMID:33771877	FYPO:0007741	abnormal protein distribution along RNA polymerase II-transcribed genes during mitotic metaphase [assayed_using] PomBase:SPBC28F2.12 [assayed_region] PomBase:SPBC1105.05 [has_severity] low	(Fig. 3)
PMID:33771877	FYPO:0007741	abnormal protein distribution along RNA polymerase II-transcribed genes during mitotic metaphase [assayed_using] PomBase:SPBC28F2.12 [assayed_region] PomBase:SPAC1705.03c [has_severity] low	(Fig. 3)
PMID:33771877	FYPO:0007741	abnormal protein distribution along RNA polymerase II-transcribed genes during mitotic metaphase [assayed_using] PomBase:SPBC28F2.12 [assayed_region] PomBase:SPAC19B12.02c [has_severity] low	(Fig. 3)
PMID:33771877	FYPO:0007741	abnormal protein distribution along RNA polymerase II-transcribed genes during mitotic metaphase [assayed_using] PomBase:SPCC306.03c [assayed_region] PomBase:SPBC28F2.12 [has_severity] low	(Fig. 3)
PMID:33771877	FYPO:0007736	protein displaced from 3' end to 5' end of RNA polymerase II-transcribed genes during mitotic metaphase [assayed_using] PomBase:SPBC146.03c [assayed_region] PomBase:SPAC19B12.02c	(Fig. 3) At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites.
PMID:33771877	FYPO:0007736	protein displaced from 3' end to 5' end of RNA polymerase II-transcribed genes during mitotic metaphase [assayed_using] PomBase:SPBC146.03c [assayed_region] PomBase:SPBC1105.05	(Fig. 3) At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites.
PMID:33771877	FYPO:0007736	protein displaced from 3' end to 5' end of RNA polymerase II-transcribed genes during mitotic metaphase [assayed_using] PomBase:SPBC146.03c [assayed_region] PomBase:SPAC1705.03c	(Fig. 3) At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites.
PMID:33771877	FYPO:0007736	protein displaced from 3' end to 5' end of RNA polymerase II-transcribed genes during mitotic metaphase [assayed_using] PomBase:SPBC146.03c [assayed_region] PomBase:SPAC821.09	(Fig. 3) At exg1, ecm33, eng1 et gas1, condensin is redistributed throughout the gene body instead of accumulating around transcription termination sites.
PMID:33775921	FYPO:0001355	decreased vegetative cell population growth	(comment: highest overexpression level)
PMID:33788833	FYPO:0001422	decreased protein processing during vegetative growth [has_severity] medium [assayed_using] PomBase:SPAC24C9.08	(comment: Affecting Cps1 carboxypeptidase)
PMID:33788833	FYPO:0001422	decreased protein processing during vegetative growth [has_severity] high [assayed_using] PomBase:SPAC24C9.08	(comment: Affecting Cps1 carboxypeptidase)
PMID:33788833	FYPO:0001422	decreased protein processing during vegetative growth [has_severity] medium [assayed_using] PomBase:SPAC24C9.08	(comment: Affecting Cps1 carboxypeptidase)
PMID:33788833	FYPO:0007059	decreased protein localization to late endosome [has_severity] medium [assayed_using] PomBase:SPAC24C9.08	(comment: Affecting Cps1 carboxypeptidase)
PMID:33788833	FYPO:0001669	abolished protein processing during vegetative growth [assayed_using] PomBase:SPAC24C9.08	(comment: Affecting Cps1 carboxypeptidase)
PMID:33788833	FYPO:0001422	decreased protein processing during vegetative growth [has_severity] low [assayed_using] PomBase:SPAC24C9.08	(comment: Affecting Cps1 carboxypeptidase)
PMID:33788833	FYPO:0007059	decreased protein localization to late endosome [has_severity] high [has_penetrance] complete [assayed_using] PomBase:SPBC16C6.06	(comment: CHECK Affecting Vps10 and the PI(3) probe Cherry-FYVE)
PMID:33788833	FYPO:0007059	decreased protein localization to late endosome [has_severity] high [has_penetrance] complete [assayed_using] PomBase:SPCC777.13	(comment: CHECK Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE)
PMID:33788833	FYPO:0007059	decreased protein localization to late endosome [has_severity] high [has_penetrance] complete [assayed_using] PomBase:SPAC19A8.05c	(comment: CHECK Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE)
PMID:33788833	FYPO:0007059	decreased protein localization to late endosome [has_severity] high [has_penetrance] complete [assayed_using] PomBase:SPBC16C6.06	(comment: CHECK Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE)
PMID:33788833	FYPO:0007059	decreased protein localization to late endosome [has_severity] high [has_penetrance] complete [assayed_using] PomBase:SPBC31E1.04	(comment: CHECK Affecting Vps10, Vps27, Vps35, Pep12 and the PI(3)P probe Cherry-FYVE)
PMID:33788833	FYPO:0007059	decreased protein localization to late endosome [assayed_using] PomBase:SPBC16C6.06	(comment: CHECK same as fsv1delta alone)
PMID:33788833	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	(comment: CONDITION 1.0 M KCl)
PMID:33788833	FYPO:0006836	sensitive to magnesium chloride [has_severity] medium	(comment: CONDITION 80 mM MgCl2)
PMID:33788833	FYPO:0005489	protein mislocalized to vacuolar membrane [assayed_using] PomBase:SPBC16C6.06	(comment: same as vps35delta alone)
PMID:33788833	FYPO:0005489	protein mislocalized to vacuolar membrane [assayed_using] PomBase:SPBC16C6.06	(comment: same as vps35delta alone)
PMID:33788833	GO:0034058	endosomal vesicle fusion	In the null mutant and the mutant without SNARE domain the fluorescence of prevacuolar endosome markers is reduced, and Cps1 processing is abnormal
PMID:33788833	FYPO:0007721	abnormal protein recycling from late endosome to Golgi [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0007721	abnormal protein recycling from late endosome to Golgi [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0005489	protein mislocalized to vacuolar membrane [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0005489	protein mislocalized to vacuolar membrane [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0007721	abnormal protein recycling from late endosome to Golgi [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0005489	protein mislocalized to vacuolar membrane [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0005489	protein mislocalized to vacuolar membrane [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0005489	protein mislocalized to vacuolar membrane [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0005489	protein mislocalized to vacuolar membrane [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0005489	protein mislocalized to vacuolar membrane [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0005489	protein mislocalized to vacuolar membrane [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0007721	abnormal protein recycling from late endosome to Golgi [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0007721	abnormal protein recycling from late endosome to Golgi [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0007721	abnormal protein recycling from late endosome to Golgi [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0007721	abnormal protein recycling from late endosome to Golgi [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0005489	protein mislocalized to vacuolar membrane [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0007721	abnormal protein recycling from late endosome to Golgi [has_penetrance] high [has_severity] high [assayed_using] PomBase:SPAC6F12.03c	The mutant protein is observed at the vacuolar surface
PMID:33788833	FYPO:0005489	protein mislocalized to vacuolar membrane [has_penetrance] low [has_severity] variable severity	The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells
PMID:33788833	FYPO:0005489	protein mislocalized to vacuolar membrane [has_penetrance] low [has_severity] variable severity	The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells
PMID:33788833	FYPO:0007721	abnormal protein recycling from late endosome to Golgi [has_penetrance] low [has_severity] variable severity	The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells
PMID:33788833	FYPO:0007721	abnormal protein recycling from late endosome to Golgi [has_penetrance] low [has_severity] variable severity	The mutant protein is observed faintly at the vacuolar surface of a low percentage of cells
PMID:33788833	GO:0005802	trans-Golgi network	co-localization with Cfr1
PMID:33788833	GO:0031902	late endosome membrane	co-localization with Vps35 and with Vps27
PMID:33823663	GO:0004708	MAP kinase kinase activity [has_input] PomBase:SPAC31G5.09c [part_of] G1 to G0 transition involved in cell differentiation [happens_during] cellular response to nitrogen starvation	(Figure 9)
PMID:33823663	GO:0004707	MAP kinase activity [part_of] G1 to G0 transition involved in cell differentiation [happens_during] cellular response to nitrogen starvation	(Figure 9) (comment: modified form is activated for sexual differentiation)
PMID:33823663	FYPO:0007963	normal mating efficiency during nitrogen stress	DNS
PMID:33823663	FYPO:0007963	normal mating efficiency during nitrogen stress	DNS
PMID:33825974	FYPO:0007802	short linear element [has_severity] high	(Figure 4d, 4e; Figure s3b)
PMID:33825974	FYPO:0004602	normal linear element morphology	(Figure S2C)
PMID:33829153	FYPO:0001667	normal cAMP level during glucose starvation	(Fig. 1A and B)
PMID:33836577	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC338.08 [assayed_protein] PomBase:SPBC6B1.09c	(Figure 1)
PMID:33836577	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC338.08	(Figure 1)
PMID:33836577	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC338.08 [assayed_protein] PomBase:SPBC6B1.09c	(Figure 1)
PMID:33836577	GO:0140656	endodeoxyribonuclease activator activity [has_input] PomBase:SPAC13C5.07	(Figure 2)
PMID:33836577	GO:0005515	protein binding	(Figure 2) (comment: requires phosphorylated T89, T154, T155 to bind Nbs1 FHA domain)
PMID:33836577	FYPO:0007807	decreased endodeoxyribonuclease activator activity [assayed_enzyme] PomBase:SPAC13C5.07	(Figure 2D)
PMID:33836577	FYPO:0007806	normal endodeoxyribonuclease activator activity [assayed_enzyme] PomBase:SPAC13C5.07	(Figure 2D)
PMID:33836577	FYPO:0007807	decreased endodeoxyribonuclease activator activity [assayed_enzyme] PomBase:SPAC13C5.07	(Figure 2E)
PMID:33836577	FYPO:0007807	decreased endodeoxyribonuclease activator activity [assayed_enzyme] PomBase:SPAC13C5.07	(Figure 2E)
PMID:33836577	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Figure 3B)
PMID:33836577	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Figure 3B)
PMID:33836577	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Figure 3B)
PMID:33836577	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Figure 3B)
PMID:33836577	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Figure 3B)
PMID:33836577	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Figure 3C)
PMID:33836577	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Figure 3C)
PMID:33836577	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Figure 3C)
PMID:33836577	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Figure 3C)
PMID:33836577	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Figure 3C)
PMID:33836577	FYPO:0002151	inviable spore [has_penetrance] high	(Figure 3D)
PMID:33836577	FYPO:0002151	inviable spore [has_penetrance] high	(Figure 3D)
PMID:33836577	FYPO:0002151	inviable spore [has_penetrance] high	(Figure 3D)
PMID:33836577	FYPO:0002151	inviable spore [has_penetrance] high	(Figure 3D)
PMID:33836577	FYPO:0002151	inviable spore [has_penetrance] high	(Figure 3D)
PMID:33836577	FYPO:0002151	inviable spore [has_penetrance] high	(Figure 3D)
PMID:33836577	FYPO:0007806	normal endodeoxyribonuclease activator activity [assayed_enzyme] PomBase:SPAC13C5.07	We therefore introduced a synthetic CT15 peptide into an endonuclease assay containing the MR complex, but lacking Nbs1 (Fig. 4A). Strikingly, the CT15 peptide stimulated the endonuclease activity of MR similarly to the unphosphorylated, full-length Ctp1 (Fig. 4B). Moreover, stimulation of MR at higher concentrations of the CT15 peptide (100 μM) was comparable to the maximal levels achieved with the MRN complex and phosphorylated full-length Ctp1 (Ctp1p in Fig. 4C).
PMID:33888556	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 17	(Figure 1B,C)
PMID:33888556	FYPO:0006425	normal meiotic sister chromatid cohesion at centromere during meiosis I	(Figure 1C)
PMID:33888556	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 12	(Figure 1C)
PMID:33888556	FYPO:0006425	normal meiotic sister chromatid cohesion at centromere during meiosis I	(Figure 1C)
PMID:33888556	FYPO:0006424	abolished meiotic sister chromatid cohesion at centromere during meiosis I	(Figure 1C)
PMID:33888556	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] ~4	(Figure 1C)
PMID:33888556	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II	(Figure 1C)
PMID:33888556	FYPO:0006426	normal attachment of spindle microtubules to kinetochore during meiosis I	(Figure 2A)
PMID:33888556	FYPO:0006424	abolished meiotic sister chromatid cohesion at centromere during meiosis I [has_penetrance] ~80	(Figure 2A) (comment: cohesion protection defect)
PMID:33888556	FYPO:0006424	abolished meiotic sister chromatid cohesion at centromere during meiosis I [has_penetrance] complete	(Figure 2D)
PMID:33888556	FYPO:0002219	normal chromosome disjunction at meiosis I	(Figure 2F)
PMID:33888556	FYPO:0007759	increased duration of meiotic sister chromatid cohesion at centromere during meiosis I	(Figure 3)
PMID:33888556	FYPO:0007760	decreased protein localization to kinetochore during meiotic prophase II	(Figure 3AB) vw repurposed this as it was essentially the same as the other annotation to this genotype (suggesting that Rec8-2A was properly expressed but not protected at centromeres during anaphase I.)
PMID:33888556	FYPO:0002219	normal chromosome disjunction at meiosis I	(Figure 3BC) Strikingly, the phenotype of rec8-2E was completely suppressed by sgo1Δ indicating that Rec8-2E was protected by Sgo1 not only at centromeres but also along the chromosome arm.
PMID:33888556	FYPO:0002060	viable vegetative cell population	(Figure 3D)
PMID:33888556	FYPO:0002060	viable vegetative cell population	(Figure 3D)
PMID:33888556	FYPO:0002061	inviable vegetative cell population	(Figure 3D) (comment: phosphomimetic rec8)
PMID:33888556	FYPO:0002061	inviable vegetative cell population	(Figure 3D) (comment: phosphomimetic rec8)
PMID:33888556	FYPO:0000678	unequal homologous chromosome segregation [has_penetrance] >90	(Figure 4)
PMID:33888556	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC29A10.14 [part_of] meiotic sister chromatid arm separation [happens_during] meiotic metaphase I	(Figure 4)
PMID:33888556	FYPO:0000678	unequal homologous chromosome segregation [has_penetrance] >90	(Figure 4) (comment: no rescue by sgo3)
PMID:33888556	FYPO:0007758	increased duration of mitotic sister chromatid cohesion [has_penetrance] high [has_severity] high	(comment: we modelled this increased duration of cohesion in mitotic anaphase, and the ectopic rec8 expression is now part of the genotype,does that sound OK?)
PMID:33888556	GO:0072542	protein phosphatase activator activity [has_input] PomBase:SPBC16H5.07c [part_of] meiotic centromeric cohesion protection in anaphase I [happens_during] meiotic anaphase I	To further examine this possibility, we reconstituted Rec8 dephosphorylation in vitro using immunoprecipitated Par1-containing PP2A complexes.
PMID:33888556	GO:0004722	protein serine/threonine phosphatase activity [has_input] PomBase:SPBC29A10.14 [part_of] meiotic centromeric cohesion protection in anaphase I [happens_during] meiotic anaphase I	To further examine this possibility, we reconstituted Rec8 dephosphorylation in vitro using immunoprecipitated Par1-containing PP2A complexes.
PMID:33888556	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC29A10.14 [part_of] meiotic centromeric cohesion protection in anaphase I [happens_during] meiotic anaphase I	refer to model in Figure 4. Therefore, consistent with the genetic analyses, this biochemical analysis supports the notion that phosphorylation at Rec8-S450 and the adjacent site plays a role in promoting the PP2A-dependent removal of CK1-dependent phosphorylation of Rec8 (Fig. 4B).
PMID:33909078	GO:0031278	alpha-1,2-galactosyltransferase activity [part_of] protein N-linked glycosylation	(comment: alpha-1,2-galactosylation of N-linked glycan)
PMID:33909078	GO:0031278	alpha-1,2-galactosyltransferase activity [part_of] protein N-linked glycosylation	(comment: alpha-1,2-galactosylation of N-linked glycan)
PMID:33909078	GO:0031278	alpha-1,2-galactosyltransferase activity [part_of] protein N-linked glycosylation	(comment: alpha-1,2-galactosylation of N-linked glycan)
PMID:33909078	GO:0031278	alpha-1,2-galactosyltransferase activity [part_of] protein O-linked glycosylation	(comment: alpha-1,2-galactosylation of O-linked glycan)
PMID:33909078	GO:0031278	alpha-1,2-galactosyltransferase activity [part_of] protein O-linked glycosylation	(comment: alpha-1,2-galactosylation of O-linked glycan)
PMID:33909078	GO:0001962	alpha-1,3-galactosyltransferase activity [part_of] protein O-linked glycosylation	(comment: alpha-1,3-galactosylation of O-linked glycan)
PMID:33909078	GO:0001962	alpha-1,3-galactosyltransferase activity [part_of] protein O-linked glycosylation	(comment: alpha-1,3-galactosylation of O-linked glycan)
PMID:33909078	GO:0001962	alpha-1,3-galactosyltransferase activity [part_of] protein O-linked glycosylation	(comment: alpha-1,3-galactosylation of O-linked glycan)
PMID:33925026	FYPO:0003022	resistance to nocodazole [has_severity] high	(comment: CHECK Assays were done in the MDR-sup (multi-drug resistance-suppressed) genetic background together with nda3-TB101)
PMID:33925026	FYPO:0005682	decreased microtubule depolymerization during vegetative growth [has_severity] medium [has_penetrance] medium	(comment: CHECK reduced frequency of microtubule catastrophe)
PMID:33925026	FYPO:0005681	decreased microtubule polymerization [has_severity] medium [has_penetrance] medium	(comment: CHECK reduced frequency of microtubule rescue)
PMID:33925026	FYPO:0000903	decreased rate of microtubule depolymerization during vegetative growth	(comment: CHECK same as alp14delta alone)
PMID:33925026	FYPO:0001355	decreased vegetative cell population growth	(comment: CHECK same as alp14delta alone)
PMID:33925026	FYPO:0005681	decreased microtubule polymerization	(comment: CHECK same as alp14delta alone)
PMID:33925026	FYPO:0005682	decreased microtubule depolymerization during vegetative growth	(comment: CHECK same as alp14delta alone)
PMID:33925026	FYPO:0005703	decreased rate of microtubule polymerization during vegetative growth	(comment: CHECK same as alp14delta alone)
PMID:33925026	FYPO:0005681	decreased microtubule polymerization	(comment: CHECK same as klp6delta alone)
PMID:33925026	FYPO:0005682	decreased microtubule depolymerization during vegetative growth	(comment: CHECK same as klp6delta alone)
PMID:33946513	FYPO:0002060	viable vegetative cell population	(Fig. 1)
PMID:33946513	FYPO:0002060	viable vegetative cell population	(Fig. 1a)
PMID:33946513	FYPO:0002060	viable vegetative cell population	(Fig. 1c) (comment: CHECK dri1 supresses cut7)
PMID:33946513	FYPO:0004456	increased protein localization to nucleus [assayed_protein] PomBase:SPAC17H9.04c	(Fig. S4a)
PMID:33946513	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_protein] PomBase:SPAC664.10	(Figure 2A,B)
PMID:33946513	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_protein] PomBase:SPAC664.10	(Figure 2A,B)
PMID:33946513	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC18G6.15	(Figure 2D)
PMID:33946513	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC18G6.15	(Figure 2D)
PMID:33946513	GO:0005737	cytoplasm [exists_during] mitotic interphase	(Figure 3A)
PMID:33946513	GO:0005737	cytoplasm [exists_during] mitotic M phase	(Figure 3A)
PMID:33946513	GO:0140453	protein aggregate center [exists_during] cellular response to heat	(Figure 4a)
PMID:33946513	FYPO:0002626	resistance to heat	(Figure 6) We found that the dri1∆ cells acquired tolerance to high temperature, as they could form colonies at 39 ◦C, whereas wild-type cells could not (Figure 6C).
PMID:33946513	FYPO:0002966	normal protein localization to mitotic spindle [assayed_protein] PomBase:SPAC18G6.15	(comment: CHECK SHOULD THIS BE NORMAL?) However, the Mal3 protein levels did not change in the presence or absence of Dri1 (Supplementary Figure S3A). Similarly, the levels of Mal3-GFP on the spindle MTs were almost the same both in wild-type and dri1∆ cells (Supplementary Figure S3B).
PMID:33946513	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPBC1734.11	(comment: CHECK to pac)
PMID:33946513	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPBC16D10.08c	(comment: CHECK to pac)
PMID:33946513	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPBC16D10.08c	(comment: CHECK to pac)
PMID:33946513	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPBC1734.11	(comment: CHECK to pac)
PMID:33946513	FYPO:0002966	normal protein localization to mitotic spindle [assayed_protein] PomBase:SPAC664.10	Klp2 levels on spindle microtubules were significantly lower than those in cut7-22 (which are increased compared to WT)
PMID:33946513	FYPO:0002966	normal protein localization to mitotic spindle [assayed_protein] PomBase:SPAC664.10	Klp2 levels on spindle microtubules were significantly lower than those in cut7-22 (which are increased compared to WT)
PMID:33970532	PomGeneEx:0000011	RNA level increased [during] cellular response to magnesium starvation	(comment: only amino acid auxotrophic cell)
PMID:33970532	FYPO:0007792	loss of viability upon magnesium starvation	(comment: only amino acid auxotrophic cell)
PMID:33970532	FYPO:0007792	loss of viability upon magnesium starvation	(comment: only amino acid auxotrophic cell)
PMID:33970532	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC70.12c	(comment: to capture target of ecl1)
PMID:33970532	FYPO:0007791	RNA absent from cell during cellular response to magnesium starvation	The control strain ED668 expressed ecl1+ when Mg2+ was depleted but not in a strain lacking fil1+ (Figure 2a)
PMID:34010645	FYPO:0007597	abolished CLRC complex binding	(Figure 2)
PMID:34010645	FYPO:0007597	abolished CLRC complex binding	(Figure 2)
PMID:34010645	FYPO:0007597	abolished CLRC complex binding	(Figure 2)
PMID:34010645	FYPO:0003234	normal histone H3-K9 methylation at heterochromatin domain during vegetative growth [assayed_region] dh_repeat	H3K9me3 levels at pericentric dh repeats and dh RNA levels in hht3-K9MK14R cells are similar to those in wild-type cells, comparing with hht3-K9M.
PMID:34019809	GO:0000822	inositol hexakisphosphate binding	(Fig. 2)
PMID:34019809	FYPO:0007841	decreased peptide alpha-N-acetyltransferase activity	(comment: CHECK fix catalytic activity)
PMID:34019809	FYPO:0007841	decreased peptide alpha-N-acetyltransferase activity	(comment: CHECK fix catalytic activity)
PMID:34028542	FYPO:0002674	normal protein localization to plasma membrane [assayed_protein] PomBase:SPCC1235.14	(Fig. 1) (comment: aly3 rescues)
PMID:34028542	PomGeneEx:0000013	RNA level unchanged [during] cellular response to glucose starvation	(Fig. 5)
PMID:34028542	FYPO:0002082	increased protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPCC1235.14	(Fig. 6)
PMID:34028542	FYPO:0002082	increased protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPCC1235.14	(Fig. 6)
PMID:34028542	FYPO:0002635	normal protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPCC1235.14	(Fig. 6) (comment: phenocopies WT)
PMID:34028542	GO:1990756	ubiquitin-like ligase-substrate adaptor activity [has_input] PomBase:SPCC1235.14 [part_of] clathrin-dependent endocytosis	(comment: although not shown directly , genetic interactions are consistent with this activity)
PMID:34028542	GO:0043609	regulation of carbon utilization [happens_during] cellular response to nitrogen starvation	(comment: negative)
PMID:34028542	PomGeneEx:0000011	RNA level increased [during] cellular response to nitrogen starvation	After cultivation in low glucose MM for 10 h, medium was replaced with low-glucose nitrogen-starved MM, and cells were further cultivated for 4 h.
PMID:34028542	FYPO:0004839	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during glucose starvation [assayed_protein] PomBase:SPCC1235.14	Cytoplasmic Ght5-GFP was observed within the vacuolar membrane stained with FM4-64.
PMID:34028542	FYPO:0003743	decreased cell population growth during glucose starvation	Proliferation defect of gad8ts aly1 mutant in low glucose was similar to that of gad8ts mutant.
PMID:34028542	FYPO:0003743	decreased cell population growth during glucose starvation	Proliferation defect of gad8ts aly2 mutant in low glucose was similar to that of gad8ts mutant.
PMID:34028542	FYPO:0000047	normal cell population growth	Proliferation defect of gad8ts mutant in low glucose was restored by SPCC584.15c deletion.
PMID:34028542	FYPO:0003743	decreased cell population growth during glucose starvation	Proliferation defect of gad8ts rod1 mutant in low glucose was similar to that of gad8ts mutant.
PMID:34028542	MOD:01148	ubiquitinylated lysine [present_during] cellular response to glucose starvation	top panel, Fig. 6A; Fig. S3B,C).
PMID:34067465	PomGeneEx:0000018	protein level increased [during] meiotic S phase	(Fig. 1C)
PMID:34067465	PomGeneEx:0000018	protein level increased [during] meiotic prophase I	(Fig. 1C)
PMID:34067465	PomGeneEx:0000018	protein level increased [during] meiosis I cell cycle phase	(Fig. 1C)
PMID:34067465	FYPO:0002043	normal premeiotic DNA replication	(Fig. 4 and Fig. S2)
PMID:34067465	FYPO:0004801	delayed onset of premeiotic DNA replication during azygotic meiosis [has_severity] high	(Fig. 4 and Fig. S2)
PMID:34067465	FYPO:0004801	delayed onset of premeiotic DNA replication during azygotic meiosis [has_severity] high	(Fig. 4 and Fig. S2)
PMID:34067465	FYPO:0004801	delayed onset of premeiotic DNA replication during azygotic meiosis [has_severity] medium	(Fig. 4 and Fig. S2)
PMID:34067465	FYPO:0004605	decreased distance travelled by the spindle pole body during horsetail movement [has_severity] low	(Fig. 7, Fig. S4 and Fig. S5)
PMID:34067465	FYPO:0008310	unstable meiotic telomere clustering [has_severity] low	(Fig. 7, Fig. S4 and Fig. S5)
PMID:34067465	FYPO:0008313	normal meiotic spindle pole body insertion into nuclear envelope in meiosis I	(Fig. 8)
PMID:34067465	FYPO:0008314	normal initial meiotic spindle pole body separation in meiosis I	(Fig. 8)
PMID:34067465	FYPO:0008311	normal protein localization to meiotic spindle pole body during prophase I [assayed_protein] PomBase:SPBC2G2.09c	(Fig. S6)
PMID:34067465	GO:0005654	nucleoplasm [exists_during] meiotic prophase I	In some nuclei, a diffuse pan-nuclear signal was also detected. (Fig. 5)
PMID:34067465	GO:0035974	meiotic spindle pole body	These data indicate that the localization of the Crs1-GFP cyclin during meiosis is similar to that of a SPB component. (Fig. 5)
PMID:34080538	FYPO:0007304	short bipolar mitotic spindle during anaphase	(Fig. 4)
PMID:34080538	FYPO:0007304	short bipolar mitotic spindle during anaphase	(Fig. 4)
PMID:34080538	FYPO:0004635	increased protein localization to mitotic spindle [assayed_protein] PomBase:SPBC15D4.01c	(Fig. 4)
PMID:34080538	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B	(Fig. 4)
PMID:34080538	FYPO:0005706	increased duration of mitotic anaphase B	(Fig. 4)
PMID:34080538	FYPO:0004833	decreased protein localization to mitotic spindle midzone during anaphase B [assayed_protein] PomBase:SPBC15D4.01c	(Fig. 4)
PMID:34080538	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B	(Fig. 4)
PMID:34080538	FYPO:0005706	increased duration of mitotic anaphase B	(Fig. 4)
PMID:34080538	FYPO:0007865	normal protein localization to spindle [assayed_protein] PomBase:SPCC736.14	(Fig. 4)
PMID:34080538	GO:0005654	nucleoplasm [exists_during] single-celled organism vegetative growth phase	(Fig. 4)
PMID:34080538	GO:1990023	mitotic spindle midzone [exists_during] mitotic anaphase B	(Fig. 4)
PMID:34080538	FYPO:0007304	short bipolar mitotic spindle during anaphase	(Fig. 4)
PMID:34080538	FYPO:0005706	increased duration of mitotic anaphase B	(Fig. 4)
PMID:34080538	FYPO:0005343	decreased rate of mitotic spindle elongation during anaphase B	(Fig. 4)
PMID:34080538	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_protein] PomBase:SPBC15D4.01c	(Fig. 5 Supp 3)
PMID:34080538	FYPO:0002966	normal protein localization to mitotic spindle [assayed_protein] PomBase:SPCC736.14	(Fig. 5 Supp 3)
PMID:34080538	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_protein] PomBase:SPBC15D4.01c	(Fig. 5)
PMID:34080538	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_protein] PomBase:SPBC15D4.01c	(Fig. 5)
PMID:34080538	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_protein] PomBase:SPBC15D4.01c	(Fig. 5)
PMID:34080538	FYPO:0003349	normal protein localization to mitotic spindle midzone during anaphase B [assayed_protein] PomBase:SPBC15D4.01c	(Fig. 5)
PMID:34080538	GO:0097431	mitotic spindle pole [exists_during] mitotic anaphase B	(Fig. 5) (comment: Dephosph form)
PMID:34080538	GO:1990537	mitotic spindle polar microtubule [exists_during] mitotic anaphase B	(Fig. 5) (comment: Dephosph form)
PMID:34080538	GO:0000776	kinetochore [exists_during] mitotic prometaphase	(Fig. 5) (comment: Phosph form) ((comment: From other publications, we know bona-fide that the localisation observed here is the kinetochore but here they study how it changes)
PMID:34086083	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC359.06	(comment: ALERTED FROM A LATER PAPER) Rst2 regulates the expression of ste11, which encodes a transcription factor to regulate sexual development (Sugimoto et al. 1991); fbp1, which encodes fructose-1,6-bisphosphatase (Hoffman and Winston 1990); and mug14, which encodes an adducin homolog (Inamura et al. 2021).
PMID:34086083	GO:0005634	nucleus	(comment: CHECK YES, YES (low-glucose))
PMID:34086083	GO:0005737	cytoplasm	(comment: CHECK YES, YES (low-glucose))
PMID:34119521	FYPO:0000562	abolished cellular respiration	Deletion of the PPR motifs in Ppr10 moderately affected the growth of S. pombe cells on glucose-containing media but severely impaired the growth on glycerol-containing media (Fig. 1E)
PMID:34119521	FYPO:0008315	normal mitochondrial ribosome assembly	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) a
PMID:34119521	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC2F7.15	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC1271.15c	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC18E5.13	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC1105.03c	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC4G9.17c	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC4F8.02c	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC1271.15c	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC1105.03c	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC4G9.17c	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC2F7.15	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC18E5.13	Disruption of ppr10, mpa1, or the PPR motifs of Ppr10 did not impair the assembly of mitoribosomes or their subunits (Fig. 2, A-D) and did not affect the steady-state levels of the protein subunits of the mt-SSU and mt-LSU (Fig. 2E).
PMID:34119521	GO:0070124	mitochondrial translational initiation	Taken together, these data reveal that the PPR motifs in Ppr10 are critical for the Ppr10-Mpa1 interaction and that disruption of the PPR motifs in Ppr10 impairs mitochondrial protein synthesis and, consequently, respiratory growth of S. pombe cells.
PMID:34119521	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBP4H10.15	The PPR motifs of Ppr10 are not involved in the association of Ppr10 with a subset of mitoribosomal proteins
PMID:34119521	FYPO:0007525	decreased ribosome binding [assayed_protein] PomBase:SPMIT.01	The association of cob1 and cox1 mRNAs with assembled mitoribosomes was reduced by ppr10 deletion, whereas their association with the mt-SSU was increased (Fig. 3).
PMID:34119521	FYPO:0007525	decreased ribosome binding [assayed_protein] PomBase:SPMIT.05	The association of cob1 and cox1 mRNAs with assembled mitoribosomes was reduced by ppr10 deletion, whereas their association with the mt-SSU was increased (Fig. 3).
PMID:34119521	FYPO:0000705	abolished protein-protein interaction	The level of Ppr10ΔPPR-Myc is reduced compared with that of WT protein (Fig. 1B). We found that only the full-length Ppr10-Myc coimmunoprecipitated with Mpa1 from whole-cell extract, whereas the mutant Ppr10 did not (Fig. 1C).
PMID:34119521	FYPO:0008316	abnormal mitochondrial translation initiation complex assembly	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU (Fig. 2, B-D).
PMID:34119521	FYPO:0008316	abnormal mitochondrial translation initiation complex assembly	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU (Fig. 2, B-D).
PMID:34119521	FYPO:0008316	abnormal mitochondrial translation initiation complex assembly	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU (Fig. 2, B-D).
PMID:34119521	FYPO:0007525	decreased ribosome binding [assayed_protein] PomBase:SPBC18E5.13	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU and reduced the association of Mti2 and Mti3 with mitoribosomes (Fig. 2, B-D).
PMID:34119521	FYPO:0007525	decreased ribosome binding [assayed_protein] PomBase:SPBC1271.15c	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU and reduced the association of Mti2 and Mti3 with mitoribosomes (Fig. 2, B-D).
PMID:34119521	FYPO:0007525	decreased ribosome binding [assayed_protein] PomBase:SPBC1271.15c	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU and reduced the association of Mti2 and Mti3 with mitoribosomes (Fig. 2, B-D).
PMID:34119521	FYPO:0007525	decreased ribosome binding [assayed_protein] PomBase:SPBC18E5.13	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU and reduced the association of Mti2 and Mti3 with mitoribosomes (Fig. 2, B-D).
PMID:34119521	FYPO:0007525	decreased ribosome binding [assayed_protein] PomBase:SPBC18E5.13	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU and reduced the association of Mti2 and Mti3 with mitoribosomes (Fig. 2, B-D).
PMID:34119521	FYPO:0007525	decreased ribosome binding [assayed_protein] PomBase:SPBC1271.15c	We consistently found that disruption of ppr10, mpa1, or the PPR motifs of Ppr10 resulted in dissociation of Mti2 and Mti3 from the mt-SSU and reduced the association of Mti2 and Mti3 with mitoribosomes (Fig. 2, B-D).
PMID:34119521	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.01	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cytochrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP synthase) (Fig. 1D).
PMID:34119521	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.04	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cytochrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP synthase) (Fig. 1D).
PMID:34119521	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.07	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cytochrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP synthase) (Fig. 1D).
PMID:34119521	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.11	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cytochrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP synthase) (Fig. 1D).
PMID:34119521	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.05	deletion of PPR motifs in Ppr10 severely reduced the steady-state levels of Cob1 (subunit of the cytochrome bc 1 complex), the core subunits of cytochrome c oxidase (Cox1, Cox2, Cox3), and Atp6 (subunit of ATP synthase) (Fig. 1D).
PMID:34133210	PomGeneEx:0000024	protein level fluctuates [during] mitotic cell cycle phase	(Fig. 1)
PMID:34133210	FYPO:0007829	premature protein localization to cell division site	(Figure 4, A and B)
PMID:34133210	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPBC4F6.12 [part_of] negative regulation of exit from mitosis	(comment: although not IDA, there is experimental data to support this inference)
PMID:34133210	FYPO:0007828	normal actomyosin contractile ring maturation	Although there was a small difference in CR formation between pxl1(9A) (13.6 +/- 2.5; 33 cells) and pxl1(9D) (12.2 +/- 2.3 min; 41 cells), formation was similar in pxl1(9D) and pxl1+ (12.4 +/- 3.0; 32 cells), and there were no significant differences in the durations of CR maturation.
PMID:34133210	FYPO:0001368	normal actomyosin contractile ring assembly	Although there was a small difference in CR formation between pxl1(9A) (13.6 +/- 2.5; 33 cells) and pxl1(9D) (12.2 +/- 2.3 min; 41 cells), formation was similar in pxl1(9D) and pxl1+ (12.4 +/- 3.0; 32 cells), and there were no significant differences in the durations of CR maturation.
PMID:34133210	GO:1990808	F-bar domain binding [occurs_in] mitotic actomyosin contractile ring	Cdk1 phosphorylation of Pxl1 reduced binding to the F-BAR domain of Cdc15 (Figure 5A), but not to Cdc15C (Figure 5B).
PMID:34133210	FYPO:0005543	increased duration of actomyosin contractile ring contraction	Constriction took longer in pxl1(9A)
PMID:34147496	GO:0006799	polyphosphate biosynthetic process	(comment: inferred from polyphosphate absent from cell)
PMID:34147496	GO:0061630	ubiquitin protein ligase activity [part_of] regulation of phosphate transmembrane transport [has_input] PomBase:SPBC8E4.01c	These results imply that: (1) Pho84 is multiply ubiquitinated; (2) ubiquitination of Pho84 depends mainly on Pqr1.
PMID:34169534	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBP35G2.11c [assayed_protein] PomBase:SPAC4F10.02	(comment: also assayed using Pil1 co-tethering with microscopy)
PMID:34169534	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBP35G2.11c [assayed_protein] PomBase:SPAC513.05	(comment: also assayed using Pil1 co-tethering with microscopy)
PMID:34198697	FYPO:0000079	sensitive to caspofungin	(Figure 1B)
PMID:34198697	FYPO:0005969	resistance to magnesium chloride	(Figure 1B)
PMID:34198697	FYPO:0007521	resistance to tacrolimus and magnesium chloride	(Figure 1B) (comment: This phenotype is known as “VIC” viable in the presence of immunosuppressant and chloride ion)
PMID:34198697	FYPO:0004295	multiseptate cell [has_penetrance] >20	(Figure 1a)
PMID:34198697	MOD:00047	O-phospho-L-threonine [increased_during] cellular response to stress	(comment: Cell wall damage induced with caspofungin)
PMID:34209806	GO:0005681	spliceosomal complex	(comment: Need to curate ref42 for earlier part of this story, but this can be. inferred here from the interactions)
PMID:34209806	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC20F10.05 [assayed_protein] PomBase:SPAC17H9.02	The interactions of the Nrl1(NRDE-2) and the Nrl1(C-term) domain constructs with Mtl1 were significantly lower
PMID:34209806	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC20F10.05 [assayed_protein] PomBase:SPAC17H9.02	We observed similar intensities of interaction of the Nrl1(N-term) and the Nrl1(N-term + NRDE-2) constructs with Mtl1 (1511.2 ± 89.4 or 1558.2 ± 159.3 Miller units for the N-terminal region and the N-terminus with NRDE2 domain and Mtl1, respectively)
PMID:34209806	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC20F10.05 [assayed_protein] PomBase:SPAC17H9.02	We observed similar intensities of interaction of the Nrl1(N-term) and the Nrl1(N-term + NRDE-2) constructs with Mtl1 (1511.2 ± 89.4 or 1558.2 ± 159.3 Miller units for the N-terminal region and the N-terminus with NRDE2 domain and Mtl1, respectively)
PMID:34228709	FYPO:0000173	abnormal mitotic cell cycle DNA replication checkpoint	(comment: CHECK Cds1 is partially phosphorylated)
PMID:34228709	FYPO:0001707	increased mitotic DNA damage checkpoint activation	(comment: CHECK Chk1 is partially phosphorylated)
PMID:34228709	FYPO:0005032	normal mutation rate	(comment: equivalent substitution to cdc20-P287R)
PMID:34228709	FYPO:0003923	decreased rate of mitotic DNA replication elongation	(comment: evidence: DNA combing)
PMID:34228709	FYPO:0000256	mutator [has_severity] medium	(comment: hypermutator)
PMID:34250083	FYPO:0001309	increased viability in stationary phase	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:34250083	FYPO:0001309	increased viability in stationary phase	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:34250083	FYPO:0001309	increased viability in stationary phase	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:34250083	FYPO:0000245	loss of viability in stationary phase	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:34250083	FYPO:0000245	loss of viability in stationary phase	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:34250083	FYPO:0000245	loss of viability in stationary phase	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:34250083	FYPO:0000245	loss of viability in stationary phase	(comment: Phenotype determined with robotics-based CFU assay.)
PMID:3428262	FYPO:0003095	viable elongated vegetative cell, with progressive elongation	(comment: CHECK mitotic G2/M transition delay)
PMID:34292936	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: worse than rad51delta alone)
PMID:34292936	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] high	(comment: worse than rad51delta alone)
PMID:34296454	FYPO:0005193	resistance to torin1 [has_severity] medium	(Fig. 5E, 5F) from paper for partial inhibition protein synthesis phenotype
PMID:34296454	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPAC13G6.07c	For the Torin1-resistant mutant, the phosphorylation levels remained constant throughout the time course
PMID:34296454	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPAC13G6.07c	For the Torin1-resistant mutant, the phosphorylation levels remained constant throughout the time course
PMID:34296454	FYPO:0007877	normal regulation of translation in response to chemical	This result indicates that the immediate decrease in protein synthesis rates upon TOR inhibition is not dependent upon the S6Ks or their downstream targets.
PMID:34296454	GO:2000767	positive regulation of cytoplasmic translation	hese observations are consistent with the idea that the essential TORC1 is the major complex responsible for the rapid inhibition of protein synthesis and that changes in phosphorylation levels relevant to regulating protein synthesis should be detectable within 20 min and significant by 40 min of TOR inhibition.
PMID:34309513	GO:0140588	chromatin looping	(comment: CHECK in vitro) (Figure 4A, Video 1).
PMID:34309513	GO:0140588	chromatin looping	(comment: CHECK in vitro) (Figure 4A, Video 1).
PMID:34309513	GO:0140588	chromatin looping	(comment: CHECK in vitro) (Figure 4A, Video 1).
PMID:34309513	GO:0140588	chromatin looping	(comment: CHECK in vitro) (Figure 4A, Video 1).
PMID:34309513	GO:0140588	chromatin looping	(comment: CHECK in vitro) (Figure 4A, Video 1).
PMID:34309513	GO:0140588	chromatin looping	(comment: CHECK in vitro) (Figure 4A, Video 1).
PMID:34346498	FYPO:0006455	abolished protein localization to meiotic spindle during meiosis I [has_penetrance] high [assayed_protein] PomBase:SPBC12D12.01	(Figure 1)
PMID:34346498	FYPO:0007851	abolished spindle assembly during meiosis I [has_penetrance] 20	(Figure 1) (comment: see above)
PMID:34346498	FYPO:0004764	normal protein localization to meiotic spindle pole body during meiosis I [assayed_protein] PomBase:SPBC12D12.01	(Figure 1) (comment: see above)
PMID:34346498	GO:0035974	meiotic spindle pole body [exists_during] meiotic M phase	(Figure 2)
PMID:34346498	FYPO:0007103	spindle collapse during meiosis I [has_penetrance] 80	(Figure 2E)
PMID:34346498	FYPO:0007103	spindle collapse during meiosis I [has_penetrance] 50	(Figure 2E)
PMID:34346498	FYPO:0007755	short meiotic spindle during metaphase I	(Figure 2F)
PMID:34346498	FYPO:0007846	short meiotic spindle during anaphase I	(Figure 2F)
PMID:34346498	FYPO:0007849	spindle self-assembly during meiosis I	(Figure 2F)
PMID:34346498	FYPO:0007852	normal meiotic spindle polarity	(Figure 3)
PMID:34346498	FYPO:0007750	normal protein localization to meiotic spindle during meiosis I [has_penetrance] high [assayed_protein] PomBase:SPAC3A11.14c	(Figure 3A)
PMID:34346498	FYPO:0007849	spindle self-assembly during meiosis I [has_penetrance] 80	(Figure 5) To confirm this, we evaluatedthe behaviour of bqt1Δ sad1.2 alp4-GFP cells harbouring the SPBmarkers Sid4-mCherry and Sad1.2-mCherry, effectively showingthat Alp4-GFP molecules located far from the nucleus wereassociated with the SPBs (Fig. 5C,D)
PMID:34346498	FYPO:0007864	abolished protein localization to meiotic spindle pole during meiosis I	(Figure 5) To confirm this, we evaluatedthe behaviour of bqt1Δ sad1.2 alp4-GFP cells harbouring the SPBmarkers Sid4-mCherry and Sad1.2-mCherry, effectively showingthat Alp4-GFP molecules located far from the nucleus wereassociated with the SPBs (Fig. 5C,D)
PMID:34346498	FYPO:0006391	meiotic spindle absent from cell during meiosis [has_penetrance] 70	(Figure 6) Remarkably, we found that, in the case of bqt1Δ sad1.2 alp14-26 meiocytes, despite clear dysfunction of alp14-26, self-assembled spindles were still able to form and behaved normally (Fig. 6C,D). However, they formed in a smaller percentage of meiocytes (from ∼80% to ∼30%, Fig. 6F), indicating that the contribution of Alp14 to self-assembled spindle formation and behaviour is substantial.
PMID:34346498	FYPO:0003614	meiotic spindle absent from cell during meiosis II	(Figure 6B)
PMID:34346498	FYPO:0004394	lagging chromosomes during meiosis II [has_severity] high	(Figure 7)
PMID:34346498	FYPO:0004393	lagging chromosomes during meiosis I [has_severity] high	(Figure 7)
PMID:34346498	FYPO:0007849	spindle self-assembly during meiosis I [has_penetrance] 67	(Figure 7) maximum length of self-assembled spindles increased upon deletion of klp6 (from 7.9±3.8 μm to 12.9±4.7 μm; Fig. 7E).
PMID:34346498	FYPO:0007847	long meiosis I spindle [has_severity] medium	(Figure 7) maximum length of self-assembled spindles increased upon deletion of klp6 (from 7.9±3.8 μm to 12.9±4.7 μm; Fig. 7E).
PMID:34346498	FYPO:0000678	unequal homologous chromosome segregation [has_penetrance] 68	(Figure 7C)
PMID:34346498	FYPO:0000678	unequal homologous chromosome segregation [has_penetrance] 39	(Figure 7C)
PMID:34346498	FYPO:0000678	unequal homologous chromosome segregation [has_penetrance] 53	(Figure 7C)
PMID:34346498	FYPO:0003379	abolished meiosis II [has_penetrance] medium	(comment: CHECK decreased abnormal SPB-independent meiosis II)
PMID:34346498	GO:0051232	meiotic spindle elongation [happens_during] meiotic M phase	(comment: late spindle elongation (move down /when GO reflect stages of meiotic spindle elongation))
PMID:34346498	FYPO:0007849	spindle self-assembly during meiosis I	analysis of bqt1Δ sad1.2 dis1Δ meiocytes showed that the percentage of selfassembled spindles with normal formation and function was similar to that in the bqt1Δ sad1.2 setting (Fig. 6F,H).
PMID:34349749	FYPO:0002637	normal growth on hygromycin B [has_severity] medium	(Figure 3C)
PMID:34349749	FYPO:0007717	sensitive to potassium nitrate [has_severity] high	(Figure 5.)
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] high	(Figure 5.)
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] high	(Figure 5.)
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] medium	(Figure 5.)
PMID:34349749	FYPO:0007717	sensitive to potassium nitrate [has_severity] high	(Figure 5.)
PMID:34349749	FYPO:0007717	sensitive to potassium nitrate [has_severity] high	(Figure 5C)
PMID:34349749	FYPO:0007717	sensitive to potassium nitrate [has_severity] medium	(Figure 5C)
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 5C)
PMID:34349749	FYPO:0007717	sensitive to potassium nitrate [has_severity] high	(Figure 5C)
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 5C)
PMID:34349749	FYPO:0005947	normal growth on potassium chloride	(Figure 5C))
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 7A). erg51 bch11 was more sensitive than the single mutants
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 7A). erg51 bch11 was more sensitive than the single mutants
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] medium	(Figure 8) All mutants exhibited a degree of sensitivity to hygromycin B that was alleviated by KCl, an indication of membrane hyperpolarization.
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] low	(Figure 8) All mutants exhibited a degree of sensitivity to hygromycin B that was alleviated by KCl, an indication of membrane hyperpolarization.
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] medium	(Figure 8) All mutants exhibited a degree of sensitivity to hygromycin B that was alleviated by KCl, an indication of membrane hyperpolarization.
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] high	(Figure 8) All mutants exhibited a degree of sensitivity to hygromycin B that was alleviated by KCl, an indication of membrane hyperpolarization.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] low	(Figure 8) We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by ggadeltadelta in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] low	(Figure 8) We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by ggadeltadelta in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] low	(Figure 8) We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by ggadeltadelta in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] low	(Figure 8) We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by ggadeltadelta in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] low	(Figure 8) We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by ggadeltadelta in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	FYPO:0001020	normal growth on calcium	(Figure 8) gga22delta, which was the only mutant that grew on CaCl2 plates as efficiently as the WT.
PMID:34349749	FYPO:0001020	normal growth on calcium	(Figure S4)
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Supplementary Figure 4).
PMID:34349749	FYPO:0004203	increased calcium import	A close observation of the results indicated that under basal conditions (0′), the WT amount of GFP was significantly greater in cfr11 than in the WT, which suggested increased intracellular Ca2 + . | However, in cfr11 cells the amount of Ca2+ continued increasing for another 15 min, and reached a peak that was more than three-fold the value of the baseline (Figure 5B). The maximum Ca2+ level in cfr11 was 67% higher than in the WT | To understand whether the cytoplasmic calcium increase was produced by influx from the exterior or by movements from internal reservoirs, we analyzed the Ca2+ level in the presence of EGTA. We found that the presence of the chelator in the medium completely blocked the increase in Ca2+ levels in both the WT and the mutant cells (Figure 5B). In summary, we concluded that Cfr1 modulated the cellular Ca2+ response to KCl stress by regulating some aspect of Ca2 + influx.
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] high	All mutants exhibited a degree of sensitivity to hygromycin B that was alleviated by KCl, an indication of membrane hyperpolarization.
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] high	All mutants exhibited a degree of sensitivity to hygromycin B that was alleviated by KCl, an indication of membrane hyperpolarization.
PMID:34349749	FYPO:0005947	normal growth on potassium chloride	As shown in Supplementary Figure 4, their deletion neither produced sensitivity to KCl nor enhanced the sensitivity of bch1delta
PMID:34349749	FYPO:0005947	normal growth on potassium chloride	As shown in Supplementary Figure 4, their deletion neither produced sensitivity to KCl nor enhanced the sensitivity of bch1delta
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] high	Conversely, double mutants were more sensitive to CaCl2 than single mutants. (Figure S4)
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] high	Conversely, double mutants were more sensitive to CaCl2 than single mutants. (Figure S4)
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] high	Conversely, double mutants were more sensitive to CaCl2 than single mutants. (Figure S4)
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] high	Conversely, double mutants were more sensitive to CaCl2 than single mutants. (Figure S4)
PMID:34349749	FYPO:0008348	increased protein localization to pre-vacuolar endosome [assayed_protein] PomBase:SPAC1F7.03	Exposure to KCl resulted in a small but significant change in Pkd2 distribution, with a reduction in the number of dots that corresponded to the TGN and an increase in the number of dots that corresponded to the PVE. Pkd2 accumulation in the PVE in the presence of KCl was stronger in cfr11 than in the WT. Thus, the effect of potassium in Pkd2 intracellular distribution was enhanced by exomer deletion.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	First, we determined whether cfr1delta sensitivity to high KCl concentrations was due to an inability to grow under ionic or osmotic stress. To do so, we analyzed cfr11 sensitivity to several potassium salts at different concentrations, which depended on the concentration that inhibited the growth of the WT, and to sorbitol (Figure 1A). cfr11 exhibited growth defects in the presence of 0.6 M potassium chloride (KCl), 0.6 M potassium nitrate (KNO3), and 0.02 M potassium acetate (CH3 CO2 K). cfr11 exhibited growth defects in the presence of 0.6 M potassium chloride (KCl), 0.6 M potassium nitrate (KNO3), and 0.02 M potassium acetate (CH3 CO2 K). |Interestingly, deleting cch1+ suppressed cfr1delta sensitivity to CaCl2 (Supplementary Figure 4).
PMID:34349749	FYPO:0002674	normal protein localization to plasma membrane [assayed_protein] PomBase:SPAC3F10.02c	GFP-Trk1 localized at the cell surface of the cell growing sites (cell poles and equator) in both, WT and cfr11 cells (Figure 2B), confirming proper Trk1 sorting in the absence of exomer.
PMID:34349749	GO:0032178	medial membrane band	GFP-Trk1 localized at the cell surface of the cell growing sites (cell poles and equator) in both, WT and cfr11 cells (Figure 2B), confirming proper Trk1 sorting in the absence of exomer. (combined with existing knowledge)
PMID:34349749	GO:0031520	plasma membrane of cell tip	GFP-Trk1 localized at the cell surface of the cell growing sites (cell poles and equator) in both, WT and cfr11 cells (Figure 2B), confirming proper Trk1 sorting in the absence of exomer. (combined with existing knowledge)
PMID:34349749	FYPO:0008347	increased protein localization to trans-Golgi network [assayed_protein] PomBase:SPAC1F7.03	In addition, there was intracellular Pkd2-GFP fluorescence. All cells exhibited a faint signal that corresponded to the vacuoles, which in S. pombe are small and numerous, and some cells exhibited at least one bright intracellular dot (denoted by an arrow in Figure 5D). In the WT, less than 20% of the cells exhibited bright intracellular dots, while this number was over 40% in cfr11 (Figure 5F). This difference was evident in the absence of KCl, showing that it was produced by a lack of exomer. Moreover, the dots were brighter in the mutant than in the control (Figure 5G). Western blotting showed that stronger fluorescence was not due to higher levels of the protein (Figure 5H). Quantitative colocalization analyses showed that most of these dots corresponded to the TGN and that fewer dots corresponded to the PVE (Figure 5I and Supplementary Figure 3).
PMID:34349749	FYPO:0000961	normal growth on sorbitol	In contrast, the mutant grew well in the presence of 1.2 M sorbitol, a medium with similar osmolarity to 0.6 M KCl.
PMID:34349749	FYPO:0000135	abnormal plasma membrane sterol distribution [has_severity] medium	In summary, in the absence of exomer and in the presence of KCl, the distribution of sterols and PI(4,5)P2 was different from that of the WT, which might contribute to altered membrane polarization and ion homeostasis in the mutant.
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] medium	Interestingly, deleting cch1+ suppressed cfr1delta sensitivity to CaCl2 (Supplementary Figure 4).
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] low	Interestingly, deleting cch1+ suppressed cfr1delta sensitivity to CaCl2 (Supplementary Figure 4).
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] low	Interestingly, deleting cch1+ suppressed cfr1delta sensitivity to CaCl2 (Supplementary Figure 4).
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] medium	Interestingly, deleting cch1+ suppressed cfr1delta sensitivity to CaCl2 (Supplementary Figure 4).
PMID:34349749	FYPO:0005947	normal growth on potassium chloride	Nonetheless, we compared the growth of trk1delta and trk2delta with that of cfr1delta in the presence of high K+ concentrations. Additionally, we constructed double and triple mutants to determine whether cfr1+ acts in the same functional pathways as trk1+ and/or trk2+. The results showed that while cfr11 was sensitive to potassium salts, neither trk11, trk21 nor trk11 trk21 (denoted by trk11 in the figure) exhibited sensitivity (Figure 2A).
PMID:34349749	FYPO:0005947	normal growth on potassium chloride	Nonetheless, we compared the growth of trk1delta and trk2delta with that of cfr1delta in the presence of high K+ concentrations. Additionally, we constructed double and triple mutants to determine whether cfr1+ acts in the same functional pathways as trk1+ and/or trk2+. The results showed that while cfr11 was sensitive to potassium salts, neither trk1delta, trk2delta nor trk1delta trk2delta exhibited sensitivity (Figure 2A).
PMID:34349749	FYPO:0005947	normal growth on potassium chloride	Nonetheless, we compared the growth of trk1delta and trk2delta with that of cfr1delta in the presence of high K+ concentrations. Additionally, we constructed double and triple mutants to determine whether cfr1+ acts in the same functional pathways as trk1+ and/or trk2+. The results showed that while cfr1delta was sensitive to potassium salts, neither trk1delta, trk2delta nor trk1delta trk2delta exhibited sensitivity (Figure 2A).
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] low	Regarding double mutants, trk1delta cfr1delta was more sensitive than cfr1delta, indicating that both genes cooperated and acted in parallel rather than in linear pathways related to K+ sensitivity.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] low	Regarding double mutants, trk1delta cfr1delta was more sensitive than cfr1delta, indicating that both genes cooperated and acted in parallel rather than in linear pathways related to K+ sensitivity.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	Regarding double mutants, trk1delta cfr1delta was more sensitive than cfr1delta, indicating that both genes cooperated and acted in parallel rather than in linear pathways related to K+ sensitivity.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	Regarding double mutants, trk1delta cfr1delta was more sensitive than cfr1delta, indicating that both genes cooperated and acted in parallel rather than in linear pathways related to K+ sensitivity.
PMID:34349749	GO:0031520	plasma membrane of cell tip	Regarding protein localization, microscopy observation showed that 1 h after the addition of KCl most Cta3-GFP accumulated at the cell periphery of the sites of polarized growth (cell poles and equator), and that the intensity of the fluorescence in this location was similar in WT and mutant cells (Figure 4E and Supplementary Figure 2).
PMID:34349749	GO:0032178	medial membrane band	Regarding protein localization, microscopy observation showed that 1 h after the addition of KCl most Cta3-GFP accumulated at the cell periphery of the sites of polarized growth (cell poles and equator), and that the intensity of the fluorescence in this location was similar in WT and mutant cells (Figure 4E and Supplementary Figure 2).
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] low	Since Cta3 was originally described as an ATP-dependent Ca2+ pump (Ghislain et al., 1990; Halachmi et al., 1992), we also analyzed growth on CaCl2 plates and found that cta3delta was only sensitive to high calcium concentrations, and only in the absence of the Tup regulators.
PMID:34349749	FYPO:0001020	normal growth on calcium	Since Cta3 was originally described as an ATP-dependent Ca2+ pump (Ghislain et al., 1990; Halachmi et al., 1992), we also analyzed growth on CaCl2 plates and found that cta3delta was only sensitive to high calcium concentrations, and only in the absence of the Tup regulators.
PMID:34349749	GO:0006874	intracellular calcium ion homeostasis	Taken together, these experiments showed that calcium homeostasis was altered in exomer mutants, that small defects in the transport of Pkd2 might contribute to this alteration, and that Cch1 facilitates a calcium import that is deleterious for exomer mutants.
PMID:34349749	GO:0006874	intracellular calcium ion homeostasis	Taken together, these experiments showed that calcium homeostasis was altered in exomer mutants, that small defects in the transport of Pkd2 might contribute to this alteration, and that Cch1 facilitates a calcium import that is deleterious for exomer mutants.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] low	The phenotype of trk1delta trk2delta cfr1delta was similar to that of trk2delta cfr1delta.
PMID:34349749	FYPO:0007717	sensitive to potassium nitrate [has_severity] high	The result was that overexpression of the extrusion pump alleviated the growth of cfr11 in the presence of high K+ concentrations (Figure 4C).
PMID:34349749	FYPO:0007717	sensitive to potassium nitrate [has_severity] low	The result was that overexpression of the extrusion pump alleviated the growth of cfr11 in the presence of high K+ concentrations (Figure 4C).
PMID:34349749	FYPO:0007717	sensitive to potassium nitrate [has_severity] low	The result was that overexpression of the extrusion pump alleviated the growth of cfr11 in the presence of high K+ concentrations (Figure 4C).
PMID:34349749	GO:0030007	intracellular potassium ion homeostasis	The results showed that this content was significantly higher in the exomer mutant than in the WT (Figure 1D), data that confirmed that exomer plays a role in the regulation of K+ homeostasis.
PMID:34349749	FYPO:0008346	increased cellular potassium level	The results showed that this content was significantly higher in the exomer mutant than in the WT (Figure 1D), data that confirmed that exomer plays a role in the regulation of K+ homeostasis.
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] medium	The results showed that trk1delta was partially sensitive to 40 mM NaCl and sensitive to 100 mM CaCl2 (Figure 3D)
PMID:34349749	FYPO:0005889	sensitive to sodium chloride [has_severity] medium	The results showed that trk1delta was partially sensitive to 40 mM NaCl and sensitive to 100 mM CaCl2 (Figure 3D)
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] medium	Under these conditions, cta31 bch11 was sensitive to lower calcium concentrations.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	We also analyzed the relationship between exomer and the calcium channels Cch1 and Yam8 (Ma et al., 2011). cch11 was sensitive to low KCl concentrations, and both cch11 cfr11 and yam81 cfr11 were more sensitive than any of the single mutants.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	We also analyzed the relationship between exomer and the calcium channels Cch1 and Yam8 (Ma et al., 2011). cch1delta was sensitive to low KCl concentrations, and both cch1delta cfr1delta and yam8delta cfr1delta were more sensitive than any of the single mutants.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	We also analyzed the relationship between exomer and the calcium channels Cch1 and Yam8 (Ma et al., 2011). cch1delta was sensitive to low KCl concentrations, and both cch1delta cfr1delta and yam8delta cfr1delta were more sensitive than any of the single mutants.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	We also analyzed the relationship between exomer and the calcium channels Cch1 and Yam8 (Ma et al., 2011). cch1delta was sensitive to low KCl concentrations, and both cch1delta cfr1delta and yam8delta cfr1delta were more sensitive than any of the single mutants.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	We also analyzed the relationship between exomer and the calcium channels Cch1 and Yam8 (Ma et al., 2011). cch1delta was sensitive to low KCl concentrations, and both cch1delta cfr1delta and yam8delta cfr1delta were more sensitive than any of the single mutants.
PMID:34349749	GO:0032178	medial membrane band	We found that Pkd2-GFP was at the cell surface, with strong accumulation at the septal area in both strains (Figure 5D). Quantitative analyses did not detect significant differences between the strains regarding the distribution and intensity of Pkd2-GFP fluorescence at the cell surface, neither under basal conditions nor in KCl (Supplementary Figure 3).
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by gga11 in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	We found that apm1delta, gga22delta, and gga21delta gga22delta (denoted by gga11 in the Figure 8) were sensitive to both high concentrations of K+ salts and sorbitol (Figure 8), which showed that they were defective in growth under osmotic stress.
PMID:34349749	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	We found that cfr11 enhanced its3-1 thermosensitivity, and that its3-1 enhanced cfr11 sensitivity to 0.6 M KCl, which showed genetic interaction (Figure 7D).
PMID:34349749	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	We found that cfr1delta enhanced its3-1 thermosensitivity, and that its3-1 enhanced cfr11 sensitivity to 0.6 M KCl, which showed genetic interaction (Figure 7D).
PMID:34349749	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	We found that cfr1delta enhanced its3-1 thermosensitivity, and that its3-1 enhanced cfr11 sensitivity to 0.6 M KCl, which showed genetic interaction (Figure 7D).
PMID:34349749	FYPO:0005947	normal growth on potassium chloride	We found that neither osr2delta nor kha1delta was sensitive to K+ salts and that the phenotype of the corresponding double mutant was similar to that of the single cfr11 mutant (Figure 2D).
PMID:34349749	FYPO:0005947	normal growth on potassium chloride	We found that neither osr2delta nor kha1delta was sensitive to K+ salts and that the phenotype of the corresponding double mutant was similar to that of the single cfr1delta mutant (Figure 2D)
PMID:34349749	FYPO:0005947	normal growth on potassium chloride	We found that neither osr2delta nor kha1delta was sensitive to K+ salts and that the phenotype of the corresponding double mutant was similar to that of the single cfr1delta mutant (Figure 2D).
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	We found that the simultaneous deletion of exomer components and cta3+ led to sensitivity to low concentrations of KCl and KNO3 (Figure 4a)
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	We found that the simultaneous deletion of exomer components and cta3+ led to sensitivity to low concentrations of KCl and KNO3 (Figure 4a)
PMID:34349749	FYPO:0007717	sensitive to potassium nitrate [has_severity] high	We found that the simultaneous deletion of exomer components and cta3+ led to sensitivity to low concentrations of KCl and KNO3 (Figure 4a)
PMID:34349749	FYPO:0007717	sensitive to potassium nitrate [has_severity] high	We found that the simultaneous deletion of exomer components and cta3+ led to sensitivity to low concentrations of KCl and KNO3 (Figure 4a)
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] low	cfr1delta was only sensitive to very high Na+ and Ca2+ concentrations (lower panels in Figure 3D)
PMID:34349749	FYPO:0005889	sensitive to sodium chloride [has_severity] low	cfr1delta was only sensitive to very high Na+ and Ca2+ concentrations (lower panels in Figure 3D)
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] medium	cfr1delta was partially sensitive to hygromycin B and deleting cfr1+ enhanced the sensitivity of trk1delta, trk2delta, and trk1delta trk2delta strains (Figure 3C).
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] low	cfr1delta was partially sensitive to hygromycin B and deleting cfr1+ enhanced the sensitivity of trk1delta, trk2delta, and trk1delta trk2delta strains (Figure 3C).
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] low	cfr1delta was partially sensitive to hygromycin B and deleting cfr1+ enhanced the sensitivity of trk1delta, trk2delta, and trk1delta trk2delta strains (Figure 3C).
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] high	cfr1delta was partially sensitive to hygromycin B and deleting cfr1+ enhanced the sensitivity of trk1delta, trk2delta, and trk1delta trk2delta strains (Figure 3C).
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] low	cfr1delta was partially sensitive to hygromycin B and deleting cfr1+ enhanced the sensitivity of trk1delta, trk2delta, and trk1delta trk2delta strains (Figure 3C).
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] high	cfr1delta was partially sensitive to hygromycin B and deleting cfr1+ enhanced the sensitivity of trk1delta, trk2delta, and trk1delta trk2delta strains (Figure 3C).
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] high	ent3delta and apm3delta were slightly sensitive to high concentrations of KCl and KNO3 and were very sensitive to CaCl2. (Figure 8)
PMID:34349749	FYPO:0000098	sensitive to calcium [has_severity] high	ent3delta and apm3delta were slightly sensitive to high concentrations of KCl and KNO3 and were very sensitive to CaCl2. (Figure 8)
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] medium	erg51 exhibited a sensitivity to K+ salts and hygromycin B, that was milder than that of exomer mutants, was slightly more sensitive to CaCl2, and grew well on sorbitol (Figure 7A)
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] low	erg51 exhibited a sensitivity to K+ salts and hygromycin B, that was milder than that of exomer mutants, was slightly more sensitive to CaCl2, and grew well on sorbitol (Figure 7A)
PMID:34349749	FYPO:0000106	sensitive to hygromycin B [has_severity] medium	erg51 exhibited a sensitivity to K+ salts and hygromycin B, that was milder than that of exomer mutants, was slightly more sensitive to CaCl2, and grew well on sorbitol (Figure 7A)
PMID:34349749	FYPO:0007717	sensitive to potassium nitrate [has_severity] medium	erg51 exhibited a sensitivity to K+ salts and hygromycin B, that was milder than that of exomer mutants, was slightly more sensitive to CaCl2, and grew well on sorbitol (Figure 7A)
PMID:34349749	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_protein] PomBase:SPBC839.06	in the WT about 10% of the cells exhibited asymmetrical and subapical Cta3 distribution, while this percentage was over 50% in the mutant (lower right panel in Figure 4F).
PMID:34349749	FYPO:0000098	sensitive to calcium	pmr11 was sensitive to 100 mM CaCl2 while pmr11 cfr11 was not (Supplementary Figure 4)
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	pmr1delta was more sensitive to KCl than cfr1delta, and the double mutants were the most sensitive (Supplementary Figure 4).
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	pmr1delta was more sensitive to KCl than cfr1delta, and the double mutants were the most sensitive (Supplementary Figure 4).
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] high	pmr1delta was more sensitive to KCl than cfr1delta, and the double mutants were the most sensitive (Supplementary Figure 4).
PMID:34349749	FYPO:0001020	normal growth on calcium	pmr1delta was sensitive to 100 mM CaCl2 while pmr1delta cfr1delta was not (Supplementary Figure 4)
PMID:34349749	FYPO:0001020	normal growth on calcium	pmr1delta was sensitive to 100 mM CaCl2 while pmr1delta cfr1delta was not (Supplementary Figure 4)
PMID:34349749	FYPO:0005889	sensitive to sodium chloride [has_severity] high	trk1delta trkdelta was the most sensitive of all the strains. ( (Figure 3D)
PMID:34349749	FYPO:0005889	sensitive to sodium chloride [has_severity] high	trk1delta trkdelta was the most sensitive of all the strains. ( (Figure 3D)
PMID:34349749	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	we analyzed the growth of prototrophic WT and bch1delta strains on YES plates with 0.6 M KCl. We found that the mutant was sensitive under these conditions (Figure 1C). | Figure 5C
PMID:34349749	FYPO:0005947	normal growth on potassium chloride [has_severity] low	while cta31 was only sensitive to 0.6 M KCl in the tup11delta tup12delta background (Figure 4a)
PMID:34352089	GO:0000182	rDNA binding [occurs_in] nucleus [occurs_in] cytosolic_rRNA_25S_gene	(Figure 1c)
PMID:34352089	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC11D3.05	(Figure 3A and Supplementary Figure S5A)
PMID:34352089	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC11D3.05	(Figure 3A and Supplementary Figure S5A)
PMID:34352089	FYPO:0003700	increased snoRNA primary transcript level [assayed_transcript] PomBase:SPSNORNA.54	(comment: 5' extended precursors, C/C box (but not H/ACA box))
PMID:34352089	FYPO:0003700	increased snoRNA primary transcript level [assayed_transcript] PomBase:SPSNORNA.21	(comment: 5' extended precursors, C/C box (but not H/ACA box))
PMID:34352089	FYPO:0003700	increased snoRNA primary transcript level [assayed_transcript] PomBase:SPSNORNA.33	(comment: 5' extended precursors, C/C box (but not H/ACA box).) Pac1 nuclear exclusion specifically led to the accumulation of 5′-extended precursors of Pac1-bound C/D box snoRNAs (Supplementary Figure S3A). This accumulation was confirmed by Northern blot assays on three C/D box snoRNAs (sno16, snoU14 and snr79), whereas a control H/ACA box snoRNA (sno12) was unaffected
PMID:34352089	GO:0030847	termination of RNA polymerase II transcription, exosome-dependent	(comment: CHECK NEW TERM REQUESTED CHILD OF BOTH termination of RNA polymerase II transcription, poly(A)-independent) We showed pac1-dependent poly(A)-independent RNA polymerase II termination for 2 mRNA genes (mfs2 and SPBC530.02), 4 snRNA genes (snU1, snU2, snU4 and snU5), and 2 snoRNA genes (snU3 and snU32) . (comment: Can this be added in the annotation extension ?)
PMID:34352089	GO:0000956	nuclear-transcribed mRNA catabolic process	(comment: CHECK waiting for GO:NEW.) We show this for only two mRNA: mfs2 and SPBC530.02. (comment: Can this be added in the annotation extension ?)
PMID:34352089	GO:0000956	nuclear-transcribed mRNA catabolic process	(comment: CHECK waiting for GO:NEW.)inferred from association with prremature termination sites
PMID:34352089	GO:0032296	double-stranded RNA-specific ribonuclease activity [has_input] PomBase:SPAC11D3.05 [part_of] nuclear-transcribed mRNA catabolic process	(comment: MOVE DOWN)
PMID:34352089	GO:0032296	double-stranded RNA-specific ribonuclease activity [has_input] PomBase:SPBC530.02 [part_of] nuclear-transcribed mRNA catabolic process	(comment: MOVE DOWN)
PMID:34352089	FYPO:0001424	abolished protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPBC119.11c	Pac1 strain (Pac1-AA) that allowed rapid rapamycin-dependent nuclear exclusion of Pac1 (Figure 1B).
PMID:34352089	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	Supplementary Figure S5B
PMID:34352089	FYPO:0007883	decreased cleavage-dependent termination of RNA polymerase II transcription	we observed a sharp decline in RNAPII occupancy inside the gene body, directly downstream of the Pac1- bound region located in the first half of the genes (Figure 2B, blue profile). In contrast, Pac1 nuclear exclusion resulted in extended RNAPII occupancy throughout the entire ORFs (Figure 2B, red profile). Such differences in RNAPII profiles are suggestive of Pac1-dependent premature termination.
PMID:34352089	FYPO:0007883	decreased cleavage-dependent termination of RNA polymerase II transcription [assayed_transcript] PomBase:SPAC11D3.05	we observed a sharp decline in RNAPII occupancy inside the gene body, directly downstream of the Pac1- bound region located in the first half of the genes (Figure 2B, blue profile). In contrast, Pac1 nuclear exclusion resulted in extended RNAPII occupancy throughout the entire ORFs (Figure 2B, red profile). Such differences in RNAPII profiles are suggestive of Pac1-dependent premature termination.
PMID:34382912	FYPO:0005148	increased protein localization to nuclear periphery [assayed_protein] PomBase:SPCC4B3.15 [has_penetrance] 30	(Fig. 4)
PMID:34382912	FYPO:0003919	abolished protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	(Fig. 4)
PMID:34382912	FYPO:0000118	multiseptate vegetative cell [has_penetrance] >10	(Fig. 4)
PMID:34382912	MOD:00046	O-phospho-L-serine	(Fig. 5)
PMID:34382912	MOD:00046	O-phospho-L-serine	(Fig. 5)
PMID:34382912	MOD:00046	O-phospho-L-serine	(Fig. 5)
PMID:34382912	MOD:00046	O-phospho-L-serine	(Fig. 5)
PMID:34382912	MOD:00046	O-phospho-L-serine	(Fig. 5)
PMID:34382912	MOD:00046	O-phospho-L-serine	(Fig. 5)
PMID:34382912	FYPO:0006434	decreased protein localization to medial cortical node, with protein distributed in cell cortex, during vegetative growth [assayed_protein] PomBase:SPCC4B3.15	(Figure 2)
PMID:34382996	FYPO:0006587	decreased protein localization to shmoo tip membrane [assayed_protein] PomBase:SPCC1919.10c	(Fig. 6 E and Fig. S4 D) By LM, Myo52 and Exo84 also showed strong signal reduction in fus1Δ .
PMID:34382996	FYPO:0007874	decreased exocytosis at shmoo tip [has_severity] high	(Fig. 6, A-C) The density of vesicles was strongly reduced in the fus1Δ cells, whether this was h+ or h−, while WT h+ cells showed slightly higher vesicle density than h− cells, as in previous analysis ()
PMID:34382996	FYPO:0007874	decreased exocytosis at shmoo tip	(Fig. 6,A-C) The density of vesicles was strongly reduced in the fus1Δ cells, whether this was h+ or h−, while WT h+ cells showed slightly higher vesicle density than h− cells, as in previous analysis ()
PMID:34382996	GO:1990819	mating projection actin fusion focus	(Figure 5)
PMID:34382996	GO:1990819	mating projection actin fusion focus	(Figure 5)
PMID:34382996	FYPO:0000413	abolished cell fusion during mating	(comment: CHECK Only when gpd1∆ is in h- cell)
PMID:34382996	FYPO:0000413	abolished cell fusion during mating	(comment: CHECK Stronger phenotype in h+ than h- cell)
PMID:34382996	FYPO:0007876	decreased plasma membrane waviness at shmoo tip	Interestingly, the reduction in local secretion correlates with a strong loss of the wPM phenotype (Fig. 6, A and B; Fig. S4, E and F; and Fig. S5): only 4% of h+ fus1Δ cells (1/27) showed wPM, whereas 73% (16/22) and 20% (4/20) of h+ WT showed wPM in WT × WT and WT × fus1Δ crosses, respectively
PMID:34382996	FYPO:0004804	abolished actin fusion focus assembly	no assembly of vesicles by (Because cell fusion completely fails when both partner cells lack fus1)
PMID:34389684	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_transcript] PomBase:SPBP8B7.16c	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_transcript] PomBase:SPCC14G10.04	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_transcript] PomBase:SPBPB8B6.05c	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_transcript] PomBase:SPBC1683.10c	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_transcript] PomBase:SPBC3H7.15	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_transcript] PomBase:SPAC688.04c	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_transcript] PomBase:SPBC215.05	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_transcript] PomBase:SPCC1795.03	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_transcript] PomBase:SPCC1393.08	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_transcript] PomBase:SPBC2F12.03c	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_transcript] PomBase:SPCC338.14	( (comment: RNA-seq poly(A) tail reads). (Figs. 3-5 collectively fortify the case for seb1-G476S as a gain-of-function mutation in Seb1 that elicits precocious lncRNA termination dependent on lncRNA PAS and cleavage/polyadenylation factors.)
PMID:34389684	FYPO:0001489	inviable vegetative cell	(DNS)
PMID:34389684	FYPO:0001489	inviable vegetative cell	(DNS)
PMID:34389684	FYPO:0001489	inviable vegetative cell	(DNS)
PMID:34389684	FYPO:0007407	increased level of phosphate starvation gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 4B), Pho1 expression from the wild-type plasmid was increased sevenfold in seb1-G476S cells versus seb1-WT cells thereby echoing the derepressive effect of seb1-G476S on pho1 expression from the chromosomal prt-pho1 locus.
PMID:34389684	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] low	(Fig. 7) (comment: compared to WT)
PMID:34389684	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7) (comment: compared to WT)
PMID:34389684	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	(Fig. 7A)
PMID:34389684	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	(Fig. 7A)
PMID:34389684	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 7a)
PMID:34389684	FYPO:0002243	increased acid phosphatase activity [has_severity] high [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 1A)
PMID:34389684	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] low	(Figure 1A) (comment: vw changed to increased with low serverity as we compare to WT)
PMID:34389684	FYPO:0000080	decreased cell population growth at low temperature	(Figure 1C)
PMID:34389684	FYPO:0001355	decreased vegetative cell population growth	(Figure 1c)
PMID:34389684	FYPO:0002060	viable vegetative cell population	(Figure 3A) Notable findings were that seb1-G476S rescued the ts growth defect of rhn1Δ at 37 °C......
PMID:34389684	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: compared to WT)
PMID:34389684	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] low	(comment: compared to WT)
PMID:34389684	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] high	(comment: compared to WT)
PMID:34389684	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(comment: similar to wt)
PMID:34389684	FYPO:0001357	normal vegetative cell population growth	..... while rhn1Δ rescued the cs growth defect of seb1-G476S at 20 °C
PMID:34389684	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] high	Although seb1- G476S asp1-H397A cells grew slowly in liquid medium at 30 °C, an assay of acid phosphatase showed that the double mutant expressed threefold higher levels of Pho1 than the seb1-G476S single mutant (Fig. 6B). (NOTE ABOUT 20 FOLD HIGHE TTHAN WT)
PMID:34389684	FYPO:0007409	abnormal mRNA alternative polyadenylation [assayed_transcript] PomBase:SPNCRNA.1698	Here, we found that tgp1 promoter-driven acid phosphatase expression was increased 30-fold in seb1-G476S cells versus seb1-WT cells and that this derepression was effaced by mutating the promoter-proximal nc- tgp1 PAS (Fig. 4D).
PMID:34389684	FYPO:0002061	inviable vegetative cell population	The seb1-G476S and aps1Δ alleles were synthetically lethal
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC17C9.03	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC794.11c	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC27.04	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC24B11.11c	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC13G7.04c	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC16C4.07	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC8D2.20c	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC323.07c	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC11C11.02	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC23A1.17	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC1795.11	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC16H5.08c	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC8C9.15c	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC16A3.18	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC6G9.14	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC18H10.03	(Figure 1A-C)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC18H10.04c	(Figure 1A-C)
PMID:34402513	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPBC11C11.02	(Figure 2D)
PMID:34402513	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPBC11C11.02	(Figure 2E)
PMID:34402513	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPBC11C11.02	(Figure 2F)
PMID:34402513	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC11C11.02	(Figure 2G)
PMID:34402513	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPBC11C11.02	(Figure 2G) However, mutation of 3 additional Cdk1 consensus sites abolished Imp2 phosphorylation by Cdk1 (Imp2-11A, Fig. 2C).
PMID:34402513	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPBC11C11.02	(Figure 2G,H)
PMID:34402513	FYPO:0006008	normal onset of protein localization to cell division site [assayed_protein] PomBase:SPBC11C11.02	(Figure 3)
PMID:34402513	FYPO:0007829	premature protein localization to cell division site [assayed_protein] PomBase:SPBC11C11.02	(Figure 3) Imp2-11A-mNG was recruited to the CR earlier (ca. 4 minutes) than Imp2-mNG (Fig. 3A, B, and C).
PMID:34402513	FYPO:0002562	delayed onset of protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPBC11C11.02	(Figure 3) Imp2-11E-mNG was not recruited to the CR later than Imp2-mNG but its peak accumulation was delayed compared to wild-type (Fig. 3A, B, and C)
PMID:34402513	FYPO:0004097	normal actomyosin contractile ring contraction	(Figure 4)
PMID:34402513	FYPO:0001368	normal actomyosin contractile ring assembly	(Figure 4)
PMID:34402513	FYPO:0007828	normal actomyosin contractile ring maturation	(Figure 4)
PMID:34402513	FYPO:0004097	normal actomyosin contractile ring contraction	(Figure 4)
PMID:34402513	FYPO:0007828	normal actomyosin contractile ring maturation	(Figure 4)
PMID:34402513	FYPO:0001368	normal actomyosin contractile ring assembly	(Figure 4)
PMID:34402513	FYPO:0001368	normal actomyosin contractile ring assembly	(Figure 4)
PMID:34402513	FYPO:0007828	normal actomyosin contractile ring maturation	(Figure 4)
PMID:34402513	FYPO:0001365	decreased rate of actomyosin contractile ring contraction	(Figure 4) However, imp2-17E cells exhibited slower CR constriction. In fact, CR remnants remained in 62% of imp2-17E cells for the duration of our observation.
PMID:34402513	FYPO:0001368	normal actomyosin contractile ring assembly	(Figure 4A-B)
PMID:34402513	FYPO:0007828	normal actomyosin contractile ring maturation	(Figure 4A-B)
PMID:34402513	FYPO:0004097	normal actomyosin contractile ring contraction	(Figure 4A-B)
PMID:34402513	FYPO:0001903	normal septation index	(Figure S2A and C)
PMID:34402513	FYPO:0001903	normal septation index	(Figure S2A and C)
PMID:34402513	FYPO:0001903	normal septation index	(Figure S2A and C)
PMID:34402513	FYPO:0001903	normal septation index	(Figure S2A and C)
PMID:34402513	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells	(Figure S2A-B)
PMID:34402513	FYPO:0001760	normal cell separation after cytokinesis	(Figure S2A-B)
PMID:34402513	FYPO:0001760	normal cell separation after cytokinesis	(Figure S2A-B)
PMID:34402513	FYPO:0001760	normal cell separation after cytokinesis	(Figure S2A-B)
PMID:34402513	FYPO:0001760	normal cell separation after cytokinesis	(Figure S2A-B)
PMID:34402513	FYPO:0001760	normal cell separation after cytokinesis	(Figure S2A-B)
PMID:34402513	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells	(Figure S2A-B) there was no detectable defect in morphology or cell division in imp2-11A, imp2-11E, imp2-17E, imp2-28A or imp2-28E cells although some imp2-17A cells failed to separate, forming chains (Fig. S2A and B).
PMID:34402513	FYPO:0001252	multinucleate multiseptate vegetative cell	(Figure S2A-C)
PMID:34402513	FYPO:0001903	normal septation index	(Figure S2C)
PMID:34402513	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPBC11C11.02	(Figure S2D and F)
PMID:34402513	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPBC11C11.02	(Figure S2D and F)
PMID:34402513	FYPO:0002442	normal protein localization to cell division site [assayed_protein] PomBase:SPBC11C11.02	(Figure S2D-E)
PMID:34402513	FYPO:0005467	decreased protein localization to actomyosin contractile ring during mitosis [assayed_protein] PomBase:SPBC11C11.02	(Figure S2D-E)
PMID:34402513	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPBC11C11.02	(Figure S2D-E)
PMID:34402513	FYPO:0005467	decreased protein localization to actomyosin contractile ring during mitosis [assayed_protein] PomBase:SPBC11C11.02	(Figure S2D-E)
PMID:34402513	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC11C11.02	(Figure S2F)
PMID:34402513	FYPO:0005289	actomyosin contractile ring sliding	(Figure S3A) Interestingly, we noticed during imaging that imp2-17A rlc1-mNG sid4-mNG cells displayed CR sliding events where the CR formed in the middle of the cell but then slid towards one cell tip (6/18 cells) (Fig. S3A).
PMID:34402513	FYPO:0002253	normal septum location	(Figure S3B-C)
PMID:34402513	FYPO:0002253	normal septum location	(Figure S3B-C)
PMID:34402513	FYPO:0000339	mislocalized septum during vegetative growth	(Figure S3B-C)
PMID:34402513	FYPO:0002253	normal septum location	(Figure S3B-C)
PMID:34402513	FYPO:0004085	decreased vegetative cell growth	(Figure S4A)
PMID:34402513	FYPO:0002062	normal cell growth	(Figure S4A)
PMID:34402513	FYPO:0002062	normal cell growth	(Figure S4A)
PMID:34402513	FYPO:0002062	normal cell growth	(Figure S4A)
PMID:34402513	FYPO:0004085	decreased vegetative cell growth	(Figure S4B)
PMID:34402513	FYPO:0000316	inviable after spore germination	(Figure S4B)
PMID:34402513	FYPO:0000316	inviable after spore germination	(Figure S4B)
PMID:34402513	FYPO:0001903	normal septation index	(Figure SA and C)
PMID:34402513	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPBC11C11.02 [part_of] negative regulation of mitotic cytokinesis [happens_during] mitotic anaphase	(comment: vw added extensions to link MF to BP & phase)
PMID:34402513	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC11C11.02	Imp2 was phosphorylated by Hhp1 in vitro, and mutation of the 15 identified and two more CK1 consensus sites eliminated this phosphorylation (Fig. 2B)
PMID:34402513	GO:0106006	cytoskeletal protein-membrane anchor activity [part_of] mitotic actomyosin contractile ring assembly	This phenotype suggests that phosphorylation of the 17 CK1 consensus sites in Imp2 promotes the medial anchoring of the CR on the membrane, possibly by stabilizing an unknown interaction involving the Imp2 IDR.
PMID:34402513	GO:1902413	negative regulation of mitotic cytokinesis [happens_during] mitotic anaphase	Together these findings implicate Cdk1 in modulating the timing of Imp2 localization to the CR, and are consistent with the general theme of Cdk1 inhibiting cytokinesis until chromosome segregation is complete
PMID:34460892	PomGeneEx:0000012	RNA level decreased [during] regulation of cellular response to glucose starvation	(comment: Evidence code was RNA-seq)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [during] cellular response to glucose starvation	(comment: Evidence form RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence form RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence form RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence form RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence form RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence form RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence form RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence form RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence form RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence form RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [during] cellular response to glucose starvation	(comment: Evidence form RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence form RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [during] cellular response to glucose starvation	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [during] cellular response to glucose starvation	(comment: Evidence from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [during] cellular response to glucose starvation	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [during] cellular response to glucose starvation	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [during] cellular response to glucose starvation	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000011	RNA level increased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq data)
PMID:34460892	PomGeneEx:0000012	RNA level decreased [in_presence_of] D-glucose	(comment: Evidence was from RNA-seq not from microarray)
PMID:34464389	FYPO:0001309	increased viability in stationary phase	(Fig. 5A) Given the increased lifespan of rnh1Δ rnh201Δ cells
PMID:34464389	FYPO:0007936	increased number of DNA breakpoint junctions	(Fig. 5B) Notably, in aged cells the double mutant showed an ~3-fold increase in chromosomal junctions on average, albeit with large variation, but no increase in indels
PMID:34464389	PomGeneEx:0000011	RNA level increased [during] mitotic G2 cell cycle arrest in response to glucose starvation	(Fig. S7A) A re-analysis of RNA-seq data from non-dividing cells [68] revealed a subtle increase in tlh2 expression during chronological ageing
PMID:34464389	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPBCPT2R1.08c	(Figure 4B) Accordingly, our smFISH experiment showed that tlh2 was de-repressed in sir2 deletion cells
PMID:34464389	FYPO:0001309	increased viability in stationary phase [has_severity] low	(Figure 5A) Cells lacking Sir2 showed a subtle extension of chronological lifespan compared to wild-type, especially at later timepoints
PMID:34464389	FYPO:0007936	increased number of DNA breakpoint junctions	(Figure S7B) The proportion of junctions downstream of tlh2 was higher in the tlh2 overexpression strain compared to wild-type
PMID:34464389	FYPO:0000245	loss of viability in stationary phase	(Figure S7C) Moreover, the tlh2 overexpression strain was substantially shorter-lived than wild-type cells
PMID:34464389	PomGeneEx:0000019	protein level decreased [in_presence_of] mitotic G2 cell cycle arrest in response to glucose starvation	(comment: CHECK during stationary phase). Figure 6C In fact, the protein levels of Scw1 markedly decreased in ageing cells.
PMID:34464389	FYPO:0007937	increased number of DNA breakpoint junctions during stationary phase	Based on DNA breakpoint junctions in genome sequence data (Fig 5B While wild-type cells showed a substantial increase of indels in aged cells, sir2Δ cells showed only a subtle increase
PMID:3448096	FYPO:0000998	elongated cell during nitrogen starvation	(comment: cells are longer than wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N)
PMID:3448096	FYPO:0000998	elongated cell during nitrogen starvation	(comment: cells are longer than wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N)
PMID:3448096	FYPO:0000998	elongated cell during nitrogen starvation	(comment: cells are longer than wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N)
PMID:3448096	FYPO:0000998	elongated cell during nitrogen starvation	(comment: cells are longer than wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N)
PMID:3448096	FYPO:0000998	elongated cell during nitrogen starvation	(comment: cells are longer than wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N)
PMID:3448096	FYPO:0000998	elongated cell during nitrogen starvation	(comment: cells are longer than wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N)
PMID:3448096	FYPO:0000998	elongated cell during nitrogen starvation	(comment: cells are longer than wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N)
PMID:3448096	FYPO:0000998	elongated cell during nitrogen starvation	(comment: cells are longer than wt under N starvation conditions, but not necessarily longer than a wt cell is when not starved for N)
PMID:34499159	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC4G3.08 [assayed_protein] PomBase:SPAC57A7.11	(Figure 1)
PMID:34499159	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAPB1E7.12	(Figure 2)
PMID:34499159	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Figure 2)
PMID:34499159	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC13G6.07c	(Figure 2)
PMID:34499159	FYPO:0001357	normal vegetative cell population growth	(Figure 3C)
PMID:34499159	FYPO:0000111	sensitive to rapamycin	(Figure 3c)
PMID:34499159	FYPO:0000111	sensitive to rapamycin	(Figure 3c)
PMID:34499159	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Figure 3d)
PMID:34499159	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC57A7.11 [assayed_protein] PomBase:SPCC4G3.08	(Figure 4B)
PMID:34499159	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC57A7.11 [assayed_protein] PomBase:SPBC216.07c	(Figure 4B)
PMID:34499159	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC57A7.11 [assayed_protein] PomBase:SPBC216.07c	(Figure 4b)
PMID:34499159	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_protein] PomBase:SPAC57A7.11	(Figure 4c)
PMID:34499159	FYPO:0002672	normal growth on rapamycin	(Figure 5A)
PMID:34499159	FYPO:0002672	normal growth on rapamycin	(Figure 5A)
PMID:34499159	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC31G5.12c	(Figure 5D) These observations indicate that the mip1 mutation does not affect the TORC1-dependent phosphorylation of Sck1, Sck2 and Maf1.
PMID:34499159	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC4F10.07c	(Figure 5E)
PMID:34499159	FYPO:0001147	normal mating efficiency	(Figure S2B)
PMID:34499159	GO:0035591	signaling adaptor activity [has_input] PomBase:SPAC4F10.07c	Thus, in addition to Psk1, Atg13 also appears to be phosphorylated by TORC1 in a manner dependent on Mip1 Tyr-533, a residue critical for the TOS motif-mediated recruitment of TORC1 substrates.
PMID:34523683	FYPO:0008389	activation of monopolar cell growth at old end during septation [has_penetrance] 3.4	(Fig. 5)
PMID:34523683	FYPO:0008389	activation of monopolar cell growth at old end during septation [has_penetrance] 3.7	(Fig. 5)
PMID:34523683	GO:0035840	old growing cell tip [exists_during] mitotic M phase	(Fig. 6)
PMID:34523683	FYPO:0003213	explosive cytokinetic cell separation resulting in vegetative cell lysis [has_penetrance] 10	(Fig. 7)
PMID:34523683	FYPO:0003213	explosive cytokinetic cell separation resulting in vegetative cell lysis [has_penetrance] 25	(Fig. 7)
PMID:34523683	FYPO:0003213	explosive cytokinetic cell separation resulting in vegetative cell lysis [has_penetrance] 10	(Fig. 7)
PMID:34523683	FYPO:0008389	activation of monopolar cell growth at old end during septation [has_penetrance] 15	(Fig. 7D)
PMID:34523683	FYPO:0008389	activation of monopolar cell growth at old end during septation [has_penetrance] 15	(Fig. 7D)
PMID:34523683	FYPO:0005468	increased protein localization to cell tip during mitosis [assayed_protein] cdc42/GTP+	(Fig. 7E and F)
PMID:34523683	FYPO:0008389	activation of monopolar cell growth at old end during septation	(Fig. S4)
PMID:34523683	FYPO:0008389	activation of monopolar cell growth at old end during septation	(Fig. S4)
PMID:34523683	FYPO:0008389	activation of monopolar cell growth at old end during septation	(Fig. S4)
PMID:34524082	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	(Fig. 4A)
PMID:34524082	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	(Fig. 4A)
PMID:34524082	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high [assayed_transcript] dg_repeat	(Fig. 4D)
PMID:34524082	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high [assayed_transcript] PomBase:SPAC212.11	(Fig. 4D)
PMID:34524082	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high [assayed_transcript] dh_repeat	(Fig. 4D)
PMID:34524082	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] PomBase:SPAC212.11 [has_severity] high	(Fig. 4D)
PMID:34524082	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low [assayed_transcript] dg_repeat	(Fig. 4D)
PMID:34524082	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat [has_severity] high	(Fig. 4D) (comment: Currently, we cannot explain why the dg transcripts in the 3FA mutant are only slightly elevated while completely losing H3K9me2/3.)
PMID:34524082	FYPO:0004577	decreased histone H3-K9 trimethylation at subtelomeric heterochromatin during vegetative growth [has_severity] high	(Fig. 4E)
PMID:34524082	FYPO:0000883	decreased histone H3-K9 trimethylation at centromere during vegetative growth [has_severity] high	(Fig. 4E)
PMID:34524082	FYPO:0004577	decreased histone H3-K9 trimethylation at subtelomeric heterochromatin during vegetative growth [has_severity] high	(Fig. 4E)
PMID:34524082	FYPO:0000883	decreased histone H3-K9 trimethylation at centromere during vegetative growth [has_severity] high	(Fig. 4E)
PMID:34524082	FYPO:0000876	decreased histone H3-K9 dimethylation during vegetative growth [has_severity] high	(Fig. 4E) (comment: CHECK REQUESTED ABOLISHED)
PMID:34524082	FYPO:0005847	decreased histone methyltransferase activity (H3-K9 specific) activity [assayed_substrate] hht2/Ubiq(K14)	(Figure 1, 3F)
PMID:34524082	FYPO:0006845	normal histone methyltransferase activity (H3-K9 specific) activity [assayed_substrate] hht1/Ubiq(K14)	(Figure 1, 3F) These experiments confirm the observation by Oya et al., 2019 that the H3K14ub substrate triggers a dramatic and specific increase in the methyltransferase activity of Clr4. However, in contrast to the previous study, we observe that the KMT domain is sufficient to mediate this regulatory mechanism.
PMID:34524082	FYPO:0005847	decreased histone methyltransferase activity (H3-K9 specific) activity [assayed_substrate] hht1/Ubiq(K14)	(Figure1 3F)
PMID:34524082	FYPO:0000876	decreased histone H3-K9 dimethylation during vegetative growth [has_severity] high	(comment: CHECK VW REQUESTED ABOLISHED) Fig. 4E Both H3K9me2 and H3K9me3 were completely abolished in clr4-GS253 and clr4-3FA strains at centromeric dg/dh repeats, being indistinguishable from clr4Δ
PMID:34524082	GO:0140006	histone H3 reader activity [has_input] hht2/Ubiq(K14) [part_of] pericentric heterochromatin formation	(comment: consistent with Clr4’s KMT domain mediating the crosstalk between H3K14ub and H3K9me2/3 as an essential step in heterochromatin formation and maintenance.)
PMID:34524082	GO:0046974	histone H3K9 methyltransferase activity [has_input] hht1/Ubiq(K14) [part_of] pericentric heterochromatin formation [occurs_in] pericentric heterochromatin	hht-ub14 substrate which both manifest a similar degree of strong stimulation by H3K14ub (Figure 1C, Figure 1—Figure supplement 1E-H).
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34580178	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1B)
PMID:34608864	MOD:01148	ubiquitinylated lysine	(comment: CHECK in presence or absence of MMS)
PMID:34608864	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_protein] PomBase:SPAPB1E7.02c	(comment: CHECK presence or absence of HU)
PMID:34608864	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_protein] PomBase:SPBC216.06c	(comment: CHECK presence or absence of HU)
PMID:34608864	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_protein] PomBase:SPAPB1E7.02c	(comment: CHECK presence or absence of HU)
PMID:34608864	FYPO:0002909	decreased protein localization to chromatin during vegetative growth [assayed_protein] PomBase:SPBC216.06c	(comment: CHECK presence or absence of HU)
PMID:34608864	FYPO:0004240	decreased histone H3-K56 acetylation during vegetative growth	(comment: CHECK presence or absence of MMS)
PMID:34608864	FYPO:0000912	abolished protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPAC1783.04c	(comment: CHECK presence or absence of MMS)
PMID:34608864	FYPO:0004240	decreased histone H3-K56 acetylation during vegetative growth	(comment: CHECK presence or absence of MMS)
PMID:34613787	FYPO:0004854	increased protein localization to actomyosin contractile ring	(Fig. 3A-B and Table 2). Contractile rings of adf1-M3 mutant cells that were able to constrict had twice as many myosin molecules as the wild-type cells, translating to one myosin motor domain for every 70 nm of filament
PMID:34613787	FYPO:0004854	increased protein localization to actomyosin contractile ring	(Fig. 3A-B and Table 2). Contractile rings of adf1-M3 mutant cells that were able to constrict had twice as many myosin molecules as the wild-type cells, translating to one myosin motor domain for every 70 nm of filament
PMID:34613787	FYPO:0004854	increased protein localization to actomyosin contractile ring	(Fig. 3C) The number of Cdc12-3GFP molecules in the contractile rings of adf1-M3 mutant cells was on average about twice that of wild-type cells and much more variable
PMID:34613787	FYPO:0000230	abnormal actomyosin contractile ring actin filament organization [has_penetrance] high [has_severity] high	(Figure 2B)
PMID:34613787	FYPO:0003838	abolished actomyosin contractile ring contraction [has_penetrance] 30	(Figure 2B)
PMID:34613787	FYPO:0001365	decreased rate of actomyosin contractile ring contraction	(comment: CHECK WHY ISNNT THIS PART. OF ????FYPO:0000230 abnormal actomyosin contractile ring actin filament organization)
PMID:34613787	FYPO:0001365	decreased rate of actomyosin contractile ring contraction	(comment: CHECK WHY ISNNT THIS PART. OF ????FYPO:0000230 abnormal actomyosin contractile ring actin filament organization)
PMID:34613787	FYPO:0007899	increased rate of protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPBC32H8.12c	Contractile rings of adf1-M3 mutant cells accumulated actin twice as fast over a similar period of time as wild-type cells (Table 2).
PMID:34613787	FYPO:0003336	increased duration of protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPCC645.05c	In contrast, these myosins persisted at nearly their highest levels for an hour and the time course of the process was much more variable in the adf1-M3 mutant cells (Fig. 4C and D). In a few cofilin mutant cells, the myosins dwelled at the cell division site for more than 10 minutes after the completion of the ring constriction (Fig. 5A).
PMID:34613787	FYPO:0007898	decreased actomyosin contractile ring actin filament length	In prior work the mutant cells appeared to assemble normal contractile rings, but our quantitative measurements revealed that the cdc12-4A mutation reduced by about half both the rate of accumulation and the peak numbers of polymerized actin in the ring (Fig. 2E and Table 1).
PMID:34613787	FYPO:0002699	decreased protein localization to actomyosin contractile ring	Mutations of either type II myosin gene in the myo2-E1 or myp2Δ strains reduced the numbers of actin molecules in contractile rings by more than half compared with wild-type cells at the end of 10 the maturation period and the onset of constriction (Fig. 6A-B and Table 1).
PMID:34613787	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPBC32H8.12c	Mutations of either type II myosin gene in the myo2-E1 or myp2Δ strains reduced the numbers of actin molecules in contractile rings by more than half compared with wild-type cells at the end of 10 the maturation period and the onset of constriction (Fig. 6A-B and Table 1).
PMID:34613787	FYPO:0003014	decreased rate of actomyosin contractile ring disassembly	Second, the normalized disassembly rate, which took the number of actin molecules in the ring into consideration, was 40% lower in the mutant than wild-type cells.
PMID:34613787	FYPO:0004854	increased protein localization to actomyosin contractile ring	Therefore, mature rings of the mutant had on average about 1.9 times as much actin as wild-type cells
PMID:34613787	GO:1902404	mitotic actomyosin contractile ring contraction	We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings.
PMID:34613787	GO:1903475	mitotic actomyosin contractile ring assembly	We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings.
PMID:34613787	GO:1903475	mitotic actomyosin contractile ring assembly	We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings.
PMID:34613787	GO:1902404	mitotic actomyosin contractile ring contraction	We conclude that type II myosins contribute to both the assembly and disassembly of actin filaments in contractile rings.
PMID:34634819	FYPO:0004751	resistance to G418 [has_severity] high	(Figure 2C)
PMID:34634819	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.05	(comment: ABOLISHED PROTEIN SPECIFIC TRANSLATION) Radioactive labeling of newly translated mitochondrial proteins showed that the combination of Δmug178 with either Δcbp7 or Δcbp8 abolished cytb translation while Δcbp7 Δcbp8 was similar to Δcbp8 (Figure 8B)
PMID:34634819	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.05	(comment: ABOLISHED PROTEIN SPECIFIC TRANSLATION) Radioactive labeling of newly translated mitochondrial proteins showed that the combination of Δmug178 with either Δcbp7 or Δcbp8 abolished cytb translation while Δcbp7 Δcbp8 was similar to Δcbp8 (Figure 8B)
PMID:34634819	FYPO:0002056	decreased mitochondrial translation [assayed_protein] PomBase:SPMIT.01	(comment: ABOLISHED PROTEIN SPECIFIC TRANSLATION) Whereas newly-synthesized Cox2 and Cox3 were radioactively labeled, Cox1 synthesis was abolished although the mature cox1 mRNA was only slightly decreased in Δi cells, showing that Mrh5 is required for cox1 translation.
PMID:34634819	GO:0005739	mitochondrion	A tagged version of Cbp7 was generated and found to be highly enriched in purified mitochondria (Figure 2B)
PMID:34634819	FYPO:0003730	abolished cell population growth on galactose carbon source	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0003731	normal growth on galactose carbon source	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0003731	normal growth on galactose carbon source	Cbp7 deletion prevented growth on non-fermentable medium in both contexts (Figure 2C and not shown)
PMID:34634819	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPMIT.05	Cytb level was partly decreased in Δmrh5 and only slightly in the point mutant.
PMID:34634819	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPMIT.05 [has_severity] low	Cytb level was partly decreased in Δmrh5 and only slightly in the point mutant.
PMID:34634819	FYPO:0002797	decreased protein degradation [assayed_protein] PomBase:SPMIT.05	Cytb showed a clear pattern of degradation over a 20 h chase in the wt, but appeared repeatedly resistant to degradation in the Δcbp7 mutant in several independent experiments (Figure 2H). This unexpected degradation pattern could indicate that in Δcbp7 cells, the newlysynthetized Cytb might escape recognition and/or accessibility by mitochondrial proteases (65), possibly because of misfolding, aggregation and/or defective membrane insertion.
PMID:34634819	FYPO:0007623	decreased mitochondrial respiratory chain complex III assembly [has_severity] high	Cytochrome spectra showed strongly decreased peaks for cytochromes b and c1 of complex III but normal to increased absorbance for cytochrome a + a3 of complex IV (Figure 2D).
PMID:34634819	GO:0005763	mitochondrial small ribosomal subunit	First, fractionations of mitochondria and post-mitochondrial supernatant in a double tagged strain showed that both are indeed mitochondrial proteins (Figure 6C). Second, western blot analysis of mitochondrial extracts from the double tagged strain fractionated on EDTA-sucrose gradients to separate both ribosomal subunits, showed that both tagged proteins co-sediment with the small ribosomal protein mS45 (Figure 6D). Third, immunoprecipitations performed under EDTA conditions showed that both Mrp51 and Mug178 did co-immunoprecipitate mS45 but not mL58 (Figure 6E).
PMID:34634819	GO:0005763	mitochondrial small ribosomal subunit	First, fractionations of mitochondria and post-mitochondrial supernatant in a double tagged strain showed that both are indeed mitochondrial proteins (Figure 6C). Second, western blot analysis of mitochondrial extracts from the double tagged strain fractionated on EDTA-sucrose gradients to separate both ribosomal subunits, showed that both tagged proteins co-sediment with the small ribosomal protein mS45 (Figure 6D). Third, immunoprecipitations performed under EDTA conditions showed that both Mrp51 and Mug178 did co-immunoprecipitate mS45 but not mL58 (Figure 6E).
PMID:34634819	FYPO:0003423	decreased mitochondrial RNA level [assayed_transcript] PomBase:SPMIT.05	First, the cytb mRNA was significantly, although never fully, destabilized (Figure 2F) whereas other mRNAs were not affected.
PMID:34634819	FYPO:0005261	increased cell population growth on galactose carbon source	High copy suppressors were also searched for starting from the Δcbp8 deletion and identified the same genes (Table 2): mug178, ppr7 and zfs1, reinforcing the idea that Cbp7 and Cbp8 are acting at the same step of Cytb biogenesis.
PMID:34634819	FYPO:0005261	increased cell population growth on galactose carbon source	High copy suppressors were also searched for starting from the Δcbp8 deletion and identified the same genes (Table 2): mug178, ppr7 and zfs1, reinforcing the idea that Cbp7 and Cbp8 are acting at the same step of Cytb biogenesis.
PMID:34634819	FYPO:0005261	increased cell population growth on galactose carbon source	High copy suppressors were also searched for starting from the Δcbp8 deletion and identified the same genes (Table 2): mug178, ppr7 and zfs1, reinforcing the idea that Cbp7 and Cbp8 are acting at the same step of Cytb biogenesis.
PMID:34634819	FYPO:0005261	increased cell population growth on galactose carbon source	High copy suppressors were also searched for starting from the Δcbp8 deletion and identified the same genes (Table 2): mug178, ppr7 and zfs1, reinforcing the idea that Cbp7 and Cbp8 are acting at the same step of Cytb biogenesis.
PMID:34634819	FYPO:0005261	increased cell population growth on galactose carbon source	High copy suppressors were also searched for starting from the Δcbp8 deletion and identified the same genes (Table 2): mug178, ppr7 and zfs1, reinforcing the idea that Cbp7 and Cbp8 are acting at the same step of Cytb biogenesis.
PMID:34634819	FYPO:0005261	increased cell population growth on galactose carbon source	High copy suppressors were also searched for starting from the Δcbp8 deletion and identified the same genes (Table 2): mug178, ppr7 and zfs1, reinforcing the idea that Cbp7 and Cbp8 are acting at the same step of Cytb biogenesis.
PMID:34634819	FYPO:0002797	decreased protein degradation [assayed_protein] PomBase:SPMIT.05	However, as with Δcbp7 cells, the newly synthesized Cytb protein showed an aberrant degradation pattern compared to the wild-type since it remained stable for up to 20 h in a chase experiment (Supplementary Figure S5).
PMID:34634819	FYPO:0003423	decreased mitochondrial RNA level [assayed_transcript] PomBase:SPMIT.05	In brief, Δcbp8 looked similar to Δcbp7 since complex III was barely detectable in BN-PAGE, cytochrome b and c1 were not spectrally detected and a low level of cytb RNA was observed
PMID:34634819	FYPO:0006446	increased mitochondrial pre-mRNA level [assayed_protein] PomBase:SPMIT.01	In Δi cells, the mature cox1 mRNA was absent in Δmrh5 and the precursor RNA containing both cox1 introns accumulated
PMID:34634819	FYPO:0006446	increased mitochondrial pre-mRNA level [assayed_protein] PomBase:SPMIT.01	In Δi cells, the mature cox1 mRNA was absent in Δmrh5 and the precursor RNA containing both cox1 introns accumulated
PMID:34634819	GO:0180065	mitochondrial small ribosomal subunit binding	In Δi cells, the mature cox1 mRNA was absent in Δmrh5 and the precursor RNA containing both cox1 introns accumulated; in the point mutant, partial splicing deficiency was observed.
PMID:34634819	GO:0008494	translation activator activity [has_input] PomBase:SPMIT.01.1	In Δi cells, the mature cox1 mRNA was absent in Δmrh5 and the precursor RNA containing both cox1 introns accumulated; in the point mutant, partial splicing deficiency was observed.
PMID:34634819	FYPO:0002060	viable vegetative cell population	On the contrary, the deletion of mug178 yielded viable cells.
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Second, we found that growth of Δmug178 cells on non-fermentable medium was restored by the ppr4, mrh5 or mrp51 suppressor alleles of Δcbp7 (Supplementary Figure S10A).
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Second, we found that growth of Δmug178 cells on non-fermentable medium was restored by the ppr4, mrh5 or mrp51 suppressor alleles of Δcbp7 (Supplementary Figure S10A).
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Second, we found that growth of Δmug178 cells on non-fermentable medium was restored by the ppr4, mrh5 or mrp51 suppressor alleles of Δcbp7 (Supplementary Figure S10A).
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Second, we found that growth of Δmug178 cells on non-fermentable medium was restored by the ppr4, mrh5 or mrp51 suppressor alleles of Δcbp7 (Supplementary Figure S10A).
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Second, we found that growth of Δmug178 cells on non-fermentable medium was restored by the ppr4, mrh5 or mrp51 suppressor alleles of Δcbp7 (Supplementary Figure S10A).
PMID:34634819	FYPO:0000251	decreased cell population growth on galactose carbon source	Second, we found that growth of Δmug178 cells on non-fermentable medium was restored by the ppr4, mrh5 or mrp51 suppressor alleles of Δcbp7 (Supplementary Figure S10A).
PMID:34634819	FYPO:0002061	inviable vegetative cell population	The complete absence of Mrp51 was unviable in a wild-type background. This is expected for an essential mitoribosomal protein because S. pombe is a petite- negative yeast, i.e. that cannot tolerate the complete loss of the mtDNA, or similarly a complete block in mitochondrial translation
PMID:34634819	FYPO:0007623	decreased mitochondrial respiratory chain complex III assembly [has_severity] high	The deletion of the cbp8 gene in both ∑i and Δi backgrounds yielded respiratory deficient but antimycin resistant cells showing that ATP synthase was not affected (Figure 3D and not shown).
PMID:34634819	FYPO:0001437	normal growth on antimycin A	The deletion of the cbp8 gene in both ∑i and Δi backgrounds yielded respiratory deficient but antimycin resistant cells showing that ATP synthase was not affected (Figure 3D and not shown).
PMID:34634819	FYPO:0003730	abolished cell population growth on galactose carbon source [has_severity] high	The deletion of the cbp8 gene in both ∑i and Δi backgrounds yielded respiratory deficient but antimycin resistant cells showing that ATP synthase was not affected (Figure 3D and not shown).
PMID:34634819	FYPO:0002060	viable vegetative cell population	The mrp51 deletion could be obtained in the ptp1-1 strain, which allows S. pombe to remain alive without mtDNA (47)
PMID:34634819	FYPO:0002060	viable vegetative cell population	The mrp51 deletion could be obtained in the ptp1-1 strain, which allows S. pombe to remain alive without mtDNA (47)
PMID:34634819	FYPO:0005261	increased cell population growth on galactose carbon source	The strength of suppression by the mug178 or ppr7 plasmids was similar in terms of respiratory growth and cytochrome spectra (Figure 5A, B).
PMID:34634819	FYPO:0005261	increased cell population growth on galactose carbon source	The strength of suppression by the mug178 or ppr7 plasmids was similar in terms of respiratory growth and cytochrome spectra (Figure 5A, B).
PMID:34634819	FYPO:0005261	increased cell population growth on galactose carbon source	The strength of suppression by the mug178 or ppr7 plasmids was similar in terms of respiratory growth and cytochrome spectra (Figure 5A, B).
PMID:34634819	FYPO:0005261	increased cell population growth on galactose carbon source	The strength of suppression by the mug178 or ppr7 plasmids was similar in terms of respiratory growth and cytochrome spectra (Figure 5A, B).
PMID:34634819	FYPO:0005261	increased cell population growth on galactose carbon source	The strength of suppression by the mug178 or ppr7 plasmids was similar in terms of respiratory growth and cytochrome spectra (Figure 5A, B).
PMID:34634819	FYPO:0005261	increased cell population growth on galactose carbon source	The strength of suppression by the mug178 or ppr7 plasmids was similar in terms of respiratory growth and cytochrome spectra (Figure 5A, B).
PMID:34634819	FYPO:0001437	normal growth on antimycin A	The Δmrh5 mutation did not impair growth on antimycin containing medium, showing that ATPase activity is not affected (Figure 9A).
PMID:34634819	FYPO:0003730	abolished cell population growth on galactose carbon source	The Δmug178 mutant was unable to grow on non-fermentable medium and lacked spectrally detectable cytochromes b and c1 but was not sensitive to antimycin A, showing that ATP synthase is not defective (Figure 7A-B).
PMID:34634819	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPMIT.05	This absence of degradation was surprising since Cytb steady state seemed dramatically decreased in the mutant compared to the wt, as revealed in purified mitochondria (Figure 2E) as well as in the total protein chase samples (Supplementary Figure S3) using our in-house antibody. We have no definitive solution to this paradox; the answer might lie with a particularity of our Cytb antibody. This only recognizes Cytb in non-boiled samples, suggesting that the epitope recognised by the antibody is a small structural motif, rather than a linear sequence. Thus, if the neo-synthesized Cytb cannot be correctly folded and inserted into the membrane, the epitope recognised by our antibody may no longer be present.
PMID:34634819	GO:0008494	translation activator activity [has_input] PomBase:SPMIT.01.1	Thus, our mass spectrometry and phenotypic analyses show that Mrh5, Ppr4, Mtf2 and Sls1 are part of a cox1 translational complex interacting with the mitoribosome, at least through Mrh5.
PMID:34634819	GO:0008494	translation activator activity [has_input] PomBase:SPMIT.01.1	Thus, our mass spectrometry and phenotypic analyses show that Mrh5, Ppr4, Mtf2 and Sls1 are part of a cox1 translational complex interacting with the mitoribosome, at least through Mrh5.
PMID:34634819	GO:0008494	translation activator activity [has_input] PomBase:SPMIT.01.1	Thus, our mass spectrometry and phenotypic analyses show that Mrh5, Ppr4, Mtf2 and Sls1 are part of a cox1 translational complex interacting with the mitoribosome, at least through Mrh5.
PMID:34634819	FYPO:0003730	abolished cell population growth on galactose carbon source	We found that Δmrh5 was essential for respiratory growth, even in Δi background, suggesting that if Mrh5 is involved in intron excision, it also has another role.
PMID:34634819	FYPO:0001983	protein absent from cell [assayed_protein] PomBase:SPMIT.01	Western blot analysis was performed on the Δmrh5 and mrh5-G230E mutants, as well as the tagged Mrh5-cMyc strain (Figure 9C). The results showed that Mrh5 is a mitochondrial protein and that Cox1 and Cox2 were undetectable in both mutants.
PMID:34634819	FYPO:0001983	protein absent from cell [assayed_protein] PomBase:SPMIT.01	Western blot analysis was performed on the Δmrh5 and mrh5-G230E mutants, as well as the tagged Mrh5-cMyc strain (Figure 9C). The results showed that Mrh5 is a mitochondrial protein and that Cox1 and Cox2 were undetectable in both mutants.
PMID:34634819	FYPO:0001983	protein absent from cell [assayed_protein] PomBase:SPMIT.11	Western blot analysis was performed on the Δmrh5 and mrh5-G230E mutants, as well as the tagged Mrh5-cMyc strain (Figure 9C). The results showed that Mrh5 is a mitochondrial protein and that Cox1 and Cox2 were undetectable in both mutants.
PMID:34634819	FYPO:0001983	protein absent from cell [assayed_protein] PomBase:SPMIT.11	Western blot analysis was performed on the Δmrh5 and mrh5-G230E mutants, as well as the tagged Mrh5-cMyc strain (Figure 9C). The results showed that Mrh5 is a mitochondrial protein and that Cox1 and Cox2 were undetectable in both mutants.
PMID:34634819	FYPO:0001437	normal growth on antimycin A	but grew normally on fermentable medium containing antimycin, showing that the ATP synthase (complex V) is not strongly affected by the mutation (Figure 2C)
PMID:34634819	FYPO:0001437	normal growth on antimycin A	but was not sensitive to antimycin A, showing that ATP synthase is not defective (Figure 7A-B)
PMID:34634819	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPMIT.11	Δsls1 cells lacked spectral a+a3 peak, were devoid of Cox1 and very depleted in Cox2 (Figure 11B, C).
PMID:34634819	FYPO:0001983	protein absent from cell [assayed_protein] PomBase:SPMIT.01	Δsls1 cells lacked spectral a+a3 peak, were devoid of Cox1 and very depleted in Cox2 (Figure 11B, C).
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress	(Figure 5)
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	(Figure 5)
PMID:34666001	FYPO:0008012	cell sensitive to mechanical stress	(comment: CHECK (vw: 25% cell death))
PMID:34666001	FYPO:0008012	cell sensitive to mechanical stress	In microchannels, where clusters form at high frequency, due to larger and more frequent compressive mechanical stresses onto the CWs, the survival behavior was markedly different. First, wsc1D cells exhibited a much higher yield of death of $28%. Second, all alleles exhibited a high yield of death around $25% including wsc1DWSC
PMID:34666001	FYPO:0008004	abolished protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	In sharp contrast, Wsc1DSTR-GFP, Wsc1DWSC-GFP and Wsc1DSTRDWSC-GFP cells were completely devoid of any clustering phenotype, with an enrichment at contacts close to $2 (Figures 5D, 5E, and S2F-S2H).
PMID:34666001	FYPO:0008004	abolished protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	In sharp contrast, Wsc1DSTR-GFP, Wsc1DWSC-GFP and Wsc1DSTRDWSC-GFP cells were completely devoid of any clustering phenotype, with an enrichment at contacts close to $2 (Figures 5D, 5E, and S2F-S2H).
PMID:34666001	FYPO:0008004	abolished protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	In sharp contrast, Wsc1DSTR-GFP, Wsc1DWSC-GFP and Wsc1DSTRDWSC-GFP cells were completely devoid of any clustering phenotype, with an enrichment at contacts close to $2 (Figures 5D, 5E, and S2F-S2H).
PMID:34666001	FYPO:0008003	normal protein localization to site of mechanical stress [assayed_protein] PomBase:SPBC30B4.01c	Remarkably, the Wsc1DCC-GFP lacking a large fraction of the cytoplasmic C-terminal tail, and thus presumably defective in downstream signal transduction was dispensable for clustering. This finding reinforces the notion that Wsc1 clustering occurs independently of downstream CWI signaling.
PMID:34666001	GO:0140897	mechanoreceptor activity [part_of] detection of mechanical stimulus	Together, these results indicate that Wsc1 clustering may be triggered by local surface compression, independently of putative ‘‘trans’’ homotypic interactions between extracellular sensors from neighbor cells or general cell-to-cell signaling.
PMID:34666001	FYPO:0006606	abnormal dynamic protein localization pattern [assayed_protein] PomBase:SPBC30B4.01c	increased lateral diffusion in membrane. Finally, Wsc1DWSC-GFP and Wsc1DSTR-GFP, which are incapable of clustering, exhibited much smaller half-times—closer to that of mCherry-Psy1 (Figures 6A, 6B, and S6A).
PMID:34666001	FYPO:0006606	abnormal dynamic protein localization pattern [assayed_protein] PomBase:SPBC30B4.01c	increased lateral diffusion in membrane. Finally, Wsc1DWSC-GFP and Wsc1DSTR-GFP, which are incapable of clustering, exhibited much smaller half-times—closer to that of mCherry-Psy1 (Figures 6A, 6B, and S6A).
PMID:34666001	FYPO:0000647	vegetative cell lysis [has_penetrance] 26	n these videos, we did not detect any lysis in WT red cells, but a high incidence of dying wsc1DCC-GFP of $26%
PMID:34674264	FYPO:0003946	delayed onset of protein localization to cell division site [assayed_protein] PomBase:SPAC17G8.10c	(Fig. 2A-C). Reduced contractile ring localization during mitosis. However, we observed that Dma1-6A was significantly more difficult to detect at the first instance of CR localization early in mitosis than either Dma1 or Dma1-6D/E
PMID:34674264	FYPO:0007946	decreased protein ubiquitination [assayed_protein] PomBase:SPAC17G8.10c [has_severity] high	(Fig. 2B). (comment: CHECK Almost abolished Dma1 auto-ubiquitination by in vitro assay)
PMID:34674264	FYPO:0007946	decreased protein ubiquitination [assayed_protein] PomBase:SPAC17G8.10c [has_severity] low	(Fig. 2B). Dma1-6D/E auto-ubiquitination was modestly but reproducibly reduced relative to wild-type. Specifically, while 82% of wild-type Dma1 became ubiquitinated on at least one site, 71% of Dma1-6D/E did.
PMID:34674264	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. 4a)
PMID:34674264	FYPO:0003762	normal mitotic spindle assembly checkpoint	(Fig. 4a) We observed that nda3-km311, dma1- 6A nda3-km311, and dma1-6D/E nda3-km311 cells delayed septation relative to wild-type cells and that dma1Δ cells did not
PMID:34674264	FYPO:0000776	normal protein phosphorylation during vegetative growth	(comment: CHECK ALLELELS) we combined analog-sensitive (cdc2-as, orb5-as) and temperature-sensitive (plo1-1) alleles. Despite these kinases targeting Dma1 in vitro, we found no evidence that inhibiting any of them singly (not shown) or together (Fig. 1G) changed Dma1 phosphostatus as monitored by SDS/PAGE mobility suggesting that these kinases are not responsible for regulating Dma1 phosphostatus in cells.
PMID:34674264	FYPO:0007946	decreased protein ubiquitination [assayed_protein] PomBase:SPAC17G8.10c	(comment: CHECK Decreased Dma1 auto-ubiquitination by in vitro assay)
PMID:34674264	GO:0061630	ubiquitin protein ligase activity [has_input] PomBase:SPAC17G8.10c	(comment: CHECK in vitro assay)
PMID:34674264	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC11B10.09	(comment: CHECK in vitro kinase assay showed S166 is phosphorylated by Cdk1)
PMID:34674264	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC23C11.16	(comment: CHECK in vitro kinase assay showed S251 is phosphorylated by Plo1)
PMID:34674264	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPAC23C11.11	(comment: CHECK in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2)
PMID:34674264	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC23C11.11	(comment: CHECK in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2)
PMID:34674264	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC23C11.11	(comment: CHECK in vitro kinase assay showed T18, S20, and S266 are phosphorylated by CK2)
PMID:34674264	MOD:00047	O-phospho-L-threonine	(comment: in vivo phosphorylation site identified by mass spectrometry)
PMID:34674264	MOD:00046	O-phospho-L-serine	(comment: in vivo phosphorylation sites identified by mass spectrometry)
PMID:34674264	FYPO:0005227	normal level of ubiquitinated protein in cell [assayed_protein] PomBase:SPBC244.01c	Although this assay is not quantitative, we found that Sid4 was ubiquitinated to similar levels as in wild-type in both dma1-6A and dma1-6D/E but was not ubiquitinated in dma1D (Fig. 2A).
PMID:34674264	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPAC17G8.10c	Localization to SPBs at the same level as wild-type during spindle stress
PMID:34674264	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC17G8.10c	Localization to SPBs at the same level as wild-type during spindle stress
PMID:34674264	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC17G8.10c	Normal localization to medial cortical nodes, SPB, and division septum as wild-type
PMID:34674264	FYPO:0002442	normal protein localization to cell division site [assayed_protein] PomBase:SPAC17G8.10c	Normal localization to medial cortical nodes, SPB, and division septum as wild-type
PMID:34674264	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC17G8.10c	Normal localization to medial cortical nodes, mitotic contractile ring, SPB, and septum as wild-type
PMID:34686329	GO:0110078	TTT Hsp90 cochaperone complex	(Figure 1A)
PMID:34686329	GO:0110078	TTT Hsp90 cochaperone complex	(Figure 1A)
PMID:34686329	FYPO:0002133	abolished protein-RNA interaction [assayed_transcript] PomBase:SPBP16F5.03c [assayed_protein] PomBase:SPBC1604.17c	(Figure 2C) Abolished interaction between Tti2 protein and tra1 mRNA
PMID:34686329	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC23B6.03c [assayed_protein] PomBase:SPAC458.03	(Figure 2H)
PMID:34686329	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBP16F5.03c [assayed_protein] PomBase:SPBC1604.17c	(Figure 3C)
PMID:34686329	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBP16F5.03c [assayed_protein] PomBase:SPBC1604.17c	(Figure 3C)
PMID:34686329	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBP16F5.03c [assayed_protein] PomBase:SPBC1604.17c	(Figure 3C)
PMID:34686329	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBP16F5.03c [assayed_protein] PomBase:SPBC1604.17c	(Figure 3D)
PMID:34686329	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBP16F5.03c [assayed_protein] PomBase:SPBC1604.17c	(Figure 3D)
PMID:34686329	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBP16F5.03c [assayed_protein] PomBase:SPBC1604.17c	(Figure 3D)
PMID:34686329	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPBC1604.17c [assayed_transcript] PomBase:SPBP16F5.03c	(Figure 3E)
PMID:34686329	FYPO:0002357	normal protein-RNA interaction [assayed_protein] PomBase:SPBC1604.17c [assayed_transcript] PomBase:SPBP16F5.03c	(Figure 3E)
PMID:34686329	FYPO:0002133	abolished protein-RNA interaction [assayed_protein] PomBase:SPBC1604.17c [assayed_transcript] PomBase:SPBP16F5.03c	(Figure 3E)
PMID:34686329	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPBC1604.17c [assayed_transcript] PomBase:SPBP16F5.03c	(Figure 3E)
PMID:34686329	FYPO:0002357	normal protein-RNA interaction [assayed_protein] PomBase:SPBC1604.17c [assayed_transcript] PomBase:SPBP16F5.03c	(Figure 3E)
PMID:34686329	FYPO:0001408	sensitive to heat shock [has_severity] high	(Figure 6B)
PMID:34686329	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Figure 6B)
PMID:34686329	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Figure 6B)
PMID:34686329	FYPO:0000271	sensitive to salt stress [has_severity] high	(Figure 6B)
PMID:34686329	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] low	(Figure 6B)
PMID:34686329	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Figure 6B)
PMID:34686329	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Figure 6B)
PMID:34686329	FYPO:0001838	decreased protein phosphorylation during vegetative growth [has_severity] high [assayed_protein] PomBase:SPCC24B10.07	(Figure 6F)
PMID:34686329	FYPO:0000280	sterile [has_severity] high	(Figure 6H)
PMID:34686329	FYPO:0000280	sterile [has_severity] high	(Figure 6H)
PMID:34686329	FYPO:0002430	inviable after spore germination, multiple cell divisions	(Figure 6I)
PMID:34686329	FYPO:0002430	inviable after spore germination, multiple cell divisions	(Figure 6I)
PMID:34686329	FYPO:0000847	increased protein degradation during vegetative growth	(Figure 6J)
PMID:34686329	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1604.17c [assayed_protein] PomBase:SPBC30D10.10c	(Figure 7A)
PMID:34686329	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1604.17c [assayed_protein] PomBase:SPBP16F5.03c	(Figure 7A)
PMID:34686329	FYPO:0003827	decreased ribosomal S6 protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAPB1E7.12	(Figure S1G)
PMID:34686329	FYPO:0003827	decreased ribosomal S6 protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC13G6.07c	(Figure S1G)
PMID:34686329	FYPO:0003827	decreased ribosomal S6 protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAPB1E7.12	(Figure S1G)
PMID:34686329	FYPO:0003827	decreased ribosomal S6 protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC13G6.07c	(Figure S1G)
PMID:34686329	GO:0005737	cytoplasm	(Figure S2B).
PMID:34686329	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC30D10.10c [assayed_protein] PomBase:SPBC1604.17c	(Figure S4C)
PMID:34686329	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBP16F5.03c [assayed_protein] PomBase:SPBC1604.17c	(Figure S4C)
PMID:34686329	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC30D10.10c [assayed_protein] PomBase:SPBC1604.17c	(Figure S4C)
PMID:34686329	FYPO:0002133	abolished protein-RNA interaction [assayed_protein] PomBase:SPBC1604.17c [assayed_transcript] PomBase:SPBC30D10.10c	(Figure S5)
PMID:34686329	GO:0051083	'de novo' cotranslational protein folding	(Figures 2A and 2B). To determine whether this interaction occurs cotranslationally, we then repeated Tti1 RIPs in cells treated either with puromycin, an inhibitor of translation elongation, or with EDTA, which dissociates ribosomes. Both treatments abolished Tti1 binding to tra1+ (Figure 2C).
PMID:34686329	GO:0051083	'de novo' cotranslational protein folding	(Figures 2A and 2B). To determine whether this interaction occurs cotranslationally, we then repeated Tti1 RIPs in cells treated either with puromycin, an inhibitor of translation elongation, or with EDTA, which dissociates ribosomes. Both treatments abolished Tti1 binding to tra1+ (Figure 2C).
PMID:34686329	FYPO:0001355	decreased vegetative cell population growth	(Figures S1C and S1D).
PMID:34686329	FYPO:0001355	decreased vegetative cell population growth	(Figures S1C and S1D).
PMID:34686329	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBC32C12.02	(Figures S1E and S1F)
PMID:34686329	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBC32C12.02	(Figures S1E and S1F)
PMID:34686329	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPAC27D7.03c	(Figures S1E and S1F)
PMID:34686329	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPAC27D7.03c	(Figures S1E and S1F)
PMID:34686329	FYPO:0000705	abolished protein-protein interaction	(comment: Abolished incorporation of Tra1 into SAGA complex)
PMID:34686329	FYPO:0000705	abolished protein-protein interaction	(comment: Abolished incorporation of Tra1 into SAGA complex)
PMID:34686329	FYPO:0000705	abolished protein-protein interaction	(comment: Abolished incorporation of Tra1 into SAGA complex)
PMID:34686329	FYPO:0000705	abolished protein-protein interaction	(comment: Abolished incorporation of Tra1 into SAGA complex)
PMID:34686329	FYPO:0000705	abolished protein-protein interaction	(comment: Abolished incorporation of Tra1 into SAGA complex)
PMID:34686329	FYPO:0000781	decreased transcription during vegetative growth [has_severity] high	(comment: evidence: RNA-seq)
PMID:34686329	FYPO:0000781	decreased transcription during vegetative growth [has_severity] high	(comment: evidence: RNA-seq)
PMID:34686329	GO:0110078	TTT Hsp90 cochaperone complex	Altogether, our quantitative proteomic analyses indicate that Tti2, Tel2, and Tti1, together with Asa1, form a stable multi-meric complex that interacts with most PIKKs in S. pombe (Figure 1A)
PMID:34686329	GO:0051083	'de novo' cotranslational protein folding	Conventional and qRT-PCR analyses revealed a specific enrichment of the tra1+ mRNA in RIPs of all three TTT subunits, Tel2, Tti1, and Tti2, compared with several negative controls (Figures 2A and 2B). To determine whether this interaction occurs cotranslationally, we then repeated Tti1 RIPs in cells treated either with puromycin, an inhibitor of translation elongation, or with EDTA, which dissociates ribosomes. Both treatments abolished Tti1 binding to tra1+ (Figure 2C).
PMID:34686329	FYPO:0001355	decreased vegetative cell population growth	Depletion of each protein reduces S. pombe viability and proliferation compared with control strains and culture conditions (Figures S1C and S1D).
PMID:34686329	FYPO:0001317	normal RNA level during vegetative growth [assayed_protein] PomBase:SPAC1F5.11c	Finally, our published transcriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (FigureS1H)
PMID:34686329	FYPO:0001317	normal RNA level during vegetative growth [assayed_protein] PomBase:SPBC216.07c	Finally, our published transcriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (FigureS1H)
PMID:34686329	FYPO:0001317	normal RNA level during vegetative growth [assayed_protein] PomBase:SPBC30D10.10c	Finally, our published transcriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (FigureS1H)
PMID:34686329	FYPO:0001317	normal RNA level during vegetative growth [assayed_protein] PomBase:SPBP16F5.03c	Finally, our published transcriptomic analysis of tti2-CKO mutants showed that PIKK mRNA levels remain unaffected following Tti2 depletion (FigureS1H)
PMID:34686329	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC23B6.03c [assayed_protein] PomBase:SPAC458.03	In contrast, Tti2 and Tti1 interaction with tra1+ does not change in the absence of Tel2 (Figure 2I)
PMID:34686329	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC458.03	Surprisingly, despite a strong decrease of Tor2 steady-state levels, its stability appears unaffected, even increasing 6 h after CHX treatment. It is possible that Tor2 is subjected to rapid turnover and compensatory mechanisms boosting its synthesis.
PMID:34686329	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPAC926.04c [has_input] PomBase:SPBP16F5.03c [part_of] 'de novo' cotranslational protein folding	We conclude that Tti1, and to a lesser extent Tti2, recruits TTT to nascent Tra1 polypeptides
PMID:34686329	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPAC926.04c [has_input] PomBase:SPBP16F5.03c [part_of] 'de novo' cotranslational protein folding	We conclude that Tti1, and to a lesser extent Tti2, recruits TTT to nascent Tra1 polypeptides
PMID:34686329	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBC32C12.02	We used qRT-PCR to determine the effect of TTT depletion on the expression of two sexual differentiation genes, ste11+ and mei2+. We observed that the mRNA levels of both genes increase upon depletion of Tel2, Tti1, and Tti2 compared with control strains and conditions (Figures S1E and S1F)
PMID:34686329	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPAC27D7.03c	We used qRT-PCR to determine the effect of TTT depletion on the expression of two sexual differentiation genes, ste11+ and mei2+. We observed that the mRNA levels of both genes increase upon depletion of Tel2, Tti1, and Tti2 compared with control strains and conditions (Figures S1E and S1F)
PMID:34686329	FYPO:0000847	increased protein degradation during vegetative growth [assayed_protein] PomBase:SPBP16F5.03c	Western blotting followed by quantification of signal intensities showed that both the steady-state levels and the stability of Tra1, Tra2, and Tor1 decrease following Tti2 depletion (Figures 1C-1F).
PMID:34686329	FYPO:0000847	increased protein degradation during vegetative growth [assayed_protein] PomBase:SPBC30D10.10c	Western blotting followed by quantification of signal intensities showed that both the steady-state levels and the stability of Tra1, Tra2, and Tor1 decrease following Tti2 depletion (Figures 1C-1F).
PMID:34686329	FYPO:0000847	increased protein degradation during vegetative growth [assayed_protein] PomBase:SPAC1F5.11c	Western blotting followed by quantification of signal intensities showed that both the steady-state levels and the stability of Tra1, Tra2, and Tor1 decrease following Tti2 depletion (Figures 1C-1F).
PMID:34686329	FYPO:0003827	decreased ribosomal S6 protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC13G6.07c	Western blotting showed decreased phosphorylation of the ribosomal protein S6, a canonical TORC1 substrate, following Tel2, Tti1, and Tti2 depletion (Figure S1G)
PMID:34686329	FYPO:0003827	decreased ribosomal S6 protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAPB1E7.12	Western blotting showed decreased phosphorylation of the ribosomal protein S6, a canonical TORC1 substrate, following Tel2, Tti1, and Tti2 depletion (Figure S1G)
PMID:34706246	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPBC428.16c	(Fig. 2C)
PMID:34706246	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPBC428.16c	(Fig. 2C)
PMID:34706246	FYPO:0003467	altered splice site specificity [assayed_transcript] PomBase:SPBC428.16c [has_severity] high	(Fig. 2D)
PMID:34706246	FYPO:0003468	normal RNA splicing [assayed_transcript] PomBase:SPBC428.16c	(Fig. 4)
PMID:34706246	FYPO:0003468	normal RNA splicing [assayed_transcript] PomBase:SPBC428.16c	(Fig. 4)
PMID:34706246	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPBC405.04c [has_severity] medium	(Fig. 5D)
PMID:34706246	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPBC405.04c [has_severity] high	(Fig. 5D)
PMID:34706246	FYPO:0003468	normal RNA splicing [assayed_transcript] PomBase:SPBC405.04c	(Fig. 5D)
PMID:34706246	FYPO:0003468	normal RNA splicing [assayed_transcript] PomBase:SPBC405.04c	(Fig. 5D)
PMID:34706246	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPBC405.04c [has_severity] low	(Fig. 5D)
PMID:34706246	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPBC405.04c [has_severity] medium	(Fig. 5D)
PMID:34706246	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPBC405.04c [has_severity] low	(Fig. 5D)
PMID:34731638	FYPO:0002360	normal chromatin silencing at centromere	(Figure 1 G)
PMID:34731638	FYPO:0003555	normal chromatin silencing at subtelomere	(Figure 1 G)
PMID:34731638	FYPO:0004604	decreased chromatin silencing at subtelomere [has_severity] high	(Figure 1B) In contrast, there was a substantial reduction of H3K9me2 at the mating-type locus, in agreement with a previous study (Holla et al., 2020) (Figure S1A), and at the subtelomeres
PMID:34731638	FYPO:0004542	increased chromatin silencing at subtelomere	(Figure 1F)
PMID:34731638	FYPO:0006299	increased chromatin silencing at centromere outer repeat	(Figure 1F)
PMID:34731638	FYPO:0005849	decreased spatial extent of heterochromatin assembly [assayed_region] mating_type_region	(Figure 2C) Conversely, in the pob3Δ strain, the orange reporter was also fully derepressed in the majority of cells, yet the green reporter remained silenced or mildly derepressed. This result implies that pob3Δ cells have a heterochromatin spreading defect
PMID:34731638	FYPO:0007480	decreased spatial extent of subtelomeric heterochromatin assembly	(Figure 2D) reduced heterochromatin spreading at mating-type and subtelomeric heterochromatin
PMID:34731638	FYPO:0007891	decreased spatial extent of mating-type region heterochromatin assembly	(Figure 2D) reduced heterochromatin spreading at mating-type and subtelomeric heterochromatin
PMID:34731638	FYPO:0004604	decreased chromatin silencing at subtelomere	(Figure 4E)
PMID:34731638	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Figure 4E)
PMID:34731638	FYPO:0004604	decreased chromatin silencing at subtelomere	(Figure 4E)
PMID:34731638	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Figure 4E)
PMID:34731638	GO:0000791	euchromatin	(Figure S1E)
PMID:34731638	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Figure S2F)
PMID:34731638	FYPO:0004137	decreased histone H3-K9 dimethylation at subtelomeric heterochromatin during vegetative growth [has_severity] low	(Figures 1B, 1C, S1D) only a subtle change of H3K9me2 at pericentromere
PMID:34731638	FYPO:0007894	increased histone H2B-K119 ubiquitination at subtelomeric heterochromatin during vegetative growth	(Figures 1E and S1D) we found increased signals of elongating RNAPII (RNAPII Ser2P) and H2B ubiquitination (H2Bub), a histone mark associated with active transcription
PMID:34731638	FYPO:0007895	increased histone H2B-K119 ubiquitination at pericentromeric heterochromatin during vegetative growth	(Figures 1E and S1D) we found increased signals of elongating RNAPII (RNAPII Ser2P) and H2B ubiquitination (H2Bub), a histone mark associated with active transcription
PMID:34731638	FYPO:0006631	decreased protein localization to chromatin [assayed_protein] PomBase:SPBP8B7.19	(Figures S2C-S2E) in chromatin/euchromatin
PMID:34731638	FYPO:0006631	decreased protein localization to chromatin [assayed_protein] PomBase:SPBC609.05	(Figures S2C-S2E) in chromatin/euchromatin
PMID:34731638	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPBC8D2.04 [has_severity] low	(Figures S4A-S4C) Histone H3 ChIP-seq revealed a small but reproducible reduction of H3 at subtelomeres in pob3Δ
PMID:34731638	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPBC1105.11c [has_severity] low	(Figures S4A-S4C) Histone H3 ChIP-seq revealed a small but reproducible reduction of H3 at subtelomeres in pob3Δ
PMID:34731638	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC1834.04	(Figures S4A-S4C) Histone H3 ChIP-seq revealed a small but reproducible reduction of H3 at subtelomeres in pob3Δ
PMID:34731638	FYPO:0002360	normal chromatin silencing at centromere	(comment: vw: changed from decreased to normal because look WT?)
PMID:34731638	FYPO:0004542	increased chromatin silencing at subtelomere [has_severity] medium	(fig 1G ) (comment: vw: changed to increased -compared to WT)
PMID:34731638	FYPO:0006299	increased chromatin silencing at centromere outer repeat	(fig 1G ) (comment: vw: changed to increased -compared to WT)
PMID:34731638	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth	Although degradation of Epe1 still occurs in pob3Δ in S phase, we found increased steady-state levels of Epe1 in cycling cells (Figure S3A).
PMID:34731638	FYPO:0004577	decreased histone H3-K9 trimethylation at subtelomeric heterochromatin during vegetative growth	Intriguingly, while H3K9me2 levels were unaltered in spt16-1, H3K9me3 levels were reduced at several loci at the TEL1L subtelomeric region (i.e., SPAC212.09c, SPAC212.08c, and SPAC212.06c; compare Figure 4B with 4A)
PMID:34731638	FYPO:0002360	normal chromatin silencing at centromere	Moreover, epe1Δ reduced the expression of several subtelomeric genes in pob3Δ, suggesting that it also counteracts heterochromatin spreading (Figure 3G)
PMID:34731638	FYPO:0007892	increased histone exchange at subtelomeric heterochromatin	Nonetheless, the pob3Δ mutant exhibited increased incorporation of H3-T7 at the TEL1L region (Figure 4G), implying that the H3 turnover rate is increased at subtelomeric heterochromatin.
PMID:34731638	FYPO:0004604	decreased chromatin silencing at subtelomere	Partial suppression of pob3∆ silencing phenotype.
PMID:34731638	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	To test this more directly, we performed the HSS assay in the double spt16-1epe1Δ mutant. Indeed, heterochromatin spreading was completely restored (Figure 3H, compare with Figure 2D)
PMID:34731638	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC664.01c	found reduced Swi6 binding in spt16-1 at subtelomeric genes close to the heterochromatin boundary (SPAC212.12, SPAC212.06c; Figure 4D).
PMID:34731638	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	synthetic defect in the silencing of dg and tlh1/2 transcripts (Figure 4C)
PMID:34731638	FYPO:0005917	increased subtelomeric heterochromatin RNA level	we observed derepression of several subtelomeric genes (Figures 2E and S2G).
PMID:34731638	FYPO:0005917	increased subtelomeric heterochromatin RNA level	we observed derepression of several subtelomeric genes (Figures 2E and S2G).
PMID:34738170	FYPO:0001357	normal vegetative cell population growth	A serial dilution spotting assay (Fig. 2B) showed that the growth of och1Δ with either pAL-pwp1+ or pAU-pwp1+ was as fast as that of wild-type cells, indicating that the growth defect of och1Δ cells was alleviated by expression of pwp1+.
PMID:34738170	FYPO:0001357	normal vegetative cell population growth	A serial dilution spotting assay (Fig. 2B) showed that the growth of och1Δ with either pAL-pwp1+ or pAU-pwp1+ was as fast as that of wild-type cells, indicating that the growth defect of och1Δ cells was alleviated by expression of pwp1+.
PMID:34738170	FYPO:0001357	normal vegetative cell population growth	A serial dilution spotting assay (Fig. 2B) showed that the growth of och1Δ with either pAL-pwp1+ or pAU-pwp1+ was as fast as that of wild-type cells, indicating that the growth defect of och1Δ cells was alleviated by expression of pwp1+.
PMID:34798057	FYPO:0005599	increased duration of meiosis I	(Figure 6E) When dus3D diploids were induced to enter meiosis, the time needed in prophase for spindle assembly in MI was increased, while a marked increase in the duration of metaphase was noted in both MI and MII (Figures 6D-6H).
PMID:34798057	FYPO:0000708	decreased mating efficiency	(Figure S1D)
PMID:34798057	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Figure S7A)
PMID:34798057	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Figure S7A)
PMID:34798057	FYPO:0002091	lagging meiotic chromosomes	(Figures 6I, 6J)
PMID:34798057	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPBC16A3.15c	(comment: CHECK V348A)
PMID:34798057	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(comment: weird!) Intriguingly, the double nda2noD nda3noD mutant was less sensitive than the single ones. Therefore, a possible explanation for the lower sensitivity of the double mutant is that defects resulting from the elevated level of one monomer are compensated for by a similar overexpression of the second monomer.
PMID:34798057	FYPO:0000708	decreased mating efficiency	Both mutants displayed meiosis defects with a reduction in gamete numbers and viability more marked in the nda2noD mutant (Figures 6A, 6B, and 6C).
PMID:34805795	FYPO:0001987	sensitive to high pH [has_severity] low	(Figure 4F) (comment: CONDITION ph9)
PMID:34805795	FYPO:0001987	sensitive to high pH [has_severity] low	(Figure 4F) (comment: CONDITION ph9)
PMID:34805795	FYPO:0001159	increased cellular pH	(Figure 4d) (comment: vw: assayed vacuolar pH as a surrogate for V-ATPase activity)
PMID:34805795	FYPO:0007909	increased vacuolar pH	(Figure 4d) (comment: vw: assayed vacuolar pH as a surrogate for V-ATPase activity)
PMID:34805795	FYPO:0000077	resistance to rapamycin [has_severity] medium	(Figure 5)
PMID:34805795	FYPO:0000077	resistance to rapamycin [has_severity] medium	(Figure 5)
PMID:34805795	FYPO:0006266	normal vacuole size during vegetative growth	(Figure S1A)
PMID:34805795	FYPO:0006266	normal vacuole size during vegetative growth	(Figure S1A)
PMID:34805795	FYPO:0000077	resistance to rapamycin [has_severity] medium	(Figure S1A)
PMID:34805795	FYPO:0000077	resistance to rapamycin [has_severity] medium	(Figure S1A)
PMID:34805795	FYPO:0006233	decreased protein localization to vacuolar membrane [has_severity] low [assayed_protein] PomBase:SPBC24C6.08c	(Figure S3) Bhd1 and Fnp1 localize to vacuoles in response to amino acid starvation and that this localization is largely independent of the presence of the other protein.
PMID:34805795	FYPO:0006233	decreased protein localization to vacuolar membrane [assayed_protein] PomBase:SPAC30C2.07 [has_severity] low	(Figure S3) Bhd1 and Fnp1 localize to vacuoles in response to amino acid starvation and that this localization is largely independent of the presence of the other protein.
PMID:34805795	FYPO:0000636	increased cell population growth rate [assayed_protein] PomBase:SPAC13G6.07c	(comment: CONDITION during amino acid starvation)
PMID:34805795	FYPO:0000636	increased cell population growth rate [assayed_protein] PomBase:SPAC13G6.07c	(comment: CONDITION during amino acid starvation)
PMID:34805795	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPAC13G6.07c	(comment: CONDITION during amino acid supplementation) (Figures 2G and S4), demonstrating that the BFC, is required for efficient activation of TORC1 following amino acid supplementation.
PMID:34805795	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPAC13G6.07c	(comment: CONDITION during amino acid supplementation) (Figures 2G and S4), demonstrating that the BFC, is required for efficient activation of TORC1 following amino acid supplementation.
PMID:34805795	GO:1904263	positive regulation of TORC1 signaling [happens_during] cellular response to amino acid stimulus	BFC augments TORC1 activation in response to amino acid stimulation
PMID:34805795	GO:0000329	fungal-type vacuole membrane [exists_during] cellular response to amino acid starvation	Bhd1 and Fnp1 appear diffusely distributed throughout the cytoplasm in amino acid replete conditions, but localize to vacuoles in response to amino acid starvation evidenced by the strong overlap between Bhd1-/Fnp1-GFP and the FM4-64 dye under amino acid starvation conditions (Figures 2A-2F)
PMID:34805795	GO:1904262	negative regulation of TORC1 signaling [happens_during] cellular response to amino acid starvation	results in a significant growth advantage of BFC mutant over wild-type strains when equal number of log phase cells are grown on rapamycin-containing EMM plates supplemented with amino acids (Figures S1A and S1B). Moreover, treating cells with 125 or 150 ng/mL of rapamycin for 90 min revealed that the growth advantage of BFC mutants correlates with an increase in P-Rps6 levels compared to wild-type cells (Figure S5C). Together, these data support a model in which BFC participates in TORC1 repression.
PMID:34810257	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPBC11C11.03 [occurs_in] chromosome, centromeric region [happens_during] mitotic M phase [part_of] kinetochore assembly	((comment: CHECK ndc80) These co-IP experiments showed that the interaction between Ndc80 and CENP-TCnp20 is drastically increased during mitosis (Fig. 7C), supporting the idea that the presence of Ccp1 interferes with the interaction between Ndc80 and CENP-TCnp2
PMID:34810257	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC36B7.08c [assayed_protein] PomBase:SPBC800.13	(Fig. 3) Our results indicate that the first 55 amino acids of CENP-TCnp20 are the minimal interaction domain with Ccp1, which we named the Ccp1- interacting motif (CIM).
PMID:34810257	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC36B7.08c [assayed_protein] PomBase:SPBC800.13	(Fig. 3) Our results indicate that the first 55 amino acids of CENP-TCnp20 are the minimal interaction domain with Ccp1, which we named the Ccp1- interacting motif (CIM). Yeast two hybrid
PMID:34810257	FYPO:0000091	sensitive to thiabendazole	(Fig. 4 E and F).
PMID:34810257	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPBC36B7.08c [occurs_in] chromosome, centromeric region [happens_during] mitotic interphase	(These data suggest that phosphorylation of the CIM domain leads to disassociation of Ccp1 from centromeres. CIM domain) Together,our data indicate that CENP-TCnp20 is required for Ccp1 centromere localization
PMID:34810257	FYPO:0001796	protein mislocalized to centromere [assayed_protein] PomBase:SPBC36B7.08c	(comment: CHECK during mitotc M-phase) In contrast, we found that GFP-Ccp1 in all cnp20-14A mutant cells remains associated with centromeres during all the stages of the cell cycle (Fig. 6 B and C).
PMID:34810257	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPBC36B7.08c	But GFP-Ccp1 is completely disassociated from centromeric regions in cnp20-ΔCIM at all stages of the cell cycle (Fig. 4 C and D and SI Appendix, Fig. S13).
PMID:34810257	FYPO:0000141	abnormal mitotic sister chromatid segregation	But most cnp20-14A cells display mitotic delay, and more than 12% of mutant cells failed to complete chromosome segregation within 30 min (Fig. 6 E and F)
PMID:34810257	FYPO:0001571	increased protein-protein interaction [assayed_protein] PomBase:SPBC36B7.08c [assayed_protein] PomBase:SPBC800.13	Cnp20-14A showed a strong interaction with Ccp1 (Fig. 5F)
PMID:34810257	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPBC11C11.03	Consistent with the key role of CENP-TCnp20 in the assembly of the Ndc80 complex, we found that the association of Ndc80-GFP with centromeres is lost in cnp20-9 at the restrictive temperature (Fig. 2 C and D).
PMID:34810257	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC11C11.03 [assayed_protein] PomBase:SPBC800.13	However, we found that Spc25-GFP appeared not to attach to microtubules in ∼20% of cnp20-14A mitotic cells, indicating that dephosphorylation of the CIM domain leads to mislocalization of Ndc80C during mitosis (Fig. 7A). Importantly, our co-IP results indicated that the interaction between Cnp20-14A and Ndc80 is significantly reduced during mitosis (Fig. 7B).
PMID:34810257	FYPO:0000450	decreased protein localization to centromere during vegetative growth [has_severity] low [assayed_protein] PomBase:SPBC1105.17	In addition, we found that CENP-ACnp1-GFP partially reduced its centromere localization in cnp20-9 at the restrictive temperature (SI Appendix, Fig. S6).
PMID:34810257	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPBC800.13 [happens_during] mitotic M phase [part_of] positive regulation of kinetochore assembly	These data demonstrate that CDK1 is capable of phosphorylating the CIM domain of CENP-TCnp20. Various slow migrating bands were observed in the assay with Cnp201-55 (Fig. 7D), indicating that the domain contains multiple phosphorylation sites, consistent with our point mutation analysis. (ASSAYED USING HUMAN CDK1)
PMID:34810257	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPBC36B7.08c	We found that GFP-Ccp1 was delocalized from centromeres at the restrictive temperature in cnp20-9 at all stages of the cell cycle (Fig. 2 E and F and SI Appendix, Fig. S3)
PMID:34810257	FYPO:0000091	sensitive to thiabendazole	We found that cnp20-14A is highly sensitive to TBZ, even more strongly than the cnp20-ΔCIM mutant (Fig. 6D and SI Appendix, Fig. S16)
PMID:34810257	FYPO:0002574	normal protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPBC800.13	We next checked the distribution of CENP-TCnp20-GFP in ccp1Δ and found that its centromere localization was unaffected in the mutant (Fig. 2 G-I).
PMID:34810257	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC800.13 [assayed_protein] PomBase:SPBC36B7.08c	Yeast two hybrid The yeast two-hybrid assays showed that the Ccp1 homodimer mutant, Ccp1-4A, was unable to interact with CENP-TCnp20 (Fig. 3A and SI Appendix, Fig. S8)
PMID:34810257	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC36B7.08c [assayed_protein] PomBase:SPBC800.13	Yeast two hybrid To investigate how phosphorylation of the CIM domain affects the interaction between Ccp1 and CENP-TCnp20, we conducted yeast two-hybrid assays with Cnp20-14D and Ccp1. We found that the interaction between Cnp20-14D and Ccp1 was dramatically reduced (Fig. 5F).
PMID:34810257	FYPO:0000450	decreased protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPBC36B7.08c [has_severity] low	whereas the localization of GFP-Ccp1 at centromeres only has a mild reduction in the CENP-A ts mutant, cnp1-1 (SI Appendix, Fig. S4).
PMID:34810257	FYPO:0000450	decreased protein localization to centromere during vegetative growth [has_severity] low [assayed_protein] PomBase:SPBC800.13	whereas the localization of GFP-Ccp1 at centromeres only has a mild reduction in the CENP-A ts mutant, cnp1-1 (SI Appendix, Fig. S4).
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	(Figure 3A)
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	(Figure 3A)
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	(Figure 3A)
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	(Figure 3A)
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	(Figure 3A)
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	(Figure 3A)
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	(Figure 3A)
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	(Figure 3A)
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	(Figure 3A)
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	(Figure 3A)
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	(Figure 3A)
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	(Figure 3A)
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	(Figure 3B)
PMID:34849791	FYPO:0000091	sensitive to thiabendazole	(Figure 3B)
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	(Figure 3B)
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	(Figure 3B)
PMID:34849791	FYPO:0000091	sensitive to thiabendazole	(Figure 3B)
PMID:34849791	FYPO:0000091	sensitive to thiabendazole	(Figure 3B)
PMID:34849791	FYPO:0000091	sensitive to thiabendazole	(Figure 3B)
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	(Figure 3B)
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	(Figure 3B)
PMID:34849791	FYPO:0000091	sensitive to thiabendazole	(Figure 3B)
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	(Figure 3B)
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	(Figure 3B)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 13	(Figure 4)
PMID:34849791	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 55	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 48	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 59	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 52	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 51	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 10	(Figure 4)
PMID:34849791	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 10	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 11	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 11	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 14	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 14	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 13	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 12	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 17	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 10	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 10	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 10	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 13	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 10	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 14	(Figure 4)
PMID:34849791	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 13	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 12	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 16	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 15	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 14	(Figure 4)
PMID:34849791	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 10	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 10	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 10	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 16	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 11	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 15	(Figure 4)
PMID:34849791	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 4)
PMID:34849791	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 11	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 10	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 17	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 11	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 13	(Figure 4)
PMID:34849791	FYPO:0001513	normal mitotic sister chromatid segregation	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 9	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 12	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 9	(Figure 4)
PMID:34849791	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 11	(Figure 4)
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S1B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S1B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S1B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S1B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S1B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S1B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S1B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S1B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S1B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S1B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S1B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S1B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S2B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S2B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S2B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S2B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S2B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S2B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S2B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S2B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S2B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S2B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S2B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S2B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S3B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S3B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S3B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S3B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S3B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S3B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S3B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S3B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S3B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S3B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S3B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S3B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S4B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S4B
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S4B
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S4B
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	Supplemental Figure S4B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S4B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S5B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S5B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S5B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S5B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S5B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S5B
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	Supplemental Figure S5B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S5B
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	Supplemental Figure S5B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S5B
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	Supplemental Figure S5B
PMID:34849791	FYPO:0000082	decreased cell population growth at high temperature	Supplemental Figure S5B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S6B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S6B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S6B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S6B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S6B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S6B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S6B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S6B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S6B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S6B
PMID:34849791	FYPO:0000964	normal growth on thiabendazole	Supplemental Figure S6B
PMID:34849791	FYPO:0000674	normal cell population growth at high temperature	Supplemental Figure S6B
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: G1M5 63%, M5 37%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: G1M6 72%, M6 28%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: G1M7 80%, M7 20%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: G1M9 100%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: G2M5 73%, G1M5 21%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: G2M6 19%, G1M6 46%, M6 35%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: G2M7 68%, M7 32%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: G2M9 52%, G1M9 48%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: G3M5 85%, G1M5 2%, M5 13%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: G3M6 24%, G2M6 48%, G1M6 10%, M6 18%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: G3M7 85%, G1M7 7%, M7 8%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: M5 100%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: M6 100%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: M7 100%)
PMID:34851357	FYPO:0008420	abnormal dolichol-linked oligosaccharide biosynthetic process	(comment: LLOs synthesized: M9 100%)
PMID:34851403	FYPO:0003613	normal meiotic sister chromatid cohesion during meiotic prophase I [has_penetrance] complete	Additionally, the DNA replication checkpoint function of Mrc1 is not required for sister kinetochore association, because deletion of cds1, which encodes an effector kinase functioning downstream of Mrc1 in the DNA replication checkpoint pathway (Alcasabas et al., 2001; Murakami and Okayama, 1995; Tanaka and Russell, 2001), did not affect the kinetochore association state or sister chromatid segregation (Fig. 3C,E; Fig. S2C).
PMID:34851403	FYPO:0006425	normal meiotic sister chromatid cohesion at centromere during meiosis I [has_penetrance] complete	In cells lacking Sgo1 (sgo1Δ), which protects centromeric cohesin during anaphase, no separated kinetochore signals were observed (Fig. 3A,C), although sister chromatids frequently underwent equational segregation in the absence of chiasmata (Fig. S2B).
PMID:34851403	FYPO:0005648	sister kinetochore dissociation in meiotic metaphase I	In mrc1Δ cells, sister kinetochores and centromere cores separated at a low, but significant, level (Fig. 3A-D; Figs S2C and S3A,B), and non-separated signals were significantly wider in shape (Fig. 3E,F; Fig. S3C,D).
PMID:34851403	FYPO:0005648	sister kinetochore dissociation in meiotic metaphase I	Non-separated signals were found to be significantly or nearly significantly wider than in wild-type cells (Fig. 3E,F;)
PMID:34864879	FYPO:0002061	inviable vegetative cell population	As shown in Figure 2a, cells overproducing Cut7 under the induced condition is lethal
PMID:34864879	FYPO:0003787	long mitotic spindle microtubules protruding beyond spindle pole body	Observation of spindle morphology showed that cells in which either Cut7 or Eg5-NLS is overproduced displayed the emergence of protruding spindles, which was never observed in the vector control strain. In these cells, the spindle MTs extended away from one side or both sides of the spindle poles, in which the spindle pole bodies (SPBs, fungi equivalents of animal centrosomes) localized to the MT tips (Figure 2b).
PMID:34864879	FYPO:0000276	monopolar mitotic spindle	We notified that a small percentage of either Eg5-NLS or Cut7 overproducing cells showed the monopolar spindle phenotype (Figure 2c; after 18 h, 10% for Cut7 vs 11% for Eg5-NLS).
PMID:34910579	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] high	(Figure 1C,D)
PMID:34910579	FYPO:0001188	sensitive to Calcofluor White	(Figure 2A)
PMID:34910579	FYPO:0000650	increased septation index	(comment: 38.5% cf WT 11.5%, cannot put % on population phenotype) Figure 1F
PMID:34910579	FYPO:0002442	normal protein localization to cell division site [assayed_protein] PomBase:SPCC1281.01	(comment: CONDITION 36 degrees)
PMID:34910579	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPBC19G7.05c	(comment: CONDITION 36 degrees)
PMID:34910579	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPAC14C4.09	(comment: CONDITION 36 degrees)
PMID:34910579	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPAC26H5.08c	(comment: CONDITION 36 degrees)
PMID:34910579	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPCC1840.02c	(comment: CONDITION 36 degrees)
PMID:34910579	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPBP22H7.03	(comment: CONDITION 36 degrees)
PMID:34910579	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPBC19G7.05c	(comment: CONDITION 36 degrees)
PMID:34910579	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC1840.02c	(comment: CONDITION 36 degrees)
PMID:34910579	FYPO:0002442	normal protein localization to cell division site [assayed_protein] PomBase:SPCC1281.01	(comment: CONDITION 36 degrees)
PMID:34910579	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPAC18G6.03	(comment: CONDITION 36 degrees)
PMID:34910579	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPCC1840.02c [part_of] mitotic division septum assembly	(comment: recruits glucanases and glucan synthases to division site)
PMID:34910579	FYPO:0004292	abnormal septum	Supplemental Figure S2, A-D
PMID:34910579	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] high	Supplemental Figure S2, A-D
PMID:34910579	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPBC19G7.05c [part_of] mitotic division septum assembly	Together, these results confirmed that Sbg1 is specific to Bgs1, while Smi1 regulates the levels of both Bgs4 and Bgs1 at the division site, with a more important role for Bgs4 (Figure 7, A-C).
PMID:34910579	FYPO:0003890	abnormal primary cell septum biogenesis	We confirmed the defects in septa ....... In cells with closed septa, the primary septum was uneven (Figure 3, red arrows) and thinner in smi1-1 cells than in WT (Figure 3A).
PMID:34910579	FYPO:0005840	incomplete, asymmetric septum	We confirmed the defects in septa ....... In cells with closed septa, the primary septum was uneven (Figure 3, red arrows) and thinner in smi1-1 cells than in WT (Figure 3A).
PMID:34910579	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPBC19G7.05c [part_of] mitotic division septum assembly	recruits glucanases and glucan synthases to division site
PMID:34951983	GO:0007052	mitotic spindle organization	Microtubule dynamics required for spindle repair following laser ablation
PMID:34951983	GO:0007052	mitotic spindle organization	Not required for spindle repair following laser ablation
PMID:34951983	GO:0007052	mitotic spindle organization	required for spindle repair following laser ablation
PMID:34951983	GO:0007052	mitotic spindle organization	required for spindle repair following laser ablation
PMID:34958661	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high	(Fig. S1A) (comment: 24.6 micron)
PMID:34958661	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high	(Fig. S1A) (comment: 26.6 micron)
PMID:34958661	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] high	(Fig. S1A) (comment: 27 micron)
PMID:34958661	GO:0010971	positive regulation of G2/M transition of mitotic cell cycle	(Figure 1)
PMID:34958661	GO:0010971	positive regulation of G2/M transition of mitotic cell cycle	(Figure 1)
PMID:34958661	FYPO:0006326	decreased protein localization to medial cortical node [assayed_protein] PomBase:SPCC4B3.15	(comment: CHECK actually mid1-Nter)
PMID:34958661	GO:0043495	protein-membrane adaptor activity [has_input] PomBase:SPAC57A10.02 [part_of] positive regulation of G2/M transition of mitotic cell cycle	(comment: Modified form is indirect because GDP bound does not localize to nodes) These defects indicate that Arf6 anchors Cdr2 stably at nodes, meaning that Arf6 and Cdr2 reciprocally promote each other’s node localization.
PMID:34958661	FYPO:0007139	abolished protein localization to medial cortical node during mitotic interphase [assayed_protein] PomBase:SPBC1539.08	A GDP-locked mutant arf6(T52N)-mNG lost node localization, (Fig. 2 F)
PMID:34958661	FYPO:0002455	abnormal septum during vegetative growth	All three double mutants exhibited synthetic defects in cell growth and cytokinesis as judged by tilted and disorganized septa (Fig. 5, C-E; and Fig. S3 M).
PMID:34958661	FYPO:0002455	abnormal septum during vegetative growth	All three double mutants exhibited synthetic defects in cell growth and cytokinesis as judged by tilted and disorganized septa (Fig. 5, C-E; and Fig. S3 M).
PMID:34958661	FYPO:0002455	abnormal septum during vegetative growth	All three double mutants exhibited synthetic defects in cell growth and cytokinesis as judged by tilted and disorganized septa (Fig. 5, C-E; and Fig. S3 M).
PMID:34958661	GO:0110115	Cdr2 medial cortical node complex [exists_during] mitotic interphase	Arf6 localizes stably to Cdr2 nodes during interphase in a manner that depends on nucleotide binding, membrane binding, and Cdr2 itself.; strongly enriched at cortical nodes in the cell middle (Fig. 2 A). Arf6 and Cdr2 colocalized at nodes (Figs. 2 B and S2 A)
PMID:34958661	FYPO:0007139	abolished protein localization to medial cortical node during mitotic interphase [assayed_protein] PomBase:SPBC1539.08	Arf6 node localization required Cdr2 but not other node proteins (Figs. 2 E and S2 B).
PMID:34958661	FYPO:0007139	abolished protein localization to medial cortical node during mitotic interphase [assayed_protein] PomBase:SPBC1539.08	Further, Arf6 localization to nodes was lost upon deletion of its GEF Syt22 (Fig. 2 G
PMID:34958661	FYPO:0007133	normal protein localization to medial cortical node during mitotic interphase [assayed_protein] PomBase:SPBC1539.08	Indeed, arf6(Q75L)-mNG localized to nodes even in syt22Δ cells (Fig. 2 G)
PMID:34958661	FYPO:0006616	viable vegetative cell with increased cell diameter	The cell length at division phenotype for arf6Δ was minor, but these cells were wider than wild type (Fig. S1 E).
PMID:34958661	FYPO:0006326	decreased protein localization to medial cortical node [assayed_protein] PomBase:SPBC1539.08	The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I)
PMID:34958661	FYPO:0006326	decreased protein localization to medial cortical node [assayed_protein] PomBase:SPBC1539.08	The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I)
PMID:34958661	FYPO:0006326	decreased protein localization to medial cortical node [assayed_protein] PomBase:SPBC1539.08	The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I)
PMID:34958661	FYPO:0006326	decreased protein localization to medial cortical node [assayed_protein] PomBase:SPAC57A10.02 [has_severity] high	The resulting arf6 alleles reduced node localization and instead enriched at the cytoplasm (Fig. S2, H and I)
PMID:34958661	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC18B5.03	The slower-migrating, hyperphosphorylated form of Wee1 was lost in arf6Δ and syt22Δ, similar to cdr2Δ (Fig. 1 H). We conclude that activated Arf6 functions in the Cdr2 pathway to control cell size at division through inhibition of Wee1.
PMID:34958661	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC18B5.03	The slower-migrating, hyperphosphorylated form of Wee1 was lost in arf6Δ and syt22Δ, similar to cdr2Δ (Fig. 1 H). We conclude that activated Arf6 functions in the Cdr2 pathway to control cell size at division through inhibition of Wee1.
PMID:34958661	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC18B5.03	The slower-migrating, hyperphosphorylated form of Wee1 was lost in arf6Δ and syt22Δ, similar to cdr2Δ (Fig. 1 H). We conclude that activated Arf6 functions in the Cdr2 pathway to control cell size at division through inhibition of Wee1.
PMID:34958661	GO:0005085	guanyl-nucleotide exchange factor activity [has_input] PomBase:SPBC1539.08 [part_of] positive regulation of G2/M transition of mitotic cell cycle	This is from GIs, phenocopy, PLUS If the Arf6 localization defect in syt22Δ is due to loss of the GTP-bound state, then it should be suppressed by arf6(Q75L). Indeed, arf6(Q75L)-mNG localized to nodes even in syt22Δ cells (Fig. 2 G)
PMID:34958661	GO:0051285	cell cortex of cell tip	Ucp3-mNG localized to spots at the cell tips, which likely represent endocytic actin patches due to colocalization with actin patch component Pan1 (Fig. S2, E and F)
PMID:34958661	FYPO:0007139	abolished protein localization to medial cortical node during mitotic interphase [assayed_protein] PomBase:SPAC57A10.02	We combined arf6Δ with the mid1(400-450Δ) mutant that cannot bind Cdr2. In the resulting cells, Cdr2 was absent from the cell cortex and formed large cytoplasmic puncta (Figs. 4 A and S2 J).
PMID:34958661	FYPO:0007133	normal protein localization to medial cortical node during mitotic interphase [assayed_protein] PomBase:SPBC1539.08	but the GTP-locked allele arf6(Q75L)-mNG remained at nodes (Fig. 2 F)
PMID:34958661	FYPO:0007139	abolished protein localization to medial cortical node during mitotic interphase [assayed_protein] PomBase:SPAC57A10.02	o explain this connection, we examined the localization of Wee1 and Cdr1 at cortical nodes in arf6Δ mutants. Wee1 localized to nodes in arf6Δ, but Cdr1 did not (Fig. 3, D and E; and Fig. S3 D)
PMID:34958661	FYPO:0003482	increased punctate cytoplasmic protein localization [assayed_protein] PomBase:SPAC57A10.02	rf6Δ cells had cytoplasmic Cdr2 clusters that were absent in wild-type cells (Figs. 3 A and S2 J), indicating defects in cortical anchoring.
PMID:34958661	GO:0032153	cell division site [exists_during] mitotic cytokinesis	trongly enriched at cortical nodes in the cell middle (Fig. 2 A). Arf6 and Cdr2 colocalized at nodes (Figs. 2 B and S2 A)
PMID:34959732	FYPO:0001367	normal cytokinesis	(Figure 3A and Figure S1A. Table 3) (comment: CHECK Suppression of the lytic phenotype at cytokinesis)
PMID:34959732	FYPO:0000417	abolished cytokinesis	(Figure 3B,S1B) Also in the Table 3. Cytokinesis is blocked in both wild-type and pbr1-8 strains treated with lethal concentrations of the echinocandin drug anidulafungin, suggesting that this drug affects the function of Bgs4 and Bgs1 and/or Bgs3
PMID:34959732	FYPO:0000005	abnormal cell morphology	(Figure 4A,S2A) (comment: Sublethal concentrations of caspofungin)
PMID:34959732	FYPO:0000005	abnormal cell morphology	(Figure 4A,S2A) (comment: Sublethal concentrations of caspofungin)
PMID:34959732	FYPO:0000164	abnormal cell separation after cytokinesis	(Figure 4B and Figure S2B) Also in the Table 3. The pbr1-8 mutation partially suppresses the slowing cytokinesis caused by lethal concentrations of caspofungin, suggesting that besides Bgs4, this drug affects other Bgs subunits (Bgs1 and/or Bgs3)
PMID:34959732	FYPO:0001367	normal cytokinesis	(Figure 4B, S2B, Table 3) The pbr1-8 mutation partially suppresses the slowing cytokinesis caused by lethal concentrations of caspofungin, suggesting that besides Bgs4, this drug affects other Bgs subunits (Bgs1 and/or Bgs3)
PMID:34959732	FYPO:0002060	viable vegetative cell population	(Table 5 and Figure S3, and Figure S4C) Vegetative cell lysis caused by lethal and sublethal concentrations of micafungin is suppressed in the pbr1-8
PMID:34959732	FYPO:0002060	viable vegetative cell population	(Table 5 and Figure S3, and Figure S4C) Vegetative cell lysis caused by lethal and sublethal concentrations of micafungin is suppressed in the pbr1-8
PMID:34959732	FYPO:0001367	normal cytokinesis	(comment: (Sub lethal and lethat doese)) Figure 5 and Figure S3. Also in the Table 3.
PMID:34959732	FYPO:0001367	normal cytokinesis	(comment: (Sub lethal and lethat doese)) Figure 5 and Figure S3. Also in the Table 3.
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	(comment: Northern Blotting, RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPAC27D7.03c	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPAC3F10.10c	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPAC29A4.12c	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPAC513.03	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBC21D10.06c	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPAC1F7.08	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPAC1F7.07c	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBC947.05c	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPAC11E3.06	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPCC1795.06	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBC8E4.12c	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBC4F6.09	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBC106.02c	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPCC1183.12	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPCC188.12	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPAC343.12	(comment: RNA-Seq)
PMID:34967420	FYPO:0000780	increased transcription during vegetative growth [assayed_transcript] PomBase:SPBC359.06	(comment: RNA-Seq)
PMID:35008733	FYPO:0006378	normal protein localization to endoplasmic reticulum during vegetative growth [assayed_protein] PomBase:SPBC3E7.15c	(Fig. 3) Live cell imaging revealed that GFP-Lac1 and Lag1-GFP remain localized at the ER in the absence of Lag1 or Lac1 respectively, indicating that their ER localizations are not interdependent.
PMID:35008733	FYPO:0006378	normal protein localization to endoplasmic reticulum during vegetative growth [assayed_protein] PomBase:SPAC1A6.09c	(Fig. 3) Live cell imaging revealed that GFP-Lac1 and Lag1-GFP remain localized at the ER in the absence of Lag1 or Lac1 respectively, indicating that their ER localizations are not interdependent.
PMID:35008733	FYPO:0006133	increased cellular phytosphingosine level	(Fig. 5b) We detected an accumulation of PHS and sphingoid bases-1-phosphate levels (PHS-1P or DHS-1P)
PMID:35008733	FYPO:0005593	increased cellular inositol phosphorylceramide level	Additionally, the pattern of complex sphingolipids in Lac1-depleted cells shows a strong accumulation of IPC and the appearance of new bands that might correspond to different IPC species
PMID:35008733	FYPO:0006823	viable small vegetative cell with slow cell growth [has_penetrance] high	Live cell imaging revealed that GFP-Lac1 and Lag1-GFP remain localized at the ER in the absence of Lag1 or Lac1 respectively, indicating that their ER localizations are not interdependent.
PMID:35011726	GO:0061631	ubiquitin conjugating enzyme activity	(Figure 1A)
PMID:35011726	GO:0061631	ubiquitin conjugating enzyme activity	(Figure 1A)
PMID:35011726	GO:0061630	ubiquitin protein ligase activity [has_input] PomBase:SPCC645.04	(Figure 1A) The MS analysis of the Nse1/3/4- and Ubc13/Mms2-containing in vitro ubiquitination assay led to the identification of Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4).
PMID:35011726	GO:0061630	ubiquitin protein ligase activity [has_input] PomBase:SPBC20F10.04c	(Figure 1A) The MS analysis of the Nse1/3/4- and Ubc13/Mms2-containing in vitro ubiquitination assay led to the identification of Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4).
PMID:35011726	FYPO:0001913	abolished ubiquitin ligase activity	(Figure 2D
PMID:35011726	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Figure 3A) ubiquitin ligase mutant
PMID:35011726	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Figure 3A) ubiquitin ligase mutant
PMID:35011726	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC550.05 [assayed_protein] PomBase:SPAC11E3.04c	Among the Nse1-bound factors, we repeatedly observed the Ubc13, Mms2, and Uba1 (Data File S1A,B, Data File S2A-C—ProteomeXchange: PXD029573, and Table S3).
PMID:35011726	FYPO:0000963	normal growth on hydroxyurea	Interestingly, the addition of nse1- C216S mutation suppressed the R188E phenotypes (Figure 3A), suggesting that it leads to a ubiquitin-ligase-independent outcome.
PMID:35011726	FYPO:0000957	normal growth on methyl methanesulfonate	Interestingly, the addition of nse1- C216S mutation suppressed the R188E phenotypes (Figure 3A), suggesting that it leads to a ubiquitin-ligase-independent outcome.
PMID:35011726	FYPO:0002061	inviable vegetative cell population	Nse1- R188E mutant shows synthetic lethality with smc6-74
PMID:35011726	FYPO:0002061	inviable vegetative cell population	Nse1- R188E mutant shows synthetic lethality with smc6-74
PMID:35011726	MOD:01148	ubiquitinylated lysine [added_by] PomBase:SPCC550.05	Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4).
PMID:35011726	MOD:01148	ubiquitinylated lysine [added_by] PomBase:SPCC550.05	Nse4 ubiquitination at K181 and Nse3 at K195 (Data Files S3 and S4).
PMID:35011726	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	The Nse1 ubiquitin ligase mutant showed a synthetic relationship with the Nse2 SUMO ligase mutant (C195S, H197A), indicating their separate roles in SMC5/6 function
PMID:35011726	FYPO:0001357	normal vegetative cell population growth	These synthetic phenotypes were again suppressed by the nse1-C216S mutation (Figure S5).
PMID:35011726	FYPO:0001355	decreased vegetative cell population growth	severe growth defects with smc6-X and nse6∆
PMID:35011726	FYPO:0001355	decreased vegetative cell population growth	severe growth defects with smc6-X and nse6∆
PMID:35011726	FYPO:0001355	decreased vegetative cell population growth	severe growth defects with smc6-X and nse6∆
PMID:35011726	FYPO:0001355	decreased vegetative cell population growth	severe growth defects with smc6-X and nse6∆
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 10A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 10A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 10A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 10A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 10A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 10A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 10A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 10A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 10A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 10A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 10A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 10A)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:35012333	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:35012333	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:35012333	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:35012333	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 11A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 11A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 11A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 11A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 11A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 11A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 11A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 11A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 11A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 11A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 11A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 11A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 11A)
PMID:35012333	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 11B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 11B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 11B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 11B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 11B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 11B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 11B)
PMID:35012333	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 11B)
PMID:35012333	FYPO:0008028	decreased rate of acid phosphatase activation during phosphate starvation	(Fig. 12A)
PMID:35012333	FYPO:0008027	increased rate of acid phosphatase activation during phosphate starvation	(Fig. 12B)
PMID:35012333	FYPO:0008027	increased rate of acid phosphatase activation during phosphate starvation	(Fig. 12B)
PMID:35012333	FYPO:0008027	increased rate of acid phosphatase activation during phosphate starvation	(Fig. 12B)
PMID:35012333	FYPO:0008024	decreased cellular polyphosphate level [has_severity] high	(Fig. 13)
PMID:35012333	FYPO:0008024	decreased cellular polyphosphate level [has_severity] high	(Fig. 13)
PMID:35012333	FYPO:0007816	increased cellular polyphosphate level [has_severity] high	(Fig. 13)
PMID:35012333	FYPO:0007820	polyphosphate absent from cell	(Fig. 13)
PMID:35012333	FYPO:0008024	decreased cellular polyphosphate level [has_severity] high	(Fig. 13)
PMID:35012333	FYPO:0008024	decreased cellular polyphosphate level [has_severity] low	(Fig. 13)
PMID:35012333	FYPO:0008024	decreased cellular polyphosphate level [has_severity] high	(Fig. 13)
PMID:35012333	FYPO:0007816	increased cellular polyphosphate level [has_severity] low	(Fig. 13)
PMID:35012333	FYPO:0007816	increased cellular polyphosphate level [has_severity] medium	(Fig. 13)
PMID:35012333	FYPO:0007816	increased cellular polyphosphate level [has_severity] high	(Fig. 13)
PMID:35012333	FYPO:0007816	increased cellular polyphosphate level [has_severity] medium	(Fig. 13)
PMID:35012333	FYPO:0007820	polyphosphate absent from cell	(Fig. 13)
PMID:35012333	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1A)
PMID:35012333	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:35012333	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature [has_severity] low	(Fig. 1A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature [has_severity] low	(Fig. 1A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 2A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature [has_severity] low	(Fig. 2A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature [has_severity] low	(Fig. 2A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature [has_severity] low	(Fig. 2A)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2B)
PMID:35012333	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2B)
PMID:35012333	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 4)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 4A)
PMID:35012333	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4B)
PMID:35012333	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4B)
PMID:35012333	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4B)
PMID:35012333	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4B)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 5A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	(Fig. 5A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 5A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 5A)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 6A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 6A)
PMID:35012333	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:35012333	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 7A)
PMID:35012333	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 7A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature [has_severity] low	(Fig. 7A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 7A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. 7A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	(Fig. 7A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	(Fig. 7A)
PMID:35012333	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:35012333	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:35012333	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature [has_severity] low	(Fig. 8A)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	(Fig. 8A)
PMID:35012333	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 8B)
PMID:35012333	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 8B)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S2)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S3)
PMID:35012333	FYPO:0002085	normal vegetative cell growth	(Fig. S3)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S3)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S3)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature	(Fig. S4)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S4)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S4)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature	(Fig. S4)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature	(Fig. S4)
PMID:35012333	FYPO:0000080	decreased cell population growth at low temperature	(Fig. S4)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S5A)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S5A)
PMID:35012333	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S5B)
PMID:35012333	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S5B)
PMID:35012333	FYPO:0008024	decreased cellular polyphosphate level [has_severity] low	(Fig. S6)
PMID:35012333	FYPO:0007820	polyphosphate absent from cell	(Fig. S6)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S7)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S7)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S7)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S7)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S7)
PMID:35012333	FYPO:0001357	normal vegetative cell population growth	(Fig. S7)
PMID:35012333	FYPO:0002061	inviable vegetative cell population	(comment: Described in Garg et al. PMID:33010152)
PMID:35012333	FYPO:0002061	inviable vegetative cell population	(comment: Described in Garg et al. PMID:33010152)
PMID:35012333	GO:0006799	polyphosphate biosynthetic process	(comment: from polyphosphate absent from cell)
PMID:35024575	FYPO:0004842	protein mislocalized to cytoplasm [assayed_protein] PomBase:SPAC688.11 [has_penetrance] complete	Conclusion is dawn by comparing Fig. 1H and Fig. 1I in https://www.micropublication.org/journals/biology/micropub-biology-000508.
PMID:35024575	FYPO:0003482	increased punctate cytoplasmic protein localization [assayed_protein] PomBase:SPAC688.11 [has_penetrance] high	Conclusion is dawn by comparing Fig. 1H and Fig. 1I in https://www.micropublication.org/journals/biology/micropub-biology-000508.
PMID:35058438	FYPO:0008059	decreased K48-linked polyubiquitin binding [assayed_protein] PomBase:SPAC25H1.04	(Figure 1j)
PMID:35058438	FYPO:0008059	decreased K48-linked polyubiquitin binding [assayed_protein] PomBase:SPAC25H1.04	(comment: CHECK abolished) Figure 1E
PMID:35058438	FYPO:0008059	decreased K48-linked polyubiquitin binding [assayed_protein] PomBase:SPAC25H1.04	(comment: CHECK abolished) Figure 1E
PMID:35075549	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPBC1706.03	(Fig. 3). We found that Fzo1 protein was not degraded at late time points in the ∆rsv2 mutant
PMID:35075549	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPBC1706.03	(Fig. 5) We found that when Fzo1 protein was overexpressed, it was no longer degraded at late time points
PMID:35075549	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPBC1706.03	(Fig. S1) The results showed that Fzo1 protein was not degraded at late time points only in the Δubc8 mutant (Fig. 4). Fzo1 protein was not degraded in ∆rsv2 and Δubc8 mutants after longer incubation times (60 and 72 h)
PMID:35075549	GO:0010637	negative regulation of mitochondrial fusion [happens_during] cellular response to glucose starvation	(comment: -ve regulation stationary phase)
PMID:35075549	PomGeneEx:0000019	protein level decreased [during] single-celled organism vegetative growth phase	(comment: CHECK ****STATIONARY PhASE****) the protein level of Fzo1 is unstable during the stationary phase.
PMID:35079912	FYPO:0002015	sensitive to iron ion starvation [has_severity] high	(Figure 3A) 25 µM of iron chelator bathophenanthroline disulfonate (BPS) was added to YES media to create iron-depleted condition.
PMID:35079912	FYPO:0002015	sensitive to iron ion starvation [has_severity] medium	(Figure 3A) 25 µM of iron chelator bathophenanthroline disulfonate (BPS) was added to YES media to create iron-depleted condition.
PMID:35079912	FYPO:0005825	sensitive to iron [has_severity] medium	(Figure 3A) Fe2(SO4)3 was added to YES media for a final concentration of 2.75 mM.
PMID:35079912	FYPO:0005825	sensitive to iron [has_severity] medium	(Figure 3A) Fe2(SO4)3 was added to YES media for a final concentration of 2.75 mM.
PMID:35079912	FYPO:0000103	sensitive to copper [has_severity] high	We found that only Δfio1 cells were sensitive to Cu2+
PMID:35082773	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Figure 1A)
PMID:35082773	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 1A)
PMID:35082773	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	(Figure 2A) significantly longer than that of wild-type cells at 27◦C
PMID:35082773	FYPO:0001128	decreased septation index [has_severity] medium	(Figure 2B) ...which was recovered by the overexpression of ppk21+
PMID:35082773	FYPO:0001128	decreased septation index [has_severity] low	(Figure 2B) ...which was recovered by the overexpression of ppk21+
PMID:35082773	FYPO:0002061	inviable vegetative cell population	(Figure 2C) (comment: CONDITION 33 degrees)
PMID:35082773	FYPO:0000339	mislocalized septum during vegetative growth	(Figure 2D and Supplementary Figure 1) The results showed that the septation ring of the ksg1-208 delta-ppk21 double mutant was off-centered at 33◦C, which was more severe than that of ksg1-208 cells
PMID:35082773	FYPO:0000650	increased septation index [has_severity] high	(Figure 3C). In addition, the cdr2+ overexpressed wild-type cells showed a higher septation index than cdr2+ non-overexpressed wild-type cells at 35◦C
PMID:35082773	FYPO:0002527	increased duration of protein localization to cell division site [assayed_protein] PomBase:SPAC57A10.02	(Figure 4c) In contrast, a fraction of ksg1-208 cells showed septum or division site localized Cdr2-mEGFP in the dividing cells at 27◦C, indicating the cortex dissociation of Cdr2 was hindered.
PMID:35082773	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC24H6.05	(Figure 5A) In addition, the Cdc25 protein level decreased in Δppk21 and Δcdr2 cells as well, indicating the role of Ppk21 and Cdr2 on regulating Cdc25 protein level .
PMID:35082773	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC24H6.05	(Figure 5A) Western blot analysis showed that the level of Cdc25 protein was dramatically lower in ksg1-208 cells than that in wild-type cells, indicating that Ksg1 played a crucial role in the accumulation of Cdc25 protein
PMID:35082773	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC24H6.05	(Figure 5A). In addition, the Cdc25 protein level decreased in Δppk21 and Δcdr2 cells as well, indicating the role of Ppk21 and Cdr2 on regulating Cdc25 protein level
PMID:35082773	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC57A10.02 [has_severity] medium	(Figure 5A). we found that the protein level of Cdr2 in ksg1-208 cells was significantly lower than that in wild-type cells (Figures 4A, 4B)
PMID:35082773	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] medium	(Figures 2D, 2E) results showed that ksg1-208 Δppk21 cells exhibited a longer cell length than either ksg1-208 or Δppk21 cells at both 27 and 33◦C
PMID:35082773	FYPO:0003503	normal vegetative cell length	(Figures 3A, 3B) overexpression of cdr2+ also reversed the defects in the cell length and the septation index of ksg1-208 cells
PMID:35082773	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC57A10.02 [has_severity] low	(Figures 4A, 4B) we found that the protein level of Cdr2 in ksg1-208 cells was significantly lower than that in wild-type cells
PMID:35082773	FYPO:0000648	viable small vegetative cell	It should be noted that cdr2+ overexpressed wild-type cells showed a shorter cell length at 27◦C, but a longer cell length at 35◦C than cdr2+ non-overexpressed wild-type cells (Figure 3B).
PMID:35099006	FYPO:0000650	increased septation index [has_severity] medium	Increased percentage of septated cells at both permissive and restrictive temperature.
PMID:35099006	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	The growth rate of pkd2-B42 at the restrictive temperature of 36C or higher is 80% lower than wild-type cells.
PMID:35099006	GO:0009992	intracellular water homeostasis	pkd2 mutants show temporary deflation followed by reinflation. pkd2-B42 has 50% lower spring constant as measured by Atomic Force Microscopy implicating reduced cellular stiffness. This indicates a reduced ability of this mutant at maintaining cellular turgor.
PMID:35108037	FYPO:0004675	normal growth on dimethyl sulfoxide	(Fig. S2D)
PMID:35108037	FYPO:0004675	normal growth on dimethyl sulfoxide	(Fig. S2D)
PMID:35108037	FYPO:0004675	normal growth on dimethyl sulfoxide	(Fig. S2D)
PMID:35108037	GO:0005515	protein binding	(Figure 1B, 1D-F, 2B-E, 3A-B, S1A-B)
PMID:35108037	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPBC4F6.12	(Figure 2B) Pxl1(AxxA1-6) reduced binding to Cdc15C(aa441-end) compared to wild-type Pxl1
PMID:35108037	FYPO:0004470	decreased protein localization to actomyosin contractile ring during mitotic anaphase [assayed_protein] PomBase:SPBC4F6.12	(Figure 4A,C)
PMID:35108037	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPBC4F6.12	(Figure 4A,C)
PMID:35108037	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPBP4H10.04	(Figure 4B,D)
PMID:35108037	FYPO:0004470	decreased protein localization to actomyosin contractile ring during mitotic anaphase [assayed_protein] PomBase:SPBP4H10.04	(Figure 4B,D)
PMID:35108037	FYPO:0004470	decreased protein localization to actomyosin contractile ring during mitotic anaphase [assayed_protein] PomBase:SPBP4H10.04	(Figure 4B,D)
PMID:35108037	FYPO:0002562	delayed onset of protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPBC4F6.12	(Figure S1D-E)
PMID:35108037	FYPO:0001903	normal septation index	(Figure S2A-C)
PMID:35108037	FYPO:0001903	normal septation index	(Figure S2A-C)
PMID:35108037	FYPO:0002177	viable vegetative cell with normal cell morphology	(Figure S2A-C)
PMID:35108037	FYPO:0002177	viable vegetative cell with normal cell morphology	(Figure S2A-C)
PMID:35108037	FYPO:0002177	viable vegetative cell with normal cell morphology	(Figure S2A-C)
PMID:35108037	FYPO:0001903	normal septation index	(Figure S2A-C)
PMID:35108037	FYPO:0003809	normal growth on latrunculin A	(Figure S2D)
PMID:35108037	FYPO:0000674	normal cell population growth at high temperature	(Figure S2D)
PMID:35108037	FYPO:0001357	normal vegetative cell population growth	(Figure S2D)
PMID:35108037	FYPO:0003809	normal growth on latrunculin A	(Figure S2D)
PMID:35108037	FYPO:0002141	normal cell population growth at low temperature	(Figure S2D)
PMID:35108037	FYPO:0002141	normal cell population growth at low temperature	(Figure S2D)
PMID:35108037	FYPO:0000674	normal cell population growth at high temperature	(Figure S2D)
PMID:35108037	FYPO:0000674	normal cell population growth at high temperature	(Figure S2D)
PMID:35108037	FYPO:0003809	normal growth on latrunculin A	(Figure S2D)
PMID:35108037	FYPO:0001357	normal vegetative cell population growth	(Figure S2D) (25,29,32)
PMID:35108037	FYPO:0001357	normal vegetative cell population growth	(Figure S2D) (25,29,32)
PMID:35108037	FYPO:0002141	normal cell population growth at low temperature	(Figure S2D) (comment: CONDITION 19 degrees C)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0002060	viable vegetative cell population	(Figure S2E)
PMID:35108037	FYPO:0007828	normal actomyosin contractile ring maturation	(Figure S3A)
PMID:35108037	FYPO:0007828	normal actomyosin contractile ring maturation	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0001365	decreased rate of actomyosin contractile ring contraction	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0006187	normal rate of actomyosin contractile ring assembly	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0006187	normal rate of actomyosin contractile ring assembly	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0001365	decreased rate of actomyosin contractile ring contraction	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0004895	normal rate of actomyosin contractile ring contraction	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0007828	normal actomyosin contractile ring maturation	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0006187	normal rate of actomyosin contractile ring assembly	(Figure S3A) (comment: CONDITION 25C)
PMID:35108037	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPAC1F5.04c	(Figure S3B) (comment: CONDITION 25C)
PMID:35108037	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC4F6.12 [assayed_protein] PomBase:SPAC20G8.05c	(comment: CHECK in vitro binding assay) Figure 3B
PMID:35108037	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPBC4F6.12	(comment: in vitro binding assay with purified Cdc15 F-BAR domain and purified Pxl1) (Fig 1E)
PMID:35108037	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPBC4F6.12	Mutant bound Cdc15C1(aa600-end) as well as wild-type Pxl1 (Figure S1A)
PMID:35108037	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPBC4F6.12	Mutant reduced binding to Cdc15C1(aa600-end) compared to wild type Pxl1 (Figure S1A)
PMID:35108037	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPBC4F6.12	Mutant reduced binding to Cdc15C1(aa600-end) compared to wild type Pxl1 (Figure S1A)
PMID:35108037	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPBC4F6.12	Mutant reduced binding to Cdc15C1(aa600-end) compared to wild type Pxl1 (Figure S1A)
PMID:35108037	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPBC4F6.12	Pxl1 (aa177-188 P181A, P184A) abolished binding to Cdc15 SH3 and Cdc15C1(aa600-end), Figure 2D
PMID:35108037	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPBC4F6.12	Pxl1-AxxA1-3 bound Cdc15C1(aa600-end) just as well as wild type Pxl1 (Figure S1A)
PMID:35108037	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC20G8.05c [assayed_protein] PomBase:SPBC4F6.12	Pxl1-AxxA6 reduced binding to full-length Cdc15 (Figure 3A) and Cdc15 C1 (Figure S1A)
PMID:35108037	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC4F6.12 [assayed_protein] PomBase:SPAC20G8.05c	Pxl1-P18A reduced binding to full-length Cdc15 compared to wild-type Pxl1 (Figure 3A)
PMID:35108037	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC4F6.12 [assayed_protein] PomBase:SPAC20G8.05c	Pxl1-P18A+AxxA6 reduced binding to full-length Cdc15 compared to wild type Pxl1 (Figure 3A)
PMID:35157728	FYPO:0003555	normal chromatin silencing at subtelomere	(Figure 2A)
PMID:35157728	FYPO:0006742	normal transcription from MCB promoter	(Figure 2A)
PMID:35157728	FYPO:0006742	normal transcription from MCB promoter	(Figure 2A)
PMID:35157728	FYPO:0006742	normal transcription from MCB promoter	(Figure 2A)
PMID:35157728	FYPO:0003555	normal chromatin silencing at subtelomere	(Figure 2A)
PMID:35157728	FYPO:0003555	normal chromatin silencing at subtelomere	(Figure 2A)
PMID:35157728	FYPO:0003555	normal chromatin silencing at subtelomere	(Figure 2A)
PMID:35157728	FYPO:0003555	normal chromatin silencing at subtelomere	(Figure 2A)
PMID:35157728	FYPO:0003555	normal chromatin silencing at subtelomere	(Figure 2A)
PMID:35157728	FYPO:0003555	normal chromatin silencing at subtelomere	(Figure 2A)
PMID:35157728	FYPO:0003555	normal chromatin silencing at subtelomere	(Figure 2A)
PMID:35157728	FYPO:0003555	normal chromatin silencing at subtelomere	(Figure 2A)
PMID:35157728	FYPO:0003555	normal chromatin silencing at subtelomere	(Figure 2A)
PMID:35157728	FYPO:0003555	normal chromatin silencing at subtelomere	(Figure 2A)
PMID:35157728	FYPO:0003555	normal chromatin silencing at subtelomere	(Figure 2A)
PMID:35157728	FYPO:0000708	decreased mating efficiency [has_severity] low	(comment: 24%)
PMID:35157728	FYPO:0000708	decreased mating efficiency [has_severity] low	(comment: 25%)
PMID:35157728	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(comment: no supression)
PMID:35157728	FYPO:0005917	increased subtelomeric heterochromatin RNA level [has_severity] high [assayed_transcript] PomBase:SPAC186.06	120 fold. Fig 2
PMID:35157728	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPAC186.05c [has_severity] high	280 fold. Fig 2
PMID:35157728	FYPO:0005917	increased subtelomeric heterochromatin RNA level [assayed_transcript] PomBase:SPAC186.04c [has_severity] medium	30 fold. Fig 2
PMID:35157728	FYPO:0006395	normal histone H3-K9 acetylation at subtelomeric heterochromatin during vegetative growth	Consistently, we detected higher levels of H3K9Ac at subtelomeric genes in Δtor1 cells compared to wild type cells, and this defect was suppressed by either Δgcn5 or Δbdf2 (Fig 4C)
PMID:35157728	FYPO:0003223	normal histone H3-K9 acetylation during vegetative growth [has_severity] medium	Consistently, we detected higher levels of H3K9Ac at subtelomeric genes in Δtor1 cells compared to wild type cells, and this defect was suppressed by either Δgcn5 or Δbdf2 (Fig 4C)
PMID:35157728	FYPO:0006395	normal histone H3-K9 acetylation at subtelomeric heterochromatin during vegetative growth	Consistently, we detected higher levels of H3K9Ac at subtelomeric genes in Δtor1 cells compared to wild type cells, and this defect was suppressed by either Δgcn5 or Δbdf2 (Fig 4C)
PMID:35157728	FYPO:0003086	normal chromatin binding [assayed_protein] PomBase:SPAC1952.05 [assayed_region] MCB	Significantly, Δbdf2 restores low levels of Gcn5 binding at MBF promoters in Δtor1 cells under normal growth conditions and also restores the normal pattern of an increased level of Gcn5 in response to HU (Fig 6C).
PMID:35157728	FYPO:0003086	normal chromatin binding [assayed_protein] PomBase:SPAC1952.05 [assayed_region] MCB	Significantly, Δbdf2 restores low levels of Gcn5 binding at MBF promoters in Δtor1 cells under normal growth conditions and also restores the normal pattern of an increased level of Gcn5 in response to HU (Fig 6C).
PMID:35157728	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPAC1952.05	The Δbdf2 mutation also suppresses the elevated levels of Gcn5 at the subtelomeric chromatin in Δtor1 cells (Fig 4E).
PMID:35157728	GO:0000122	negative regulation of transcription by RNA polymerase II	Tor1 inhibits the binding of Gcn5 at sub-telomeric genes and MBF promoters
PMID:35157728	FYPO:0006740	increased protein localization to chromatin at MCB promoters during vegetative growth [assayed_protein] PomBase:SPAC1952.05	Unexpectedly, although there is no increase in MBF-dependent transcription, we detected an increase in Gcn5 binding at the promoters of cdc22+ or cdc18+ in Δtor1 or Δgad8 cells under normal or replication stress conditions (Fig 5A)
PMID:35157728	FYPO:0006740	increased protein localization to chromatin at MCB promoters during vegetative growth	Unexpectedly, although there is no increase in MBF-dependent transcription, we detected an increase in Gcn5 binding at the promoters of cdc22+ or cdc18+ in Δtor1 or Δgad8 cells under normal or replication stress conditions (Fig 5A)
PMID:35157728	FYPO:0006740	increased protein localization to chromatin at MCB promoters during vegetative growth [assayed_protein] PomBase:SPAC1952.05	Unexpectedly, although there is no increase in MBF-dependent transcription, we detected an increase in Gcn5 binding at the promoters of cdc22+ or cdc18+ in Δtor1 or Δgad8 cells under normal or replication stress conditions (Fig 5A)
PMID:35157728	FYPO:0003010	increased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC1952.05	We detected a markedly higher level of Gcn5 binding at subtelomeric genes in Δtor1 cells, compared with wild type cells (Fig 4A).
PMID:3516412	GO:0004672	protein kinase activity	(comment: CHECK activated_by(CHEBI:18420))
PMID:35171902	FYPO:0001798	decreased translation [assayed_protein] PomBase:SPCC622.16c	(comment: polysome profiling)
PMID:35171902	FYPO:0001798	decreased translation [assayed_protein] PomBase:SPCC622.16c	(comment: polysome profiling)
PMID:35171902	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC622.16c	. Interestingly, although git3Δ nmt41-epe1+ cells form heterochromatin at pericentric repeats
PMID:35171902	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] low	Consistent with the results of the genetic screen, serial dilution analyses show that git1Δ, git3Δ, git5Δ, gpa2Δ, pka1Δ, and cyr1Δ all rescue silencing defects of otr::ura4+ caused by Epe1 overexpression, as indicated by better growth on EMM medium containing 5-FOA (Fig 1D)
PMID:35171902	FYPO:0003574	normal histone H3-K14 acetylation at centromere outer repeat during vegetative growth	H3K9me2 levels at dh repeats are restored close to wild-type levels in git3Δ nmt41-epe1+ cells (Fig 1E).
PMID:35171902	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC622.16c	nterestingly, we found that Epe1 protein levels are significantly reduced in git3Δ nmt41-epe1+ and pka1Δ nmt41-epe1+ cells (Fig 2F)
PMID:35172472	FYPO:0002654	enlarged exocytic vesicles	Even without TAM treatment, the vps54 heterozygous mutant showed a high penetrance of enlarged vesicles (red arrows in Fig. 3) without any detectable change in cell shape (Fig. 3) and growth fitness (Fig. 2), compared with the SP286 control strain (comment: vw: cells are in fact quite misshapen)
PMID:35172472	FYPO:0005252	sensitive to tamoxifen [has_severity] low	Table 1. List of the 13 TAM-sensitive heterozygous strains/ Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	FYPO:0005252	sensitive to tamoxifen [has_severity] high	Table 1. List of the 13 TAM-sensitive heterozygous strains/ Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	FYPO:0005252	sensitive to tamoxifen [has_severity] high	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	FYPO:0005252	sensitive to tamoxifen [has_severity] high	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	FYPO:0005252	sensitive to tamoxifen [has_severity] medium	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	FYPO:0005252	sensitive to tamoxifen [has_severity] high	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	FYPO:0005252	sensitive to tamoxifen [has_severity] high	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	FYPO:0005252	sensitive to tamoxifen [has_severity] medium	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	FYPO:0005252	sensitive to tamoxifen [has_severity] medium	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	FYPO:0005252	sensitive to tamoxifen [has_severity] high	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	FYPO:0005252	sensitive to tamoxifen [has_severity] low	Table 1. List of the 13 TAM-sensitive heterozygous strains/Fig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	FYPO:0005252	sensitive to tamoxifen [has_severity] low	Table 1. List of the 13 TAM-sensitive heterozygous strainsFig. 2. Confirmation of the tamoxifen (TAM)-sensitive candidate strains by spotting assays
PMID:35172472	FYPO:0002655	enlarged exocytic vesicles present in increased numbers [has_severity] high	When treated with TAM, the vps54 heterozygous mutants showed more enlarged vesicles (yellow arrows in Fig. 3) ....., compared with the SP286 control.
PMID:35194019	FYPO:0001357	normal vegetative cell population growth	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0002061	inviable vegetative cell population	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0002061	inviable vegetative cell population	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0001357	normal vegetative cell population growth	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0001357	normal vegetative cell population growth	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0001357	normal vegetative cell population growth	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0001357	normal vegetative cell population growth	(Fig. S10) (comment: tetrad analysis)
PMID:35194019	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Figure 5C) (comment: forward strand RT-qPCR (dh repeat))
PMID:35194019	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Figure 5C) (comment: forward strand RT-qPCR (dh repeat))
PMID:35194019	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Figure 5C) (comment: forward strand RT-qPCR (dh repeat))
PMID:35194019	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Figure 5C) (comment: forward strand RT-qPCR (dh repeat))
PMID:35194019	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Figure 5C) (comment: forward strand RT-qPCR (dh repeat))
PMID:35194019	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Figure 5C) (comment: forward strand RT-qPCR (dh repeat))
PMID:35194019	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 13	(Figure 5D)
PMID:35194019	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 5	(Figure 5D)
PMID:35194019	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(comment: CHECK TBZ 15ug/ml)
PMID:35194019	FYPO:0000964	normal growth on thiabendazole	(comment: CHECK TBZ 15ug/ml)
PMID:35194019	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(comment: CHECK TBZ 15ug/ml)
PMID:35194019	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(comment: CHECK TBZ 15ug/ml)
PMID:35194019	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(comment: CHECK TBZ 15ug/ml)
PMID:35277511	FYPO:0002060	viable vegetative cell population	(comment: CONDITION growth >48 hrs, growth to exponential phase)
PMID:35277511	FYPO:0002239	shortened telomeres during vegetative growth	(comment: telomere southern (experiment))
PMID:35277511	FYPO:0002239	shortened telomeres during vegetative growth	(comment: telomere southern (experiment))
PMID:35286199	FYPO:0001357	normal vegetative cell population growth	(Fig. 1)
PMID:35286199	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1)
PMID:35286199	FYPO:0001357	normal vegetative cell population growth	(Fig. 1)
PMID:35286199	FYPO:0001357	normal vegetative cell population growth	(Fig. 1)
PMID:35286199	FYPO:0002058	viable cell population	(Fig. 1)
PMID:35286199	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1)
PMID:35286199	FYPO:0002060	viable vegetative cell population	(Fig. 1)
PMID:35286199	FYPO:0002058	viable cell population	(Fig. 1)
PMID:35286199	FYPO:0002061	inviable vegetative cell population	(Fig. 1)
PMID:35286199	FYPO:0002058	viable cell population	(Fig. 1)
PMID:35286199	FYPO:0002058	viable cell population	(Fig. 1)
PMID:35286199	FYPO:0002058	viable cell population	(Fig. 1)
PMID:35286199	FYPO:0002058	viable cell population	(Fig. 1)
PMID:35286199	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1)
PMID:35286199	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1)
PMID:35286199	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1)
PMID:35286199	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 1)
PMID:35286199	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1)
PMID:35286199	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1)
PMID:35286199	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1)
PMID:35286199	FYPO:0000276	monopolar mitotic spindle	(Fig. 2)
PMID:35286199	FYPO:0002822	decreased protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC428.20c	(Fig. 2)
PMID:35286199	FYPO:0000276	monopolar mitotic spindle [has_penetrance] 30	(Fig. 3)
PMID:35286199	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPCC4B3.15	(Fig. 4)
PMID:35286199	FYPO:0000339	mislocalized septum during vegetative growth	(Fig. 4)
PMID:35286199	FYPO:0002561	abolished protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPCC4B3.15	(Fig. 4)
PMID:35286199	FYPO:0002822	decreased protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC21.06c	(Fig. 4)
PMID:35286199	FYPO:0000069	resistance to thiabendazole	(Fig. 4)
PMID:35286199	FYPO:0003227	interphase microtubules present during mitosis	(Fig. 4)
PMID:35286199	FYPO:0000276	monopolar mitotic spindle [has_penetrance] 1	(Fig. 5)
PMID:35286199	FYPO:0000276	monopolar mitotic spindle [has_penetrance] 29	(Fig. 5)
PMID:35293864	FYPO:0007976	increased duration of interpolar microtubule growth events during anaphase B [has_severity] low	(Fig. 2) Figure supplement 1 klp5Δklp6Δ cells exhibited slightly longer microtubule growth events
PMID:35293864	FYPO:0007971	increased rate of interpolar microtubule polymerization during mitotic anaphase B [has_severity] low	(Fig. 2) Figure supplement 2E
PMID:35293864	FYPO:0007972	decreased rate of interpolar microtubule polymerization during mitotic anaphase B [has_severity] low	(Fig. 2) Figure supplement 2F
PMID:35293864	FYPO:0007974	increased rate of interpolar microtubule polymerization inside the mitotic nuclear membrane bridge	(Fig. 4) Figure supplement 2 We found that in both les1Δ and nem1Δ cells microtubule growth speed inside the nuclear bridge was faster than in wild-type cells
PMID:35293864	FYPO:0007974	increased rate of interpolar microtubule polymerization inside the mitotic nuclear membrane bridge	(Fig. 4) Figure supplement 2 We found that in both les1Δ and nem1Δ cells microtubule growth speed inside the nuclear bridge was faster than in wild-type cells
PMID:35293864	FYPO:0007971	increased rate of interpolar microtubule polymerization during mitotic anaphase B [has_severity] low	(Fig. 5 supp 3E)
PMID:35293864	FYPO:0007975	abnormal distribution of interpolar microtubule rescue during anaphase B [has_penetrance] complete [has_severity] high	(Fig. 5E) Ase1 is required for normal rescue distribution
PMID:35293864	FYPO:0007974	increased rate of interpolar microtubule polymerization inside the mitotic nuclear membrane bridge	(Fig. 5F, G) The decrease in growth speed associated with internalisation of microtubules in the nuclear membrane bridge is reduced upon Ase1 deletion
PMID:35293864	FYPO:0007971	increased rate of interpolar microtubule polymerization during mitotic anaphase B	(Fig. 5F,G) The decrease in growth speed associated with internalisation of microtubules in the nuclear membrane bridge is reduced upon Ase1 deletion
PMID:35293864	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_severity] low	(comment: Note: not sure about the term name and the child.) Fig. 3 supp 1A, C
PMID:35293864	FYPO:0007972	decreased rate of interpolar microtubule polymerization during mitotic anaphase B	mal3Δ cells exhibited lower microtubule growth speed throughout anaphase B (Fig. 2G)
PMID:35300005	FYPO:0001029	resistance to canavanine	(comment: CONDITION 100 ug/ml canavanine)
PMID:35314193	FYPO:0004303	abolished phosphatase activity [assayed_enzyme] PomBase:SPCC1393.13	(Figure 10)
PMID:35314193	FYPO:0004303	abolished phosphatase activity [assayed_enzyme] PomBase:SPAC806.04c	(Figure 10)
PMID:35314193	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 12)
PMID:35314193	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 12)
PMID:35314193	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 12)
PMID:35314193	FYPO:0002085	normal vegetative cell growth	(Figure 12)
PMID:35314193	FYPO:0002085	normal vegetative cell growth	(Figure 12)
PMID:35314193	FYPO:0004303	abolished phosphatase activity [assayed_enzyme] PomBase:SPAC806.04c	(Figure 8)
PMID:35314193	FYPO:0004303	abolished phosphatase activity [assayed_enzyme] PomBase:SPAC806.04c	(Figure 8)
PMID:35314193	FYPO:0004303	abolished phosphatase activity [assayed_enzyme] PomBase:SPAC806.04c	(Figure 8)
PMID:35314193	FYPO:0004303	abolished phosphatase activity [assayed_enzyme] PomBase:SPAC806.04c	(Figure 8)
PMID:35314193	FYPO:0004303	abolished phosphatase activity [assayed_enzyme] PomBase:SPAC806.04c	(Figure 8)
PMID:35314193	FYPO:0004303	abolished phosphatase activity [assayed_enzyme] PomBase:SPCC1393.13	(Figures 1 and 3)
PMID:35314193	FYPO:0004303	abolished phosphatase activity [assayed_enzyme] PomBase:SPCC1393.13	(Figures 1 and 3)
PMID:35314193	GO:0016791	phosphatase activity	(comment: Cobalt/nickel-dependent inorganic pyrophosphatase activity) Figure 1
PMID:35314193	GO:0004427	inorganic diphosphate phosphatase activity [part_of] intracellular phosphate ion homeostasis	(comment: Cobalt/nickel-dependent inorganic pyrophosphatase activity) Figure 3
PMID:35314193	GO:0004427	inorganic diphosphate phosphatase activity [part_of] intracellular phosphate ion homeostasis	(comment: Cobalt/nickel-dependent inorganic pyrophosphatase activity) Figure 4
PMID:35314193	GO:0016791	phosphatase activity	(comment: Cobalt/nickel-dependent inorganic pyrophosphatase activity) Figure 4
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC5E4.04 [has_severity] high	(Figure 1B, 2D, 5B, 6C, 7B, 7C)
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC14C8.01c [has_severity] high	(Figure 1B, 5B)
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC582.03 [has_severity] medium	(Figure 1B, 5B)
PMID:35320724	FYPO:0001489	inviable vegetative cell	(Figure 2A) even if securin levels were elevated to only about eight times the wild-type level (Kamenz et al., 2015) (Figure 2A
PMID:35320724	FYPO:0001491	viable vegetative cell	(Figure 2C)
PMID:35320724	FYPO:0001489	inviable vegetative cell	(Figure 2C)
PMID:35320724	FYPO:0001491	viable vegetative cell	(Figure 2C)
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC14C8.01c [has_severity] high	(Figure 3, S1)
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC5E4.04 [has_severity] high	(Figure 3, S1)
PMID:35320724	FYPO:0005410	normal protein degradation during mitosis [assayed_protein] PomBase:SPBC14C8.01c	(Figure 3a) However, the cellular degradation kinetics of securin-GFP were indistinguishable in cdc48+ and cdc48-353 mutant cells after normalizing for the reduced level (Figure 3A), suggesting that securin degradation was unaffected in the cdc48-353 mutant.
PMID:35320724	FYPO:0005410	normal protein degradation during mitosis [assayed_protein] PomBase:SPBC582.03	(Figure 3a) Similar results were obtained for Cdc13-GFP (Figure S1). Hence securin and Cdc13 are still efficiently targeted for proteasomal degradation in the cdc48-353 mutant.
PMID:35320724	FYPO:0002061	inviable vegetative cell population	(Figure 4)
PMID:35320724	FYPO:0003165	cut with abnormal chromosome segregation [has_severity] high	(Figure 4)
PMID:35320724	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC5E4.04	(Figure 4)
PMID:35320724	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC14C8.01c	(Figure 4)
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [has_severity] low [assayed_protein] PomBase:SPCC5E4.04	(Figure 4)
PMID:35320724	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:35320724	FYPO:0003165	cut with abnormal chromosome segregation [has_severity] low	(Figure 4)
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC14C8.01c [has_severity] medium	(Figure 4)
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC5E4.04 [has_severity] high	(Figure 4)
PMID:35320724	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:35320724	FYPO:0001234	slow vegetative cell population growth	(Figure 4)
PMID:35320724	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [has_severity] low [assayed_protein] PomBase:SPBC14C8.01c	(Figure 5)
PMID:35320724	FYPO:0001327	increased protein level during vegetative growth [has_severity] low [assayed_protein] PomBase:SPBC14C8.01c	(Figure 5)
PMID:35320724	FYPO:0002060	viable vegetative cell population	(Figure 5)
PMID:35320724	FYPO:0002061	inviable vegetative cell population	(Figure 5)
PMID:35320724	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC5E4.04	(Figure 5)
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC5E4.04 [has_severity] low	(Figure 5)
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC5E4.04 [has_severity] high	(Figure 6)
PMID:35320724	FYPO:0001489	inviable vegetative cell	(Figure 6)
PMID:35320724	FYPO:0002060	viable vegetative cell population	(Figure 6)
PMID:35320724	FYPO:0001489	inviable vegetative cell	(Figure 6)
PMID:35320724	FYPO:0002060	viable vegetative cell population	(Figure 6)
PMID:35320724	FYPO:0002061	inviable vegetative cell population	(Figure 6)
PMID:35320724	FYPO:0002060	viable vegetative cell population	(Figure 6)
PMID:35320724	FYPO:0002060	viable vegetative cell population	(Figure 6)
PMID:35320724	FYPO:0002061	inviable vegetative cell population	(Figure 6)
PMID:35320724	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPCC5E4.04 [has_severity] high	(Figure 7)
PMID:35320724	FYPO:0000835	decreased protein level [has_severity] high [assayed_protein] PomBase:SPBC14C8.01c	(Figure 7)
PMID:35320724	FYPO:0003165	cut with abnormal chromosome segregation [has_severity] medium	(Figure 7)
PMID:35320724	FYPO:0003165	cut with abnormal chromosome segregation [has_severity] medium	(Figure 7)
PMID:35320724	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPCC5E4.04 [has_severity] high	(Figure 7)
PMID:35320724	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPCC5E4.04 [has_severity] high	(Figure 7)
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC582.03 [has_severity] medium	(Figure S1)
PMID:35320724	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPCC5E4.04	(Figure S4)
PMID:35320724	FYPO:0001327	increased protein level during vegetative growth [has_severity] low [assayed_protein] PomBase:SPCC5E4.04	(Figure S5)
PMID:35320724	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC5E4.04 [has_severity] medium	(Figure S5)
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC5E4.04 [has_severity] high	(Figure S6B)
PMID:35320724	FYPO:0002061	inviable vegetative cell population	(Figure S6D)
PMID:35320724	FYPO:0004395	short bipolar mitotic spindle during metaphase [has_severity] medium	(Figure S6G)
PMID:35320724	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC5E4.04 [has_severity] high	(Figure S7)
PMID:35320724	FYPO:0004705	delayed onset of mitotic sister chromatid separation	Consistent with the low levels of separase, we found that sister chromatid separation was delayed in cdc48- 353 mutant cells relative to the decline in CDK1 activity at mitotic exit (Figure 1C).
PMID:35325114	FYPO:0007990	growth auxotrophic for isoleucine	(comment: CHECK TERM REQUESTED growth auxotrophic for isoleucine)
PMID:35325114	FYPO:0007991	growth auxotrophic for valine	(comment: CHECK TERM REQUESTED growth auxotrophic for valine)
PMID:35333350	FYPO:0007942	increased length of chromatin loops during meiotic prophase I	(Figure 4c,e) Fluorescence images of Rec8- GFP showed that axial structures in meiotic chromosomes were more prominent in wpl1Δ than in the wild-type
PMID:35333350	FYPO:0003613	normal meiotic sister chromatid cohesion during meiotic prophase I	(Figure 5C) The rec8-F204S mutant maintained sister chromatid cohesion as assessed at the cut3 gene locus
PMID:35333350	FYPO:0002890	abnormal horsetail nucleus morphology	(Figure 5D, Supplemental Movies 1, and 3) In the rec8-F204S mutant, only the leading edge of the nucleus followed the horsetail movement, while the bulk of chromosomes were left behind, similar to rec8Δ
PMID:35333350	FYPO:0007945	abnormal homologous chromosome pairing at cis-acting homologous chromosome pairing region during meiotic prophase I	(Figure 6B). The alignment index of chromosome 1 at meiotic prophase (2.5 h) decreased in rec8-F204S (1.6) compared with the wild-type (rec8-wt, 2.6)
PMID:35333350	FYPO:0003179	decreased intragenic meiotic recombination	(Figure 7)
PMID:35333350	FYPO:0002485	decreased intergenic meiotic recombination	(Figure 7) rec8-F204S mutant is defective in LinE formation and recombination
PMID:35333350	FYPO:0000900	abnormal linear element assembly	(Figure 7) rec8-F204S mutant is defective in LinE formation and recombination (Rec10-mCherry forms aberrant dotty or filamentous aggregates within the nucleus, similar to rec8∆.)
PMID:35333350	FYPO:0007945	abnormal homologous chromosome pairing at cis-acting homologous chromosome pairing region during meiotic prophase I	(Figure S4B)
PMID:35333350	FYPO:0001357	normal vegetative cell population growth	(Figure S5B)
PMID:35333350	FYPO:0001357	normal vegetative cell population growth	(Figure S5B)
PMID:35333350	FYPO:0007939	normal chromatin loop formation during meiotic prophase I	(Figures 2A and B) Hi-C analysis for rec10Δ and rec12Δ cells showed X-shaped contacts similar to wild-type cells AND (Figure 3A).... punctate Hi-C interactions observed in the wild-type were mostly lost in rec8Δ
PMID:35333350	FYPO:0007939	normal chromatin loop formation during meiotic prophase I	(Figures 2A and B) Hi-C analysis for rec10Δ and rec12Δ cells showed X-shaped contacts similar to wild-type cells AND (Figure 3A).... punctate Hi-C interactions observed in the wild-type were mostly lost in rec8Δ
PMID:35333350	FYPO:0003054	decreased homologous chromosome pairing at cis-acting homologous chromosome pairing region	(comment: CHECK during horsetail/ prophase)
PMID:35333350	FYPO:0007944	abnormal chromatin loop formation during meiotic prophase I	(comment: DECREASED NUMBER) (Figure 6 and Figure 5e, S6BC) defective loop formation also supported by increased distance between the telomere-ade8 distance was longer in the rec8-F204S mutant than in the wild-type, suggesting that the chromatin of the rec8-F204S mutant was flexible and was abnormally stretched by the traction of the horsetail movement
PMID:35333350	FYPO:0000197	abnormal horsetail movement	Supplementary Figure S4B) wpl1Δ rarely showed torsional turning (Supplementary Figure S4C, Supplemental Movies 1, and 2) during horsetail movements that is important for the alignment of homologs
PMID:35333350	GO:0140588	chromatin looping [happens_during] meiotic prophase I	These results sugest that in the rec8-F204S mutant, as in rec8Δ, the Rec8- dependent meiosis-specific short chromatin loop structures are lost, resulting in a concomitant loss of the structural property of the chromosome required for proper alignment.
PMID:35333350	GO:0007129	homologous chromosome pairing at meiosis	These results suggest that Wpl1 plays a role in alignment of homologs through Rec8-dependent formation of axis-loop chromatin structure.
PMID:35333350	GO:0007129	homologous chromosome pairing at meiosis	These results suggest that Wpl1 plays a role in alignment of homologs through Rec8-dependent formation of axis-loop chromatin structure.
PMID:35333350	FYPO:0002092	abnormal meiotic sister chromatid cohesion	rec8-S552P and rec8Δ, which showed the cohesion defect, were used as a control strain (see Supplementary Figure S5C, S5D, and S5E for details of the rec8-S552P mutant)
PMID:35354597	FYPO:0003750	normal nuclear pore density	(Fig. 2B)
PMID:35354597	FYPO:0003750	normal nuclear pore density	(Fig. 2B)
PMID:35354597	FYPO:0003750	normal nuclear pore density	(Fig. 2C)
PMID:35354597	FYPO:0003750	normal nuclear pore density	(Fig. 2C)
PMID:35354597	FYPO:0003750	normal nuclear pore density	(Fig. 2C)
PMID:35354597	FYPO:0003750	normal nuclear pore density	(Fig. 2D)
PMID:35354597	FYPO:0003750	normal nuclear pore density	(Fig. 2D)
PMID:35354597	FYPO:0008171	increased nuclear pore complex clustering [has_penetrance] medium	(Fig. 3A, B and C)
PMID:35354597	FYPO:0008171	increased nuclear pore complex clustering	(Fig. 3D)
PMID:35354597	FYPO:0007547	abnormal nuclear pore localization to mitotic nuclear bridge midzone membrane [has_severity] high	(Fig. 3E)
PMID:35354597	GO:0044732	mitotic spindle pole body	(Fig. 6A)
PMID:35354597	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC26A3.15c	(Fig. 6B)
PMID:35354597	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC26A3.15c	(Fig. 6B)
PMID:35354597	FYPO:0002969	increased protein localization to mitotic spindle pole body [has_severity] medium [assayed_protein] PomBase:SPAC26A3.15c	(Fig. 6B)
PMID:35354597	FYPO:0002969	increased protein localization to mitotic spindle pole body [has_severity] medium [assayed_protein] PomBase:SPAC26A3.15c	(Fig. 6D)
PMID:35354597	FYPO:0002969	increased protein localization to mitotic spindle pole body [has_severity] medium [assayed_protein] PomBase:SPAC26A3.15c	(Fig. 6D)
PMID:35354597	FYPO:0002969	increased protein localization to mitotic spindle pole body [has_severity] medium [assayed_protein] PomBase:SPAC26A3.15c	(Fig. 6D)
PMID:35354597	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC26A3.15c	(Fig. 6D)
PMID:35354597	FYPO:0002969	increased protein localization to mitotic spindle pole body [has_severity] high [assayed_protein] PomBase:SPAC26A3.15c	(Fig. 6E)
PMID:35354597	FYPO:0008171	increased nuclear pore complex clustering [has_severity] high	NPC clusters in nup132Δ nuclei coalesced into larger clusters that preferentially localized to the SPBs in mitosis. Fig. 3F
PMID:35416247	PomGeneEx:0000011	RNA level increased [in_presence_of] tschimganine	(comment: CHECK in presence of tschimganine)
PMID:35416247	PomGeneEx:0000011	RNA level increased [in_presence_of] tschimganine	(comment: CHECK in presence of tschimganine)
PMID:35416247	PomGeneEx:0000012	RNA level decreased [in_presence_of] tschimganine	(comment: CHECK in presence of tschimganine)
PMID:35416247	PomGeneEx:0000012	RNA level decreased [in_presence_of] tschimganine	(comment: CHECK in presence of tschimganine)
PMID:35416247	PomGeneEx:0000012	RNA level decreased [in_presence_of] tschimganine	(comment: CHECK in presence of tschimganine)
PMID:35416247	PomGeneEx:0000012	RNA level decreased [in_presence_of] tschimganine	(comment: CHECK in presence of tschimganine)
PMID:35416247	PomGeneEx:0000011	RNA level increased [in_presence_of] tschimganine	(comment: CHECK in presence of tschimganine)
PMID:35416247	PomGeneEx:0000011	RNA level increased [in_presence_of] tschimganine	(comment: CHECK in presence of tschimganine)
PMID:35512546	GO:0008266	poly(U) RNA binding	(comment: At RRM3 motif)
PMID:35536002	FYPO:0004300	normal ATPase activity [assayed_enzyme] PomBase:SPCC1672.06c	(Fig. 1)
PMID:35536002	FYPO:0003674	abolished ATPase activity [assayed_enzyme] PomBase:SPCC1672.06c	(Fig. 1)
PMID:35536002	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBP4G3.02 [has_severity] medium	(Fig. 12)
PMID:35536002	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBP4G3.02 [has_severity] high	(Fig. 12)
PMID:35536002	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBP4G3.02 [has_severity] high	(Fig. 12)
PMID:35536002	FYPO:0008013	normal inositol hexakisphosphate kinase activity [assayed_enzyme] PomBase:SPCC1672.06c	(Fig. 12) (Note how the levels are the same as when the pyrophosphatase is inactivated in the full-length protein)
PMID:35536002	FYPO:0006892	abolished inositol hexakisphosphate kinase activity [assayed_enzyme] PomBase:SPCC1672.06c	(Fig. 7)
PMID:35536002	FYPO:0006892	abolished inositol hexakisphosphate kinase activity [assayed_enzyme] PomBase:SPCC1672.06c	(Fig. 7)
PMID:35536002	FYPO:0006892	abolished inositol hexakisphosphate kinase activity [assayed_enzyme] PomBase:SPCC1672.06c	(Fig. 7)
PMID:35536002	FYPO:0006893	decreased inositol hexakisphosphate kinase activity [assayed_enzyme] PomBase:SPCC1672.06c [has_severity] medium	(Fig. 7)
PMID:35536002	FYPO:0006892	abolished inositol hexakisphosphate kinase activity [assayed_enzyme] PomBase:SPCC1672.06c	(Fig. 7)
PMID:35536002	FYPO:0006893	decreased inositol hexakisphosphate kinase activity [assayed_enzyme] PomBase:SPCC1672.06c [has_severity] medium	(Fig. 7)
PMID:35536002	FYPO:0008013	normal inositol hexakisphosphate kinase activity [assayed_enzyme] PomBase:SPCC1672.06c	(Fig. 7)
PMID:35536002	FYPO:0006893	decreased inositol hexakisphosphate kinase activity [assayed_enzyme] PomBase:SPCC1672.06c [has_severity] medium	(Fig. 7)
PMID:35536002	FYPO:0006892	abolished inositol hexakisphosphate kinase activity [assayed_enzyme] PomBase:SPCC1672.06c	(Fig. 7)
PMID:35536002	FYPO:0006893	decreased inositol hexakisphosphate kinase activity [assayed_enzyme] PomBase:SPCC1672.06c [has_severity] high	(Fig. 7)
PMID:35536002	FYPO:0006893	decreased inositol hexakisphosphate kinase activity [assayed_enzyme] PomBase:SPCC1672.06c [has_severity] high	(Fig. 7)
PMID:35536002	FYPO:0008013	normal inositol hexakisphosphate kinase activity [assayed_enzyme] PomBase:SPCC1672.06c	(Fig. 7)
PMID:35536002	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBP4G3.02 [has_severity] low	(Fig. 8)
PMID:35536002	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBP4G3.02 [has_severity] medium	(Fig. 8)
PMID:35536002	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBP4G3.02 [has_severity] low	(Fig. 8)
PMID:35536002	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBP4G3.02 [has_severity] low	(Fig. 8)
PMID:35536002	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBP4G3.02	(Fig. 8) and text
PMID:35536002	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBP4G3.02 [has_severity] high	(Fig. 8, 12)
PMID:35609605	FYPO:0006186	increased rate of actomyosin contractile ring assembly [has_severity] low	(Fig. S3C bottom panel) (comment: COMPACTION I asked is this the correct genotype? Dan answered: Our quantification in FigS3C bottom panel shows that ring compaction is slightly faster in scs2Δscs22Δmyo2-E1 than wt at 24 degree, although such a difference is not significant quantitatively. Qualitatively, compaction -in terms of mobility of individual nodes was indeed faster. So, I felt reluctant to use either “normal” or “abnormal” to describe that.)
PMID:35609605	FYPO:0000161	abnormal actomyosin contractile ring assembly [has_penetrance] 80 [has_severity] high	(Figure 3) (comment: COMPACTION)
PMID:35609605	FYPO:0003210	mislocalized, misoriented septum [has_penetrance] >60	(Figure 4D)
PMID:35609605	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] >80	(Figure 4D)
PMID:35609605	FYPO:0001009	abolished actomyosin contractile ring assembly	"(Figures 3A, 3B, and S3A)(comment: no rescue dan says ""FigS3A (bottom panel) shows that ring compaction completely failed in scs2Δscs22Δmyo2-E1(aaG345R) at 36 degree. In fact, we did not directly show that these cells failed ring contraction similarly as myo2-E1(aaG345R) at high temperature (which is well known) in the paper, as we mainly focused on ring compaction process. But we have implied that in the context."""
PMID:35609605	FYPO:0000161	abnormal actomyosin contractile ring assembly [has_penetrance] 40 [has_severity] medium	(comment: COMPACTION )Figures 3A, 3B, and S3A (inhibiting exocytosis rescues defect of compaction)
PMID:35609605	FYPO:0000161	abnormal actomyosin contractile ring assembly [has_penetrance] 35	(comment: COMPACTION) Figures 3A, 3B, and S3A
PMID:35609605	FYPO:0003339	decreased rate of actomyosin contractile ring assembly [has_severity] low [has_penetrance] 80	Incomplete ring compaction was still observed in myo2- E1pil1D, although such fraction was reduced as compared with myo2-E1 (Figure 3B) (comment: I don't see the images - this is from the bar chart))
PMID:35609605	FYPO:0003339	decreased rate of actomyosin contractile ring assembly [has_severity] low [has_penetrance] 80	Incomplete ring compaction was still observed in myo2- E1pil1D, although such fraction was reduced as compared with myo2-E1 (Figure 3B) (comment: I don't see the images - this is from the bar chart))
PMID:35609605	FYPO:0003339	decreased rate of actomyosin contractile ring assembly	and is already defective in actomyosin  17 compaction at the permissive temperature of 24 C (Figure S1C, video S2) and (Figures 3A, 3B, and S3A))
PMID:35622906	FYPO:0001874	abnormal asymmetric protein localization, with protein localized to both mitotic spindle pole bodies [assayed_protein] PomBase:SPBC365.15	(comment: CHECK OLD SPB)
PMID:35639710	FYPO:0001029	resistance to canavanine [has_severity] medium	(Fig. 1)
PMID:35639710	FYPO:0001029	resistance to canavanine [has_severity] medium	(Fig. 1)
PMID:35639710	FYPO:0001029	resistance to canavanine [has_severity] high	(Figure 1)
PMID:35639710	FYPO:0001545	normal growth on L-canavanine	(Figure 1) (comment: same as WT)
PMID:35639710	FYPO:0000099	sensitive to canavanine [has_severity] high	(Figure 2A)
PMID:35639710	FYPO:0001029	resistance to canavanine [has_severity] high	(Figure 3) (comment: confirms dominance of can1-1)
PMID:35639710	FYPO:0002082	increased protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPBC18H10.20c	(comment: CHECK Increased protein ubiquitination.)
PMID:35639710	FYPO:0005226	decreased level of ubiquitinated protein in cell [assayed_protein] PomBase:SPBC18H10.20c	Second, Any1R175C does not show an increase but rather a strong decrease in its ubiquitination level.
PMID:35657410	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8D2.15	(Table 2)
PMID:35657410	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC16E9.01c	(Table 2)
PMID:35657410	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1F8.02c	(Table 2)
PMID:35657410	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1683.09c	(Table 2)
PMID:35657410	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1F8.03c	(Table 2)
PMID:35657410	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC227.13c	(Table 2)
PMID:35657410	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1F7.08	(Table 2)
PMID:35657410	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1F12.10c	(Table 2)
PMID:35657410	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC24C9.06c	(Table 2)
PMID:35657410	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1020.03	(Table 2)
PMID:35657410	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1F7.07c	(Table 2)
PMID:35657410	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC4F6.09	(Table 2)
PMID:35657410	FYPO:0008396	sensitive to ferric iron	+ Fe2(SO4)3 Deletion of ppr2 also increased the sensitivity of cells to ferrous iron (Fe2+) and ferric iron (Fe3+) (Fig. 1b).
PMID:35657410	FYPO:0008395	sensitive to ferrous iron	+ Fe2(SO4)3 Deletion of ppr2 also increased the sensitivity of cells to ferrous iron (Fe2+) and ferric iron (Fe3+) (Fig. 1b).
PMID:35657410	FYPO:0000245	loss of viability in stationary phase [has_severity] medium	As shown in Fig. 1a, Δppr2 cells progressively lost viability during growth in YES medium (Fig. 1a)
PMID:35657410	FYPO:0008395	sensitive to ferrous iron	Deletion of ppr2 also increased the sensitivity of cells to ferrous iron (Fe2+) and ferric iron (Fe3+) (Fig. 1b).
PMID:35657410	FYPO:0001934	abolished cell population growth on glycerol carbon source	However, DFO could not enables growth of Δppr2 cells on glycerol medium, which requires mitochondrial respiration, suggesting that DFO could not rescue of the respiratory growth defect of Δppr2 cells (Fig. 1d)
PMID:35657410	FYPO:0001934	abolished cell population growth on glycerol carbon source	However, DFO could not enables growth of Δppr2 cells on glycerol medium, which requires mitochondrial respiration, suggesting that DFO could not rescue of the respiratory growth defect of Δppr2 cells (Fig. 1d)
PMID:35657410	FYPO:0001934	abolished cell population growth on glycerol carbon source	However, deletion of frp1 could not rescue respiratory growth defect in Δppr2 cells as Δppr2Δfrp1 could not grow on glycerol medium (Fig. 4b).
PMID:35657410	FYPO:0008397	increased lipid peroxidation	Increased lipid peroxidation was detected in Δppr2 cells
PMID:35657410	FYPO:0008399	increased lipid peroxidation during stationary phase	Increased lipid peroxidation was detected in Δppr2 cells
PMID:35657410	FYPO:0001310	normal viability in stationary phase	We found that DFO significantly increases the viability of Δppr2 cells (Fig. 1c). (normal compared to WT)
PMID:35658118	FYPO:0001357	normal vegetative cell population growth	(Figure 1b, 3C)
PMID:35658118	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 1b, 3c)
PMID:35658118	FYPO:0003896	normal mitochondrial morphology [has_penetrance] 80	(Figure 2a, 2b)
PMID:35658118	FYPO:0003896	normal mitochondrial morphology [has_penetrance] 80	(Figure 2a, 2b)
PMID:35658118	FYPO:0007610	decreased mitochondrial volume [has_severity] medium	(Figure 2c)
PMID:35658118	FYPO:0007610	decreased mitochondrial volume [has_penetrance] high	(Figure 2c)
PMID:35658118	FYPO:0007610	decreased mitochondrial volume [has_penetrance] high	(Figure 2c)
PMID:35658118	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] medium	(comment: phenotypoe seems to be additive on glycerol) Consistently, the growth of acb1Δ and acb1Δdnm1Δ cells on nonfermentable medium plates (YE plates plus 0.1% glucose and 3% glycerol) was comparable but was slower than the growth of WT and dnm1Δ cells (Fig. 2D,F).
PMID:35658118	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] low	As shown in Fig. 1B, acb1Δ grew slightly slower on fermentable medium than acb1+ cells and much slower on nonfermentable medium.
PMID:35658118	FYPO:0007611	small fragmented mitochondria present in decreased numbers [has_penetrance] 74	By contrast, mitochondria became fragmented/aggregated (74.4%) PLUS This result indicates that mitochondrial mass/biogenesis was reduced by the absence of Acb1 or Dnm1. Note that dnm1-deletion in acb1Δ cells did not restore mitochondrial mass (Fig. 2C)
PMID:35658118	FYPO:0003807	net-like mitochondrial morphology [has_penetrance] 48	Consistent with the finding reported previously by our group [8], mitochondria formed a highly branch network (47.8%) in dnm1Δ cells (Fig. 2A,B)
PMID:35658118	FYPO:0008137	decreased size and number of lipid droplets	Intriguingly, the size of lipid droplets became larger and the number of lipid droplets became less as acb1+ and acb1Δ+acb1 cells grew older in nutrient-rich medium (Fig. 4C,D). By contrast, the size and number of lipid droplets did not change as acb1Δ cells grew older in nutrient-rich medium (Fig. 4C,D).
PMID:35658118	FYPO:0007193	small fragmented mitochondria [has_severity] high	Microscopic observation showed that mitochondria were tubular in acb1+ cells but became fragmented in acb1Δ cells (Fig. 1A).
PMID:35658118	FYPO:0001489	inviable vegetative cell [has_penetrance] 9	Therefore, increased cell death rather than abnormal cell division was the consequence of the impaired cell proliferation caused by the absence of Acb1 (Fig. 3D).
PMID:35658118	FYPO:0009007	decreased vegetative cell population viability	Therefore, increased cell death rather than abnormal cell division was the consequence of the impaired cell proliferation caused by the absence of Acb1 (Fig. 3D).
PMID:35658118	FYPO:0002009	decreased oxygen consumption during vegetative growth	Three independent experiments consistently showed that the oxygen consumption rate of acb1Δ cells was significantly decreased when the cells were cultured in nutrient-rich medium (i.e. YE) (Fig. 3B).
PMID:35658118	FYPO:0007193	small fragmented mitochondria [has_severity] medium	We noticed that mitochondrial fragmentation caused by the absence of Acb1 was more apparent when cells were cultured in nutrient-rich medium than in minimal medium.
PMID:35658118	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC12C2.08	he expression of Dnm1 was comparable in wild-type and acb1Δ cells (Fig. 2E).
PMID:35673994	FYPO:0005989	abnormal protein localization during mating	(Fig. 2A)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] 40	(Fig. 2B)
PMID:35673994	FYPO:0008002	cell lysis during mating [has_penetrance] medium	(Fig. 2B)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] 60	(Fig. 2B)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] 90	(Fig. 2B)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] 90	(Fig. 2B)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] medium	(Fig. 2C)
PMID:35673994	FYPO:0007094	increased duration of cell fusion during mating [has_severity] high	(Fig. 2D)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] low	(Fig. 2H)
PMID:35673994	FYPO:0004806	incomplete cell wall disassembly at cell fusion site [has_severity] low	(Fig. 3)
PMID:35673994	FYPO:0007683	wide actin fusion focus	(Fig. 3)
PMID:35673994	FYPO:0007094	increased duration of cell fusion during mating [has_severity] low	(Fig. 4E)
PMID:35673994	FYPO:0007095	increased protein localization to actin fusion focus [assayed_protein] PomBase:SPAC27F1.02c	(Fig. 4E)
PMID:35673994	FYPO:0007094	increased duration of cell fusion during mating [has_severity] low	(Fig. 4E)
PMID:35673994	FYPO:0007094	increased duration of cell fusion during mating [has_severity] medium	(Fig. 4E)
PMID:35673994	FYPO:0006108	abnormal actin fusion focus assembly	(Fig. 5)
PMID:35673994	FYPO:0006108	abnormal actin fusion focus assembly	(Fig. 5)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] low	(Fig. 5)
PMID:35673994	FYPO:0007095	increased protein localization to actin fusion focus [assayed_protein] PomBase:SPAC27F1.02c	(Fig. 5)
PMID:35673994	FYPO:0006108	abnormal actin fusion focus assembly [has_severity] high	(Fig. 5)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] high	(Fig. 5)
PMID:35673994	FYPO:0008002	cell lysis during mating [has_penetrance] medium	(Fig. 5)
PMID:35673994	FYPO:0006108	abnormal actin fusion focus assembly	(Fig. 5)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] medium	(Fig. 5)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] high	(Fig. 5)
PMID:35673994	FYPO:0007095	increased protein localization to actin fusion focus [assayed_protein] PomBase:SPAC27F1.02c	(Fig. 5)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] high	(Fig. 5C)
PMID:35673994	FYPO:0007096	decreased protein localization to actin fusion focus [assayed_protein] PomBase:SPAC27F1.02c	(Fig. 5F)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] medium	(Fig. 6)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] high	(Fig. 6)
PMID:35673994	FYPO:0008002	cell lysis during mating [has_penetrance] medium	(Fig. 6)
PMID:35673994	FYPO:0006108	abnormal actin fusion focus assembly	(Fig. 6)
PMID:35673994	FYPO:0006108	abnormal actin fusion focus assembly	(Fig. 6)
PMID:35673994	FYPO:0008002	cell lysis during mating [has_penetrance] medium	(Fig. 6)
PMID:35673994	FYPO:0006108	abnormal actin fusion focus assembly	(Fig. 6)
PMID:35673994	FYPO:0000413	abolished cell fusion during mating [has_penetrance] high	(comment: chimera expressed from the ura4 locus [@ura4] - kept because not assayed from fus1 locus)
PMID:35781263	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1F8.01	(comment: CHECK decreased)
PMID:35781263	FYPO:0001309	increased viability in stationary phase [has_severity] high	"The Δght5 strain is always in 27 a ""low glucose state"" even when cultured in high glucose medium, and this may be the reason why the 28 lifespan extension phenotype appears."
PMID:35820914	FYPO:0000342	decreased cellular respiration [has_severity] high	(0.08% Glu) that promote respiratory metabolism (Fig. 4A). We observed that the short-lived mutants lon1Δ and yta12Δ showed a severe growth defect in respiratory-prone media, comparable to that detected in cox6Δ lacking a subunit of the ETC complex IV
PMID:35820914	FYPO:0000342	decreased cellular respiration	(0.08% Glu) that promote respiratory metabolism (Fig. 4A). We observed that the short-lived mutants lon1Δ and yta12Δ showed a severe growth defect in respiratory-prone media, comparable to that detected in cox6Δ lacking a subunit of the ETC complex IV
PMID:35820914	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPMIT.07	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPMIT.11	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPMIT.11	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPMIT.01	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPMIT.07	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPMIT.04	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPMIT.04	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPMIT.01	(Fig. 4E) show that the levels of Cox1, Cox2, Cox3, and Atp6 proteins are similar in wild-type and the long-lived mutants mgr3Δ and yme1Δ. However, the blots demonstrate highly reduced levels of these proteins in lon1Δ and yta12Δ mutants which might explain the respi
PMID:35820914	FYPO:0003004	increased cellular reactive oxygen species level during vegetative growth	(vw: increased hydrogen peroxide formation) In contrast, the yta12Δ strain displayed enhanced levels of basal probe oxidation (OxD0 of 0.46) at the mitochondrial matrix compared to the wild-type strain (OxD0 of 0.4), indicative of higher steady-state levels of H2O2 (Additional file 5: Fig. S2). Cells lacking Lon1 displayed a slight increase in basal oxidation of MTS-Hyper7, suggesting that both short-lived mutants show enhanced production of mitochondrial ROS (Additional file 5: Fig. S2).
PMID:35820914	FYPO:0000565	increased cellular respiration	In contrast, long-lived mutants mgr3Δ and yme1Δ displayed a normal growth in low glucose conditions (Fig. 4A).
PMID:35820914	FYPO:0000565	increased cellular respiration	In contrast, long-lived mutants mgr3Δ and yme1Δ displayed a normal growth in low glucose conditions (Fig. 4A).
PMID:35820914	FYPO:0003004	increased cellular reactive oxygen species level during vegetative growth	In contrast, the yta12Δ strain displayed enhanced levels of basal probe oxidation (OxD0 of 0.46) at the mitochondrial matrix compared to the wild-type strain (OxD0 of 0.4), indicative of higher steady-state levels of H2O2 (Additional file 5: Fig. S2). Cells lacking Lon1 displayed a slight increase in basal oxidation of MTS-Hyper7, suggesting that both short-lived mutants show enhanced production of mitochondrial ROS (Additional file 5: Fig. S2).
PMID:35820914	FYPO:0003811	asymmetric mitochondrial aggregation	Interestingly, the short-lived mutant yta12Δ displayed aggregated mitochondria at the cell poles similar to msp1Δ cells, suggesting that this matrix protease may participate in the regulation of mitochondrial fusion (Fig. 5D, E).
PMID:35820914	FYPO:0003811	asymmetric mitochondrial aggregation	Interestingly, the short-lived mutant yta12Δ displayed aggregated mitochondria at the cell poles similar to msp1Δ cells, suggesting that this matrix protease may participate in the regulation of mitochondrial fusion (Fig. 5D, E).
PMID:35820914	FYPO:0000245	loss of viability in stationary phase	Lack of the mitochondrial protease Lon1 reduced longevity whereas the absence of Mgr3, adaptor protein of the protease Yme1 [13], led to increased lifespan.
PMID:35820914	FYPO:0001309	increased viability in stationary phase	Lack of the mitochondrial protease Lon1 reduced longevity whereas the absence of Mgr3, adaptor protein of the protease Yme1 [13], led to increased lifespan.
PMID:35820914	FYPO:0000245	loss of viability in stationary phase	Moreover, cells lacking the protease Yme1 displayed increased lifespan in a similar manner to mgr3Δ mutant, whereas the loss of the protease Yta12 resulted in a significant reduction of longevity (Fig. 3B).
PMID:35820914	FYPO:0001309	increased viability in stationary phase [has_severity] high	Moreover, cells lacking the protease Yme1 displayed increased lifespan in a similar manner to mgr3Δ mutant, whereas the loss of the protease Yta12 resulted in a significant reduction of longevity (Fig. 3B). This increase in the respiratory activity was more evident for yme1Δ mutant in high glucose medium (Fig. 4B, left panel).
PMID:35820914	FYPO:0000342	decreased cellular respiration	cells lacking Lon1 or Yta12 displayed decreased respiratory capacity in high and low glucose (Fig. 4B)
PMID:35820914	FYPO:0000342	decreased cellular respiration	cells lacking Lon1 or Yta12 displayed decreased respiratory capacity in high and low glucose (Fig. 4B)
PMID:35820914	FYPO:0004944	decreased mitochondrial membrane potential	we detected a significant loss of ΔΨ in yta12Δ mutant and increased ΔΨ in yme1Δ cells, both results in consonance with our previous findings (Fig. 4C, Additional file 4: Fig. S1).
PMID:35820914	FYPO:0007737	increased mitochondrial membrane potential	we detected a significant loss of ΔΨ in yta12Δ mutant and increased ΔΨ in yme1Δ cells, both results in consonance with our previous findings (Fig. 4C, Additional file 4: Fig. S1).
PMID:35820914	FYPO:0001309	increased viability in stationary phase	we have found that deletion of the fission genes dnm1 or fis1 caused a significant increase of longevity whereas the loss of the fusion GTPase Msp1 had no effect on lifespan (Fig. 5C).
PMID:35820914	FYPO:0001309	increased viability in stationary phase	we have found that deletion of the fission genes dnm1 or fis1 caused a significant increase of longevity whereas the loss of the fusion GTPase Msp1 had no effect on lifespan (Fig. 5C).
PMID:35901126	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S1)
PMID:35901126	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S1)
PMID:35901126	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	As anticipated, the resulting trm6Δ imt06Δ strain grew very poorly at 30 ̊C, and was temperature sensitive at higher temperatures, not growing at all at 37 ̊C
PMID:35901126	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	As anticipated, the resulting trm6Δ imt06Δ strain grew very poorly at 30 ̊C, and was temperature sensitive at higher temperatures, not growing at all at 37 ̊C
PMID:35901126	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	As anticipated, the resulting trm6Δ imt06Δ strain grew very poorly at 30 ̊C, and was temperature sensitive at higher temperatures, not growing at all at 37 ̊C, These results show a prominent synthetic growth defect in the S. pombe trm6Δ imt06Δ strain, due only to reduced levels of tRNAiMet(CAU).
PMID:35901126	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	As anticipated, the resulting trm6Δ imt06Δ strain grew very poorly at 30 ̊C, and was temperature sensitive at higher temperatures, not growing at all at 37 ̊C, These results show a prominent synthetic growth defect in the S. pombe trm6Δ imt06Δ strain, due only to reduced levels of tRNAiMet(CAU).
PMID:35901126	FYPO:0001772	decreased tRNA methyltransferase activity [has_severity] high [assayed_enzyme] tRNA (m1A) methyltransferase complex [assayed_substrate] PomBase:SPBTRNAMET.06	Examination by HPLC of the nucleoside composition of purified tRNATyr(GUA) from trm6Δ and trm61Δ mutants revealed that m1A levels were less than 0.03 moles/mole, compared to 0.60 moles/mole in WT cells, whereas levels of C, m5C, and m7G were very similar in the tRNATyr(GUA) from both mutant and WT cells (Fig 1B and 1C)
PMID:35901126	FYPO:0001772	decreased tRNA methyltransferase activity [has_severity] high [assayed_enzyme] tRNA (m1A) methyltransferase complex [assayed_substrate] PomBase:SPBTRNAMET.06	Examination by HPLC of the nucleoside composition of purified tRNATyr(GUA) from trm6Δ and trm61Δ mutants revealed that m1A levels were less than 0.03 moles/mole, compared to 0.60 moles/mole in WT cells, whereas levels of C, m5C, and m7G were very similar in the tRNATyr(GUA) from both mutant and WT cells (Fig 1B and 1C)
PMID:35901126	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	Growth analysis on plates showed that the trm6Δ dhp1-5 and trm6Δ dhp1-6 mutants were nearly as healthy at high temperatures as the WT strain on both YES and EMMC-his media, whereas the trm6Δ tol1-1 mutant was slightly less healthy at higher temperatures (Fig 3A).
PMID:35901126	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	Growth analysis on plates showed that the trm6Δ dhp1-5 and trm6Δ dhp1-6 mutants were nearly as healthy at high temperatures as the WT strain on both YES and EMMC-his media, whereas the trm6Δ tol1-1 mutant was slightly less healthy at higher temperatures (Fig 3A).
PMID:35901126	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	Growth analysis on plates showed that the trm6Δ dhp1-5 and trm6Δ dhp1-6 mutants were nearly as healthy at high temperatures as the WT strain on both YES and EMMC-his media, whereas the trm6Δ tol1-1 mutant was slightly less healthy at higher temperatures (Fig 3A).
PMID:35901126	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	Growth analysis on plates showed that the trm6Δ dhp1-5 and trm6Δ dhp1-6 mutants were nearly as healthy at high temperatures as the WT strain on both YES and EMMC-his media, whereas the trm6Δ tol1-1 mutant was slightly less healthy at higher temperatures (Fig 3A).
PMID:35901126	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_transcript] PomBase:SPBTRNAMET.06 [has_severity] low	Northern analysis of tRNA from strains grown at 30 ̊C and after temperature shift to 38.5 ̊C showed that the dhp1 and tol1 suppressors substantially restored tRNAiMet(CAU) levels at both high and low temperatures, without affecting any of a number of other tRNAs (Fig 3B and 3C).
PMID:35901126	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_transcript] PomBase:SPBTRNAMET.06 [has_severity] low	Northern analysis of tRNA from strains grown at 30 ̊C and after temperature shift to 38.5 ̊C showed that the dhp1 and tol1 suppressors substantially restored tRNAiMet(CAU) levels at both high and low temperatures, without affecting any of a number of other tRNAs (Fig 3B and 3C).
PMID:35901126	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_transcript] PomBase:SPBTRNAMET.06 [has_severity] low	Northern analysis of tRNA from strains grown at 30 ̊C and after temperature shift to 38.5 ̊C showed that the dhp1 and tol1 suppressors substantially restored tRNAiMet(CAU) levels at both high and low temperatures, without affecting any of a number of other tRNAs (Fig 3B and 3C).
PMID:35901126	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_transcript] PomBase:SPBTRNAMET.06 [has_severity] low	Northern analysis of tRNA from strains grown at 30 ̊C and after temperature shift to 38.5 ̊C showed that the dhp1 and tol1 suppressors substantially restored tRNAiMet(CAU) levels at both high and low temperatures, without affecting any of a number of other tRNAs (Fig 3B and 3C).
PMID:35901126	FYPO:0001773	abolished tRNA methyltransferase activity [assayed_substrate] PomBase:SPBTRNAMET.06 [assayed_enzyme] tRNA (m1A) methyltransferase complex	Similarly, poison primer extension showed that tRNAiMet(CAU) was nearly completely modified with m1A58 in WT cells (97%), but not visibly modified in trm6Δ and trm61Δ mutants (although quantification with the high background gave 2.0% for trm6Δ and 2.8% in trm61Δ).
PMID:35901126	FYPO:0001772	decreased tRNA methyltransferase activity [assayed_substrate] PomBase:SPBTRNAMET.06 [assayed_enzyme] tRNA (m1A) methyltransferase complex	Similarly, poison primer extension showed that tRNAiMet(CAU) was nearly completely modified with m1A58 in WT cells (97%), but not visibly modified in trm6Δ and trm61Δ mutants (although quantification with the high background gave 2.0% for trm6Δ and 2.8% in trm61Δ).
PMID:35901126	FYPO:0001357	normal vegetative cell population growth	Similarly, the temperature sensitivity of the S. pombe trm61Δ strain was completely suppressed by expression of the stand-alone imt06+ gene (S5 Fig).
PMID:35901126	FYPO:0000674	normal cell population growth at high temperature	Similarly, the temperature sensitivity of the S. pombe trm61Δ strain was completely suppressed by expression of the stand-alone imt06+ gene (S5 Fig).
PMID:35901126	FYPO:0001357	normal vegetative cell population growth	Similarly, the temperature sensitivity of the S. pombe trm61Δ strain was completely suppressed by expression of the stand-alone imt06+ gene (S5 Fig).
PMID:35901126	FYPO:0000674	normal cell population growth at high temperature	Similarly, the temperature sensitivity of the S. pombe trm61Δ strain was completely suppressed by expression of the stand-alone imt06+ gene (S5 Fig).
PMID:35901126	GO:0180037	rapid tRNA decay	The discovery of dhp1 and tol1 mutations as suppressors of the S. pombe trm6Δ temperature sensitivity demonstrates the involvement of the RTD pathway in decay of tRNAiMet(CAU) lacking m1A58 in S. pombe.
PMID:35901126	GO:0180037	rapid tRNA decay	The discovery of dhp1 and tol1 mutations as suppressors of the S. pombe trm6Δ temperature sensitivity demonstrates the involvement of the RTD pathway in decay of tRNAiMet(CAU) lacking m1A58 in S. pombe.
PMID:35901126	FYPO:0002583	decreased mature tRNA level during vegetative growth [assayed_transcript] PomBase:SPBTRNAMET.06 [has_severity] high	The northern analysis revealed that tRNAiMet(CAU) levels were substantially reduced in the S. pombe trm6Δ mutants, both at 30 ̊C and 38.5 ̊C. At 30 ̊C, tRNAiMet(CAU) levels were 49% of those in WT cells, whereas each of the other eight tRNAs had levels between 82% and 121% of those in WT cells (Figs 2A, 2B and S3).
PMID:35901126	GO:0160107	tRNA (adenine(58)-N1)-methyltransferase activity [has_input] PomBase:SPBTRNAMET.06	These results show that S. pombe trm6+ and trm61+ are required for all detectable m1A58 modification of cytoplasmic tRNAs.
PMID:35901126	GO:0160107	tRNA (adenine(58)-N1)-methyltransferase activity [has_input] PomBase:SPBTRNAMET.06	These results show that S. pombe trm6+ and trm61+ are required for all detectable m1A58 modification of cytoplasmic tRNAs.
PMID:35901126	FYPO:0000674	normal cell population growth at high temperature	We found that the temperature sensitive growth defect of S. pombe trm6Δ mutants on EMMC-leu media was completely suppressed by expression of the stand-alone imt06+ gene, growing identically to that of an S. pombe trm6Δ [Ptrm6 trm6+] strain at high temperature (Fig 2C)
PMID:35901126	FYPO:0000674	normal cell population growth at high temperature	We found that the temperature sensitive growth defect of S. pombe trm6Δ mutants on EMMC-leu media was completely suppressed by expression of the stand-alone imt06+ gene, growing identically to that of an S. pombe trm6Δ [Ptrm6 trm6+] strain at high temperature (Fig 2C)
PMID:35901126	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	We observed little, if any, suppression of the trm6Δ growth defect in the trm6Δ cid14Δ strains (S13A Fig), and only very minor restoration of tRNAiMet(CAU) levels at high temperature, relative to levels in trm6Δ mutants (21% vs 18%, compared to 39% in the trm6Δ dhp1-5 strain) (S13B and S13C Fig). Thus, we infer that tRNAiMet(CAU) is degraded in S. pombe trm6Δ and trm6Δ imt06Δ mutants primarily by the RTD pathway, and not appreciably by the TRAMP complex of the nuclear surveillance pathway.
PMID:35908934	FYPO:0000468	abnormal mating type switching	(Fig. 2A)
PMID:35908934	FYPO:0000468	abnormal mating type switching	(Fig. 2A)
PMID:35908934	FYPO:0000468	abnormal mating type switching	(Fig. 2A)
PMID:35908934	FYPO:0000468	abnormal mating type switching [has_penetrance] medium	(Fig. 2A, Fig. 4A)
PMID:35908934	FYPO:0000708	decreased mating efficiency	(Fig. 2B)
PMID:35908934	FYPO:0000708	decreased mating efficiency	(Fig. 2B)
PMID:35908934	FYPO:0000708	decreased mating efficiency	(Fig. 2B)
PMID:35908934	FYPO:0000708	decreased mating efficiency	(Fig. 2B)
PMID:35908934	FYPO:0000969	normal growth during cellular response to UV	(Fig. 2D)
PMID:35908934	FYPO:0000969	normal growth during cellular response to UV	(Fig. 2D)
PMID:35908934	FYPO:0000969	normal growth during cellular response to UV	(Fig. 2D)
PMID:35908934	FYPO:0000468	abnormal mating type switching [has_penetrance] low	(Fig. 4A)
PMID:35908934	FYPO:0000468	abnormal mating type switching [has_penetrance] low	(Fig. 4A)
PMID:35908934	FYPO:0000468	abnormal mating type switching [has_penetrance] low	(Fig. 4C, Fig. 6C)
PMID:35908934	FYPO:0000468	abnormal mating type switching	(Fig. 4D)
PMID:35908934	FYPO:0000472	normal mating type switching	(Fig. 4E)
PMID:35908934	FYPO:0000472	normal mating type switching	(Fig. 4E)
PMID:35908934	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 5B)
PMID:35908934	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 5B)
PMID:35908934	FYPO:0006987	increased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth	(Fig. 5C)
PMID:35908934	FYPO:0002355	decreased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth	(Fig. 5C)
PMID:35908934	FYPO:0000472	normal mating type switching	(Fig. 5C)
PMID:35908934	FYPO:0000472	normal mating type switching	(Fig. 5C)
PMID:35908934	FYPO:0007509	increased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth	(Fig. 5D)
PMID:35908934	FYPO:0008364	normal histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth	(Fig. 5D)
PMID:35908934	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 6B)
PMID:35908934	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 6B)
PMID:35908934	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 6B)
PMID:35908934	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 6B)
PMID:35908934	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 6B)
PMID:35908934	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 6B)
PMID:35908934	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 6B)
PMID:35908934	FYPO:0000468	abnormal mating type switching [has_penetrance] high	(Fig. 6C)
PMID:35908934	FYPO:0000468	abnormal mating type switching [has_penetrance] low	(Fig. 6C)
PMID:35908934	FYPO:0000468	abnormal mating type switching [has_penetrance] low	(Fig. 6C)
PMID:35908934	FYPO:0000468	abnormal mating type switching [has_penetrance] low	(Fig. 6C)
PMID:35908934	FYPO:0000468	abnormal mating type switching [has_penetrance] low	(Fig. 6C)
PMID:35908934	FYPO:0000468	abnormal mating type switching [has_penetrance] low	(Fig. 6C)
PMID:35908934	FYPO:0000468	abnormal mating type switching [has_penetrance] high	(Fig. 6C)
PMID:35908934	FYPO:0000468	abnormal mating type switching [has_penetrance] medium	(Fig. 6C)
PMID:35908934	GO:0007535	donor selection	We propose that the resultant chromatin organization is at least in part responsible for the altered donor choices in HULC and Set1C mutants (Fig. 7).
PMID:35908934	GO:0007535	donor selection	We propose that the resultant chromatin organization is at least in part responsible for the altered donor choices in HULC and Set1C mutants (Fig. 7).
PMID:35908934	GO:0007535	donor selection	We propose that the resultant chromatin organization is at least in part responsible for the altered donor choices in HULC and Set1C mutants (Fig. 7).
PMID:35908934	GO:0007535	donor selection	We propose that the resultant chromatin organization is at least in part responsible for the altered donor choices in HULC and Set1C mutants (Fig. 7).
PMID:35908934	GO:0007535	donor selection	We propose that the resultant chromatin organization is at least in part responsible for the altered donor choices in HULC and Set1C mutants (Fig. 7).
PMID:35924983	GO:0005737	cytoplasm [exists_during] cellular response to glucose starvation	(Fig. 6)
PMID:35924983	GO:0005654	nucleoplasm [exists_during] cellular response to glucose stimulus	(Fig. 6)
PMID:35924983	FYPO:0001492	viable elongated vegetative cell [has_severity] medium	(Figure 3)
PMID:35924983	FYPO:0001492	viable elongated vegetative cell [has_severity] low	(Figure 3)
PMID:35924983	FYPO:0001492	viable elongated vegetative cell [has_severity] medium	(Figure 3)
PMID:35924983	FYPO:0001327	increased protein level during vegetative growth [has_penetrance] high [has_severity] high [assayed_protein] PomBase:SPBC1D7.02c	(Figure 6)
PMID:35924983	FYPO:0001327	increased protein level during vegetative growth [has_penetrance] high [has_severity] high [assayed_protein] PomBase:SPBC1D7.02c	(Figure 6)
PMID:35924983	FYPO:0001327	increased protein level during vegetative growth [has_penetrance] high [has_severity] high [assayed_protein] PomBase:SPBC1D7.02c	(Figure 6)
PMID:35924983	FYPO:0001130	increased protein localization to nucleus during vegetative growth [has_penetrance] high [has_severity] high [assayed_protein] PomBase:SPBC1D7.02c	(Figure 6)
PMID:35924983	FYPO:0001327	increased protein level during vegetative growth [has_penetrance] high [has_severity] high [assayed_protein] PomBase:SPBC1D7.02c	(Figure 6)
PMID:35924983	FYPO:0001130	increased protein localization to nucleus during vegetative growth [has_penetrance] high [has_severity] high [assayed_protein] PomBase:SPBC1D7.02c	(Figure 6)
PMID:35924983	FYPO:0009111	increased flocculation during vegetative growth	(Figure 7)
PMID:35924983	FYPO:0009111	increased flocculation during vegetative growth [has_severity] high	(Figure 7)
PMID:35924983	FYPO:0009112	abolished flocculation during vegetative growth [has_penetrance] high	(Figure 7)
PMID:35924983	FYPO:0009112	abolished flocculation during vegetative growth [has_penetrance] high	(Figure 7)
PMID:35924983	FYPO:0009112	abolished flocculation during vegetative growth [has_penetrance] high	(Figure 7)
PMID:35924983	FYPO:0009112	abolished flocculation during vegetative growth [has_penetrance] high	(Figure 7)
PMID:35924983	FYPO:0009112	abolished flocculation during vegetative growth [has_penetrance] high	(Figure 7)
PMID:35924983	FYPO:0009111	increased flocculation during vegetative growth [has_severity] high	(Figure 7)
PMID:35924983	GO:1900735	positive regulation of flocculation [happens_during] cellular response to glucose starvation	(comment: through degradation by ubiquitination)
PMID:35924983	GO:1900735	positive regulation of flocculation [happens_during] cellular response to glucose starvation	(comment: through degradation by ubiquitination)
PMID:35924983	GO:1900735	positive regulation of flocculation [happens_during] cellular response to glucose starvation	(comment: through nuclear exclusion)
PMID:35924983	GO:1900735	positive regulation of flocculation [happens_during] cellular response to glucose starvation	(comment: through nuclear exclusion)
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth	Supplemental Figure 4
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001492	viable elongated vegetative cell	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001492	viable elongated vegetative cell	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001492	viable elongated vegetative cell [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001492	viable elongated vegetative cell [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Supplemental Figure 4, Table 1
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35924983	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Supplemental Figure 6
PMID:35940128	FYPO:0003480	queuosine absent from tRNA	(comment: Queuosine absent from tRNA when cells are supplied with queuosine nucleoside, but not when supplied with queuine nucleobase)
PMID:35970865	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 2a)
PMID:35970865	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 2a)
PMID:35970865	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 2a)
PMID:35970865	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 2a)
PMID:35970865	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 2a) The resultant mis6-302 cut9-665 double mutant exhibited severe growth defects, even at the semi-restrictive temperature (Fig. 2a). This suggests that the mitotic function of Mis6 is crucial for prolonged metaphase.
PMID:35970865	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 2a) The resultant mis6-302 cut9-665 double mutant exhibited severe growth defects, even at the semi-restrictive temperature (Fig. 2a). This suggests that the mitotic function of Mis6 is crucial for prolonged metaphase.
PMID:35970865	FYPO:0008014	decreased protein localization to CENP-A containing chromatin during mitosis [assayed_region] regional_centromere [assayed_protein] PomBase:SPBC1105.17	"(Fig. 2c, d) (comment: CHECK ""decreased CENP-A maintenance during M-phase"".) defective in CENP-A maintenance during M phase, as well as defective in CENP-A loading during interphase The GFP-Cnp1 intensity at centromeres decayed more rapidly in mis6-302 cells than in WT cells (Fig. 2f, g and Supplementary Figs. 4 and 5a). Taken together, these results suggest that Mis6, but not Scm3, is responsible for the maintenance of Cnp1 at centromeres during metaphase."
PMID:35970865	FYPO:0008025	normal protein localization to CENP-A containing chromatin during mitosis [assayed_protein] PomBase:SPBC1105.17	(Figure 2a) (comment: CHECK during M-phase)
PMID:35970865	FYPO:0003217	decreased chromatin silencing at centromere central core [has_penetrance] medium	(Figure 4)
PMID:35970865	FYPO:0003217	decreased chromatin silencing at centromere central core [has_penetrance] high	(Figure 4)
PMID:35970865	FYPO:0004313	decreased protein localization to CENP-A containing chromatin [assayed_protein] PomBase:SPBC1105.17	(comment: CHECK decreased CENP-A maintenance)
PMID:35970865	FYPO:0008025	normal protein localization to CENP-A containing chromatin during mitosis	(comment: CHECK during M-phase) Mis15 localises to the inner regions of centromeres as does Mis6, while Mis12 and Nuf2 localise to the outer regions relative to Mis6, and Mis6 localised to centromeres in the mis12 and nuf2 mutants but not in the mis15 mutant (Supplementary Fig. 6)
PMID:35970865	FYPO:0002360	normal chromatin silencing at centromere	(comment: CHECK during M-phase) Supplementary Fig. 9b). These results demonstrate that kinetochore mutants with the intact inner kinetochore architecture retained the ability to silence transcription at the central core region.
PMID:35970865	FYPO:0002360	normal chromatin silencing at centromere	(comment: CHECK during M-phase) Supplementary Fig. 9b). These results demonstrate that kinetochore mutants with the intact inner kinetochore architecture retained the ability to silence transcription at the central core region.
PMID:35970865	FYPO:0004314	normal protein localization to CENP-A containing chromatin [assayed_protein] PomBase:SPBC1105.17	(comment: CHECK normal CENP-A maintenance)
PMID:35970865	FYPO:0004314	normal protein localization to CENP-A containing chromatin [assayed_protein] PomBase:SPBC1105.17	(comment: CHECK normal CENP-A maintenance)
PMID:35970865	FYPO:0004314	normal protein localization to CENP-A containing chromatin [assayed_protein] PomBase:SPBC1105.17	(comment: CHECK normal CENP-A maintenance)
PMID:35970865	FYPO:0004314	normal protein localization to CENP-A containing chromatin [assayed_protein] PomBase:SPBC1105.17	(comment: CHECK normal CENP-A maintenance)
PMID:35970865	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_protein] PomBase:SPBC28F2.12	(comment: Note that an increase of transcript levels from centromeres has not been demonstrated in the paper. What has been exactly demonstrated is an increased association of RNA polII to the cnt region of centromeres.)
PMID:35970865	FYPO:0007295	increased protein localization to CENP-A containing chromatin [assayed_protein] PomBase:SPBC28F2.12	(comment: Note that an increase of transcript levels from centromeres has not been demonstrated in the paper. What has been exactly demonstrated is an increased association of RNA polII to the cnt region of centromeres.)
PMID:35970865	FYPO:0008014	decreased protein localization to CENP-A containing chromatin during mitosis [assayed_protein] PomBase:SPBC1105.17	Defective in CENP-A maintenance. Mis15 localises to the inner regions of centromeres as does Mis6, while Mis12 and Nuf2 localise to the outer regions relative to Mis6, and Mis6 localised to centromeres in the mis12 and nuf2 mutants but not in the mis15 mutant (Supplementary Fig. 6)In the mis15-68 mutants, signal intensities of Cnp1 at centromeres during mitotic arrest were decreased like in the mis6-302 mutant, whereas not in the mis12-537 and nuf2-2 mutants (Fig. 2h-j and Supplementary Figs. 5b-d and 7)
PMID:35970865	GO:0140713	histone chaperone activity [has_input] PomBase:SPBC1105.17	When we followed the temporal kinetics of GFP- Cnp1 intensity during metaphase, the reduction of GFP-Cnp1 intensity seen in mis6-302 and mis15-68 cells was rescued by the additional knockout of Fft3 (mis6-302 fft3Δ, Supplementary Fig. 11a-c; mis15-68 fft3Δ, Supplementary Fig. 11d-f), confirming that Fft3 removes Cnp1 upon transcription at centromeres.
PMID:35970865	FYPO:0008025	normal protein localization to CENP-A containing chromatin during mitosis	during M-phase Mis15 localises to the inner regions of centromeres as does Mis6, while Mis12 and Nuf2 localise to the outer regions relative to Mis6, and Mis6 localised to centromeres in the mis12 and nuf2 mutants but not in the mis15 mutant (Supplementary Fig. 6)
PMID:36002457	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	A similar growth defect was visible for the red1-E32R-TAP mutant cells grown on minimal medium, suggesting that Red1-Ars2 interaction, depending on the growth conditions, can be important for the normal growth of the cell population (Fig. 5h).
PMID:36002457	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02	However, no significant changes were observed for several meiotic mRNAs and PROMPTs/CUTs MTREC targets (Supplementary Fig. 8b, c)
PMID:36002457	FYPO:0008152	normal CUT RNA level [assayed_transcript] PomBase:SPNCRNA.4748	However, no significant changes were observed for several meiotic mRNAs and PROMPTs/CUTs MTREC targets (Supplementary Fig. 8b, c)
PMID:36002457	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC70.09c	However, no significant changes were observed for several meiotic mRNAs and PROMPTs/CUTs MTREC targets (Supplementary Fig. 8b, c)
PMID:36002457	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1952.15c	However, no significant changes were observed for several meiotic mRNAs and PROMPTs/CUTs MTREC targets (Supplementary Fig. 8b, c)
PMID:36002457	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	Importantly, red1-L205R cells showed a similar growth defect, when grown on minimal medium, suggesting that Red1-Iss10 interaction can be important for Red1-dependent cell growth function depending on the environmental conditions (Fig. 3b).
PMID:36002457	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC1006.03c [assayed_protein] PomBase:SPBC725.08	In Strep-tag pull down assays, both mutations (K483D, F490D) essentially disrupted the Red1 binding (Supplementary Fig. 7d, lanes 3, 4).
PMID:36002457	FYPO:0007280	decreased protein localization to nuclear exosome focus [assayed_protein] PomBase:SPBC725.08	Interestingly, quantification of the intensity of the signal within each nucleus showed a reduction of Ars2-GFP nuclear signal in red1-E32R mutant cells compared to wild-type cells, suggesting that some of Ars2-GFP proteins diffuse to the cytoplasm (Supplementary Fig. 8e).
PMID:36002457	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPAC7D4.14c [part_of] nuclear mRNA surveillance of meiosis-specific transcripts	These findings indicate that the interaction of Iss10 with Red1 is required for Iss10 recruitment to Red1 nuclear foci and suggest that it may promote the clustering of Red1 nuclear foci.
PMID:36002457	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC1006.03c [assayed_protein] PomBase:SPBC725.08	Using Y2H assays, we could show that the Red1 E32R mutation is sufficient to prevent the interaction with Ars2 in the context of full-length proteins (Fig. 5f). mportantly, while Red1-TAP and Ars2-GFP interact, as expected, this interaction was lost in cells expressing Red1-E32R-TAP (Fig. 5g).
PMID:36002457	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC7D4.14c [assayed_protein] PomBase:SPAC1006.03c	Using these cells, reciprocal co-immunoprecipitation experiments showed that the Red1-L205R mutation also compromised Red1 association with Iss10 in S. pombe (Fig. 3a and Supplementary Fig. 3a).
PMID:36002457	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1D7.05	We examined the possible effect of red1-E32R mutation on pho1 and byr2 mRNAs. However, no significant changes in pho1 and byr2 mRNA levels were observed between wild-type and red1-E32R mutant cells (Supplementary Fig. 8d).
PMID:36002457	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	We examined the possible effect of red1-E32R mutation on pho1 and byr2 mRNAs. However, no significant changes in pho1 and byr2 mRNA levels were observed between wild-type and red1-E32R mutant cells (Supplementary Fig. 8d).
PMID:36002457	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02 [has_severity] medium	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1952.15c [has_severity] medium	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC70.09c	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC70.09c [has_severity] medium	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1952.15c [has_severity] medium	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02 [has_severity] medium	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	FYPO:0007280	decreased protein localization to nuclear exosome focus [assayed_protein] PomBase:SPAC7D4.14c	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	FYPO:0002964	increased protein localization to nuclear exosome focus [assayed_protein] PomBase:SPAC1006.03c	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [has_severity] high [assayed_transcript] PomBase:SPCC70.09c	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [has_severity] high [assayed_transcript] PomBase:SPAC1952.15c	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02 [has_severity] high	We observed that the red1-L205R mutation had an effect on both Iss10 and Red1 localization by, respectively, inducing the disappearance of Iss10 nuclear foci and the increase in the number of Red1 foci per nucleus (Fig. 3c-e)
PMID:36002457	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC7D4.14c [assayed_protein] PomBase:SPAC1006.03c	While A198E retained the WT level of binding (Fig. 2i, lanes 3 and 7), the L205R and F215R mutants no longer bound Iss10 (Fig. 2i, lanes 4, 5, 8 and 9).
PMID:36002457	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC7D4.14c [assayed_protein] PomBase:SPAC1006.03c	While A198E retained the WT level of binding (Fig. 2i, lanes 3 and 7), the L205R and F215R mutants no longer bound Iss10 (Fig. 2i, lanes 4, 5, 8 and 9).
PMID:36002457	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	While red1Δ cells showed only a moderate growth defect on solid rich medium at 30°C, this defect was more pronounced at lower temperature of 25 or 18°C (Supplementary Fig. 3b), as published previously1
PMID:36002457	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	While red1Δ cells showed only a moderate growth defect on solid rich medium at 30°C, this defect was more pronounced at lower temperature of 25 or 18°C (Supplementary Fig. 3b), as published previously1
PMID:36002457	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	While red1Δ cells showed only a moderate growth defect on solid rich medium at 30°C, this defect was more pronounced at lower temperature of 25 or 18°C (Supplementary Fig. 3b), as published previously14,34 or when the cells were grown on minimal medium (Supplementary Fig. 3c).
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint	(Figure 1D)
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] high	(Figure 1D)
PMID:36006032	FYPO:0005728	normal deactivation of mitotic spindle assembly checkpoint	(Figure 1D)
PMID:36006032	FYPO:0005728	normal deactivation of mitotic spindle assembly checkpoint	(Figure 1D)
PMID:36006032	FYPO:0005728	normal deactivation of mitotic spindle assembly checkpoint	(Figure 1D)
PMID:36006032	FYPO:0005728	normal deactivation of mitotic spindle assembly checkpoint	(Figure 1D)
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint	(Figure 1D)
PMID:36006032	FYPO:0006559	delayed onset of mitotic spindle disassembly [has_severity] low	(Figure 1D)
PMID:36006032	FYPO:0005728	normal deactivation of mitotic spindle assembly checkpoint	(Figure 1D)
PMID:36006032	FYPO:0001758	increased protein phosphatase activity [assayed_enzyme] PomBase:SPAP8A3.09c	Our in vitro dephosphorylation assay results demonstrated that individually overexpressing PP2A subunits indeed boosted the overall phosphatase activity compared to expressing endogenous subunits alone (Figure 3B).
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] medium	Overexpression of Par1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] medium	Overexpression of Par1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] medium	Overexpression of Par2 suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] medium	Overexpression of Par2 suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] medium	Overexpression of Ppa2 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] medium	Overexpression of Ppa2 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] medium	Overexpression of Ppa2 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] medium	Overexpression of Ppa2 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] medium	Overexpression of all Ppa1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] medium	Overexpression of all Ppa1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrest-and-release in the nda3-KM311 mutant background.
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] medium	Pab1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrestand-release in the nda3-KM311 mutant background (Figure 2 and Figure S2).
PMID:36006032	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] medium	Pab1 slightly suppressed the SAC silencing defects and allowed dis2Δ cells to enter anaphase earlier after arrestand-release in the nda3-KM311 mutant background (Figure 2 and Figure S2).
PMID:36088506	PomGeneEx:0000018	protein level increased [during] single-celled organism vegetative growth phase [during] cellular response to glucose starvation [in_presence_of] N-benzyloxycarbonyl-L-leucyl-L-leucyl-L-leucinal	(comment: proteasome inhibitor MG132)
PMID:36088506	GO:0005741	mitochondrial outer membrane	As observed, most of Mrz1 was localized in the mitochondrial fraction (Fig. 1B).
PMID:36088506	PomGeneEx:0000019	protein level decreased [during] single-celled organism vegetative growth phase [during] cellular response to glucose starvation	As shown in Fig. 2A, Mrz1 expression was decreased during the stationary phase grown on YES.
PMID:36088506	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC16G5.03	Assessment of Mrz1 levels in these strains (Fig. 3) showed that the levels of Mrz1 markedly increased in ubc13 deletion background and no others, apart from the expected increase in the addition of MG132 controls.
PMID:36088506	FYPO:0001164	normal growth on glucose carbon source	The growth of the mrz1 mutant was almost like WT strain in both glucose- and glycerol-containing media at 30 °C (Fig. 4A).
PMID:36090151	FYPO:0001245	sensitive to cobalt [has_severity] high	(comment: CONDITION 1.6 mM)
PMID:36090151	FYPO:0001245	sensitive to cobalt [has_severity] high	(comment: CONDITION 1.6 mM)
PMID:36095128	FYPO:0008118	decreased splicing of introns with branch point-distant 3’-splice site	(Figure 1)
PMID:36095128	FYPO:0008118	decreased splicing of introns with branch point-distant 3’-splice site	(Figure 1)
PMID:36095128	FYPO:0008118	decreased splicing of introns with branch point-distant 3’-splice site	(Figure 1)
PMID:36095128	FYPO:0008118	decreased splicing of introns with branch point-distant 3’-splice site [assayed_transcript] PomBase:SPAC11E3.09	(Figure 1) (comment: rap1 intron2, ftp105 intron 3 and pyp3 intron 1)
PMID:36095128	FYPO:0008118	decreased splicing of introns with branch point-distant 3’-splice site [assayed_transcript] PomBase:SPBC1778.02	(Figure 1) (comment: rap1 intron2, ftp105 intron 3 and pyp3 intron 1)
PMID:36095128	FYPO:0008118	decreased splicing of introns with branch point-distant 3’-splice site [assayed_transcript] PomBase:SPAC17A5.16	(Figure 1) (comment: rap1 intron2, ftp105 intron 3 and pyp3 intron 1)
PMID:36095128	FYPO:0003619	normal mRNA splicing, via spliceosome	(Figure 1) (rap1 intron2 branch site distance decreased)
PMID:36095128	FYPO:0003619	normal mRNA splicing, via spliceosome	(Figure 1) (rap1 intron2 branch site distance decreased)
PMID:36095128	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC428.06c	(Figure S12B)
PMID:36095128	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC1778.02	(Figure S12B)
PMID:36095128	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC582.04c	(Figure S12B)
PMID:36095128	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPCC1235.09	(Figure S12B)
PMID:36095128	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC428.06c	(Figure S12B)
PMID:36095128	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC1778.02	(Figure S12B)
PMID:36095128	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC582.04c	(Figure S12B)
PMID:36095128	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPCC1235.09	(Figure S12B)
PMID:36095128	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC428.06c	(Figure S12B)
PMID:36095128	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPCC1235.09	(Figure S12B)
PMID:36095128	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC1778.02	(Figure S12B)
PMID:36095128	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC582.04c	(Figure S12B)
PMID:36095128	GO:0045292	mRNA cis splicing, via spliceosome	(Figure S13C)
PMID:36095128	GO:0045292	mRNA cis splicing, via spliceosome	(Figure S13C)
PMID:36095128	GO:0045292	mRNA cis splicing, via spliceosome	(Figure S13C)
PMID:36095128	GO:0045292	mRNA cis splicing, via spliceosome	(Figure S13C)
PMID:36095128	GO:0045292	mRNA cis splicing, via spliceosome	(Figure S13C)
PMID:36095128	GO:0045292	mRNA cis splicing, via spliceosome	(Figure S13C)
PMID:36095128	GO:0045292	mRNA cis splicing, via spliceosome	(Figure S13C)
PMID:36095128	GO:0045292	mRNA cis splicing, via spliceosome	(Figure S13C)
PMID:36095128	GO:0045292	mRNA cis splicing, via spliceosome	(Figure S13C)
PMID:36095128	GO:0045292	mRNA cis splicing, via spliceosome	(Figure S13C)
PMID:36095128	GO:0045292	mRNA cis splicing, via spliceosome	(Figure S13C)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(Figure S13C) (comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(Figure S13C) (comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPBC1778.02	(Supplementary Figures S6 and S7A). (comment: rap1 intron 2)
PMID:36095128	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPCC16A11.08	(Supplementary Figures S6 and S7A). ...the disruption of secondary structures by exposure to elevated temperatures could open the fold and increase the distance between the BP and 3′ss.... Indeed, excision of introns with secondary structures such as rap1 intron 2, whi5 intron 1, atg20 intron 2 and mug65 intron 2 was sensitive to 15 min treatment at 42◦C. After lowering the temperature to 25◦C, splicing defects of these introns recovered in wt cells, but the recovery with whi5 and atg20 introns was slower in Δsde2.
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_transcript] PomBase:SPBC1778.02	(comment: A shorter form of the protein translated from intron-retained transcript)
PMID:36095128	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPBC582.04c	(comment: Semi quantitative RT-PCR followed by gel electrophoresis); Intron retention observed in absence of sde2, cay1 and tls1
PMID:36095128	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPCC1235.09	(comment: Semi quantitative RT-PCR followed by gel electrophoresis); Intron retention observed in absence of sde2, cay1 and tls1
PMID:36095128	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPBC582.04c	(comment: Semi quantitative RT-PCR followed by gel electrophoresis); Intron retention observed in absence of sde2, cay1 and tls1
PMID:36095128	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPCC1235.09	(comment: Semi quantitative RT-PCR followed by gel electrophoresis); Intron retention observed in absence of sde2, cay1 and tls1
PMID:36095128	FYPO:0008118	decreased splicing of introns with branch point-distant 3’-splice site	Among the mutants studied, Δcay1 and Δtls1 strains also showed splicing defects specific for rap1 intron 2 (Supplementary Figure S10A).
PMID:36095128	FYPO:0008118	decreased splicing of introns with branch point-distant 3’-splice site	Among the mutants studied, Δcay1 and Δtls1 strains also showed splicing defects specific for rap1 intron 2 (Supplementary Figure S10A).
PMID:36108046	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(comment: I changed to decreased. becasue the phenotype is compared to WT,)
PMID:36108046	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(comment: I changed to decreased. becasue the phenotype is compared to WT,)
PMID:36108046	FYPO:0000091	sensitive to thiabendazole [has_severity] low	Consequently, sensitivity of dnt1Δ cells to TBZ was largely but not completely suppressed by excessive Slp1Cdc20 expression achieved by three copies of slp1+ (Fig 3E).
PMID:36108046	FYPO:0000670	abnormal mitotic sister chromatid separation [has_severity] medium	Consistent with this assumption, we found that dnt1Δ cells lost minichromosomes (Ch16, ade6-M216) at an elevated rate that is almost 100 times higher than that of the wild-type (Fig 1B), and displayed increased frequency of lagging chromosomes and chromosome mis-segregation at mitotic anaphase (Fig 1C).
PMID:36108046	FYPO:0000835	decreased protein level [has_severity] medium [assayed_protein] PomBase:SPAC821.08c	Surprisingly, Slp1Cdc20 was slightly, but appreciably and reproducibly, less abundant (ranging from roughly 20% to 50% at different time points) in dnt1Δ cells than in wild-type cells (Fig 3B), suggesting Dnt1 may indeed positively regulate the levels of intact Slp1Cdc20. In addition, this regulation of Slp1Cdc20 stability by Dnt1 is Dma1-independent, as the dnt1Δ dma1Δ double mutant has a similar level and degradation profile of Slp1Cdc20 as dnt1Δ single mutant (S5 Fig).
PMID:36108046	FYPO:0008032	normal mitotic spindle checkpoint activation	but dnt1Δ cells stayed for extended length of time at anaphase B (Fig 1D-1F)
PMID:36108046	FYPO:0005706	increased duration of mitotic anaphase B	but dnt1Δ cells stayed for extended length of time at anaphase B (Fig 1D-1F)
PMID:36108046	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint	inefficient anaphase initiation upon SAC inactivation/ persistent MCC-APC/C binding upon SAC activation The SAC was first robustly activated by the nda3-KM311 mutant then inactivated by shifting mitotically arrested cells back to permissive temperature(30˚C)/ We found that dnt1Δ cells retained high amounts of SPB-localized Cdc13-GFP and nuclear Cut2-GFP for much prolonged period compared to wild-type cells, almost to the same degree as previously identified SAC-inactivation defective mutant dis2Δ
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	(Fig. 1) (double mutant with cyr1 is more sensitive)
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Fig. 1b)
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] low	(Fig. 2) Overexpression of Pka1 restores the KCl-sensitive phenotype of the plb1∆ strain.
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] low	(Fig. 2) Overexpression of Pka1 restores the KCl-sensitive phenotype of the plb1∆ strain.
PMID:36112198	FYPO:0005947	normal growth on potassium chloride	(Fig. 4)
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] low	(Fig. 4) rst2∆ partially rescues plb1∆ on KCl
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] low	(Fig. 4) rst2∆ partially rescues plb1∆ on KCl
PMID:36112198	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC106.10	(Fig. 5)
PMID:36112198	FYPO:0006717	normal growth on sodium chloride	(Fig. S2)
PMID:36112198	FYPO:0001020	normal growth on calcium	(Fig. S2)
PMID:36112198	FYPO:0006717	normal growth on sodium chloride	(Fig. S2)
PMID:36112198	FYPO:0000098	sensitive to calcium [has_severity] medium	(Fig. S2)
PMID:36112198	FYPO:0000098	sensitive to calcium [has_severity] medium	(Fig. S2)
PMID:36112198	FYPO:0000098	sensitive to calcium	(Fig. S2)
PMID:36112198	FYPO:0000961	normal growth on sorbitol	(Fig. S2)
PMID:36112198	FYPO:0006717	normal growth on sodium chloride	(Fig. S2)
PMID:36112198	FYPO:0000112	sensitive to sorbitol	(Figure 2)
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	(Figure 2)
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	(Figure 2)
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 2)
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 2)
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 2)
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 2)
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 2b)
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 2b)
PMID:36112198	FYPO:0005947	normal growth on potassium chloride	(Figure 3)
PMID:36112198	FYPO:0006717	normal growth on sodium chloride	(Figure S2)
PMID:36112198	GO:0005783	endoplasmic reticulum [exists_during] cellular response to potassium ion	(comment: CHECK glucose MM)
PMID:36112198	GO:0005783	endoplasmic reticulum [exists_during] cell cycle phase	(comment: CHECK glucose MM)
PMID:36112198	GO:0005783	endoplasmic reticulum [exists_during] cellular response to glucose starvation	(comment: CHECK low glucose MM)
PMID:36112198	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC106.10	(comment: observed Pka1-GFP)
PMID:36112198	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPBC106.10	(comment: observed Pka1-GFP)
PMID:36112198	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPBC106.10	(comment: observed Pka1-GFP)
PMID:36112198	FYPO:0006552	increased protein localization to cytoplasm [assayed_protein] PomBase:SPBC106.10	(comment: observed Pka1-GFP)
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] low	cgs1∆ partially rescues cyr1∆ plb1∆ on KCl
PMID:36112198	FYPO:0001214	sensitive to potassium chloride	cgs1∆ partially rescues plb1∆ on KCl
PMID:36112198	FYPO:0001214	sensitive to potassium chloride	cgs1∆ partially rescues plb1∆ on KCl
PMID:36112198	FYPO:0000961	normal growth on sorbitol	cgs1∆ rescues cyr1∆ plb1∆ on sorbitol
PMID:36112198	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	rst2∆ partially rescues pka1∆ plb1∆ on KCl
PMID:36112198	FYPO:0005947	normal growth on potassium chloride	rst2∆ rescues pka1∆ on KCl
PMID:36112198	FYPO:0005947	normal growth on potassium chloride	rst2∆ rescues pka1∆ on KCl
PMID:36112198	FYPO:0000961	normal growth on sorbitol	rst2∆ rescues pka1∆ plb1∆ on KCl
PMID:36138017	FYPO:0000912	abolished protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPAC3C7.12	(Fig. 2d)
PMID:36138017	FYPO:0002657	normal occurrence of NETO	(Fig. 4)
PMID:36138017	FYPO:0001017	premature NETO	(Fig. 4)
PMID:36138017	GO:1902716	cell cortex of growing cell tip [exists_during] mitotic interphase	(Figure 1D)
PMID:36138017	FYPO:0001571	increased protein-protein interaction [assayed_protein] PomBase:SPBC1706.01 [assayed_protein] PomBase:SPAC3C7.12 [has_severity] medium	More interestingly, in the presence of HU, the binding between Tea4 and Tip1 was elevated in dma1Δ cells and in wild-type cells treated with deubiquitinating enzyme USP2 to remove Tip1 ubiquitination (Fig. 4f), this is consistent with increased polar growth in dma1Δ cells (Fig. 4b).
PMID:36138017	FYPO:0000912	abolished protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPAC3C7.12	Strikingly, Tip1 ubiquitination was abolished in both dma1 mutants (Fig. 2d), demonstrating that both functional FHA and RF domains in Dma1 are required for Tip1 ubiquitination in vivo.
PMID:36138017	FYPO:0007552	normal protein ubiquitination during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC3C7.12	We found that Tip1 was efficiently ubiquitinated in the absence of the calcineurin catalytic subunit Ppb1, with a similar degree of modification to that of wild-type cells (Fig. 6a).
PMID:36138017	FYPO:0004601	normal S-phase DNA damage checkpoint during cellular response to hydroxyurea	though HU treatment caused equally efficient arrest at S phase in both wild-type and dma1Δ cells (Supplementary Fig. 4)
PMID:36174923	FYPO:0008043	increased protein localization to nucleus during stationary phase [assayed_protein] PomBase:SPAC1783.07c	(Fig. 4)
PMID:36174923	FYPO:0000245	loss of viability in stationary phase	(Fig. 5)
PMID:36174923	FYPO:0000245	loss of viability in stationary phase [has_severity] high	(Fig. 5)
PMID:36174923	FYPO:0000245	loss of viability in stationary phase [has_severity] high	(Fig. 5)
PMID:36174923	FYPO:0000245	loss of viability in stationary phase [has_severity] high	(Fig. 5)
PMID:36174923	FYPO:0000245	loss of viability in stationary phase	(Fig. 5)
PMID:36174923	FYPO:0000245	loss of viability in stationary phase [has_severity] high	(Fig. 5)
PMID:36174923	FYPO:0000245	loss of viability in stationary phase	(Fig. 6)
PMID:36174923	FYPO:0000245	loss of viability in stationary phase	(Fig. 7b) (comment: partial rescue - still loses viabiltiy at 48 hours)
PMID:36174923	FYPO:0000245	loss of viability in stationary phase	(Fig. 7b) (comment: partial rescue - still loses viabiltiy at 48 hours)
PMID:36174923	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPBC354.12	(Fig. S2)
PMID:36174923	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPCC1281.07c	(Fig. S2)
PMID:36174923	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPAC688.04c	(Fig. S2)
PMID:36174923	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPBC32F12.03c	(Fig. S2)
PMID:36174923	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPAC1486.01	(Fig. S2)
PMID:36174923	FYPO:0002060	viable vegetative cell population	(Fig. S5)
PMID:36174923	FYPO:0001357	normal vegetative cell population growth	(Fig. S5)
PMID:36174923	FYPO:0001357	normal vegetative cell population growth	(Fig. S5)
PMID:36174923	FYPO:0003991	increased RNA level in stationary phase [assayed_transcript] PomBase:SPBC609.04 [has_severity] high	(Figure 1)
PMID:36174923	FYPO:0003095	viable elongated vegetative cell, with progressive elongation	Microscopic examination revealed that Δsty1Δppr10 cells were highly elongated compared to WT, Δppr10, and Δsty1 cells (Fig. 5B), suggesting that progression from G2 into mitosis was impaired in Δsty1Δppr10 cells.
PMID:36200823	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC1250.01	(Figure 3E). As reported previously, deletion of clr3 increased the loading of Snf21 at pericentromeric repeats; however, we did not observe greater Snf21 occupancy in our sfh1-13 clr3Δ double mutant relative to a sfh1-13 single mutant, suggesting that sfh1-13 prevents the acetylation- dependent recruitment of Snf21 at pericentromeres, and that the elimination of misloaded CENP-ACnp1 in sfh1-13Δ clr3Δ cells is not due to the increase in Snf21 level.
PMID:36200823	FYPO:0006842	normal spatial extent of CENP-A containing nucleosome assembly	Furthermore, we observed ectopic CENP-ACnp1 deposition at pericentromeric heterochromatin domains in snf21-36 but not in rsc1 and rsc4 deletion mutants (Figure 1F)
PMID:36200823	FYPO:0000047	normal cell population growth	However, deletion strains of two genes encoding SWI/SNF core components, snf5 and snf22, did not exhibit sensitivity to CENP-ACnp1 overexpression (Supplementary Figure S2A).
PMID:36200823	FYPO:0000047	normal cell population growth	However, deletion strains of two genes encoding SWI/SNF core components, snf5 and snf22, did not exhibit sensitivity to CENP-ACnp1 overexpression (Supplementary Figure S2A).
PMID:36200823	FYPO:0006857	decreased histone H3-K37 methylation [has_severity] low	However, the sfh1-13 mutation had only a mild influence on H3K9me levels (Figure 1C), as we reported previously (12).
PMID:36200823	FYPO:0008036	increased nucleosome occupancy at CENP-A boundary	Importantly, MNase protection at sites i, iii, and v, which are located between CENP-ACnp1 and heterochromatin domains, was elevated in sfh1-13 cells (site i: 1.5-fold, P-value = 0.027; site iii: 2.2-fold, P-value = 0.0001; site v: 1.2-fold, P-value = 0.02; left panel of Figure 5B), indicating that Sfh1/RSC contributes to chromatin decompaction at the boundary.
PMID:36200823	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC1105.17	Importantly, no significant difference in the level of Cnp1 protein or mRNA was seen in sfh1-13 cells (Figure 1E).
PMID:36200823	FYPO:0000091	sensitive to thiabendazole [has_severity] high	In addition, a low concentration of TBZ enhanced the chromosome segregation defects of the temperature-sensitive sfh1-13 mutant (Supplementary Figure S1A).
PMID:36200823	FYPO:0000141	abnormal mitotic sister chromatid segregation	In addition, a low concentration of TBZ enhanced the chromosome segregation defects of the temperature-sensitive sfh1-13 mutant (Supplementary Figure S1A).
PMID:36200823	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPBC1861.01c	In sfh1-13 mutant cells, a small but significant increase in the localization of CENP-CCnp3 and CENP- IMis6 was observed at surrounding pericentromeric repeats (Figure 2B and C)
PMID:36200823	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC1687.20c	In sfh1-13 mutant cells, a small but significant increase in the localization of CENP-CCnp3 and CENP- IMis6 was observed at surrounding pericentromeric repeats (Figure 2B and C)
PMID:36200823	FYPO:0008035	ectopic CENP-A containing chromatin assembly at pericentromeric heterochromatin [assayed_region] regional_centromere_outer_repeat_region	at pericentromeric heterochromatin When CENP-ACnp1 was expressed at wild-type levels, specific accumulation at pericentromeric heterochromatin domains of all centromeres (Figure 1A), but not at non-centromeric locations
PMID:36200823	FYPO:0008035	ectopic CENP-A containing chromatin assembly at pericentromeric heterochromatin [assayed_region] regional_centromere_outer_repeat_region	at pericentromeric heterochromatin When CENP-ACnp1 was expressed at wild-type levels, specific accumulation at pericentromeric heterochromatin domains of all centromeres (Figure 1A), but not at non-centromeric locations
PMID:36200823	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	sfh1-13 clr3Δ cells were faster growing on TBZ-containing plates than sfh1-13 cells, indicating that deletion of clr3 partially rescues the TBZ sensitivity of sfh1-13.
PMID:36200823	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	sfh1-13 clr3Δ cells were faster growing on TBZ-containing plates than sfh1-13 cells, indicating that deletion of clr3 partially rescues the TBZ sensitivity of sfh1-13.
PMID:36200823	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	sfh1-13 clr3Δ cells were faster growing on TBZ-containing plates than sfh1-13 cells, indicating that deletion of clr3 partially rescues the TBZ sensitivity of sfh1-13.
PMID:36200823	FYPO:0001234	slow vegetative cell population growth	sfh1-13 mutant strain exhibited a slow growth phenotype at 32◦C upon nmt41-cnp1 expression (sfh1-13 at 32◦C in the lower panel of Supplementary Figure S1B
PMID:36200823	FYPO:0001234	slow vegetative cell population growth	sfh1-13 mutant strain exhibited a slow growth phenotype at 32◦C upon nmt41-cnp1 expression (sfh1-13 at 32◦C in the lower panel of Supplementary Figure S1B
PMID:36200823	FYPO:0006842	normal spatial extent of CENP-A containing nucleosome assembly	while loss of Clr3 eliminated CENP-ACnp1 accumulation at the pericentromere in a sfh1- 13 mutant background, indicating that Clr3 is required for ectopic deposition of CENP-ACnp1 (Figure 3D).
PMID:36200871	GO:0015275	stretch-activated, monoatomic cation-selective, calcium channel activity [part_of] calcium ion import into cytosol [part_of] cellular hyperosmotic response [happens_during] mitotic cytokinesis	(Figure 2E,F) We concluded that Pkd2 is calcium-permeable under the mechanical stimulus of membrane stretching.
PMID:36200871	FYPO:0001197	decreased cellular calcium level	At 36°C, the average calcium level of pkd2-B42 cells was 34% lower than that of wild type cells (Figure 3, C and D).
PMID:36200871	GO:0005886	plasma membrane	Supplemental Figure S5A). We concluded that the calcium-permeable Pkd2 primarily localizes to the plasma membrane.
PMID:36200871	FYPO:0008063	decreased immediate intracellular calcium spike following osmotic shock	The peak amplitude of the calcium spikes in pkd2-B42 cells was similarly reduced by 62% (Figure 4D).
PMID:36202103	FYPO:0006505	abolished protein localization to shmoo tip [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c	(Fig. 1B)
PMID:36202103	FYPO:0000413	abolished cell fusion during mating [has_penetrance] high	(Fig. 1C)
PMID:36202103	FYPO:0000413	abolished cell fusion during mating [has_penetrance] high	(Fig. 1C)
PMID:36202103	FYPO:0003527	protein mislocalized to cell tip [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c	(Fig. 1D)
PMID:36202103	FYPO:0005503	abnormally monopolar protein localization to cell tip [has_penetrance] high [assayed_protein] PomBase:SPCC1919.10c	(Fig. 1D)
PMID:36202103	FYPO:0005503	abnormally monopolar protein localization to cell tip [has_penetrance] high [assayed_protein] PomBase:SPCC1919.10c	(Fig. 1E)
PMID:36202103	FYPO:0003527	protein mislocalized to cell tip [has_penetrance] high [has_severity] medium [assayed_protein] PomBase:SPAC20G4.02c	(Fig. 1E, F and G)
PMID:36202103	FYPO:0003482	increased punctate cytoplasmic protein localization [has_penetrance] high [has_severity] medium [assayed_protein] PomBase:SPAC20G4.02c	(Fig. 1F and G)
PMID:36202103	FYPO:0003482	increased punctate cytoplasmic protein localization [has_penetrance] high [has_severity] medium [assayed_protein] PomBase:SPAC20G4.02c	(Fig. 1F and G)
PMID:36202103	FYPO:0003527	protein mislocalized to cell tip [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c [has_severity] high	(Fig. 1F and G)
PMID:36202103	FYPO:0003527	protein mislocalized to cell tip [has_penetrance] high [has_severity] medium [assayed_protein] PomBase:SPAC20G4.02c	(Fig. 1F and G)
PMID:36202103	FYPO:0003482	increased punctate cytoplasmic protein localization [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c [has_severity] high	(Fig. 1F and G)
PMID:36202103	FYPO:0003482	increased punctate cytoplasmic protein localization [has_penetrance] high [has_severity] medium [assayed_protein] PomBase:SPAC20G4.02c	(Fig. 1F and G)
PMID:36202103	FYPO:0003482	increased punctate cytoplasmic protein localization [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c [has_severity] low	(Fig. 1F and G)
PMID:36202103	FYPO:0003527	protein mislocalized to cell tip [has_penetrance] high [has_severity] medium [assayed_protein] PomBase:SPAC20G4.02c	(Fig. 1F and G)
PMID:36202103	FYPO:0003527	protein mislocalized to cell tip [has_penetrance] high [has_severity] low [assayed_protein] PomBase:SPAC20G4.02c	(Fig. 1F and G)
PMID:36202103	FYPO:0003482	increased punctate cytoplasmic protein localization [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c [has_severity] low	(Fig. 1F ang G)
PMID:36202103	FYPO:0006098	abnormal protein localization to cytoplasm [assayed_protein] PomBase:SPAC20G4.02c [has_severity] high [has_penetrance] high	(Fig. 1G)
PMID:36202103	FYPO:0008400	exocytic vesicles present in decreased numbers at the fusion focus of mating cells	(Fig. 2)
PMID:36202103	FYPO:0006386	protein abnormally dispersed at shmoo tip [has_penetrance] high [has_severity] medium [assayed_protein] PomBase:SPCC1919.10c	(Fig. 3A)
PMID:36202103	FYPO:0006386	protein abnormally dispersed at shmoo tip [assayed_protein] PomBase:SPAC20G4.02c [has_penetrance] high [has_severity] medium	(Fig. 3A, B, C and D)
PMID:36202103	FYPO:0006505	abolished protein localization to shmoo tip [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c	(Fig. 3D)
PMID:36202103	FYPO:0006386	protein abnormally dispersed at shmoo tip [assayed_protein] PomBase:SPAC20G4.02c [has_penetrance] high [has_severity] high	(Fig. 3D)
PMID:36202103	FYPO:0006386	protein abnormally dispersed at shmoo tip [assayed_protein] PomBase:SPAC20G4.02c [has_penetrance] high [has_severity] high	(Fig. 3D)
PMID:36202103	FYPO:0006386	protein abnormally dispersed at shmoo tip [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c [has_severity] medium	(Fig. 3F and G)
PMID:36202103	FYPO:0006386	protein abnormally dispersed at shmoo tip [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c [has_severity] low	(Fig. 3F and G)
PMID:36202103	FYPO:0006386	protein abnormally dispersed at shmoo tip [has_severity] high [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c	(Fig. 3F and G)
PMID:36202103	FYPO:0006386	protein abnormally dispersed at shmoo tip [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c [has_severity] low	(Fig. 3F and G)
PMID:36202103	FYPO:0006386	protein abnormally dispersed at shmoo tip [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c [has_severity] low	(Fig. 3F and G)
PMID:36202103	FYPO:0008002	cell lysis during mating [has_penetrance] low	(Fig. 3I)
PMID:36202103	FYPO:0008002	cell lysis during mating [has_penetrance] high	(Fig. 3I)
PMID:36202103	FYPO:0000413	abolished cell fusion during mating [has_penetrance] medium	(Fig. 3I)
PMID:36202103	FYPO:0000413	abolished cell fusion during mating [has_penetrance] medium	(Fig. 3I)
PMID:36202103	FYPO:0008002	cell lysis during mating [has_penetrance] medium	(Fig. 3I)
PMID:36202103	FYPO:0000413	abolished cell fusion during mating [has_penetrance] high	(Fig. 3I)
PMID:36202103	FYPO:0000413	abolished cell fusion during mating [has_penetrance] high	(Fig. 4C)
PMID:36202103	FYPO:0000413	abolished cell fusion during mating [has_penetrance] medium	(Fig. 4C)
PMID:36202103	FYPO:0000413	abolished cell fusion during mating [has_penetrance] high	(Fig. 4C)
PMID:36202103	FYPO:0000413	abolished cell fusion during mating [has_penetrance] medium	(Fig. 4C)
PMID:36202103	FYPO:0007095	increased protein localization to actin fusion focus [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c [has_severity] low	(Fig. 4D)
PMID:36202103	FYPO:0007095	increased protein localization to actin fusion focus [has_penetrance] high [has_severity] high [assayed_protein] PomBase:SPAC20G4.02c	(Fig. 4D)
PMID:36202103	FYPO:0007095	increased protein localization to actin fusion focus [has_penetrance] high [has_severity] high [assayed_protein] PomBase:SPAC20G4.02c	(Fig. 4D)
PMID:36202103	FYPO:0008393	normal cell fusion during mating	(Fig. 4E and F)
PMID:36202103	FYPO:0008393	normal cell fusion during mating	(Fig. 4E and F)
PMID:36202103	FYPO:0007094	increased duration of cell fusion during mating [has_severity] low	(Fig. 4F)
PMID:36202103	FYPO:0007096	decreased protein localization to actin fusion focus [has_penetrance] high [has_severity] high [assayed_protein] PomBase:SPCC1919.10c	(Fig. 4H)
PMID:36202103	FYPO:0007096	decreased protein localization to actin fusion focus [has_penetrance] high [has_severity] high [assayed_protein] PomBase:SPCC1919.10c	(Fig. 4H)
PMID:36202103	FYPO:0007096	decreased protein localization to actin fusion focus [has_penetrance] high [has_severity] high [assayed_protein] PomBase:SPAC27F1.02c	(Fig. 4I)
PMID:36202103	FYPO:0007096	decreased protein localization to actin fusion focus [has_penetrance] high [has_severity] high [assayed_protein] PomBase:SPAC27F1.02c	(Fig. 4I)
PMID:36202103	FYPO:0005503	abnormally monopolar protein localization to cell tip [has_penetrance] high [assayed_protein] PomBase:SPAC27F1.02c	(Fig. S1A)
PMID:36202103	FYPO:0005503	abnormally monopolar protein localization to cell tip [has_penetrance] high [assayed_protein] PomBase:SPCC1223.06 [has_severity] medium	(Fig. S1D)
PMID:36202103	FYPO:0005503	abnormally monopolar protein localization to cell tip [has_penetrance] high [assayed_protein] PomBase:SPCC1223.06 [has_severity] high	(Fig. S1D)
PMID:36202103	FYPO:0003532	increased monopolar index [has_severity] high	(Fig. S1E)
PMID:36202103	FYPO:0003532	increased monopolar index [has_severity] medium	(Fig. S1E)
PMID:36202103	FYPO:0006386	protein abnormally dispersed at shmoo tip [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c [has_severity] medium	(Fig. S2)
PMID:36202103	FYPO:0006386	protein abnormally dispersed at shmoo tip [has_penetrance] high [assayed_protein] PomBase:SPAC20G4.02c [has_severity] high	(Fig. S2)
PMID:36202103	FYPO:0005503	abnormally monopolar protein localization to cell tip [has_penetrance] high [assayed_protein] PomBase:SPAC27F1.02c	(Figure S1)
PMID:36259651	FYPO:0006155	increased level of mating gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC32C12.02	When cells were grown in media containing nitrogen sources, some of the nc1669Δ cells underwent mating (followed by meiosis), whereas WT cells never initiated mating (Figure 3B, C)
PMID:36259651	FYPO:0003031	mating without nitrogen starvation	When cells were grown in media containing nitrogen sources, some of the nc1669Δ cells underwent mating (followed by meiosis), whereas WT cells never initiated mating (Figure 3B, C)
PMID:36287824	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic telophase	(comment: Its localization to the ring is dependent on actin (LatA treatment).)
PMID:36287824	FYPO:0005289	actomyosin contractile ring sliding	This result suggests that rings either slid off the center of the cell after assembly or assembled off center in ∆imp2 cells (Figure 1B).
PMID:36302945	FYPO:0002988	sensitive to ammonium	(Figure 1) Cells with leucine auxotrophy (leu1-32 strain) show weak growth on the synthetic medium EMM supplemented with 0.2 mM leucine (Fig. 1B). EMM contains 0.5% NH4Cl
PMID:36302945	FYPO:0002988	sensitive to ammonium	(Figure 3) this phenotype was observed for cat1_delta leu1-32 double mutant.
PMID:36302945	FYPO:0002988	sensitive to ammonium	(Figure 4) In 3.0% NH4Cl medium, the growth speed of both strains became slower after exposure to the high NH4Cl condition for 14 h.
PMID:36302945	FYPO:0001723	ferrichrome absent from cell	data not shown, related data in Figure 2A
PMID:36361590	GO:0030674	protein-macromolecule adaptor activity [part_of] mRNA cis splicing, via spliceosome	(Figure 2)
PMID:36361590	GO:0030674	protein-macromolecule adaptor activity [part_of] mRNA cis splicing, via spliceosome	(Figure 2, 4) These results indicated that the Gih35 helicase is part of the Gih35 and Wdr83 on one side, and as an anchoring protein that allows the binding of the Gpl1-Gih35-Wdr83 complex to the spliceosome on the other side. Gpl1- Gih35-Wdr83 complex, but to associate with the spliceosome, it requires the interaction with Gpl1. Altogether, these findings confirmed the above results of the Y2H assay and provided further support for the hypothesis that Gpl1 functions as a bridging protein for
PMID:36361590	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC20H4.06c [assayed_protein] PomBase:SPBC713.05	(Figure 3)
PMID:36361590	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC20H4.09 [assayed_protein] PomBase:SPAC20H4.06c	(Figure 3)
PMID:36361590	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC20H4.09 [assayed_protein] PomBase:SPAC20H4.06c	(Figure 3)
PMID:36361590	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC20H4.06c [assayed_protein] PomBase:SPBC713.05	(Figure 3)
PMID:36361590	GO:0005681	spliceosomal complex	(comment: Gpl1-Gih35-Wdr83 complex)
PMID:36361590	GO:0005681	spliceosomal complex	(comment: Gpl1-Gih35-Wdr83 complex)
PMID:36361590	GO:0005681	spliceosomal complex	(comment: Gpl1-Gih35-Wdr83 complex)
PMID:36361590	FYPO:0000840	normal RNA level [assayed_transcript] PomBase:SPBC713.05	We detected wdr83 (Figure S1) and performed the Western blot and RT-qPCR analyses. We detected no significant changes in the mRNA levels of gpl1, gih35 or wdr83 in the analyzed mu- no significant changes in the mRNA levels of gpl1, gih35 or wdr83 in the analyzed mutants tants (Figure 5a).
PMID:36408846	FYPO:0005641	abnormal chromosome segregation during meiosis I with premature sister kinetochore separation, lagging chromosomes, and normal chromosome separation	(Fig 3C and D). Indeed, the distribution of the GFP dots revealed aberrant segregation of sister chromatids in MI of clr4F449Y/clr4F449Y cells, with a high frequency of equational segregation that normally occurs during MII (Fig 3D
PMID:36408846	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] ~20	(Fig 3C and D). Indeed, the distribution of the GFP dots revealed aberrant segregation of sister chromatids in MI of clr4F449Y/clr4F449Y cells, with a high frequency of equational segregation that normally occurs during MII (Fig 3D
PMID:36408846	FYPO:0002150	inviable spore population	(Figure 3F)
PMID:36408846	FYPO:0007853	normal protein localization to centromere [assayed_protein] PomBase:SPAC664.01c	(Figure 4A) (This observation indicates that highest binding affinity of Swi6 towards H3 is necessary for proper subnuclear localization in meiocytes, for which H3K9 needs to be tri-methylated.
PMID:36408846	FYPO:0005888	decreased protein localization to centromeric chromatin, with protein mislocalized to nucleoplasm [assayed_protein] PomBase:SPAC664.01c	(Figure 4a)
PMID:36408846	FYPO:0005888	decreased protein localization to centromeric chromatin, with protein mislocalized to nucleoplasm [assayed_protein] PomBase:SPAC664.01c	(Figure 4a)
PMID:36408846	FYPO:0008050	abolished histone H3-K4 methylation during meiosis	(comment: CHECK Check tomorrow should this be tri methylation)
PMID:36408846	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] 20	Consistent with earlier findings, we frequently observed spores with two GFP dots in a single nucleus of a tetrad derived from clr4D/clr4D cells (Fig 3E, green fraction). Such a pattern (i.e., normal segregation during MI but not MII) occurred in < 1% of clr4F449Y/clr4F449Y cells that we have analyzed (Fig 3E)
PMID:36408846	FYPO:0004159	abnormal homologous chromosome segregation [has_penetrance] 10	Furthermore, fewer clr4F449Y/clr4F449Y cells displayed lagging DNA upon expression of Swi6Chp1-like-CD (Fig 4C and D).
PMID:36408846	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC428.08c [part_of] regulation of heterochromatin organization [happens_during] meiosis I/meiosis II transition	Indeed, CDK1/Cyclin B phosphorylated recombinant Clr4 specifically at S458 (Fig 6E).
PMID:36408846	FYPO:0008048	increased histone H3-K4 dimethylation at centromere during meiosis	This revealed reduced H3K9me2, but increased H3K9me3 levels upon 1-NM-PP1 addition in cdk1-as cells specifically (Fig 6F)
PMID:36408846	FYPO:0005577	decreased protein phosphorylation during meiotic cell cycle [assayed_protein] PomBase:SPBC428.08c	Upon inhibition of Cdk1-as, Clr4S458 phosphorylation rapidly decreased and was undetectable 3 h postinhibition, whereas Clr4 phosphorylation levels remained unaffected in cdk1+ cells (Figs 6D and EV5D).
PMID:36408846	FYPO:0008038	abolished histone H3-K4 trimethylation during mitosis	clr4F449Y/clr4F449Y cells displayed strongly elevated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A).
PMID:36408846	FYPO:0008047	decreased histone H3-K4 dimethylation  at centromere during meiosis	clr4F449Y/clr4F449Y cells displayed strongly elevated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A).
PMID:36408846	FYPO:0008052	increased histone H3-K4 dimethylation during mitosis	clr4F449Y/clr4F449Y cells displayed strongly elevated H3K9me2 levels when in mitosis, while H3K9me3 was absent (Figs 2A and EV3A).
PMID:36408846	FYPO:0000278	decreased cell population growth following spore germination	spores formed colonies again (Fig 4G).
PMID:36423630	GO:0042273	ribosomal large subunit biogenesis	(comment: Fkbp39 separates nascent ribosomes from chromatinin cells)
PMID:36423630	GO:0042274	ribosomal small subunit biogenesis	(comment: Fkbp39 separates nascent ribosomes from chromatinin cells)
PMID:36423630	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC1347.02	Although the overall Fkbp39 protein levels are slightly reduced in fkbp41D total lysates (Figure S7E), there was a marked reduction of Fkbp39 localization specifically at 25S rDNA in those cells compared with wild- type (Figures 6A, 6B, and S7F).
PMID:36423630	GO:0000785	chromatin	By contrast, Fkbp41 is found primarily in the insoluble chromatin fraction (Figure S1C).
PMID:36423630	FYPO:0001679	abnormal protein localization to chromatin [assayed_protein] PomBase:SPAC890.04c	By contrast, in fkbp39D cells, we detected Ytm1 on chromatin, primarily at the 30 end of the rDNA repeats, specifically enriched at the 30 ETS and the non-transcribed spacer (NTS) DNA sites (Figures 4A, S5A, and S5B).
PMID:36423630	GO:1902626	assembly of large subunit precursor of preribosome	In state 3, RNA domain III is folded and the biogenesis complex Ytm1-Erb1-Ppp1 (Ytm1-Erb1-Nop7 in S. cerevisiae) is incorporated32 for a total of 30 ribosomal proteins and 15 biogenesis factors (Figure 2A).
PMID:36423630	GO:1902626	assembly of large subunit precursor of preribosome	In state 3, RNA domain III is folded and the biogenesis complex Ytm1-Erb1-Ppp1 (Ytm1-Erb1-Nop7 in S. cerevisiae) is incorporated32 for a total of 30 ribosomal proteins and 15 biogenesis factors (Figure 2A).
PMID:36423630	GO:1902626	assembly of large subunit precursor of preribosome	In state 3, RNA domain III is folded and the biogenesis complex Ytm1-Erb1-Ppp1 (Ytm1-Erb1-Nop7 in S. cerevisiae) is incorporated32 for a total of 30 ribosomal proteins and 15 biogenesis factors (Figure 2A).
PMID:36423630	GO:0031491	nucleosome binding	On the other hand, Fkbp39 could bind to DNA and nucleosomes with a 40-bp-long linker DNA (Figures 1C, S1I, and S1J) but not to nucleosomes lacking or with short 10 bp linker DNA (Figure S2A).
PMID:36423630	GO:0000182	rDNA binding	On the other hand, Fkbp39 could bind to DNA and nucleosomes with a 40-bp-long linker DNA (Figures 1C, S1I, and S1J) but not to nucleosomes lacking or with short 10 bp linker DNA (Figure S2A).
PMID:36423630	GO:0003723	RNA binding	Similarly to human nucleosphosmin,12 Fkbp39 can bind RNA in vitro and phase separate with RNA (Figures S4A and S4B). Fkbp39 robustly forms liquid-like condensates with RNA in sharp contrast to condensates with DNA (Figures S4B and S2D).
PMID:36423630	GO:1902626	assembly of large subunit precursor of preribosome	State 2 has 24 ribosomal proteins but only 9 biogenesis factors, and ITS2 is cleaved and its associated factors are released (Figures 2A and S3D; Table S2).
PMID:36423630	GO:1902626	assembly of large subunit precursor of preribosome	State 2 has 24 ribosomal proteins but only 9 biogenesis factors, and ITS2 is cleaved and its associated factors are released (Figures 2A and S3D; Table S2).
PMID:36423630	GO:1902626	assembly of large subunit precursor of preribosome	State 2 has 24 ribosomal proteins but only 9 biogenesis factors, and ITS2 is cleaved and its associated factors are released (Figures 2A and S3D; Table S2).
PMID:36423630	GO:1902626	assembly of large subunit precursor of preribosome	State 2 has 24 ribosomal proteins but only 9 biogenesis factors, and ITS2 is cleaved and its associated factors are released (Figures 2A and S3D; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0030684	preribosome	The structure of state 1 shows an early assembly intermediate with 23 ribosomal proteins and 19 biogenesis factors (Figure 2A; Table S2).
PMID:36423630	GO:0140693	molecular condensate scaffold activity	This supports the role of histones in promoting heterotypic LLPS of Fkbp39 with DNA (Figures 1D and S2E). These observations suggest that Fkbp39 could organize the rDNA-containing chromatin into a phase-separated compartment.
PMID:36423630	GO:0030874	nucleolar chromatin [coincident_with] cytosolic_rRNA_25S_gene	We found that chromatin-associated Fkbp39 and Fkbp41 predominately localized to the rDNA locus, similar to previous observations on budding yeast and mammalian nucleophosmins,20-23 but our ChIP-seq data also revealed a strong enrichment at the 25S rDNA, which had not been described before (Figures 1A, 1B, and S1D).
PMID:36423630	GO:0030874	nucleolar chromatin [coincident_with] cytosolic_rRNA_25S_gene	We found that chromatin-associated Fkbp39 and Fkbp41 predominately localized to the rDNA locus, similar to previous observations on budding yeast and mammalian nucleophosmins,20-23 but our ChIP-seq data also revealed a strong enrichment at the 25S rDNA, which had not been described before (Figures 1A, 1B, and S1D).
PMID:36423630	GO:0030684	preribosome	We identified 4 major states of nascent 60S, and each state could be further classified into multiple substates (Figures 2A and S3; Table 1). The nascent 60S associated with Fkbp39 represents early ribosome biogenesis stages as described below.
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	GO:0032040	small-subunit processome	We isolated nascent 40S (also known as small subunit processome) by pulling down fibrillarin (Nop1)-associated particles (Figure S4I Table S3; Data S1)
PMID:36423630	FYPO:0004227	decreased nucleosome binding	We mutated the active site of the prolyl isomerase domain of Fkbp39 (F301C/W314C/Y337K)29 and found that it was impaired in the ability to bind nucleosomes but not DNA (Figure S2B).
PMID:36423630	FYPO:0003694	decreased mature 18S rRNA level	reduced levels of 18S and 25S rRNA and accumulation of 50 ETS RNA and unprocessed rRNA in the mutant compared with wild-type cells (Figures S5D and S5E).
PMID:36423630	FYPO:0001137	decreased mature 25S rRNA level	reduced levels of 18S and 25S rRNA and accumulation of 50 ETS RNA and unprocessed rRNA in the mutant compared with wild-type cells (Figures S5D and S5E).
PMID:36435910	FYPO:0009057	decreased rate of microtubule catastrophe involved in meitotic centromere clustering during meiotic prophase I [has_severity] medium	(Figure 2a)
PMID:36435910	FYPO:0009057	decreased rate of microtubule catastrophe involved in meitotic centromere clustering during meiotic prophase I	(Figure 2a)
PMID:36435910	FYPO:0009057	decreased rate of microtubule catastrophe involved in meitotic centromere clustering during meiotic prophase I [has_severity] high	(Figure 2a)
PMID:36435910	FYPO:0009057	decreased rate of microtubule catastrophe involved in meitotic centromere clustering during meiotic prophase I [has_severity] medium	(Figure 2a)
PMID:36435910	GO:0170060	microtubule destabilizing activity [part_of] plus-end specific microtubule depolymerization	(comment: CHECK Evidence: in vitro biochemical assays using purified tubulin and recombinant Dis1 protein / New GO term requested: microtubule destabilization activity)
PMID:36435910	GO:0051010	microtubule plus-end binding [part_of] plus-end specific microtubule depolymerization	(comment: Dis1 uses its TOG domains to induce microtubule catastrophe, in which polymerisation turns into depolymerisation)
PMID:36481249	FYPO:0002151	inviable spore	(Figure 1a)
PMID:36481249	FYPO:0000648	viable small vegetative cell	In contrast, under the same condition, the wat1Δ and wat1-17 mutant cells became shorter in size with a round morphology having an average cell length of 7.7 and 8.3 μm, respectively (Fig. 3A and 3B)
PMID:36481249	FYPO:0000648	viable small vegetative cell	Interestingly, the average cell size of tor-287 mutant cells also decreases from 18.2 μm at 25 ◦C to 7.0 μm at 36 ◦C (Fig. 3A and 3B
PMID:36481249	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1039.09	Real-time quantitative PCR analysis revealed the up-regulation of transcripts of per1 and isp5 genes and down regulation of cat1 gene in wat1Δ, wat1-17, and tor2-287 mutant background at the non-permissive temperature (Fig. 4B)
PMID:36481249	FYPO:0002678	abolished protein phosphorylation [assayed_protein] PomBase:SPAPB1E7.12	The phosphorylation of Psk1 and Rps602 was completely abolished in wat1Δ, wat1-17, and tor2-287 mutants after shifting the cells at non-permissive temperature (Fig. 4A, upper and middle panel).
PMID:36481249	FYPO:0002678	abolished protein phosphorylation [assayed_protein] PomBase:SPCC4G3.08	The phosphorylation of Psk1 and Rps602 was completely abolished in wat1Δ, wat1-17, and tor2-287 mutants after shifting the cells at non-permissive temperature (Fig. 4A, upper and middle panel).
PMID:36481249	FYPO:0005097	abnormal cell cycle arrest in mitotic G1 phase	The tor2-287 mutant cells also showed a similar phenotype after shifting at 36 ◦C (Fig. 3C, upper panel), indicating the G1 arrest.
PMID:36481249	FYPO:0001029	resistance to canavanine	cells were unable to grow on the plates containing canavanine (Fig. 4C). Interestingly, wat1Δ, wat1-17, and tor2-287 mutant cells exhibited resistance to canavanine (Fig. 4C) suggesting that disruption of wat1 leads to inactivation of the TORC1 pathway resulting in the defect in amino acid uptake
PMID:36481249	FYPO:0005097	abnormal cell cycle arrest in mitotic G1 phase	having 1C and 2C DNA peak (Fig. 3C, upper panel) with a majority of cells having 1C DNA peak indicating a G1 arrest while only 2C DNA peak was observed in wild type cells grown under similar conditions
PMID:36481249	FYPO:0001492	viable elongated vegetative cell	wat1Δ and wat1-17 mutant cells were a little elongated with an average size of 18.5 μm (Fig. 3A and 3B).
PMID:36481249	FYPO:0001492	viable elongated vegetative cell	wat1Δ and wat1-17 mutant cells were a little elongated with an average size of 18.5 μm (Fig. 3A and 3B).
PMID:36537249	FYPO:0001375	abolished protein localization [assayed_protein] PomBase:SPBC2D10.16	(comment: CHECK abolished Mhf1 localization)
PMID:36537249	GO:0005515	protein binding	(comment: CHECK binds to Mhf1)
PMID:36537249	GO:0005515	protein binding	(comment: CHECK binds to Mhf2)
PMID:36537249	GO:0000776	kinetochore [exists_during] mitotic prophase	(comment: CHECK mitotic prophase)
PMID:36537249	FYPO:0004318	abolished mitotic spindle assembly checkpoint	As shown in Fig. 1A,B, the percentage of mitotic WT cells displaying Plo1-GFP signals increased over time upon incubation at 16°C and, 8 h after cold treatment, ∼90% of WT cells were arrested at preanaphase presumably due to the activation of the SAC. As Bub1 is a core component of the SAC (Fischer et al., 2021), the absence of Bub1 was expected to abolish the SAC. Consistently, the percentage of mitotic bub1Δ cells remained low (<10%) throughout the period of cold treatment (Fig. 1A,B).
PMID:36537249	FYPO:0005727	decreased rate of deactivation of mitotic spindle assembly checkpoint [has_severity] low	Intriguingly, similar to the percentage of mitotic WT cells, the percentage of mitotic mhf2Δ cells increased over time upon cold treatment, but to a lesser degree (Fig. 1A,B).
PMID:36574843	FYPO:0003482	increased punctate cytoplasmic protein localization [assayed_protein] PomBase:SPCC4B3.15	(Figure 3)
PMID:36574843	FYPO:0003482	increased punctate cytoplasmic protein localization [assayed_protein] PomBase:SPCC18B5.03	(Figure 3)
PMID:36574843	FYPO:0000648	viable small vegetative cell [has_severity] medium [has_penetrance] high	(comment: (vw: did not reduce cell size further) EPISTATIC) Consistent with this prediction, PTet-cdr2 did not reduce cell J. Biol. Chem. (2023) 299(2) 102831 3 Regulation of cell size and Wee1 by elevated levels of Cdr2 size in the temperature-sensitive wee1-50 mutant grown at 36 C (Fig. 2E).
PMID:36574843	GO:0035591	signaling adaptor activity [has_input] PomBase:SPCC18B5.03	(comment: CHECK HYPERPHOSPHORYLATED WEE1 (get identifier))
PMID:36574843	GO:0031569	mitotic G2 cell size control checkpoint signaling	(comment: dosage dependent) (We conclude that increased levels of Cdr2 cause hyperphosphorylation of Wee1 leading to reduced cell size at division.)
PMID:36574843	FYPO:0000648	viable small vegetative cell [has_severity] medium [has_penetrance] high	Addition of Tet to PTet-cdr2 cells caused a marked and significant decrease in cell length at division (Fig. 2, A and B)
PMID:36574843	FYPO:0000648	viable small vegetative cell	However, induction of PTet-cdr2 in cdr1Δ cdr2Δ cells still reduced cell size, whereas PTet-cdr2(E177A) had no effect (Fig. 2, C and D).
PMID:36574843	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	In contrast, Tet-based overexpression of cdr2(E177A) increased the size of dividing cells, consistent with dominant-negative effects for
PMID:36574843	FYPO:0000017	elongated cell	neither Cdr2(1-330) nor Cdr2(1-590) truncations reduced cell size or formed cytoplasmic clusters (Fig. 7, B-D) despite expression of all constructs to similar levels (Fig. S3A).
PMID:36574843	FYPO:0000017	elongated cell	neither Cdr2(1-330) nor Cdr2(1-590) truncations reduced cell size or formed cytoplasmic clusters (Fig. 7, B-D) despite expression of all constructs to similar levels (Fig. S3A).
PMID:36617881	GO:0010964	regulation of regulatory ncRNA-mediated heterochromatin formation	These results suggest that Epe1 promotes assembly of the RNAi machinery at constitutive heterochromatin by expressing dg/dh ncRNAs.
PMID:36626373	GO:0031520	plasma membrane of cell tip [exists_during] cellular response to nitrogen starvation	Thus we found that wild-type Cat1-GFP cells growing in nitrogen-starvation conditions is localised to the plasma membrane, particularly at the growing cell ends, as previously reported [12,26].
PMID:36633091	FYPO:0009002	increased mitochondrial-associated microtubule fraction during mitotic interphase	(Fig. 1A, 1B, S1A)
PMID:36633091	FYPO:0000056	mitochondria fused	(Fig. 1A, 1B, S1A)
PMID:36633091	FYPO:0000895	mitochondrial aggregation	(Fig. 1A, 1B, S1A)
PMID:36633091	FYPO:0002029	abnormal cell division, large and small daughter cells [has_severity] medium	(Fig. 1C, 1D and 1E)
PMID:36633091	FYPO:0002029	abnormal cell division, large and small daughter cells [has_severity] medium	(Fig. 1C, Fig. 1D and Fig. 1E)
PMID:36633091	FYPO:0002029	abnormal cell division, large and small daughter cells [has_severity] high	(Fig. 1C, ID and 1E)
PMID:36633091	FYPO:0009000	decreased rate of cytoplasmic microtubule polymerization during mitotic interphase [has_severity] high	(Fig. 2A and 2B)
PMID:36633091	FYPO:0009001	decreased duration of cytoplasmic microtubule growth events during mitotic interphase [has_severity] high	(Fig. 2A and 2C)
PMID:36633091	FYPO:0003190	decreased rate of cytoplasmic microtubule depolymerization during vegetative growth [has_severity] high	(Fig. 2A and 2C)
PMID:36633091	FYPO:0003190	decreased rate of cytoplasmic microtubule depolymerization during vegetative growth	(Fig. 2C)
PMID:36633091	FYPO:0003194	increased rate of microtubule depolymerization during vegetative growth	(Fig. 2C)
PMID:36633091	FYPO:0008008	increased duration of cytoplasmic microtubule growth events during mitotic interphase [has_severity] high	(Fig. 2D)
PMID:36633091	FYPO:0002071	mislocalized nucleus during vegetative growth	(Fig. 3B)
PMID:36633091	FYPO:0002071	mislocalized nucleus during vegetative growth	(Fig. 3B)
PMID:36633091	FYPO:0002071	mislocalized nucleus during vegetative growth	(Fig. 3B)
PMID:36633091	FYPO:0000906	abnormal mitochondrion inheritance during vegetative growth [has_severity] medium	(Fig. 5C)
PMID:36633091	FYPO:0000907	abolished mitochondrion inheritance during vegetative growth [has_penetrance] low	(Fig. 5C)
PMID:36633091	FYPO:0000907	abolished mitochondrion inheritance during vegetative growth [has_penetrance] low	(Fig. 5C)
PMID:36633091	FYPO:0000906	abnormal mitochondrion inheritance during vegetative growth [has_severity] medium	(Fig. 5C)
PMID:36633091	FYPO:0002029	abnormal cell division, large and small daughter cells [has_severity] high	(Fig. S1D and S1E)
PMID:36633091	FYPO:0002029	abnormal cell division, large and small daughter cells	Supplementary Fig. S1D and S1E
PMID:36650056	FYPO:0000510	abnormal nuclear fusion during mating	(comment: Change to: Nuclear congression without nuclear fusion)
PMID:36650056	FYPO:0000510	abnormal nuclear fusion during mating	(comment: Change to: Nuclear congression without nuclear fusion)
PMID:36650056	FYPO:0000510	abnormal nuclear fusion during mating	(comment: Change to: Nuclear congression without nuclear fusion)
PMID:36650056	MOD:00115	S-palmitoyl-L-cysteine [added_by] PomBase:SPAC2F7.10	(comment: Lower levels in the akr1 mutant)
PMID:36650056	MOD:00115	S-palmitoyl-L-cysteine [added_by] PomBase:SPAC2F7.10	(comment: Lower levels in the akr1 mutant)
PMID:36650056	FYPO:0002505	decreased protein palmitoylation [assayed_protein] PomBase:SPAC13C5.03 [has_severity] high	(comment: akr1Δ affecting tht1)
PMID:36650056	FYPO:0002890	abnormal horsetail nucleus morphology	(comment: change to: twin horsetail nucleus)
PMID:36650056	FYPO:0002890	abnormal horsetail nucleus morphology	(comment: change to: twin horsetail nucleus)
PMID:36650056	FYPO:0002890	abnormal horsetail nucleus morphology	(comment: change to: twin horsetail nucleus)
PMID:36650056	GO:0019706	protein-cysteine S-palmitoyltransferase activity [has_input] PomBase:SPAC13C5.03 [part_of] protein targeting to membrane	(comment: palmitoylation of tht1D is reduced by akr1D)
PMID:36695178	FYPO:0000316	inviable after spore germination [has_penetrance] 90	(comment: Sub-lethal phenotype, with only 10% of expected double mutants recovered.)
PMID:36695178	FYPO:0000252	increased spontaneous diploidization [has_penetrance] high [has_severity] high	(comment: Very high levels of diploidization in minimal medium)
PMID:36695178	FYPO:0001489	inviable vegetative cell [has_penetrance] medium	(comment: Very prominent in minimal medium due to the lack of the Kennedy pathway precursors)
PMID:36695178	FYPO:0000229	cut	(comment: Very prominent in minimal medium due to the lack of the Kennedy pathway precursors)
PMID:36695178	FYPO:0007546	abolished nuclear envelope division [has_penetrance] high [has_severity] high	(comment: Very prominent in minimal medium due to the lack of the Kennedy pathway precursors)
PMID:36695178	FYPO:0006716	large and small daughter nuclei, with unequal nuclear envelope distribution	Severe buckling of the mitotic spindle was observed in 31% of cells, resulting in bowshaped nuclear intermediates during anaphase (Fig. 4D). It took longer for these nuclei to divide, and they often formed daughter nuclei of unequal sizes (Fig. S4E)
PMID:36695178	FYPO:0005721	curved mitotic spindle during anaphase B [has_penetrance] 31	Severe buckling of the mitotic spindle was observed in 31% of cells, resulting in bowshaped nuclear intermediates during anaphase (Fig. 4D). It took longer for these nuclei to divide, and they often formed daughter nuclei of unequal sizes (Fig. S4E)
PMID:36705602	GO:0000940	outer kinetochore [exists_during] mitotic M phase	(Figure 3) summarizes data
PMID:36705602	GO:0000939	inner kinetochore [exists_during] mitotic M phase	(Figure 3) summarizes data
PMID:36705602	GO:0000939	inner kinetochore [exists_during] mitotic M phase	(Figure 3) summarizes data
PMID:36705602	GO:0000939	inner kinetochore [exists_during] mitotic M phase	(Figure 3) summarizes data
PMID:36705602	GO:0000940	outer kinetochore [exists_during] mitotic M phase	(Figure 3) summarizes data
PMID:36705602	GO:0000940	outer kinetochore [exists_during] mitotic M phase	(Figure 3) summarizes data
PMID:36705602	GO:0000940	outer kinetochore [exists_during] mitotic M phase	(Figure 3) summarizes data
PMID:36705602	GO:0000940	outer kinetochore [exists_during] mitotic M phase	(Figure 3) summarizes data
PMID:36705602	GO:0000940	outer kinetochore [exists_during] mitotic M phase	(Figure 3) summarizes data
PMID:36749320	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC20G8.05c [has_severity] high	(Fig. 3E)
PMID:36749320	FYPO:0007393	septum mislocalized to cell tip [has_penetrance] 95	(Fig. 5 S2)
PMID:36749320	FYPO:0007393	septum mislocalized to cell tip [has_penetrance] 20	(Fig. 5 S2)
PMID:36749320	FYPO:0007393	septum mislocalized to cell tip [has_penetrance] 5	(Fig. 5 S2)
PMID:36749320	FYPO:0007393	septum mislocalized to cell tip [has_penetrance] 30	(Fig. 5 S2)
PMID:36749320	FYPO:0007393	septum mislocalized to cell tip [has_penetrance] 30	(Fig. 5 S2)
PMID:36749320	FYPO:0007393	septum mislocalized to cell tip [has_penetrance] 30	(Fig. 5 S2)
PMID:36749320	FYPO:0007393	septum mislocalized to cell tip [has_penetrance] 30	(Fig. 5 S2)
PMID:36749320	FYPO:0007393	septum mislocalized to cell tip [has_penetrance] 20	(Fig. 5 S2)
PMID:36749320	FYPO:0008075	increased protein localization to cell cortex of cell tip during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAC20G8.05c	(Figure 10)
PMID:36749320	FYPO:0008075	increased protein localization to cell cortex of cell tip during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAC926.03	(Figure 10)
PMID:36749320	FYPO:0009059	increased protein localization to cell cortex during vegetative growth [has_severity] high [assayed_protein] PomBase:SPBC83.18c	(Figure 10)
PMID:36749320	FYPO:0009059	increased protein localization to cell cortex during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAC926.03	(Figure 10)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] high [assayed_protein] PomBase:SPAC20G8.05c	(Figure 10) (comment: Manu: transfer to FYPO:0008075)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] high [assayed_protein] PomBase:SPAC20G8.05c	(Figure 10) (comment: Manu: transfer to FYPO:0008075)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC1604.14c	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC1604.14c	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC1604.14c	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC1604.14c	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC1604.14c	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC17G8.14c	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC4F6.06	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC1604.14c	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC4F6.06	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC1604.14c	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC4F6.06	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC1604.14c	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC1604.14c	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC4F6.06	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC1604.14c	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC4F6.06	(Figure 3)
PMID:36749320	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC1604.14c	(Figure 3)
PMID:36749320	FYPO:0006186	increased rate of actomyosin contractile ring assembly [has_severity] medium	(Figure 4)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] low [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] high [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] high [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] high [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] high [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] low [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] medium [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] low [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] high [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] medium [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] high [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] low [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] low [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] high [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] low [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] medium [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] high [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] medium [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] medium [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] medium [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5A)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] low [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5B)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] medium [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5C)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] medium [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5C)
PMID:36749320	FYPO:0009061	increased protein localization to cell cortex during mitotic interphase [has_severity] high [assayed_protein] PomBase:SPAC20G8.05c	(Figure 5C)
PMID:36779416	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 1A, B)
PMID:36779416	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.12c	(comment: phosphate replete) Zfs1 is involved in the repression of the ecl3+ transcript level in a nutrient-rich environment but is not required for the induction by phosphate starvation.
PMID:36779416	FYPO:0004416	decreased RNA level during cellular response to phosphate starvation [has_severity] high [assayed_transcript] PomBase:SPBC8E4.12c	Phosphate starvation did not induce ecl3+ expression in Δckb1 cells, indicating that the induction was dependent on Ckb1 (Fig. 2B)
PMID:36779416	FYPO:0004416	decreased RNA level during cellular response to phosphate starvation [has_severity] high [assayed_transcript] PomBase:SPBC8E4.12c	non detectable Fig. 1. Phosphate starvation induces ecl3+ expression in a pho7+-dependent manner.
PMID:36779416	FYPO:0004416	decreased RNA level during cellular response to phosphate starvation [has_severity] high [assayed_transcript] PomBase:SPBC8E4.01c	non detectable Fig. 1. Phosphate starvation induces ecl3+ expression in a pho7+-dependent manner.
PMID:36779416	FYPO:0004416	decreased RNA level during cellular response to phosphate starvation [has_severity] high [assayed_transcript] PomBase:SPBP4G3.02	non detectable Fig. 1. Phosphate starvation induces ecl3+ expression in a pho7+-dependent manner.
PMID:36793083	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3)
PMID:36793083	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 3)
PMID:36793083	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 3)
PMID:36793083	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3)
PMID:36793083	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3)
PMID:36793083	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3)
PMID:36793083	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3)
PMID:36793083	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3)
PMID:36793083	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 3)
PMID:36793083	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3)
PMID:36793083	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3)
PMID:36793083	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3)
PMID:36793083	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 3)
PMID:36793083	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 3)
PMID:36793083	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC20F10.04c [assayed_region] PomBase:SPAC1B3.16c	(Fig. 4D)
PMID:36793083	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC20F10.04c [assayed_region] PomBase:SPAC328.10c	(Fig. 4D)
PMID:36793083	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC20F10.04c [assayed_region] PomBase:SPAC328.10c	(Fig. 4D)
PMID:36793083	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC20F10.04c [assayed_region] PomBase:SPCC364.07	(Fig. 4D)
PMID:36793083	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC20F10.04c [assayed_region] PomBase:SPCC417.08	(Fig. 4D)
PMID:36793083	FYPO:0004032	increased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC20F10.04c	(Fig. 4D)
PMID:36793083	FYPO:0000451	increased protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPBC20F10.04c	(Fig. 4D)
PMID:36793083	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC20F10.04c [assayed_region] PomBase:SPAC1B3.16c	(Fig. 4D)
PMID:36793083	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC20F10.04c	(Fig. 4D)
PMID:36794724	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation [assayed_enzyme] PomBase:SPBP4G3.02	(Figure 1B)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure 2)
PMID:36794724	PomGeneEx:0000012	RNA level decreased [during] cellular response to phosphate starvation [in_presence_of] cycloheximide	(Figure 3A)
PMID:36794724	PomGeneEx:0000012	RNA level decreased [during] cellular response to phosphate starvation [in_presence_of] cycloheximide	(Figure 3B)
PMID:36794724	PomGeneEx:0000012	RNA level decreased [during] cellular response to phosphate starvation [in_presence_of] cycloheximide	(Figure 3C)
PMID:36794724	FYPO:0008123	loss  of viability in stationary phase upon phosphate starvation	(Figure 5B)
PMID:36794724	FYPO:0008119	normal morphology during phosphate starvation	(Figure 5D,G)
PMID:36794724	FYPO:0008100	increased polyadenylated 5S rRNA level during cellular response to phosphate starvation [assayed_transcript] PomBase:SPRRNA.38	(Figure 6)
PMID:36794724	FYPO:0008100	increased polyadenylated 5S rRNA level during cellular response to phosphate starvation [assayed_transcript] PomBase:SPRRNA.53	(Figure 6)
PMID:36794724	FYPO:0008100	increased polyadenylated 5S rRNA level during cellular response to phosphate starvation [assayed_transcript] PomBase:SPRRNA.24	(Figure 6)
PMID:36794724	FYPO:0008100	increased polyadenylated 5S rRNA level during cellular response to phosphate starvation [assayed_transcript] PomBase:SPRRNA.05	(Figure 6)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPCTRNAHIS.03	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPCTRNAPHE.04	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPATRNAALA.06	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPATRNAARG.01	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPATRNAARG.03	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPATRNACYS.01	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPATRNAILE.01	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPBTRNAASN.04	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPCTRNAASN.05	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPCTRNAGLY.12	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPBTRNAASN.02	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPBTRNAASN.01	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPATRNATHR.03	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPATRNAPRO.02	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPCTRNATHR.10	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPATRNAVAL.01	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPATRNATYR.01	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPATRNAPHE.01	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPATRNATHR.04	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPATRNAMET.02	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPBTRNAGLN.02	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPBTRNAGLY.04	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPBTRNAGLY.09	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPBTRNAHIS.01	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPBTRNAMET.05	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPBTRNAMET.06	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPBTRNAPRO.07	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPBTRNATHR.06	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPBTRNATRP.02	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPBTRNATRP.03	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPCTRNAALA.12	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0001555	formation of abnormal tRNA processing intermediates [assayed_transcript] PomBase:SPCTRNAARG.10	(Figure 6, 7, 9 and 10)
PMID:36794724	FYPO:0008102	increased tRNA level during cellular response to phosphate starvation	(Figure 8)
PMID:36794724	PomGeneEx:0000012	RNA level decreased [during] cellular response to phosphate starvation	(Figure S3)
PMID:36794724	PomGeneEx:0000012	RNA level decreased [during] cellular response to phosphate starvation	(Figure S3)
PMID:36794724	PomGeneEx:0000012	RNA level decreased [during] cellular response to phosphate starvation	(Figure S3)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36794724	PomGeneEx:0000011	RNA level increased [during] cellular response to phosphate starvation	(Figure S4)
PMID:36799444	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPAC589.12	(Fig. 2D)
PMID:36799444	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPBC26H8.03	Finally, we examined whether Lem2 affected their subcellular localization. GFP-Cho2, GFP-Ole1 and Erg11-GFP were localized in the cortical ER and NE (or perinuclear ER), and deletion of the lem2+ gene did not affect the localization (Fig. 2B), indicating that Lem2 is not necessary for their NE localization
PMID:36799444	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPCC1281.06c	Finally, we examined whether Lem2 affected their subcellular localization. GFP-Cho2, GFP-Ole1 and Erg11-GFP were localized in the cortical ER and NE (or perinuclear ER), and deletion of the lem2+ gene did not affect the localization (Fig. 2B), indicating that Lem2 is not necessary for their NE localization
PMID:36799444	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPAC13A11.02c	Finally, we examined whether Lem2 affected their subcellular localization. GFP-Cho2, GFP-Ole1 and Erg11-GFP were localized in the cortical ER and NE (or perinuclear ER), and deletion of the lem2+ gene did not affect the localization (Fig. 2B), indicating that Lem2 is not necessary for their NE localization
PMID:36799444	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC18G6.10 [assayed_protein] PomBase:SPAC13A11.02c	We performed an IP-WB experiment on the bqt4Δ background (‘bqt4Δ’ in Fig. 2A). Deletion of bqt4+ did not affect these interactions, indicating that Cho2, Ole1 and Erg11 interact with Lem2 independent of Bqt4.
PMID:36799444	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC18G6.10 [assayed_protein] PomBase:SPCC1281.06c	We performed an IP-WB experiment on the bqt4Δ background (‘bqt4Δ’ in Fig. 2A). Deletion of bqt4+ did not affect these interactions, indicating that Cho2, Ole1 and Erg11 interact with Lem2 independent of Bqt4.
PMID:36799444	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC18G6.10 [assayed_protein] PomBase:SPBC26H8.03	We performed an IP-WB experiment on the bqt4Δ background (‘bqt4Δ’ in Fig. 2A). Deletion of bqt4+ did not affect these interactions, indicating that Cho2, Ole1 and Erg11 interact with Lem2 independent of Bqt4.
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC186.04c	(Fig. 2)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC186.04c	(Fig. 2)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC186.05c	(Fig. 2)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC186.05c	(Fig. 2)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC186.05c	(Fig. 2)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC186.06	(Fig. 2)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC186.06	(Fig. 2)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC186.06	(Fig. 2)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC186.04c	(Fig. 2)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1711.15c	(Table 1)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC186.05c	(Table 1)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC186.06	(Table 1)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC750.01	(Table 1)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC186.04c	(Table 1)
PMID:36820394	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1223.13	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC16E9.16c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1289.14	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC794.04c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPACUNK4.17	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB21E7.01c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC336.08	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC16A3.08c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC15E1.02c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC354.12	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC27D7.03c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC21C3.19	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAP8A3.04c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1235.14	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC637.03	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC725.10	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC23G7.13c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC13G7.02c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC660.06	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC794.09c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC23H3.15c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC794.01c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB8B6.04c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC737.04	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC839.15c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC22A12.17c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC26H5.09c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC24C6.09c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC23A1.10	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1039.09	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC338.12	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1815.01	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC29B5.02c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC26F1.14c	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1805.10	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC186.01	(Table 1)
PMID:36820394	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1020.06c	(Table 1)
PMID:36854376	FYPO:0008215	resistance to Rho GTPase inhibitor O1	(comment: ...decreased the average population cell length from 12 µm to 10.3 µm in the wild-type strain after incubation for 6 h at 29°C whereas no such decrease by O1 was observed in the rho1-A62T strain, where average cell size is 12.3 µm in the DMSO control and 11.8 µm in the presence of O1 (Figure 2c).)
PMID:36854376	FYPO:0001357	normal vegetative cell population growth	(comment: The mutant strain appears to grow normally) (Figure 2b).
PMID:36882296	FYPO:0001355	decreased vegetative cell population growth	(Fig. 10A)
PMID:36882296	FYPO:0001355	decreased vegetative cell population growth	(Fig. 10A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 10A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 10A)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 10B)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 11A)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 11B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 11B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 11B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 11B)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 12A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 12A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 12A)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 12B)
PMID:36882296	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 12B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] medium	(Fig. 13)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] medium	(Fig. 13)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 13)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] medium	(Fig. 13)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] medium	(Fig. 13)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 1A)
PMID:36882296	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 1A)
PMID:36882296	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 1A)
PMID:36882296	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 1A)
PMID:36882296	FYPO:0002061	inviable vegetative cell population	(Fig. 1A)
PMID:36882296	FYPO:0002061	inviable vegetative cell population	(Fig. 1A)
PMID:36882296	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 1A) Redundancy with rpb1-T4A
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1B)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1712 [has_severity] high	(Fig. 3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 3)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] low	(Fig. 4)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] low	(Fig. 4)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 5A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 5A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 5A)
PMID:36882296	FYPO:0002061	inviable vegetative cell population	(Fig. 5A)
PMID:36882296	FYPO:0002061	inviable vegetative cell population	(Fig. 5A)
PMID:36882296	FYPO:0002061	inviable vegetative cell population	(Fig. 5A)
PMID:36882296	FYPO:0002061	inviable vegetative cell population	(Fig. 5A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 5A)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:36882296	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 6A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 6A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 6A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 6A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 6A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 6A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 6A, 10A)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 7A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 7A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 7A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 7A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 7A)
PMID:36882296	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	(Fig. 7A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 7A)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:36882296	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B, 10B, 12B)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 8A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. 8A)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 8B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 8B)
PMID:36882296	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 9A)
PMID:36882296	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 9A)
PMID:36882296	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 9A)
PMID:36882296	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 9A)
PMID:36882296	FYPO:0001357	normal vegetative cell population growth	(Fig. 9A)
PMID:36882296	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 9A)
PMID:36882296	FYPO:0001355	decreased vegetative cell population growth	(Fig. 9A)
PMID:36882296	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 9A)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 9B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 9B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 9B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 9B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 9B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 9B)
PMID:36882296	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 9B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 9B)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC24C9.15c	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC36.03c	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC26H8.11c	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC330.21	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC364.06	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC25B2.08	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1884.01	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1289.16c	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC216.02	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC947.04	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.12c	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB2B2.06c	(Fig. S3)
PMID:36882296	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	(Fig. S3)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.08c	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC4F6.09	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB21E7.01c	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC21E11.04	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC11D3.19	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC26H5.09c	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC13G7.02c	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC19C2.04c	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC637.03	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC21C3.19	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.07c	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC15E1.02c	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB21E7.07	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC106.02c	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC70.12c	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC26F1.05	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPACUNK4.17	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1F7.07c	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC2G2.04c	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAP8A3.04c	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1235.14	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC70.08c	(Fig. S4)
PMID:36882296	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC23G7.13c	(Fig. S4)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. S5A)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] medium	(Fig. S5B)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. S6A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. S6A)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S6B)
PMID:36882296	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S6B)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. S7A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. S7A)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Fig. S7A)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S7B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S7B)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S7B)
PMID:36882296	FYPO:0001355	decreased vegetative cell population growth	(Fig. S8)
PMID:36882296	FYPO:0002061	inviable vegetative cell population	(Fig. S8)
PMID:36882296	FYPO:0002061	inviable vegetative cell population	(Fig. S8)
PMID:36882296	FYPO:0002061	inviable vegetative cell population	(Fig. S8)
PMID:36882296	FYPO:0002061	inviable vegetative cell population	(Fig. S8)
PMID:36882296	FYPO:0001355	decreased vegetative cell population growth	(Fig. S8)
PMID:36882296	FYPO:0001355	decreased vegetative cell population growth	(Fig. S8)
PMID:36882296	FYPO:0001355	decreased vegetative cell population growth	(Fig. S8)
PMID:36882296	FYPO:0001355	decreased vegetative cell population growth	(Fig. S8)
PMID:36882296	FYPO:0001355	decreased vegetative cell population growth	(Fig. S8)
PMID:36882296	FYPO:0001355	decreased vegetative cell population growth	(Fig. S8)
PMID:36882296	FYPO:0001355	decreased vegetative cell population growth	(Fig. S8)
PMID:36882296	FYPO:0002085	normal vegetative cell growth	(Figs. 1A, 5A, 6A, 7A, 8A)
PMID:36882296	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Figs. 1B, 5B, 6B, 7B, 8B, 9B, 10B)
PMID:36951094	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC1142.03c [assayed_protein] PomBase:SPAC664.01c	(Fig. 2A)
PMID:36951094	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1142.03c [assayed_protein] PomBase:SPAC664.01c	(Fig. 2A)
PMID:36951094	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC1142.03c [assayed_protein] PomBase:SPAC664.01c	(Fig. 2D)
PMID:36951094	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC1142.03c [assayed_protein] PomBase:SPAC664.01c	(Fig. 2D)
PMID:36951094	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC1142.03c [assayed_protein] PomBase:SPAC664.01c	(Fig. 2D)
PMID:36951094	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1142.03c [assayed_protein] PomBase:SPAC664.01c	(Fig. 2D)
PMID:36951094	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1142.03c [assayed_protein] PomBase:SPAC664.01c	(Fig. 2D)
PMID:36951094	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1142.03c [assayed_protein] PomBase:SPAC664.01c	(Fig. 2D)
PMID:36951094	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC1142.03c [assayed_protein] PomBase:SPAC664.01c	(Fig. 2D)
PMID:36951094	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC1142.03c [assayed_protein] PomBase:SPAC664.01c	(Fig. 2D)
PMID:36951094	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC1142.03c [assayed_protein] PomBase:SPAC664.01c	(Fig. 2D)
PMID:36951094	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC1142.03c [assayed_protein] PomBase:SPAC664.01c	(Fig. 2D)
PMID:36951094	FYPO:0005018	decreased double-stranded DNA binding [assayed_protein] PomBase:SPAC1142.03c [has_severity] low [assayed_region] mating_type_region	(Fig. 3C)
PMID:36951094	FYPO:0005018	decreased double-stranded DNA binding [assayed_protein] PomBase:SPAC1142.03c [has_severity] high [assayed_region] mating_type_region	(Fig. 3C)
PMID:36951094	FYPO:0005018	decreased double-stranded DNA binding [assayed_protein] PomBase:SPAC1142.03c [has_severity] low [assayed_region] mating_type_region	(Fig. 3C)
PMID:36951094	FYPO:0000468	abnormal mating type switching [has_severity] high	(Fig. 5B and 5C)
PMID:36951094	FYPO:0000468	abnormal mating type switching [has_severity] medium	(Fig. 5B and 5C)
PMID:36951094	FYPO:0000468	abnormal mating type switching	(Fig. 5B)
PMID:36951094	FYPO:0000468	abnormal mating type switching	(Fig. 5B)
PMID:36951094	FYPO:0000468	abnormal mating type switching [has_severity] low	(Fig. 5C)
PMID:36951094	FYPO:0000468	abnormal mating type switching [has_severity] high	(Fig. 5C)
PMID:36951094	FYPO:0000468	abnormal mating type switching [has_severity] medium	(Fig. 5C)
PMID:36951094	FYPO:0000468	abnormal mating type switching [has_severity] low	(Fig. 5C)
PMID:36951094	FYPO:0000468	abnormal mating type switching [has_severity] low	(Fig. 5C)
PMID:36951094	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC1142.03c	(Fig. 6A)
PMID:36951094	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC1142.03c	(Fig. 6A)
PMID:36951094	FYPO:0000468	abnormal mating type switching [has_severity] low	(Fig. 6C)
PMID:36951094	FYPO:0000468	abnormal mating type switching [has_severity] medium	(Fig. 6C)
PMID:36951094	FYPO:0000468	abnormal mating type switching [has_severity] high	(Fig. 6C)
PMID:36951094	GO:0007534	gene conversion at mating-type locus	Rad54 further stimulates the activation of strand invasion of Rad51 by the Swi2-Swi5 complex.
PMID:36951094	GO:1990837	sequence-specific double-stranded DNA binding [occurs_in] mating_type_region [part_of] donor selection	the AT-hook motifs were required for the mat3-M donor choice.
PMID:36951094	GO:0140463	chromatin-protein adaptor activity [part_of] donor selection [has_input] PomBase:SPAC1142.03c	the Swi6-binding site was required for the mat2-P donor choice
PMID:36951094	GO:0007534	gene conversion at mating-type locus	we demonstrated that the Swi2-Swi5 complex promotes Rad51-driven strand invasion in vitro
PMID:36951094	GO:0007534	gene conversion at mating-type locus	we demonstrated that the Swi2-Swi5 complex promotes Rad51-driven strand invasion in vitro
PMID:36951094	GO:0007535	donor selection	we demonstrated that the Swi2-Swi5 complex promotes Rad51-driven strand invasion in vitro
PMID:37039135	FYPO:0007829	premature protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. 3)
PMID:37039135	FYPO:0007829	premature protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. 4)
PMID:37039135	FYPO:0006008	normal onset of protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. 4)
PMID:37039135	FYPO:0001357	normal vegetative cell population growth	(Fig. 5A)
PMID:37039135	FYPO:0001357	normal vegetative cell population growth	(Fig. 5A)
PMID:37039135	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 5A)
PMID:37039135	FYPO:0001357	normal vegetative cell population growth	(Fig. 5A)
PMID:37039135	FYPO:0001357	normal vegetative cell population growth	(Fig. 5A)
PMID:37039135	FYPO:0006008	normal onset of protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. 5D)
PMID:37039135	FYPO:0007829	premature protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. 5D)
PMID:37039135	FYPO:0003946	delayed onset of protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. 6)
PMID:37039135	FYPO:0006008	normal onset of protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. 6)
PMID:37039135	FYPO:0006008	normal onset of protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. 6D)
PMID:37039135	FYPO:0007829	premature protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. 6D)
PMID:37039135	FYPO:0006008	normal onset of protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. 6D,S7F)
PMID:37039135	FYPO:0007829	premature protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. 6D,S7F)
PMID:37039135	FYPO:0006008	normal onset of protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. 7)
PMID:37039135	FYPO:0003250	premature septum assembly	(Fig. 7)
PMID:37039135	FYPO:0006008	normal onset of protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. S4)
PMID:37039135	FYPO:0006008	normal onset of protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. S4)
PMID:37039135	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_protein] rho1/GTP+	(Fig. S4A)
PMID:37039135	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. S4A)
PMID:37039135	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_protein] rho1/GTP+	(Fig. S4A)
PMID:37039135	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. S4A)
PMID:37039135	FYPO:0001880	abolished protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. S5)
PMID:37039135	FYPO:0001880	abolished protein localization to cell division site [assayed_protein] rho1/GTP+	(Fig. S5)
PMID:37039135	FYPO:0006008	normal onset of protein localization to cell division site [assayed_protein] PomBase:SPCC645.06c	(Fig. S7C)
PMID:37039135	FYPO:0006008	normal onset of protein localization to cell division site [assayed_protein] PomBase:SPCC645.07	(Fig. S7D)
PMID:37039135	FYPO:0006008	normal onset of protein localization to cell division site [assayed_protein] rho1/GTP+	However, early RBD-mNG localization at the division site observed in gef1Δ cells was rescued upon pak1OE, restoring it to late anaphase (Fig. S6A, B).
PMID:37039135	FYPO:0006008	normal onset of protein localization to cell division site [assayed_protein] rho1/GTP+	However, early RBD-mNG localization at the division site observed in gef1Δ cells was rescued upon pak1OE, restoring it to late anaphase (Fig. S6A, B).
PMID:37039135	GO:0032153	cell division site [exists_during] mitotic anaphase	we found that in most cells, Rgf1- GFP and Rgf3-eGFP was localized to the division site at early stages in anaphase (Fig. S3D,E).
PMID:37039135	GO:0032153	cell division site [exists_during] mitotic anaphase	we found that in most cells, Rgf1- GFP and Rgf3-eGFP was localized to the division site at early stages in anaphase (Fig. S3D,E).
PMID:37039135	GO:0032153	cell division site [exists_during] mitotic anaphase	we found that the Rho probe RBD-tdTomato localized to the division site in late anaphase, immediately preceding the onset of ring constriction and septum ingression. Fig. 2
PMID:37039135	GO:0032153	cell division site [exists_during] mitotic anaphase	we observed Cdc42 activation in early anaphase, at the time of ring assembly. Fig. 2
PMID:37052630	FYPO:0000069	resistance to thiabendazole [has_severity] medium	(Fig. 2b)
PMID:37052630	FYPO:0000069	resistance to thiabendazole [has_severity] low	(Fig. 2b)
PMID:37052630	FYPO:0000069	resistance to thiabendazole [has_severity] low	(Fig. 2b)
PMID:37052630	FYPO:0000069	resistance to thiabendazole [has_severity] low	(Fig. 2b)
PMID:37052630	FYPO:0000069	resistance to thiabendazole [has_severity] medium	(Fig. 2b)
PMID:37052630	FYPO:0000069	resistance to thiabendazole [has_severity] low	(Fig. 2b)
PMID:37052630	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. 2b) (comment: control)
PMID:37052630	FYPO:0000107	sensitive to latrunculin A [has_severity] medium	(Fig. S1)
PMID:37052630	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	(Fig. S1)
PMID:37052630	FYPO:0000098	sensitive to calcium [has_severity] medium	(Fig. S1)
PMID:37052630	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	Main text Table S1
PMID:37052630	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	Main text Table S1
PMID:37052630	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	Main text Table S1
PMID:37052630	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	Main text Table S1
PMID:37052630	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	Main text Table S1
PMID:37076472	GO:0033698	Rpd3L complex	(Figure 1)
PMID:37076472	GO:0033698	Rpd3L complex	(Figure 1)
PMID:37076472	GO:0033698	Rpd3L complex	(Figure 1)
PMID:37076472	GO:0033698	Rpd3L complex	(Figure 1)
PMID:37076472	GO:0033698	Rpd3L complex	(Figure 1)
PMID:37076472	GO:0033698	Rpd3L complex	(Figure 1)
PMID:37076472	GO:0033698	Rpd3L complex	(Figure 1)
PMID:37076472	GO:0033698	Rpd3L complex	(Figure 1)
PMID:37076472	GO:0033698	Rpd3L complex	(Figure 1)
PMID:37076472	GO:0032221	Rpd3S complex	(Figure 3)
PMID:37076472	GO:0032221	Rpd3S complex	(Figure 3)
PMID:37076472	GO:0032221	Rpd3S complex	(Figure 3)
PMID:37076472	GO:0032221	Rpd3S complex	(Figure 3)
PMID:37076472	GO:0032221	Rpd3S complex	(Figure 3)
PMID:37076472	GO:0032221	Rpd3S complex	(Figure 3)
PMID:37099380	FYPO:0009106	nucleus mislocalized towards cell equator during mitotic telophase	(comment: Closer to ring)
PMID:37099380	FYPO:0006338	nucleus mislocalized towards cell tip during mitotic telophase	(comment: Closer to ring)
PMID:37099380	FYPO:0006338	nucleus mislocalized towards cell tip during mitotic telophase	(comment: Closer to ring)
PMID:37120429	FYPO:0002061	inviable vegetative cell population	Sz. pombe cells expressing SpHsp90-EA had an osmolyte-remediated temperature sensitivity phenotype, which strongly suggested conservation of EA-specific phenotypes (Fig. 3b).
PMID:37120429	FYPO:0001357	normal vegetative cell population growth	Sz. pombe cells expressing SpHsp90-EA had an osmolyte-remediated temperature sensitivity phenotype, which strongly suggested conservation of EA-specific phenotypes (Fig. 3b).
PMID:37120429	FYPO:0001234	slow vegetative cell population growth	The suppressive effect of TA and EK on EA defects in non-essential functions were not specific to S. cerevisiae, as these mutations also rescued SpHsp90-EA mediated temperature sensitivity in Sz. pombe (Fig. 5d).
PMID:37120429	FYPO:0001234	slow vegetative cell population growth	The suppressive effect of TA and EK on EA defects in non-essential functions were not specific to S. cerevisiae, as these mutations also rescued SpHsp90-EA mediated temperature sensitivity in Sz. pombe (Fig. 5d).
PMID:37120429	FYPO:0002060	viable vegetative cell population	Using this system, we observed that SpHsp90-EA supported viability of Sz. pombe cells (Fig. 1b).
PMID:37128864	GO:0140602	nucleolar peripheral inclusion body	(comment: Localization depends on Cdc2 kinase activity but not on Clp1)
PMID:37128864	FYPO:0001187	decreased cell density in stationary phase [has_severity] low	(comment: The phenotype can be seen at 32 degree.)
PMID:37128864	FYPO:0007517	increased chromatin mobility [has_severity] medium	(comment: The phenotype can be seen at 32˚C. The phenotype can be seen at 32˚C.) Furthermore, the log phase chromosomes more actively fluctuated in cdc2-L7 cells than in WT cells, and despite a repression in chromosome fluctuation, fluctuation was still elevated in the stationary phase, as demonstrated by an upward shift of the cdc2-L7 MSD plot of the ade6 locus and a complete lack of an overlap of their 95% confidence intervals with those of the WT plot (Fig. 5H).
PMID:37128864	FYPO:0003160	elongated cell during stationary phase [has_severity] low	Cell length increases during log and stationary phases at 32 degree.
PMID:37128864	FYPO:0000245	loss of viability in stationary phase [has_severity] medium	Loss of viability is evident only when cells are exposed to 32 degree before and upon entry into stationary phase.
PMID:37128864	FYPO:0008106	increased cell size during stationary phase [has_severity] medium	The N/C ratio was also reduced but not significantly different from that of stationary phase cells (Fig. 1E; Fig. S1G), suggesting that the observed nuclear size differences from stationary phase originate from the cell size differences.
PMID:37156397	FYPO:0000037	growth auxotrophic for cysteine [has_severity] high	(Fig. 2A) By contrast, the ∆coq12 strain showed almost no growth on PMLU medium containing cysteine.
PMID:37156397	FYPO:0001413	increased cellular sulfide level [has_severity] high	(Fig. 4) The results revealed higher sulfide levels in both Δcoq11 and Δcoq12 strains
PMID:37156397	FYPO:0001413	increased cellular sulfide level	(Fig. 4) The results revealed higher sulfide levels in both Δcoq11 and Δcoq12 strains
PMID:37156397	FYPO:0000037	growth auxotrophic for cysteine [has_severity] high	(Figs. 2A, S1A) Like other mutants lacking CoQ, the ∆coq11 strain showed better growth on cysteine-containing medium.
PMID:37156397	FYPO:0002061	inviable vegetative cell population	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	inviable vegetative cell population	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	inviable vegetative cell population	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	inviable vegetative cell population	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	inviable vegetative cell population	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	inviable vegetative cell population	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	inviable vegetative cell population	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	inviable vegetative cell population	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	inviable vegetative cell population	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	inviable vegetative cell population	(Figs. 2B, S1B)
PMID:37156397	FYPO:0002061	inviable vegetative cell population	(Figs. 2B, S1B)
PMID:37156397	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Figs. 3, S1C) Similar to the Δcoq2 (ppt1) strain, the Δcoq11 and Δcoq12 strains grew more slowly in the presence of 1 and 2 mM hydrogen peroxide or 0.5 mM CuSO4 than in its absence
PMID:37156397	FYPO:0000103	sensitive to copper	(Figs. 3, S1C) Similar to the Δcoq2 (ppt1) strain, the Δcoq11 and Δcoq12 strains grew more slowly in the presence of 1 and 2 mM hydrogen peroxide or 0.5 mM CuSO4 than in its absence
PMID:37156397	FYPO:0000103	sensitive to copper [has_severity] high	(Figs. 3, S1C) Similar to the Δcoq2 (ppt1) strain, the Δcoq11 and Δcoq12 strains grew more slowly in the presence of 1 and 2 mM hydrogen peroxide or 0.5 mM CuSO4 than in its absence
PMID:37156397	FYPO:0000087	sensitive to hydrogen peroxide	(Figs. 3, S1C) Similar to the Δcoq2 (ppt1) strain, the Δcoq11 and Δcoq12 strains grew more slowly in the presence of 1 and 2 mM hydrogen peroxide or 0.5 mM CuSO4 than in its absence
PMID:37156397	GO:0005739	mitochondrion	(comment: LC-MS)
PMID:37156397	GO:0005739	mitochondrion	(comment: LC-MS)
PMID:37156397	GO:0006744	ubiquinone biosynthetic process	(comment: low CoQ10 level)
PMID:37156397	GO:0006744	ubiquinone biosynthetic process	(comment: low CoQ10 level)
PMID:37156397	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	FYPO:0006978	decreased cellular coenzyme Q10 level [has_severity] medium	As a result, we obtained 42 strains in which the CoQ10 content was lower than half that of the wild-type (WT) strain. The 10 mutants with the lowest CoQ10 levels are listed in Table 1
PMID:37156397	GO:0005739	mitochondrion	Coq12-GFP fusion (Fig. 8A). The GFP fluorescence pattern was similar to that of Mitotracker Red, a mitochondria stain. Mitochondrial localization of Coq12 was therefore confirmed
PMID:37156397	GO:0036382	flavin reductase (NADH) activity [part_of] ubiquinone biosynthetic process	Interestingly, NAD+ reduction activity was clearly detected in purified Coq12-8xHis from S. pombe (Fig. 9A)
PMID:37156397	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPAC1687.12c	The amount of Coq4 was significantly reduced in ∆coq11 and ∆coq12 single mutants
PMID:37156397	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPAC1687.12c [has_severity] medium	The amount of Coq4 was significantly reduced in ∆coq11 and ∆coq12 single mutants
PMID:37156397	FYPO:0001355	decreased vegetative cell population growth	We first noticed that ∆coq11 and ∆coq12 strains did not grow well on minimal medium, as was observed for CoQ-deficient S. pombe (Fig. 2A, S1A)
PMID:37158439	FYPO:0008090	normal onset of mitotic anaphase B	(Figure 1)
PMID:37158439	FYPO:0008090	normal onset of mitotic anaphase B	(Figure 1)
PMID:37158439	FYPO:0008090	normal onset of mitotic anaphase B	(Figure 1)
PMID:37158439	FYPO:0008090	normal onset of mitotic anaphase B	(Figure 1)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature [has_severity] medium	(Figure 1B)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure 1B) From this screen we observed one significant interaction: fic1’s phospho-ablating mutant, fic1-2A, suppressed myo2-E1
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure 1C)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure 1C)
PMID:37158439	FYPO:0000202	abnormal regulation of cytokinetic cell separation	(Figure 1E and G)
PMID:37158439	FYPO:0005905	normal onset of actomyosin contractile ring assembly	(Figure 1E and G)
PMID:37158439	FYPO:0005905	normal onset of actomyosin contractile ring assembly	(Figure 1E and G)
PMID:37158439	FYPO:0000202	abnormal regulation of cytokinetic cell separation	(Figure 1E and G)
PMID:37158439	FYPO:0008090	normal onset of mitotic anaphase B	(Figure 2)
PMID:37158439	FYPO:0006879	normal cleavage furrow ingression	(Figure 2)
PMID:37158439	FYPO:0001760	normal cell separation after cytokinesis	(Figure 2)
PMID:37158439	FYPO:0000949	aseptate [has_penetrance] 100	(Figure 2)
PMID:37158439	FYPO:0000639	delayed onset of septum assembly	(Figure 2) fic1-2A myo2-E1 cells can achieve membrane ingression and cell separation at myo2-E1’s restrictive temperature
PMID:37158439	FYPO:0000639	delayed onset of septum assembly	(Figure 2) fic1-2A myo2-E1 cells can achieve membrane ingression and cell separation at myo2-E1’s restrictive temperature
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure 3B)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure 3B)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure 3B)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure 3C)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure 3C)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure 3C)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure 3C)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure 3C)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure 3C)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure 3C) We next asked if S. pombe Cyk3 was required for fic1-2A’s suppression of myo2-E1. Indeed, cyk3Δ prevented fic1-2A from suppressing myo2-E1
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure 3C) We next asked if S. pombe Cyk3 was required for fic1-2A’s suppression of myo2-E1. Indeed, cyk3Δ prevented fic1-2A from suppressing myo2-E1
PMID:37158439	FYPO:0003532	increased monopolar index	(Figure 4A)
PMID:37158439	FYPO:0003532	increased monopolar index	(Figure 4A)
PMID:37158439	FYPO:0003532	increased monopolar index	(Figure 4A)
PMID:37158439	FYPO:0003532	increased monopolar index	(Figure 4A)
PMID:37158439	FYPO:0003532	increased monopolar index	(Figure 4A)
PMID:37158439	FYPO:0003532	increased monopolar index	(Figure 4A)
PMID:37158439	FYPO:0003532	increased monopolar index	(Figure 4A)
PMID:37158439	FYPO:0007774	increased invasive hyphal growth	(Figure 4C)
PMID:37158439	FYPO:0007774	increased invasive hyphal growth	(Figure 4C)
PMID:37158439	FYPO:0007774	increased invasive hyphal growth	(Figure 4C)
PMID:37158439	FYPO:0007774	increased invasive hyphal growth	(Figure 4C)
PMID:37158439	FYPO:0007774	increased invasive hyphal growth	(Figure 4C)
PMID:37158439	FYPO:0007774	increased invasive hyphal growth	(Figure 4C)
PMID:37158439	FYPO:0000082	decreased cell population growth at high temperature	(Figure 4D)
PMID:37158439	FYPO:0000082	decreased cell population growth at high temperature	(Figure 4D)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure 4D)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure S1)
PMID:37158439	FYPO:0000080	decreased cell population growth at low temperature	(Figure S1)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure S1)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure S1)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure S1)
PMID:37158439	FYPO:0000082	decreased cell population growth at high temperature	(Figure S1)
PMID:37158439	FYPO:0000082	decreased cell population growth at high temperature	(Figure S1)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure S2)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure S2)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure S2)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure S2)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure S3)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure S3)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure S3)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure S3)
PMID:37158439	FYPO:0000674	normal cell population growth at high temperature	(Figure S3)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure S3)
PMID:37158439	FYPO:0004481	abolished cell population growth at high temperature	(Figure S3)
PMID:37158439	FYPO:0004557	increased vegetative cell population growth	From this screen we observed one significant interaction: fic1’s phospho-ablating mutant, fic1-2A, suppressed myo2-E1
PMID:37158439	FYPO:0004557	increased vegetative cell population growth	From this screen we observed one significant interaction: fic1’s phospho-ablating mutant, fic1-2A, suppressed myo2-E1
PMID:37160462	FYPO:0002550	sensitive to UV [has_severity] medium	(comment: Phenotype complementation by human RAD23A)
PMID:37162093	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Figure 3A,D, 6A,C,E)
PMID:37162093	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 3B,E; Figure 6A,C,E)
PMID:37162093	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 3C,F; Figure 6A,C,E)
PMID:37162093	FYPO:0002058	viable cell population	(Figure 4A,C)
PMID:37162093	FYPO:0002058	viable cell population	(Figure 4A,C)
PMID:37162093	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 4A,C; Figure 6B,D,E)
PMID:37162093	FYPO:0002058	viable cell population	(Figure 4B,D)
PMID:37162093	FYPO:0002058	viable cell population	(Figure 4B,D)
PMID:37162093	FYPO:0001420	normal vegetative cell population growth rate	(Figure 4B,D, 6B,D,E)
PMID:37162093	FYPO:0002058	viable cell population	(Figure 5A,B)
PMID:37162093	FYPO:0002058	viable cell population	(Figure 5A,B)
PMID:37162093	FYPO:0001420	normal vegetative cell population growth rate	(Figure 5AB; Figure S3)
PMID:37162093	FYPO:0001420	normal vegetative cell population growth rate	(Figure 6B,D,E, S2)
PMID:37162093	FYPO:0000017	elongated cell	(Figure 7)
PMID:37162093	FYPO:0002105	inviable vegetative cell with normal cell shape	(Figure 7)
PMID:37162093	FYPO:0002273	inviable vegetative cell with abnormal cell morphology	(Figure 7)
PMID:37162093	FYPO:0002104	viable vegetative cell with normal cell shape	(Figure 7)
PMID:37162093	FYPO:0002104	viable vegetative cell with normal cell shape	(Figure 7)
PMID:37162093	FYPO:0002104	viable vegetative cell with normal cell shape	(Figure 7)
PMID:37162093	FYPO:0002058	viable cell population	(Figure S2)
PMID:37162093	FYPO:0002058	viable cell population	(Figure S2)
PMID:37164017	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: CHECK Growth rate improved by addition of arginine)
PMID:37164017	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: CHECK Growth rate improved by addition of either glutamate, glutamine, or arginine)
PMID:37164017	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: CHECK Growth rate improved by addition of either glutamate, glutamine, or arginine)
PMID:37164017	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: CHECK Growth rate improved by addition of either glutamate, glutamine, or arginine)
PMID:37164017	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(comment: CHECK Growth rate improved by addition of either glutamate, glutamine, or arginine)
PMID:37164017	FYPO:0007368	increased energy charge	Consistent with previous work,63 the higher Pyk1 activity in S. pombe increased the cellular ATP/ADP ratio, whereas the lower Pyk1 activity in S. japonicus reduced it (Figure 3B).
PMID:37164017	GO:0019643	reductive tricarboxylic acid cycle	Interestingly, both wild-type and cox6D S. pombe, and wild-type S. japonicus, showed high M + 3 fumarate fractions (Figure 2D). This indicates that not only S. japonicus and nonrespiring S. pombe but also the wild-type S. pombe operate the reductive TCA branch.
PMID:37164017	GO:0006099	tricarboxylic acid cycle	M + 2 fumarate is typically associated with the oxidative TCA cycle52,57-59 (Figure 2A). Indeed, only respiro-fermenting wild-type S. pombe showed M + 2 fumarate (Figure 2C). M + 3 fumarate likely originates from the reductive TCA branch52,57-59 (Figure 2B).
PMID:37164017	FYPO:0001420	normal vegetative cell population growth rate	Strikingly, while the deletion of gpd1 in S. pombe did not negatively affect its growth, regardless of respiratory activity (Figures 1E and S1J)
PMID:37164017	FYPO:0001357	normal vegetative cell population growth [has_severity] low	Surprisingly, the growth defect of S. pombe cox6D mutants in EMM could be rescued by arginine but not glutamate or glutamine (Figure 2H).
PMID:37164017	FYPO:0001563	decreased cellular glutamate level	The non-respiring S. pombe cox6D mutant did not upregulate G3P synthesis as compared with the wild-type. S. japonicus also maintained a larger pool of G3P than S. pombe (Figure S1G)
PMID:37164017	FYPO:0002009	decreased oxygen consumption during vegetative growth [has_penetrance] high	Whereas the deletion of cox6 critically decreased oxygen consumption in S. pombe, we observed no such effect in S. japonicus (Figure 1A).
PMID:37164017	GO:0006099	tricarboxylic acid cycle	inferred from isotope labelling Figure 1A & We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	tricarboxylic acid cycle	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	tricarboxylic acid cycle	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	tricarboxylic acid cycle	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	tricarboxylic acid cycle	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	tricarboxylic acid cycle	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	tricarboxylic acid cycle	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37164017	GO:0006099	tricarboxylic acid cycle	inferred from isotope labelling Figure 1A and We assessed the TCA cycle architecture in S. pombe and S. japonicus using stable isotope tracing metabolomics, quantifying the ratios of different TCA-intermediate isotopologs after feeding cells with 13C6-glucose (Figures 2A and 2B).
PMID:37191320	FYPO:0001013	abnormal membrane organization [has_severity] low	(Fig. S4E) revealed that the ER-shaping activities of the ΔC21-60 and ΔN29 mutants were partially and severely impaired, respectively (Fig. S4E)
PMID:37191320	FYPO:0001013	abnormal membrane organization [has_penetrance] high	(Fig. S4E) revealed that the ER-shaping activities of the ΔC21-60 and ΔN29 mutants were partially and severely impaired, respectively (Fig. S4E)
PMID:37191320	FYPO:0007445	abnormal reticulophagy during vegetative growth [has_penetrance] low	(Fig. S4F), the ΔC21-60 and ΔN29 mutants exhibited partial and severe defects in reticulophagy, respectively, whereas the both mutant proteins were detectable on the ER (Fig. S4G)
PMID:37191320	FYPO:0007445	abnormal reticulophagy during vegetative growth [has_penetrance] high	(Fig. S4F), the ΔC21-60 and ΔN29 mutants exhibited partial and severe defects in reticulophagy, respectively, whereas the both mutant proteins were detectable on the ER (Fig. S4G)
PMID:37191320	GO:0005783	endoplasmic reticulum	Consistently, Hva22 was observed on the ER under both nitrogen-rich and starvation conditions (Figure 3C).
PMID:37191320	GO:0061709	reticulophagy [happens_during] cellular response to nitrogen starvation	In hva22Δ cells, reticulophagy was abolished, similar to cells lacking the core autophagy protein Atg1 (Figure 1B).
PMID:37191320	GO:0016236	macroautophagy	Next, selective types of autophagy, such as mitophagy and pexophagy, were monitored by the processing of the mitochondrial protein Tuf1- RFP or Sdh2-GFP [21] and the peroxisomal protein Pex11- GFP, respectively. We observed that the hva22Δ mutant was partially defective in both mitophagy (Figure 2D and Fig. S2E) and pexophagy (Figure 2E).
PMID:37191320	GO:0090158	endoplasmic reticulum membrane organization	The growth defect of the triple mutant strain defective in Spo7, Rtn1, and Yop1 is restored by the overexpression of the budding yeast reticulophagy receptor Atg40, a reticulon- and REEP-like protein that contains an ER-shaping activity
PMID:37191320	GO:0044804	nucleophagy	We further found that the inner nuclear membrane protein Lem2 [26] was also degraded in a manner dependent on Hva22 (Figure 1H,I), indicating that the nuclear envelope undergoes Hva22- dependent reticulophagy. (vw I think this should be nucleophagy becasue IMN is not comnnected to ER)
PMID:37192628	FYPO:0000500	decreased mitophagy [has_penetrance] high	As expected, in S. pombe atg44D cellslacking Mgm1, some of the mitochondria became fragmented and mitophagy was partially rescued (Figures 4A and S3F).
PMID:37192628	FYPO:0000500	decreased mitophagy [has_penetrance] high	As expected, in S. pombe atg44D cellslacking Mgm1, some of the mitochondria became fragmented and mitophagy was partially rescued (Figures 4A and S3F).
PMID:37192628	GO:0008289	lipid binding	Atg44 binds to lipid membranes in vitro (Figures 5A and 5E), and the cryo-EM and HS-AFM analyses (Figures 5F-5I) suggest that Atg44 tends to bind to lipid membranes with high curvature.
PMID:37192628	GO:0005758	mitochondrial intermembrane space	Based on these results, we conclude that Atg44 localizes in the IMS and is not a transmembrane protein.
PMID:37192628	FYPO:0007594	abolished mitophagy during nitrogen starvation	In atg44D cells, mitophagy was completely blocked similarly to cells lacking Atg1, a core autophagy protein (Figures 1A and S1B).
PMID:37192628	FYPO:0007448	normal reticulophagy during nitrogen starvation	Loss of Atg44 in either S. pombe or S. cerevisiae did not or only marginally affected non-selective macroautophagy, as measured by GFP/RFP processing (Figures S1C, S1D, and S1F) or the Pho8D60 assay (Figure 1E), or other types of selective autophagy including the Cvt pathway that delivers the precursor form of the hydrolase aminopeptidase I to the vacuole (Figure S1G), endoplasmic reticulum-phagy/reticulophagy (Figures S1E and S1H), and pexophagy (Figure S1I), suggesting that Atg44 is specifically required for mitophagy.
PMID:37192628	FYPO:0003810	small fragmented mitochondria present in increased numbers	Overexpression of Atg44 in both species caused mitochondrial fragmentation not only in wild-type cells but also in Dnm1-deficient cells (Figures 3E and 3F).
PMID:37192628	FYPO:0004340	abnormal mitochondrial fission	Similarly, loss of Atg44 in S. pombe affected mitochondrial morphology; some of the Sp-atg44D cells showed spherically enlarged mitochondria like Sp-dnm1D cells (Figure 3D)
PMID:37192628	GO:0140912	membrane destabilizing activity [part_of] mitophagy	Unexpectedly, we noticed that addition of Sp-Atg44 caused fragmentation of lipid bilayers on the mica (compare Figures 7B and 7C), and the fragmented lipid bilayers abundant with Sp-Atg44 underwent division and fusion (Figure 7D; Video S6). These observations suggest that Sp-Atg44 has the ability to cause membrane fragility through physical interaction.
PMID:37200372	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 1)
PMID:37200372	FYPO:0000088	sensitive to hydroxyurea	(Fig. 1)
PMID:37200372	FYPO:0000088	sensitive to hydroxyurea	(Fig. 1)
PMID:37200372	FYPO:0000088	sensitive to hydroxyurea	(Fig. 1)
PMID:37200372	FYPO:0000088	sensitive to hydroxyurea	(Fig. 1)
PMID:37200372	FYPO:0000088	sensitive to hydroxyurea	(Fig. 1)
PMID:37200372	FYPO:0000088	sensitive to hydroxyurea	(Fig. 1)
PMID:37200372	FYPO:0000088	sensitive to hydroxyurea	(Fig. 1)
PMID:37200372	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 1)
PMID:37200372	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 1)
PMID:37200372	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 1)
PMID:37200372	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 1)
PMID:37200372	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 1)
PMID:37200372	FYPO:0002099	normal protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC694.06c	(Fig. 1)
PMID:37200372	FYPO:0002099	normal protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC694.06c	(Fig. 1)
PMID:37200372	FYPO:0002099	normal protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC694.06c	(Fig. 1)
PMID:37200372	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC694.06c [has_severity] low	(Fig. 1)
PMID:37200372	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC694.06c [has_severity] high	(Fig. 1)
PMID:37200372	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [has_severity] high [assayed_protein] PomBase:SPCC18B5.11c	(Fig. 1)
PMID:37200372	FYPO:0002096	increased protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPCC18B5.11c	(Fig. 1)
PMID:37200372	FYPO:0002096	increased protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPCC18B5.11c	(Fig. 1)
PMID:37200372	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPCC18B5.11c [has_severity] low	(Fig. 1)
PMID:37200372	FYPO:0002897	decreased protein phosphorylation during cellular response to DNA damage [has_severity] high [assayed_protein] PomBase:SPCC1259.13	(Fig. 1)
PMID:37200372	FYPO:0002899	normal protein phosphorylation during cellular response to DNA damage [assayed_protein] PomBase:SPCC1259.13	(Fig. 1)
PMID:37200372	FYPO:0002899	normal protein phosphorylation during cellular response to DNA damage [assayed_protein] PomBase:SPCC1259.13	(Fig. 1)
PMID:37200372	FYPO:0002897	decreased protein phosphorylation during cellular response to DNA damage [assayed_protein] PomBase:SPCC1259.13 [has_severity] low	(Fig. 1)
PMID:37200372	FYPO:0002897	decreased protein phosphorylation during cellular response to DNA damage [assayed_protein] PomBase:SPCC1259.13 [has_severity] low	(Fig. 1)
PMID:37200372	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC660.13c [has_severity] high	(Fig. 2)
PMID:37200372	FYPO:0009109	decreased vegetative cell population growth after short incubation in hydroxyurea [has_severity] low	(Fig. 2)
PMID:37200372	FYPO:0009110	normal vegetative cell population growth after short incubation in hydroxyurea [has_severity] low	(Fig. 2)
PMID:37200372	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC660.13c [has_severity] high	(Fig. 2)
PMID:37200372	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC660.13c [has_severity] low	(Fig. 2)
PMID:37200372	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC660.13c [has_severity] high	(Fig. 2)
PMID:37200372	FYPO:0009110	normal vegetative cell population growth after short incubation in hydroxyurea [has_severity] low	(Fig. 2)
PMID:37200372	FYPO:0009110	normal vegetative cell population growth after short incubation in hydroxyurea [has_severity] low	(Fig. 2)
PMID:37200372	FYPO:0009109	decreased vegetative cell population growth after short incubation in hydroxyurea [has_severity] low	(Fig. 2)
PMID:37200372	FYPO:0009109	decreased vegetative cell population growth after short incubation in hydroxyurea [has_severity] high	(Fig. 2)
PMID:37200372	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC660.13c [has_severity] low	(Fig. 2)
PMID:37200372	FYPO:0009109	decreased vegetative cell population growth after short incubation in hydroxyurea [has_severity] high	(Fig. 2)
PMID:37200372	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 6)
PMID:37200372	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 6)
PMID:37200372	FYPO:0000088	sensitive to hydroxyurea	(Fig. 6)
PMID:37200372	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [has_severity] high [assayed_protein] PomBase:SPCC18B5.11c	(Fig. 6)
PMID:37200372	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [has_severity] high [assayed_protein] PomBase:SPCC18B5.11c	(Fig. 6)
PMID:37200372	FYPO:0002899	normal protein phosphorylation during cellular response to DNA damage [assayed_protein] PomBase:SPCC1259.13	(Fig. 6)
PMID:37200372	FYPO:0002897	decreased protein phosphorylation during cellular response to DNA damage [assayed_protein] PomBase:SPCC1259.13 [has_severity] low	(Fig. 6)
PMID:37200372	FYPO:0009109	decreased vegetative cell population growth after short incubation in hydroxyurea [has_severity] low	(Fig. 6)
PMID:37200372	FYPO:0009109	decreased vegetative cell population growth after short incubation in hydroxyurea [has_severity] low	(Fig. 6)
PMID:37200372	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC664.07c	(Fig. 6)
PMID:37200372	FYPO:0000088	sensitive to hydroxyurea	(Fig. 6)
PMID:37200372	FYPO:0002897	decreased protein phosphorylation during cellular response to DNA damage [assayed_protein] PomBase:SPAC664.07c	(Fig. 6)
PMID:37200372	FYPO:0002897	decreased protein phosphorylation during cellular response to DNA damage [assayed_protein] PomBase:SPAC664.07c	(Fig. 6)
PMID:37200372	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC664.07c	(Fig. 6)
PMID:37200372	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC694.06c [has_severity] low	(Fig. 6B)
PMID:37200372	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC694.06c	(Fig. 6B)
PMID:37200372	FYPO:0000268	sensitive to UV during vegetative growth	(Fig. 7)
PMID:37200372	FYPO:0000095	sensitive to bleomycin [has_severity] high	(Fig. 7)
PMID:37200372	FYPO:0000095	sensitive to bleomycin [has_severity] high	(Fig. 7)
PMID:37200372	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 7)
PMID:37200372	FYPO:0000268	sensitive to UV during vegetative growth	(Fig. 7)
PMID:37200372	FYPO:0000095	sensitive to bleomycin [has_severity] high	(Fig. 7)
PMID:37200372	FYPO:0000095	sensitive to bleomycin [has_severity] high	(Fig. 7)
PMID:37200372	FYPO:0000095	sensitive to bleomycin [has_severity] high	(Fig. 7)
PMID:37200372	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 7)
PMID:37200372	FYPO:0000085	sensitive to camptothecin	(Fig. 7)
PMID:37200372	FYPO:0000085	sensitive to camptothecin	(Fig. 7)
PMID:37200372	FYPO:0000268	sensitive to UV during vegetative growth	(Fig. 7)
PMID:37200372	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 7)
PMID:37200372	FYPO:0000268	sensitive to UV during vegetative growth	(Fig. 7)
PMID:37200372	FYPO:0001053	cut, normal size cell [has_penetrance] 5	(Fig. S12)
PMID:37200372	FYPO:0001053	cut, normal size cell [has_penetrance] 5	(Fig. S12)
PMID:37200372	FYPO:0001052	cut, small cell [has_penetrance] high	(Fig. S12)
PMID:37200372	FYPO:0001053	cut, normal size cell [has_penetrance] 30	(Fig. S12)
PMID:37200372	FYPO:0001053	cut, normal size cell [has_penetrance] 4	(Fig. S12)
PMID:37200372	FYPO:0001355	decreased vegetative cell population growth	(Fig. S2) and text
PMID:37200372	FYPO:0002060	viable vegetative cell population	(Fig. S2) and text
PMID:37200372	FYPO:0002061	inviable vegetative cell population	(Fig. S2) and text
PMID:37200372	FYPO:0002061	inviable vegetative cell population	(Fig. S2) and text
PMID:37237082	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	(Fig. 1e) Genome sequencing of one of them identified the srr1/ ber1-W157R and skb1-A377V mutations in their SRR1-like and arginine methyltransferase (RMTase) domains, respectively (Fig. 1b).
PMID:37237082	FYPO:0005371	increased linear minichromosome loss during vegetative growth	(Fig. 3e)
PMID:37237082	FYPO:0005371	increased linear minichromosome loss during vegetative growth	(Fig. 3e)
PMID:37237082	FYPO:0005371	increased linear minichromosome loss during vegetative growth [has_severity] high	(Fig. 3e) We found that srr1Δ and srr1-W157R increased the rate of chromosome loss. (In WT and rad51 backgrounds)
PMID:37237082	FYPO:0005371	increased linear minichromosome loss during vegetative growth [has_severity] high	(Fig. 3e) We found that srr1Δ and srr1-W157R increased the rate of chromosome loss. (In WT and rad51 backgrounds)
PMID:37237082	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(Fig. 6A)
PMID:37237082	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(Fig. 6A)
PMID:37237082	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(Fig. 6A)
PMID:37237082	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] low	(Fig. 6A)
PMID:37237082	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Figure 3a)
PMID:37237082	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Figure 3a)
PMID:37237082	FYPO:0000963	normal growth on hydroxyurea	(Figure 3a)
PMID:37237082	FYPO:0001690	normal growth on camptothecin	(Figure 3a)
PMID:37237082	FYPO:0000957	normal growth on methyl methanesulfonate	(Figure 3a)
PMID:37237082	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Figure 3a)
PMID:37237082	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Figure 3a)
PMID:37237082	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Figure 3a)
PMID:37237082	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Figure 3a)
PMID:37237082	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Figure 5e)
PMID:37237082	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Figure 5e)
PMID:37237082	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Figure 5e)
PMID:37237082	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Figure 5e)
PMID:37237082	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Figure 5e)
PMID:37237082	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Figure 5e)
PMID:37237082	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	Both srr1-D111A,P112A and srr1- H148A mutations reduced GCR rates (Fig. 5d).
PMID:37237082	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	Both srr1-D111A,P112A and srr1- H148A mutations reduced GCR rates (Fig. 5d).
PMID:37237082	FYPO:0006810	decreased gross chromosomal rearrangement [has_severity] low	In the wild-type background, srr1Δ but not skb1Δ slightly reduced GCR rates, showing that Srr1 is required for GCRs even in the presence of Rad51
PMID:37237082	FYPO:0001355	decreased vegetative cell population growth	Like srr1Δ cells, srr1-W157R, srr1-D111A,P112A, and srr1-H184A cells produced small colonies (Supplementary Fig. 2b), consistent with the role of the SRR1-like domain even in the absence of exogenous DNA damage.
PMID:37237082	FYPO:0001355	decreased vegetative cell population growth	Like srr1Δ cells, srr1-W157R, srr1-D111A,P112A, and srr1-H184A cells produced small colonies (Supplementary Fig. 2b), consistent with the role of the SRR1-like domain even in the absence of exogenous DNA damage.
PMID:37237082	FYPO:0001355	decreased vegetative cell population growth	Like srr1Δ cells, srr1-W157R, srr1-D111A,P112A, and srr1-H184A cells produced small colonies (Supplementary Fig. 2b), consistent with the role of the SRR1-like domain even in the absence of exogenous DNA damage.
PMID:37237082	FYPO:0001355	decreased vegetative cell population growth	Like srr1Δ cells, srr1-W157R, srr1-D111A,P112A, and srr1-H184A cells produced small colonies (Supplementary Fig. 2b), consistent with the role of the SRR1-like domain even in the absence of exogenous DNA damage.
PMID:37237082	FYPO:0006437	normal mitotic DNA damage checkpoint during cellular response to methyl methanesulfonate	Normal Chk1 phosphorylation and cell cycle arrest
PMID:37237082	FYPO:0006437	normal mitotic DNA damage checkpoint during cellular response to methyl methanesulfonate	Normal Chk1 phosphorylation and cell cycle arrest
PMID:37237082	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	The rad52-R45K, rad52Δ, and srr1Δ mutations eliminate ~90% of isochromosomes in rad51Δ cells (Fig. 2c and ref. 32), indicating that both Rad52 and Srr1 are essential for the major pathway of isochromosome formation.
PMID:37237082	FYPO:0001840	increased minichromosome loss during vegetative growth [has_severity] low	To our surprise, not only srr1Δ but also skb1Δ reduced GCR rates in the rad51Δ background, demonstrating that both Srr1 and Skb1 cause GCRs.
PMID:37237082	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	To our surprise, not only srr1Δ but also skb1Δ reduced GCR rates in the rad51Δ background, demonstrating that both Srr1 and Skb1 cause GCRs.
PMID:37237082	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	To our surprise, not only srr1Δ but also skb1Δ reduced GCR rates in the rad51Δ background, demonstrating that both Srr1 and Skb1 cause GCRs.
PMID:37237082	FYPO:0001840	increased minichromosome loss during vegetative growth [has_severity] low	To our surprise, not only srr1Δ but also skb1Δ reduced GCR rates in the rad51Δ background, demonstrating that both Srr1 and Skb1 cause GCRs.
PMID:37237082	FYPO:0002150	inviable spore population	We crossed srr1Δ and rad52Δ haploid strains and dissected the tetrads but failed to obtain srr1Δ rad52Δ progenies (Fig. 4b)
PMID:37237082	FYPO:0002150	inviable spore population	We crossed srr1Δ and rad52Δ haploid strains and dissected the tetrads but failed to obtain srr1Δ rad52Δ progenies (Fig. 4b)
PMID:37237082	FYPO:0001742	increased isochromosome formation [has_severity] low	skb1∆ and srr1∆ additively reduce the rate of gross chromosomal rearrangements in rad51 deletion background.
PMID:37237082	FYPO:0001742	increased isochromosome formation [has_severity] low	skb1∆ and srr1∆ additively reduce the rate of gross chromosomal rearrangements in rad51 deletion background.
PMID:37237082	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	srr1-W157R and rad52-R45K or pcn1-K107R additively reduce gross chromosomal rearrangement. srr1-W157R and pcn1-K107R also additively reduced GCR rates in rad51Δ cells (Fig. 4a).
PMID:37237082	FYPO:0001740	increased gross chromosomal rearrangement [has_severity] medium	srr1-W157R and rad52-R45K or pcn1-K107R additively reduce gross chromosomal rearrangement. srr1-W157R and pcn1-K107R also additively reduced GCR rates in rad51Δ cells (Fig. 4a).
PMID:37279920	FYPO:0002355	decreased histone H3-K9 dimethylation at silent mating-type cassette during vegetative growth [has_severity] low	(Figure 2)
PMID:37279920	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette [has_severity] high	Strikingly, however, silencing at the mating type locus was completely abolished in the 22 absence of Caf1 and Mot2, similar to clr4∆ cells, as revealed by the lack of cell growth on 23 5FOA-containing medium and the marked accumulation of ura4+ transcripts (Fig. 1g-h).
PMID:37279920	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette [has_severity] high	Strikingly, however, silencing at the mating type locus was completely abolished in the 22 absence of Caf1 and Mot2, similar to clr4∆ cells, as revealed by the lack of cell growth on 23 5FOA-containing medium and the marked accumulation of ura4+ transcripts (Fig. 1g-h).
PMID:37279920	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	We also detected intermediate phenotypes for the 8 ccr4∆ mutant, pointing to a partial contribution of this RNA deadenylase (Fig. 1g-h; 9 Supplementary Fig. 1b-d).
PMID:37288768	FYPO:0001273	mitotic spindle elongation with incomplete, unequal mitotic sister chromatid segregation and unseparated DNA [has_penetrance] low	(Fig. 1B)
PMID:37288768	FYPO:0004592	cut following normal mitosis [has_penetrance] medium	(Fig. 1B)
PMID:37288768	FYPO:0003268	decreased rate of mitotic spindle elongation [has_severity] variable severity	(Fig. 2E)
PMID:37288768	FYPO:0000274	increased duration of mitotic M phase [has_severity] variable severity	(Fig. 2G)
PMID:37288768	FYPO:0003165	cut [has_penetrance] low	(Fig. 3)
PMID:37288768	FYPO:0003165	cut [has_penetrance] medium	(Fig. 3)
PMID:37288768	FYPO:0003165	cut [has_penetrance] medium	(Fig. 3)
PMID:37288768	FYPO:0003165	cut [has_penetrance] low	(Fig. 3)
PMID:37288768	FYPO:0003165	cut [has_penetrance] low	(Fig. 3)
PMID:37288768	FYPO:0003165	cut [has_penetrance] low	(Fig. 3)
PMID:37288768	FYPO:0000891	abnormal histone H3-K9 acetylation during vegetative growth	(Fig. 4A, S2)
PMID:37288768	FYPO:0000886	abnormal histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 4A, S3)
PMID:37288768	FYPO:0001861	increased minichromosome loss upon segregation during vegetative growth [has_penetrance] medium [has_severity] medium	(Fig. 4C)
PMID:37288768	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPBC29A10.04	(Fig. 4D)
PMID:37288768	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. S2A) We first validated the previous report of cbf11Δ cells being sensitive to TBZ. When plated on YES medium containing TBZ, the cbf11Δ mutant indeed showed strong sensitivity to the drug (Fig. S2A)
PMID:37288768	FYPO:0007664	mononucleate monoseptate vegetative cell with anucleate compartment	Notably, the nuclear displacement phenotypewas associated with mid-anaphase spindle bending and/or detachment of one of the daughter chromosome masses from the spindle, and subsequent spindle disassembly and merger of the two daughter chromosome masses into one diploid nucleus (Figs 1B and 2B).
PMID:37400983	FYPO:0000658	decreased DNA binding [assayed_protein] PomBase:SPAC664.01c	(comment: CHECK ****NEED TO FIX allele description*****.) The N-terminal disordered region of Swi6 (Swi6-N) bound weakly to DNA (Fig. 2D and L)
PMID:37400983	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(comment: mat3M::ura4+ reporter silencing )| combined mutations of the hinge and one of the mutations in the N-terminus of CSD (mut3 and mut5) showed a silencing defect (Fig. 4C)
PMID:37400983	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: mat3M::ura4+ reporter silencing )| combined mutations of the hinge and one of the mutations in the N-terminus of CSD (mut3 and mut5) showed a silencing defect (Fig. 4C)
PMID:37400983	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(comment: mat3M::ura4+ reporter silencing)
PMID:37400983	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(comment: mat3M::ura4+ reporter silencing)
PMID:37400983	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(comment: mat3M::ura4+ reporter silencing)
PMID:37400983	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(comment: mat3M::ura4+ reporter silencing) |combined mutations of the hinge and one of the mutations in the N-terminus of CSD (mut3 and mut5) showed a silencing defect (Fig. 4C)
PMID:37400983	FYPO:0006631	decreased protein localization to chromatin [assayed_protein] PomBase:SPAC664.01c	As previously reported, in wild-type cells, Swi6 was present in both the soluble (S) and chromatin-enriched pellet (P) fractions, with approximately 40% of the total Swi6 protein detected in the pellet fraction, and most of the Swi6 in the pellet fraction was redistributed to the soluble fraction in clr4∆ cells (Fig. 1A).
PMID:37400983	FYPO:0005929	decreased chromatin binding at centromere outer repeat	Chp2 mutants lacking DNA-binding activities associated with both the hinge and the N-terminus of CSD (mut 3 and mut 5) exhibited reduced heterochromatin association compared to wild-type Chp2 at representative heterochromatic regions (centromeric dg, the mating-type cenH, telomere and mat3M::ura4+), and the reduction was more severe for Chp2-mut3 compared to Chp2-mut5 (Fig. 6A).
PMID:37400983	FYPO:0003231	decreased histone H3-K9 methylation at heterochromatin domain during vegetative growth	Chp2 mutants lacking DNA-binding activities associated with both the hinge and the N-terminus of CSD (mut 3 and mut 5) exhibited reduced heterochromatin association compared to wild-type Chp2 at representative heterochromatic regions (centromeric dg, the mating-type cenH, telomere and mat3M::ura4+), and the reduction was more severe for Chp2-mut3 compared to Chp2-mut5 (Fig. 6A).
PMID:37400983	FYPO:0004984	decreased chromatin binding at centromere central core	Chp2 mutants lacking DNA-binding activities associated with both the hinge and the N-terminus of CSD (mut 3 and mut 5) exhibited reduced heterochromatin association compared to wild-type Chp2 at representative heterochromatic regions (centromeric dg, the mating-type cenH, telomere and mat3M::ura4+), and the reduction was more severe for Chp2-mut3 compared to Chp2-mut5 (Fig. 6A).
PMID:37400983	FYPO:0000659	abolished DNA binding [assayed_protein] PomBase:SPBC16C6.10	Chp2-CSD (Chp2-CSD3A) no longer bound DNA (Fig. 3F and Supplementary Fig. S2B), Chp2 with H5A mutation in the hinge (Chp2-mut1) or with either CSD2A or CSD3A mutation in the CSD (Chp2-mut2 and Chp2- mut4) exhibited weaker DNA-binding activity compared to wild-type Chp2 (Chp2-WT) (Fig. 3H, I, J and L and Supplementary Fig. S2C and S2F)
PMID:37400983	FYPO:0006163	normal protein localization to chromatin [assayed_protein] PomBase:SPBC16C6.10	In contrast, Chp2 was preferentially present in the chromatin-enriched pellet fraction in wild-type cells, and the Chp2 in this fraction was not altered by the clr4+ depletion (Fig. 1B).
PMID:37400983	FYPO:0006163	normal protein localization to chromatin [assayed_protein] PomBase:SPBC16C6.10	Interestingly, we found that Chp2 in the chromatin-enriched pellet fraction was not affected by the Mit1I11R mutation (Fig. 1B).
PMID:37400983	FYPO:0000655	normal DNA binding [assayed_protein] PomBase:SPBC16C6.10	Interestingly, we found that Chp2-CSD exhibited a robust DNA binding activity (Fig. 2K and M)
PMID:37400983	FYPO:0000659	abolished DNA binding [assayed_protein] PomBase:SPBC16C6.10	Interestingly, when amino acid substitutions in the hinge and CSD were combined, the resulting Chp2 mutants (Chp2-mut3 and Chp3-mut5) no longer bound DNA (Fig. 3K and M, and Supplementary Fig. S2F)
PMID:37400983	FYPO:0000659	abolished DNA binding [assayed_protein] PomBase:SPBC16C6.10	Interestingly, when amino acid substitutions in the hinge and CSD were combined, the resulting Chp2 mutants (Chp2-mut3 and Chp3-mut5) no longer bound DNA (Fig. 3K and M, and Supplementary Fig. S2F)
PMID:37400983	FYPO:0000655	normal DNA binding [assayed_protein] PomBase:SPBC16C6.10	The hinge and the N-terminal disordered regions of Chp2 (Chp2-H and Chp2-N) also bound DNA (Fig. 2H, J and M)
PMID:37400983	FYPO:0000655	normal DNA binding [assayed_protein] PomBase:SPBC16C6.10	The hinge and the N-terminal disordered regions of Chp2 (Chp2-H and Chp2-N) also bound DNA (Fig. 2H, J and M)
PMID:37400983	GO:0003677	DNA binding	Using purified full-length, dimerized Chp2 and Swi6, we performed EMSAs using pericentromeric DNA as a probe. Consistent with previous results, Swi6 bound DNA efficiently, and Chp2 also showed similar DNA binding activity (Fig. 2B and C).
PMID:37400983	GO:0003677	DNA binding	Using purified full-length, dimerized Chp2 and Swi6, we performed EMSAs using pericentromeric DNA as a probe. Consistent with previous results, Swi6 bound DNA efficiently, and Chp2 also showed similar DNA binding activity (Fig. 2B and C).
PMID:37400983	FYPO:0000658	decreased DNA binding [has_severity] high [assayed_protein] PomBase:SPBC16C6.10	exhibited only a very weak DNA binding activity compared to wild-type Chp2-CD (Chp2-CSDWT ) (Fig. 3D and E, and Supplementary Fig. S2B and S2E)
PMID:37400983	FYPO:0000659	abolished DNA binding [assayed_protein] PomBase:SPAC664.01c	no detectable DNA-binding activity was observed for Chp2-CD (Fig. 2I and M).
PMID:37400983	FYPO:0000659	abolished DNA binding [assayed_protein] PomBase:SPBC16C6.10	when these were replaced by alanine (Fig. 3A), the resulting Chp2-H mutant (Chp2-H5A) no longer bound to DNA (Fig. 3B and C, and Supplementary Fig. S2A and S2D)
PMID:37400983	FYPO:0000659	abolished DNA binding [assayed_protein] PomBase:SPAC664.01c	whereas no DNA binding activity was detected for Swi6-CD or Swi6-CSD (Fig. 2E, G and L).
PMID:37400983	FYPO:0000659	abolished DNA binding [assayed_protein] PomBase:SPAC664.01c	whereas no DNA binding activity was detected for Swi6-CD or Swi6-CSD (Fig. 2E, G and L).
PMID:37403782	GO:1990276	RNA 5'-gamma-phosphate methyltransferase activity [has_input] PomBase:SPSNRNA.06 [part_of] RNA capping	(comment: Bmc1 5 capping catalytic activity is not required for promoting 2 -O-methylation of U6)
PMID:37403782	GO:0016180	snRNA processing	(comment: U6)
PMID:37403782	GO:0016180	snRNA processing	(comment: U6)
PMID:37403782	GO:0016180	snRNA processing	(comment: U6)
PMID:37403782	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPBC1861.04c [assayed_transcript] PomBase:SPSNRNA.06	Deletion of snoZ30 and sno530 resulted in a loss of 2′-O-methylation at A41 and A64, respectively, suggesting that sno530 is indeed the A64 U6-modifying snoRNA (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	FYPO:0008109	abolished U6 2'-O-snRNA methylation at residue A64 [assayed_transcript] PomBase:SPSNRNA.06	Deletion of snoZ30 and sno530 resulted in a loss of 2′-O-methylation at A41 and A64, respectively, suggesting that sno530 is indeed the A64 U6-modifying snoRNA (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	FYPO:0003622	abolished U6 2'-O-snRNA methylation at residue A41 [assayed_transcript] PomBase:SPSNRNA.06	Deletion of snoZ30 and sno530 resulted in a loss of 2′-O-methylation at A41 and A64, respectively, suggesting that sno530 is indeed the A64 U6-modifying snoRNA (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPBC1861.04c [assayed_transcript] PomBase:SPSNRNA.06	Deletion of snoZ30 and sno530 resulted in a loss of 2′-O-methylation at A41 and A64, respectively, suggesting that sno530 is indeed the A64 U6-modifying snoRNA (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	FYPO:0002133	abolished protein-RNA interaction [assayed_protein] PomBase:SPBC2A9.10 [assayed_transcript] PomBase:SPSNORNA.25	Further supporting the idea that U6 complex formation is contingent on the presence of all three proteins, we observed a loss of snoZ30 binding to Bmc1 upon knockout of any member of the complex (Supplementary Figure S2A).
PMID:37403782	FYPO:0002133	abolished protein-RNA interaction [assayed_protein] PomBase:SPBC2A9.10 [assayed_transcript] PomBase:SPSNORNA.25	Further supporting the idea that U6 complex formation is contingent on the presence of all three proteins, we observed a loss of snoZ30 binding to Bmc1 upon knockout of any member of the complex (Supplementary Figure S2A).
PMID:37403782	FYPO:0002133	abolished protein-RNA interaction [assayed_protein] PomBase:SPBC2A9.10 [assayed_transcript] PomBase:SPSNORNA.25	Further supporting the idea that U6 complex formation is contingent on the presence of all three proteins, we observed a loss of snoZ30 binding to Bmc1 upon knockout of any member of the complex (Supplementary Figure S2A).
PMID:37403782	FYPO:0008112	abnormal U6 snRNP assembly	Importantly, co-migration of Pof8 with U6 was lost upon deletion of Bmc1 (Figure 1B), as well as co-migration of Bmc1 with U6 upon deletion of Pof8 (Supplementary Figure S1C).
PMID:37403782	FYPO:0008112	abnormal U6 snRNP assembly	Importantly, co-migration of Pof8 with U6 was lost upon deletion of Bmc1 (Figure 1B), as well as co-migration of Bmc1 with U6 upon deletion of Pof8 (Supplementary Figure S1C).
PMID:37403782	FYPO:0008113	increased intron retention	Still, as mean intron retention values indeed showed an increase upon Bmc1 deletion (Figure 5A), we chose several representative intron retention events to validate with semi-quantitative RT-PCR (one of which, intron 1 of pud1, displayed a statistically significant increase upon Bmc1 deletion at 32 ̊C in our RNA Seq dataset).
PMID:37403782	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_transcript] PomBase:SPBC543.05c	Still, as mean intron retention values indeed showed an increase upon Bmc1 deletion (Figure 5A), we chose several representative intron retention events to validate with semi-quantitative RT-PCR (one of which, intron 1 of pud1, displayed a statistically significant increase upon Bmc1 deletion at 32 ̊C in our RNA Seq dataset).
PMID:37403782	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPAC4C5.01	Still, as mean intron retention values indeed showed an increase upon Bmc1 deletion (Figure 5A), we chose several representative intron retention events to validate with semiquantitative RT-PCR (one of which, intron 1 of pud1, displayed a statistically significant increase upon Bmc1 deletion at 32 ̊C in our RNA Seq dataset).
PMID:37403782	GO:0030515	snoRNA binding	We validated the interaction between Bmc1 and sno530 by RNP immunoprecipitation/qPCR and showed that much like snoZ30 and U6, this interaction is dependent on the presence of the assembled Bmc1-Pof8-Thc1 complex (Figure 1A).
PMID:37403782	FYPO:0008110	decreased U6 2'-O-snRNA methylation at residue A64	reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	FYPO:0008110	decreased U6 2'-O-snRNA methylation at residue A64	reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	FYPO:0008110	decreased U6 2'-O-snRNA methylation at residue A64	reproducible decrease in modification at several other sites, most notably A64 (Figure 1C, D, Supplementary Figure S3).
PMID:37403782	GO:0030515	snoRNA binding	we examined our Bmc1 RIP-Seq dataset (20), which revealed an interaction between Bmc1 and snoZ30, which guides 2′-O-methylation of U6 at position 41 (41) (Supplementary Figures S1A, S2A, B).
PMID:37403782	GO:0005732	sno(s)RNA-containing ribonucleoprotein complex	we found that all three proteins are necessary for an interaction with U6 (Figure 1A, Supplementary Figure S1B).
PMID:37403782	GO:0005732	sno(s)RNA-containing ribonucleoprotein complex	we found that all three proteins are necessary for an interaction with U6 (Figure 1A, Supplementary Figure S1B).
PMID:37403782	GO:0005732	sno(s)RNA-containing ribonucleoprotein complex	we found that all three proteins are necessary for an interaction with U6 (Figure 1A, Supplementary Figure S1B).
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0001986	resistance to 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0001986	resistance to 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0001986	resistance to 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0001986	resistance to 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0001986	resistance to 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0001986	resistance to 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0001986	resistance to 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0001986	resistance to 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0001986	resistance to 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0001986	resistance to 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0001986	resistance to 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0001986	resistance to 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 1)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 2)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 3)
PMID:37445861	FYPO:0007035	normal growth on 5-fluorouracil	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 3)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. 3)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 35	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 35	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 35	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 50	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 35	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 30	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 25	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 35	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 30	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 25	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 15	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 10	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 10	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 12	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 40	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 50	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 55	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 50	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 50	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 60	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 30	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 30	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 10	(Fig. 4)
PMID:37445861	FYPO:0000029	abnormal chromosome segregation [has_penetrance] 35	(Fig. 4)
PMID:37445861	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat [has_severity] high	(Fig. 5)
PMID:37445861	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat [has_severity] low	(Fig. 5)
PMID:37445861	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat [has_severity] low	(Fig. 5)
PMID:37445861	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat [has_severity] medium	(Fig. 5)
PMID:37445861	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat [has_severity] medium	(Fig. 5)
PMID:37445861	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat [has_severity] medium	(Fig. 5)
PMID:37445861	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat [has_severity] medium	(Fig. 5)
PMID:37445861	FYPO:0004742	normal chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat	(Fig. 5)
PMID:37445861	FYPO:0006299	increased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat	(Fig. 5)
PMID:37445861	FYPO:0004742	normal chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat	(Fig. 5)
PMID:37445861	FYPO:0006299	increased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat	(Fig. 5)
PMID:37445861	FYPO:0004742	normal chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat	(Fig. 5)
PMID:37445861	FYPO:0004742	normal chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat	(Fig. 5)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. S2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. S2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. S2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. S2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. S2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. S2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. S2)
PMID:37445861	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] low	(Fig. S2)
PMID:37445861	FYPO:0000069	resistance to thiabendazole	(Fig. S3)
PMID:37445861	FYPO:0000069	resistance to thiabendazole	(Fig. S3)
PMID:37445861	FYPO:0000069	resistance to thiabendazole	(Fig. S3)
PMID:37445861	FYPO:0000069	resistance to thiabendazole	(Fig. S3)
PMID:37445861	FYPO:0000069	resistance to thiabendazole	(Fig. S3)
PMID:37445861	FYPO:0000069	resistance to thiabendazole	(Fig. S3)
PMID:37445861	FYPO:0000964	normal growth on thiabendazole	(Fig. S3)
PMID:37445861	FYPO:0000964	normal growth on thiabendazole	(Fig. S3)
PMID:37445861	FYPO:0000964	normal growth on thiabendazole	(Fig. S3)
PMID:37445861	FYPO:0000964	normal growth on thiabendazole	(Fig. S3)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S3)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S3)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S3)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S3)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S3)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S3)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. S3)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. S3)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. S3)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. S3)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. S3)
PMID:37445861	FYPO:0000069	resistance to thiabendazole	(Fig. S3)
PMID:37445861	FYPO:0000069	resistance to thiabendazole	(Fig. S3)
PMID:37445861	FYPO:0000069	resistance to thiabendazole	(Fig. S3)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S4)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S4)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S4)
PMID:37445861	FYPO:0000964	normal growth on thiabendazole	(Fig. S4)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S4)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S4)
PMID:37445861	FYPO:0000964	normal growth on thiabendazole	(Fig. S4)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S4)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S4)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S4)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S4)
PMID:37445861	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S4)
PMID:37446379	FYPO:0008363	abolished nucleolar ring formation	(Figure 7b) the absence of Mas5 also blocked the accumulation of Hsp104-GFP into NuRs (Figure 7b)
PMID:37459529	GO:0180032	histone H4K5 deacetylase activity, hydrolytic mechanism	(comment: assayed complex)
PMID:37459529	GO:0034739	histone H4K16 deacetylase activity, hydrolytic mechanism	(comment: assayed complex)
PMID:37459529	GO:0140937	histone H4K12 deacetylase activity, hydrolytic mechanism	(comment: assayed complex)
PMID:37459529	GO:0180033	histone H4K8 deacetylase activity, hydrolytic mechanism	(comment: assayed complex)
PMID:37459529	GO:0032221	Rpd3S complex	All six subunits of the Clr6S complex are seen in the map (Fig. 2 B and C and SI Appendix, Table S1). Unexpectedly, the structure also reveals two copies of Alp13 (hereafter referred to as Alp13a and Alp13b) (Fig. 2C)
PMID:37459529	GO:0032221	Rpd3S complex	Alp13b is connected to the complex by both Cph1 and Cph2 (Figs. 2C and 3A)
PMID:37459529	GO:0032221	Rpd3S complex	Alp13b is connected to the complex by both Cph1 and Cph2 (Figs. 2C and 3A)
PMID:37459529	FYPO:0003704	decreased histone deacetylase activity [assayed_enzyme] PomBase:SPBC36.05c	Deletion of the active center loop compromised the HDAC activity of Clr6S (Fig. 6G), consistent with a role of the loop in catalytic activity, although a secondary effect, due to perturbation of the protein structure could not be excluded.
PMID:37459529	GO:0060090	molecular adaptor activity	Pst2 evidently serves as a structural platform, bringing together almost all the other subunits of the complex.
PMID:37459529	GO:0032221	Rpd3S complex	The structure shows that Pst2, Clr6, and Prw1, a WD40-containing subunit, form a subcomplex, within which Pst2 associates with the catalytic subunit Clr6, as well as interacting with Prw1 (Fig. 2C)
PMID:37459529	GO:0032221	Rpd3S complex	The structure shows that Pst2, Clr6, and Prw1, a WD40-containing subunit, form a subcomplex, within which Pst2 associates with the catalytic subunit Clr6, as well as interacting with Prw1 (Fig. 2C)
PMID:37459529	GO:0060090	molecular adaptor activity	Thus, Cph2 interacts with all the other subunits except Prw1, whose association with the complex occurs only through the Pst2-CTD (Fig. 4C).
PMID:37459529	GO:0032221	Rpd3S complex	Unexpectedly, the structure also reveals two copies of Alp13 (hereafter referred to as Alp13a and Alp13b) (Fig. 2C)
PMID:37531259	GO:0017024	myosin I binding [occurs_in] cytoplasm [part_of] endocytosis	(Fig. 1, 1B, 2D)
PMID:37531259	FYPO:0000744	normal protein localization to actin cortical patch [assayed_protein] PomBase:SPBC1778.06c	(Figure 1C)
PMID:37531259	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPAC3A12.14	(Figure 1C)
PMID:37531259	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC3A12.14	(Figure 1C)
PMID:37531259	GO:0051285	cell cortex of cell tip	(Figure 1C)
PMID:37531259	GO:0051285	cell cortex of cell tip	(Figure 1C)
PMID:37531259	FYPO:0006344	protein mislocalized to plasma membrane during vegetative growth [assayed_protein] PomBase:SPBC146.13c	(Figure 1C)
PMID:37531259	FYPO:0006344	protein mislocalized to plasma membrane during vegetative growth [assayed_protein] PomBase:SPAC3A12.14	(Figure 1C)
PMID:37531259	FYPO:0006344	protein mislocalized to plasma membrane during vegetative growth [assayed_protein] PomBase:SPAC29A4.05	(Figure 1C)
PMID:37531259	FYPO:0001366	normal actin cytoskeleton organization	(Figure 1C)
PMID:37531259	GO:0061645	endocytic patch	(Figure 1C,F)
PMID:37531259	FYPO:0000422	decreased endocytosis during vegetative growth [assayed_protein] PomBase:SPBC1778.06c [has_severity] medium	(Figure 1D)
PMID:37531259	FYPO:0002151	inviable spore [has_penetrance] 100	(Figure 1E)
PMID:37531259	FYPO:0002151	inviable spore [has_penetrance] 100	(Figure 1E)
PMID:37531259	GO:0005737	cytoplasm	(Figure 1F)
PMID:37531259	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPBC1778.06c	(Figure 3A)
PMID:37531259	FYPO:0006552	increased protein localization to cytoplasm [assayed_protein] PomBase:SPBC146.13c	(Figure 3A) in myo1-mNG fim1-mCherry cells overproducing Ank1, while Fim1-mCherry was at patches, almost all Myo1-mNG was cytoplasmic (Fig. 3A).
PMID:37531259	FYPO:0000422	decreased endocytosis during vegetative growth [assayed_protein] PomBase:SPBC1778.06c [has_severity] high	(Figure 3B) Furthermore, in cells overproducing ank1+, ~10% of Fim1-mCherry patches internalized compared to ~95% of Fim1-mCherry patches internalized in the control cells (Fig. 3B)
PMID:37531259	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC105.02c [assayed_protein] PomBase:SPBC146.13c	(Figure 3C)
PMID:37531259	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC105.02c [assayed_protein] PomBase:SPBC146.13c	(Figure 3C)
PMID:37531259	FYPO:0000422	decreased endocytosis during vegetative growth [assayed_protein] PomBase:SPBC1778.06c [has_severity] medium	(Figure 3E)
PMID:37531259	FYPO:0000422	decreased endocytosis during vegetative growth [assayed_protein] PomBase:SPBC1778.06c [has_severity] medium	(Figure 3E)
PMID:37531259	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC105.02c [assayed_protein] PomBase:SPAC3A12.14	(Figure S1A)
PMID:37531259	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC105.02c [assayed_protein] PomBase:SPAC29A4.05	(Figure S1B)
PMID:37531259	FYPO:0000744	normal protein localization to actin cortical patch [assayed_protein] PomBase:SPAC4F10.15c	(Figure S1C)
PMID:37531259	FYPO:0000744	normal protein localization to actin cortical patch	(Figure S1C)
PMID:37531259	FYPO:0004085	decreased vegetative cell growth	(Figure S1D)
PMID:37531259	FYPO:0004085	decreased vegetative cell growth	(Figure S1D)
PMID:37531259	FYPO:0004085	decreased vegetative cell growth	(Figure S1D)
PMID:37531259	FYPO:0004085	decreased vegetative cell growth	(Figure S1D)
PMID:37531259	FYPO:0001357	normal vegetative cell population growth	(Figure S1D) (comment: vw: same pathway)
PMID:37531259	GO:0008289	lipid binding	(comment: vw: I think we can conclude this from the EXP, especially as we know that myo1 binds phopshilipids in other species) Addition of Ank1 resulted in a reduction in the amount of co-pelleting of the Myo1(1-964)-FLAG-Cam1-Cam2 complex with liposomes (Fig. 2F). We therefore conclude that Ank1 directly binds and inhibits Myo1 membrane binding, supporting our model.
PMID:37531259	GO:0140311	protein sequestering activity [has_input] PomBase:SPBC146.13c [occurs_in] cytoplasm	Given the AF model and the above results, we hypothesized that Ank1 In contrast, in myo1-mNG fim1-mCherry cells overproducing Ank1, while Fim1-mCherry was at patches, almost all Myo1-mNG was cytoplasmic (Fig. 3A). These data support our model that Ank1 blocks Myo1 membrane association and normally sequesters the bulk of Myo1 in the cytoplasm.precludes Myo1 membrane binding and sequesters the myosin-1 complex in the cytoplasm (Fig. 2F).Addition of Ank1 resulted in a reduction in the amount of co-pelleting of the Myo1(1-964)-FLAG-Cam1-Cam2 complex with liposomes (Fig. 2F). We therefore conclude that Ank1 directly binds and inhibits Myo1 membrane binding, supporting our model.
PMID:37540145	FYPO:0003807	net-like mitochondrial morphology [has_penetrance] ~70	(Figure 4F) (comment: mitochondrial net-like morphology)
PMID:37540145	FYPO:0003807	net-like mitochondrial morphology [has_penetrance] ~85	(Figure 4F) (comment: mitochondrial net-like morphology)
PMID:37540145	FYPO:0008067	constricted chained mitochondrion [has_penetrance] ~30	(Figure 4G)
PMID:37540145	FYPO:0008067	constricted chained mitochondrion [has_penetrance] ~15	(Figure 4G)
PMID:37540145	GO:0000266	mitochondrial fission	Thus, our data indicate that Mdi1 plays a conserved role as a profission factor that is not required for Dnm1 recruitment but is required to facilitate the completion of mitochondrial division. Fig 4
PMID:37540145	FYPO:0003768	normal protein localization to mitochondrion [assayed_protein] PomBase:SPBC12C2.08	loss of Mdi1 did not impact Dnm1 recruitment to mitochondria and Dnm1 foci appeared associated with the hyperfused net structures (Fig. 4 F, arrows).
PMID:37550452	FYPO:0002061	inviable vegetative cell population	(Figure 5)
PMID:37550452	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 5)
PMID:37550452	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 5)
PMID:37550452	FYPO:0005011	decreased histone H4 acetylation during vegetative growth [has_severity] variable severity	(Figure 6)
PMID:37550452	FYPO:0005011	decreased histone H4 acetylation during vegetative growth [has_severity] medium	(Figure 6)
PMID:37550452	FYPO:0005011	decreased histone H4 acetylation during vegetative growth [has_severity] low	(Figure 6)
PMID:37550452	FYPO:0005011	decreased histone H4 acetylation during vegetative growth [has_severity] high	(Figure 6)
PMID:37550452	FYPO:0002430	inviable after spore germination, multiple cell divisions [has_penetrance] 100	Extended Data Figure 9e
PMID:37553386	FYPO:0007448	normal reticulophagy during nitrogen starvation	(Fig. 1B and C)
PMID:37553386	FYPO:0007447	abolished reticulophagy during cellular response to endoplasmic reticulum stress [has_penetrance] complete	(Fig. 1B and C)
PMID:37553386	FYPO:0008084	abolished reticulophagy during nitrogen starvation [has_penetrance] complete	(Fig. 1B and C)
PMID:37553386	FYPO:0007447	abolished reticulophagy during cellular response to endoplasmic reticulum stress [has_penetrance] complete	(Fig. 1B and C)
PMID:37553386	FYPO:0007447	abolished reticulophagy during cellular response to endoplasmic reticulum stress [has_penetrance] medium	(Fig. 1B and C)
PMID:37553386	FYPO:0008084	abolished reticulophagy during nitrogen starvation [has_penetrance] complete	(Fig. 1B and C)
PMID:37553386	GO:0098826	endoplasmic reticulum tubular network membrane [exists_during] single-celled organism vegetative growth phase	(Fig. 1B)
PMID:37553386	FYPO:0000381	decreased macroautophagy	(Fig. 1D and E)
PMID:37553386	FYPO:0001357	normal vegetative cell population growth	(Fig. 1F)
PMID:37553386	FYPO:0001030	normal growth on dithiothreitol	(Fig. 1F)
PMID:37553386	FYPO:0001030	normal growth on dithiothreitol	(Fig. 1F)
PMID:37553386	FYPO:0000843	sensitive to dithiothreitol [has_severity] high	(Fig. 1F)
PMID:37553386	FYPO:0000843	sensitive to dithiothreitol [has_severity] high	(Fig. 1F)
PMID:37553386	FYPO:0000843	sensitive to dithiothreitol [has_severity] high	(Fig. 1F)
PMID:37553386	FYPO:0001357	normal vegetative cell population growth	(Fig. 1F)
PMID:37553386	FYPO:0001357	normal vegetative cell population growth	(Fig. 1F)
PMID:37553386	FYPO:0001357	normal vegetative cell population growth	(Fig. 1F)
PMID:37553386	FYPO:0001357	normal vegetative cell population growth	(Fig. 1F)
PMID:37553386	FYPO:0007596	decreased mitophagy during nitrogen starvation [has_severity] high	(Fig. 1G)
PMID:37553386	FYPO:0007596	decreased mitophagy during nitrogen starvation [has_severity] high	(Fig. 1G)
PMID:37553386	FYPO:0006376	decreased protein processing during nitrogen starvation [has_severity] medium [assayed_protein] PomBase:SPBC1709.05	(Fig. 2C)
PMID:37553386	FYPO:0006376	decreased protein processing during nitrogen starvation [has_severity] high [assayed_protein] PomBase:SPBC1709.05	(Fig. 2C)
PMID:37553386	FYPO:0000381	decreased macroautophagy [has_severity] high	(Fig. 3G)
PMID:37553386	FYPO:0000843	sensitive to dithiothreitol [has_severity] high	(Fig. 5A)
PMID:37553386	FYPO:0000843	sensitive to dithiothreitol [has_severity] high	(Fig. 5A)
PMID:37553386	FYPO:0000843	sensitive to dithiothreitol [has_severity] medium	(Fig. 5A)
PMID:37553386	FYPO:0001030	normal growth on dithiothreitol	(Fig. 5A)
PMID:37553386	FYPO:0001030	normal growth on dithiothreitol	(Fig. 5A)
PMID:37553386	FYPO:0001030	normal growth on dithiothreitol	(Fig. 5A)
PMID:37553386	FYPO:0000843	sensitive to dithiothreitol [has_severity] low	(Fig. 5A)
PMID:37553386	FYPO:0000843	sensitive to dithiothreitol [has_severity] low	(Fig. 5A)
PMID:37553386	FYPO:0008197	decreased reticulophagy during vegetative growth [has_severity] high	(Fig. 5B)
PMID:37553386	FYPO:0008197	decreased reticulophagy during vegetative growth [has_severity] medium	(Fig. 5B)
PMID:37553386	FYPO:0008197	decreased reticulophagy during vegetative growth [has_severity] low	(Fig. 5B)
PMID:37553386	FYPO:0008197	decreased reticulophagy during vegetative growth [has_severity] high	(Fig. 5B)
PMID:37553386	GO:0061908	phagophore [exists_during] cellular response to starvation	(Fig. 6)
PMID:37553386	GO:0061908	phagophore [exists_during] cellular response to starvation	(Fig. 6)
PMID:37553386	FYPO:0000355	normal endoplasmic reticulum morphology	(Fig. S2D)
PMID:37553386	FYPO:0000526	decreased peroxisome degradation [has_severity] high	(Fig. S2G and H)
PMID:37553386	FYPO:0000526	decreased peroxisome degradation [has_severity] high	(Fig. S2G and H)
PMID:37553386	GO:0180020	membrane bending activity [part_of] macroautophagy	Assayed using S. japonicus rop1 in vitro. Fig. 4
PMID:37553386	GO:0180020	membrane bending activity [part_of] endoplasmic reticulum tubular network organization [occurs_in] endoplasmic reticulum tubular network	Assayed using S. japonicus yop1 in vitro. Fig. 4
PMID:37572670	FYPO:0002680	increased protein phosphorylation [assayed_protein] PomBase:SPAC24B11.06c	(Figure 1) Strikingly, Sty1 phosphorylation was increased in cells expressing either Sty1-Tpx1 or Sty1-Tpx1C48S (Figure 1D)
PMID:37572670	FYPO:0002680	increased protein phosphorylation [assayed_protein] PomBase:SPAC24B11.06c	(Figure 1) Strikingly, Sty1 phosphorylation was increased in cells expressing either Sty1-Tpx1 or Sty1-Tpx1C48S (Figure 1D)
PMID:37572670	FYPO:0002680	increased protein phosphorylation [assayed_protein] PomBase:SPBC409.07c	(Figure 3) Sty1-Tpx1 fusion proteins, Wis1 was hyperphosphorylated to less electrophoretically mobile forms even in the absence of stress (Figures 3A and 3D).
PMID:37572670	GO:1900745	positive regulation of p38MAPK cascade [happens_during] cellular response to oxidative stress	(comment: CHECK Tpx1 is required for H2O2-induced activation of Sty1, over a range of concentrations up to 10 mM H2O2.31)
PMID:37572670	FYPO:0002680	increased protein phosphorylation [assayed_protein] PomBase:SPAC24B11.06c [has_severity] low	Although expression of Sty-Tpx1C48S stimulated a bigger increase in Sty1 activity in cells expressing wild-type Wis1, expression of Sty1-Tpx1C48S also increased Sty1 phosphorylation and partially rescued the cell-cycle defect of Wis1AA cells (Figures 4B and 4C)
PMID:37572670	FYPO:0007620	decreased protein phosphorylation during cellular response to oxidative stress [assayed_protein] PomBase:SPAC24B11.06c	Although, both Wis1M395G and Wis1M395A were expressed at wild-type levels, Sty1 phosphorylation was very low and minimally increased even in response to 6 mM H2O2 in these cells (Figure 4D).
PMID:37572670	FYPO:0007620	decreased protein phosphorylation during cellular response to oxidative stress [assayed_protein] PomBase:SPAC24B11.06c	Although, both Wis1M395G and Wis1M395A were expressed at wild-type levels, Sty1 phosphorylation was very low and minimally increased even in response to 6 mM H2O2 in these cells (Figure 4D).
PMID:37572670	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC24B11.06c	As expected, Sty1 phosphorylation was increased in Dpyp1 mutant cells, confirming the importance of this phosphatase in maintaining low levels of Sty1 activity (Figure 2A)
PMID:37572670	FYPO:0002680	increased protein phosphorylation [assayed_protein] PomBase:SPAC19D5.01	By contrast, cells expressing Sty1-Tpx1C48S contained substantially increased levels of lower mobility and phosphorylated Pyp2 (p-Pyp2), even prior to addition of H2O2. Together these data strongly support the conclusion that the Sty1-Tpx1 and Sty1-Tpx1C48S fusion proteins are constitutively hyperactive compared with wild-type Sty1 (Figures 1F and 1G).
PMID:37572670	FYPO:0003692	increased protein phosphorylation during cellular response to oxidative stress [assayed_protein] PomBase:SPAC24B11.06c	By contrast, overexpression of Tpx1 increased H2O2-induced Sty1 phosphorylation in wild-type cells and also restored some H2O2-inducibility to Sty1 phosphorylation in Dpyp2 cells (Figures 2A and S3E).
PMID:37572670	FYPO:0007620	decreased protein phosphorylation during cellular response to oxidative stress [assayed_protein] PomBase:SPAC24B11.06c [has_severity] low	By contrast, overexpression of Tpx1 increased H2O2-induced Sty1 phosphorylation in wild-type cells and also restored some H2O2-inducibility to Sty1 phosphorylation in Dpyp2 cells (Figures 2A and S3E).
PMID:37572670	FYPO:0007620	decreased protein phosphorylation during cellular response to oxidative stress [assayed_protein] PomBase:SPAC24B11.06c [has_severity] low	Consistent with Pyp1 oxidation providing a similar mechanism to reversibly inhibit Pyp1 and activate Sty1, there was a much smaller H2O2-induced increase in Sty1 phosphorylation in Dtrx1 mutant cells, where H2O2-induced Pyp1 disulfides were not detected (Figures 2D and 2F).
PMID:37572670	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC26F1.10c	Consistent with lower Sty1 activity, Sty15CS-expressing cells contained less Pyp1 than wild-type cells (Figure S1F). This likely explains the slightly elevated phosphorylation of Sty15CS (Figure S1G)
PMID:37572670	FYPO:0000726	sensitive to oxidative stress [has_severity] low	Crucially, both Sty1-Tpx1 fusions were expressed at similar levels to wild-type Sty1 and supported growth under stress conditions, confirming retention of Sty1 function (Figures 1B and 1D). By contrast, the oxidative stress sensitivity and lower Pyp1 levels in cells expressing a Sty15CS-Tpx1 fusion protein, provided further evidence that cysteines in Sty1 are required for Sty1 function independently from forming disulfide-bonded complexes with Tpx1 (Figures 1B and S1F).39
PMID:37572670	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	Dmcs4 mutant cells are delayed in entry to mitosis, reaching a significantly longer size than wild-type cells before dividing (Figure 5A).45,47,48
PMID:37572670	FYPO:0009007	decreased vegetative cell population viability	Hence, the lower viability of cells co-expressing sty1-tpx1 and wis1DD suggested a synthetic negative interaction, with both alleles acting independently to increase Sty1 phosphorylation to lethal levels.
PMID:37572670	FYPO:0001122	elongated vegetative cell	Indeed, consistent with the requirement of Wis1-dependent phosphorylation of Sty1 for timely entry into mitosis, cells expressing Wis1M395G or Wis1M395A were elongated (Figure S6B).
PMID:37572670	FYPO:0001122	elongated vegetative cell	Indeed, consistent with the requirement of Wis1-dependent phosphorylation of Sty1 for timely entry into mitosis, cells expressing Wis1M395G or Wis1M395A were elongated (Figure S6B).
PMID:37572670	FYPO:0003692	increased protein phosphorylation during cellular response to oxidative stress [assayed_protein] PomBase:SPBC409.07c	Indeed, our analysis of Dtpx1 mutant cells indicated that Tpx1 was important for maximal Wis1 phosphorylation (pppWis1) in response to 6 mM H2O2 (Figures 3C, S4E, and S4F).
PMID:37572670	FYPO:0001122	elongated vegetative cell	Indeed, our examination indicated that ‘‘sty1-tpx1 wis1DD’’ strains, which genotypically bore both alleles, had adapted to the deleterious effect of hyperactivated Sty1 by lowering Sty1 expression to such an extent that they exhibited the long cell phenotype associated with its loss (Figures S3A and S3B).
PMID:37572670	FYPO:0002059	inviable cell population	Moreover, when we crossed strains expressing Sty1-Tpx1 fusion and Dpyp1 mutant alleles, we observed a very strong synthetic lethal interaction, with 95% of spores with a sty1-tpx1 Dpyp1 genotype failing to give rise to a colony (Figure 2I and not shown). This strongly suggests that sty1- tpx1 and Dpyp1 alleles act independently to increase Sty1 phosphorylation, thus increasing it to lethal levels when co-expressed. Indeed, analysis of colonies bearing markers of both alleles revealed that surviving cells had completely eliminated Sty1-Tpx1 expression and activity (Figures 2J and 2K and not shown).
PMID:37572670	FYPO:0002059	inviable cell population	Moreover, when we crossed strains expressing Sty1-Tpx1 fusion and Dpyp1 mutant alleles, we observed a very strong synthetic lethal interaction, with 95% of spores with a sty1-tpx1 Dpyp1 genotype failing to give rise to a colony (Figure 2I and not shown). This strongly suggests that sty1- tpx1 and Dpyp1 alleles act independently to increase Sty1 phosphorylation, thus increasing it to lethal levels when co-expressed. Indeed, analysis of colonies bearing markers of both alleles revealed that surviving cells had completely eliminated Sty1-Tpx1 expression and activity (Figures 2J and 2K and not shown).
PMID:37572670	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	Next, we co-expressed the Sty1-Tpx1C48S fusion with a Wis1AA mutant, in which the MAP3K-phosphorylated residues are substituted with alanine. Wis1AA cells are significantly elongated, reflecting the mitotic delay associated with Sty1 hypophosphorylation (Figures 4B, 4C, and S6A).50
PMID:37572670	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	Next, we co-expressed the Sty1-Tpx1C48S fusion with a Wis1AA mutant, in which the MAP3K-phosphorylated residues are substituted with alanine. Wis1AA cells are significantly elongated, reflecting the mitotic delay associated with Sty1 hypophosphorylation (Figures 4B, 4C, and S6A).50
PMID:37572670	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	Our analysis revealed that Sty15CS-mutant-expressing cells were longer at the point of division than wild-type cells, strongly suggesting that Sty15CS’s promitotic function was compromised (Figures S1D and S1E).
PMID:37572670	FYPO:0007620	decreased protein phosphorylation during cellular response to oxidative stress [assayed_protein] PomBase:SPAC24B11.06c	Significantly, this stress-induced increase in Wis1DD phosphorylation was mirrored by stress-induced increases in Sty1 phosphorylation, strongly suggesting that it increases Wis1 activity (Figure 4A).
PMID:37572670	FYPO:0007620	decreased protein phosphorylation during cellular response to oxidative stress [assayed_protein] PomBase:SPBC409.07c	Strikingly, the stress-induced phosphorylation of Wis1M395G and Wis1M395A was also compromised, strongly suggesting that Wis1 kinase activity was required for the stress-induced phosphorylation and activation of Wis1 (Figure 4D).
PMID:37572670	FYPO:0007620	decreased protein phosphorylation during cellular response to oxidative stress [assayed_protein] PomBase:SPBC409.07c	Strikingly, the stress-induced phosphorylation of Wis1M395G and Wis1M395A was also compromised, strongly suggesting that Wis1 kinase activity was required for the stress-induced phosphorylation and activation of Wis1 (Figure 4D).
PMID:37572670	GO:0005078	MAP kinase scaffold activity	Sty1-Tpx1 complexes provide a scaffold for Wis1
PMID:37572670	FYPO:0000544	abolished protein modification during vegetative growth [assayed_protein] PomBase:SPCC576.03c [assayed_protein] PomBase:SPAC24B11.06c	Sty1-Tpx1 disulfide formation abrogated (Figure S1C).
PMID:37572670	FYPO:0002680	increased protein phosphorylation [assayed_protein] PomBase:SPBC409.07c	Sty1-Tpx1 expression stimulated similar levels of constitutive Wis1 phosphorylation in Dmcs4 mutant as in wild-type (mcs4+) cells (Figure 5B). Accordingly, there were similar levels of Sty1 phosphorylati
PMID:37572670	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	Sty15CS-expressing cells were able to adapt to osmotic stress but were less tolerant than wild-type cells to higher levels of H2O2 (Figure 1B).
PMID:37572670	FYPO:0005947	normal growth on potassium chloride	Sty15CS-expressing cells were able to adapt to osmotic stress but were less tolerant than wild-type cells to higher levels of H2O2 (Figure 1B).
PMID:37572670	FYPO:0006822	viable small vegetative cell with normal cell growth rate	This revealed that Sty1- Tpx1- and Sty1-Tpx1C48S-expressing cells both divided at a significantly smaller size than wild-type cells (Figure 1F).
PMID:37572670	FYPO:0006822	viable small vegetative cell with normal cell growth rate	This revealed that Sty1- Tpx1- and Sty1-Tpx1C48S-expressing cells both divided at a significantly smaller size than wild-type cells (Figure 1F).
PMID:37572670	FYPO:0007620	decreased protein phosphorylation during cellular response to oxidative stress [assayed_protein] PomBase:SPBC409.07c	We observed a small, but reproducible, stress-induced decrease in Wis1DD mobility in these cells, corroborating that Wis1 undergoes a stressinduced phosphorylation on different sites from those phosphorylated by the MAP3K (Figures 4A, S5A, S4A, S4B, and S4F).
PMID:37590302	FYPO:0007194	mitochondria present in increased numbers	(Figure 1)
PMID:37590302	FYPO:0003810	small fragmented mitochondria present in increased numbers	(Figure 1)
PMID:37590302	FYPO:0007197	increased mitochondrial fission	(Figure 1F and 1G) Analysis by live-cell microscopy further showed that both fission and fusion frequencies increased significantly in cells lacking Yta4
PMID:37590302	FYPO:0008122	increased mitochondrial fusion	(Figure 1F and 1G) Analysis by live-cell microscopy further showed that both fission and fusion frequencies increased significantly in cells lacking Yta4
PMID:37590302	FYPO:0007197	increased mitochondrial fission	(Figure 1F and 1G) Analysis by live-cell microscopy further showed that both fission and fusion frequencies increased significantly in cells lacking Yta4
PMID:37590302	FYPO:0007600	decreased protein localization to mitochondrial outer membrane [assayed_protein] PomBase:SPBC12C2.08	As shown in Figs 4D and S1C, overexpression of WT Yta4 impaired the formation of Dnm1 foci on mitochondria but did not change the tubular mitochondrial morphology.
PMID:37590302	GO:0005095	GTPase inhibitor activity [has_input] PomBase:SPBC12C2.08 [part_of] negative regulation of mitochondrial fission [occurs_in] cytoplasmic side of mitochondrial outer membrane	Hence, these results show the characteristic property of Yta4 in reducing the affinity of Dnm1 for GTP and in inhibiting Dnm1 assembly.
PMID:37590302	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC12C2.08	Quantification showed that the expression levels of endogenous Dnm1 were comparable in WT and yta4Δ cells (Fig 3B)
PMID:37590302	FYPO:0001531	decreased GTPase activity	To reduce the complexity in analyzing Dnm1 GTPase activity, we performed colorimetric assays by using the assembly-defective version of Dnm1 (i.e., Dnm1(G380D), see S6A Fig). Interestingly, Dnm1(G380D) still exhibited a GTPase activity but has a very low rate of GTP hydrolysis (Km = 85.00 μM, Vmax = 1.02 μM/min, versus the control Dnm1(WT): Km = 126.59 μM, Vmax = 4.82 μM/min) (S8 Fig).
PMID:37590302	FYPO:0000895	mitochondrial aggregation	Yta4(EQ) impaired the formation of Dnm1 foci on mitochondria but unexpectedly caused mitochondria to aggregate (Figs 4D and S1C)
PMID:37590302	FYPO:0003768	normal protein localization to mitochondrion [assayed_protein] PomBase:SPBC11G11.01	showed that the delocalized GFP-Fis1 appeared to be present in the cytoplasm of Yta4-overexpressing cells, while GFP-Fis1 in Yta4(AA)-overexpressing or Yta4 (EQ)-overexpressing cells was still present on mitochondria, which were clearly separated from the ER (S1D and S2 Figs).
PMID:37590302	FYPO:0003768	normal protein localization to mitochondrion [assayed_protein] PomBase:SPBC11G11.01	showed that the delocalized GFP-Fis1 appeared to be present in the cytoplasm of Yta4-overexpressing cells, while GFP-Fis1 in Yta4(AA)-overexpressing or Yta4 (EQ)-overexpressing cells was still present on mitochondria, which were clearly separated from the ER (S1D and S2 Figs).
PMID:37590302	FYPO:0000897	normal mitochondrial fission	the expression of Yta4(WT), Yta4(AA), or Yta4(EQ) from the yta4 promoter restored Dnm1-associated mitochondrial fission to the WT level in yta4∆ cells (S3D Fig)
PMID:37590302	FYPO:0000897	normal mitochondrial fission	the expression of Yta4(WT), Yta4(AA), or Yta4(EQ) from the yta4 promoter restored Dnm1-associated mitochondrial fission to the WT level in yta4∆ cells (S3D Fig)
PMID:37615341	FYPO:0006603	decreased replication fork arrest at RTS1 barrier	(Fig. 1)
PMID:37615341	FYPO:0001357	normal vegetative cell population growth	(Fig. 2-S1A)
PMID:37615341	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 2-S1A)
PMID:37615341	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 2-S1A)
PMID:37615341	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 2-S1A)
PMID:37615341	FYPO:0000963	normal growth on hydroxyurea	(Fig. 2-S1A)
PMID:37615341	FYPO:0000963	normal growth on hydroxyurea	(Fig. 2-S1A)
PMID:37615341	FYPO:0000963	normal growth on hydroxyurea	(Fig. 2-S1A)
PMID:37615341	FYPO:0001357	normal vegetative cell population growth	(Fig. 2-S1A)
PMID:37615341	FYPO:0001357	normal vegetative cell population growth	(Fig. 2-S1A)
PMID:37615341	FYPO:0008113	increased intron retention [assayed_transcript] PomBase:SPAC22F8.07c	(Fig. 3C and D)
PMID:37615341	FYPO:0005353	normal replication fork arrest at RTS1 barrier	(Fig. 4)
PMID:37615341	FYPO:0005353	normal replication fork arrest at RTS1 barrier	(Fig. 4)
PMID:37615341	FYPO:0005353	normal replication fork arrest at RTS1 barrier	(Fig. 4)
PMID:37615341	FYPO:0002799	normal protein degradation [assayed_protein] PomBase:SPAC1D4.09c	This further suggests that Mud1 is not playing the same role in regulating Rtf2 in S. pombe as has been observed for DDI1/2 in human cells. Fig. 2-S1B
PMID:37615341	FYPO:0006603	decreased replication fork arrest at RTS1 barrier	expression of an intron-less rtf1 gene that encodes the same additional 15 amino acids between residues 202-203 (Rtf1 intron2NE) does not provoke increased replication slippage downstream of RTS1 (Figure 4—Figure supplement 3), indicating that this protein is indeed dysfunctional.
PMID:37637271	FYPO:0002061	inviable vegetative cell population	(Figure 1D)
PMID:37637271	FYPO:0002061	inviable vegetative cell population	(Figure 1D)
PMID:37637271	FYPO:0001355	decreased vegetative cell population growth	(Figure 1E)
PMID:37637271	FYPO:0001235	decreased extent of cell population growth	(Figure 1E)
PMID:37637271	FYPO:0001235	decreased extent of cell population growth	(Figure 1E)
PMID:37637271	FYPO:0001355	decreased vegetative cell population growth	(Figure 1E)
PMID:37637271	FYPO:0001355	decreased vegetative cell population growth	(Figure 1E)
PMID:37637271	FYPO:0001355	decreased vegetative cell population growth	(Figure 1E)
PMID:37637271	FYPO:0001355	decreased vegetative cell population growth	(Figure 1E)
PMID:37637271	FYPO:0001355	decreased vegetative cell population growth	(Figure 1E)
PMID:37637271	FYPO:0001355	decreased vegetative cell population growth	(Figure 1G)
PMID:37637271	FYPO:0001355	decreased vegetative cell population growth	(Figure 1G)
PMID:37637271	FYPO:0000964	normal growth on thiabendazole	(Figure 1H)
PMID:37637271	FYPO:0000964	normal growth on thiabendazole	(Figure 1H)
PMID:37637271	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Figure 1H)
PMID:37637271	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Figure 1H)
PMID:37694715	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	(Fig. 5B)
PMID:37694715	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	(Fig. 5C and D)
PMID:37694715	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	(Fig. S1)
PMID:37694715	GO:0016020	membrane	(comment: Bqt4 is an integral membrane protein)
PMID:37694715	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	GFP-Bqt4 fluorescence in the nuclei of both bqt3+ and bqt3Δ cells was elevated (Fig. 1A)
PMID:37694715	FYPO:0004887	normal protein localization to nuclear envelope during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	The Bqt4 fragment containing the helix domain and the adjacent intrinsically disordered sequence (Bqt4C369-432) reproduced the behavior of full-length Bqt4 (Fig. 1A), that is, localization to the NE and responses to BZ, both in the presence and absence of Bqt3 (Fig. 6A, Bqt4C369-432).
PMID:37694715	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC19C7.10	The Bqt4 fragment containing the helix domain and the adjacent intrinsically disordered sequence (Bqt4C369-432) reproduced the behavior of full-length Bqt4 (Fig. 1A), that is, localization to the NE and responses to BZ, both in the presence and absence of Bqt3 (Fig. 6A, Bqt4C369-432).
PMID:37694715	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC19C7.10	The TMD alone (Bqt4C414-432) showed even weaker localization at the NE with diffusion to the cytoplasm, but showed the same responses, that is, degradation in the absence of Bqt3 and increased levels upon BZ treatment (Fig. 6A, Bqt4C414-432).
PMID:37694715	FYPO:0007073	decreased protein localization to nuclear envelope during vegetative growth [assayed_protein] PomBase:SPBC19C7.10 [has_severity] medium	The TMD alone (Bqt4C414-432) showed even weaker localization at the NE with diffusion to the cytoplasm, but showed the same responses, that is, degradation in the absence of Bqt3 and increased levels upon BZ treatment (Fig. 6A, Bqt4C414-432).
PMID:37694715	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC19C7.10	The fragment Bqt4C369-425 lost its dependency on Bqt3 for degradation and exhibited similar behaviors in the presence or absence of Bqt3 (Fig. 6A, Bqt4C369-425):
PMID:37694715	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC19C7.10	The fragment Bqt4C369-425 lost its dependency on Bqt3 for degradation and exhibited similar behaviors in the presence or absence of Bqt3 (Fig. 6A, Bqt4C369-425):
PMID:37694715	FYPO:0007073	decreased protein localization to nuclear envelope during vegetative growth [assayed_protein] PomBase:SPBC19C7.10 [has_severity] low	The helix domain alone (Bqt4C394-432) showed weaker localization to the NE and was somewhat diffused to the membrane compartments in the cytoplasm; (Fig. 6A, Bqt4C394-432)
PMID:37694715	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPCC594.07c [assayed_protein] PomBase:SPBC19C7.10	The results of the yeast-two-hybrid assay showed that the fragments lacking the last seven residues did not bind to Bqt3 (Fig. 6B).
PMID:37694715	GO:0005637	nuclear inner membrane	These results are consistent with previous studies that showed that Doa10 partially localizes to the INM and is involved in the degradation of certain nuclear and INM substrates, whereas Hrd1 is found exclusively in the ER (Deng and Hochstrasser, 2006; Boban et al., 2014).
PMID:37694715	FYPO:0000769	abnormal nuclear envelope morphology during vegetative growth	To ascertain whether this abnormal phenotype was caused by an accumulation of Bqt4, we overexpressed GFP-Bqt4 under the nmt1 promoter using the chemical compound YAM2 to control the expression level. YAM2 suppresses nmt1 promoter activity depending on its concentration (Nakamura et al., 2011). Overexpression of GFP-Bqt4 reproduced the nuclear-deformed morphology (Fig. 7B)
PMID:37694715	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	To confirm this result, we measured protein levels by western blotting, which consistently showed an increase in GFP-Bqt4 protein levels in these strains upon proteasomal inhibition by BZ Fig. 1B
PMID:37694715	FYPO:0002774	increased level of ubiquitinated protein in cell during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	Ubiquitinated forms of Bqt4 were detected in bqt3Δ cells and were enriched in both bqt3+ and bqt3Δ cells when proteasomal activity was inhibited (Fig. 1E), suggesting that Bqt4 was targeted to the proteasome by polyubiquitin modification.
PMID:37694715	MOD:01148	ubiquitinylated lysine	Ubiquitinated forms of Bqt4 were detected in bqt3Δ cells and were enriched in both bqt3+ and bqt3Δ cells when proteasomal activity was inhibited (Fig. 1E), suggesting that Bqt4 was targeted to the proteasome by polyubiquitin modification.
PMID:37694715	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	We confirmed it by microscopy as well. Fig 1C and D.
PMID:37694715	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	We confirmed it by microscopy as well. Fig 2A and B. We found that GFP-Bqt4 degradation was suppressed in cut8-563 cells shifted to the nonpermissive temperature of 36°C (Fig. 2A,B).
PMID:37694715	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	We confirmed it by microscopy as well. Fig 3A and B. Deletion of doa10+ partially restored GFP-Bqt4 levels in the absence of Bqt3, whereas deletion of hrd1+ did not (Fig. 3A,B, comparing hrd1Δ to doa10Δ)
PMID:37694715	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	We confirmed it by microscopy as well. Fig 3C and D. We also measured the amount of GFP-Bqt4 in mutants lacking Ubc6 and Ubc7, which are E2 ubiquitin-conjugating enzymes associated with Doa10 (Swanson et al., 2001). We found that GFP-Bqt4 levels increased to some extent in ubc6Δ and ubc7Δ single and ubc6Δ ubc7Δ double mutants (Fig. 3C,D).
PMID:37694715	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	We confirmed it by microscopy as well. Fig 3C and D. We also measured the amount of GFP-Bqt4 in mutants lacking Ubc6 and Ubc7, which are E2 ubiquitin-conjugating enzymes associated with Doa10 (Swanson et al., 2001). We found that GFP-Bqt4 levels increased to some extent in ubc6Δ and ubc7Δ single and ubc6Δ ubc7Δ double mutants (Fig. 3C,D).
PMID:37694715	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	We constructed mutants of E3 ligases and their components that have been suggested to localize to or function in the ER and nucleus, namely ......... The mutants tested showed no detectable increase in fluorescence, except for the hul5Δ mutant (Fig. S2)
PMID:37694715	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPBC19C7.10	nevertheless, this fragment was degraded in the absence of Bqt3 and its levels increased with BZ treatment (Fig. 6A, Bqt4C394-432) These results indicate that the C-terminal fragment containing residues 369-432 was necessary and sufficient for the NE localization of Bqt4, and its truncation successively reduced NE localization. These results also indicate that the C-terminal TMD of Bqt4 is sufficient for its proteasome-mediated degradation.
PMID:37723847	FYPO:0002061	inviable vegetative cell population	(Figure 3b) (comment: tetrad analysis)
PMID:37723847	FYPO:0002060	viable vegetative cell population	(Figure 3b) (comment: tetrad analysis)
PMID:37723847	FYPO:0001252	multinucleate multiseptate vegetative cell	Although C-terminal deleted cells (mCh-pkd2ΔC) did not affect to the growth under the normal condition, the strain was hypersensitive to CaCl2 (Figure 3c)
PMID:37723847	FYPO:0000098	sensitive to calcium [has_severity] high	Although C-terminal deleted cells (mCh-pkd2ΔC) did not affect to the growth under the normal condition, the strain was hypersensitive to CaCl2 (Figure 3c)
PMID:37723847	FYPO:0002061	inviable vegetative cell population	Although the CDRE signal is disappeared (Figure S1B), the cells did not grow in inducible condition in prz1 deletion background (Figure 1b), suggesting that the activation of calcium signaling and the cytotoxicity induced by overexpression of pkd2+ are independent.
PMID:37723847	FYPO:0002061	inviable vegetative cell population	In accordance with previous observation, the colony did not form under the inducible condition of pkd2+ overexpression (Figure 1b).
PMID:37723847	FYPO:0002061	inviable vegetative cell population	Interestingly, the internal transmembrane region was sufficient to induce both CDRE activation and growth inhibition (Figure 1a,d).
PMID:37723847	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPAC1F7.03	Localizations of Pkd2ΔN170, Pkd2ΔC577, or Pkd2TM were identical to full length Pkd2 (Figures 2b and S2A).
PMID:37723847	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPAC1F7.03	Localizations of Pkd2ΔN170, Pkd2ΔC577, or Pkd2TM were identical to full length Pkd2 (Figures 2b and S2A).
PMID:37723847	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPAC1F7.03	Localizations of Pkd2ΔN170, Pkd2ΔC577, or Pkd2TM were identical to full length Pkd2 (Figures 2b and S2A).
PMID:37723847	FYPO:0000783	protein mislocalized to cytoplasm during vegetative growth [assayed_protein] PomBase:SPAC1F7.03 [has_severity] medium	N-terminus of Pkd2 (Pkd2N) localized to the cytoplasm and slightly to the ER
PMID:37723847	FYPO:0002061	inviable vegetative cell population	Overexpression of either construct inhibited the growth like full length (Figure 1d), indicating that each of them is capable of inducing cytotoxicity upon overexpression.
PMID:37723847	FYPO:0002061	inviable vegetative cell population	Overexpression of either construct inhibited the growth like full length (Figure 1d), indicating that each of them is capable of inducing cytotoxicity upon overexpression.
PMID:37723847	GO:0005783	endoplasmic reticulum	full length of Pkd2 (GFP-Pkd2) colocalized with Pmr1, a marker for the ER (Nakazawa et al., 2019)
PMID:37723847	GO:0000935	division septum	localized to the septum and the plasma membrane, especially enriched at cell tips (Figure 2d).
PMID:37723847	GO:0031520	plasma membrane of cell tip	localized to the septum and the plasma membrane, especially enriched at cell tips (Figure 2d).
PMID:37723847	FYPO:0000783	protein mislocalized to cytoplasm during vegetative growth [assayed_protein] PomBase:SPAC1F7.03 [has_severity] high	whereas C-terminus of Pkd2 (Pkd2C) displayed a uniform cytoplasmic pattern (Figures 2b and S2A).
PMID:37746062	FYPO:0007393	septum mislocalized to cell tip [has_severity] medium	(Figure 1G-H)
PMID:37746062	FYPO:0007393	septum mislocalized to cell tip [has_severity] medium	(Figure 1G-H)
PMID:37746062	FYPO:0007393	septum mislocalized to cell tip [has_severity] high	(Figure 1G-H)
PMID:37746062	FYPO:0007393	septum mislocalized to cell tip [has_severity] medium	(Figure 1G-H)
PMID:37772819	FYPO:0004303	abolished phosphatase activity	(Fig. 1B)
PMID:37772819	FYPO:0004303	abolished phosphatase activity	(Fig. 1B)
PMID:37772819	GO:0004427	inorganic diphosphate phosphatase activity	(Fig. 3)
PMID:37772819	GO:0004309	exopolyphosphatase activity	(Fig. 4)
PMID:37772819	FYPO:0005485	abolished inositol phosphate phosphatase activity	(Fig. 5)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 7)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 7)
PMID:37772819	FYPO:0002061	inviable vegetative cell population	(Fig. 7)
PMID:37772819	FYPO:0002061	inviable vegetative cell population	(Fig. 7)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 7)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 7)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 7)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 8)
PMID:37772819	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 8)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 8)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 8)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 8)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 8)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 8)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:37772819	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 9)
PMID:37772819	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:37772819	FYPO:0008134	normal cellular polyphosphate level	(Fig. S1)
PMID:37772819	FYPO:0004469	normal phosphatase activity	(Figs. 1B and 2B)
PMID:37772819	GO:0052843	inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity	(Figs. 5 and 6)
PMID:37772819	GO:0052845	inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity	(Figs. 5 and 6)
PMID:37772819	GO:0052847	inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity	Siw14 acts on 1,5-IP8, but it has no preference for either the 5 or 1-beta phosphates (Figs.5 and 6)
PMID:37772819	GO:0052846	inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity	Siw14 acts on 1,5-IP8, but it has no preference for either the 5 or 1-beta phosphates (Figs.5 and 6)
PMID:37772819	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC27D7.03c	Table S3
PMID:37772819	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC26H5.09c	Table S3
PMID:37772819	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC14F5.01	Table S3
PMID:37772819	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPACUNK4.14	Table S3
PMID:37772819	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC15E1.02c	Table S3
PMID:37772819	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAP8A3.04c	Table S3
PMID:37772819	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC637.03	Table S3
PMID:37772819	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPACUNK4.17	Table S3
PMID:37772819	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1683.09c	Table S3
PMID:37772819	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC70.08c	Table S3
PMID:37772819	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC725.10	Table S3
PMID:37772819	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC16E9.16c	Table S3
PMID:37783794	GO:0180028	mitotic spindle pole body attachment site [exists_during] mitotic anaphase B	(Fig. 1B-D)
PMID:37783794	GO:0180028	mitotic spindle pole body attachment site [exists_during] mitotic anaphase B	(Fig. 1B-D)
PMID:37783794	GO:0180028	mitotic spindle pole body attachment site [exists_during] mitotic G1 phase	(Fig. 1B-D)
PMID:37783794	GO:0180028	mitotic spindle pole body attachment site [exists_during] mitotic G1 phase	(Fig. 1B-D)
PMID:37783794	GO:0180028	mitotic spindle pole body attachment site [exists_during] mitotic G1 phase	(Fig. 1B-D)
PMID:37783794	GO:0180028	mitotic spindle pole body attachment site [exists_during] mitotic anaphase B	(Fig. 1B-D)
PMID:37783794	GO:0180028	mitotic spindle pole body attachment site [exists_during] mitotic G1 phase	(Fig. 1B-D)
PMID:37783794	GO:0180028	mitotic spindle pole body attachment site [exists_during] mitotic G1 phase	(Fig. 1B-D)
PMID:37783794	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC1604.18c	(Fig. 3A,B)
PMID:37783794	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC1604.18c	(Fig. 3A,B)
PMID:37783794	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC9E9.14	(Fig. 3C)
PMID:37783794	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC4F8.01	(Fig. 3C)
PMID:37783794	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC1442.17c	(Fig. 3C)
PMID:37783794	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC1142.07c	(Fig. 3C)
PMID:37783794	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC4F8.01	(Fig. 3D)
PMID:37783794	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC9E9.14	(Fig. 3D)
PMID:37783794	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC1604.18c	(Fig. 3D)
PMID:37783794	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC1142.07c	(Fig. 3D)
PMID:37783794	FYPO:0007475	delayed onset of protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC1442.17c	(Fig. 3E)
PMID:37783794	FYPO:0001837	increased duration of protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC1604.18c	(Fig. 3F,G) (comment: CHECK into G2)
PMID:37783794	FYPO:0001837	increased duration of protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC1604.18c	(Fig. 3H-J) (comment:CHECK into G2)
PMID:37783794	FYPO:0008135	decreased protein localization tomitotic spindle pole body during G1/S [assayed_protein] PomBase:SPCC1442.17c	(Fig. 3I)
PMID:37783794	GO:0006998	nuclear envelope organization [happens_during] mitotic anaphase B	(Fig. 4)
PMID:37783794	GO:0007084	mitotic nuclear membrane reassembly [happens_during] mitotic G1 phase	(Fig. 4)
PMID:37783794	FYPO:0008124	increased nuclear envelope SPB fenestra size	(Fig. 4E-H)
PMID:37783794	FYPO:0008125	increased duration of nuclear envelope SPB fenestra	(Fig. 4H)
PMID:37783794	GO:0007084	mitotic nuclear membrane reassembly [happens_during] mitotic G1 phase	(Fig. 5)
PMID:37783794	FYPO:0008125	increased duration of nuclear envelope SPB fenestra	(Fig. 5A-C)
PMID:37783794	FYPO:0008126	cytoplasmic protein mislocalized to nucleoplasm during mitotic M-phase	(Fig. 6B-I)
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	(Fig. 7B)
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	(Fig. 7B)
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	(Fig. 7B)
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	(Fig. 7B)
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	(Fig. 7B)
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	(Fig. 7B)
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	(Fig. 7B)
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	(Fig. 7B)
PMID:37783794	FYPO:0008126	cytoplasmic protein mislocalized to nucleoplasm during mitotic M-phase	(Fig. 7C,D)
PMID:37783794	FYPO:0008126	cytoplasmic protein mislocalized to nucleoplasm during mitotic M-phase	(Fig. 7C-E)
PMID:37783794	FYPO:0008126	cytoplasmic protein mislocalized to nucleoplasm during mitotic M-phase	(Fig. 7C-E)
PMID:37783794	FYPO:0008127	ribosome mislocalized to nucleoplasm	(Fig. 7G)
PMID:37783794	FYPO:0008127	ribosome mislocalized to nucleoplasm	(Fig. 7G)
PMID:37783794	PomGeneEx:0000021	protein present [during] mitotic G1 phase	(comment: 15 ± 8 molecules at the spindle pole body) Fig. 2
PMID:37783794	PomGeneEx:0000021	protein present [during] mitotic anaphase B	(comment: 16 ± 8 molecules at the spindle pole body) Fig. 2
PMID:37783794	PomGeneEx:0000021	protein present [during] mitotic G1 phase	(comment: 25 ± 10 molecules at the spindle pole body) Fig. 2
PMID:37783794	PomGeneEx:0000021	protein present [during] mitotic anaphase B	(comment: 25 ± 13 molecules at the spindle pole body) Fig. 2
PMID:37783794	PomGeneEx:0000021	protein present [during] mitotic G1 phase	(comment: 30 ± 17 molecules at the spindle pole body) Fig. 2
PMID:37783794	PomGeneEx:0000021	protein present [during] mitotic G1 phase	(comment: 69 ± 37 molecules at the spindle pole body) Fig. 2
PMID:37783794	PomGeneEx:0000021	protein present [during] mitotic anaphase B	(comment: 75 ± 45 molecules at the spindle pole body) Fig. 2
PMID:37783794	PomGeneEx:0000021	protein present [during] mitotic G1 phase	(comment: 77 ± 51 molecules at the spindle pole body) Fig. 2
PMID:37783794	FYPO:0002821	decreased protein localization to mitotic spindle pole body during interphase [assayed_protein] PomBase:SPAC9E9.14	(comment: CEHCK ******** Fig. 3I decreased protein localization to spindle pole body during G1/S)
PMID:37783794	FYPO:0002821	decreased protein localization to mitotic spindle pole body during interphase [assayed_protein] PomBase:SPCC1442.17c	(comment: CHECK *********** Fig. 3G decreased protein localization to spindle pole body during G1/S)
PMID:37783794	GO:0005737	cytoplasm	Extended Data Fig. 1A,B
PMID:37783794	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC1442.17c	Extended Data Fig. 3C
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0002141	normal cell population growth at low temperature	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	normal vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	normal vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	normal vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	normal vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	normal vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	normal vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	normal vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001355	decreased vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	normal vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0001357	normal vegetative cell population growth	Extended Data Fig. 4
PMID:37783794	FYPO:0008126	cytoplasmic protein mislocalized to nucleoplasm during mitotic M-phase [has_penetrance] 65	Extended Data Fig. 5B,C
PMID:37783794	FYPO:0008126	cytoplasmic protein mislocalized to nucleoplasm during mitotic M-phase [has_penetrance] 65	Extended Data Fig. 5B,C
PMID:37783794	FYPO:0008126	cytoplasmic protein mislocalized to nucleoplasm during mitotic M-phase	Extended Data Fig. 5E,F
PMID:37783794	FYPO:0008126	cytoplasmic protein mislocalized to nucleoplasm during mitotic M-phase	Extended Data Fig. 5E,F
PMID:37783794	FYPO:0008126	cytoplasmic protein mislocalized to nucleoplasm during mitotic M-phase	Extended Data Fig. 5E,F
PMID:37783794	FYPO:0004429	normal rate of mitotic spindle elongation	Extended Data Fig. 5G
PMID:37783794	FYPO:0005695	abolished astral microtubule nucleation during mitosis	Extended Data Fig. 5G
PMID:37783794	FYPO:0004429	normal rate of mitotic spindle elongation	Extended Data Fig. 5G
PMID:37783794	FYPO:0005695	abolished astral microtubule nucleation during mitosis	Extended Data Fig. 5H
PMID:37783794	FYPO:0004429	normal rate of mitotic spindle elongation	Extended Data Fig. 5H
PMID:37783794	FYPO:0004429	normal rate of mitotic spindle elongation	Extended Data Fig. 5H
PMID:37783794	FYPO:0000276	monopolar mitotic spindle [has_penetrance] low	Extended Data Fig. 5I
PMID:37783794	FYPO:0008126	cytoplasmic protein mislocalized to nucleoplasm during mitotic M-phase	Extended Data Fig. B,C
PMID:37787465	MOD:00696	phosphorylated residue [decreased_in_presence_of] lactate	(Fig. 1C and D)
PMID:37787465	MOD:00696	phosphorylated residue [increased_in_presence_of] lactate	(Fig. 1I and J)
PMID:37787465	FYPO:0008213	increased vegetative cell population growth on lactate carbon source	(Fig. 2I)
PMID:37787465	FYPO:0008213	increased vegetative cell population growth on lactate carbon source	(Fig. 2I)
PMID:37787465	FYPO:0008213	increased vegetative cell population growth on lactate carbon source	(Fig. 2J)
PMID:37787465	FYPO:0008213	increased vegetative cell population growth on lactate carbon source	(Fig. 2J)
PMID:37787465	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC24B11.06c [has_severity] medium	(Fig. 3A and B)
PMID:37787465	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC24B11.06c	(Fig. 3C and D)
PMID:37787465	FYPO:0001038	increased protein phosphorylation during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAC24B11.06c	(Fig. 4C and D)
PMID:37787465	FYPO:0001038	increased protein phosphorylation during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPAC24B11.06c	(Fig. 4F and G)
PMID:37787465	FYPO:0004166	increased oxygen consumption during vegetative growth	(Fig. 5A)
PMID:37787465	FYPO:0008231	increased lactate dehydrogenase activity [has_severity] high	(Fig. 5B)
PMID:37787465	FYPO:0008231	increased lactate dehydrogenase activity [has_severity] medium	(Fig. 5B)
PMID:37787465	FYPO:0002780	decreased cellular reactive oxygen species level during vegetative growth	(Fig. 5C and D)
PMID:37787465	FYPO:0002780	decreased cellular reactive oxygen species level during vegetative growth	(Fig. 5C and D)
PMID:37787465	FYPO:0001046	premature mitosis [has_severity] medium	(Fig. 5E and F)
PMID:37787465	FYPO:0000420	delayed onset of cytokinesis [has_severity] low	Table 1
PMID:37787465	FYPO:0001046	premature mitosis [has_severity] medium	Table 1
PMID:37787465	FYPO:0001046	premature mitosis [has_severity] low	Table 1
PMID:37787465	FYPO:0001046	premature mitosis [has_severity] high	Table 1
PMID:37787465	FYPO:0000420	delayed onset of cytokinesis [has_severity] low	Table 1
PMID:37787465	FYPO:0001046	premature mitosis [has_severity] low	Table 1
PMID:37787465	FYPO:0001046	premature mitosis [has_severity] medium	Table 1
PMID:37787465	FYPO:0000420	delayed onset of cytokinesis [has_severity] low	Table 1
PMID:37788281	FYPO:0001043	increased mating efficiency [has_severity] high	(comment: CHECK by expression of rad24-E185K)
PMID:37788281	PomGeneEx:0000018	protein level increased [during] cellular response to nitrogen starvation	(comment: CHECK in sam3 mutant)
PMID:37788281	GO:0005654	nucleoplasm	(comment: CHECK in sam3 mutant)
PMID:37788281	FYPO:0001864	mating without glucose starvation	(comment: dominat negative)
PMID:37788281	GO:0005654	nucleoplasm	exclusion from nucleoplasm is delayed in rad24 deletion background
PMID:37792890	FYPO:0001235	decreased extent of cell population growth	(ags1-664, bgs1-191 and/or bgs4-1 of α1,3-glucan synthase, linear β1,3-glucan synthase and 1,6 branched β1,3-glucan synthase, respectively) [18,24,39], improved css1-3 cell growth at semi-permissive temperatures (S1B Fig) while growth in hypoosomotic conditions (sorbitol-containing media) did not (S1C Fig).
PMID:37792890	FYPO:0001235	decreased extent of cell population growth	(ags1-664, bgs1-191 and/or bgs4-1 of α1,3-glucan synthase, linear β1,3-glucan synthase and 1,6 branched β1,3-glucan synthase, respectively) [18,24,39], improved css1-3 cell growth at semi-permissive temperatures (S1B Fig) while growth in hypoosomotic conditions (sorbitol-containing media) did not (S1C Fig).
PMID:37792890	FYPO:0000135	abnormal plasma membrane sterol distribution	(comment: Using GFP-D4H biosensor)
PMID:37792890	FYPO:0005803	decreased rate of protein movement within plasma membrane at cell side	(comment: assayed using FRAP)
PMID:37792890	FYPO:0000135	abnormal plasma membrane sterol distribution	(comment: using GFP-D4H biosensor)
PMID:37792890	FYPO:0002627	altered level of substance in cell wall during vegetative growth	In the periplasmic space***** glucans were deposited between the PM and the cell wall at the restrictive temperature (Fig 1B).
PMID:37792890	FYPO:0001357	normal vegetative cell population growth	Indeed, we isolated a cold-sensitive mutant of cut6, cut6-1, as a strong suppressor of css1-3 (S3A Fig).
PMID:37792890	FYPO:0001357	normal vegetative cell population growth	Indeed, we isolated a cold-sensitive mutant of cut6, cut6-1, as a strong suppressor of css1-3 (S3A Fig).
PMID:37792890	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPCC1281.01	we predicted that the glucan synthases Ags1, Bgs1, Bgs3, and Bgs4 would localize normally and adjacent to the glucan deposits in css1-3 mutant cells. Indeed, all four proteins localized at tips and septa of css1-3, as in wild-type cells
PMID:37805140	FYPO:0008129	increased tRNA guanosine N2,N2-dimethylation	(Figure 4a)
PMID:37805140	FYPO:0007020	normal tRNA guanosine N2-methylation	(Figure 4a)
PMID:37805140	FYPO:0000257	normal phenotype	(comment: normal stop codon readthrough)
PMID:37805140	GO:0160104	tRNA (guanine(26)-N2)-dimethyltransferase activity [has_input] PomBase:SPBTRNALEU.08 [part_of] tRNA processing [occurs_in] nucleus	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	GO:0160104	tRNA (guanine(26)-N2)-dimethyltransferase activity [has_input] PomBase:SPBTRNALEU.09 [part_of] tRNA processing [occurs_in] nucleus	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	GO:0160104	tRNA (guanine(26)-N2)-dimethyltransferase activity [has_input] PomBase:SPCTRNALEU.11 [part_of] tRNA processing [occurs_in] nucleus	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	GO:0160104	tRNA (guanine(26)-N2)-dimethyltransferase activity [has_input] PomBase:SPATRNALEU.04 [part_of] tRNA processing [occurs_in] nucleus	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	GO:0160104	tRNA (guanine(26)-N2)-dimethyltransferase activity [has_input] PomBase:SPATRNASER.03 [part_of] tRNA processing [occurs_in] nucleus	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	GO:0160104	tRNA (guanine(26)-N2)-dimethyltransferase activity [has_input] PomBase:SPCTRNASER.11 [part_of] tRNA processing [occurs_in] nucleus	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	GO:0160104	tRNA (guanine(26)-N2)-dimethyltransferase activity [has_input] PomBase:SPBTRNALEU.10 [part_of] tRNA processing [occurs_in] nucleus	Trm1 robustly modified nuclear- and mitochondrial-encoded tRNAs, consistent with its proposed localization to the nucleus and mitochondria, while M1 Trm1 only modified mitochondrially-encoded tRNAs Certain nuclear-encoded tRNAs, including tRNA SerUGA and tRNA LeuAAG were robustly modified by endogenous Trm1 (Figure 1D, “wild type”, lane 1) and overexpressed M24 Trm1 (Figure 1D, lane 3)
PMID:37805140	FYPO:0008130	increased stop codon readthrough	We found that both wild type and catalytically inactive nuclear-targeted (M24) Trm1 promoted suppression of the tRNA SerUCA allele in a sla1∆ background, suggesting that modification is not strictly required for suppression activity and that Trm1 promotes pre-tRNA maturation even in the absence of catalysis (Figure 3A, B).
PMID:37805140	FYPO:0006253	normal tRNA binding	Wild type and D201A exhibited comparable binding affinity, suggesting that disruption of the putative catalytic site does not impair tRNA binding affinity or binding cooperativity (Figure 2A, B, Figure S2, Table S5).
PMID:37805140	FYPO:0004529	normal mitochondrial translation	pulse labeling revealed no defects in mitochondrial translation upon Trm1 deletion (Figure S1)
PMID:37805140	FYPO:0003957	abolished tRNA guanosine N2,N2-dimethylation	the D201A mutant showed the same lack of modification of nuclear- and mitochondrial-encoded tRNAs as trm1∆ cells transformed with an empty vector, despite similar levels of protein accumulation as the wild type overexpressed isoform (Figure 1D).
PMID:37805140	FYPO:0003957	abolished tRNA guanosine N2,N2-dimethylation	the D201A mutant showed the same lack of modification of nuclear- and mitochondrial-encoded tRNAs as trm1∆ cells transformed with an empty vector, despite similar levels of protein accumulation as the wild type overexpressed isoform (Figure 1D).
PMID:37815455	FYPO:0001903	normal septation index	(Fig. 1D-E).
PMID:37815455	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPBC2G2.02	(Fig. S1D)
PMID:37815455	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPAC9G1.10c	(Fig. S1D)
PMID:37815455	FYPO:0002674	normal protein localization to plasma membrane [assayed_protein] PomBase:SPBC577.06c	(Fig. S1D)
PMID:37815455	FYPO:0001355	decreased vegetative cell population growth	(Fig. S2A)
PMID:37815455	FYPO:0001355	decreased vegetative cell population growth	(Fig. S2A)
PMID:37815455	FYPO:0001355	decreased vegetative cell population growth	(Fig. S2A)
PMID:37815455	FYPO:0001355	decreased vegetative cell population growth	(Fig. S2A)
PMID:37815455	FYPO:0003736	normal mitotic index	(Figure 1F)
PMID:37815455	GO:0180048	phosphatidylinositol 4-phosphate biosynthetic process	(comment: This is known from the MF but can be further supported from the fact that PIP4 levels decrease when stt4 is not localized correctly)
PMID:37815455	FYPO:0002127	increased protein localization to plasma membrane during vegetative growth [assayed_protein] PomBase:SPAC19G12.14	In contrast, PM Its3-mNG was mildly reduced at 25°C and increased 1.8-fold at 36°C in pik1-11 compared to wild-type cells (Fig. 2E-F and S1E)
PMID:37815455	GO:0004430	1-phosphatidylinositol 4-kinase activity [part_of] phosphatidylinositol phosphate biosynthetic process [occurs_in] trans-Golgi network membrane	We conclude that pik1-11 cells lack a Golgi PI4P pool, and have reduced PM PI4P that does not result in a corresponding decrease in PM PI(4,5)P2.
PMID:37815455	GO:0046854	phosphatidylinositol phosphate biosynthetic process	We conclude that pik1-11 cells lack a Golgi PI4P pool, and have reduced PM PI4P that does not result in a corresponding decrease in PM PI(4,5)P2.
PMID:37815455	FYPO:0007489	decreased protein localization to Golgi apparatus, with protein mislocalized to cytosol	We found that Pik1-D450- mNG still localized to the trans-Golgi marked by Sec72-mCherry in ncs1∆ cells (Fig. 4C), Interestingly, there was a high cytoplasmic Pik1 population in ncs1Δ cells that was not observed in wild-type cells; indeed, there was >2- fold more Pik1 overall (Fig. 4D). We currently do not have a mechanistic explanation for this observation.
PMID:37815455	GO:0032588	trans-Golgi network membrane	found co-localization only with the trans-Golgi marker (Fig. 3B)
PMID:37815455	FYPO:0002060	viable vegetative cell population	pik1-11 cells grow similarly to wild-type at 25 ̊C and 29 ̊C but pik1-11 cells do not grow at 32 ̊C or 36 ̊C (Fig. 1C)
PMID:37815455	FYPO:0002061	inviable vegetative cell population	pik1-11 cells grow similarly to wild-type at 25 ̊C and 29 ̊C but pik1-11 cells do not grow at 32 ̊C or 36 ̊C (Fig. 1C)
PMID:37815455	GO:0032588	trans-Golgi network membrane	we observed co-localization of Ncs1-mCherry with Pik1- D450-mNG at the trans-Golgi (Fig. 4B)
PMID:37815455	FYPO:0002150	inviable spore population	when we attempted to combine ncs1Δ with pik1-11 we found that they were synthetically lethal (Fig. 4A)
PMID:37815455	FYPO:0002150	inviable spore population	when we attempted to combine ncs1Δ with pik1-11 we found that they were synthetically lethal (Fig. 4A)
PMID:37820734	GO:0003690	double-stranded DNA binding	(comment: author suggested) double-stranded DNA gripping or clamping A DNA binding activity, stimulated by the binding of a non-hydrolylsable ATP analogue, where a ATPase protein complex tightly grips a stretch of double-stranded DNA with some or all of its subunits. Such a conformation is usually interpretted as the intermediate state before the ATP hydrolysis by the protein complex.
PMID:37820734	GO:0061776	ATP-dependent topological DNA co-entrapment activity	A reaction time course revealed that most dsDNA binding occurred within the first 15 min of incubation, whereas dsDNA binding by Walker A ATPase motif mutant condensin was not stimulated by ATP addition (Figures S1B and S1C). These results show that recombinant fission yeast condensin binds to DNA in an ATP-stimulated, high-salt-resistant manner, characteristic of topological DNA interactions by SMC complexes.
PMID:37820734	GO:0061776	ATP-dependent topological DNA co-entrapment activity	A reaction time course revealed that most dsDNA binding occurred within the first 15 min of incubation, whereas dsDNA binding by Walker A ATPase motif mutant condensin was not stimulated by ATP addition (Figures S1B and S1C). These results show that recombinant fission yeast condensin binds to DNA in an ATP-stimulated, high-salt-resistant manner, characteristic of topological DNA interactions by SMC complexes.
PMID:37820734	GO:0061776	ATP-dependent topological DNA co-entrapment activity	A reaction time course revealed that most dsDNA binding occurred within the first 15 min of incubation, whereas dsDNA binding by Walker A ATPase motif mutant condensin was not stimulated by ATP addition (Figures S1B and S1C). These results show that recombinant fission yeast condensin binds to DNA in an ATP-stimulated, high-salt-resistant manner, characteristic of topological DNA interactions by SMC complexes.
PMID:37820734	GO:0061776	ATP-dependent topological DNA co-entrapment activity	A reaction time course revealed that most dsDNA binding occurred within the first 15 min of incubation, whereas dsDNA binding by Walker A ATPase motif mutant condensin was not stimulated by ATP addition (Figures S1B and S1C). These results show that recombinant fission yeast condensin binds to DNA in an ATP-stimulated, high-salt-resistant manner, characteristic of topological DNA interactions by SMC complexes. Although an intact supercoiled plasmid remained stably bound to condensin in the bead fraction, linearized dsDNA was released into the supernatant. This experiment confirms that ATP-dependent condensin loading results in a topological DNA interaction.
PMID:37820734	GO:0061776	ATP-dependent topological DNA co-entrapment activity	A reaction time course revealed that most dsDNA binding occurred within the first 15 min of incubation, whereas dsDNA binding by Walker A ATPase motif mutant condensin was not stimulated by ATP addition (Figures S1B and S1C). These results show that recombinant fission yeast condensin binds to DNA in an ATP-stimulated, high-salt-resistant manner, characteristic of topological DNA interactions by SMC complexes. Three topologically closed dsDNA substrates—supercoiled, relaxed circular, and nicked circular— were all recovered with similar efficiency (Figure 1B). Condensin also bound, albeit less efficiently, circular single-stranded DNA (ssDNA). By contrast, we observed no detectable recovery of linear dsDNA, consistent with a topological condensin-DNA interaction.
PMID:37820734	GO:0106260	DNA-DNA tethering activity	DNA-DNA tethering activity, sequential topological entrapment: sequential topological entrapment of two or more DNAs, A DNA tethering activity where a protein complex encircles two or more DNA molecules, one at a time, with its loose fitting ring.
PMID:37820734	GO:0106260	DNA-DNA tethering activity	sequential topological entrapment of two or more DNAs, A DNA tethering activity where a protein complex encircles two or more DNA molecules, one at a time, with its loose fitting ring.
PMID:37820734	GO:0106260	DNA-DNA tethering activity	sequential topological entrapment of two or more DNAs, A DNA tethering activity where a protein complex encircles two or more DNA molecules, one at a time, with its loose fitting ring.
PMID:37820734	GO:0106260	DNA-DNA tethering activity	sequential topological entrapment of two or more DNAs, A DNA tethering activity where a protein complex encircles two or more DNA molecules, one at a time, with its loose fitting ring.
PMID:37820734	GO:0106260	DNA-DNA tethering activity	sequential topological entrapment of two or more DNAs, A DNA tethering activity where a protein complex encircles two or more DNA molecules, one at a time, with its loose fitting ring.
PMID:37831774	GO:0106006	cytoskeletal protein-membrane anchor activity [occurs_in] clathrin-coated endocytic vesicle membrane	A gradient of force is detected along End4 molecule in wild-type cells. ~19 piconewton force near the actin cytoskeleton (G857), ~11 piconewtons near the clathrin lattice (P337), and ~9 piconewtons near the plasma membrane (D155).
PMID:37831774	GO:0106006	cytoskeletal protein-membrane anchor activity [occurs_in] clathrin-coated endocytic vesicle membrane [part_of] clathrin-mediated membrane bending	In ent1-Δ(572-702) cells, force on End4 is increased to above 20 piconewton at G857, but remains the same as in wild type at P337 and D155.
PMID:37831774	FYPO:0002177	viable vegetative cell with normal cell morphology	In ent1-Δ(572-702) cells, force on End4 is increased to above 20 piconewton at G857, but remains the same as in wild type at P337 or D155.
PMID:37831774	GO:0051285	cell cortex of cell tip [exists_during] mitotic M phase	In wild-type cells, fluorescently tagged End4p is present at endocytic sites and appears as diffraction-limited puncta (hereafter referred to as End4p patches) that are enriched at cell tips during interphase and around the division plane during mitosis (Fig. 1F; figs. S2A and S5, B and C; and movie S1).
PMID:37831774	GO:0032153	cell division site [exists_during] mitotic M phase	In wild-type cells, fluorescently tagged End4p is present at endocytic sites and appears as diffraction-limited puncta (hereafter referred to as End4p patches) that are enriched at cell tips during interphase and around the division plane during mitosis (Fig. 1F; figs. S2A and S5, B and C; and movie S1).
PMID:37831774	GO:0061645	endocytic patch	In wild-type cells, fluorescently tagged End4p is present at endocytic sites and appears as diffraction-limited puncta (hereafter referred to as End4p patches) that are enriched at cell tips during interphase and around the division plane during mitosis (Fig. 1F; figs. S2A and S5, B and C; and movie S1).
PMID:37913773	FYPO:0001134	normal mature 18S rRNA level	Although the downstream S6K kinase Psk1 in the TORC1 pathway has been implicated in RP phosphorylation,39 our finding demonstrated that rRNA abundance was unaffected in the psk1D strain (Figure S3A)
PMID:37913773	GO:0030874	nucleolar chromatin [coincident_with] cytosolic_rRNA_18S_gene	Chromatin immunoprecipitation (ChIP) experiments targeting FLAG-tagged Tor2, Pop3/LST8, Tco89, and Mip1/Raptor, constituents of TORC1,31 exhibited significant TORC1 accumulation across the rDNA, predominantly in the 18S and 28S regions (Figures 1A and 1B).
PMID:37913773	GO:0030874	nucleolar chromatin [coincident_with] cytosolic_rRNA_28S_gene	Chromatin immunoprecipitation (ChIP) experiments targeting FLAG-tagged Tor2, Pop3/LST8, Tco89, and Mip1/Raptor, constituents of TORC1,31 exhibited significant TORC1 accumulation across the rDNA, predominantly in the 18S and 28S regions (Figures 1A and 1B).
PMID:37913773	GO:0030874	nucleolar chromatin [coincident_with] cytosolic_rRNA_18S_gene	Chromatin immunoprecipitation (ChIP) experiments targeting FLAG-tagged Tor2, Pop3/LST8, Tco89, and Mip1/Raptor, constituents of TORC1,31 exhibited significant TORC1 accumulation across the rDNA, predominantly in the 18S and 28S regions (Figures 1A and 1B).
PMID:37913773	GO:0030874	nucleolar chromatin [coincident_with] cytosolic_rRNA_28S_gene	Chromatin immunoprecipitation (ChIP) experiments targeting FLAG-tagged Tor2, Pop3/LST8, Tco89, and Mip1/Raptor, constituents of TORC1,31 exhibited significant TORC1 accumulation across the rDNA, predominantly in the 18S and 28S regions (Figures 1A and 1B).
PMID:37913773	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC4C3.05c	Furthermore, we discovered that this reduction was caused by the dissociation of RNA polymerase I from the rDNA region (Figures 3B and S3B).
PMID:37913773	GO:0042134	rRNA primary transcript binding	In addition, the RNA immunoprecipitation analysis revealed a notable association between FLAG-Tor2 and rDNA transcripts, specifically at the 18S, 5.8S, and 28S regions (Figures 2E and S2D)
PMID:37913773	FYPO:0001134	normal mature 18S rRNA level	Moreover, we found that the diminution of 18S rRNA levels in the tor2-287 mutant could be mitigated by overexpression of Atf1 (atf1 o.p) or disruption of the ago1+ gene (ago1D), which encodes a crucial factor for RNAi-dependent heterochromatinization (Figure 3I).
PMID:37913773	FYPO:0001134	normal mature 18S rRNA level	Moreover, we found that the diminution of 18S rRNA levels in the tor2-287 mutant could be mitigated by overexpression of Atf1 (atf1 o.p) or disruption of the ago1+ gene (ago1D), which encodes a crucial factor for RNAi-dependent heterochromatinization (Figure 3I).
PMID:37913773	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] PomBase:SPBC216.07c	Nevertheless, our analysis revealed that deletion of atf1+ gene (atf1D) did not significantly affect Tor2 accumulation in rDNA (Figures S2A and S2B).
PMID:37913773	FYPO:0003694	decreased mature 18S rRNA level	Our result indicated that the total amount of 18S rRNA transcripts was reduced by half in the tor2-287 mutant, even under nutrient-rich conditions (Figure 3A).
PMID:37913773	GO:0060963	positive regulation of ribosomal protein gene transcription by RNA polymerase II	Taken together, the transcription of ribosome-associated genes is regulated by TORC1.
PMID:37913773	FYPO:0006074	increased histone H3-K9 dimethylation at rDNA during vegetative growth	To investigate this, we performed ChIP-qPCR targeting H3K9 methylation, a marker of heterochromatin formation, in both wild-type and tor2-287 cells. We found that tor2-287 cells exhibited a marked increase in H3K9me2 levels, accompanied by a slight increase in histone H3 occupancy in the rDNA region (Figures 3C and S3C).
PMID:37913773	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC664.06	We performed RT-qPCR and found that transcription of selected ribosome-related genes (rpl102+, rlp7+, and gar2+) was reduced in the tor2-287 mutant (Figure 4A).
PMID:37913773	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC30D10.18c	We performed RT-qPCR and found that transcription of selected ribosome-related genes (rpl102+, rlp7+, and gar2+) was reduced in the tor2-287 mutant (Figure 4A).
PMID:37913773	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC140.02	We performed RT-qPCR and found that transcription of selected ribosome-related genes (rpl102+, rlp7+, and gar2+) was reduced in the tor2-287 mutant (Figure 4A).
PMID:37913773	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC216.07c	We then examined their accumulation at rDNA using ChIP assays and found a decrease in the rDNA accumulation of FLAG-Tor2 lacking the HTH domain (Figure 2G).
PMID:37913773	GO:0061188	negative regulation of rDNA heterochromatin formation	We thus conclude that heterochromatinization of rDNA induced by glucose starvation is initiated by TORC1 inactivation (Figure 3F).
PMID:37913773	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC29B5.01	heterochromatin formation in rDNA is prompted by the dissociation of the stress- responsive transcription factor Atf1 and the accumulation of the histone chaperone FACT, which maintains H3K9 methylation,40 in addition to the RNAi-dependent pathway.14 We therefore performed ChIP-qPCR targeting Atf1 and FLAG-tagged Pob3 (a component of FACT), and found that Atf1 diminished from the entire rDNA region, while Pob3-FLAG selectively accumulated between rDNA repeats (Figures 3D and 3E).
PMID:37913773	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC216.07c	nuc1-632 mutant strain, wherein RNA polymerase I function was impaired.33,34 As a result, we found a considerable reduction in Tor2 accumulation in the rDNA region compared with wild-type cells, concomitant with a decrease in rRNA abundance (Figures 2A and 2B).
PMID:37913773	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPAC1952.05	we conducted ChIP-qPCR targeting Gcn5-HA and found that it diminished from rDNA in the tor2-287 mutant compared with wild-type (Figure S3D).
PMID:37913773	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC29B5.01	we found that the intracellular Atf1 protein levels were significantly reduced in the tor2-287 mutants when detected with an anti-Atf1 antibody (Figures 3G and 3H).
PMID:37923140	FYPO:0005487	decreased iron-sulfur cluster binding [has_severity] medium	(Fig. 3)
PMID:37923140	FYPO:0005487	decreased iron-sulfur cluster binding [has_severity] low	(Fig. 3)
PMID:37923140	FYPO:0005487	decreased iron-sulfur cluster binding [has_severity] high	(Fig. 3)
PMID:37923140	FYPO:0007933	sensitive to 2,2′-dipyridyl	(Fig. 4)
PMID:37923140	FYPO:0007933	sensitive to 2,2′-dipyridyl	(Fig. 4)
PMID:37923140	FYPO:0007933	sensitive to 2,2′-dipyridyl	(Fig. 4)
PMID:37923140	FYPO:0007933	sensitive to 2,2′-dipyridyl	(Fig. 4)
PMID:37923140	FYPO:0000826	decreased RNA level [has_severity] high [assayed_transcript] PomBase:SPBC1683.09c	(Fig. 5)
PMID:37923140	FYPO:0000826	decreased RNA level [has_severity] high [assayed_transcript] PomBase:SPBC1683.09c	(Fig. 5)
PMID:37923140	FYPO:0000826	decreased RNA level [has_severity] medium [assayed_transcript] PomBase:SPBC1683.09c	(Fig. 5)
PMID:37923140	PomGeneEx:0000011	RNA level increased [in_presence_of] 2,2'-bipyridine	(Fig. 5)
PMID:37923140	FYPO:0000826	decreased RNA level [has_severity] high [assayed_transcript] PomBase:SPBC1683.09c	(Fig. 5)
PMID:37923140	GO:0008270	zinc ion binding	Metal and acid-labile sulfide analysis of anaerobically purified Fep1-DBD from three independent samples indicated 0.76 ± 0.12 Zn, 0.69 ± 0.08 Fe, and 0.85 ± 0.10 S2- bound per monomer.
PMID:37939137	FYPO:0007447	abolished reticulophagy during cellular response to endoplasmic reticulum stress	(Fig. 1C) Consistent with this idea, deletion of yep1 severely diminished the relocalization of Ost4-CFP to the vacuole upon DTT treatment (+DTT) or nitrogen starvation treatment (−N) (Fig 1C).
PMID:37939137	FYPO:0008084	abolished reticulophagy during nitrogen starvation	(Fig. 1C) Consistent with this idea, deletion of yep1 severely diminished the relocalization of Ost4-CFP to the vacuole upon DTT treatment (+DTT) or nitrogen starvation treatment (−N) (Fig 1C). yep1Δ cells also exhibited a severe defect in the autophagic processing of GFP-tagged integral ER membrane protein Erg11 into free GFP (Fig 1D and 1E).
PMID:37939137	FYPO:0008084	abolished reticulophagy during nitrogen starvation	(Fig. 1D)
PMID:37939137	FYPO:0007447	abolished reticulophagy during cellular response to endoplasmic reticulum stress	(Fig. 1E)
PMID:37939137	FYPO:0008385	abolished nucleophagy during cellular response to Endoplasmic Reticulum stress	(Fig. 1H)
PMID:37939137	FYPO:0008086	abolished nucleophagy during nitrogen starvation	(Fig. 1I) Deletion of yep1 abolished the processing of Pus1-mECitrine in both DTT- and starvation-treated cells, indicating that Yep1 is essential for nucleophagy.
PMID:37939137	FYPO:0007444	normal macroautophagy during cellular response to endoplasmic reticulum stress	(Fig. 1J) In contrast to the severe ER-phagy and nucleophagy defects of yep1Δ cells, bulk autophagy in yep1Δ cells was largely normal as indicated by the processing of CFP-Atg8 (Fig 1J).
PMID:37939137	FYPO:0006294	normal macroautophagy during nitrogen starvation	(Fig. 1J) In contrast to the severe ER-phagy and nucleophagy defects of yep1Δ cells, bulk autophagy in yep1Δ cells was largely normal as indicated by the processing of CFP-Atg8 (Fig 1J). In addition, another readout of bulk autophagy, the processing of fluorescent protein-tagged cytosolic protein Tdh1 (glyceraldehyde-3-phosphate dehydrogenase (GAPDH)) [43], was also largely unaffected in yep1Δ cells (S1E Fig). Consistent with the lack of bulk autophagy defects, transmission (TEM) analysis showed that autophagosome accumulation in the fsc1Δ mutant, which is defective in autophagosome-vacuole fusion [44], was not notably affected by the deletion of yep1 (S1F Fig).
PMID:37939137	FYPO:0007447	abolished reticulophagy during cellular response to endoplasmic reticulum stress	(Fig. 3 J-K, S6 E)
PMID:37939137	FYPO:0000164	abnormal cell separation after cytokinesis [has_severity] low	(Fig. 3C)
PMID:37939137	FYPO:0000164	abnormal cell separation after cytokinesis [has_severity] high	(Fig. 3C) We observed that yep1Δ caused a noticeable but even weaker septum positioning defect than rtn1Δ, yop1Δ, or tts1Δ. Combined yep1Δ with the double and triple deletion of rtn1, yop1, and tts1 invariably resulted in a more severe phenotype (Fig 3C).
PMID:37939137	FYPO:0007447	abolished reticulophagy during cellular response to endoplasmic reticulum stress	(Fig. 3J-K, S6 E)
PMID:37939137	FYPO:0007447	abolished reticulophagy during cellular response to endoplasmic reticulum stress	(Fig. 3J-K, S6 E)
PMID:37939137	FYPO:0007446	decreased reticulophagy during cellular response to endoplasmic reticulum stress	(Fig. 3K)
PMID:37939137	FYPO:0007446	decreased reticulophagy during cellular response to endoplasmic reticulum stress	(Fig. 3K)
PMID:37939137	FYPO:0007447	abolished reticulophagy during cellular response to endoplasmic reticulum stress	(Fig. 3L)
PMID:37939137	FYPO:0007446	decreased reticulophagy during cellular response to endoplasmic reticulum stress	(Fig. 3L)
PMID:37939137	FYPO:0007446	decreased reticulophagy during cellular response to endoplasmic reticulum stress	(Fig. 3L)
PMID:37939137	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC30D10.09c [assayed_protein] PomBase:SPBC30D10.09c	(Fig. S5, S6)
PMID:37939137	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC30D10.09c [assayed_protein] PomBase:SPBC30D10.09c	(Fig. S5, S6)
PMID:37939137	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC30D10.09c [assayed_protein] PomBase:SPBC30D10.09c	(Fig. S5, S6)
PMID:37939137	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC30D10.09c [assayed_protein] PomBase:SPBC30D10.09c	(Fig. S5; Fig S6)
PMID:37939137	FYPO:0007447	abolished reticulophagy during cellular response to endoplasmic reticulum stress	(Fig. S6A)
PMID:37939137	FYPO:0007446	decreased reticulophagy during cellular response to endoplasmic reticulum stress	(Fig. S6A)
PMID:37939137	FYPO:0008083	abnormal reticulophagy [has_severity] low	(Figure 2) Taken together, the above findings demonstrate that Yep1 is required for the autophagosomal enclosure of ER-phagy/nucleophagy cargos.
PMID:37939137	FYPO:0008083	abnormal reticulophagy [has_severity] high	(Figure 2) Taken together, the above findings demonstrate that Yep1 is required for the autophagosomal enclosure of ER-phagy/nucleophagy cargos.
PMID:37939137	FYPO:0008388	abnormal autophagosomal enclosure during nucleophagy	(Figure 2) Taken together, the above findings demonstrate that Yep1 is required for the autophagosomal enclosure of ER-phagy/nucleophagy cargos.
PMID:37939137	GO:0061736	engulfment of target by autophagosome [happens_during] cellular response to nitrogen starvation	(comment: during nucleophagy abnd reticulophagy)
PMID:37939137	GO:0097038	perinuclear endoplasmic reticulum	As Ost4 and Erg11 localize to both the cortical ER and the nuclear envelope..... (Fig 1F and 1G)
PMID:37939137	GO:0032541	cortical endoplasmic reticulum	As Ost4 and Erg11 localize to both the cortical ER and the nuclear envelope..... (Fig 1F and 1G)
PMID:37939137	GO:0097038	perinuclear endoplasmic reticulum	As Ost4 and Erg11 localize to both the cortical ER and the nuclear envelope..... (Fig 1F and 1G)
PMID:37939137	GO:0032541	cortical endoplasmic reticulum	As Ost4 and Erg11 localize to both the cortical ER and the nuclear envelope..... (Fig 1F and 1G)
PMID:37939137	GO:0005783	endoplasmic reticulum	Human REEP1-4 are ER-localizing proteins [38,41,42], Similarly, we found that Yep1 exhibited an ER localization pattern during vegetative growth (S1B Fig).
PMID:37939137	FYPO:0008387	normal protein localization to autophagic structure [assayed_protein] PomBase:SPBP8B7.24c	In both wild-type and yep1Δ cells, Epr1 and Atg8 colocalized at punctate structures shortly after ER-phagy induction by DTT or starvation treatment (S2A Fig), indicating that Yep1 is not essential for the initial stage of ER-phagy during which Epr1 mediates a connection between the ER and Atg8-decorated autophagic membranes.
PMID:37939137	FYPO:0008387	normal protein localization to autophagic structure [assayed_protein] PomBase:SPAC6B12.08	In both wild-type and yep1Δ cells, Epr1 and Atg8 colocalized at punctate structures shortly after ER-phagy induction by DTT or starvation treatment (S2A Fig), indicating that Yep1 is not essential for the initial stage of ER-phagy during which Epr1 mediates a connection between the ER and Atg8-decorated autophagic membranes.
PMID:37939137	FYPO:0006433	abnormal tubular endoplasmic reticulum morphology [has_severity] low	In the absence of Rtn1, Yop1, and Tts1, the cortical ER becomes less reticulate and more sheet-like, with the frequent appearance of large holes in images of the top or bottom plane of the cells and extended gaps in images of the midplane of the cells [50]. We found that this alteration of ER morphology can be reversed to a large extent by either introducing back Rtn1 or increasing the expression level of Yep1 (Figs 3B and S4B)
PMID:37939137	FYPO:0006433	abnormal tubular endoplasmic reticulum morphology [has_severity] high	In the absence of Rtn1, Yop1, and Tts1, the cortical ER becomes less reticulate and more sheet-like, with the frequent appearance of large holes in images of the top or bottom plane of the cells and extended gaps in images of the midplane of the cells [50]. We found that this alteration of ER morphology can be reversed to a large extent by either introducing back Rtn1 or increasing the expression level of Yep1 (Figs 3B and S4B).
PMID:37939137	FYPO:0008386	decreased nucleophagy	The loss of the ER-phagy receptor Epr1 diminished the processing of Pus1-mECi- trine, suggesting that Epr1 also acts as a nucleophagy receptor
PMID:37939137	GO:0180020	membrane bending activity [part_of] nucleophagy	These results demonstrate that Yep1 shares the membrane-shaping ability of Rtn1, Yop1, and Tts1 and contributes to the maintenance of normal ER structure.
PMID:37939137	GO:0180020	membrane bending activity [part_of] reticulophagy	These results demonstrate that Yep1 shares the membrane-shaping ability of Rtn1, Yop1, and Tts1 and contributes to the maintenance of normal ER structure.
PMID:37939137	FYPO:0006433	abnormal tubular endoplasmic reticulum morphology [has_severity] low	Thus, Yep1, when overexpressed, can fulfill the function of maintaining tubular ER independently of Rtn1, Yop1, and Tts1.
PMID:37949217	FYPO:0008269	decreased total cellular phosphate (Pi) level [has_severity] medium	(Figure 1A)
PMID:37949217	FYPO:0008267	normal total cellular phosphate (Pi) level	(Figure 1A)
PMID:37949217	FYPO:0008269	decreased total cellular phosphate (Pi) level [has_severity] medium	(Figure 1A)
PMID:37949217	FYPO:0008226	increased total cellular phosphate (Pi) level [has_severity] high	(Figure 1a)
PMID:37949217	FYPO:0008226	increased total cellular phosphate (Pi) level [has_severity] medium	(Figure 1a)
PMID:37949217	FYPO:0008227	increased free cellular phosphate (Pi) level	(Figure 3)
PMID:37949217	FYPO:0000364	abnormal plasma membrane morphology during vegetative growth	(Figure 3)
PMID:37949217	FYPO:0002060	viable vegetative cell population	All double mutants, Δpqr1Δxpr1, Δpqr1Δvtc4, and Δxpr1Δvtc4, were able to form colonies at 100 mM Pi. Δpqr1Δxpr1 showed slow growth at 100 mM Pi and failed to grow at 300 mM Pi (Fig. 2C).
PMID:37949217	FYPO:0001355	decreased vegetative cell population growth	All double mutants, Δpqr1Δxpr1, Δpqr1Δvtc4, and Δxpr1Δvtc4, were able to form colonies at 100 mM Pi. Δpqr1Δxpr1 showed slow growth at 100 mM Pi and failed to grow at 300 mM Pi (Fig. 2C).
PMID:37949217	FYPO:0002060	viable vegetative cell population	All double mutants, Δpqr1Δxpr1, Δpqr1Δvtc4, and Δxpr1Δvtc4, were able to form colonies at 100 mM Pi. Δpqr1Δxpr1 showed slow growth at 100 mM Pi and failed to grow at 300 mM Pi (Fig. 2C).
PMID:37949217	FYPO:0000646	swollen vegetative cell	Cells were severely deformed/swollen and many were collapsed and probably dying (Figs. 2D and S2).
PMID:37949217	FYPO:0005572	normal protein localization to cell periphery [assayed_protein] PomBase:SPCC1827.07c	In the mutants, Xpr1- GFP was similarly localized to the cell periphery, suggesting that accelerated Pi export in these mutants may not be caused by dynamic alteration of the localization of the exporter, Xpr1
PMID:37949217	FYPO:0005572	normal protein localization to cell periphery [assayed_protein] PomBase:SPCC1827.07c	In the mutants, Xpr1- GFP was similarly localized to the cell periphery, suggesting that accelerated Pi export in these mutants may not be caused by dynamic alteration of the localization of the exporter, Xpr1
PMID:37949217	FYPO:0005572	normal protein localization to cell periphery [assayed_protein] PomBase:SPCC1827.07c	In the mutants, Xpr1- GFP was similarly localized to the cell periphery, suggesting that accelerated Pi export in these mutants may not be caused by dynamic alteration of the localization of the exporter, Xpr1
PMID:37949217	GO:0005886	plasma membrane	It was localized mainly in the cell periphery, probably at the plasma membrane (Fig. 1C), consistent with its role in Pi export.
PMID:37949217	FYPO:0001357	normal vegetative cell population growth	The Pi hyper-sensitivity of Δpqr1Δxpr1 was suppressed by the double gene deletion of Pho84 and Pho842 (Figs. 6A and S6).
PMID:37949217	FYPO:0002060	viable vegetative cell population	This time, we obtained Δpqr1Δxpr1Δvtc4 colonies on PMG with 0.15 mM Pi, which did not grow on either normal PMG (15 mM Pi) or YES.
PMID:37949217	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPCC1827.07c	We found that Xpr1-GFP did not increase in Δpqr1, Δvtc4, or Δpqr1Δvtc4 (Fig. 5G). Accelerated Pi export in these mutants may not be caused by increased amounts of Xpr1 protein.
PMID:37949217	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPCC1827.07c	We found that Xpr1-GFP did not increase in Δpqr1, Δvtc4, or Δpqr1Δvtc4 (Fig. 5G). Accelerated Pi export in these mutants may not be caused by increased amounts of Xpr1 protein.
PMID:37949217	FYPO:0004083	normal protein level [assayed_protein] PomBase:SPCC1827.07c	We found that Xpr1-GFP did not increase in Δpqr1, Δvtc4, or Δpqr1Δvtc4 (Fig. 5G). Accelerated Pi export in these mutants may not be caused by increased amounts of Xpr1 protein.
PMID:37949217	FYPO:0002061	inviable vegetative cell population	We found that spores assumed to be Δpqr1Δxpr1Δvtc4 did not form colonies, suggesting synthetic lethality of gene deletions of pqr1+, xpr1+, and vtc4+ on YES.
PMID:37949217	FYPO:0008228	abnormal phosphate export	Xpr1-dependent Pi export is accelerated by either Δpqr1 or Δvtc4. Importantly, the elevation of Pi export activity in Δpqr1 and Δvtc4 is synergistic. In Δpqr1Δvtc4, exported Pi was far greater than that in the single mutant (Fig. 5D
PMID:37949217	FYPO:0008228	abnormal phosphate export	Xpr1-dependent Pi export is accelerated by either Δpqr1 or Δvtc4. Importantly, the elevation of Pi export activity in Δpqr1 and Δvtc4 is synergistic. In Δpqr1Δvtc4, exported Pi was far greater than that in the single mutant (Fig. 5D
PMID:37949217	FYPO:0008228	abnormal phosphate export [has_severity] high	Xpr1-dependent Pi export is accelerated by either Δpqr1 or Δvtc4. Importantly, the elevation of Pi export activity in Δpqr1 and Δvtc4 is synergistic. In Δpqr1Δvtc4, exported Pi was far greater than that in the single mutant (Fig. 5D
PMID:37949217	FYPO:0008228	abnormal phosphate export [has_severity] high	Xpr1-dependent Pi export is accelerated by either Δpqr1 or Δvtc4. Importantly, the elevation of Pi export activity in Δpqr1 and Δvtc4 is synergistic. In Δpqr1Δvtc4, exported Pi was far greater than that in the single mutant (Fig. 5D
PMID:37949217	FYPO:0008228	abnormal phosphate export [has_severity] high	Xpr1-dependent Pi export is accelerated by either Δpqr1 or Δvtc4. Importantly, the elevation of Pi export activity in Δpqr1 and Δvtc4 is synergistic. In Δpqr1Δvtc4, exported Pi was far greater than that in the single mutant (Fig. 5D
PMID:37956308	FYPO:0005951	decreased nucleosome occupancy at highly transcribed RNA polymerase II genes	15 min after stress imposition, only few nucleosomes were still partially evicted in a wild-type background, whereas the number of nucleosomes which remained significantly less occupied relative to untreated conditions was much higher in cells lacking Top1 (Figure 4D and E; Supplementary Table S5). Of note, the differences observed for the averaged nucleosome maps of the 494 stress genes between wild-type and Δtop1 strains was more dramatic for the highly expressed genes of the quartil 1, than for the genes of the other quartils (unpublished data).
PMID:37956308	GO:0000785	chromatin [coincident_with] promoter_element	As shown in Figure 2A, Top1-HA accumulated at ORFs of the ctt1 and gpd1 genes after peroxide stress
PMID:37956308	GO:0006338	chromatin remodeling	As shown in Supplementary Figure S7F, the stress-dependent recruitment of Ser2-phosphorylated Pol II to the ctt1 gene was significantly higher in cells lacking Hrp1 than in wild-type cells.
PMID:37956308	FYPO:0001103	resistance to hydrogen peroxide	Cells expressing a catalytically-dead version of the enzyme, Top1.Y773F, also displayed resistance to peroxides (Supplementary Figure S1B), suggesting that lack of topoisomerase activity is involved in this phenotype.
PMID:37956308	GO:0045815	transcription initiation-coupled chromatin remodeling	Cells lacking Snf22 and Hrp3 were largely unable to open the chromatin structure at the ctt1 gene upon stress imposition.
PMID:37956308	GO:0045815	transcription initiation-coupled chromatin remodeling	Cells lacking Snf22 and Hrp3 were largely unable to open the chromatin structure at the ctt1 gene upon stress imposition.
PMID:37956308	FYPO:0004066	increased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPCC1442.10c [assayed_region] PomBase:SPCC757.07c	In cells lacking Top1, Pol II recruitment was more sustained than in wild-type cells (compare 60 min in both backgrounds in Figure 2B).
PMID:37956308	FYPO:0001032	resistance to camptothecin	In fact, the Top1 deficient strains displayed resistance to camptothecin, as expected (Supplementary Figure S1C):
PMID:37956308	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPBC29B5.01	Nevertheless, we showed by western blot that Atf1 phosphorylation was not exacerbated in cells lacking Top1 (Figure 1C).
PMID:37956308	FYPO:0001103	resistance to hydrogen peroxide	On the contrary, deletion of hrp1 yielded a strain resistant to H2 O2 , almost to the same extent as Δtop1 (Figure 6B).
PMID:37956308	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	Regarding tolerance to oxidative stress, cells lacking Hrp3 or Snf22 are severely sensitive to oxidative stress (Figure 6A)
PMID:37956308	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	Regarding tolerance to oxidative stress, cells lacking Hrp3 or Snf22 are severely sensitive to oxidative stress (Figure 6A)
PMID:37956308	FYPO:0008245	normal protein localization to chromatin at gene promoter region [assayed_protein] PomBase:SPBC29B5.01	Similarly, we determined by ChIP that Atf1 recruitment to stress promoters was unaltered in Δtop1 cells (Figure 1D).
PMID:37956308	FYPO:0001103	resistance to hydrogen peroxide	The resistance phenotypes of the single deletes did not add in the double deletion strain, suggesting that Top1 and Hrp1 contribute to H2O2 tolerance through a similar mechanism.
PMID:37956308	FYPO:0001103	resistance to hydrogen peroxide	To our surprise, cells lacking Top1 were resistant to H2O2 on plates, when compared to a wild-type strain (Figure 1A).
PMID:37956308	FYPO:0004571	increased RNA level during cellular response to hydrogen peroxide [assayed_transcript] PomBase:SPBC106.02c	We determined by northern blot that the ctt1, srx1 and hsp9 genes, coding for the anti-stress proteins catalase, sulfiredoxin and the chaperone Hsp9, respectively, were up-regulated in Δtop1 cells to a larger extent that in a wild-type strain upon H2O2 stress (Figure 1B and Supplementary Figure S1E)
PMID:37956308	FYPO:0004571	increased RNA level during cellular response to hydrogen peroxide [assayed_transcript] PomBase:SPAP8A3.04c	We determined by northern blot that the ctt1, srx1 and hsp9 genes, coding for the anti-stress proteins catalase, sulfiredoxin and the chaperone Hsp9, respectively, were up-regulated in Δtop1 cells to a larger extent that in a wild-type strain upon H2O2 stress (Figure 1B and Supplementary Figure S1E)
PMID:37956308	FYPO:0004571	increased RNA level during cellular response to hydrogen peroxide [assayed_transcript] PomBase:SPCC757.07c	We determined by northern blot that the ctt1, srx1 and hsp9 genes, coding for the anti-stress proteins catalase, sulfiredoxin and the chaperone Hsp9, respectively, were up-regulated in Δtop1 cells to a larger extent that in a wild-type strain upon H2O2 stress (Figure 1B and Supplementary Figure S1E)
PMID:37956308	FYPO:0000962	normal growth on hydrogen peroxide	and the combination of gene deletions of Δtop1 with either Δhrp3 or Δsnf22 yielded strains with intermediate phenotypes, suggesting that Top1 and these chromatin remodelers affect oxidative stress tolerance through independent mechanisms. (Figure 6A)
PMID:37956308	FYPO:0000962	normal growth on hydrogen peroxide	and the combination of gene deletions of Δtop1 with either Δhrp3 or Δsnf22 yielded strains with intermediate phenotypes, suggesting that Top1 and these chromatin remodelers affect oxidative stress tolerance through independent mechanisms. (Figure 6A)
PMID:37956308	FYPO:0000962	normal growth on hydrogen peroxide	and the combination of gene deletions of Δtop1 with either Δhrp3 or Δsnf22 yielded strains with intermediate phenotypes, suggesting that Top1 and these chromatin remodelers affect oxidative stress tolerance through independent mechanisms. (Figure 6A)
PMID:37956308	FYPO:0000962	normal growth on hydrogen peroxide	and the combination of gene deletions of Δtop1 with either Δhrp3 or Δsnf22 yielded strains with intermediate phenotypes, suggesting that Top1 and these chromatin remodelers affect oxidative stress tolerance through independent mechanisms. (Figure 6A)
PMID:37970674	FYPO:0006995	normal chromatin silencing at centromere inner repeat	(Figure 3D)
PMID:37970674	GO:0061665	SUMO ligase activity [has_input] PomBase:SPAC18G6.10 [part_of] centromere clustering at the mitotic interphase nuclear envelope	(comment: CHECK inhibits)
PMID:37970674	GO:0072766	centromere clustering at the mitotic interphase nuclear envelope	(comment: CHECK inhibits)
PMID:37970674	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] medium	, deletion of either nup132+ or pli1+ results in reduced growth in the presence of 5-FOA, indicating increased expression of ura4+ and hence loss of silencing (Fig. 1C).
PMID:37970674	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] medium	, deletion of either nup132+ or pli1+ results in reduced growth in the presence of 5-FOA, indicating increased expression of ura4+ and hence loss of silencing (Fig. 1C).
PMID:37970674	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC1687.05 [has_severity] high	However, in nup132Δ cells, whereas wild-type Pli1 was destabilised, Pli1K3R levels remained high (Fig. 1B).
PMID:37970674	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC1687.05	However, in nup132Δ cells, whereas wild-type Pli1 was destabilised, Pli1K3R levels remained high (Fig. 1B).
PMID:37970674	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] medium	If the silencing defect in nup132Δ cells were due to destabilisation of Pli1, we would expect it to be rescued by expression of the stabilised Pli1K3R mutant. However, this was not the case - nup132Δ cells expressing Pli1K3R-Flag displayed a defect in silencing equivalent to those expressing wild-type Pli1-Flag
PMID:37970674	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	Similarly, both nup132Δ and pli1Δ cells showed sensitivity to the microtubule-stabilising drug thiabendazole (TBZ), consistent with defects in centromere function, and this TBZ sensitivity was also not rescued by the Pli1K3R mutation (Fig. 1C). T
PMID:37970674	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	Similarly, both nup132Δ and pli1Δ cells showed sensitivity to the microtubule-stabilising drug thiabendazole (TBZ), consistent with defects in centromere function, and this TBZ sensitivity was also not rescued by the Pli1K3R mutation (Fig. 1C). T
PMID:37970674	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	Similarly, both nup132Δ and pli1Δ cells showed sensitivity to the microtubule-stabilising drug thiabendazole (TBZ), consistent with defects in centromere function, and this TBZ sensitivity was also not rescued by the Pli1K3R mutation (Fig. 1C). T
PMID:37970674	FYPO:0000964	normal growth on thiabendazole	Similarly, both nup132Δ and pli1Δ cells showed sensitivity to the microtubule-stabilising drug thiabendazole (TBZ), consistent with defects in centromere function, and this TBZ sensitivity was also not rescued by the Pli1K3R mutation (Fig. 1C). T
PMID:38041816	GO:0110085	mitotic actomyosin contractile ring [exists_during] mitotic metaphase	As expected, Rng2 localized to the nodes and ring upon entry into mitosis (Figure 4B), w
PMID:38041816	FYPO:0005022	decreased rate of protein localization to actomyosin contractile ring	GFP-Rng2-CHDΔ behaved like the WT in all aspects (Figures 5E-5H), except for the loss of accumulation during the slow phase (Figure 5F, from −15 to 0 min).
PMID:38041816	FYPO:0002023	abnormal septum morphology during vegetative growth [has_penetrance] 50	However, when both domains were deleted together (rng2-CHDΔ-CykFΔ), most cells showed strong defects in cytokinesis, especially at 36°C, where >90% of the cells formed cell chains with various abnormal septa, including some “catastrophic” structures (Figures 5B-5D).
PMID:38041816	FYPO:0002023	abnormal septum morphology during vegetative growth [has_penetrance] 90	However, when both domains were deleted together (rng2-CHDΔ-CykFΔ), most cells showed strong defects in cytokinesis, especially at 36°C, where >90% of the cells formed cell chains with various abnormal septa, including some “catastrophic” structures (Figures 5B-5D).
PMID:38041816	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPAC4F8.13c	Indeed, the fragment (aa 185-300) containing the CykF domain localized weakly, but consistently, to the division site during cytokinesis (Figures 4E and S4A and Video S3), suggesting that the binding affinity between CykF and the cytokinesis factor(s) is low.
PMID:38041816	FYPO:0002559	normal protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPAC4F8.13c	Strikingly, the Rng2 fragment (aa 1-300), previously called Rng2Ns,44 began to localize to the division site at the onset of anaphase and constricted during cytokinesis (Figure 4D and Video S3)
PMID:38041816	FYPO:0001365	decreased rate of actomyosin contractile ring contraction	The removal of GFP-Rng2-CykFΔ was also slowed down (Figures 5E and 5F), and its rate of constriction was reduced by ~30% compared with GFP-Rng2 (Figure 5H, p < 0.01)
PMID:38041816	FYPO:0000729	delayed onset of actomyosin contractile ring assembly	The rng2-CykFΔ cells also assembled actin rings (Figures 6A and 6B), but the ring emergence and removal were significantly delayed (Figures 6B-6D)
PMID:38041816	FYPO:0002023	abnormal septum morphology during vegetative growth [has_penetrance] 10	The rng2-CykFΔ cells did not show any apparent defect in cell morphology, but ~10% of the cells formed a partial or complete septum doublet at both temperatures, suggesting a moderate defect in cytokinesis (Figures 5B-5D and S4C).
PMID:38041816	FYPO:0006213	normal septum morphology	We found that the rng2-CHDΔ cells displayed similar cell and septum morphologies compared with the WT (rng2 +) cells at both temperatures (Figures 5B-5D and S4C).
PMID:38041816	FYPO:0004652	normal actomyosin contractile ring morphology	s. Surprisingly, the rng2- CHDΔ cells formed WT-like actin rings, as revealed by phalloidin staining (Figure 6A), despite the ability of CHD to bind F-actin.3
PMID:38041816	FYPO:0002699	decreased protein localization to actomyosin contractile ring [assayed_protein] PomBase:SPAC4F8.13c	whereas the CHD (aa 1-190) localized to all F-actin structures including actin cables, actin patches, and the actin ring (Figure 4C and Video S3).44,45
PMID:38048463	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] high	(Fig. 1C)
PMID:38048463	FYPO:0006814	increased histone H3-K9 acetylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 1E)
PMID:38048463	FYPO:0006814	increased histone H3-K9 acetylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 1E)
PMID:38048463	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 1F)
PMID:38048463	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] high	(Fig. 1G)
PMID:38048463	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] high	(Fig. 1G)
PMID:38048463	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 1G)
PMID:38048463	FYPO:0004604	decreased chromatin silencing at subtelomere [has_penetrance] high	(Fig. 1H)
PMID:38048463	GO:0031509	subtelomeric heterochromatin formation	(Fig. 1H)
PMID:38048463	FYPO:0003555	normal chromatin silencing at subtelomere	(Fig. 1H)
PMID:38048463	FYPO:0004604	decreased chromatin silencing at subtelomere [has_penetrance] high	(Fig. 1H)
PMID:38048463	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] medium	(Fig. 2E)
PMID:38048463	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] medium	(Fig. 2F)
PMID:38048463	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] medium	(Fig. 3B)
PMID:38048463	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] medium	(Fig. 3B)
PMID:38048463	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] high	(Fig. 3B)
PMID:38048463	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] high	(Fig. 3C)
PMID:38048463	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] high	(Fig. 4B)
PMID:38048463	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPBC36.05c [has_severity] low	(Fig. 4C)
PMID:38048463	FYPO:0002387	decreased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPBC36.05c [has_severity] medium	(Fig. 4D)
PMID:38048463	FYPO:0003576	normal protein localization to subtelomeric heterochromatin [assayed_protein] PomBase:SPBC36.05c	(Fig. 4E)
PMID:38048463	FYPO:0003010	increased protein localization to subtelomeric heterochromatin during vegetative growth [assayed_protein] PomBase:SPBC36.05c [has_severity] high	(Fig. 4E)
PMID:38048463	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] low	(Fig. 5B and C)
PMID:38048463	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPAC18G6.02c [has_severity] medium	(Fig. 5C)
PMID:38048463	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] medium	(Fig. 5D)
PMID:38048463	GO:0031509	subtelomeric heterochromatin formation	(Fig. 5D)
PMID:38048463	FYPO:0004604	decreased chromatin silencing at subtelomere [has_penetrance] low	(Fig. 5D)
PMID:38048463	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] medium	(Fig. 5D)
PMID:38048463	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] high	Phenotype of rad25 deletion amplified by rex1BD deletion at otr3R10 (Fig. 5B)
PMID:38048463	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] high	Phenotype of rad25 deletion amplified by rex1BD deletion at otr3R10 (Fig. 5B)
PMID:38048463	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	We found that the rex1BDΔ cells were also sensitive to MMS, but relatively mild compared with apn2Δ (SI Appendix, Fig. S4).
PMID:38048463	GO:0005634	nucleus	We observed that overexpressed Rex1BD-GFP was enriched within the nucleus, consistent with its role as a heterochromatin factor (SI Appendix, Fig. S3).
PMID:38051102	FYPO:0002798	decreased protein degradation during nitrogen starvation [assayed_protein] PomBase:SPAC16.05c	(SHOULD I CHANGE THIS TO DELAYED?????) The reduction of the Sfp1 protein upon nitrogen starvation was significantly delayed in the mts3-1 mutant (Fig. 2K), suggesting that the stability of Sfp1 during starvation is regulated by the proteasome.
PMID:38051102	FYPO:0001409	normal growth on glycerol carbon source	Although the growth defect of the Dsfp1 mutant was observed on glucose medium, it grew normally on medium containing glycerol as the carbon source (Fig. 1H), similar to the situation in budding yeast.27
PMID:38051102	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	Although the growth defect of the Dsfp1 mutant was observed on glucose medium, it grew normally on medium containing glycerol as the carbon source (Fig. 1H), similar to the situation in budding yeast.27. ALSO Figure 4B for severity
PMID:38051102	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	Although the growth defect of the Dsfp1 mutant was observed on glucose medium, it grew normally on medium containing glycerol as the carbon source (Fig. 1H), similar to the situation in budding yeast.27. ALSO Figure 4B for severity
PMID:38051102	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC16.05c	An in vitro kinase assay using Sfp1 as a substrate indicated that Sfp1 is a substrate of TORC1 (Fig. 2M).
PMID:38051102	GO:0005634	nucleus	Fhl1 was constitutively found in the nucleus, without being affected by TORC1 inactivation (Fig. 6D) or the loss of Sfp1 (Fig. 6F).
PMID:38051102	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	Importantly, no significant additive phenotype was observed when the mutations were combined (Fig. 4B), suggesting that Sfp1, Ifh1, and Fhl1 function in the same pathway that regulates cell proliferation. Consistently, like the Dsfp1 mutation (Fig. 1I), the Difh1 and Dfhl1 mutations were also able to ameliorate the growth defect caused by the absence of the functional GATOR1 complex (Fig. 4C).
PMID:38051102	FYPO:0000111	sensitive to rapamycin [has_severity] low	In contrast, the Dsfp1 mutant exhibited a modest growth defect as well as limited rapamycin sensitivity (Fig. 1G), consistent with the notion that Sfp1 is involved in cell proliferation regulated by TORC1.
PMID:38051102	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPAC16.05c	In the tor2-287 and tor2-13 mutants, the Sfp1 protein dramatically decreased within 2h after shifting to the restrictive temperature (Fig. 2A)
PMID:38051102	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPAC16.05c	In the tor2-287 and tor2-13 mutants, the Sfp1 protein dramatically decreased within 2h after shifting to the restrictive temperature (Fig. 2A)
PMID:38051102	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPAC1142.08 [assayed_protein] PomBase:SPAC22H10.11c	It was found, however, that the amount of the Ifh1-Fhl1 complex was reduced in the Dsfp1 mutant when compared to that in the wild-type strain.
PMID:38051102	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPAC16.05c	Moreover, the nuclear signal of Ifh1 was also significantly reduced in the Dsfp1 mutant (Fig. 6F), though neither the protein level nor the mobility shift of Ifh1 was affected by the Dsfp1 mutation (Fig. 6G).
PMID:38051102	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] high	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] high	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] high	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	Notably, the absence of Sfp1 modestly alleviates the growth defect of the mutants lacking functional GATOR1 (Fig. 1I); the absence of GATOR1 causes a severe growth defect due to deregulated TORC1 activation,28 and therefore, the observed genetic interaction corroborates a functional link between Sfp1 and TORC1.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC21B10.10	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1071.08	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC11G7.04	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC144.11	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1687.06c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1783.08c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC17G6.06	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1805.12c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1F7.13c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC22A12.04c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC31G5.03	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC3G9.03	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC3H5.05c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC589.10c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC644.15	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC664.05	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC6G9.09c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC806.03c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC890.08	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC959.07	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC959.08	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAP7G5.05	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAPB1E7.12	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC106.18	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC16D10.11c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC18H10.13	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC18H10.14	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC23G7.15c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC2F12.07c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC3D6.15	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC577.02	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC685.07c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC839.05c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBP22H7.08	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC1322.11	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC1322.15	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC1393.03	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC330.14c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC576.08c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC576.09	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC576.11	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC5E4.07	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC613.06	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCP1E11.09c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCP31B10.08c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1142.04	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC140.02	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1486.09	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1556.05c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1565.05	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1687.11	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC16C9.03	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1782.10c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC18G6.07c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC19A8.07c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC19B12.11c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1B3.13	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1B9.03c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1F7.02c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC20G8.09c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC222.06	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC22E12.13c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC22G7.05	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC23H4.15	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC29A4.04c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC2F7.05c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC30D11.03	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC3F10.16c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC3F10.17	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC3G6.04	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC4F10.09c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC4F8.04	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC57A7.06	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC607.03c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC664.06	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC664.08c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC6F12.16c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC6G9.02c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC823.08c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC890.04c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC8F11.04	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC959.03c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC11G11.03	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC14F5.06	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1604.06c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1604.09c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC16H5.08c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC16H5.10c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1711.07	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC1711.16	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC17D1.06	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC19F5.05c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC20F10.01	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC215.06c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC21H7.04	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC23E6.05	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC23G7.07c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC24C6.02	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC26H8.08c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC29A3.06	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC29A3.16	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC2D10.10c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC336.02	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC3B8.09	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC3F6.04c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC4F6.13c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC4F6.14	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC646.10c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC651.01c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC800.06	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC8D2.10c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBP8B7.16c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBP8B7.20c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC1494.06c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC1672.07	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC16A11.02	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC16C4.08c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC18.12c	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC1919.09	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC330.09	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCC830.03	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPCP1E11.08	Our RNA-seq data indicated that among 141 RP and 292 Ribi genes in fission yeast (Supplementary material, Table S1), 31.9% of the RP genes (45 genes) and 26.4% of the Ribi genes (77 genes) are downregulated in the Dsfp1 mutant (Fig. 3B and C, and Supplementary material, Table S2). Collectively, these results imply that the Sfp1 transcription factor promotes the expression of the genes required for ribosome biosynthesis, a critical process for protein synthesis linked to cell growth.
PMID:38051102	GO:0005634	nucleus	Remarkably, we discovered that Ifh1 accumulates in the nucleus in a TORC1- dependent manner. In wild-type cells expressing Ifh1 with the fluorescent mEGFP tag, Ifh1 appeared to be concentrated in the nucleus, with some cytoplasmic signals (Fig. 6D).
PMID:38051102	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPBC216.07c [assayed_substrate] PomBase:SPCC4G3.08	TORC1 activity monitored by the Psk1 phosphorylation was comparable between wild-type and Dsfp1 cells before and after nitrogen starvation (Fig. 1F), further confirming that Sfp1 does not affect TORC1 activity.
PMID:38051102	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1142.08 [assayed_protein] PomBase:SPAC22H10.11c	The Ifh1-Fhl1 association was detected both in the presence and absence of Sfp1, suggesting that Sfp1 is not required for their interaction (Fig. 4F).
PMID:38051102	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC1142.08 [assayed_protein] PomBase:SPAC22H10.11c	The interaction between Fhl1 and Ifh1 was impaired in the mutant expressing Fhl1 without the N-terminal 150 amino acid residues (Fig. 4E), indicating that the Ifh1-FHl1 interaction depends on the forkhead-associated (FHA) domain of Fhl1.
PMID:38051102	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPBC216.07c [assayed_substrate] PomBase:SPCC4G3.08	The level of Psk1 phosphorylation was comparable between wild-type and tor2-287 cells growing at 25  C (Fig. 1E). Upon temperature shift to the restrictive temperature, dephosphorylation of Psk1 was observed with similar kinetics both in the presence and absence of Sfp1 overexpression (Fig. 1E), suggesting that Sfp1 does not affect TORC1 activity.
PMID:38051102	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	The screen isolated a plasmid, pALSK53, which suppressed the ts growth phenotype and rapamycin sensitivity of the tor2-13 mutant (Fig. 1A).
PMID:38051102	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	The screen isolated a plasmid, pALSK53, which suppressed the ts growth phenotype and rapamycin sensitivity of the tor2-13 mutant (Fig. 1A).
PMID:38051102	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	The screen isolated a plasmid, pALSK53, which suppressed the ts growth phenotype and rapamycin sensitivity of the tor2-13 mutant (Fig. 1A).
PMID:38051102	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	Truncation of amino acids 84 to 105 or amino acids 293 to 442 of Sfp1, which removes the N-terminal or C-terminal zinc finger domains, resulted in reduced growth defect suppression in the tor2-287 mutant compared to full-length Sfp1 (Fig. 1D).
PMID:38051102	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	Truncation of amino acids 84 to 105 or amino acids 293 to 442 of Sfp1, which removes the N-terminal or C-terminal zinc finger domains, resulted in reduced growth defect suppression in the tor2-287 mutant compared to full-length Sfp1 (Fig. 1D).
PMID:38051102	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPAC22H10.11c	When TORC1 was inactivated in the tor2-13 or tor2-287 mutants at the restrictive temperature, the electrophoretic mobility of Ifh1 was notably decreased (Fig. 6A). The slow migrating form of Ifh1 was also observed when TORC1 was inactivated in wild-type cells starved of nitrogen (Fig. 6B). Phosphatase treatment experiments confirmed that slow-migrating Ifh1 was its phosphorylated form (Fig. 6B).
PMID:38051102	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPAC22H10.11c	When TORC1 was inactivated in the tor2-13 or tor2-287 mutants at the restrictive temperature, the electrophoretic mobility of Ifh1 was notably decreased (Fig. 6A). The slow migrating form of Ifh1 was also observed when TORC1 was inactivated in wild-type cells starved of nitrogen (Fig. 6B). Phosphatase treatment experiments confirmed that slow-migrating Ifh1 was its phosphorylated form (Fig. 6B).
PMID:38051102	FYPO:0004455	decreased protein localization to nucleus [assayed_protein] PomBase:SPAC22H10.11c	or the tor2-287 mutation (Fig. 6E), the nuclear accumulation of Ifh1 was largely lost while no change in the Ifh1 protein levels was observed (Fig. 6B), implying that TORC1 promotes the nuclear localization of Ifh
PMID:38084929	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 1C)
PMID:38084929	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1E)
PMID:38084929	FYPO:0003786	abolished protein localization to centromere central core during vegetative growth [assayed_protein] PomBase:SPAPB1A10.02	(Fig. 2A-B)
PMID:38084929	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAPB1A10.02	(Fig. 2C)
PMID:38084929	FYPO:0003786	abolished protein localization to centromere central core during vegetative growth [assayed_protein] PomBase:SPAPB1A10.02	(Fig. 3A)
PMID:38084929	FYPO:0002060	viable vegetative cell population	(Fig. 3B)
PMID:38084929	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3B)
PMID:38084929	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3B)
PMID:38084929	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3B)
PMID:38084929	FYPO:0001357	normal vegetative cell population growth	(Fig. 3C and 3E)
PMID:38084929	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAPB1A10.02	(Fig. 3D)
PMID:38084929	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3E)
PMID:38084929	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 4A)
PMID:38084929	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 4A)
PMID:38084929	FYPO:0000450	decreased protein localization to centromere during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPBC1861.01c	(Fig. 4B-C)
PMID:38084929	FYPO:0001840	increased minichromosome loss during vegetative growth	(Fig. 4D)
PMID:38084929	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] high [has_penetrance] 50	(Fig. 4E)
PMID:38084929	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAPB1A10.02	(Fig. 5B)
PMID:38084929	FYPO:0000450	decreased protein localization to centromere during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPAPB1A10.02	(Fig. 5B-C)
PMID:38084929	FYPO:0003786	abolished protein localization to centromere central core during vegetative growth [assayed_protein] PomBase:SPAPB1A10.02	(Fig. 6A)
PMID:38084929	FYPO:0001357	normal vegetative cell population growth	(Fig. 6B)
PMID:38084929	FYPO:0001357	normal vegetative cell population growth	(Fig. 6B)
PMID:38084929	FYPO:0001357	normal vegetative cell population growth	(Fig. 6B)
PMID:38084929	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 6B)
PMID:38084929	FYPO:0001357	normal vegetative cell population growth	(Fig. 6B)
PMID:38084929	FYPO:0001357	normal vegetative cell population growth	(Fig. 6B)
PMID:38084929	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 80	(Fig. 6C-D)
PMID:38084929	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPBC1861.01c	(Fig. 7)
PMID:38084929	FYPO:0007853	normal protein localization to centromere [assayed_protein] PomBase:SPBC18E5.03c	(Fig. 7)
PMID:38084929	FYPO:0007853	normal protein localization to centromere [assayed_protein] PomBase:SPBC1861.01c	(Fig. 7)
PMID:38084929	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPBC1105.17	(Fig. 7)
PMID:38084929	FYPO:0007853	normal protein localization to centromere [assayed_protein] PomBase:SPBC1105.17	(Fig. 7)
PMID:38084929	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPBC18E5.03c	(Fig. 7)
PMID:38084929	FYPO:0001355	decreased vegetative cell population growth	(Fig. S3B)
PMID:38084929	FYPO:0003744	abolished protein localization to centromeric chromatin during vegetative growth	(Fig. S5)
PMID:38084929	FYPO:0000634	abolished protein localization to centromere during vegetative growth	(Fig. S6A)
PMID:38084929	FYPO:0003786	abolished protein localization to centromere central core during vegetative growth	(Fig. S6B)
PMID:38084929	FYPO:0000450	decreased protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAPB1A10.02	(Fig. S7A)
PMID:38084929	FYPO:0000450	decreased protein localization to centromere during vegetative growth [has_severity] high [assayed_protein] PomBase:SPBC1105.17	(Fig. S7C-D)
PMID:38084929	FYPO:0006238	decreased protein localization to centromere [has_severity] medium [assayed_protein] PomBase:SPAPB1A10.02	(Fig. S9B)
PMID:38084929	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAPB1A10.02	As expected, the combination of mutations in both CYS (i.e. Scm34A) and Mis16 abrogated the formation of Scm3 cen- tromeric foci (Supplementary Figure S7A).
PMID:38084929	FYPO:0000634	abolished protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAPB1A10.02	As expected, the combination of mutations in both CYS (i.e. Scm34A) and Mis16 abrogated the formation of Scm3 cen- tromeric foci (Supplementary Figure S7A).
PMID:38084929	FYPO:0002574	normal protein localization to centromere during vegetative growth [assayed_protein] PomBase:SPAPB1A10.02	CT shows normal localization (Fig. 5B)
PMID:38084929	GO:0008270	zinc ion binding	However,upon the removal of Zn2+ using EDTA,the spectrum reverted to that of the free peptide (Supplementary Figure S2C,right) indicating that,as predicted,CYS can bind Zn2+ .
PMID:38084929	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	Whereas scm3FL successfully rescued the growth defect, scm3ΔCYS did not show any noticeable res- cue of the temperature-sensitive growth phenotype (Figure 1E).
PMID:38097609	FYPO:0001489	inviable vegetative cell	(Fig. 6A)
PMID:38097609	FYPO:0001489	inviable vegetative cell	(Fig. 6A)
PMID:38097609	FYPO:0001489	inviable vegetative cell	(Fig. 6A)
PMID:38097609	FYPO:0001489	inviable vegetative cell	(Fig. 6A)
PMID:38097609	FYPO:0001489	inviable vegetative cell	(Fig. 6A)
PMID:38097609	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 6A)
PMID:38097609	FYPO:0001489	inviable vegetative cell	(Fig. 6A)
PMID:38097609	FYPO:0001489	inviable vegetative cell	(Fig. 6A)
PMID:38097609	FYPO:0001489	inviable vegetative cell	(Fig. 6A)
PMID:38097609	FYPO:0001489	inviable vegetative cell	(Fig. 6A)
PMID:38097609	FYPO:0001357	normal vegetative cell population growth	(Fig. S6A)
PMID:38097609	FYPO:0001357	normal vegetative cell population growth	(Fig. S6A)
PMID:38097609	FYPO:0001357	normal vegetative cell population growth	(Fig. S6A)
PMID:38097609	FYPO:0001357	normal vegetative cell population growth	(Fig. S6A)
PMID:38097609	FYPO:0001357	normal vegetative cell population growth	(Fig. S6A)
PMID:38097609	FYPO:0001357	normal vegetative cell population growth	(Fig. S6A)
PMID:38097609	FYPO:0001489	inviable vegetative cell	(Fig. S6C)
PMID:38097609	FYPO:0001357	normal vegetative cell population growth	(Fig. S6C)
PMID:38097609	FYPO:0001357	normal vegetative cell population growth	(Fig. S6C)
PMID:38097609	FYPO:0001489	inviable vegetative cell	(Fig. S6C)
PMID:38097609	FYPO:0001489	inviable vegetative cell	(Fig. S6D)
PMID:38097609	FYPO:0001489	inviable vegetative cell	(Fig. S6D)
PMID:38133430	FYPO:0001355	decreased vegetative cell population growth	(Fig. 2, Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0001355	decreased vegetative cell population growth	(Fig. 2, Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 2, Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 2, Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	(Fig. 3B)
PMID:38133430	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC23D3.12	(Fig. 3B)
PMID:38133430	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1683.01	(Fig. 3B)
PMID:38133430	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 3B)
PMID:38133430	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB2B2.06c	(Fig. 3B)
PMID:38133430	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	(Fig. 3B)
PMID:38133430	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 3B)
PMID:38133430	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 3B)
PMID:38133430	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1683.01	(Fig. 3B)
PMID:38133430	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC23D3.12	(Fig. 3B)
PMID:38133430	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB2B2.06c	(Fig. 3B)
PMID:38133430	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 3B)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0005369	abolished cell population growth at low temperature	(Fig. 4A)
PMID:38133430	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 4A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 4A)
PMID:38133430	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 4A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:38133430	FYPO:0005369	abolished cell population growth at low temperature	(Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0005369	abolished cell population growth at low temperature	(Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 4A, Fig. S3A)
PMID:38133430	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:38133430	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:38133430	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:38133430	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:38133430	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:38133430	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C, Fig. S3B)
PMID:38133430	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C, S3B)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 5A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 5A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 5A)
PMID:38133430	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 5A)
PMID:38133430	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 5A)
PMID:38133430	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 5A)
PMID:38133430	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 5A)
PMID:38133430	FYPO:0002141	normal cell population growth at low temperature	(Fig. 5A)
PMID:38133430	FYPO:0002141	normal cell population growth at low temperature	(Fig. 5A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 5A)
PMID:38133430	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:38133430	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 5B)
PMID:38133430	FYPO:0002141	normal cell population growth at low temperature	(Fig. 6A)
PMID:38133430	FYPO:0000674	normal cell population growth at high temperature	(Fig. 6A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 6A)
PMID:38133430	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 6A)
PMID:38133430	FYPO:0000674	normal cell population growth at high temperature	(Fig. 6A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 6A)
PMID:38133430	FYPO:0002141	normal cell population growth at low temperature	(Fig. 6A)
PMID:38133430	FYPO:0004481	abolished cell population growth at high temperature	(Fig. 6A)
PMID:38133430	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 6A, S3A)
PMID:38133430	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 6A, S3A)
PMID:38133430	FYPO:0001355	decreased vegetative cell population growth	(Fig. 6A, S3A)
PMID:38133430	FYPO:0001355	decreased vegetative cell population growth	(Fig. 6A, S3A)
PMID:38133430	FYPO:0005369	abolished cell population growth at low temperature	(Fig. 6A, S3A)
PMID:38133430	FYPO:0005369	abolished cell population growth at low temperature	(Fig. 6A, S3A)
PMID:38133430	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:38133430	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:38133430	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:38133430	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:38133430	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6B)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 7A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 7A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 7A)
PMID:38133430	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:38133430	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:38133430	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 7B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB2B2.06c	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB2B2.06c	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB2B2.06c	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.12c	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.12c	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.12c	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1271.09	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 8B)
PMID:38133430	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 8B)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38133430	FYPO:0001355	decreased vegetative cell population growth	(Fig. 9)
PMID:38133430	FYPO:0001355	decreased vegetative cell population growth	(Fig. 9)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38133430	FYPO:0000082	decreased cell population growth at high temperature	(Fig. S3A)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. S3A)
PMID:38133430	FYPO:0005369	abolished cell population growth at low temperature	(Fig. S3A)
PMID:38133430	FYPO:0002085	normal vegetative cell growth	(Fig. S3A)
PMID:38133430	FYPO:0002085	normal vegetative cell growth	(Fig. S3A)
PMID:38133430	FYPO:0001355	decreased vegetative cell population growth	(Fig. S3A)
PMID:38133430	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S3B)
PMID:38133430	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S3B)
PMID:38133430	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. S3B)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. S5)
PMID:38133430	FYPO:0001357	normal vegetative cell population growth	(Fig. S5)
PMID:38166399	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	As mitosis progressed, it was faintly found on the entire length of the spindle and SPB in the wild-type cells (Figure 3a). By contrast, Mad2 was found as one or two bright speckles in the vicinity of the spindle during mitosis in the wee1 mutant (Figure 3b,c). Judged by the length of the spindle, anaphase was initiated soon after Mad2 speckles disappeared (Figure 4a,b). In approximately 28% (28 cells out of 101 cells observed) of the wee1 mutants, the Mad2 speckle appeared at least once (Figure 4c). The observation thus suggested that the spindle checkpoint was activated in the wee1 mutants.
PMID:38166399	FYPO:0002061	inviable vegetative cell population	As shown in electronic supplementary material, Figure S1A, we found that a wee1-50 mad2Δ double mutant is lethal at 36°C.
PMID:38166399	FYPO:0002061	inviable vegetative cell population	As shown in electronic supplementary material, Figure S1A, we found that a wee1-50 mad2Δ double mutant is lethal at 36°C.
PMID:38166399	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	As shown in electronic supplementary material, Figure S1B, introduction of deletion for mad2+ did not cause the lethality in the cdc2-1w and cdc2-3w mutants.
PMID:38166399	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	As shown in electronic supplementary material, Figure S1B, introduction of deletion for mad2+ did not cause the lethality in the cdc2-1w and cdc2-3w mutants.
PMID:38166399	FYPO:0000730	long spindle	Importantly, the onset of anaphase was postponed until all the satellite kinetochores merged with the main cluster in the mutant (Figure 2a,b).
PMID:38166399	FYPO:0000324	mitotic metaphase/anaphase transition delay	Importantly, the onset of anaphase was postponed until all the satellite kinetochores merged with the main cluster in the mutant (Figure 2a,b).
PMID:38166399	FYPO:0004562	binucleate aseptate vegetative cell [has_penetrance] 10	Importantly, the onset of anaphase was postponed until all the satellite kinetochores merged with the main cluster in the mutant (Figure 2a,b).
PMID:38166399	FYPO:0005411	increased number of unattached kinetochores [has_penetrance] 29	Time-lapse imaging analysis revealed abnormal positioning of kinetochores in the wee1 (wee1Δ) mutant. ThBecause the kinetochores, which are captured and bioriented, are clustered and found on the spindle, the satellite kinetochores remained unattached, or detached from the spindle during the progression to anaphase in the wee1 mutant (electronic supplementary material, Figure S2).e cluster of kinetochores frequently fell apart into a main cluster and a small ‘satellite kinetochore’ during mitosis (Figure 1b).
PMID:38166399	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 9	s shown in Figure 5, the wee1 mutants with no functional spindle checkpoint indeed failed in accurate chromosome segregation and generated two sister cells with unequal nuclear size.
PMID:38166399	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 42	s shown in Figure 5, the wee1 mutants with no functional spindle checkpoint indeed failed in accurate chromosome segregation and generated two sister cells with unequal nuclear size.
PMID:38166399	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 9	s shown in Figure 5, the wee1 mutants with no functional spindle checkpoint indeed failed in accurate chromosome segregation and generated two sister cells with unequal nuclear size.
PMID:38166399	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 7	s shown in Figure 5, the wee1 mutants with no functional spindle checkpoint indeed failed in accurate chromosome segregation and generated two sister cells with unequal nuclear size.
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c	(Fig 5A)
PMID:38181050	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1E)
PMID:38181050	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1E)
PMID:38181050	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1E)
PMID:38181050	FYPO:0003151	decreased protein level during cellular response to heat [assayed_protein] PomBase:SPBC146.09c	(Figure 6)
PMID:38181050	FYPO:0003151	decreased protein level during cellular response to heat [assayed_protein] PomBase:SPCC306.04c	(Figure 6)
PMID:38181050	FYPO:0003151	decreased protein level during cellular response to heat [assayed_protein] PomBase:SPCC306.04c	(Figure 6)
PMID:38181050	FYPO:0003151	decreased protein level during cellular response to heat [assayed_protein] PomBase:SPBC146.09c	(Figure 6)
PMID:38181050	FYPO:0003151	decreased protein level during cellular response to heat [assayed_protein] PomBase:SPAC23E2.02	(Figure 6)
PMID:38181050	FYPO:0003151	decreased protein level during cellular response to heat [assayed_protein] PomBase:SPAC23E2.02	(Figure 6)
PMID:38181050	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC23E2.02	A similar pattern was observed in the Lsd2 samples, although the Lsd2 protein levels also decreased with shg1Δ (Fig 3B).
PMID:38181050	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC23E2.02	A similar pattern was observed in the Lsd2 samples, although the Lsd2 protein levels also decreased with shg1Δ (Fig 3B).
PMID:38181050	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC23E2.02	A similar pattern was observed in the Lsd2 samples, although the Lsd2 protein levels also decreased with shg1Δ (Fig 3B).
PMID:38181050	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC23E2.02	A similar pattern was observed in the Lsd2 samples, although the Lsd2 protein levels also decreased with shg1Δ (Fig 3B).
PMID:38181050	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC23E2.02	A similar pattern was observed in the Lsd2 samples, although the Lsd2 protein levels also decreased with shg1Δ (Fig 3B).
PMID:38181050	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC23E2.02	A similar pattern was observed in the Lsd2 samples, although the Lsd2 protein levels also decreased with shg1Δ (Fig 3B).
PMID:38181050	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC30D11.08c [assayed_protein] PomBase:SPAC23E2.02	Additionally, we established that the loss of the HMG-domain of Lsd1 does not affect the interaction between Lsd1 and Phf1 (Fig 1D) or Phf2 (Fig 1E)
PMID:38181050	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC4G3.07c [assayed_protein] PomBase:SPAC23E2.02	Additionally, we established that the loss of the HMG-domain of Lsd1 does not affect the interaction between Lsd1 and Phf1 (Fig 1D) or Phf2 (Fig 1E)
PMID:38181050	FYPO:0003151	decreased protein level during cellular response to heat [assayed_protein] PomBase:SPCC306.04c	Although no significant alterations were detected for Flag-Set1 protein levels between wild-type and clr4W31G cells at 30 ̊C, the elevated Flag-Set1 is less pronounced in clr4W31G compared to clr4Δ at 37 ̊C (Fig 5B)
PMID:38181050	FYPO:0003151	decreased protein level during cellular response to heat [assayed_protein] PomBase:SPAC23E2.02	At 37 ̊C, only marginal changes in Lsd1 protein levels were observed in H3K4R and H2B-K119R mutants (Fig 6D). However, a significant reduction of Lsd2 was seen in both H3K4R and H2B K119R mutants (Fig 6E)
PMID:38181050	FYPO:0003151	decreased protein level during cellular response to heat [assayed_protein] PomBase:SPAC23E2.02	At 37 ̊C, only marginal changes in Lsd1 protein levels were observed in H3K4R and H2B-K119R mutants (Fig 6D). However, a significant reduction of Lsd2 was seen in both H3K4R and H2B K119R mutants (Fig 6E)
PMID:38181050	PomGeneEx:0000018	protein level increased	Both Lsd1 (Fig 4C) and Lsd2 (Fig 4D) protein levels drastically increase after heat treatment, although the mRNA levels of Lsd1 and Lsd2 were not significantly altered between wild-type and set1Δ cells (S10 Fig), suggesting that enhanced Lsd1/2 proteins are required for cell survival under heat stress [61].
PMID:38181050	PomGeneEx:0000018	protein level increased	Both Lsd1 (Fig 4C) and Lsd2 (Fig 4D) protein levels drastically increase after heat treatment, although the mRNA levels of Lsd1 and Lsd2 were not significantly altered between wild-type and set1Δ cells (S10 Fig), suggesting that enhanced Lsd1/2 proteins are required for cell survival under heat stress [61].
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c	Both cul4-1 or ddb1Δ enhanced the amount of Set1 protein, indicating that both CLRC and CRL4 complexes modulate Set1 levels (Fig 5C)
PMID:38181050	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC146.09c	However, the loss of Shg1 and Sdc1 seems to have little or no effect on Lsd1 protein levels.
PMID:38181050	FYPO:0006163	normal protein localization to chromatin [assayed_protein] PomBase:SPBC146.09c	However, the loss of Shg1 and Sdc1 seems to have little or no effect on Lsd1 protein levels.
PMID:38181050	FYPO:0003151	decreased protein level during cellular response to heat [assayed_protein] PomBase:SPAC23E2.02	However, without Set1, Lsd1/2 protein levels are no longer upregulated during heat stress (Fig 4C and 4D), which implies that Set1 is required to elevate the protein levels of Lsd1 and Lsd2 under heat stress.
PMID:38181050	FYPO:0003151	decreased protein level during cellular response to heat [assayed_protein] PomBase:SPBC146.09c	However, without Set1, Lsd1/2 protein levels are no longer upregulated during heat stress (Fig 4C and 4D), which implies that Set1 is required to elevate the protein levels of Lsd1 and Lsd2 under heat stress.
PMID:38181050	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC146.09c	In contrast, the protein levels of Lsd1-FTP and Lsd2-FTP show a notable decrease in the absence of Set1 (Fig 2I).
PMID:38181050	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC23E2.02	In contrast, the protein levels of Lsd1-FTP and Lsd2-FTP show a notable decrease in the absence of Set1 (Fig 2I).
PMID:38181050	PomGeneEx:0000024	protein level fluctuates [during] cellular response to heat	In wild-type cells, we observed a significantly increased amount of Set1 at 37 ̊C (Fig 6A), indicating that Set1 is also stabilized during heat stress.
PMID:38181050	FYPO:0008211	decreased antisense RNA level during heat stress [assayed_protein] PomBase:SPBC146.09c	Intriguingly, about 72% of downregulated genes in lsd1-ΔHMG, lsd2-ΔC, and set1Δ are antisense non-coding RNAs (S1 Table)
PMID:38181050	FYPO:0004816	decreased antisense RNA level [assayed_protein] PomBase:SPBC146.09c	Intriguingly, about 72% of downregulated genes in lsd1-ΔHMG, lsd2-ΔC, and set1Δ are antisense non-coding RNAs (S1 Table)
PMID:38181050	FYPO:0008211	decreased antisense RNA level during heat stress [assayed_protein] PomBase:SPBC146.09c	Intriguingly, about 72% of downregulated genes in lsd1-ΔHMG, lsd2-ΔC, and set1Δ are antisense non-coding RNAs (S1 Table)
PMID:38181050	FYPO:0008211	decreased antisense RNA level during heat stress [assayed_protein] PomBase:SPBC146.09c	Intriguingly, about 72% of downregulated genes in lsd1-ΔHMG, lsd2-ΔC, and set1Δ are antisense non-coding RNAs (S1 Table)
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC146.09c	Loss of Ddb1 slightly enhances the Lsd1-FTP level, while having no significant effect on the Lsd2-FTP level (Fig 3E).
PMID:38181050	FYPO:0002082	increased protein ubiquitination during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAC23E2.02	Lsd1 (Fig 4A) or Lsd2 (Fig 4B) was detected in the presence of a temperature-sensitive 26S proteasome subunit mutant, mts2-1, which inactivates the proteasome at 33 ̊C [111] and thereby stabilizes Lsd1 and Lsd2 (Fig 4A and 4B).
PMID:38181050	FYPO:0002082	increased protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPBC146.09c [has_severity] high	Lsd1 (Fig 4A) or Lsd2 (Fig 4B) was detected in the presence of a temperature-sensitive 26S proteasome subunit mutant, mts2-1, which inactivates the proteasome at 33 ̊C [111] and thereby stabilizes Lsd1 and Lsd2 (Fig 4A and 4B).
PMID:38181050	FYPO:0002061	inviable vegetative cell population	Notably, deletion of the Lsd2 HMG-domain results in lethality akin to that in the complete loss of Lsd2, which further implies the unknown and important functions of the C-terminus of these two proteins
PMID:38181050	FYPO:0008210	abolished chromatin binding at promoter region [assayed_region] promoter	Notably, the localizations of Lsd1 and Lsd2 are diminished at the promoter regions in the absence of a functional C-terminus (Fig 1C). This result demonstrates that the C-terminal domains of Lsd1 and Lsd2 are involved in their chromatin binding at these regions.
PMID:38181050	FYPO:0008210	abolished chromatin binding at promoter region [assayed_region] promoter	Notably, the localizations of Lsd1 and Lsd2 are diminished at the promoter regions in the absence of a functional C-terminus (Fig 1C). This result demonstrates that the C-terminal domains of Lsd1 and Lsd2 are involved in their chromatin binding at these regions.
PMID:38181050	GO:1990841	promoter-specific chromatin binding	Previous studies have shown that Lsd1/2 proteins bind to the promoters of a few hundred genes [70,73,74], suggesting that Lsd1/2 proteins are selectively recruited to those genes. Our ChIP-Seq analysis yields a highly similar set of genomic loci where Lsd1 and Lsd2 are enriched just upstream of the transcriptional start site (TSS) (Fig 1C). This result indicates that Lsd1 and Lsd2 mostly bind to the promoter region of genes and are likely to cooperate with other transcription factors that are involved in regulating gene expression.
PMID:38181050	GO:1990841	promoter-specific chromatin binding	Previous studies have shown that Lsd1/2 proteins bind to the promoters of a few hundred genes [70,73,74], suggesting that Lsd1/2 proteins are selectively recruited to those genes. Our ChIP-Seq analysis yields a highly similar set of genomic loci where Lsd1 and Lsd2 are enriched just upstream of the transcriptional start site (TSS) (Fig 1C). This result indicates that Lsd1 and Lsd2 mostly bind to the promoter region of genes and are likely to cooperate with other transcription factors that are involved in regulating gene expression.
PMID:38181050	FYPO:0003153	normal protein level during cellular response to heat [assayed_protein] PomBase:SPBC146.09c	Protein levels of Lsd1 and Lsd2 are similar between wild-type and clr4Δ cells at 37 ̊C, indicating that Clr4 is not responsible for Lsd1/2 upregulation in this condition (Fig 4C and 4D)
PMID:38181050	FYPO:0003152	increased protein level during cellular response to heat [assayed_protein] PomBase:SPCC306.04c	Protein levels of Lsd1 and Lsd2 are similar between wild-type and clr4Δ cells at 37 ̊C, indicating that Clr4 is not responsible for Lsd1/2 upregulation in this condition (Fig 4C and 4D)
PMID:38181050	FYPO:0003153	normal protein level during cellular response to heat [assayed_protein] PomBase:SPAC23E2.02	Protein levels of Lsd1 and Lsd2 are similar between wild-type and clr4Δ cells at 37 ̊C, indicating that Clr4 is not responsible for Lsd1/2 upregulation in this condition (Fig 4C and 4D)
PMID:38181050	FYPO:0003152	increased protein level during cellular response to heat [assayed_protein] PomBase:SPCC306.04c	Set1 significantly at 37 ̊C compared to that at 30 ̊C, which is due to the temperature sensitive nature of cul4-1.
PMID:38181050	GO:0003713	transcription coactivator activity	The Lsd2-BD and Phf1-BD strains could self-activate the reporter genes without Gal4 activating domain, suggesting that Lsd2 and Phf1 alone could recruit basal transcriptional factors to initiate reporter gene transcription (S4 Fig).
PMID:38181050	GO:0003713	transcription coactivator activity	The Lsd2-BD and Phf1-BD strains could self-activate the reporter genes without Gal4 activating domain, suggesting that Lsd2 and Phf1 alone could recruit basal transcriptional factors to initiate reporter gene transcription (S4 Fig).
PMID:38181050	FYPO:0002061	inviable vegetative cell population [has_severity] high	The triple mutants lsd1- ΔHMG set1Δ clr4Δ and lsd2-ΔC set1Δ clr4Δ are lethal (S1D Fig).
PMID:38181050	FYPO:0002061	inviable vegetative cell population [has_severity] high	The triple mutants lsd1- ΔHMG set1Δ clr4Δ and lsd2-ΔC set1Δ clr4Δ are lethal (S1D Fig).
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC146.09c	The western blot results suggest that the loss of any member of CLRC complex enhances the protein amount of Lsd1 (Fig 3C) or Lsd2 (Fig 3D).
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC146.09c	The western blot results suggest that the loss of any member of CLRC complex enhances the protein amount of Lsd1 (Fig 3C) or Lsd2 (Fig 3D).
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c	The western blot results suggest that the loss of any member of CLRC complex enhances the protein amount of Lsd1 (Fig 3C) or Lsd2 (Fig 3D).
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC23E2.02	The western blot results suggest that the loss of any member of CLRC complex enhances the protein amount of Lsd1 (Fig 3C) or Lsd2 (Fig 3D).
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC23E2.02	The western blot results suggest that the loss of any member of CLRC complex enhances the protein amount of Lsd1 (Fig 3C) or Lsd2 (Fig 3D).
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC146.09c	The western blot results suggest that the loss of any member of CLRC complex enhances the protein amount of Lsd1 (Fig 3C) or Lsd2 (Fig 3D).
PMID:38181050	FYPO:0005893	increased protein level in chromatin [assayed_protein] PomBase:SPBC146.09c [has_severity] low	To our surprise, clr4Δ increases the enrichments of Lsd1/2 while set1Δ decreases the enrichments of Lsd1 at its enriched genomic loci (Figs 2G, 2H, S6 and S7).
PMID:38181050	FYPO:0006631	decreased protein localization to chromatin [assayed_protein] PomBase:SPBC146.09c [has_severity] low	To our surprise, clr4Δ increases the enrichments of Lsd1/2 while set1Δ decreases the enrichments of Lsd1 at its enriched genomic loci (Figs 2G, 2H, S6 and S7).
PMID:38181050	FYPO:0005893	increased protein level in chromatin [assayed_protein] PomBase:SPAC23E2.02 [has_severity] low	To our surprise, clr4Δ increases the enrichments of Lsd1/2 while set1Δ decreases the enrichments of Lsd1 at its enriched genomic loci (Figs 2G, 2H, S6 and S7).
PMID:38181050	FYPO:0002774	increased level of ubiquitinated protein in cell during vegetative growth [assayed_protein] PomBase:SPBC146.09c	Under heat stress (37 ̊C), it was consistently found that ubiquitination of Lsd1 and Lsd2 is drastically enhanced in set1Δ cells, even without mts2-1 as a background (Fig 4F)
PMID:38181050	FYPO:0002774	increased level of ubiquitinated protein in cell during vegetative growth [assayed_protein] PomBase:SPAC23E2.02	Under heat stress (37 ̊C), it was consistently found that ubiquitination of Lsd1 and Lsd2 is drastically enhanced in set1Δ cells, even without mts2-1 as a background (Fig 4F)
PMID:38181050	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC146.09c [assayed_protein] PomBase:SPCC4G3.07c	We also observed that the loss of the C-terminus of Lsd2 does not disrupt the interactions between Lsd2 and Phf1 (Fig 1F) or Phf2 (Fig 1G).
PMID:38181050	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC30D11.08c [assayed_protein] PomBase:SPBC146.09c	We also observed that the loss of the C-terminus of Lsd2 does not disrupt the interactions between Lsd2 and Phf1 (Fig 1F) or Phf2 (Fig 1G).
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c	We found that the loss of any members in CLRC promotes the protein levels of Set1, both at 30 ̊C or 37 ̊C (Fig 5A), indicating that the intact CLRC restricts the amount of Set1.
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c	We found that the loss of any members in CLRC promotes the protein levels of Set1, both at 30 ̊C or 37 ̊C (Fig 5A), indicating that the intact CLRC restricts the amount of Set1.
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC306.04c	We found that the loss of any members in CLRC promotes the protein levels of Set1, both at 30 ̊C or 37 ̊C (Fig 5A), indicating that the intact CLRC restricts the amount of Set1.
PMID:38181050	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC146.09c	loss of most members of the COMPASS complex, including Set1, Spp1, Swd1, Swd3, Swd2, and Ash2 leads to a significantly decreased amount of Lsd1 protein (Fig 3A)
PMID:38181050	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC146.09c	loss of most members of the COMPASS complex, including Set1, Spp1, Swd1, Swd3, Swd2, and Ash2 leads to a significantly decreased amount of Lsd1 protein (Fig 3A)
PMID:38181050	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC146.09c	loss of most members of the COMPASS complex, including Set1, Spp1, Swd1, Swd3, Swd2, and Ash2 leads to a significantly decreased amount of Lsd1 protein (Fig 3A)
PMID:38181050	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC146.09c	loss of most members of the COMPASS complex, including Set1, Spp1, Swd1, Swd3, Swd2, and Ash2 leads to a significantly decreased amount of Lsd1 protein (Fig 3A)
PMID:38181050	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC146.09c	loss of most members of the COMPASS complex, including Set1, Spp1, Swd1, Swd3, Swd2, and Ash2 leads to a significantly decreased amount of Lsd1 protein (Fig 3A)
PMID:38181050	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	lsd1-ΔHMG clr4Δ cells are viable but sick, which implies a negative genetic interaction between Lsd1 and Clr4 (Figs 2A and S1B).
PMID:38181050	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	lsd1-ΔHMG clr4Δ cells are viable but sick, which implies a negative genetic interaction between Lsd1 and Clr4 (Figs 2A and S1B).
PMID:38181050	FYPO:0002061	inviable vegetative cell population	lsd1-ΔHMG set1Δ and lsd2-ΔC clr4Δ double mutants resulted in inviable daughter cells, suggesting that Lsd1 has essential overlapping functions with Set1, while Lsd2 has critical overlapping roles with Clr4 (Fig 2A).
PMID:38181050	FYPO:0002061	inviable vegetative cell population	lsd1-ΔHMG set1Δ and lsd2-ΔC clr4Δ double mutants resulted in inviable daughter cells, suggesting that Lsd1 has essential overlapping functions with Set1, while Lsd2 has critical overlapping roles with Clr4 (Fig 2A).
PMID:38181050	FYPO:0002061	inviable vegetative cell population	lsd1-ΔHMG set1Δ and lsd2-ΔC clr4Δ double mutants resulted in inviable daughter cells, suggesting that Lsd1 has essential overlapping functions with Set1, while Lsd2 has critical overlapping roles with Clr4 (Fig 2A).
PMID:38181050	FYPO:0002061	inviable vegetative cell population	lsd1-ΔHMG set1Δ and lsd2-ΔC clr4Δ double mutants resulted in inviable daughter cells, suggesting that Lsd1 has essential overlapping functions with Set1, while Lsd2 has critical overlapping roles with Clr4 (Fig 2A).
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC146.09c	that without Clr4, both Lsd1-FTP and Lsd2-FTP show an increase in protein levels, compared to the wild-type cells (Fig 2I).
PMID:38181050	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC23E2.02	that without Clr4, both Lsd1-FTP and Lsd2-FTP show an increase in protein levels, compared to the wild-type cells (Fig 2I).
PMID:38188419	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1A)
PMID:38188419	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1A)
PMID:38188419	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1D)
PMID:38188419	FYPO:0008295	sensitive to guanazole [has_severity] high	(Fig. 1D)
PMID:38188419	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC18B5.11c	(Fig. 1F)
PMID:38188419	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1G)
PMID:38188419	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1G)
PMID:38188419	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1G)
PMID:38188419	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1G)
PMID:38188419	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1G)
PMID:38269097	MOD:00696	phosphorylated residue [increased_during] cellular response to heat [added_by] PomBase:SPBC216.07c	(Fig. 2C)
PMID:38269097	MOD:00696	phosphorylated residue [increased_during] cellular response to heat [added_by] PomBase:SPBC216.07c	(Fig. 2C)
PMID:38269097	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC8E11.02c [assayed_protein] PomBase:SPAC1420.01c	(Fig. 4C)
PMID:38269097	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c [has_severity] high	(Fig. 6A)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 6A)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 6A)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 6A)
PMID:38269097	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c [has_severity] medium	(Fig. 6A)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 6A)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Fig. 6B)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Fig. 6B)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Fig. 6B)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Fig. 6B)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Fig. 6B)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Fig. 6D)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Fig. 6D)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. S7)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. S7)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. S7)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. S7)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. S7)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. S7)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. S7)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. S7)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. S7)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. S7)
PMID:38269097	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC1420.01c [assayed_protein] PomBase:SPAC8E11.02c	(Fig. S7)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 1)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 1)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 1)
PMID:38269097	FYPO:0002672	normal growth on rapamycin	(Figure 1)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 1)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] low	(Figure 1)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] medium	(Figure 1)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 1)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 1)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 2 and 3)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 2 and 3)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 2 and 3)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 2 and 3)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 2)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 2)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 2)
PMID:38269097	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Figure 2)
PMID:38269097	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Figure 2)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 2)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 2)
PMID:38269097	PomGeneEx:0000018	protein level increased [during] cellular response to heat	(Figure 2)
PMID:38269097	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Figure 2)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 2)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 2)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 2)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 2)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 2)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 2)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 2)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 2)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 2)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 2)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 2)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 2)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 3)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 3)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 3)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] medium	(Figure 3)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 3)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] medium	(Figure 3)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] low	(Figure 3)
PMID:38269097	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 3)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 3)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] medium	(Figure 3)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 3)
PMID:38269097	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Figure 3)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 3)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 3)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 3)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 3)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 3)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 3)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 3)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 3)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 4)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 4)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 4)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 4)
PMID:38269097	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Figure 4)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 4)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 4)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 4)
PMID:38269097	FYPO:0000674	normal cell population growth at high temperature	(Figure 4)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 4)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 4)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 4)
PMID:38269097	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Figure 4)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 4)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] medium	(Figure 4)
PMID:38269097	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Figure 4)
PMID:38269097	PomGeneEx:0000018	protein level increased [in_presence_of] sirolimus	(Figure 5)
PMID:38269097	MOD:00696	phosphorylated residue [added_by] PomBase:SPBC216.07c [added_during] cellular response to heat	(Figure 5)
PMID:38269097	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPAC1420.01c	(Figure 5)
PMID:38269097	PomGeneEx:0000013	RNA level unchanged [during] cellular response to heat	(Figure 5)
PMID:38269097	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPAC24H6.05	(Figure 5)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] low	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] medium	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] medium	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] low	(Figure 6)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] medium	(Figure 6)
PMID:38269097	PomGeneEx:0000018	protein level increased [during] cellular response to heat	(Figure S2)
PMID:38269097	FYPO:0003153	normal protein level during cellular response to heat [assayed_protein] PomBase:SPBC3E7.02c	(Figure S3)
PMID:38269097	FYPO:0003153	normal protein level during cellular response to heat [assayed_protein] PomBase:SPBC3E7.02c	(Figure S3)
PMID:38269097	FYPO:0002141	normal cell population growth at low temperature	(Figure S3)
PMID:38269097	FYPO:0002141	normal cell population growth at low temperature	(Figure S3)
PMID:38269097	FYPO:0002141	normal cell population growth at low temperature	(Figure S3)
PMID:38269097	FYPO:0002141	normal cell population growth at low temperature	(Figure S3)
PMID:38269097	MOD:00696	phosphorylated residue	(Figure S3)
PMID:38269097	FYPO:0002141	normal cell population growth at low temperature	(Figure S3)
PMID:38269097	FYPO:0002141	normal cell population growth at low temperature	(Figure S3)
PMID:38269097	FYPO:0002141	normal cell population growth at low temperature	(Figure S3)
PMID:38269097	FYPO:0002141	normal cell population growth at low temperature	(Figure S3)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure S4)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure S4)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure S4)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure S4)
PMID:38269097	FYPO:0005258	increased cell population growth at high temperature [has_severity] high	(Figure S4)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure S4)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure S4)
PMID:38269097	FYPO:0001357	normal vegetative cell population growth	(Figure S4)
PMID:38269097	FYPO:0003153	normal protein level during cellular response to heat [assayed_protein] PomBase:SPAC1420.01c	(Figure S6)
PMID:38269097	FYPO:0003153	normal protein level during cellular response to heat [assayed_protein] PomBase:SPAC1420.01c	(Figure S6)
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC63.14 [has_severity] medium	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1105.05 [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1F8.03c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1703.13c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC56F2.09c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC839.16 [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC4F6.09 [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC3D6.02 [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC26F1.07 [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB1E7.04c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC162.07 [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1281.06c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC20G4.06c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC17A5.03 [has_severity] low	Table S2
PMID:38269097	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1142.04 [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB1E7.12 [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC18.01c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC18.14c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1840.02c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1A6.04c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.10 [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09 [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC19A8.04 [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1259.01c [has_severity] low	Table S2
PMID:38269097	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1919.02 [has_severity] medium	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB15E9.01c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC513.01c [has_severity] low	Table S2
PMID:38269097	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC21H7.04 [has_severity] low	Table S2
PMID:38269097	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC17D4.04 [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC19G12.10c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB18E9.05c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1739.13 [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1071.10c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC794.12c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC22G7.06c [has_severity] low	Table S2
PMID:38269097	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC23H4.09 [has_severity] low	Table S2
PMID:38269097	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC6G9.02c [has_severity] low	Table S2
PMID:38269097	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC57A7.06 [has_severity] low	Table S2
PMID:38269097	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC22F8.09 [has_severity] low	Table S2
PMID:38269097	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC4F6.14 [has_severity] low	Table S2
PMID:38269097	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1734.01c [has_severity] low	Table S2
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1F7.08 [has_severity] medium	Table S2
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000012	RNA level decreased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000011	RNA level increased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000011	RNA level increased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000011	RNA level increased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000011	RNA level increased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000011	RNA level increased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000011	RNA level increased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000011	RNA level increased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000011	RNA level increased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000011	RNA level increased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000011	RNA level increased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000011	RNA level increased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000011	RNA level increased [in_presence_of] sirolimus	Table S3
PMID:38269097	PomGeneEx:0000011	RNA level increased [in_presence_of] sirolimus	Table S3
PMID:38269097	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC21C3.08c [has_severity] low	Table S4
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC965.04c [has_severity] high	Table S4
PMID:38269097	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC30D11.12 [has_severity] low	Table S4
PMID:38269097	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC17G9.05 [has_severity] high	Table S4
PMID:38269097	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	We serendipitously discovered that fission yeast cells exhibit significant proliferation even at 38°C and 39°C, but not at 40°C, on agar medium supplemented with rapamycin, a TORC1-specific inhibitor [...] the fkh1 null mutant failed to grow at 39°C even in the presence of rapamycin. Figure 1
PMID:38272226	PomGeneEx:0000018	protein level increased [during] single-celled organism vegetative growth phase [in_presence_of] bortezomib	(Fig. 1B)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 1C)
PMID:38272226	MOD:01148	ubiquitinylated lysine [added_by] PomBase:SPAC12B10.01c	(Fig. 1D)
PMID:38272226	MOD:01148	ubiquitinylated lysine [added_by] PomBase:SPAC12B10.01c	(Fig. 1D)
PMID:38272226	FYPO:0007952	normal protein level during stationary phase [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 2B)
PMID:38272226	FYPO:0007952	normal protein level during stationary phase [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 2B)
PMID:38272226	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 2B)
PMID:38272226	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 2C)
PMID:38272226	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 2C)
PMID:38272226	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPBC16E9.01c [has_severity] high	(Fig. 2D)
PMID:38272226	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPBC16E9.01c [has_severity] medium	(Fig. 2D)
PMID:38272226	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPBC16E9.01c [has_severity] medium	(Fig. 2D)
PMID:38272226	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 3A and 3E)
PMID:38272226	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC12B10.01c [assayed_protein] PomBase:SPBC16E9.01c [has_severity] low	(Fig. 3C)
PMID:38272226	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC12B10.01c [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 3C)
PMID:38272226	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC12B10.01c [assayed_protein] PomBase:SPBC16E9.01c [has_severity] low	(Fig. 3C)
PMID:38272226	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC12B10.01c [assayed_protein] PomBase:SPBC16E9.01c [has_severity] low	(Fig. 3C)
PMID:38272226	FYPO:0002768	decreased protein ubiquitination during vegetative growth [assayed_protein] PomBase:SPBC16E9.01c [has_severity] high	(Fig. 3D)
PMID:38272226	PomGeneEx:0000018	protein level increased [during] single-celled organism vegetative growth phase	(Fig. 3F)
PMID:38272226	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] low	(Fig. 4A and Fig. S6B)
PMID:38272226	FYPO:0005825	sensitive to iron [has_severity] low	(Fig. 4A and Fig. S6B)
PMID:38272226	FYPO:0001814	normal cell population growth during iron starvation	(Fig. 4A)
PMID:38272226	FYPO:0005825	sensitive to iron [has_severity] medium	(Fig. 4A)
PMID:38272226	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] medium	(Fig. 4A)
PMID:38272226	FYPO:0001409	normal growth on glycerol carbon source	(Fig. 4A)
PMID:38272226	FYPO:0001814	normal cell population growth during iron starvation	(Fig. 4A)
PMID:38272226	FYPO:0001814	normal cell population growth during iron starvation	(Fig. 4A)
PMID:38272226	FYPO:0007121	normal growth on iron	(Fig. 4A)
PMID:38272226	FYPO:0002015	sensitive to iron ion starvation [has_severity] medium	(Fig. 4A)
PMID:38272226	FYPO:0005825	sensitive to iron [has_severity] low	(Fig. 4A)
PMID:38272226	FYPO:0002015	sensitive to iron ion starvation [has_severity] medium	(Fig. 4A)
PMID:38272226	FYPO:0001409	normal growth on glycerol carbon source	(Fig. 4A)
PMID:38272226	FYPO:0001409	normal growth on glycerol carbon source	(Fig. 4A)
PMID:38272226	FYPO:0007121	normal growth on iron	(Fig. 4A)
PMID:38272226	FYPO:0007121	normal growth on iron	(Fig. 4A)
PMID:38272226	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] low	(Fig. 4A)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPCC338.10c	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1683.10c [has_severity] medium	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP23A10.16 [has_severity] low	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP23A10.16 [has_severity] medium	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP23A10.16 [has_severity] medium	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPCC737.02c	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPCC737.02c	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPCC737.02c	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC338.10c [has_severity] medium	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC338.10c [has_severity] medium	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPCC1235.02	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPCC1235.02	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPCC1235.02	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1683.10c [has_severity] medium	(Fig. 4B)
PMID:38272226	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1683.10c [has_severity] medium	(Fig. 4B)
PMID:38272226	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1235.02 [has_severity] medium	(Fig. 4B)
PMID:38272226	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC338.10c [has_severity] medium	(Fig. 4B)
PMID:38272226	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC737.02c [has_severity] medium	(Fig. 4B)
PMID:38272226	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP23A10.16 [has_severity] medium	(Fig. 4B)
PMID:38272226	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1683.10c [has_severity] medium	(Fig. 4B)
PMID:38272226	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1235.02 [has_severity] low	(Fig. 4B)
PMID:38272226	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC338.10c [has_severity] low	(Fig. 4B)
PMID:38272226	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC737.02c [has_severity] low	(Fig. 4B)
PMID:38272226	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP23A10.16 [has_severity] low	(Fig. 4B)
PMID:38272226	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1683.10c [has_severity] low	(Fig. 4B)
PMID:38272226	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC737.02c [has_severity] low	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPCC1235.02	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [has_severity] low [assayed_protein] PomBase:SPCC737.02c	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPCC338.10c	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPCC338.10c	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [has_severity] low [assayed_protein] PomBase:SPCC737.02c	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPCC1235.02	(Fig. 4C)
PMID:38272226	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC1235.02 [has_severity] high	(Fig. 4C)
PMID:38272226	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC338.10c [has_severity] medium	(Fig. 4C)
PMID:38272226	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC737.02c [has_severity] medium	(Fig. 4C)
PMID:38272226	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBP23A10.16 [has_severity] high	(Fig. 4C)
PMID:38272226	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC1683.10c [has_severity] medium	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPCC1235.02	(Fig. 4C)
PMID:38272226	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC338.10c [has_severity] low	(Fig. 4C)
PMID:38272226	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC1235.02 [has_severity] medium	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPCC338.10c	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC1683.10c [has_severity] medium	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBP23A10.16 [has_severity] low	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBP23A10.16 [has_severity] low	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC1683.10c [has_severity] medium	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC1683.10c [has_severity] medium	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [has_severity] low [assayed_protein] PomBase:SPCC737.02c	(Fig. 4C)
PMID:38272226	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBP23A10.16 [has_severity] medium	(Fig. 4C)
PMID:38272226	FYPO:0001324	decreased protein level during vegetative growth [has_severity] low [assayed_protein] PomBase:SPBC1683.10c	(Fig. 4C)
PMID:38272226	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBP23A10.16 [has_severity] low	(Fig. 4C)
PMID:38272226	FYPO:0000519	decreased oxidative phosphorylation [has_severity] low	(Fig. 5B and 5C)
PMID:38272226	FYPO:0000519	decreased oxidative phosphorylation [has_severity] low	(Fig. 5B and 5C)
PMID:38272226	FYPO:0000519	decreased oxidative phosphorylation [has_severity] medium	(Fig. 5B and 5C)
PMID:38272226	PomGeneEx:0000018	protein level increased [in_presence_of] 2,2'-bipyridine [during] single-celled organism vegetative growth phase	(Fig. 7A)
PMID:38272226	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 7B)
PMID:38272226	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPBC16E9.01c	(Fig. 7C)
PMID:38272226	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPBC16E9.01c	(Fig. S5B)
PMID:38272226	PomGeneEx:0000019	protein level decreased [during] single-celled organism vegetative growth phase	Php4 degraded in stationary phase (Fig. 1A)
PMID:38272226	GO:0032473	cytoplasmic side of mitochondrial outer membrane	These results suggest that Hul6 loosely associates with the outer mitochondrial membrane. (Fig. 6)
PMID:38272226	GO:0005741	mitochondrial outer membrane	These results suggest that Hul6 loosely associates with the outer mitochondrial membrane. (Fig. 6)
PMID:38272226	FYPO:0000245	loss of viability in stationary phase	Δhul6 cells show a progressive loss of viability, starting at 72 h (Fig. S6B).
PMID:38285941	FYPO:0003246	normal mitotic S phase progression	(Fig. 2D and E and SI Appendix, Figs. S2A-D and S3). Mcm2 mapping was performed 60 min after release from the cdc25-22 block. A similar septation index for WT and swi6Δ cells indicated normal progression of swi6Δ cells through S phase (SI Appendix, Fig. S2B).
PMID:38285941	FYPO:0007158	decreased histone H3 binding [has_severity] high	(Fig. 4E and F).
PMID:38285941	FYPO:0007159	decreased histone H4 binding	(Fig. 4E and F).
PMID:38285941	FYPO:0008187	abolished histone H4 binding	(Fig. 4E and F).
PMID:38285941	FYPO:0003247	abolished histone H3 binding	(Fig. 4E and F).
PMID:38285941	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1) (comment: Genetic screen for mutants defective in heterochromatin propagation.)
PMID:38285941	FYPO:0003044	abnormal heterochromatin assembly [has_severity] medium	, mcm2-1 and mcl1-4 cells failed to maintain heterochromatin, as indicated by white colony color and loss of the H3K9me3 mark (SI Appendix, Fig. S7). Thus, both Mcl1 and Mcm2 are required for propagation of heterochromatin at an ectopic site.
PMID:38285941	FYPO:0003044	abnormal heterochromatin assembly [has_severity] medium	, mcm2-1 and mcl1-4 cells failed to maintain heterochromatin, as indicated by white colony color and loss of the H3K9me3 mark (SI Appendix, Fig. S7). Thus, both Mcl1 and Mcm2 are required for propagation of heterochromatin at an ectopic site.
PMID:38285941	FYPO:0000217	abnormal DNA replication	Compared to WT, swi6Δ cells showed a considerable decrease in BrdU incorporation across mat, which persisted through the time course (Fig. 2D and SI Appendix, Fig. S3). Mcm2 was still detected, although with more defined peaks, likely reflecting licensed, but not activated, replication ori­ gins across the domain (Fig. 2D)
PMID:38285941	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC609.05 [assayed_protein] PomBase:SPAC227.16c	FACT associates with subunits of MCM (Mcm2) and GINS (Psf3) when Mcl1 is present, but these interactions are lost in cells lacking Mcl1 (Fig. 6A)
PMID:38285941	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC609.05 [assayed_protein] PomBase:SPBC4.04c	FACT associates with subunits of MCM (Mcm2) and GINS (Psf3) when Mcl1 is present, but these interactions are lost in cells lacking Mcl1 (Fig. 6A)
PMID:38285941	GO:0000792	heterochromatin [exists_during] mitotic S phase	Mcl1 localized to heterochromatic loci in S phase, like Mcm2 (Fig. 2B).
PMID:38285941	GO:0000792	heterochromatin [exists_during] mitotic S phase	Mcl1 localized to heterochromatic loci in S phase, like Mcm2 (Fig. 2B).
PMID:38285941	GO:0000510	H3-H4 histone complex chaperone activity [part_of] DNA replication-dependent chromatin assembly	Notably, the addition of the WT Mcm2 HBD during the purification of the H3 and H4 histones promoted their solubili­ zation, highlighting its role as a histone chaperone (SI Appendix, Fig. S5D).
PMID:38285941	FYPO:0000088	sensitive to hydroxyurea	The mcm2-6 mutant showed sensitivity to hydroxyurea (HU) (SI Appendix, Fig. S5C), indicating defective replication, and was not further analyzed.
PMID:38285941	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	The other two mutants showed defective silencing of the mat2P::ura4+ reporter and haploid meiosis (Fig. 4C), as well as detectable levels of the mat2P transcript (Fig. 4D).
PMID:38285941	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	The other two mutants showed defective silencing of the mat2P::ura4+ reporter and haploid meiosis (Fig. 4C), as well as detectable levels of the mat2P transcript (Fig. 4D).
PMID:38285941	FYPO:0007160	abnormal DNA replication-dependent nucleosome assembly [has_severity] medium	Thus, although both mutants affect the retention of parental histones, Mcl1 plays a more critical role in the process.
PMID:38289024	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 3 S2A,B)
PMID:38289024	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Figure 3 S2A,B) More strikingly, Patf1-atf1(10D/E) also visibly compromised epigenetic silencing even at 30°C (Figure 3—Figure supplement 2A, B).
PMID:38289024	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 3D) (comment: CHECK endogenous atf1+ was deleted)
PMID:38289024	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	(Figure 5B) Notably, cells expressing two copies, but not one copy, of wis1-DD showed severe gene silencing defects (Figure 5B and Figure 5—Figure supplement 1B), and consistently the mRNA levels of the kΔ::ade6+ increased dramatically in these cells (Figure 5C and Figure 5—Figure supplement 1C).
PMID:38289024	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 6B) (comment: CHECK endogenous atf1 was deleted)
PMID:38289024	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 6B) (comment: CHECK endogenous atf1+ was deleted)
PMID:38289024	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 6B) (comment: CHECK endogenous atf1+ was deleted)
PMID:38289024	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 6B) (comment: CHECK endogenous atf1+ was deleted)
PMID:38289024	FYPO:0004376	increased chromatin silencing at silent mating-type cassette	(Figure 6B) (comment: CHECK endogenous atf1+ was deleted)
PMID:38289024	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Figure 6B; Figure 3-S1) (comment: CHECK endogenous atf1+ was deleted)
PMID:38289024	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Figure 8A)
PMID:38289024	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC664.01c [assayed_protein] PomBase:SPBC29B5.01	Binding affinity between Atf1 and Swi6HP1 is maintained for non-phosphorylatable Atf1(10A/I) at 37°C, but disrupted for phosphomimetic Atf1(10D/E) even at 30°C.
PMID:38289024	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC664.01c [assayed_protein] PomBase:SPBC29B5.01	Binding affinity between Atf1 and Swi6HP1 is maintained for non-phosphorylatable Atf1(10A/I) at 37°C, but disrupted for phosphomimetic Atf1(10D/E) even at 30°C.
PMID:38289024	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c	Consistently, ChIP- qPCR analyses showed that the abundance of both H3K9me3 and Swi6HP1 bound at the mat locus but not at pericentromere decreased dramatically in cells with two copies of wis1-DD (Figure 5F and Figure 5—Figure supplement 1F).
PMID:38289024	FYPO:0003571	decreased histone H3-K9 methylation at silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPAC664.01c	Consistently, ChIP- qPCR analyses showed that the abundance of both H3K9me3 and Swi6HP1 bound at the mat locus but not at pericentromere decreased dramatically in cells with two copies of wis1-DD (Figure 5F and Figure 5—Figure supplement 1F).
PMID:38289024	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC664.01c [assayed_protein] PomBase:SPBC29B5.01	Furthermore, in vitro pull-down assays demonstrated that the interaction between Atf1 and Swi6HP1 was also largely disrupted in wis1-DD mutants (Figure 5E and Figure 5—Figure supplement 1E).
PMID:38289024	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC29B5.01 [assayed_protein] PomBase:SPAC664.01c	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC29B5.01 [assayed_protein] PomBase:SPAC664.01c	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC29B5.01 [assayed_protein] PomBase:SPAC664.01c	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC29B5.01 [assayed_protein] PomBase:SPAC664.01c	Intriguingly, removal of Sty1 kinase activity by introducing either sty1 deletion mutant (sty1Δ) or ATP analogue-sensitive mutant of sty1 (sty1-T97A, i.e. sty1-as2) (Zuin et al., 2010) into wis1-DD mutant background could relieve the negative effect of constitutive activation of MAPK Sty1 on kΔ::ade6+ reporter gene silencing, binding affinity between Atf1 and Swi6HP1 and heterochromatin stability at the mat locus (Figure 5 and Figure 5—Figure supplement 2).
PMID:38289024	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette	cells at 37°C restored gene silencing rapidly at normal temperature 30°C after being re-plated on medium containing limited adenine (Figure 2A and B). However, when this re-plating assay was applied to dcr1Δ, one of the RNAi mutants, a considerable proportion of cells still emerged as variegated colonies (designated as dcr1ΔV), which was in sharp contrast to wild type cells (Figure 2B).
PMID:38289024	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	demonstrating that tethering Swi6HP1 to the mat locus was sufficient to rescue heat stress-induced defective epigenetic maintenance of heterochromatin.
PMID:38289024	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	indicating full rescue of silencing defects at the mat locus under heat stress.
PMID:38295128	FYPO:0008342	decreased pre-tRNA or mature level during vegetative growth [has_severity] medium [assayed_transcript] prolyl_tRNA	(Fig 1B and 1C)
PMID:38295128	FYPO:0008342	decreased pre-tRNA or mature level during vegetative growth [has_severity] medium [assayed_transcript] prolyl_tRNA	(Fig 1B and 1C)
PMID:38295128	FYPO:0008342	decreased pre-tRNA or mature level during vegetative growth [has_severity] medium [assayed_transcript] prolyl_tRNA	(Fig 1B and 1C).
PMID:38295128	FYPO:0008342	decreased pre-tRNA or mature level during vegetative growth [has_severity] medium [assayed_transcript] prolyl_tRNA	(Fig 1B and 1C). Similarly, tRNAPro(AGG) levels were not efficiently restored in trm8Δ rpl502Δ mutants (38%) relative to 25% in trm8Δ mutants and 49% in trm8Δ gcn2Δ strains.
PMID:38295128	FYPO:0008342	decreased pre-tRNA or mature level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPATRNALEU.03	(Fig 6A and 6B) Relative tRNALeu(AAG) levels are reduced substantially in tan1Δ strains after growth at 39 ̊C (to 24% of WT)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38295128	FYPO:0001097	sensitive to amitrole [has_severity] low	(Fig. 1A)
PMID:38295128	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	(Fig. 1A)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38295128	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1A)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38295128	FYPO:0009030	resistance to amitrole [has_severity] low	(Fig. 1A)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I) [23
PMID:38295128	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	(Figs 1A and S1) However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C (Figs 1A)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	(Figs 1A and S1) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0009030	resistance to amitrole [has_severity] high	(Figs 1A and S1) and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C
PMID:38295128	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Figure 4 B) S. pombe tan1Δ mutants are temperature sensitive due to decay of two tRNA species by the RTD pathway.
PMID:38295128	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Figure 4 B) S. pombe tan1Δ mutants are temperature sensitive due to decay of two tRNA species by the RTD pathway.
PMID:38295128	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Figure 4 B) S. pombe tan1Δ mutants are temperature sensitive due to decay of two tRNA species by the RTD pathway.
PMID:38295128	FYPO:0008345	abolished tRNA cytidine N4-acetylation [has_severity] medium [assayed_transcript] seryl_tRNA	(Figure 4 C) As anticipated based on the conservation of Tan1 sequence and the Tan1 requirement for ac4C12 modification of tRNALeu and tRNASer within a CCG motif [35-38], purified tRNALeu(CAA) from S. pombe tan1Δ mutants lacks any detectable ac4C, compared to that in WT cells, but has similar levels of four control modifications (Fig 4A).
PMID:38295128	FYPO:0008342	decreased pre-tRNA or mature level during vegetative growth [has_severity] medium [assayed_transcript] seryl_tRNA	(Figure 4 C) Consistent with the biology of Tan1 in S. cerevisiae, we find that S. pombe tan1Δ mutants are temperature sensitive due to decay of two tRNA species by the RTD pathway.
PMID:38295128	FYPO:0008342	decreased pre-tRNA or mature level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPATRNALEU.03	(Figure 4 C) Consistent with the biology of Tan1 in S. cerevisiae, we find that S. pombe tan1Δ mutants are temperature sensitive due to decay of two tRNA species by the RTD pathway.
PMID:38295128	GO:0180014	protein-tRNA adaptor activity [has_input] PomBase:SPAC20G8.09c [has_input] PomBase:SPATRNALEU.03	"(comment: phenotypes support conservation of role in S. cerevisiae which is binding tRNA and) ""The interaction of NAT10 and THUMPD1 suggests that they work together in tRNA acetylation and that THUMPD1 acts as a specific tRNA adaptor. In agreement with this view, we found Kre33 and Tan1 to interact in a 2-hybrid assay in budding yeast cells (Figure 5J)."
PMID:38295128	FYPO:0001986	resistance to 5-fluorouracil [has_severity] low	(comment: vw: grows slightly better than WT) However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C, and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Figs 1A and S1)
PMID:38295128	FYPO:0001986	resistance to 5-fluorouracil [has_severity] low	(comment: vw: grows slightly better than WT) However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C, and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Figs 1A and S1)
PMID:38295128	FYPO:0001986	resistance to 5-fluorouracil [has_severity] low	(comment: vw: grows slightly better than WT) However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C, and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Figs 1A and S1)
PMID:38295128	FYPO:0001986	resistance to 5-fluorouracil [has_severity] low	(comment: vw: grows slightly better than WT) However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C, and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Figs 1A and S1)
PMID:38295128	FYPO:0001097	sensitive to amitrole [has_severity] medium	(fig 3) By contrast, we found that 3-AT resistance was not correlated with the efficiency of suppression in trm8Δ rplΔ strain, as one of the robust trm8Δ suppressors was almost completely 3-AT sensitive (trm8Δ rpl1202Δ) and two other robust suppressors were only moderately 3-AT resistant (trm8Δ rps2801Δ and trm8Δ rps802Δ), whereas the robust trm8Δ rplΔ2802Δ and trm8Δ rpl1701Δ suppressor strains were strongly 3-AT resistant. This result is consistent with our finding above that 3-AT resistance is a property of the mutation in the ribosomal protein gene, and not the trm8Δ mutation, However, it is not immediately clear why some mutations in ribosomal protein genes result in 3-AT resistance and others result in sensitivity
PMID:38295128	FYPO:0001097	sensitive to amitrole [has_severity] high	(fig 3) By contrast, we found that 3-AT resistance was not correlated with the efficiency of suppression in trm8Δ rplΔ strain, as one of the robust trm8Δ suppressors was almost completely 3-AT sensitive (trm8Δ rpl1202Δ) and two other robust suppressors were only moderately 3-AT resistant (trm8Δ rps2801Δ and trm8Δ rps802Δ), whereas the robust trm8Δ rplΔ2802Δ and trm8Δ rpl1701Δ suppressor strains were strongly 3-AT resistant. This result is consistent with our finding above that 3-AT resistance is a property of the mutation in the ribosomal protein gene, and not the trm8Δ mutation, However, it is not immediately clear why some mutations in ribosomal protein genes result in 3-AT resistance and others result in sensitivity
PMID:38295128	FYPO:0001097	sensitive to amitrole [has_severity] high	(fig 3) By contrast, we found that 3-AT resistance was not correlated with the efficiency of suppression in trm8Δ rplΔ strain, as one of the robust trm8Δ suppressors was almost completely 3-AT sensitive (trm8Δ rpl1202Δ) and two other robust suppressors were only moderately 3-AT resistant (trm8Δ rps2801Δ and trm8Δ rps802Δ), whereas the robust trm8Δ rplΔ2802Δ and trm8Δ rpl1701Δ suppressor strains were strongly 3-AT resistant. This result is consistent with our finding above that 3-AT resistance is a property of the mutation in the ribosomal protein gene, and not the trm8Δ mutation, However, it is not immediately clear why some mutations in ribosomal protein genes result in 3-AT resistance and others result in sensitivity
PMID:38295128	FYPO:0001097	sensitive to amitrole [has_severity] medium	(fig 3) By contrast, we found that 3-AT resistance was not correlated with the efficiency of suppression in trm8Δ rplΔ strain, as one of the robust trm8Δ suppressors was almost completely 3-AT sensitive (trm8Δ rpl1202Δ) and two other robust suppressors were only moderately 3-AT resistant (trm8Δ rps2801Δ and trm8Δ rps802Δ), whereas the robust trm8Δ rplΔ2802Δ and trm8Δ rpl1701Δ suppressor strains were strongly 3-AT resistant. This result is consistent with our finding above that 3-AT resistance is a property of the mutation in the ribosomal protein gene, and not the trm8Δ mutation, However, it is not immediately clear why some mutations in ribosomal protein genes result in 3-AT resistance and others result in sensitivity
PMID:38295128	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(vw: growth seems slightly reduced compared to WT) Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(vw: growth seems slightly reduced compared to WT) Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0008342	decreased pre-tRNA or mature level during vegetative growth [assayed_transcript] tyrosyl_tRNA [has_severity] medium	As expected, in trm8Δ mutants at 38.5 ̊C, relative tRNATyr(GUA) levels were reduced, to 30% of WT levels (Fig 1B and 1C).
PMID:38295128	FYPO:0008342	decreased pre-tRNA or mature level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPATRNALEU.03	As we saw for the trm8Δ rpl502Δ strain, we find that the tan1Δ rpl502Δ strain does not have restored tRNA levels after growth at 39 ̊C (Fig 6A and 6B).... Relative tRNALeu(AAG) levels are reduced substantially in tan1Δ strains after growth at 39 ̊C (to 24% of WT)
PMID:38295128	FYPO:0008361	normal integrated stress response signaling [assayed_using] PomBase:SPBC1105.02c	By contrast, trm8Δ rpl1701-Q72X and trm8Δ rpl502-Y44X mutants had near baseline relative lys4+ expression at both temperatures (0.97 and 0.88 vs 0.88 for WT, at 38.5 ̊C) (Fig 1D).
PMID:38295128	FYPO:0008361	normal integrated stress response signaling [assayed_using] PomBase:SPBC1105.02c	By contrast, trm8Δ rpl1701-Q72X and trm8Δ rpl502-Y44X mutants had near baseline relative lys4+ expression at both temperatures (0.97 and 0.88 vs 0.88 for WT, at 38.5 ̊C) (Fig 1D).
PMID:38295128	FYPO:0008361	normal integrated stress response signaling [assayed_using] PomBase:SPBC1105.02c	By contrast, trm8Δ rpl1701-Q72X and trm8Δ rpl502-Y44X mutants had near baseline relative lys4+ expression at both temperatures (0.97 and 0.88 vs 0.88 for WT, at 38.5 ̊C) (Fig 1D).
PMID:38295128	FYPO:0008361	normal integrated stress response signaling [assayed_using] PomBase:SPBC1105.02c	By contrast, trm8Δ rpl1701-Q72X and trm8Δ rpl502-Y44X mutants had near baseline relative lys4+ expression at both temperatures (0.97 and 0.88 vs 0.88 for WT, at 38.5 ̊C) (Fig 1D).
PMID:38295128	FYPO:0001234	slow vegetative cell population growth	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	FYPO:0001234	slow vegetative cell population growth	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	FYPO:0001234	slow vegetative cell population growth	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	FYPO:0001234	slow vegetative cell population growth	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	FYPO:0001234	slow vegetative cell population growth	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	FYPO:0001234	slow vegetative cell population growth	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	FYPO:0001234	slow vegetative cell population growth	Consistent with a defect in translation due to loss of ribosomal protein paralogs, we find that each of four rplΔ mutants and three rpsΔ mutants has a substantially reduced growth rate (increased generation time) relative to that of the WT strain in YES media at 30 ̊C (Fig 7A and 7B and S1 Table).
PMID:38295128	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	Deletion of each of the two rps genes (rps2801Δ and rps802Δ, encoding Rps28 and Rps8) and four rpl genes examined (rpl1601Δ, rpl1202Δ, rpl2802Δ, and rpl1701Δ, encoding Rpl16, Rpl12, Rpl28, and Rpl17) resulted in efficient suppression of the trm8Δ temperature sensitivity in EMMC-His media, although suppression was somewhat weaker for the rpl1601Δ mutation (Fig 3A and 3B)
PMID:38295128	FYPO:0008361	normal integrated stress response signaling [assayed_using] PomBase:SPBC1105.02c	Furthermore, like trm8Δ rpl502-Y44X mutants, trm8Δ rpl502Δ mutants efficiently suppressed the GAAC activation observed in trm8Δ mutants, measured by relative lys4+ levels (from a 14.5-fold increase in trm8Δ mutants, to a 1.9-fold increase in trm8Δ rpl502Δ mutants), compared to a near baseline 1.2-fold increase in a trm8Δ gcn2Δ strain (Figs 2D and S5).
PMID:38295128	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C (Fig 1A)
PMID:38295128	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C (Fig 1A)
PMID:38295128	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	However, unlike the dhp1 suppressors, these suppressors grew poorly on media containing 5-FU at 33 ̊C (Fig 1A)
PMID:38295128	FYPO:0008343	increased integrated stress response signaling [assayed_using] PomBase:SPBC1105.02c [has_severity] low	However, we find that although an S. pombe tan1Δ mutant activates the GAAC pathway, based on analysis of relative lys4+ mRNA levels, the activation is weak, and is only modestly reduced in a tan1Δ rpl502Δ strain (Fig 6C).
PMID:38295128	FYPO:0006037	decreased cytosolic half-mer polysome level	Moreover, both rplΔ mutant profiles, but not the WT, exhibit substantial populations of halfmers, monosomes and polysomes with an additional 40S subunit
PMID:38295128	FYPO:0006037	decreased cytosolic half-mer polysome level	Moreover, both rplΔ mutant profiles, but not the WT, exhibit substantial populations of halfmers, monosomes and polysomes with an additional 40S subunit
PMID:38295128	GO:0002181	cytoplasmic translation	Polysome profiling of three of these mutants provides additional evidence for a defect in translation in the mutants (Fig 7C).
PMID:38295128	FYPO:0007317	decreased cytoplasmic translation	Polysome profiling of three of these mutants provides additional evidence for a defect in translation in the mutants (Fig 7C).
PMID:38295128	GO:0002181	cytoplasmic translation	Polysome profiling of three of these mutants provides additional evidence for a defect in translation in the mutants (Fig 7C).
PMID:38295128	FYPO:0007317	decreased cytoplasmic translation	Polysome profiling of three of these mutants provides additional evidence for a defect in translation in the mutants (Fig 7C).
PMID:38295128	FYPO:0008342	decreased pre-tRNA or mature level during vegetative growth [has_severity] medium [assayed_transcript] tyrosyl_tRNA	Similar analysis shows that the trm8Δ rpl502-Y44X suppressor had slightly increased levels of tRNATyr(GUA) (36% vs 30%) and of tRNAPro(AGG) (13% vs 9%) relative to WT (Fig 1B and 1C)
PMID:38295128	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	Similarly, all five of the trm8Δ rplΔ and trm8Δ rpsΔ mutants that were robust trm8Δ suppressors were also sensitive on YES +5-FU media at 33 ̊C, whereas the weak trm8Δ rpl1601Δ suppressor was slightly sensitive on YES+5-FU.
PMID:38295128	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	Similarly, all five of the trm8Δ rplΔ and trm8Δ rpsΔ mutants that were robust trm8Δ suppressors were also sensitive on YES +5-FU media at 33 ̊C, whereas the weak trm8Δ rpl1601Δ suppressor was slightly sensitive on YES+5-FU.
PMID:38295128	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] medium	Similarly, all five of the trm8Δ rplΔ and trm8Δ rpsΔ mutants that were robust trm8Δ suppressors were also sensitive on YES +5-FU media at 33 ̊C, whereas the weak trm8Δ rpl1601Δ suppressor was slightly sensitive on YES+5-FU.
PMID:38295128	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	Similarly, all five of the trm8Δ rplΔ and trm8Δ rpsΔ mutants that were robust trm8Δ suppressors were also sensitive on YES +5-FU media at 33 ̊C, whereas the weak trm8Δ rpl1601Δ suppressor was slightly sensitive on YES+5-FU.
PMID:38295128	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	Similarly, all five of the trm8Δ rplΔ and trm8Δ rpsΔ mutants that were robust trm8Δ suppressors were also sensitive on YES +5-FU media at 33 ̊C, whereas the weak trm8Δ rpl1601Δ suppressor was slightly sensitive on YES+5-FU.
PMID:38295128	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	Similarly, all five of the trm8Δ rplΔ and trm8Δ rpsΔ mutants that were robust trm8Δ suppressors were also sensitive on YES +5-FU media at 33 ̊C, whereas the weak trm8Δ rpl1601Δ suppressor was slightly sensitive on YES+5-FU.
PMID:38295128	FYPO:0008342	decreased pre-tRNA or mature level during vegetative growth [has_severity] medium [assayed_transcript] tyrosyl_tRNA	Surprisingly, we found that in the trm8Δ rpl1701-Q72X suppressor the tRNATyr(GUA) levels were not restored, but were if anything slightly reduced, relative to the trm8Δ mutant (23% vs 30%).....Thus, for the trm8Δ rpl1701-Q72X suppressor, suppression is occurring without a detectable increase in levels of tRNATyr(GUA) or of tRNAPro(AGG).
PMID:38295128	FYPO:0007317	decreased cytoplasmic translation	The rps23Δ mutant also has reduced polysome density, indicative of reduced translation, accompanied by an undetectable 40S peak and a greatly pronounced 60S peak that substantially overshadows the 80 monosome peak
PMID:38295128	GO:0002181	cytoplasmic translation	The rps23Δ mutant also has reduced polysome density, indicative of reduced translation, accompanied by an undetectable 40S peak and a greatly pronounced 60S peak that substantially overshadows the 80 monosome peak
PMID:38295128	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	These weak effects of the tan1Δ mutant and the tan1Δ rpl502Δ mutant on GAAC activation are consistent with the observation that an rpl502Δ mutation is a more efficient suppressor of the temperature sensitivity of an S. pombe tan1Δ mutant than is a gcn2Δ mutation, on either YES media or EMMC-His media at 38 ̊C (Fig 6D).
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	These weak effects of the tan1Δ mutant and the tan1Δ rpl502Δ mutant on GAAC activation are consistent with the observation that an rpl502Δ mutation is a more efficient suppressor of the temperature sensitivity of an S. pombe tan1Δ mutant than is a gcn2Δ mutation, on either YES media or EMMC-His media at 38 ̊C (Fig 6D).
PMID:38295128	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	These weak effects of the tan1Δ mutant and the tan1Δ rpl502Δ mutant on GAAC activation are consistent with the observation that an rpl502Δ mutation is a more efficient suppressor of the temperature sensitivity of an S. pombe tan1Δ mutant than is a gcn2Δ mutation, on either YES media or EMMC-His media at 38 ̊C (Fig 6D).
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	These weak effects of the tan1Δ mutant and the tan1Δ rpl502Δ mutant on GAAC activation are consistent with the observation that an rpl502Δ mutation is a more efficient suppressor of the temperature sensitivity of an S. pombe tan1Δ mutant than is a gcn2Δ mutation, on either YES media or EMMC-His media at 38 ̊C (Fig 6D).
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	We found that a reconstructed trm8Δ rpl502Δ strain suppressed the growth defect of a trm8Δ mutant almost identically to the trm8Δ rpl502-Y44X mutant, with similar growth in YES and EMMC media at high temperature, and similar 5-FU sensitivity and 3-AT resistance (Fig 2A)
PMID:38295128	FYPO:0004325	sensitive to 5-fluorouracil [has_severity] high	We found that a reconstructed trm8Δ rpl502Δ strain suppressed the growth defect of a trm8Δ mutant almost identically to the trm8Δ rpl502-Y44X mutant, with similar growth in YES and EMMC media at high temperature, and similar 5-FU sensitivity and 3-AT resistance (Fig 2A)
PMID:38295128	FYPO:0009030	resistance to amitrole [has_severity] high	We found that a reconstructed trm8Δ rpl502Δ strain suppressed the growth defect of a trm8Δ mutant almost identically to the trm8Δ rpl502-Y44X mutant, with similar growth in YES and EMMC media at high temperature, and similar 5-FU sensitivity and 3-AT resistance (Fig 2A)
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	We found that a reconstructed trm8Δ rpl502Δ strain suppressed the growth defect of a trm8Δ mutant almost identically to the trm8Δ rpl502-Y44X mutant, with similar growth in YES and EMMC media at high temperature, and similar 5-FU sensitivity and 3-AT resistance (Fig 2A)(Figs 1A) In this way, we identified a group of four trm8Δ suppressors that suppressed trm8Δ temperature sensitivity in rich (YES) and complete minimal media lacking histidine (EMMC-His) almost as efficiently as a trm8Δ suppressor with a representative dhp1 mutation (trm8Δ dhp1-W326L) or GAAC mutation (trm8Δ gcn2-M1I)
PMID:38295128	FYPO:0008342	decreased pre-tRNA or mature level during vegetative growth [has_severity] medium	and a follow-up analysis shows that the trm8Δ rpl1102-K93X suppressor also did not restore the reduced levels of tRNATyr(GUA) and tRNAPro(AGG), whereas levels of a known unaffected Trm8 substrate (tRNAVal(AAC)) remained constant (S3 Fig).
PMID:38295128	FYPO:0009030	resistance to amitrole [has_severity] high	and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Fig 1A)
PMID:38295128	FYPO:0009030	resistance to amitrole [has_severity] high	and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Fig 1A)
PMID:38295128	FYPO:0009030	resistance to amitrole [has_severity] high	and unlike the GAAC or dhp1 suppressors, these suppressors were resistant to 3-AT at 37 ̊C (Fig 1A)
PMID:38295128	GO:0180014	protein-tRNA adaptor activity [has_input] PomBase:SPAC20G8.09c [has_input] seryl_tRNA	"phenotypes support conservation of role in S. cerevisiae which is binding tRNA and ""The interaction of NAT10 and THUMPD1 suggests that they work together in tRNA acetylation and that THUMPD1 acts as a specific tRNA adaptor. In agreement with this view, we found Kre33 and Tan1 to interact in a 2-hybrid assay in budding yeast cells (Figure 5J)."
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	rpl2802Δ mutation efficiently suppresses the growth phenotypes of an S. pombe tan1Δ mutant, resulting in temperature resistance on EMMC-His media and YES media at 38 ̊C, 3-AT resistance at 35 ̊C ..... (Fig 5A).
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	rpl2802Δ mutation efficiently suppresses the growth phenotypes of an S. pombe tan1Δ mutant, resulting in temperature resistance on EMMC-His media and YES media at 38 ̊C, 3-AT resistance at 35 ̊C ..... (Fig 5A).
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	rpl2802Δ mutation efficiently suppresses the growth phenotypes of an S. pombe tan1Δ mutant, resulting in temperature resistance on EMMC-His media and YES media at 38 ̊C, 3-AT resistance at 35 ̊C ..... (Fig 5A).
PMID:38295128	FYPO:0000674	normal cell population growth at high temperature	rpl2802Δ mutation efficiently suppresses the growth phenotypes of an S. pombe tan1Δ mutant, resulting in temperature resistance on EMMC-His media and YES media at 38 ̊C, 3-AT resistance at 35 ̊C ..... (Fig 5A).
PMID:38295128	FYPO:0009030	resistance to amitrole [has_severity] high	rpl2802Δ mutation efficiently suppresses the growth phenotypes of an S. pombe tan1Δ mutant, resulting in temperature resistance on EMMC-His media and YES media at 38 ̊C, 3-AT resistance at 35 ̊C .....Fig 5A).
PMID:38295128	FYPO:0008342	decreased pre-tRNA or mature level during vegetative growth [assayed_transcript] tyrosyl_tRNA [has_severity] low	whereas levels of tRNATyr(GUA) were modestly restored in trm8Δ gcn2Δ mutants (58% vs 41%), as we observed previously [23] (Fig 2B and 2C).
PMID:38359013	FYPO:0002061	inviable vegetative cell population	(comment: erratum corrected previous annotation)
PMID:38360270	FYPO:0003004	increased cellular reactive oxygen species level during vegetative growth	((Fig. 1) As shown in Figure 1, D and E, mitochondrial ROS was higher in erd2Δ cells than in WT cells.)
PMID:38360270	FYPO:0007193	small fragmented mitochondria [has_penetrance] 60	(Fig. 1) Intriguingly, we observed that the absence of erd2 caused mitochondrial fragmentation (Fig. 1, A and B)
PMID:38360270	FYPO:0004166	increased oxygen consumption during vegetative growth	(Fig. 1C) Moreover, the oxygen consumption rate of erd2Δ cells was higher than that of WT cells (Figs. 1C and S1A), suggesting that mitochondrial respiration was increased in erd2Δ cells.
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC29A10.08	(Fig. 2A)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC29A10.08	(Fig. 2A)
PMID:38360270	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPBC29A10.08	(Fig. 2A)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC830.08c	(Fig. 2A)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC830.08c	(Fig. 2A)
PMID:38360270	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPCC830.08c	(Fig. 2A)
PMID:38360270	FYPO:0001457	sensitive to tunicamycin [has_severity] high	(Fig. 2B)
PMID:38360270	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:38360270	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 2B)
PMID:38360270	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 2B) Under unstressed conditions, that is, when cells were grown on EMM plates, ire1Δ and erd2Δ had no noticeable effect on cell growth, but ire1Δerd2Δ impaired cell growth (Fig. 2B).
PMID:38360270	FYPO:0003118	normal cellular reactive oxygen species level during vegetative growth	(Fig. 3)
PMID:38360270	FYPO:0003118	normal cellular reactive oxygen species level during vegetative growth	(Fig. 3)
PMID:38360270	FYPO:0003896	normal mitochondrial morphology	(Fig. 3) mitochondria were fragmented in erd2Δ cells but not in WT, ire1Δ, or erd2Δire1Δ cells
PMID:38360270	FYPO:0003896	normal mitochondrial morphology	(Fig. 3) mitochondria were fragmented in erd2Δ cells but not in WT, ire1Δ, or erd2Δire1Δ cells
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC16H5.06	(Fig. 4)
PMID:38360270	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.14 [has_severity] variable severity	(Fig. 4)
PMID:38360270	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC222.12c [has_severity] low	(Fig. 4)
PMID:38360270	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1739.09c [has_severity] medium	(Fig. 4)
PMID:38360270	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC16H5.06 [has_severity] variable severity	(Fig. 4)
PMID:38360270	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC725.11c [has_severity] low	(Fig. 4)
PMID:38360270	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC23C11.08 [has_severity] low	(Fig. 4)
PMID:38360270	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC16E9.01c [has_severity] high	(Fig. 4)
PMID:38360270	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC3B8.02 [has_severity] medium	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.14	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.14	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC222.12c	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC222.12c	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1739.09c	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1739.09c	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC16H5.06	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1739.09c	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC222.12c	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.14	(Fig. 4)
PMID:38360270	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC16H5.06 [has_severity] medium	(Fig. 4)
PMID:38360270	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1739.09c [has_severity] medium	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC16E9.01c	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC23C11.08	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC23C11.08	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC725.11c	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC725.11c	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC16H5.06	(Fig. 4)
PMID:38360270	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC222.12c [has_severity] medium	(Fig. 4)
PMID:38360270	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC14C4.14 [has_severity] medium	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC3B8.02	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC3B8.02	(Fig. 4)
PMID:38360270	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC16E9.01c	(Fig. 4)
PMID:38360270	FYPO:0000440	sensitive to antimycin A [has_severity] medium	(Fig. 5)
PMID:38360270	FYPO:0008194	sensitive to trolox [has_severity] high	(Fig. 5)
PMID:38360270	FYPO:0001457	sensitive to tunicamycin	(Fig. 5) Cells defective in UPR are sensitive to tunicamycin (32). Consistently, ire1Δ cells failed to grow on EMM plates containing tunicamycin (Fig. 2B)
PMID:38360270	FYPO:0004166	increased oxygen consumption during vegetative growth [has_penetrance] low	(comment: CHECK DID WE NEED TO CHANGE THIS TO LOW) Fig. 3 The results showed that the oxygen consumption rate of erd2Δ cells, but not ire1Δ or erd2Δire1Δ cells, was increased.
PMID:38360270	FYPO:0004166	increased oxygen consumption during vegetative growth [has_penetrance] low	(comment: CHECK DID WE NEED TO CHANGE THIS TO LOW) Fig. 3 The results showed that the oxygen consumption rate of erd2Δ cells, but not ire1Δ or erd2Δire1Δ cells, was increased.
PMID:38360270	FYPO:0001457	sensitive to tunicamycin	Paradoxically, erd2Δ cells, in which UPR was activated (Fig. 2A), also grew poorly on EMM plates containing tunicamycin.
PMID:38376141	FYPO:0007159	decreased histone H4 binding	(Fig. 2 supplement 1A)
PMID:38376141	FYPO:0007158	decreased histone H3 binding	(Fig. 2 supplement 1A)
PMID:38376141	FYPO:0001571	increased protein-protein interaction [assayed_protein] PomBase:SPBC16D10.09 [assayed_protein] PomBase:SPBC29A10.03c [has_severity] high	(Fig. 6)
PMID:38376141	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC16D10.09 [assayed_protein] PomBase:SPBC29A10.03c	(Fig. 6)
PMID:38376141	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC16D10.09 [assayed_protein] PomBase:SPBC29A10.03c	(Fig. 6A)
PMID:38376141	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC16D10.09 [assayed_protein] PomBase:SPBC29A10.03c	(Fig. 6A)
PMID:38376141	FYPO:0004910	normal punctate nuclear protein localization [assayed_protein] PomBase:SPAC26H5.03	(Fig. 6C and D)
PMID:38376141	FYPO:0002624	decreased punctate nuclear protein localization [has_severity] high [assayed_protein] PomBase:SPAC26H5.03	(Fig. 6C and D)
PMID:38376141	FYPO:0005116	increased punctate nuclear protein localization [has_severity] medium [assayed_protein] PomBase:SPAC26H5.03	(Fig. 6C and D)
PMID:38376141	FYPO:0002624	decreased punctate nuclear protein localization [has_severity] high [assayed_protein] PomBase:SPAC26H5.03	(Fig. 6C and D)
PMID:38376141	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. 7A)
PMID:38376141	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. 7A)
PMID:38376141	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 7A)
PMID:38376141	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. 7A)
PMID:38376141	FYPO:0007328	normal number of Rad52 foci during vegetative growth	(Fig. 7B and C)
PMID:38376141	FYPO:0004709	increased number of Rad52 foci [has_severity] low	(Fig. 7B and C)
PMID:38376141	FYPO:0004709	increased number of Rad52 foci [has_severity] medium	(Fig. 7B and C)
PMID:38376141	FYPO:0004709	increased number of Rad52 foci [has_severity] medium	(Fig. 7B and C)
PMID:38376141	FYPO:0004709	increased number of Rad52 foci [has_severity] low	(Fig. 7B and C)
PMID:38376141	FYPO:0002150	inviable spore population	(Fig. 7D)
PMID:38376141	FYPO:0002150	inviable spore population	(Fig. 7D)
PMID:38376141	FYPO:0002150	inviable spore population	(Fig. 7D)
PMID:38376141	FYPO:0002150	inviable spore population	(Fig. 7D)
PMID:38376141	FYPO:0000278	decreased cell population growth following spore germination	(Fig. 7D)
PMID:38376141	FYPO:0000278	decreased cell population growth following spore germination	(Fig. 7D)
PMID:38376141	FYPO:0002150	inviable spore population	(Fig. 7D)
PMID:38376141	FYPO:0002150	inviable spore population	(Fig. 7D)
PMID:38376141	FYPO:0008273	normal histone H4 binding [assayed_protein] PomBase:SPBC29A10.03c	In addition, the NMR signals of all IDR for this mutant with or without histones were close to that of the WT (Figure 3—Figure supplement 3A-B) indicating that the KER* mutation did not impair histone binding.
PMID:38376141	FYPO:0008272	normal histone H3 binding [assayed_protein] PomBase:SPBC29A10.03c	In addition, the NMR signals of all IDR for this mutant with or without histones were close to that of the WT (Figure 3—Figure supplement 3A-B) indicating that the KER* mutation did not impair histone binding.
PMID:38376141	FYPO:0007160	abnormal DNA replication-dependent nucleosome assembly [has_severity] high	In contrast, when we complemented the depleted extract with SpCAF-1 mutant complexes SpCAF-1-ED*, SpCAF-1-KER*, SpCAF- 1-ΔWHD we did not detect the supercoiled form I. This indicates that these mutants cannot promote nucleosome assembly (Figure 5).
PMID:38376141	FYPO:0007160	abnormal DNA replication-dependent nucleosome assembly [has_severity] high	In contrast, when we complemented the depleted extract with SpCAF-1 mutant complexes SpCAF-1-ED*, SpCAF-1-KER*, SpCAF- 1-ΔWHD we did not detect the supercoiled form I. This indicates that these mutants cannot promote nucleosome assembly (Figure 5).
PMID:38376141	FYPO:0007160	abnormal DNA replication-dependent nucleosome assembly [has_severity] high	In contrast, when we complemented the depleted extract with SpCAF-1 mutant complexes SpCAF-1-ED*, SpCAF-1-KER*, SpCAF- 1-ΔWHD we did not detect the supercoiled form I. This indicates that these mutants cannot promote nucleosome assembly (Figure 5).
PMID:38376141	FYPO:0005018	decreased double-stranded DNA binding [has_severity] medium [assayed_using] CAF-1 complex	The KER* mutation was then introduced in the full complex SpCAF-1-KER* (Figure 1—Figure supplement 1B, Figure 2— Figure supplement 2B) and we confirmed by MST and EMSA its lower affinity for dsDNA (Figure 3B, Figure 3—Figure supplement 2G, Table 1).
PMID:38376141	FYPO:0007542	normal double-stranded DNA binding [assayed_using] CAF-1 complex	We observed the similar DNA binding property and IDR properties for SpCAF-1-ΔWHD and the WT complex (Table 1, Figure 3B, Figure 3—Figure supplement 2G, Figure 3—Figure supplement 3A-B).
PMID:38376141	FYPO:0007160	abnormal DNA replication-dependent nucleosome assembly [has_severity] low	When we used the SpCAF-1-PIP* mutant, we did not detect supercoiling on labeled DNA at 45 min, yet at 2 hr supercoiling ultimately reached levels achieved using the WT SpCAF-1 (Figure 5, bottom, synthesized DNA).
PMID:38399762	FYPO:0000387	decreased biofilm formation	The extent of biofilm formed in SPBPJ4664.02∆ decreased by 40% as compared to WT (p < 0.05), indicating that SPBPJ4664.02 is required for biofilm formation.
PMID:38424265	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38424265	FYPO:0001309	increased viability in stationary phase [has_severity] medium	(Fig. 1A)
PMID:38424265	FYPO:0001309	increased viability in stationary phase [has_severity] high	(Fig. 2C)
PMID:38424265	FYPO:0001357	normal vegetative cell population growth	(Fig. 2C)
PMID:38424265	FYPO:0001043	increased mating efficiency	(Fig. 3A)
PMID:38424265	FYPO:0001043	increased mating efficiency	(Fig. 3A)
PMID:38424265	FYPO:0005947	normal growth on potassium chloride	(Fig. 3B)
PMID:38424265	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Fig. 3B)
PMID:38424265	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] high	(Fig. 3C)
PMID:38424265	FYPO:0000087	sensitive to hydrogen peroxide [has_severity] medium	(Fig. 3C)
PMID:38424265	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1A6.04c	(Fig. 4A)
PMID:38424265	FYPO:0006847	increased total protein level during vegetative growth [assayed_protein] PomBase:SPAC1A6.04c	(Fig. 4B)
PMID:38424265	FYPO:0008237	normal glycerophospholipid level during vegetative growth	(Fig. 5)
PMID:38424265	FYPO:0008237	normal glycerophospholipid level during vegetative growth	(Fig. 5)
PMID:38424265	FYPO:0000245	loss of viability in stationary phase	(Fig. 6A)
PMID:38424265	FYPO:0000245	loss of viability in stationary phase	(Fig. 6A)
PMID:38424265	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC24B11.06c	(Fig. 6B)
PMID:38424265	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC24B11.06c	(Fig. 6B)
PMID:38424265	FYPO:0000841	sensitive to sodium dodecyl sulfate [has_severity] low	(Fig. 7A)
PMID:38424265	FYPO:0000841	sensitive to sodium dodecyl sulfate [has_severity] medium	(Fig. 7A)
PMID:38424265	FYPO:0001190	sensitive to cell wall-degrading enzymes	(Fig. 7B)
PMID:38442865	FYPO:0008234	normal protein localization to cytoplasmic puncta [assayed_protein] PomBase:SPCC417.07c	((Fig. 3A and C))
PMID:38442865	FYPO:0003482	increased punctate cytoplasmic protein localization [has_severity] low [assayed_protein] PomBase:SPCC417.07c	((Fig. 3A and C))
PMID:38442865	FYPO:0002444	loss of punctate cytoplasmic protein localization [has_severity] low [assayed_protein] PomBase:SPCC417.07c	((Fig. 3A and C))
PMID:38442865	FYPO:0003482	increased punctate cytoplasmic protein localization [has_severity] medium [assayed_protein] PomBase:SPBC902.06	((Fig. 3B and C))
PMID:38442865	FYPO:0008234	normal protein localization to cytoplasmic puncta [assayed_protein] PomBase:SPBC902.06	((Fig. 3B and C))
PMID:38442865	FYPO:0002444	loss of punctate cytoplasmic protein localization [has_severity] medium [assayed_protein] PomBase:SPBC902.06	((Fig. 3B and C))
PMID:38442865	FYPO:0008232	microtubule bundles present in increased numbers during mitotic M phase [has_penetrance] 20	(Fig. 1A and B)
PMID:38442865	FYPO:0000177	abnormal mitotic spindle assembly	(Fig. 1C)
PMID:38442865	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1D)
PMID:38442865	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 1D)
PMID:38442865	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1D)
PMID:38442865	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. 1D)
PMID:38442865	FYPO:0000029	abnormal chromosome segregation [has_penetrance] medium	(Fig. 1E)
PMID:38442865	FYPO:0000029	abnormal chromosome segregation [has_penetrance] low	(Fig. 1E)
PMID:38442865	FYPO:0007114	normal microtubule bundle	(Fig. 2A, B and C)
PMID:38442865	FYPO:0002401	microtubule bundles present in increased numbers [has_severity] medium	(Fig. 2A, B and C)
PMID:38442865	FYPO:0007114	normal microtubule bundle	(Fig. 2A, B and C)
PMID:38442865	FYPO:0002818	microtubule bundles present in decreased numbers [has_severity] medium	(Fig. 2D, E and F)
PMID:38442865	FYPO:0002401	microtubule bundles present in increased numbers [has_severity] high	(Fig. 2D, E and F)
PMID:38442865	FYPO:0002401	microtubule bundles present in increased numbers [has_severity] low	(Fig. 2D, E and F)
PMID:38442865	FYPO:0008233	microtubule bundles present in normal numbers	(Fig. 2D, E and F)
PMID:38442865	FYPO:0002818	microtubule bundles present in decreased numbers [has_severity] high	(Fig. 3D, E and F)
PMID:38442865	FYPO:0002818	microtubule bundles present in decreased numbers [has_severity] medium	(Fig. 3D, E and F)
PMID:38442865	FYPO:0008233	microtubule bundles present in normal numbers	(Fig. 3D, E and F)
PMID:38442865	FYPO:0008233	microtubule bundles present in normal numbers	(Fig. 3D, E and F)
PMID:38442865	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC902.06	(Fig. 4B)
PMID:38442865	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. S1)
PMID:38442865	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. S1)
PMID:38442865	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. S1)
PMID:38442865	FYPO:0002401	microtubule bundles present in increased numbers [has_severity] medium	(Fig. S1E and F)
PMID:38442865	FYPO:0002401	microtubule bundles present in increased numbers [has_severity] medium	(Fig. S1E and F)
PMID:38442865	FYPO:0002401	microtubule bundles present in increased numbers [has_severity] high	(Fig. S1E and F)
PMID:38442865	FYPO:0002401	microtubule bundles present in increased numbers [has_severity] low	(Fig. S1E and F)
PMID:38442865	FYPO:0008233	microtubule bundles present in normal numbers	(Fig. S4)
PMID:38442865	FYPO:0008233	microtubule bundles present in normal numbers	(Fig. S4)
PMID:38442865	FYPO:0008233	microtubule bundles present in normal numbers	(Fig. S4)
PMID:38442865	FYPO:0008233	microtubule bundles present in normal numbers	(Fig. S4)
PMID:38442865	FYPO:0008233	microtubule bundles present in normal numbers	(Fig. S4)
PMID:38442865	FYPO:0008233	microtubule bundles present in normal numbers	(Fig. S4)
PMID:38442865	GO:0070507	regulation of microtubule cytoskeleton organization [occurs_in] cytoplasm [happens_during] mitotic interphase	Our studies have shed light on novel functions of the MOR in non-centrosomal MTOCs and cytoplasmic microtubule organization.
PMID:38442865	GO:0070507	regulation of microtubule cytoskeleton organization [occurs_in] cytoplasm [happens_during] mitotic interphase	Our studies have shed light on novel functions of the MOR in non-centrosomal MTOCs and cytoplasmic microtubule organization.
PMID:38442865	GO:0070507	regulation of microtubule cytoskeleton organization [occurs_in] cytoplasm [happens_during] mitotic interphase	Our studies have shed light on novel functions of the MOR in non-centrosomal MTOCs and cytoplasmic microtubule organization.
PMID:38442865	GO:0070507	regulation of microtubule cytoskeleton organization [occurs_in] cytoplasm [happens_during] mitotic interphase	Our studies have shed light on novel functions of the MOR in non-centrosomal MTOCs and cytoplasmic microtubule organization.
PMID:38448160	FYPO:0008193	normal protein localization to pericentric heterochromatin during meiotic prophase I [assayed_protein] PomBase:SPAC110.02	(Fig. 1B)
PMID:38448160	FYPO:0008192	increased protein localization to pericentric heterochromatin during meiotic prophase I [assayed_protein] PomBase:SPBC29A10.14 [has_penetrance] medium	(Fig. 1B)
PMID:38448160	FYPO:0008190	increased protein localization to chromatin at centromere central core during meiotic prophase I [assayed_protein] PomBase:SPBC29A10.14 [has_penetrance] high	(Fig. 1B) In moa1Δ cells, Rec8 cohesin localization increases at the core centromere although sister chromatid cohesion is abolished at this sit
PMID:38448160	FYPO:0003176	normal meiotic chromosome segregation	(Fig. 2B)
PMID:38448160	FYPO:0005633	sister kinetochore dissociation in meiotic metaphase I, normal chromosome segregation in meiosis I, and sister chromatid non-disjunction in meiosis II [has_penetrance] 40	(Fig. 2B)
PMID:38448160	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 11	(Fig. 2B) In moa1Δ cells, a minority population (11%) of cells underwent equational segregation at meiosis I (because of defects in mono-orientation), whereas the majority underwent reductional segregation due to the presence of chiasmata and tension exerted across homologs, as reported previously (Miyazaki et al, 2017) (Fig 2B).
PMID:38448160	FYPO:0008189	equational sister chromatid segregation during achiasmatic meiosis I [has_penetrance] 20	(Fig. 3C)
PMID:38448160	FYPO:0003176	normal meiotic chromosome segregation	(Fig. 3D)
PMID:38448160	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 90	(Fig. 3D)
PMID:38448160	FYPO:0004666	decreased meiotic sister chromatid cohesion along chromosome arms [has_penetrance] medium	(Fig. 3E)
PMID:38448160	FYPO:0004666	decreased meiotic sister chromatid cohesion along chromosome arms [has_penetrance] low	(Fig. 3E)
PMID:38448160	FYPO:0004212	decreased protein localization to kinetochore during meiosis I [has_severity] high [assayed_protein] PomBase:SPBC29A10.14	(Fig. 3F)
PMID:38448160	FYPO:0003176	normal meiotic chromosome segregation	(Fig. 4D)
PMID:38448160	FYPO:0003176	normal meiotic chromosome segregation	(Fig. 4D)
PMID:38448160	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC10F6.09c [part_of] homologous chromosome orientation in meiotic metaphase I	(Figs 3A and S3A-E) We examined if Psm3 is phosphorylated by Plo1 in vitro and found phosphorylation of T182 in the N terminus and S1001 in the C terminus, both locate in the coiled-coil region of the DNA exit gate (Figs 3A and S3A-E), These results suggest that the phosphorylation at Psm3-S110 specifically regulates Rec8 cohesin at centromeres most likely depending on Moa1-Plo1.
PMID:38448160	FYPO:0008189	equational sister chromatid segregation during achiasmatic meiosis I [has_penetrance] 12	(Figure 2D)
PMID:38448160	FYPO:0008189	equational sister chromatid segregation during achiasmatic meiosis I [has_penetrance] 16	(Figure 2D)
PMID:38448160	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 90	(Figure 2D)
PMID:38448160	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 36	(Figure 2D) Remarkably, introducing the rec8-15A mutation into rec12Δ rec8-2A cells increased equational segregation to 36% (Fig 2D), suggesting that phosphorylation at some or all 15S/T sites in Rec8 is contributing at least partly to establishing mono-orientation, most likely by promoting cohesion at the core centromeres.
PMID:38448160	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 70	(Figure 3D)
PMID:38448160	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 80	(Figure 3D)
PMID:38448160	FYPO:0008189	equational sister chromatid segregation during achiasmatic meiosis I [has_penetrance] 50	(Figure 4B)
PMID:38448160	FYPO:0008189	equational sister chromatid segregation during achiasmatic meiosis I [has_penetrance] 50	(Figure 4B)
PMID:38448160	FYPO:0008189	equational sister chromatid segregation during achiasmatic meiosis I [has_penetrance] 50	(Figure 4E)
PMID:38448160	FYPO:0008189	equational sister chromatid segregation during achiasmatic meiosis I [has_penetrance] 15	(Figure 4E)
PMID:38448160	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 70	(Figure 4E)
PMID:38448160	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 40	(Figure 4E)
PMID:38448160	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 20	(Figure 4E)
PMID:38448160	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 20	(Figure 4E)
PMID:38448160	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] 20	(comment: CHECK Unequal sister chromatid segregation in meiosis II after reductional segregation in meiosis I.) Fig. 2B
PMID:38448160	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC29A10.14 [assayed_protein] PomBase:SPAC110.02	(comment: Measured in two-hybrid assay using only the N-terminal 245aa part of Rec8) (Fig. 2F)
PMID:38448160	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] 10	(comment: Unequal sister chromatid segregation in meiosis II after reductional segregation in meiosis I.) Fig. 3D
PMID:38448160	FYPO:0003182	sister chromatid nondisjunction at meiosis II [has_penetrance] 10	(comment: Unequal sister chromatid segregation in meiosis II after reductional segregation in meiosis I.) Fig. 3D
PMID:38448160	GO:0031619	homologous chromosome orientation in meiotic metaphase I	Accordingly, rec8-15A psm3-3A double mutant showed more defects in mono-orientation than either rec8-15A or psm3-3A mutant (Fig 4E), suggesting that the phosphorylation on Rec8 and Psm3 cooperatively act to establish cohesion at the core centromeres.
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	MOD:00696	phosphorylated residue	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	Furthermore, we examined the in vitro phosphorylation by Plo1 using recombinant Mis4 protein and found that the N terminus of Mis4 is preferentially phosphorylated by Plo1 (Fig S2A-C).
PMID:38448160	GO:0031619	homologous chromosome orientation in meiotic metaphase I	In moa1Δ cells, a minority population (11%) of cells underwent equational segregation at meiosis I (because of defects in mono-orientation), whereas the majority underwent reductional segregation due to the presence of chiasmata and tension exerted across homologs, as reported previously (Miyazaki et al, 2017) (Fig 2B)
PMID:38448160	GO:0031619	homologous chromosome orientation in meiotic metaphase I	Indeed, cells expressing Psm3-2A (alanine substitution at T182 and S1001) showed mono-orientation defects (20%) albeit mildly, compared with WT (12%) (Fig 3C), suggesting that phosphorylation of these sites might contribute to establishing cohesion at the core centromeres.
PMID:38448160	GO:0031619	homologous chromosome orientation in meiotic metaphase I	Indeed, cells expressing Psm3-2A (alanine substitution at T182 and S1001) showed mono-orientation defects (20%) albeit mildly, compared with WT (12%) (Fig 3C), suggesting that phosphorylation of these sites might contribute to establishing cohesion at the core centromeres.....We speculate that the Psm3 phosphorylation at the gate may play a role in transiently loosening Rec8-Psm3 gate to facilitate establishment of cohesion at the core centromere.
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We examined if Psm3 is phosphorylated by Plo1 in vitro and found phosphorylation of T182 in the N terminus and S1001 in the C terminus (Fig. S3)
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We examined if Psm3 is phosphorylated by Plo1 in vitro and found phosphorylation of T182 in the N terminus and S1001 in the C terminus (Fig. S3)
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We examined if Psm3 is phosphorylated by Plo1 in vitro and found phosphorylation of T182 in the N terminus and S1001 in the C terminus (Fig. S3)
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C11.16	We identified 11 polo-kinase consensus N/Q/E/D-X-S/T sites and four non-consensus S/T in this domain, which were phosphorylated by Plo1 in vitro and some of them were detected also in vivo (Fig S1A-C).
PMID:38448160	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 40	segregation defects in psm3-3A in achiasmatic meiosis I suppressed by wpl1 deletion. Figure 4E
PMID:38448160	FYPO:0005634	sister kinetochore dissociation in meiotic metaphase I with  equational sister chromatid  segregation in meiosis I [has_penetrance] 40	segregation defects in psm3-3A in achiasmatic meiosis I suppressed by wpl1 deletion. Figure 4E
PMID:38448160	GO:1990813	meiotic centromeric cohesion protection in anaphase I	suggesting that 40% of the reductional population underwent random segregation at meiosis II which is originated from loss of cohesion (a defect in cohesion protection) in anaphase I.
PMID:38448439	GO:0051015	actin filament binding [part_of] actin filament branching	All subunits in the Arp2/3 complex, except for Arp2 and ARPC5, contact the mother filament directly.
PMID:38448439	GO:0051015	actin filament binding [part_of] actin filament branching	All subunits in the Arp2/3 complex, except for Arp2 and ARPC5, contact the mother filament directly.
PMID:38448439	GO:0051015	actin filament binding [part_of] actin filament branching	All subunits in the Arp2/3 complex, except for Arp2 and ARPC5, contact the mother filament directly.
PMID:38448439	GO:0051015	actin filament binding [part_of] actin filament branching	All subunits in the Arp2/3 complex, except for Arp2 and ARPC5, contact the mother filament directly.
PMID:38448439	GO:0051015	actin filament binding [part_of] actin filament branching	All subunits in the Arp2/3 complex, except for Arp2 and ARPC5, contact the mother filament directly.
PMID:38448439	GO:0051015	actin filament binding [part_of] actin filament branching	All subunits in the Arp2/3 complex, except for Arp2 and ARPC5, contact the mother filament directly.
PMID:38448439	GO:0090135	actin filament branching	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38448439	GO:0090135	actin filament branching	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38448439	GO:0090135	actin filament branching	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38448439	GO:0090135	actin filament branching	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38448439	GO:0090135	actin filament branching	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38448439	GO:0090135	actin filament branching	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38448439	GO:0090135	actin filament branching	Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 comple
PMID:38479839	FYPO:0003217	decreased chromatin silencing at centromere central core [has_severity] low	(Fig. 1)
PMID:38479839	FYPO:0003217	decreased chromatin silencing at centromere central core [has_severity] low	(Fig. 1)
PMID:38479839	FYPO:0003217	decreased chromatin silencing at centromere central core [has_severity] high	(Fig. 1)
PMID:38479839	FYPO:0003217	decreased chromatin silencing at centromere central core [has_severity] low	(Fig. 1)
PMID:38479839	FYPO:0008186	normal histone H3-K9 trimethylation at centromere central core during vegetative growth	(Fig. 1E)
PMID:38479839	FYPO:0008185	decreased histone H3-K9 trimethylation at centromere central core during vegetative growth [has_severity] high	(Fig. 1E)
PMID:38479839	FYPO:0008186	normal histone H3-K9 trimethylation at centromere central core during vegetative growth	(Fig. 1E)
PMID:38479839	FYPO:0008186	normal histone H3-K9 trimethylation at centromere central core during vegetative growth	(Fig. 1E)
PMID:38479839	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] low	(Fig. 2)
PMID:38479839	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] low	(Fig. 2)
PMID:38479839	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] high	(Fig. 2)
PMID:38479839	FYPO:0004742	normal chromatin silencing at centromere outer repeat [assayed_transcript] PomBase:SPCC1795.05c	(Fig. 3)
PMID:38479839	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. 3)
PMID:38479839	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 3)
PMID:38479839	FYPO:0000890	decreased histone H3-K9 trimethylation at centromere outer repeat during vegetative growth [has_severity] low	(Fig. 3D)
PMID:38479839	FYPO:0000890	decreased histone H3-K9 trimethylation at centromere outer repeat during vegetative growth [has_severity] low	(Fig. 3D)
PMID:38479839	FYPO:0008199	normal histone H3-K9 trimethylation at centromere outer repeat during vegetative growth	(Fig. 3D)
PMID:38479839	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat [has_severity] high	(Fig. 3E)
PMID:38479839	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat [has_severity] high	(Fig. 3E)
PMID:38479839	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat [has_severity] high	(Fig. 3E)
PMID:38479839	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat [has_severity] high	(Fig. 3E)
PMID:38479839	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [assayed_transcript] dh_repeat [has_severity] medium	(Fig. 3E)
PMID:38479839	FYPO:0000890	decreased histone H3-K9 trimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 3F)
PMID:38479839	FYPO:0000890	decreased histone H3-K9 trimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 3F)
PMID:38479839	FYPO:0000890	decreased histone H3-K9 trimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 3F)
PMID:38479839	FYPO:0000890	decreased histone H3-K9 trimethylation at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 3F)
PMID:38479839	FYPO:0000890	decreased histone H3-K9 trimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 3F)
PMID:38479839	FYPO:0002834	decreased chromatin silencing at centromere [has_penetrance] complete [has_severity] high	(Fig. 5D)
PMID:38479839	FYPO:0008188	abolished histone H3-K9 trimethylation at centromere central core during vegetative growth [has_penetrance] complete	(Fig. 5D)
PMID:38479839	FYPO:0008185	decreased histone H3-K9 trimethylation at centromere central core during vegetative growth [has_severity] high	(Fig. 6A)
PMID:38479839	FYPO:0003217	decreased chromatin silencing at centromere central core [has_severity] high	(Fig. 6A)
PMID:38479839	FYPO:0003217	decreased chromatin silencing at centromere central core [has_severity] high	(Fig. 6A)
PMID:38479839	FYPO:0008185	decreased histone H3-K9 trimethylation at centromere central core during vegetative growth [has_severity] medium	(Fig. 6A)
PMID:38479839	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] medium	(Fig. 6B, C and D)
PMID:38479839	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] high	(Fig. 6B, C and D)
PMID:38479839	FYPO:0003217	decreased chromatin silencing at centromere central core [has_severity] low	(Fig. S2)
PMID:38479839	FYPO:0003217	decreased chromatin silencing at centromere central core [has_severity] low	(Fig. S2)
PMID:38479839	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] low	(Fig. S2)
PMID:38479839	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] low	(Fig. S2)
PMID:38479839	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. S2)
PMID:38479839	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. S2)
PMID:38479839	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] high	(Fig. S5)
PMID:38479839	GO:0006335	DNA replication-dependent chromatin assembly	(comment: Deposits parental histone H3-H4 on both daughter strands during DNA replication)
PMID:38479839	GO:0031491	nucleosome binding [happens_during] S phase [part_of] DNA replication-dependent chromatin assembly	(comment: Deposits parental histone H3-H4 on both daughter strands during DNA replication.)
PMID:38479839	GO:0031491	nucleosome binding [happens_during] S phase [part_of] DNA replication-dependent chromatin assembly	(comment: Transfers parental histone H3-H4 on the lagging strand.)
PMID:38479839	GO:0006335	DNA replication-dependent chromatin assembly	(comment: Transfers parental histone H3-H4 on the lagging strand.)
PMID:38479839	GO:0031491	nucleosome binding [happens_during] S phase [part_of] DNA replication-dependent chromatin assembly	(comment: Work with Dpb3 for parental histone H3-H4 transfer on the leading strand)
PMID:38479839	GO:0031491	nucleosome binding [happens_during] S phase [part_of] DNA replication-dependent chromatin assembly	(comment: Work with Dpb4 for parental histone H3-H4 transfer on the leading strand)
PMID:38479839	GO:0006335	DNA replication-dependent chromatin assembly	(comment: Works with Dpb3 for parental histone H3-H4 transfer on the leading strand)
PMID:38482739	FYPO:0001403	increased cell-substrate adhesion	(Fig. 1A)
PMID:38482739	FYPO:0001403	increased cell-substrate adhesion	(Fig. 1A)
PMID:38482739	FYPO:0000010	abolished cell-substrate adhesion	(Fig. 1B)
PMID:38482739	FYPO:0000010	abolished cell-substrate adhesion	(Fig. 1B)
PMID:38482739	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1742.01	(Fig. 1C)
PMID:38482739	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.04c [has_severity] high	(Fig. 1C)
PMID:38482739	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1742.01	(Fig. 1C)
PMID:38482739	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.04c [has_severity] high	(Fig. 1C)
PMID:38482739	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1223.13	(Fig. 1C)
PMID:38482739	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPCC1223.13 [assayed_region] PomBase:SPBC359.04c [has_severity] high	(Fig. 1D and E)
PMID:38482739	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPCC1223.13 [has_severity] medium [assayed_region] PomBase:SPCC1742.01	(Fig. 1D and E)
PMID:38482739	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPCC1223.13 [assayed_region] PomBase:SPCC1223.13 [has_severity] medium	(Fig. 1D and E)
PMID:38482739	FYPO:0003165	cut [has_penetrance] 10	(Fig. 2A and B)
PMID:38482739	FYPO:0000229	cut [has_penetrance] 8.4	(Fig. 2A and B)
PMID:38482739	FYPO:0002737	abnormal mitotic cell cycle process	(Fig. 2A)
PMID:38482739	FYPO:0001118	abnormal vegetative cell morphology	(Fig. 2A)
PMID:38482739	FYPO:0002552	lipid droplets present in decreased numbers [has_severity] low	(Fig. 3A and B)
PMID:38482739	FYPO:0002552	lipid droplets present in decreased numbers [has_severity] low	(Fig. 3A and B)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC22A12.06c	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBP4H10.11c	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC18H10.02	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1281.06c	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC56E4.04c	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1B3.16c	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC22A12.06c	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBP4H10.11c	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC18H10.02	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1281.06c	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC56E4.04c	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1235.02	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC4A8.11c	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1235.02	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1B3.16c	(Fig. 3C and D)
PMID:38482739	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC4A8.11c	(Fig. 3C and D)
PMID:38482739	FYPO:0007505	decreased protein localization to chromatin at promoter [has_severity] high [assayed_protein] PomBase:SPCC736.08 [assayed_region] PomBase:SPBC18H10.02	(Fig. 3F and G)
PMID:38482739	FYPO:0007505	decreased protein localization to chromatin at promoter [has_severity] high [assayed_protein] PomBase:SPCC736.08 [assayed_region] PomBase:SPCC1281.06c	(Fig. 3F and G)
PMID:38482739	FYPO:0007505	decreased protein localization to chromatin at promoter [has_severity] high [assayed_region] PomBase:SPAC56E4.04c [assayed_protein] PomBase:SPCC736.08	(Fig. 3F and G)
PMID:38482739	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 4)
PMID:38482739	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 4)
PMID:38482739	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 4)
PMID:38482739	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 4B)
PMID:38482739	FYPO:0001690	normal growth on camptothecin	(Fig. 4B)
PMID:38482739	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 4C)
PMID:38482739	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 4C)
PMID:38482739	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 4D)
PMID:38482739	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 4D)
PMID:38482739	FYPO:0002578	resistance to hydroxyurea [has_severity] low	(Fig. 4D)
PMID:38482739	FYPO:0002578	resistance to hydroxyurea [has_severity] medium	(Fig. 4D)
PMID:38482739	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 4D)
PMID:38482739	FYPO:0001355	decreased vegetative cell population growth	(Fig. 4D)
PMID:38482739	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 4D)
PMID:38482739	FYPO:0000006	abnormal mitotic DNA damage checkpoint	(Fig. 4G and H)
PMID:38482739	FYPO:0005995	increased lncRNA level	(Fig. 5)
PMID:38482739	FYPO:0005995	increased lncRNA level	(Fig. 5)
PMID:38482739	FYPO:0000006	abnormal mitotic DNA damage checkpoint	(Fig. 6)
PMID:38482739	FYPO:0000972	increased number of Rad52 foci during vegetative growth	(Fig. 7A and B)
PMID:38482739	FYPO:0006494	decreased rDNA copy number during vegetative growth	(Fig. 7C)
PMID:38482739	FYPO:0006470	decreased mature rRNA level	(Fig. 7D)
PMID:38482739	FYPO:0004032	increased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC1198.11c	(Fig. 7F)
PMID:38482739	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 7G)
PMID:38482739	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. 7G)
PMID:38482739	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 7G)
PMID:38482739	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. 7G)
PMID:38482739	FYPO:0001355	decreased vegetative cell population growth	(Fig. S1)
PMID:38482739	FYPO:0001357	normal vegetative cell population growth	(Fig. S1)
PMID:38482739	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1742.01 [has_severity] medium	(Fig. S2C)
PMID:38482739	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1223.13 [has_severity] low	(Fig. S2C)
PMID:38482739	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1223.13 [has_severity] medium	(Fig. S2C)
PMID:38482739	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1742.01 [has_severity] high	(Fig. S2C)
PMID:38482739	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.04c [has_severity] medium	(Fig. S2C)
PMID:38482739	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.04c [has_severity] high	(Fig. S2C)
PMID:38482739	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB15E9.01c [has_severity] medium	(Fig. S2C)
PMID:38482739	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB15E9.01c [has_severity] medium	(Fig. S2C)
PMID:38482739	FYPO:0007505	decreased protein localization to chromatin at promoter [assayed_protein] PomBase:SPCC736.08 [assayed_region] PomBase:SPCC1450.16c	(Fig. S2E)
PMID:38482739	FYPO:0007505	decreased protein localization to chromatin at promoter [assayed_protein] PomBase:SPCC736.08 [assayed_region] PomBase:SPAC22A12.06c	(Fig. S2E)
PMID:38482739	FYPO:0007505	decreased protein localization to chromatin at promoter [assayed_protein] PomBase:SPCC736.08 [assayed_region] PomBase:SPBP4H10.11c	(Fig. S2E)
PMID:38482739	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S3)
PMID:38482739	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. S3)
PMID:38482739	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [part_of] positive regulation of lipid metabolic process	in the present study we show that the DNA-binding activity of Cbf11 is implicated in all its known functions, with the regulation of lipid metabolism genes remaining the best characterized role of Cbf11.
PMID:38499131	FYPO:0001357	normal vegetative cell population growth	(Figure 2C) control We found that the overexpression of Gpx1 could rescue the viability of Δppr2 cells as Gpx1-HA showed significantly increased viability compared with Δppr2 cells and similar to WT strain on YE plates (Fig. 2C). Additionally, overexpression of Gpx1 could also partially rescue respiratory growth defect in Δppr2 cells as Gpx1-HA could grow on Gly plates better than Δppr2 cells (Fig. 2D).
PMID:38499131	FYPO:0001357	normal vegetative cell population growth	(Figure 2C) control We found that the overexpression of Gpx1 could rescue the viability of Δppr2 cells as Gpx1-HA showed significantly increased viability compared with Δppr2 cells and similar to WT strain on YE plates (Fig. 2C). Additionally, overexpression of Gpx1 could also partially rescue respiratory growth defect in Δppr2 cells as Gpx1-HA could grow on Gly plates better than Δppr2 cells (Fig. 2D).
PMID:38499131	FYPO:0001357	normal vegetative cell population growth	(Figure 2C) control We found that the overexpression of Gpx1 could rescue the viability of Δppr2 cells as Gpx1-HA showed significantly increased viability compared with Δppr2 cells and similar to WT strain on YE plates (Fig. 2C). Additionally, overexpression of Gpx1 could also partially rescue respiratory growth defect in Δppr2 cells as Gpx1-HA could grow on Gly plates better than Δppr2 cells (Fig. 2D).
PMID:38499131	FYPO:0000087	sensitive to hydrogen peroxide	(Figure 4) (comment: vw: not mentioned in text)
PMID:38499131	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPBC32F12.03c	. Interestingly, deletion of ppr2 increased Gpx1 in cytosolic, whereas decreased Gpx1 in the mitochondria (Fig. 2A).
PMID:38499131	FYPO:0006847	increased total protein level during vegetative growth [assayed_protein] PomBase:SPBC32F12.03c	. Interestingly, deletion of ppr2 increased Gpx1 in cytosolic, whereas decreased Gpx1 in the mitochondria (Fig. 2A).
PMID:38499131	FYPO:0001375	abolished protein localization [assayed_protein] PomBase:SPAC1783.07c	3.7. Sty1 and Pap1 accumulate in the nucleus during the stationary phase in Δppr2 cells
PMID:38499131	FYPO:0004456	increased protein localization to nucleus [assayed_protein] PomBase:SPAC24B11.06c	3.7. Sty1 and Pap1 accumulate in the nucleus during the stationary phase in Δppr2 cells
PMID:38499131	FYPO:0008043	increased protein localization to nucleus during stationary phase [assayed_protein] PomBase:SPBC16E9.01c	In Δppr2 cells, Php4-GFP was localized in the nucleus at time points from 6 h to 36 h, in iron-replete conditions. In wild-type strains, Php4-GFP was exported from the nucleus, exhibiting fluorescence in the cytoplasm of cells from 6hto36h(Fig. 2).
PMID:38499131	FYPO:0004164	increased cellular reactive oxygen species level in stationary phase	The levels of ROS in Ppr2-deficient cells were significantly higher compared to WT cells (Fig. 4A). The ppr2 deletion mutant was sensitive to H2O2 during the stationary phase, whereas WT retained tolerance to H2O2 (Fig. 4B).
PMID:38499131	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC320.09 [has_severity] low	The results in our qRT-PCR analysis on the genes of hem15 showed to be slightly down-regulated and the expression of sdh2 was not significantly altered by deletion of ppr2 (Fig. S1).
PMID:38499131	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPCC965.07c	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	FYPO:0003991	increased RNA level in stationary phase [assayed_transcript] PomBase:SPCC965.07c	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	FYPO:0003991	increased RNA level in stationary phase [assayed_transcript] PomBase:SPAC22H10.13	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	FYPO:0003991	increased RNA level in stationary phase [assayed_transcript] PomBase:SPBC1105.14	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPAC1486.01	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPAC22H10.13	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPBC1105.14	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	FYPO:0003914	increased protein level in stationary phase [assayed_protein] PomBase:SPBC32F12.03c	We found that Rsv2, Zym1 and Gst2 were upregulated both at the mRNA and protein levels in Δppr2 cells in exponential phase (6 h after incubation) (Fig. 5). The protein levels of Sod2 was increased in Δppr2 cells but their mRNA levels were unchanged (Fig. 5).
PMID:38499131	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC140.01	We found that Sdh2 and Hem15 were downregulated at the protein levels in Δppr2 cells (Fig. 1B)
PMID:38499131	FYPO:0001117	decreased RNA level during vegetative growth [assayed_protein] PomBase:SPAC140.01	We found that Sdh2 and Hem15 were downregulated at the protein levels in Δppr2 cells (Fig. 1B)
PMID:38499131	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC320.09	We found that Sdh2 and Hem15 were downregulated at the protein levels in Δppr2 cells (Fig. 1B)
PMID:38499131	FYPO:0000251	decreased cell population growth on galactose carbon source [has_severity] high	We observed reduced growth of the ppr2 deletion mutant on glycerol- and galactose-containing media compared to on the glucose-containing media (Fig. 1A).
PMID:38499131	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] high	We observed reduced growth of the ppr2 deletion mutant on glycerol- and galactose-containing media compared to on the glucose-containing media (Fig. 1A).
PMID:38499131	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] low	We observed reduced growth of the ppr2 deletion mutant on glycerol- and galactose-containing media compared to on the glucose-containing media (Fig. 1A).
PMID:38499131	FYPO:0000342	decreased cellular respiration [has_severity] high	respiration deficient: Glycerol is a carbon source that can be metabolized only through oxidative phosphorylation, producing ATP through the electron transport chain in the mitochondria. . Like other respiration-deficient mutants, the reduced growth rate of the ppr2 mutant on this medium indicates that it is not able to effectively carry out this process.
PMID:38499131	FYPO:0000342	decreased cellular respiration [has_severity] high	respiration deficient: Glycerol is a carbon source that can be metabolized only through oxidative phosphorylation, producing ATP through the electron transport chain in the mitochondria. . Like other respiration-deficient mutants, the reduced growth rate of the ppr2 mutant on this medium indicates that it is not able to effectively carry out this process.
PMID:38499152	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC25D12.06	(Fig. 1A)
PMID:38499152	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAP8A3.14c	(Fig. 1A)
PMID:38499152	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.01 [has_severity] high	(comment: CHECK ABOLISHED ********) These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C).
PMID:38499152	FYPO:0002056	decreased mitochondrial translation	(comment: [35S]-methionine/cysteine labeling)
PMID:38499152	FYPO:0002056	decreased mitochondrial translation	(comment: [35S]-methionine/cysteine labeling)
PMID:38499152	FYPO:0002056	decreased mitochondrial translation	(comment: [35S]-methionine/cysteine labeling)
PMID:38499152	FYPO:0003423	decreased mitochondrial RNA level [assayed_transcript] PomBase:SPMIT.01 [has_severity] high	A single Asp261 to Ala or Glu262 to Ala mutation gave rise to a substantially reduced level of cox1 mRNA but little or no reduction of the levels of other mt- mRNAs and mt-rRNAs (Fig. 5A).
PMID:38499152	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC5D6.12 [has_severity] medium	Additionally, the Mtf2 protein level was moderately reduced in Δmrh5 cells (Fig. 1A).
PMID:38499152	FYPO:0000704	abnormal protein-protein interaction [assayed_protein] PomBase:SPBC25D12.06 [assayed_protein] PomBase:SPAC8C9.06c	Co-immunoprecipitation experiments using anti-Myc beads revealed that loss of sls1 abolished the association of Mrh5-Myc with Prp4-CBP and Mtf2-HA (Fig. 2C).
PMID:38499152	FYPO:0000704	abnormal protein-protein interaction [assayed_protein] PomBase:SPBC25D12.06 [assayed_protein] PomBase:SPAC5D6.12	Co-immunoprecipitation experiments using anti-Myc beads revealed that loss of sls1 abolished the association of Mrh5-Myc with Prp4-CBP and Mtf2-HA (Fig. 2C).
PMID:38499152	FYPO:0000704	abnormal protein-protein interaction [assayed_protein] PomBase:SPAP8A3.14c [assayed_protein] PomBase:SPAC8C9.06c	Co-immunoprecipitation experiments with anti-FLAG beads showed that deletion of mtf2 abolished the interaction of Sls1- FLAG with Mrh5-Myc and Ppr4-CBP (Fig. 2A).
PMID:38499152	FYPO:0000704	abnormal protein-protein interaction [assayed_protein] PomBase:SPAP8A3.14c [assayed_protein] PomBase:SPBC25D12.06	Co-immunoprecipitation experiments with anti-FLAG beads showed that deletion of mtf2 abolished the interaction of Sls1- FLAG with Mrh5-Myc and Ppr4-CBP (Fig. 2A).
PMID:38499152	FYPO:0000704	abnormal protein-protein interaction [assayed_protein] PomBase:SPBC25D12.06 [assayed_protein] PomBase:SPAC8C9.06c	Co-immunoprecipitation experiments with anti-FLAG beads showed that deletion of mtf2 abolished the interaction of Sls1- FLAG with Mrh5-Myc and Ppr4-CBP (Fig. 2A).
PMID:38499152	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAP8A3.14c [assayed_protein] PomBase:SPAC5D6.12	Deletion of mrh5 did not impair the interaction among Prp4-CBP, Sls1-FLAG, and Mtf2-HA (Fig. 2D).
PMID:38499152	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAP8A3.14c [assayed_protein] PomBase:SPAC8C9.06c	Deletion of mrh5 did not impair the interaction among Prp4-CBP, Sls1-FLAG, and Mtf2-HA (Fig. 2D).
PMID:38499152	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC8C9.06c	Deletion of mrh5 did not reduce the protein level of Ppr4 (Fig. 1A)
PMID:38499152	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC2F7.15	Deletion of mtf2 or other subunits of Mrh5C dramatically reduced the levels of mtSSU proteins but not the large subunit of the mitoribosome (mtLSU) proteins tested (Figure 3, B and C)
PMID:38499152	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC23A1.18c	Deletion of mtf2 or other subunits of Mrh5C dramatically reduced the levels of mtSSU proteins but not the large subunit of the mitoribosome (mtLSU) proteins tested (Figure 3, B and C)
PMID:38499152	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC1105.03c	Deletion of mtf2 or other subunits of Mrh5C dramatically reduced the levels of mtSSU proteins but not the large subunit of the mitoribosome (mtLSU) proteins tested (Figure 3, B and C)
PMID:38499152	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC4F8.02c	Deletion of mtf2 or other subunits of Mrh5C dramatically reduced the levels of mtSSU proteins but not the large subunit of the mitoribosome (mtLSU) proteins tested (Figure 3, B and C)
PMID:38499152	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC4G9.17c	Deletion of mtf2 or other subunits of Mrh5C dramatically reduced the levels of mtSSU proteins but not the large subunit of the mitoribosome (mtLSU) proteins tested (Figure 3, B and C)
PMID:38499152	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC5D6.12 [has_severity] high	Deletion of sls1 resulted in a drastic reduction in the protein level of Mtf2 (Fig. 1B). A
PMID:38499152	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC25D12.06 [assayed_protein] PomBase:SPAP8A3.14c	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPAC4G9.17c [assayed_transcript] PomBase:SPMIT.05	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPAC4G9.17c [assayed_transcript] PomBase:SPMIT.01	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC25D12.06 [assayed_protein] PomBase:SPAC5D6.12	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC25D12.06 [assayed_protein] PomBase:SPAP8A3.14c	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC25D12.06 [assayed_protein] PomBase:SPAC8C9.06c	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC25D12.06 [assayed_protein] PomBase:SPAC5D6.12	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC25D12.06 [assayed_protein] PomBase:SPAC8C9.06c	Immunoblot analysis of factions revealed that mutation of the DEAD-box of Mrh5 abolished the association of the cox1 mRNA with the mtSSU (Fig. 8).
PMID:38499152	FYPO:0007525	decreased ribosome binding [assayed_protein] PomBase:SPAC8C9.06c	In contrast, Mrh5C subunits no longer co-sedimented with the mtSSU in Δmtf2 cells (Fig. 3D)
PMID:38499152	FYPO:0007525	decreased ribosome binding [assayed_protein] PomBase:SPAP8A3.14c	In contrast, Mrh5C subunits no longer co-sedimented with the mtSSU in Δmtf2 cells (Fig. 3D)
PMID:38499152	FYPO:0007525	decreased ribosome binding [assayed_protein] PomBase:SPBC25D12.06	In contrast, Mrh5C subunits no longer co-sedimented with the mtSSU in Δmtf2 cells (Fig. 3D)
PMID:38499152	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC25D12.06	In contrast, the deletion of ppr4 and mtf2 did not or only moderately affect the protein levels of other Mrh5C subunits (Fig. 1, C and D).
PMID:38499152	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAP8A3.14c	In contrast, the deletion of ppr4 and mtf2 did not or only moderately affect the protein levels of other Mrh5C subunits (Fig. 1, C and D).
PMID:38499152	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC25D12.06	In contrast, the deletion of ppr4 and mtf2 did not or only moderately affect the protein levels of other Mrh5C subunits (Fig. 1, C and D).
PMID:38499152	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC8C9.06c	In contrast, the deletion of ppr4 and mtf2 did not or only moderately affect the protein levels of other Mrh5C subunits (Fig. 1, C and D).
PMID:38499152	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAP8A3.14c	In contrast, the deletion of ppr4 and mtf2 did not or only moderately affect the protein levels of other Mrh5C subunits (Fig. 1, C and D).
PMID:38499152	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC5D6.12	In contrast, the deletion of ppr4 and mtf2 did not or only moderately affect the protein levels of other Mrh5C subunits (Fig. 1, C and D).
PMID:38499152	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPAC4G9.17c [assayed_transcript] PomBase:SPMIT.01	In control cells (Δpnu1[Δi]), the cox1 and cob1 mRNAs appeared in two peaks, a major peak (peak A) comigrating with the mtSSU and a second peak (peak B) comigrating with the mitoribosome (Fig. 4). In Δmtf2 cells, peak A was up-shifted to the lower-density regions and did not comigrate with the mtSSU, and peak B decreased dramatically (Fig. 4).
PMID:38499152	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPAC4G9.17c [assayed_transcript] PomBase:SPMIT.05	In control cells (Δpnu1[Δi]), the cox1 and cob1 mRNAs appeared in two peaks, a major peak (peak A) comigrating with the mtSSU and a second peak (peak B) comigrating with the mitoribosome (Fig. 4). In Δmtf2 cells, peak A was up-shifted to the lower-density regions and did not comigrate with the mtSSU, and peak B decreased dramatically (Fig. 4).
PMID:38499152	FYPO:0000342	decreased cellular respiration [has_severity] high	It is likely that the abolishment of Cox1 synthesis results in the downregulation of OXPHOS complexes. Consistent with these results, cells harboring mrh5D261A-Myc or mrh5E262A-Myc could not grow on glycerol-containing medium, suggesting that they are respiratory-deficient (Fig. S5).
PMID:38499152	FYPO:0000342	decreased cellular respiration [has_severity] high	It is likely that the abolishment of Cox1 synthesis results in the downregulation of OXPHOS complexes. Consistent with these results, cells harboring mrh5D261A-Myc or mrh5E262A-Myc could not grow on glycerol-containing medium, suggesting that they are respiratory-deficient (Fig. S5).
PMID:38499152	FYPO:0000704	abnormal protein-protein interaction [assayed_protein] PomBase:SPBC25D12.06 [assayed_protein] PomBase:SPAC4G9.17c	Mrh5C subunits no longer associate with each other. Mrh5 co-immunoprecipitated with the mtSSU as expected (Fig. 3A). Deletion of mtf2 dramatically reduced this association, suggesting that the whole complex is involved in mtSSU binding (Fig. 3A).
PMID:38499152	GO:0097177	mitochondrial ribosome binding	Mrh5C subunits no longer associate with each other. Mrh5 co-immunoprecipitated with the mtSSU as expected (Fig. 3A). Deletion of mtf2 dramatically reduced this association, suggesting that the whole complex is involved in mtSSU binding (Fig. 3A). |Mrh5C was predominantly associated with the mtSSU in WT cells (Fig. 3D)
PMID:38499152	FYPO:0000704	abnormal protein-protein interaction [assayed_protein] PomBase:SPBC25D12.06 [assayed_protein] PomBase:SPAC2F7.15	Mutations of the DEAD-box in Mrh5-Myc resulted in the dissociation of the Mrh5 mutants with the mtSSU (Figs. 7 and S6).
PMID:38499152	FYPO:0000704	abnormal protein-protein interaction [assayed_protein] PomBase:SPAC4G9.17c [assayed_protein] PomBase:SPBC25D12.06	Mutations of the DEAD-box in Mrh5-Myc resulted in the dissociation of the Mrh5 mutants with the mtSSU (Figs. 7 and S6).
PMID:38499152	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAP8A3.14c [assayed_protein] PomBase:SPBC25D12.06	Similarly, deletion of ppr4 did not impair the interaction among Mrh5-Myc, Sls1-FLAG, and Mtf2-HA (Fig. 2E).
PMID:38499152	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAP8A3.14c [assayed_protein] PomBase:SPAC5D6.12	Similarly, deletion of ppr4 did not impair the interaction among Mrh5-Myc, Sls1-FLAG, and Mtf2-HA (Fig. 2E).
PMID:38499152	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.05	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.04	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.07	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.01 [has_severity] high	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.11	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C)
PMID:38499152	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.04	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C).
PMID:38499152	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.05	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C).
PMID:38499152	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.07	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C).
PMID:38499152	FYPO:0003915	decreased mitochondrial protein level [assayed_protein] PomBase:SPMIT.11	These mutations also completely abolished Cox1 synthesis and decreased the synthesis of other mtDNA-encoded proteins (Fig. 5, B and C).
PMID:38598031	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	(Figure 1a)
PMID:38598031	FYPO:0000098	sensitive to calcium [has_severity] medium	(Figure 1b)
PMID:38598031	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 2)
PMID:38598031	FYPO:0000098	sensitive to calcium [has_severity] high	(Figure 2)
PMID:38598031	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 2)
PMID:38598031	FYPO:0000098	sensitive to calcium [has_severity] medium	(Figure 2)
PMID:38598031	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	(Figure 2)
PMID:38598031	FYPO:0000098	sensitive to calcium [has_severity] medium	(Figure 2)
PMID:38598031	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	(Figure 2)
PMID:38598031	FYPO:0001020	normal growth on calcium	(Figure 2)
PMID:38598031	FYPO:0005947	normal growth on potassium chloride	(Figure 2)
PMID:38598031	FYPO:0000098	sensitive to calcium [has_severity] high	(Figure 2)
PMID:38598031	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	(Figure 3a)
PMID:38598031	FYPO:0000098	sensitive to calcium [has_severity] high	(Figure 3a)
PMID:38598031	FYPO:0000098	sensitive to calcium [has_severity] high	(Figure 3a)
PMID:38598031	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 3a)
PMID:38598031	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 3a)
PMID:38598031	FYPO:0000098	sensitive to calcium [has_severity] medium	(Figure 3a)
PMID:38598031	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	(Figure 3b)
PMID:38598031	FYPO:0000098	sensitive to calcium [has_severity] medium	(Figure 3b)
PMID:38598031	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	(Figure 3b)
PMID:38598031	FYPO:0001020	normal growth on calcium	(Figure 3b)
PMID:38598031	FYPO:0001214	sensitive to potassium chloride [has_severity] medium	(Figure 3c)
PMID:38598031	FYPO:0005947	normal growth on potassium chloride	(Figure 3c)
PMID:38598031	FYPO:0000098	sensitive to calcium [has_severity] medium	(Figure 3c)
PMID:38598031	FYPO:0001020	normal growth on calcium	(Figure 3c)
PMID:38598031	FYPO:0000098	sensitive to calcium [has_severity] medium	(Figure 3c) rst2∆ partially rescues the pps1∆ pka1∆ strain on CaCl2
PMID:38598031	FYPO:0001214	sensitive to potassium chloride [has_severity] high	(Figure 3c) rst2∆ partially rescues the pps1∆ pka1∆ strain on KCl
PMID:38598031	GO:0005886	plasma membrane	(Figure 4)
PMID:38598031	GO:0005783	endoplasmic reticulum	(Figure 4)
PMID:38598031	GO:0005886	plasma membrane [exists_during] cellular response to potassium ion	(Figure 4)
PMID:38598031	GO:0005783	endoplasmic reticulum [exists_during] cellular response to potassium ion	(Figure 4)
PMID:38598031	FYPO:0002126	abolished protein localization to plasma membrane during vegetative growth [assayed_protein] PomBase:SPCC1442.12	(Figure 4a)
PMID:38598031	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPCC1442.12	(Figure 4a)
PMID:38598031	GO:0005737	cytoplasm [exists_during] cellular response to calcium ion	(Figure 5)
PMID:38598031	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPBC106.10	(Figure 5)
PMID:38598031	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPBC106.10	(Figure 5)
PMID:38598031	FYPO:0004056	decreased protein localization to nucleus, with protein mislocalized to cytoplasm [assayed_protein] PomBase:SPBC106.10 [has_penetrance] 100 [has_severity] high	(Figure 5)
PMID:38598031	FYPO:0005890	normal protein localization to nucleus during cellular response to calcium ion [assayed_protein] PomBase:SPBC106.10	(Figure 5)
PMID:38598031	GO:0005634	nucleus	(Figure 5)
PMID:38598031	GO:0005737	cytoplasm	(Figure 5)
PMID:38598031	GO:0005737	cytoplasm [exists_during] cellular response to potassium ion	(Figure 5)
PMID:38598031	FYPO:0004056	decreased protein localization to nucleus, with protein mislocalized to cytoplasm [assayed_protein] PomBase:SPBC106.10 [has_penetrance] 100 [has_severity] high	(Figure 5)
PMID:38598031	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPBC106.10	(Figure 5)
PMID:38598031	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPBC106.10	(Figure 5)
PMID:38598031	FYPO:0005890	normal protein localization to nucleus during cellular response to calcium ion [assayed_protein] PomBase:SPBC106.10	(Figure 5)
PMID:38598031	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0001266	normal protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0001266	normal protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0001266	normal protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0001266	normal protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38598031	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_protein] PomBase:SPBC106.10	(Figure 6)
PMID:38677290	FYPO:0008358	increased protein aggregate level [assayed_protein] PomBase:SPBC19G7.13	Furthermore, we found that all S100A, T104A, and N107A mutant proteins formed aggregation easily during concentration in our purification process, indicating that these three mutations also resulted in protein instability of spTbf1TRFH
PMID:38677290	FYPO:0008358	increased protein aggregate level [assayed_protein] PomBase:SPBC19G7.13	Furthermore, we found that all S100A, T104A, and N107A mutant proteins formed aggregation easily during concentration in our purification process, indicating that these three mutations also resulted in protein instability of spTbf1TRFH
PMID:38677290	FYPO:0005018	decreased double-stranded DNA binding	Interestingly, although the internal loop region (spTbf1loop, residues 320- 407) could not bind S. pombe telomeric DNA alone, it enhanced the binding affinity of both spTbf1TRFH and spTbf1Myb-L (Figure 4F), indicative of important roles of spTbf1loop in spTbf1 recognition of telomeric DNA. Consistently, deletion of the loop region (spTbf1Dloop) significantly reduced the binding affinity of spTbf1 with S. pombe telomeric DNA (Figure 4F).
PMID:38677290	FYPO:0002276	increased protein degradation [assayed_protein] PomBase:SPBC19G7.13	Surprisingly, arginine substitutions of the hydrophobic residues (L101R, L108R, V141R, and V148R) led to degradation and insolubility of mutant proteins of spTbf1TRFH (Figures S3) | Consistently, all L101R, L108R, V141R, and V148R mutations resulted in great degradation of spTbf1 in cells (Figure 2E).
PMID:38677290	FYPO:0002276	increased protein degradation [assayed_protein] PomBase:SPBC19G7.13	Surprisingly, arginine substitutions of the hydrophobic residues (L101R, L108R, V141R, and V148R) led to degradation and insolubility of mutant proteins of spTbf1TRFH (Figures S3) | Consistently, all L101R, L108R, V141R, and V148R mutations resulted in great degradation of spTbf1 in cells (Figure 2E).
PMID:38677290	FYPO:0002276	increased protein degradation [assayed_protein] PomBase:SPBC19G7.13	Surprisingly, arginine substitutions of the hydrophobic residues (L101R, L108R, V141R, and V148R) led to degradation and insolubility of mutant proteins of spTbf1TRFH (Figures S3). | Consistently, all L101R, L108R, V141R, and V148R mutations resulted in great degradation of spTbf1 in cells (Figure 2E).
PMID:38677290	FYPO:0002276	increased protein degradation [assayed_protein] PomBase:SPBC19G7.13	Surprisingly, arginine substitutions of the hydrophobic residues (L101R, L108R, V141R, and V148R) led to degradation and insolubility of mutant proteins of spTbf1TRFH (Figures S3). | Consistently, all L101R, L108R, V141R, and V148R mutations resulted in great degradation of spTbf1 in cells (Figure 2E).
PMID:38677290	GO:0003691	double-stranded telomeric DNA binding	The spTbf1- TeloDNA complex exhibited a significant supershift, consistent with the previous report that spTbf1 binds S. pombe telomeric dsDNA with high affinity (Figure 4F).32
PMID:38692277	FYPO:0000443	abnormal protein localization during vegetative growth [assayed_protein] PomBase:SPAC1610.04	(comment: CHECK ******NEW TERM REQUIRED ******)In contrast, in the absence of Mic10 and Mic26, which are constituents of a second MICOS subcomplex, Mmc1 lost its semi-punctate appearance and was more uniformly localized throughout the mitochondrial network (Figures 3A and 3B).
PMID:38692277	FYPO:0000443	abnormal protein localization during vegetative growth [assayed_protein] PomBase:SPAC1610.04	(comment: CHECK ******NEW TERM REQUIRED ******)In contrast, in the absence of Mic10 and Mic26, which are constituents of a second MICOS subcomplex, Mmc1 lost its semi-punctate appearance and was more uniformly localized throughout the mitochondrial network (Figures 3A and 3B).
PMID:38692277	GO:0042407	cristae formation	(comment: complex member)
PMID:38692277	GO:0042407	cristae formation	(comment: complex member)
PMID:38692277	GO:0042407	cristae formation	(comment: complex member)
PMID:38692277	GO:0044284	mitochondrial crista junction	. These data, in combination with previous immuno-EM-labeling experiments of MICOS subunits,31,38 suggest that Mmc1 concentrates at cristae junctions, where it associates in proximity with the MICOS complex.
PMID:38692277	FYPO:0005419	abnormal mitochondrial crista morphology [has_severity] low	Approximately half of the Dmmc1 cells had abnormal mitochondrial morphology, and many cells contained the lamellar and ring-shaped mitochondria characteristic of cells with MICOS subunit deletions (Figures 2H and 2I)
PMID:38692277	GO:0061617	MICOS complex	As expected, all core MICOS subunits were identified among the top hits by both Mic60 and Mic26 (Figures 1F and 1G, blue).
PMID:38692277	GO:0061617	MICOS complex	As expected, all core MICOS subunits were identified among the top hits by both Mic60 and Mic26 (Figures 1F and 1G, blue).
PMID:38692277	GO:0061617	MICOS complex	As expected, all core MICOS subunits were identified among the top hits by both Mic60 and Mic26 (Figures 1F and 1G, blue).
PMID:38692277	GO:0061617	MICOS complex	As expected, all core MICOS subunits were identified among the top hits by both Mic60 and Mic26 (Figures 1F and 1G, blue).
PMID:38692277	GO:0044284	mitochondrial crista junction	Both Mic60 and Mic26 appeared in a semi-punctate pattern distributed throughout the mitochondrial network (Figure 1E). These localization data are similar to observations in both budding yeast and human cells,26,38 suggesting that MICOS complexes also concentrate at cristae junctions in fission yeast.
PMID:38692277	GO:0044284	mitochondrial crista junction	Both Mic60 and Mic26 appeared in a semi-punctate pattern distributed throughout the mitochondrial network (Figure 1E). These localization data are similar to observations in both budding yeast and human cells,26,38 suggesting that MICOS complexes also concentrate at cristae junctions in fission yeast.
PMID:38692277	GO:0099617	matrix side of mitochondrial inner membrane	Instead, Mmc1-FLAG was only degraded after the combined addition of Proteinase K and the detergent Triton X-100, suggesting that the C terminus of Mmc1 localizes to the matrix. Mmc1 was found in the pellet fraction, indicating that it is an integral membrane protein (Figure 2C).
PMID:38692277	GO:0005739	mitochondrion	Mmc1-FLAG was detected in the purified mitochondria by western analysis and was protected from Proteinase K digestion, suggesting the protein indeed localizes to mitochondria (Figure 2B
PMID:38692277	FYPO:0000342	decreased cellular respiration [has_severity] high	Strikingly, we observed a severe synthetic growth defect specifically on respiration-requiring media in the absence of Mmc1 and MICOS subunits (Figure 5D).
PMID:38692277	FYPO:0000342	decreased cellular respiration [has_severity] high	Strikingly, we observed a severe synthetic growth defect specifically on respiration-requiring media in the absence of Mmc1 and MICOS subunits (Figure 5D).
PMID:38692277	GO:0042407	cristae formation	Together, these data indicate that Mmc1 is a MICOS complex-associated protein required for normal cristae morphology.
PMID:38692277	FYPO:0003393	abnormal respiratory electron transport	disruption of cristae architecture through loss of the core MICOS subunit Mic60 caused a growth defect specifically on media that requires respiration (Figure 1D).
PMID:38692277	FYPO:0003393	abnormal respiratory electron transport	disruption of cristae architecture through loss of the core MICOS subunit Mic60 caused a growth defect specifically on media that requires respiration (Figure 1D).
PMID:38692277	FYPO:0003393	abnormal respiratory electron transport	disruption of cristae architecture through loss of the core MICOS subunit Mic60 caused a growth defect specifically on media that requires respiration (Figure 1D).
PMID:38692277	FYPO:0003393	abnormal respiratory electron transport	disruption of cristae architecture through loss of the core MICOS subunit Mic60 caused a growth defect specifically on media that requires respiration (Figure 1D).
PMID:38692277	FYPO:0005419	abnormal mitochondrial crista morphology	the absence of MICOS subunits caused characteristic alterations in mitochondrial morphology (Figure 1A).
PMID:38692277	FYPO:0005419	abnormal mitochondrial crista morphology [has_severity] high	the absence of MICOS subunits caused characteristic alterations in mitochondrial morphology (Figure 1A).
PMID:38692277	FYPO:0005419	abnormal mitochondrial crista morphology [has_severity] high	the absence of MICOS subunits caused characteristic alterations in mitochondrial morphology (Figure 1A).
PMID:38692277	FYPO:0005419	abnormal mitochondrial crista morphology	the absence of MICOS subunits caused characteristic alterations in mitochondrial morphology (Figure 1A).
PMID:38692277	FYPO:0005419	abnormal mitochondrial crista morphology	the absence of MICOS subunits caused characteristic alterations in mitochondrial morphology (Figure 1A).
PMID:38692277	FYPO:0005419	abnormal mitochondrial crista morphology	the absence of MICOS subunits caused characteristic alterations in mitochondrial morphology (Figure 1A).
PMID:3870979	FYPO:0002043	normal premeiotic DNA replication	(comment: at 33.5 degrees, which is restrictive for cdc10-129 but allows sporulation)
PMID:3870979	FYPO:0000583	abolished sporulation	(comment: at 33.5 degrees, which is restrictive for cdc10129 but allows sporulation)
PMID:3870979	FYPO:0000681	abnormal sporulation resulting in formation of two-spore ascus	(comment: at 33.5 degrees, which is restrictive for cdc2-33 but allows sporulation)
PMID:3870979	FYPO:0002043	normal premeiotic DNA replication	(comment: at 33.5 degrees, which is restrictive for cdc2-33 but allows sporulation)
PMID:3870979	FYPO:0001886	meiotic cell cycle entry and sporulation in haploid	(comment: done in h- cells kinetics depend on medium composition (see fig 6B))
PMID:38718864	FYPO:0001690	normal growth on camptothecin	(Fig. 1A)
PMID:38718864	FYPO:0001690	normal growth on camptothecin	(Fig. 1A)
PMID:38718864	FYPO:0001690	normal growth on camptothecin	(Fig. 1A)
PMID:38718864	FYPO:0001690	normal growth on camptothecin	(Fig. 1A)
PMID:38718864	FYPO:0001690	normal growth on camptothecin	(Fig. 1A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 1A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 1A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 1A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 1A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 1A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 1A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 1A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 1A)
PMID:38718864	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1A)
PMID:38718864	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1A)
PMID:38718864	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1A)
PMID:38718864	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1A)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 1A)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 1A)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 1A)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0001690	normal growth on camptothecin	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1A)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] medium	(Fig. 1B)
PMID:38718864	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1B)
PMID:38718864	FYPO:0003670	sensitive to mycophenolic acid [has_severity] high	(Fig. 1B)
PMID:38718864	FYPO:0003670	sensitive to mycophenolic acid [has_severity] medium	(Fig. 1B)
PMID:38718864	FYPO:0003670	sensitive to mycophenolic acid [has_severity] medium	(Fig. 1B)
PMID:38718864	FYPO:0003670	sensitive to mycophenolic acid [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0003670	sensitive to mycophenolic acid [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 1B)
PMID:38718864	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 1B)
PMID:38718864	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 1B)
PMID:38718864	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 1B)
PMID:38718864	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 1B)
PMID:38718864	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 1B)
PMID:38718864	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 1B)
PMID:38718864	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 1B)
PMID:38718864	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 1B)
PMID:38718864	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 1B)
PMID:38718864	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 1B)
PMID:38718864	FYPO:0007074	normal growth on mycophenolic acid	(Fig. 1B)
PMID:38718864	FYPO:0000069	resistance to thiabendazole	(Fig. 1B)
PMID:38718864	FYPO:0000069	resistance to thiabendazole	(Fig. 1B)
PMID:38718864	FYPO:0000069	resistance to thiabendazole	(Fig. 1B)
PMID:38718864	FYPO:0000069	resistance to thiabendazole	(Fig. 1B)
PMID:38718864	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1B)
PMID:38718864	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 1B)
PMID:38718864	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0000964	normal growth on thiabendazole	(Fig. 1B)
PMID:38718864	FYPO:0000964	normal growth on thiabendazole	(Fig. 1B)
PMID:38718864	FYPO:0000964	normal growth on thiabendazole	(Fig. 1B)
PMID:38718864	FYPO:0000964	normal growth on thiabendazole	(Fig. 1B)
PMID:38718864	FYPO:0000964	normal growth on thiabendazole	(Fig. 1B)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 1B)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 1B)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 1B)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 1B)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 1B)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 1B)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1B)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1B)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1B)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1B)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1B)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1B)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1B)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1B)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1B)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] high	(Fig. 1B)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] high	(Fig. 1B)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] medium	(Fig. 1B)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] medium	(Fig. 1B)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] medium	(Fig. 1B)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 1B)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 1B)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 1B)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 1B)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 1B)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 1B)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 1B)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 1B)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 1B)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 1B)
PMID:38718864	FYPO:0002578	resistance to hydroxyurea [has_severity] medium	(Fig. 1B)
PMID:38718864	FYPO:0002578	resistance to hydroxyurea [has_severity] medium	(Fig. 1B)
PMID:38718864	FYPO:0002578	resistance to hydroxyurea [has_severity] medium	(Fig. 1B)
PMID:38718864	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1B)
PMID:38718864	FYPO:0002578	resistance to hydroxyurea [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0002578	resistance to hydroxyurea [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1B)
PMID:38718864	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1B)
PMID:38718864	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1B)
PMID:38718864	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1B)
PMID:38718864	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1B)
PMID:38718864	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1B)
PMID:38718864	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1B)
PMID:38718864	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1B)
PMID:38718864	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1B)
PMID:38718864	FYPO:0005159	decreased DNA synthesis involved in mitotic DNA replication [has_severity] low [has_penetrance] 10	(Fig. 2A and B)
PMID:38718864	FYPO:0005159	decreased DNA synthesis involved in mitotic DNA replication [has_penetrance] 30 [has_severity] low	(Fig. 2A and B)
PMID:38718864	FYPO:0005159	decreased DNA synthesis involved in mitotic DNA replication [has_penetrance] 40 [has_severity] medium	(Fig. 2C and D)
PMID:38718864	FYPO:0005159	decreased DNA synthesis involved in mitotic DNA replication [has_penetrance] 30 [has_severity] low	(Fig. 2C and D)
PMID:38718864	FYPO:0005159	decreased DNA synthesis involved in mitotic DNA replication [has_penetrance] 30 [has_severity] low	(Fig. 2C and D)
PMID:38718864	FYPO:0005159	decreased DNA synthesis involved in mitotic DNA replication [has_severity] medium [has_penetrance] 30	(Fig. 2C and D)
PMID:38718864	FYPO:0005159	decreased DNA synthesis involved in mitotic DNA replication [has_penetrance] 10	(Fig. 2I)
PMID:38718864	FYPO:0005159	decreased DNA synthesis involved in mitotic DNA replication [has_penetrance] 10	(Fig. 2I)
PMID:38718864	FYPO:0005159	decreased DNA synthesis involved in mitotic DNA replication [has_penetrance] 15	(Fig. 2J)
PMID:38718864	FYPO:0005159	decreased DNA synthesis involved in mitotic DNA replication [has_penetrance] 25	(Fig. 2J)
PMID:38718864	FYPO:0005159	decreased DNA synthesis involved in mitotic DNA replication [has_penetrance] 30	(Fig. 2J)
PMID:38718864	FYPO:0005159	decreased DNA synthesis involved in mitotic DNA replication [has_penetrance] 15	(Fig. 2J)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 3A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 3A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3A)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3A)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3A)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3B)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3B)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3B)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3B)
PMID:38718864	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 3B)
PMID:38718864	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 3B)
PMID:38718864	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 3B)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3B)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3B)
PMID:38718864	FYPO:0001690	normal growth on camptothecin	(Fig. 3B)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3B)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3B)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3B)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3B)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3C)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 3C)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3C)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3C)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3C)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3C)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3C)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3C)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3C)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3D)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3D)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3D)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3D)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3D)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3D)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3E)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3E)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 3E)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3E)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3E)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 3E)
PMID:38718864	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 3E)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3E)
PMID:38718864	FYPO:0004557	increased vegetative cell population growth [has_severity] low	(Fig. 3E)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 3F)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 3F)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 3F)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 3F)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3F)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 3F)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3H)
PMID:38718864	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 3H)
PMID:38718864	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 3H)
PMID:38718864	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 3H)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3H)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3H)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3H)
PMID:38718864	FYPO:0000725	resistance to methyl methanesulfonate [has_severity] low	(Fig. 3H)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3H)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3H)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 3I)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 3I)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 3I)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3I)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3I)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3I)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 3I)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 3I)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3J)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3J)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 3J)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3J)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3J)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 3J)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 3J)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3J)
PMID:38718864	FYPO:0007881	increased duration of histone H2A phosphorylation during cellular response to methyl methanesulfonate	(Fig. 4B)
PMID:38718864	FYPO:0007881	increased duration of histone H2A phosphorylation during cellular response to methyl methanesulfonate	(Fig. 4C)
PMID:38718864	FYPO:0005677	decreased number of Rad52 foci during mitotic S phase	(Fig. 4E)
PMID:38718864	FYPO:0000972	increased number of Rad52 foci during vegetative growth	(Fig. 4E)
PMID:38718864	FYPO:0000972	increased number of Rad52 foci during vegetative growth	(Fig. 4E)
PMID:38718864	FYPO:0005677	decreased number of Rad52 foci during mitotic S phase	(Fig. 4E)
PMID:38718864	FYPO:0002340	decreased DNA recombination during vegetative growth	(Fig. 4F)
PMID:38718864	FYPO:0002340	decreased DNA recombination during vegetative growth	(Fig. 4F)
PMID:38718864	FYPO:0003486	abolished protein localization to double-strand break site [assayed_protein] PomBase:SPAC644.14c	(Fig. 5)
PMID:38718864	FYPO:0003486	abolished protein localization to double-strand break site [assayed_protein] PomBase:SPAC644.14c	(Fig. 5)
PMID:38718864	FYPO:0002475	increased protein localization to double-strand break site [assayed_protein] PomBase:SPCC622.09	(Fig. 6A-D)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] low	(Fig. 7)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 7B and G)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 7B and G)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 7B and G)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 7B and G)
PMID:38718864	FYPO:0009031	resistance to bleomycin	(Fig. 7B and G)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7B and G)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] low	(Fig. 7B and G)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] low	(Fig. 7B and G)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7B and G)
PMID:38718864	FYPO:0009010	resistance to UV during vegetative growth	(Fig. 7B and G)
PMID:38718864	FYPO:0009010	resistance to UV during vegetative growth	(Fig. 7B and G)
PMID:38718864	FYPO:0009010	resistance to UV during vegetative growth	(Fig. 7B and G)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7B and G)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 7B and G)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(Fig. 7B and G)
PMID:38718864	FYPO:0004752	resistance to phleomycin	(Fig. 7B and G)
PMID:38718864	FYPO:0004752	resistance to phleomycin	(Fig. 7B and G)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 7B and G)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature	(Fig. 7B and G)
PMID:38718864	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 7B and G)
PMID:38718864	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 7B and G)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 7B and G)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 7B and G)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7B and G)
PMID:38718864	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 7B and G)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7C and H)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 7C and H)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 7C and H)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(Fig. 7C and H)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7C and H)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7C and H)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7C and H)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7C and H)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7C and H)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7C and H)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7C and H)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 7C and H)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 7C and H)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 7C and H)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 7C and H)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 7C and H)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 7C and H)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 7C and H)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 7C and H)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 7C and H)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 7C and H)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 7C and H)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 7C and H)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7C and H)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7C and H)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7C and H)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7D)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7D)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7D)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 7D)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7D)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 7D)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 7D)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 7D)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 7D)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 7D)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7D)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7D)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7D)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7D)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7D)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 7D)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7D)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 7D)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7D)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 7D)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 7D)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7D)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7D)
PMID:38718864	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 7D)
PMID:38718864	FYPO:0004752	resistance to phleomycin	(Fig. 7E)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7E)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7E)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 7E)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7E)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7E)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7E)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7E)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7E)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7E)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] low	(Fig. 7E)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 7E)
PMID:38718864	FYPO:0004752	resistance to phleomycin	(Fig. 7E)
PMID:38718864	FYPO:0004752	resistance to phleomycin	(Fig. 7E)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7E)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7E)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7E)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 7E)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 7E)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 7E)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. 7E)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7E)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7F)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7F)
PMID:38718864	FYPO:0000674	normal cell population growth at high temperature	(Fig. 7F)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(Fig. 7F)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7F)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7F)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7F)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 7F)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 7F)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 7F)
PMID:38718864	FYPO:0003183	normal growth on phleomycin	(Fig. 7F)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7F)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7F)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7F)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 7F)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] low	(Fig. 7F)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7F)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7F)
PMID:38718864	FYPO:0003906	normal growth on bleomycin	(Fig. 7F)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7F)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7F)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7F)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7F)
PMID:38718864	FYPO:0000969	normal growth during cellular response to UV	(Fig. 7G)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7G)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7G)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 7G)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 7G)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7G)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 7G)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] medium	(Fig. 7G)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] high	(Fig. 7G)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] high	(Fig. 7G)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7G)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7G)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7G)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 7G)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] high	(Fig. 7G)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] high	(Fig. 7G)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 7G)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7G)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7H)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] high	(Fig. 7H)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] medium	(Fig. 7H)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 7H)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 7H)
PMID:38718864	FYPO:0001357	normal vegetative cell population growth	(Fig. 7H)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7H)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7H)
PMID:38718864	FYPO:0009010	resistance to UV during vegetative growth	(Fig. 7H)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] high	(Fig. 7H)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 7H)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7H)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7J)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] high	(Fig. 7J)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] high	(Fig. 7J)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 7J)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7J)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] high	(Fig. 7J)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 7J)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7J)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] high	(Fig. 7J)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 7J)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7J)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 7K)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 7K)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] high	(Fig. 7K)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7K)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] high	(Fig. 7K)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 7K)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 7K)
PMID:38718864	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 7K)
PMID:38718864	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 7K)
PMID:38718864	FYPO:0000095	sensitive to bleomycin [has_severity] medium	(Fig. 7K)
PMID:38718864	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 7K)
PMID:38718864	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 7K)
PMID:38718864	FYPO:0002344	sensitive to phleomycin [has_severity] high	(Fig. 7K)
PMID:38718864	FYPO:0002922	abolished histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8A)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8A)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8A)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8A)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8A)
PMID:38718864	FYPO:0007386	decreased histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8A, 8D)
PMID:38718864	FYPO:0007386	decreased histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8A-H)
PMID:38718864	FYPO:0007386	decreased histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8A-H)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8B)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8B)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8B)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8B)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8B)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8B)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8B)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8B)
PMID:38718864	FYPO:0002922	abolished histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8C)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8D)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8D)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8D)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8D)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8D)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8D)
PMID:38718864	FYPO:0002922	abolished histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8D)
PMID:38718864	FYPO:0002922	abolished histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8D)
PMID:38718864	FYPO:0002922	abolished histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8D, 8E)
PMID:38718864	FYPO:0002922	abolished histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8E)
PMID:38718864	FYPO:0002922	abolished histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8E)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8E)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8E)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8E)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8E)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8E)
PMID:38718864	FYPO:0007386	decreased histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8F)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8F)
PMID:38718864	FYPO:0008439	increased histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8F)
PMID:38718864	FYPO:0008439	increased histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8G)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8G)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8G)
PMID:38718864	FYPO:0008439	increased histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8H)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8H)
PMID:38718864	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 8H)
PMID:38718864	FYPO:0005608	decreased histone H2B-K119 ubiquitination at double-strand break site during vegetative growth [has_severity] medium	(Fig. 8I-N)
PMID:38718864	FYPO:0005608	decreased histone H2B-K119 ubiquitination at double-strand break site during vegetative growth [has_severity] high	(Fig. 8I-N)
PMID:38718864	FYPO:0008250	normal protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPCC1919.15 [assayed_region] PomBase:SPCC622.09	(Fig. 9A)
PMID:38718864	FYPO:0008250	normal protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPCC1919.15 [assayed_region] PomBase:SPAC22F8.12c	(Fig. 9A)
PMID:38718864	FYPO:0008250	normal protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPCC1919.15 [assayed_region] PomBase:SPBC32H8.12c	(Fig. 9A)
PMID:38718864	FYPO:0004066	increased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPAC13A11.04c [assayed_region] PomBase:SPAC18B11.07c	(Fig. 9B)
PMID:38718864	FYPO:0004066	increased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPAC13A11.04c [assayed_region] PomBase:SPAC1952.05	(Fig. 9B)
PMID:38718864	FYPO:0004066	increased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPAC13A11.04c [assayed_region] PomBase:SPAC664.07c	(Fig. 9B)
PMID:38718864	FYPO:0004066	increased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPAC13A11.04c [assayed_region] PomBase:SPCC970.10c	(Fig. 9B)
PMID:38718864	FYPO:0004066	increased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPAC13A11.04c [assayed_region] PomBase:SPAC22F8.12c	(Fig. 9B)
PMID:38718864	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_penetrance] 30	HR frequency goes from 20% in WT to 14% in mutant (Fig. 7I)
PMID:38718864	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_penetrance] 25	HR frequency goes from 20% in WT to 15% in mutant (Fig. 7I)
PMID:38718864	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_penetrance] 25	HR frequency goes from 20% in WT to 15% in mutant (Fig. 7I)
PMID:38718864	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_penetrance] 25	HR frequency goes from 20% in WT to 15% in mutant (Fig. 7I)
PMID:38718864	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_penetrance] 25	HR frequency goes from 20% in WT to 15% in mutant (Fig. 7I)
PMID:38718864	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_penetrance] 85	HR frequency goes from 20% in WT to 3% in mutant (Fig. 7I)
PMID:38718864	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_penetrance] 75	HR frequency goes from 20% in WT to 5% in mutant (Fig. 7I)
PMID:38718864	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_penetrance] 75	HR frequency goes from 20% in WT to 5% in mutant (Fig. 7I)
PMID:38718864	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_penetrance] 65	HR frequency goes from 20% in WT to 7% in mutant (Fig. 7I)
PMID:38718864	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_penetrance] 65	HR frequency goes from 20% in WT to 7% in mutant (Fig. 7I)
PMID:38780300	FYPO:0000229	cut [has_severity] high	(Fig. 1B)
PMID:38780300	FYPO:0000229	cut [has_severity] medium	(Fig. 1B)
PMID:38780300	FYPO:0000229	cut [has_severity] medium	(Fig. 1B)
PMID:38780300	FYPO:0000229	cut [has_severity] medium	(Fig. 1D)
PMID:38780300	FYPO:0000229	cut [has_severity] high	(Fig. 1E)
PMID:38780300	FYPO:0000229	cut [has_severity] high	(Fig. 1E)
PMID:38780300	FYPO:0000229	cut [has_severity] medium	(Fig. 1E)
PMID:38780300	FYPO:0000229	cut [has_severity] medium	(Fig. 1E)
PMID:38780300	FYPO:0000365	small nucleus	(Fig. 2)
PMID:38780300	FYPO:0000365	small nucleus	(Fig. 2)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] low	(Fig. 3)
PMID:38780300	PomGeneEx:0000011	RNA level increased [in_presence_of] cerulenin	(Fig. 3)
PMID:38780300	PomGeneEx:0000011	RNA level increased [in_presence_of] cerulenin	(Fig. 3)
PMID:38780300	PomGeneEx:0000011	RNA level increased [in_presence_of] cerulenin	(Fig. 3)
PMID:38780300	PomGeneEx:0000011	RNA level increased [in_presence_of] cerulenin	(Fig. 3)
PMID:38780300	PomGeneEx:0000011	RNA level increased [in_presence_of] cerulenin	(Fig. 3)
PMID:38780300	PomGeneEx:0000011	RNA level increased [in_presence_of] cerulenin	(Fig. 3)
PMID:38780300	PomGeneEx:0000011	RNA level increased [in_presence_of] cerulenin	(Fig. 3)
PMID:38780300	PomGeneEx:0000012	RNA level decreased [in_presence_of] cerulenin	(Fig. 3)
PMID:38780300	PomGeneEx:0000012	RNA level decreased [in_presence_of] cerulenin	(Fig. 3)
PMID:38780300	PomGeneEx:0000012	RNA level decreased [in_presence_of] cerulenin	(Fig. 3)
PMID:38780300	PomGeneEx:0000012	RNA level decreased [in_presence_of] cerulenin	(Fig. 3)
PMID:38780300	PomGeneEx:0000012	RNA level decreased [in_presence_of] cerulenin	(Fig. 3)
PMID:38780300	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1B3.16c [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPCC1450.16c	(Fig. 3)
PMID:38780300	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC926.09c	(Fig. 3)
PMID:38780300	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPCC1235.02	(Fig. 3)
PMID:38780300	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC22A12.06c	(Fig. 3)
PMID:38780300	FYPO:0005187	decreased level of transport gene mRNA during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPAC1039.09	(Fig. 3)
PMID:38780300	FYPO:0005187	decreased level of transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAP7G5.06 [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1450.16c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1786.01c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC1039.09	(Fig. 3)
PMID:38780300	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC926.09c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1786.01c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC4A8.11c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC4A8.11c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC1039.09	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAP7G5.06 [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAP7G5.06 [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAP7G5.06 [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAP7G5.06 [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC4A8.11c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC926.09c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1786.01c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1786.01c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0005187	decreased level of transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0005187	decreased level of transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0005187	decreased level of transport gene mRNA during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC869.10c	(Fig. 3)
PMID:38780300	FYPO:0005187	decreased level of transport gene mRNA during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC869.10c	(Fig. 3)
PMID:38780300	FYPO:0005187	decreased level of transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC869.10c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0005187	decreased level of transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0005187	decreased level of transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC869.10c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0005187	decreased level of transport gene mRNA during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC869.10c	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC869.10c	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC869.10c	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAP7G5.06 [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAP7G5.06 [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1B3.16c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1B3.16c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1450.16c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1450.16c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC4A8.11c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC926.09c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC926.09c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1235.02 [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1235.02 [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1235.02 [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1B3.16c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC22A12.06c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC22A12.06c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC22A12.06c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0000825	increased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPCC1281.06c	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1281.06c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1281.06c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1281.06c [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4H10.11c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBP4H10.11c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBP4H10.11c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBP4H10.11c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC18H10.02 [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC18H10.02 [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC18H10.02 [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC56E4.04c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC56E4.04c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC56E4.04c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1039.09 [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAP7G5.06 [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC869.10c	(Fig. 3)
PMID:38780300	FYPO:0005187	decreased level of transport gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0005187	decreased level of transport gene mRNA during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC869.10c	(Fig. 3)
PMID:38780300	PomGeneEx:0000012	RNA level decreased [in_presence_of] ammonium	(Fig. 3)
PMID:38780300	PomGeneEx:0000012	RNA level decreased [in_presence_of] ammonium	(Fig. 3)
PMID:38780300	PomGeneEx:0000012	RNA level decreased [in_presence_of] ammonium	(Fig. 3)
PMID:38780300	PomGeneEx:0000012	RNA level decreased [in_presence_of] ammonium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1450.16c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC4A8.11c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC926.09c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1235.02 [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1B3.16c [has_severity] low	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC22A12.06c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1281.06c [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBP4H10.11c [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC18H10.02 [has_severity] medium	(Fig. 3)
PMID:38780300	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC56E4.04c [has_severity] high	(Fig. 3)
PMID:38780300	FYPO:0005583	increased fatty acid saturation	(Fig. 4B)
PMID:38780300	FYPO:0005583	increased fatty acid saturation	(Fig. 4B)
PMID:38780300	FYPO:0002317	increased cellular squalene level	(Fig. 4D and E)
PMID:38780300	FYPO:0002235	increased cellular sterol ester level	(Fig. 4D and E)
PMID:38780300	FYPO:0002317	increased cellular squalene level	(Fig. 4D and E)
PMID:38780300	FYPO:0002235	increased cellular sterol ester level	(Fig. 4D and E)
PMID:38780300	FYPO:0006257	normal duration of mitotic prophase	(Fig. 5)
PMID:38780300	FYPO:0000618	increased duration of mitotic anaphase	(Fig. 5)
PMID:38780300	FYPO:0004646	normal duration of mitotic anaphase	(Fig. 5)
PMID:38780300	FYPO:0005683	increased duration of mitotic prophase	(Fig. 5)
PMID:38780300	FYPO:0000229	cut [has_penetrance] 32	(Fig. 6A)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 10	(Fig. 6A)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 28	(Fig. 6A)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 20	(Fig. 6A)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 25	(Fig. 6A)
PMID:38780300	FYPO:0000229	cut [has_penetrance] 3	(Fig. 6A)
PMID:38780300	FYPO:0000229	cut [has_penetrance] 2	(Fig. 6B)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 7	(Fig. 6B)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 4	(Fig. 6B)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 34	(Fig. 6B)
PMID:38780300	FYPO:0000229	cut [has_penetrance] 22	(Fig. 6B)
PMID:38780300	FYPO:0000229	cut [has_penetrance] 3	(Fig. 6B)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 8	(Fig. 6C)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 13	(Fig. 6C)
PMID:38780300	FYPO:0000229	cut [has_penetrance] 6	(Fig. 6C)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 45	(Fig. 6C)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 15	(Fig. 6C)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 10	(Fig. 6C)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 25	(Fig. 6C)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 50	(Fig. 6C)
PMID:38780300	FYPO:0000229	cut [has_penetrance] 6	(Fig. 7A)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 10	(Fig. 7A)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 5	(Fig. 7A)
PMID:38780300	FYPO:0003165	cut [has_penetrance] 5	(Fig. 7A)
PMID:38780300	FYPO:0000229	cut [has_severity] low	(Fig. 7B)
PMID:38780300	FYPO:0000229	cut [has_severity] low	(Fig. 7B)
PMID:38780300	FYPO:0000229	cut [has_severity] medium	(Fig. 7C)
PMID:38780300	FYPO:0000229	cut [has_severity] medium	(Fig. 7C)
PMID:38825008	SO:0001534	nuclear_rim_localization_signal	(comment: This region was identified as a lipid binding region.)
PMID:38825008	FYPO:0004887	normal protein localization to nuclear envelope during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	All these fragments as well as wild-type Bqt4 (FL) were localized to the NE (Fig. 1C), suggesting that the lethality was not caused by the loss of NE localization.
PMID:38825008	FYPO:0004887	normal protein localization to nuclear envelope during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	All these fragments as well as wild-type Bqt4 (FL) were localized to the NE (Fig. 1C), suggesting that the lethality was not caused by the loss of NE localization.
PMID:38825008	FYPO:0004887	normal protein localization to nuclear envelope during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	All these fragments as well as wild-type Bqt4 (FL) were localized to the NE (Fig. 1C), suggesting that the lethality was not caused by the loss of NE localization.
PMID:38825008	FYPO:0004887	normal protein localization to nuclear envelope during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	All these fragments as well as wild-type Bqt4 (FL) were localized to the NE (Fig. 1C), suggesting that the lethality was not caused by the loss of NE localization.
PMID:38825008	FYPO:0004887	normal protein localization to nuclear envelope during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	All these fragments as well as wild-type Bqt4 (FL) were localized to the NE (Fig. 1C), suggesting that the lethality was not caused by the loss of NE localization.
PMID:38825008	FYPO:0004887	normal protein localization to nuclear envelope during vegetative growth [assayed_protein] PomBase:SPBC19C7.10	All these fragments as well as wild-type Bqt4 (FL) were localized to the NE (Fig. 1C), suggesting that the lethality was not caused by the loss of NE localization.
PMID:38825008	FYPO:0008431	nuclear lipid droplet formation [has_penetrance] 66	As expected, the number of cells with nuclear LDs increased in the cells overexpressing Bqt4-FL (Fig. 6, C and D; 65.9%; see arrowhead in FL) compared to the control cells under the suppressive conditions (0-0.3%).
PMID:38825008	FYPO:0002060	viable vegetative cell population	As predicted, the 4KRA mutant did not restore lethality upon shut-off, whereas the other three mutants did (Fig. 4C)
PMID:38825008	FYPO:0002061	inviable vegetative cell population	As predicted, the 4KRA mutant did not restore lethality upon shut-off, whereas the other three mutants did (Fig. 4C)
PMID:38825008	FYPO:0002060	viable vegetative cell population	As predicted, the 4KRA mutant did not restore lethality upon shut-off, whereas the other three mutants did (Fig. 4C)
PMID:38825008	FYPO:0002060	viable vegetative cell population	As predicted, the 4KRA mutant did not restore lethality upon shut-off, whereas the other three mutants did (Fig. 4C)
PMID:38825008	FYPO:0006692	cut with septum between unequally sized nuclei	Consequently, the chromosome was missegregated during the next mitosis (Fig. 3C). Alternatively, the entire chromosome moved to one side or the cells showed a cut phenotype (untimely torn cell phenotype); these cells displayed nuclear membrane extrusion along the spindle microtubule (Movie S2).
PMID:38825008	FYPO:0007457	excess nuclear envelope present during mitotic interphase [has_severity] high	Figure 2 Under overexpression conditions, GFP-IDR was localized in the nucleoplasm, accompanied by a herniated structure adja- cent to the nucleus (Fig. 2E, arrows).
PMID:38825008	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase	Overexpression of the GFP-IDR and GFP-IDR-TM fragments, but not GFP and GFP-KSE, caused dissociation of the centromeres from the NE and their declustering (Fig. 3, A and B).
PMID:38825008	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase	Overexpression of the GFP-IDR and GFP-IDR-TM fragments, but not GFP and GFP-KSE, caused dissociation of the centromeres from the NE and their declustering (Fig. 3, A and B).
PMID:38825008	FYPO:0008431	nuclear lipid droplet formation [has_penetrance] 63	Similar PA accumulation in the nucleus was observed in IDR-TM-overexpressing cells (IDR-TM in Figure 6, A and B for quantification).
PMID:38825008	FYPO:0000772	perforated nuclear envelope	The DKSE mutant was expressed in lem2- shut-off bqt4D cells expressing GFP-GST-NLS, a nuclear protein marker, and nuclear protein leakage from the nucleus was assessed by calculating the fluorescence intensity ratio of the nucleus to the cytoplasm. Upon thiamine addition, GFP- GST-NLS severely leaked from the nucleus of DKSE mutant-expressing cells, but not from the nucleus of FL-expressing cells (Fig. 1, G and H), indicating NE rupture in the DKSE mutant-expressing cells. These results suggest that the KSE domain is vital for NE maintenance.
PMID:38825008	FYPO:0002338	abnormal protein localization to nuclear periphery [assayed_protein] PomBase:SPBC365.12c	The Ish1 signal, which was localized in the NE under normal conditions, was distributed on cytoplasmic membranes besides the NE under overexpression conditions (Fig. 2E)
PMID:38825008	FYPO:0002061	inviable vegetative cell population	The deletion mutants D340 to 383 and D364 to 383, but not D340 to 363, showed growth defect in the lem2-shut-off bqt4D strain (Fig. 1E)
PMID:38825008	FYPO:0002060	viable vegetative cell population	The deletion mutants D340 to 383 and D364 to 383, but not D340 to 363, showed growth defect in the lem2-shut-off bqt4D strain (Fig. 1E)
PMID:38825008	FYPO:0002061	inviable vegetative cell population	The deletion mutants D340 to 383 and D364 to 383, but not D340 to 363, showed growth defect in the lem2-shut-off bqt4D strain (Fig. 1E)
PMID:38825008	FYPO:0002360	normal chromatin silencing at centromere	This dissociation did not affect transcriptional silencing in the centromeric region (Fig. S6A).
PMID:38825008	GO:0070300	phosphatidic acid binding	To confirm the binding of PA to the IDR, we performed a liposome-mediated binding assay. Liposomes with different percentages of PA were prepared and incubated with purified GFP-IDR protein. After isolation of the liposomes via density gradient centrifugation, the proteins bound to the liposomes were electrophoresed and detected using silver staining. GFP-IDR co-sedimented with PA-containing liposomes but not with control liposomes (Fig. 4B). Therefore, we conclude that the IDR region directly binds to PA in vitro.
PMID:38825008	FYPO:0001556	excess nuclear envelope present	Under overexpression conditions, GFP-IDR was localized in the nucleoplasm, accompanied by a herniated structure adjacent to the nucleus (Fig. 2E, arrows). The Ish1 signal, which was localized in the NE under normal conditions, was distributed on cytoplasmic membranes besides the NE under overexpression conditions (Fig. 2E), suggesting that overexpression of GFP-IDR may cause abnormal membrane proliferation.
PMID:38825008	FYPO:0002061	inviable vegetative cell population	Upon shut-off of lem2, the cells expressing D1-140 and D259 to 383 fragments of Bqt4 did not grow, whereas the cells expressing D141 to 262 did (Fig. 1B)
PMID:38825008	FYPO:0002060	viable vegetative cell population	Upon shut-off of lem2, the cells expressing D1-140 and D259 to 383 fragments of Bqt4 did not grow, whereas the cells expressing D141 to 262 did (Fig. 1B)
PMID:38825008	FYPO:0002061	inviable vegetative cell population	Upon shut-off of lem2, the cells expressing D1-140 and D259 to 383 fragments of Bqt4 did not grow, whereas the cells expressing D141 to 262 did (Fig. 1B)
PMID:38825008	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	When GFP-IDR was overexpressed in S. pombe cells under the control of the nmt1 promoter, its overexpression resulted in severe growth defects in the spot assay (Fig. 2D).
PMID:38825008	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC19C7.10 [assayed_protein] PomBase:SPCC594.07c	and retained interaction with Bqt3 (Fig. S1B)
PMID:38825008	FYPO:0004924	normal telomere tethering at nuclear periphery during vegetative growth	and the telomere anchoring (Fig. S1C).
PMID:38830897	FYPO:0001355	decreased vegetative cell population growth	(comment: referring to growth defect) Mutating three other conserved residues in the Sororin domain of Sor1 (F299A, V302A and Y305A) resulted in a similar phenotype (Fig. 2e).
PMID:38830897	FYPO:0001355	decreased vegetative cell population growth	(comment: referring to growth defect) Mutating three other conserved residues in the Sororin domain of Sor1 (F299A, V302A and Y305A) resulted in a similar phenotype (Fig. 2e).
PMID:38830897	FYPO:0001355	decreased vegetative cell population growth	(comment: referring to growth defect) Mutating three other conserved residues in the Sororin domain of Sor1 (F299A, V302A and Y305A) resulted in a similar phenotype (Fig. 2e).
PMID:38830897	GO:0005634	nucleus	In an asynchronously growing culture, Sor1- GFP localized to the nucleus in most cells (Supplementary Fig. 2a)
PMID:38830897	GO:0007064	mitotic sister chromatid cohesion	In metaphase, sor1Δ mutant cells showed a small, but significant, increase of split sister centromeres (Fig. 2a), indicative of a cohesion defect between sister centromeres.
PMID:38830897	FYPO:0000228	lagging mitotic chromosomes [has_severity] low	Indeed, we observed a higher frequency of lagging chromosomes associated with a higher rate of chromosome mis-segregation in eso1-G799D sor1Δ and mis4-242 sor1Δ double mutants as compared to single mutants (Fig. 2b).
PMID:38830897	FYPO:0003241	unequal mitotic sister chromatid segregation [has_severity] low	Indeed, we observed a higher frequency of lagging chromosomes associated with a higher rate of chromosome mis-segregation in eso1-G799D sor1Δ and mis4-242 sor1Δ double mutants as compared to single mutants (Fig. 2b).
PMID:38830897	FYPO:0007198	normal mitotic centromeric sister chromatid cohesion [has_severity] low	Interestingly, the increase in split sister centromeres in sor1Δ mutant cells was prevented in sor1Δ wpl1Δ double mutants (compared to wild type), suggesting that similarly to mammalian cells wpl1 deletion reduces the sister chromatid cohesion defect caused by the sor1Δ mutation (Fig. 2a).
PMID:38830897	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC9E9.05 [assayed_protein] PomBase:SPAC10F6.09c	Sor1-D303A-Pk co-immunoprecipitated less efficiently with the Psm3-GFP protein, compared to wild-type Sor1- Pk, suggesting that the conserved residue D303 in the Sororin domain of Sor1 is important for the association of Sor1 with cohesin (Fig. 2d).
PMID:38833506	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [assayed_using] PomBase:SPCC736.12c	(comment: demonstrated by cDNA copy)
PMID:38833506	GO:1905746	positive regulation of mRNA cis splicing, via spliceosome	(comment: highly expressed genes (or conditionally expressed))
PMID:38833506	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [has_severity] high	Among the 41 tested strains, three showed a markedly low YFP/RFP ratio when compared to the wild type strain: Δcwf12, Δsaf5 and Δsaf1. (Figure 2A)
PMID:38833506	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [has_severity] high	Among the 41 tested strains, three showed a markedly low YFP/RFP ratio when compared to the wild type strain: Δcwf12, Δsaf5 and Δsaf1. (Figure 2A)
PMID:38833506	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [has_severity] high	Among the 41 tested strains, three showed a markedly low YFP/RFP ratio when compared to the wild type strain: Δcwf12, Δsaf5 and Δsaf1. (Figure 2A)
PMID:38833506	FYPO:0006549	decreased gene expression [assayed_using] PomBase:SPCC736.12c	As shown in S3A Fig, the amount of Mmi1 was significantly reduced in Δsaf5 cells to less than 50% (S3B Fig), when compared to a wild type strain. On the other hand, replacing the wild type mmi1 gene with a copy without introns (sfGFP-Mmi1 cDNA), nearly abolished the effect of the absence of Saf5 on the amount of Mmi1 (S3A and S3B Fig).
PMID:38833506	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [has_severity] low	Of these candidates, only 4 were already known to be involved in the regulation of splicing (Cwf12, Saf5, Cwf19 and SPAC1705.02), whereas the remaining 33 were unrelated or not clearly assigned to the regulation of splicing
PMID:38833506	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific	Of these candidates, only 4 were already known to be involved in the regulation of splicing (Cwf12, Saf5, Cwf19 and SPAC1705.02), whereas the remaining 33 were unrelated or not clearly assigned to the regulation of splicing
PMID:38833506	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [has_severity] low	Therefore, when Cdk9 was inactivated, transcription was slowed down [34,35]. We analyzed the splicing of the single intron of cbf11, which is one of the most affected in the Δsaf5 strain, with 60% of intron retention. The addition of the bulky ATP analog barely affected intron retention in a wild type or a Δsaf5 strains (Fig 5A). However, upon adding 3-MB-PP1 to the culture of the cdk9as Δsaf5 strain, splicing of the cbf11 intron was noticeably improved, with intron retention reduced to 25%. Splicing also improved in the cdk9as saf5+ strain (depicted by the pale orange bars), probably as the result of decreasing transcription rate and giving more time for the splicing to occur; however, this improvement was not statistically significant. When we analyzed how inactivation of Cdk9 affected the splicing of multi-intronic genes, such as atg5 or urm1 (Fig 5B and 5C), we consistently observed improvements in all introns 30 minutes after adding 3-MB-PP1
PMID:38833506	FYPO:0003244	decreased mRNA splicing, via spliceosome, intron-specific [has_severity] high	the effect observed in the Δmpn1 strain was comparable to that observed in Δsaf5 cells.
PMID:38865179	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC3H7.13	GFP-Csc1(FHA) localized to SPBs in mitotic cells (Figure 1D).
PMID:38865179	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC3H7.13	In both wild-type and ppa3-D82N cells, Csc1-GFP localized to mitotic SPBs (Figure 4C).
PMID:38865179	FYPO:0002061	inviable vegetative cell population	Interestingly, we found that cells producing both Csc1-GFP and either Ppc89-GBP-mCherry (Figure S2A) or Sid4-GBP-mCherry (Figure 3A) were inviable.
PMID:38865179	FYPO:0002061	inviable vegetative cell population	Interestingly, we found that cells producing both Csc1-GFP and either Ppc89-GBP-mCherry (Figure S2A) or Sid4-GBP-mCherry (Figure 3A) were inviable.
PMID:38865179	FYPO:0005258	increased cell population growth at high temperature	Like ppa3∆, ppa3-D82N cells were viable and 9 rescued growth of cdc11-136, an indication that it is a loss-of-function ppa3 allele (Figure S3A)
PMID:38865179	FYPO:0002060	viable vegetative cell population [assayed_protein] PomBase:SPBC21.06c	Like ppa3∆, ppa3-D82N cells were viable and 9 rescued growth of cdc11-136, an indication that it is a loss-of-function ppa3 allele (Figure S3A)
PMID:38865179	FYPO:0005258	increased cell population growth at high temperature	Like ppa3∆, ppa3-D82N cells were viable and 9 rescued growth of cdc11-136, an indication that it is a loss-of-function ppa3 allele (Figure S3A)
PMID:38865179	FYPO:0005258	increased cell population growth at high temperature	SIP null mutants rescue cdc11- 136 (Singh et al., 2011) and we observed that csc1-R31A also did (Figure 2D).
PMID:38865179	FYPO:0005258	increased cell population growth at high temperature	SIP null mutants rescue cdc11- 136 (Singh et al., 2011) and we observed that csc1-R31A also did (Figure 2D).
PMID:38865179	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Thus, we tested whether csc1-R31A interacted negatively with cdc16-116 cells and found that it did (Figure 2C).
PMID:38865179	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Thus, we tested whether csc1-R31A interacted negatively with cdc16-116 cells and found that it did (Figure 2C).
PMID:38865179	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC1773.01	We also did not detect Csc2-GFP, Csc3-GFP or Csc4-GFP at SPBs in csc1-R31A cells although these proteins were detected at SPBs in wild-type cells (Figure S1B).
PMID:38865179	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC27B12.04c	We also did not detect Csc2-GFP, Csc3-GFP or Csc4-GFP at SPBs in csc1-R31A cells although these proteins were detected at SPBs in wild-type cells (Figure S1B).
PMID:38865179	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC2C4.10c	We also did not detect Csc2-GFP, Csc3-GFP or Csc4-GFP at SPBs in csc1-R31A cells although these proteins were detected at SPBs in wild-type cells (Figure S1B).
PMID:38865179	FYPO:0002061	inviable vegetative cell population	We found that cells producing both Csc1-R31A-GFP and Ppc89-GBP-mCherry (Figure S2B) or Sid4-GBP-mCherry (Figure 3B) were also inviable.
PMID:38865179	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC2C4.10c	We found that this is also true for Csc4. Csc4-GFP was not detected at SPBs in csc1∆, csc2∆, csc3∆ or ppa3∆ cells (Figure S1A).
PMID:38865179	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC2C4.10c	We found that this is also true for Csc4. Csc4-GFP was not detected at SPBs in csc1∆, csc2∆, csc3∆ or ppa3∆ cells (Figure S1A).
PMID:38865179	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPAC2C4.10c	We found that this is also true for Csc4. Csc4-GFP was not detected at SPBs in csc1∆, csc2∆, csc3∆ or ppa3∆ cells (Figure S1A).
PMID:38865179	FYPO:0001490	inviable elongated vegetative cell	died as single elongated cells, consistent with SIN inactivation (Figure S2, C and D)
PMID:38865179	FYPO:0001490	inviable elongated vegetative cell	died as single elongated cells, consistent with SIN inactivation (Figure S2, C and D)
PMID:38865179	FYPO:0001490	inviable elongated vegetative cell	died as single elongated cells, consistent with SIN inactivation (Figure S2, C and D)
PMID:38865179	FYPO:0005709	normal protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC3H7.13	is independent of the SIN because GFP- Csc1(FHA) expressed from the nmt81 promoter of pREP81 localized to mitotic SPBs marked by Sad1-mCherry in the SIN scaffold mutant sid4-SA1 cells at the restrictive temperature (Figure 1E).
PMID:38865179	FYPO:0001875	decreased asymmetric protein localization, with protein localized to both mitotic spindle pole bodies [assayed_protein] PomBase:SPBC21.06c	ppa3-D82N cells producing Sid4-RFP displayed symmetric Sid1-GFP and Cdc7-GFP localization on anaphase SPBs whereas the localization is asymmetric in wild-type cells (Figure 4B). This further demonstrates that ppa3-D82N is a loss of function allele.
PMID:38865179	FYPO:0001875	decreased asymmetric protein localization, with protein localized to both mitotic spindle pole bodies [assayed_protein] PomBase:SPAC9G1.09	ppa3-D82N cells producing Sid4-RFP displayed symmetric Sid1-GFP and Cdc7-GFP localization on anaphase SPBs whereas the localization is asymmetric in wild-type cells (Figure 4B). This further demonstrates that ppa3-D82N is a loss of function allele.
PMID:38865179	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_protein] PomBase:SPBC3H7.13	we did not detect Csc1-R31A-GFP on SPBs at any point in the cell cycle (Figure 1C).
PMID:38865179	FYPO:0001875	decreased asymmetric protein localization, with protein localized to both mitotic spindle pole bodies [assayed_protein] PomBase:SPBC21.06c	we found that Cdc7 and Sid1 localized symmetrically to both SPBs during anaphase in contrast to its asymmetrical distribution to a single SPB in wild-type anaphase cells (Figure 2, A and B).
PMID:38865179	FYPO:0001875	decreased asymmetric protein localization, with protein localized to both mitotic spindle pole bodies [assayed_protein] PomBase:SPAC9G1.09	we found that Cdc7 and Sid1 localized symmetrically to both SPBs during anaphase in contrast to its asymmetrical distribution to a single SPB in wild-type anaphase cells (Figure 2, A and B).
PMID:38889144	FYPO:0000582	decreased rate of spore germination [has_penetrance] high	(Fig. 2)
PMID:38889144	FYPO:0000582	decreased rate of spore germination [has_penetrance] high	(Fig. 2)
PMID:38889144	FYPO:0000582	decreased rate of spore germination	(Fig. 2D)
PMID:38889144	FYPO:0002686	increased cellular trehalose level in spore	(Fig. 4C)
PMID:38889144	FYPO:0002686	increased cellular trehalose level in spore	(Fig. 4C)
PMID:38889144	FYPO:0000582	decreased rate of spore germination	(Fig. 4D)
PMID:38889144	FYPO:0000582	decreased rate of spore germination [has_severity] high	(Fig. 4I and K)
PMID:38889144	FYPO:0000582	decreased rate of spore germination [has_severity] medium	(Fig. 4I and K)
PMID:38889144	FYPO:0000582	decreased rate of spore germination [has_severity] medium	(Fig. 4I and K)
PMID:38889144	FYPO:0002686	increased cellular trehalose level in spore [has_severity] high	(Fig. 4J)
PMID:38889144	FYPO:0002686	increased cellular trehalose level in spore [has_severity] medium	(Fig. 4J)
PMID:38889144	GO:0004555	alpha,alpha-trehalase activity [part_of] spore germination	These results suggest that Ntp1-mediated trehalose degra­dation is required for cytoplasmic fluidization and rapid germi­ nation through the cAMP-PKA pathway.
PMID:38889144	GO:0004691	cAMP-dependent protein kinase activity [part_of] positive regulation of trehalose catabolic process	These results suggest that Ntp1-mediated trehalose degra­dation is required for cytoplasmic fluidization and rapid germi­nation through the cAMP-PKA pathway.
PMID:38899862	FYPO:0006658	decreased acid phosphatase activity during cellular response to phosphate starvation	(Fig. 12)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1B)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 1B). The asp1-STF7 pyrophosphatase mutation resulted in derepression of Pho1 expression, by 23-fold compared to the wild-type control.
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. 2A)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. 2A)
PMID:38899862	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 2A)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. 2A)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. 2A)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. 2A)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. 2A)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. 2A)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. 2A)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2B)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 2B)
PMID:38899862	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 3A)
PMID:38899862	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 3A)
PMID:38899862	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 3A)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. 3A)
PMID:38899862	FYPO:0002141	normal cell population growth at low temperature	(Fig. 3A)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. 3A, 4A)
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 3B)
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 3B)
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 3B)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 3B)
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 3B)
PMID:38899862	FYPO:0002141	normal cell population growth at low temperature	(Fig. 4A)
PMID:38899862	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 4A)
PMID:38899862	FYPO:0000080	decreased cell population growth at low temperature	(Fig. 4A)
PMID:38899862	FYPO:0002141	normal cell population growth at low temperature	(Fig. 4A)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] low	(Fig. 4B)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4B)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] low	(Fig. 4B)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4B)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C, 6E)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 4C, 6E)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1271.09	(Fig. 5)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1271.09	(Fig. 5)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1271.09	(Fig. 5)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1271.09	(Fig. 5)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1271.09	(Fig. 5)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 5)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 5)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 5)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 5)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 5)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 5)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 5)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 5)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 5)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 5)
PMID:38899862	FYPO:0001355	decreased vegetative cell population growth	(Fig. 6A,D) (STF6)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. 6D)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. 6D)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. 6D)
PMID:38899862	FYPO:0001355	decreased vegetative cell population growth	(Fig. 6D) (STF9)
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 6E)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [has_severity] low	(Fig. 6E)
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [has_severity] low	(Fig. 6E)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1271.07c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC584.16c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC584.16c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC5H10.03	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC5H10.03	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC36.03c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC110.01	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC110.01	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC70.08c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC70.08c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCPB1C11.03	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCPB1C11.03	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBPB10D8.01	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC513.07	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC513.07	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC26H8.11c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBPB8B6.04c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBPB21E7.07	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1271.08c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1271.08c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1685.17	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1685.17	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBPB2B2.01	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBPB2B2.01	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBPB2B2.06c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBPB2B2.06c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBP4G3.02	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.01c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC17D4.01	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC17D4.01	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBPB2B2.05	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBPB2B2.05	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC23G7.13c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC23G7.13c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC1039.02	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC1039.02	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAPB24D3.07c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAPB24D3.07c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1289.14	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1289.14	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC2E1P3.05c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC2E1P3.05c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC794.04c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.12c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC8E4.12c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC29B5.02c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC29B5.02c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC1223.03c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC1223.03c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC3C7.14c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC3C7.14c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC757.07c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC757.07c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1861.02	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1861.02	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC794.12c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPCC794.12c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC1271.07c	(Fig. 7)
PMID:38899862	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC15E1.02c	(Fig. 7)
PMID:38899862	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	(Fig. S1A)
PMID:38899862	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	(Fig. S1A)
PMID:38899862	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	(Fig. S1A)
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] high	(Fig. S1B)
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] high	(Fig. S1B)
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] high	(Fig. S1B)
PMID:38899862	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S2A)
PMID:38899862	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S2A)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. S2B)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. S2B)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBPB21E7.04c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1F8.01	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1683.08	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC1235.14	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC359.02	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC1235.18	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC359.06	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1F7.08	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC1739.08c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC1739.08c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC186.05c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4H10.09	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC794.01c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBPB2B2.12c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4H10.10	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBPB2B2.12c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBP4H10.10	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1A6.04c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1A6.04c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC11D3.19	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC56F2.06	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC56F2.06	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC4H3.03c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC4H3.03c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC27D7.11c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC17A2.11	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC17A2.11	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBPB2B2.10c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1F8.03c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBPB21E7.11	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAPB8E5.05	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1348.14c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC11H11.04	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1683.09c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC4F6.09	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBPB2B2.10c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC1235.17	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBPB21E7.04c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC1235.17	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC1683.08	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC1235.14	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC359.02	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC1235.18	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC359.06	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1F7.08	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC1F8.01	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC548.07c	(Fig. S3)
PMID:38899862	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPCC548.07c	(Fig. S3)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. S4)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. S4)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. S4)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. S4)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. S4)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. S4)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. S4)
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	(Fig. S4)
PMID:38899862	FYPO:0002141	normal cell population growth at low temperature	(i) snf22∆ suppressed the cold-sensitive slow growth phenotype associated with seb1-G476S (Fig. 2A)
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	Deletion of the Nudix-family pyrophosphatase Aps1 or the Duf89 phosphatase-pyro­ phosphatase also results in the derepression of Pho1 expression (15, 30), an effect that was suppressed by snf22∆ (Fig. 2B).
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	Deletion of the Nudix-family pyrophosphatase Aps1 or the Duf89 phosphatase-pyro­ phosphatase also results in the derepression of Pho1 expression (15, 30), an effect that was suppressed by snf22∆ (Fig. 2B).
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	Here we constructed a snf22∆ rad24∆ double mutant (Fig. 2A) and found that loss of Snf22 abolished Pho1 derepression by rad24∆ (Fig. 2B).
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	Moreover, snf22-(D996A-E997A) reversed the derepression of Pho1 accompanying deletion of erh1 (Fig. 3B), which results from precocious 3′-processing/termination of prt lncRNA synthesis (38).
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	Moreover, snf22-(D996A-E997A) reversed the derepression of Pho1 accompanying deletion of erh1 (Fig. 3B), which results from precocious 3′-processing/termination of prt lncRNA synthesis (38).
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	Pho1 expression is therefore derepressed in seb1-G476S cells (Fig. 2B). , 3B
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	Production of full-length interfering prt lncRNA is inhibited in rad24∆ cells (31) concomitant with increased production of pho1 mRNA and greatly increased Pho1 activity (as in Fig. 2B).
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	SST-612 in Fig. 6A
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [has_severity] low	SST-612 in Fig. 6B
PMID:38899862	FYPO:0001355	decreased vegetative cell population growth	The STF7 (H686Y) pyrophosphatase domain mutation of asp1 elicits a severe growth defect at all temperatures (Fig. 1A).
PMID:38899862	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	The derepression of Pho1 seen in asp1-H397A cells was erased by snf22∆, to the extent that acid phosphatase activity in snf22∆ asp1-H397A cells was the same as that of the wild-type control (Fig. 2B).
PMID:38899862	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	The derepression of Pho1 seen in asp1-H397A cells was erased by snf22∆, to the extent that acid phosphatase activity in snf22∆ asp1-H397A cells was the same as that of the wild-type control (Fig. 2B).
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	The snf22∆ asp1-H397A double mutant grew well on YES agar at all temperatures from 20°C to 37°C (Fig. 2A)
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	and (ii) snf22∆ suppressed the derepression of Pho1 by seb1-G476S (Fig. 2B).
PMID:38899862	FYPO:0001357	normal vegetative cell population growth	snf22∆ cells grew similarly to wild-type cells on YES agar at all temperatures tested (Fig. 2A).
PMID:38899862	FYPO:0001045	decreased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	snf22∆ elicited a sevenfold hyper-repression of Pho1 expression in phosphate-replete cells compared to the wild-type control (Fig. 2B, P value <0.0001).
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 2)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 2)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 2)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 2)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 2)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 2)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c [has_severity] medium	(Fig. 3)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 3)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 3)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c [has_severity] high	(Fig. 4)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c [has_severity] low	(Fig. 4)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c [has_severity] low	(Fig. 4)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c [has_severity] low	(Fig. 4)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c [has_severity] medium	(Fig. 4)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c [has_severity] medium	(Fig. 4)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [has_severity] high [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 4)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 4)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 5)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c [has_severity] high	(Fig. 5)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c [has_severity] high	(Fig. 5)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c [has_severity] high	(Fig. 5)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c [has_severity] high	(Fig. 5)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c [has_severity] high	(Fig. 5)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 5)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 5)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 5)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 5)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 5)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 5)
PMID:38913087	FYPO:0001571	increased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c [has_severity] medium	(Fig. 5)
PMID:38913087	FYPO:0001571	increased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c [has_severity] medium	(Fig. 5)
PMID:38913087	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c [has_severity] medium	(Fig. 5)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 5)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 5)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 5)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 5)
PMID:38913087	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 5)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 5)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 5)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC17A2.13c	(Fig. 5)
PMID:38913087	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC1D7.05 [assayed_protein] PomBase:SPAC8E11.02c	(Fig. 5)
PMID:38913087	FYPO:0007962	decreased mating efficiency during nitrogen starvation [has_severity] medium	(Fig. 6C)
PMID:38913087	FYPO:0007950	increased mating efficency during nitrogen stress [has_severity] high	(Fig. 6D)
PMID:38913087	FYPO:0007962	decreased mating efficiency during nitrogen starvation [has_severity] medium	(Fig. 6F)
PMID:38913087	FYPO:0000280	sterile	(Fig. 6F)
PMID:38913087	FYPO:0007950	increased mating efficency during nitrogen stress [has_severity] high	(Fig. 6G)
PMID:38913087	FYPO:0000708	decreased mating efficiency [has_severity] high	(Fig. 6G)
PMID:38913087	FYPO:0001147	normal mating efficiency	(Fig. 6G)
PMID:38913087	FYPO:0000280	sterile	(Fig. 6H)
PMID:38913087	FYPO:0000280	sterile	(Fig. 6I)
PMID:38913087	FYPO:0000280	sterile	(Fig. 6J)
PMID:38913087	FYPO:0007962	decreased mating efficiency during nitrogen starvation [has_severity] medium	(Table 2)
PMID:38913087	FYPO:0007962	decreased mating efficiency during nitrogen starvation [has_severity] low	(Table 2)
PMID:38913087	FYPO:0007962	decreased mating efficiency during nitrogen starvation [has_severity] medium	(Table 2)
PMID:38913087	FYPO:0007963	normal mating efficiency during nitrogen stress	(Table 2)
PMID:38913087	FYPO:0007950	increased mating efficency during nitrogen stress [has_severity] low	(Table 2)
PMID:38913087	FYPO:0007962	decreased mating efficiency during nitrogen starvation [has_severity] high	(Table 2)
PMID:38917328	FYPO:0007255	decreased replication fork processing	(Fig. 1B and C)
PMID:38917328	FYPO:0006320	normal replication slippage during replication fork processing	(Fig. 2B)
PMID:38917328	FYPO:0003589	decreased replication slippage during replication fork processing [has_severity] medium	(Fig. 2B)
PMID:38917328	FYPO:0003589	decreased replication slippage during replication fork processing [has_severity] medium	(Fig. 2B)
PMID:38917328	FYPO:0006320	normal replication slippage during replication fork processing	(Fig. 2B)
PMID:38917328	FYPO:0006319	normal extent of DNA resection during replication fork processing	(Fig. 2D)
PMID:38917328	FYPO:0006319	normal extent of DNA resection during replication fork processing	(Fig. 2D)
PMID:38917328	FYPO:0006319	normal extent of DNA resection during replication fork processing	(Fig. 2D)
PMID:38917328	FYPO:0006319	normal extent of DNA resection during replication fork processing	(Fig. 2D)
PMID:38917328	FYPO:0000344	enlarged nucleus during vegetative growth [has_severity] medium	(Fig. 3A and B)
PMID:38917328	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC19G7.09 [has_severity] medium	(Fig. 3A)
PMID:38917328	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC19G7.09 [has_severity] medium	(Fig. 3A)
PMID:38917328	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC19G7.09 [has_severity] low	(Fig. 3A)
PMID:38917328	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC19G7.09 [has_severity] high	(Fig. 3A)
PMID:38917328	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC19G7.09 [has_severity] high	(Fig. 3A)
PMID:38917328	FYPO:0002568	abolished protein localization to nuclear periphery [assayed_protein] PomBase:SPBC19G7.09 [has_penetrance] high	(Fig. 3B)
PMID:38917328	FYPO:0002568	abolished protein localization to nuclear periphery [assayed_protein] PomBase:SPBC19G7.09 [has_penetrance] high	(Fig. 3B)
PMID:38917328	FYPO:0005630	decreased cellular HMW SUMO conjugate level [has_severity] high [assayed_protein] PomBase:SPBC365.06	(Fig. 3C)
PMID:38917328	FYPO:0005630	decreased cellular HMW SUMO conjugate level [has_severity] high [assayed_protein] PomBase:SPBC365.06	(Fig. 3C)
PMID:38917328	FYPO:0002339	decreased protein localization to nuclear periphery [assayed_protein] PomBase:SPAC1786.03 [has_severity] low	(Fig. 4C)
PMID:38917328	FYPO:0003589	decreased replication slippage during replication fork processing [has_severity] medium	(Fig. 5A)
PMID:38917328	FYPO:0006320	normal replication slippage during replication fork processing	(Fig. 5C)
PMID:38917328	FYPO:0006320	normal replication slippage during replication fork processing	(Fig. 5C)
PMID:38917328	FYPO:0006320	normal replication slippage during replication fork processing	(Fig. 5C)
PMID:38917328	FYPO:0007537	increased replication slippage during replication fork processing [has_severity] medium	(Fig. 5D and E)
PMID:38917328	FYPO:0006320	normal replication slippage during replication fork processing [has_penetrance] 100	(Fig. 5D)
PMID:38917328	FYPO:0006320	normal replication slippage during replication fork processing [has_penetrance] 100	(Fig. 5D)
PMID:38917328	FYPO:0003589	decreased replication slippage during replication fork processing [has_severity] medium	(Fig. 5E)
PMID:38917328	FYPO:0003589	decreased replication slippage during replication fork processing [has_severity] high	(Fig. 6A and D)
PMID:38917328	FYPO:0003589	decreased replication slippage during replication fork processing [has_severity] high	(Fig. 6A)
PMID:38917328	FYPO:0003589	decreased replication slippage during replication fork processing [has_severity] high	(Fig. 6D)
PMID:38917328	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. S1A)
PMID:38917328	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. S1A)
PMID:38917328	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. S1A)
PMID:38917328	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. S1A)
PMID:38917328	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. S1A)
PMID:38917328	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. S1A)
PMID:38917328	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. S1A)
PMID:38917328	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. S1A)
PMID:38917328	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. S1A)
PMID:38917328	FYPO:0000095	sensitive to bleomycin [has_severity] medium	(Fig. S1A)
PMID:38917328	FYPO:0004003	delayed onset of replication fork processing	(Fig. S1B)
PMID:38917328	FYPO:0004003	delayed onset of replication fork processing	(Fig. S1B)
PMID:38917328	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. S2A)
PMID:38917328	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. S2A)
PMID:38917328	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. S2A)
PMID:38917328	FYPO:0000095	sensitive to bleomycin [has_severity] high	(Fig. S2A)
PMID:38917328	FYPO:0005629	increased cellular HMW SUMO conjugate level [assayed_protein] PomBase:SPBC365.06 [has_severity] medium	(Fig. S6B)
PMID:38917328	FYPO:0004251	increased DNA resection during replication fork processing [has_severity] medium	(Fig. S6D)
PMID:38917328	GO:0016929	deSUMOylase activity [part_of] positive regulation of mitotic recombination-dependent replication fork processing [occurs_in] nucleoplasmic side of nuclear pore	The Ulp1 SUMO protease ensures an efficient initiation of restarted DNA synthesis. This mechanism requires the sequestration of Ulp1 at the NP which is coordinated by the Y complex and the nuclear basket nucleoporin Nup60
PMID:38917328	GO:0120292	positive regulation of mitotic recombination-dependent replication fork processing	The Ulp1 SUMO protease ensures an efficient initiation of restarted DNA synthesis. This mechanism requires the sequestration of Ulp1 at the NP which is coordinated by the Y complex and the nuclear basket nucleoporin Nup60
PMID:38917328	GO:0120292	positive regulation of mitotic recombination-dependent replication fork processing	The Ulp1 SUMO protease ensures an efficient initiation of restarted DNA synthesis. This mechanism requires the sequestration of Ulp1 at the NP which is coordinated by the Y complex and the nuclear basket nucleoporin Nup60
PMID:38917328	GO:0120292	positive regulation of mitotic recombination-dependent replication fork processing	Thus, Alm1 and Nup60 promote RDR in a preand post-anchoring manner, respectively.
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 10)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 10)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 10)
PMID:38940614	FYPO:0001575	abolished vegetative cell population growth	(Fig. 10)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 10)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 10)
PMID:38940614	FYPO:0001575	abolished vegetative cell population growth	(Fig. 10)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 10)
PMID:38940614	FYPO:0001575	abolished vegetative cell population growth	(Fig. 10)
PMID:38940614	FYPO:0001575	abolished vegetative cell population growth	(Fig. 10)
PMID:38940614	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 10)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 10)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 10)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 10)
PMID:38940614	FYPO:0008281	decreased cellular 1,5-IP8 level [has_severity] high	(Fig. 11)
PMID:38940614	FYPO:0008277	increased cellular 1,5-IP8 level [has_severity] low	(Fig. 11)
PMID:38940614	FYPO:0008279	increased cellular 1-IP7 level [has_severity] high	(Fig. 11)
PMID:38940614	FYPO:0008279	increased cellular 1-IP7 level [has_severity] high	(Fig. 11)
PMID:38940614	FYPO:0008279	increased cellular 1-IP7 level [has_severity] high	(Fig. 11)
PMID:38940614	FYPO:0008282	decreased cellular 5-IP7 level [has_severity] medium	(Fig. 11)
PMID:38940614	FYPO:0008285	normal cellular 5-IP7 level	(Fig. 11)
PMID:38940614	FYPO:0008278	increased cellular 5-IP7 level [has_severity] high	(Fig. 11)
PMID:38940614	FYPO:0008278	increased cellular 5-IP7 level [has_severity] high	(Fig. 11)
PMID:38940614	FYPO:0008278	increased cellular 5-IP7 level [has_severity] low	(Fig. 11)
PMID:38940614	FYPO:0008278	increased cellular 5-IP7 level [has_severity] low	(Fig. 11)
PMID:38940614	FYPO:0008279	increased cellular 1-IP7 level [has_severity] high	(Fig. 11)
PMID:38940614	FYPO:0008277	increased cellular 1,5-IP8 level [has_severity] low	(Fig. 11)
PMID:38940614	FYPO:0008277	increased cellular 1,5-IP8 level [has_severity] low	(Fig. 11)
PMID:38940614	FYPO:0008277	increased cellular 1,5-IP8 level [has_severity] high	(Fig. 11)
PMID:38940614	FYPO:0008277	increased cellular 1,5-IP8 level [has_severity] high	(Fig. 11)
PMID:38940614	FYPO:0008281	decreased cellular 1,5-IP8 level [has_severity] medium	(Fig. 11)
PMID:38940614	FYPO:0008283	decreased cellular 1-IP7 level [has_severity] high	(Fig. 11)
PMID:38940614	FYPO:0008283	decreased cellular 1-IP7 level [has_severity] high	(Fig. 11)
PMID:38940614	FYPO:0008283	decreased cellular 1-IP7 level [has_severity] medium	(Fig. 11)
PMID:38940614	FYPO:0008286	normal cellular 1-IP7 level	(Fig. 11)
PMID:38940614	FYPO:0008285	normal cellular 5-IP7 level	(Fig. 11)
PMID:38940614	FYPO:0008285	normal cellular 5-IP7 level	(Fig. 11)
PMID:38940614	FYPO:0008281	decreased cellular 1,5-IP8 level [has_severity] high	(Fig. 11)
PMID:38940614	FYPO:0008275	normal polyphosphatase activity [assayed_enzyme] PomBase:SPAC13G6.14	(Fig. 3A)
PMID:38940614	FYPO:0008275	normal polyphosphatase activity [assayed_enzyme] PomBase:SPAC13G6.14	(Fig. 3A)
PMID:38940614	FYPO:0008276	abolished polyphosphatase activity [assayed_enzyme] PomBase:SPAC13G6.14	(Fig. 4A)
PMID:38940614	GO:0052843	inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity	(Fig. 5A, 6A and 7)
PMID:38940614	GO:0052845	inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity	(Fig. 6B and 7)
PMID:38940614	GO:0052847	inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity	(Fig. 6C and 7)
PMID:38940614	GO:0052846	inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity	(Fig. 6C and 7)
PMID:38940614	FYPO:0005485	abolished inositol phosphate phosphatase activity [assayed_enzyme] PomBase:SPAC13G6.14	(Fig. 7)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 8A)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 8A)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 8A)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 8A)
PMID:38940614	FYPO:0005369	abolished cell population growth at low temperature	(Fig. 8A)
PMID:38940614	FYPO:0005369	abolished cell population growth at low temperature	(Fig. 8A)
PMID:38940614	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 8A)
PMID:38940614	FYPO:0003267	normal acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02	(Fig. 8B)
PMID:38940614	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] high	(Fig. 8B)
PMID:38940614	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] high	(Fig. 8B)
PMID:38940614	FYPO:0002243	increased acid phosphatase activity [assayed_enzyme] PomBase:SPBP4G3.02 [has_severity] medium	(Fig. 8B)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0000674	normal cell population growth at high temperature	(Fig. 9)
PMID:38940614	FYPO:0000674	normal cell population growth at high temperature	(Fig. 9)
PMID:38940614	FYPO:0000674	normal cell population growth at high temperature	(Fig. 9)
PMID:38940614	FYPO:0000674	normal cell population growth at high temperature	(Fig. 9)
PMID:38940614	FYPO:0000674	normal cell population growth at high temperature	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 9)
PMID:38940614	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 9)
PMID:38940614	FYPO:0005369	abolished cell population growth at low temperature	(Fig. 9)
PMID:38940614	FYPO:0005369	abolished cell population growth at low temperature	(Fig. 9)
PMID:38940614	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 9)
PMID:38940614	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001357	normal vegetative cell population growth	(Fig. 9)
PMID:38940614	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S1)
PMID:38940614	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S1)
PMID:38940614	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	(Fig. S1)
PMID:38940614	FYPO:0000080	decreased cell population growth at low temperature [has_severity] medium	(Fig. S1)
PMID:38940614	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S1)
PMID:38940614	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S1)
PMID:38971312	FYPO:0008378	decreased histone H2A phosphorylation during cellular response to camptothecin [has_severity] high	(Fig. 1A and B)
PMID:38971312	FYPO:0008378	decreased histone H2A phosphorylation during cellular response to camptothecin [has_severity] high	(Fig. 1A, B and C and Fig. 5)
PMID:38971312	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC24B10.07 [has_severity] high	(Fig. 1A,3A)
PMID:38971312	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC24B10.07 [has_severity] high	(Fig. 1A,3A)
PMID:38971312	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC24B10.07 [has_severity] high	(Fig. 1A,3A)
PMID:38971312	FYPO:0008378	decreased histone H2A phosphorylation during cellular response to camptothecin [has_severity] high	(Fig. 1B)
PMID:38971312	FYPO:0008378	decreased histone H2A phosphorylation during cellular response to camptothecin [has_severity] high	(Fig. 1B)
PMID:38971312	FYPO:0008378	decreased histone H2A phosphorylation during cellular response to camptothecin [has_severity] high	(Fig. 1B)
PMID:38971312	FYPO:0008378	decreased histone H2A phosphorylation during cellular response to camptothecin [has_severity] high	(Fig. 1B)
PMID:38971312	FYPO:0008378	decreased histone H2A phosphorylation during cellular response to camptothecin [has_severity] high	(Fig. 1B)
PMID:38971312	FYPO:0008438	decreased histone H2A phosphorylation during cellular response to methyl methanesulfonate [has_severity] high	(Fig. 1B)
PMID:38971312	FYPO:0008438	decreased histone H2A phosphorylation during cellular response to methyl methanesulfonate [has_severity] high	(Fig. 1B)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 1D)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 1D)
PMID:38971312	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 1E)
PMID:38971312	FYPO:0001357	normal vegetative cell population growth	(Fig. 1E)
PMID:38971312	FYPO:0001357	normal vegetative cell population growth	(Fig. 1E)
PMID:38971312	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1E)
PMID:38971312	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 1E)
PMID:38971312	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1E)
PMID:38971312	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1E)
PMID:38971312	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1E)
PMID:38971312	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1E)
PMID:38971312	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1E)
PMID:38971312	FYPO:0008379	decreased histone H2A phosphorylation during nitrogen starvation	(Fig. 2A)
PMID:38971312	FYPO:0008379	decreased histone H2A phosphorylation during nitrogen starvation	(Fig. 2A,B)
PMID:38971312	FYPO:0008379	decreased histone H2A phosphorylation during nitrogen starvation	(Fig. 2C)
PMID:38971312	FYPO:0008379	decreased histone H2A phosphorylation during nitrogen starvation	(Fig. 2C)
PMID:38971312	FYPO:0008379	decreased histone H2A phosphorylation during nitrogen starvation	(Fig. 2C)
PMID:38971312	FYPO:0005034	decreased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPCC24B10.07 [has_severity] high	(Fig. 3A)
PMID:38971312	FYPO:0005034	decreased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPCC24B10.07 [has_severity] high	(Fig. 3A)
PMID:38971312	FYPO:0005034	decreased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPCC24B10.07 [has_severity] high	(Fig. 3A)
PMID:38971312	FYPO:0005034	decreased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPCC24B10.07	(Fig. 3B)
PMID:38971312	FYPO:0005034	decreased protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPCC24B10.07	(Fig. 3C)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 4A)
PMID:38971312	MOD:00696	phosphorylated residue [decreased_in_presence_of] torin 1	(Fig. 4B)
PMID:38971312	MOD:00046	O-phospho-L-serine [decreased_in_presence_of] torin 1	(Fig. 4B)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5A)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5A)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5A)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5A)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5A)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5A)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5B)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5B)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5B)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5B)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5B)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5B)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5C)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5C)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5C)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5C)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5C)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5C)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5D)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5D)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5D)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5D)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5D)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5D)
PMID:38971312	FYPO:0008380	normal histone H2A phosphorylation during cellular response to camptothecin	(Fig. 5E)
PMID:38971312	FYPO:0008378	decreased histone H2A phosphorylation during cellular response to camptothecin [has_severity] high	(Fig. 5E)
PMID:38985524	FYPO:0002061	inviable vegetative cell population	(Figure 1B)
PMID:38985524	FYPO:0002061	inviable vegetative cell population	(Figure 1B)
PMID:38985524	FYPO:0002061	inviable vegetative cell population	(Figure 1B)
PMID:38985524	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC4H3.11c	Additionally, while GFP-Pcp1(PACT) localized at the SPB, GFP-Pcp1(PACT-I1151A) was diffuse throughout the cytosol and nucleus (Figure 6D)
PMID:38985524	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC4H3.11c	GFP-Ppc89(261-550) localized to SPBs marked by Sad1-mCherry
PMID:38985524	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC6G9.06c	Importantly, we also found that Pcp1-GFP could not localize to SPBs marked by Sad1-mCherry in cam1-E14 cells at the restrictive temperature (Figure 4E), suggest-ing that the PACT domain-Cam1 module directs SPB targeting.
PMID:38985524	FYPO:0001475	fragmented mitotic spindle pole body [has_penetrance] 28	In contrast, Ppc89 N+M expressing cells displayed multiple foci of endogenous Ppc89-GFP (Figure 1D).
PMID:38985524	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC6G9.06c	Like GFP-Pcp1 expressed from the weak nmt81 promoter, the GFP-PACT domain alone colocalized with Ppc89-mCherry (Figure 4B). Thus, Pcp1’s PACT domain is sufficient for SPB targeting.
PMID:38985524	FYPO:0002969	increased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC6G9.06c	Pcp1 accumulated in enlarged Ppc89-containing structures upon overproduction of FL Ppc89 (Figure 3).
PMID:38985524	FYPO:0006431	enlarged mitotic spindle pole body	Ppc89 and Ppc89 M+C expressing cells exhibited the enlarged SPB phenotype (Figure 1D), as observed previously for FL Ppc89 (Rosenberg et al., 2006).
PMID:38985524	FYPO:0006431	enlarged mitotic spindle pole body [has_penetrance] 26	Ppc89 and Ppc89 M+C expressing cells exhibited the enlarged SPB phenotype (Figure 1D), as observed previously for FL Ppc89 (Rosenberg et al., 2006).
PMID:38985524	FYPO:0002969	increased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC4H3.11c	Similarly, we would expect overexpressed GFP-M+C to bind endogenous Pcp89 at the SPB to form larger SPBs and this was also observed (Supplemental Figure S1B).
PMID:38985524	FYPO:0002969	increased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC244.01c	The Sid4 C-terminus interacts with the Ppc89 C-terminus (Rosenberg et al., 2006). Sid4- mCherry colocalized with endogenous Ppc89-GFP when FL or M+C were overexpressed, both forming enlarged SPBs (Figure 2). This is consistent with the idea that as additional Ppc89 C-termini becomes available at the SPB, more Sid4 can interact and localize there.
PMID:38985524	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC3A12.14	We found that mNG-Cam1 could not localize to the SPB marked by Sad1-mCherry in pcp1-14 cells at the restrictive temperature (Figure 4D).
PMID:38985524	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC244.01c	When untagged Ppc89 N+M was overproduced, Sid4 was lost from the SPBs of cells that formed multiple Ppc89 foci (Figure 2). This result is consistent with the idea that N+M acts as a dominant negative, outcompeting endogenous Ppc89 at SPBs and diluting the Sid4-mCherry signal to such an extent that it can no longer be detected.
PMID:38985524	FYPO:0000941	abolished protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC4H3.11c	but GFP-Ppc89(267-550-K299A) was diffuse in the cytoplasm and nucleus or present in foci that did not overlap with the SPB (Figure 6C).
PMID:38989013	FYPO:0002049	elongated multinucleate aseptate vegetative cell	(Figure 1E)
PMID:38989013	FYPO:0002002	multiseptate vegetative cell, septa grouped	(Figure 1H)
PMID:38989013	FYPO:0000118	multiseptate vegetative cell	(Figure 1H)
PMID:38989013	FYPO:0000082	decreased cell population growth at high temperature	A spot assay revealed that sid1-L2 had an intermediate restrictive temperature compared to sid1-125 and sid1-239 (Figure 1F).
PMID:38989013	FYPO:0000082	decreased cell population growth at high temperature	A spot assay showed that the cdc14-E2 allele was comparable in its temperature sensitivity to cdc14-118 (Figure 1C).
PMID:38989013	FYPO:0000082	decreased cell population growth at high temperature	A spot assay showed that the cdc14-E2 allele was comparable in its temperature sensitivity to cdc14-118 (Figure 1C).
PMID:38989013	FYPO:0000082	decreased cell population growth at high temperature	All temperature-sensitive alleles grew less than wild-type at 36°C with the cdc16-C1 allele showing the greatest temperature-sensitivity (Figure 1I).
PMID:38989013	FYPO:0000082	decreased cell population growth at high temperature	All temperature-sensitive alleles grew less than wild-type at 36°C with the cdc16-C1 allele showing the greatest temperature-sensitivity (Figure 1I).
PMID:38989013	FYPO:0000082	decreased cell population growth at high temperature	All temperature-sensitive alleles grew less than wild-type at 36°C with the cdc16-C1 allele showing the greatest temperature-sensitivity (Figure 1I).
PMID:38989013	FYPO:0001972	abnormal cell separation after cytokinesis resulting in septated cell	Nuclei and septa staining revealed predominantly a boomerang-shape phenotype that was often accompanied by cell lysis at septation (Figure 1E).
PMID:38989013	FYPO:0002002	multiseptate vegetative cell, septa grouped	The phenotypes of the three mutants were comparable. At 25 ̊C, the percent of septated cells was 17-20 with none showing more than one septa and at 36 ̊C, all cells arrested with multiple septa and one or two nuclei (Figure 1H).
PMID:38989013	FYPO:0000133	elongated multinucleate vegetative cell	While cdc14-118 cells showed the classic sin phenotype of multinucleation and cell elongation at the non-permissive temperature, cdc14-E2 cells arrested uniformly at a very late stage of septation and frequently lysed (Figure 1B).
PMID:38989013	FYPO:0003213	explosive cytokinetic cell separation resulting in vegetative cell lysis	While cdc14-118 cells showed the classic sin phenotype of multinucleation and cell elongation at the non-permissive temperature, cdc14-E2 cells arrested uniformly at a very late stage of septation and frequently lysed (Figure 1B).
PMID:39010328	FYPO:0006345	increased duration of protein phosphorylation during nitrogen starvation [assayed_protein] PomBase:SPCC4G3.08	(Fig. 1B)
PMID:39010328	FYPO:0002830	delayed onset of protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 1C)
PMID:39010328	FYPO:0002672	normal growth on rapamycin	(Fig. 2A)
PMID:39010328	FYPO:0002672	normal growth on rapamycin	(Fig. 2A)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 2A, 2B)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 2A, 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 2B)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39010328	FYPO:0000047	normal cell population growth	(Fig. 2B)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 2B)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2B)
PMID:39010328	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 2C)
PMID:39010328	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 2C)
PMID:39010328	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 2C)
PMID:39010328	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 2C)
PMID:39010328	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 2C)
PMID:39010328	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 2C)
PMID:39010328	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 2C)
PMID:39010328	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 2C)
PMID:39010328	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 2C)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 2D)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2D)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 2D)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 2D)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2D)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 2D)
PMID:39010328	FYPO:0004248	normal protein localization to vacuolar membrane [assayed_protein] PomBase:SPBC9B6.03	(Fig. 3C)
PMID:39010328	FYPO:0004250	abolished protein localization to vacuolar membrane [assayed_protein] PomBase:SPBC9B6.03	(Fig. 3C)
PMID:39010328	FYPO:0004250	abolished protein localization to vacuolar membrane [assayed_protein] PomBase:SPBC9B6.03	(Fig. 3D)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 4A)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 4A)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 4A)
PMID:39010328	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 4A)
PMID:39010328	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:39010328	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 4B)
PMID:39010328	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 4B)
PMID:39010328	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 4B)
PMID:39010328	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 4B)
PMID:39010328	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	(Fig. 4B)
PMID:39010328	GO:0005774	vacuolar membrane	As shown in Fig. 3B, GFP- Pib2 was detectable on vacuolar membranes, which can be visualized by the FM4-64 dye
PMID:39012625	FYPO:0007708	normal dynamic protein localization to cell tip [assayed_protein] PomBase:SPAC110.03	(Fig. 1)
PMID:39012625	FYPO:0008075	increased protein localization to cell cortex of cell tip during vegetative growth [assayed_protein] PomBase:SPBC1604.14c	(Fig. 4A)
PMID:39012625	FYPO:0000929	decreased protein localization to cell cortex during vegetative growth [assayed_protein] PomBase:SPBC1604.14c	(Fig. 4A)
PMID:39012625	FYPO:0005503	abnormally monopolar protein localization to cell tip [assayed_protein] PomBase:SPBC1604.14c	(Fig. 4A)
PMID:39012625	FYPO:0005503	abnormally monopolar protein localization to cell tip [assayed_protein] PomBase:SPAC16E8.09 [has_penetrance] high	(Fig. 5A)
PMID:39012625	FYPO:0007285	abnormal dynamic protein localization to cell tip [assayed_protein] PomBase:SPAC110.03	(Fig. 7A and B)
PMID:39012625	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_protein] PomBase:SPAC16E8.09	(Fig. 7C and D)
PMID:39012625	FYPO:0007285	abnormal dynamic protein localization to cell tip [assayed_protein] PomBase:SPBC1604.14c	(Fig. 7G)
PMID:39012625	FYPO:0000422	decreased endocytosis during vegetative growth	(Fig. 9)
PMID:39012625	FYPO:0004730	protein mislocalized to lateral cell cortex [assayed_protein] PomBase:SPAC110.03 [has_penetrance] 40	(Fig. S1A and B)
PMID:39012625	FYPO:0004730	protein mislocalized to lateral cell cortex [assayed_protein] PomBase:SPAC24H6.09 [has_penetrance] 20	(Fig. S1C and D)
PMID:39012625	GO:0045807	positive regulation of endocytosis	Interestingly, we also find that Pak1 is required for normal endocytic patch dynamics. Fig. 9
PMID:39012625	FYPO:0005503	abnormally monopolar protein localization to cell tip [assayed_protein] PomBase:SPAC16E8.09 [has_penetrance] medium	The pak1-ts cells are characteristically monopolar; however, we unexpectedly found that around 40% of these cells treated with CK-666 showed bipolar localization of Scd1-mNG (Fig. 5 A, asterisks).
PMID:39012625	GO:0061361	positive regulation of maintenance of bipolar cell polarity regulating cell shape	When the branched actin nucleator Arp2/3 complex is inhibited, Pak1 stabilizes at a cell end, preventing localization of the GEF and Scd1, and disrupting the positive and negative feedback loops needed for periodic Cdc42 activity at that end.
PMID:39016088	FYPO:0000964	normal growth on thiabendazole	(Fig. 2) (comment: CHECK TBZ sensitivity testing for wild-type, 9A, and 9D)
PMID:39016088	FYPO:0000964	normal growth on thiabendazole	(Fig. 2) (comment: CHeCK TBZ sensitivity testing for wild-type, 9A, and 9D)
PMID:39016088	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] medium [has_severity] medium	(comment: CHECK The defect was observed in rec12-deletion rec8-2A mutant background) Fig 3C.
PMID:39016088	FYPO:0008202	equational sister chromatid separation at meiosis I [has_penetrance] low [has_severity] low	(comment: CHECK The defect was observed in the rec12-deletion rec8-2A mutation background. The defect of fta2-9D was less than that of fta2-9A) Fig 3C.
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	(Fig. 1D and E)
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	(Fig. 1D and E)
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] low	(Fig. 1D and E)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC428.08c [has_severity] medium	(Fig. 1F, Fig. S1G and Fig. 2C)
PMID:39094565	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPBC428.08c	(Fig. 2D)
PMID:39094565	FYPO:0008326	increased histone H3-K9 trimethylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPBC428.08c	(Fig. 2E)
PMID:39094565	FYPO:0004540	increased chromatin silencing	(Fig. 3)
PMID:39094565	FYPO:0008327	increased histone H3-K9 trimethylation at heterochromatin island during vegetative growth	(Fig. 3, Fig. S3)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC17G9.13c	(Fig. 3G)
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] high	(Fig. 4D and E)
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] low	(Fig. 4D and E)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC428.08c [has_severity] high	(Fig. 4G)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPBC428.08c	(Fig. 5A)
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	(Fig. 5B, Fig. S6C)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC428.08c [has_severity] low	(Fig. 5F)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC428.08c [has_severity] medium	(Fig. 7C)
PMID:39094565	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPBC428.08c	(Fig. S1B)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC428.08c	(Fig. S1C)
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] low	(Fig. S1E and F)
PMID:39094565	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC428.08c	(Fig. S1G)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC428.08c [has_severity] medium	(Fig. S1G)
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] high	(Fig. S1I and J)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC428.08c [has_severity] low	(Fig. S1K)
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] low	(Fig. S2B)
PMID:39094565	FYPO:0006268	increased histone H3-K9 dimethylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPBC428.08c	(Fig. S2C)
PMID:39094565	FYPO:0008326	increased histone H3-K9 trimethylation at protein coding gene during vegetative growth [assayed_region] PomBase:SPBC428.08c	(Fig. S2D)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1488	(Fig. S2F)
PMID:39094565	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.606	(Fig. S2F)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC1711.02	(Fig. S2F)
PMID:39094565	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC1F8.05	(Fig. S2F)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC10F6.12c	(Fig. S2F)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC513.04	(Fig. S2F)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC1494.11c	(Fig. S2F)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC23G7.10c	(Fig. S2F)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC11H11.04	(Fig. S2F)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC25B2.02c	(Fig. S2F)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC23G7.13c	(Fig. S2F)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAPB8E5.05	(Fig. S2F)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC513.03	(Fig. S2F)
PMID:39094565	FYPO:0008327	increased histone H3-K9 trimethylation at heterochromatin island during vegetative growth	(Fig. S4)
PMID:39094565	FYPO:0004540	increased chromatin silencing	(Fig. S4)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC428.08c [has_severity] high	(Fig. S6A)
PMID:39094565	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC428.08c [has_severity] medium	(Fig. S6A)
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] high	(Fig. S6B)
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	(Fig. S6B)
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] medium	(Fig. S6C)
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] low	(Fig. S6F)
PMID:39094565	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] high	(Fig. S7B)
PMID:39094565	FYPO:0001458	decreased histone H3-K14 acetylation during vegetative growth [has_severity] low	(Fig. S7D)
PMID:39094565	FYPO:0001458	decreased histone H3-K14 acetylation during vegetative growth [has_severity] high	(Fig. S7D)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. 1C)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. 1C)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. 1C)
PMID:39094570	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1C)
PMID:39094570	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1C)
PMID:39094570	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1C)
PMID:39094570	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1C)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. 1C-D)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. 1F)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. 1F)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. 1F)
PMID:39094570	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 1F)
PMID:39094570	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1F)
PMID:39094570	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1F)
PMID:39094570	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1F)
PMID:39094570	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1F)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. 1F)
PMID:39094570	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. 1F)
PMID:39094570	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1F)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. 1F)
PMID:39094570	FYPO:0007158	decreased histone H3 binding [has_severity] high	(Fig. 4B)
PMID:39094570	FYPO:0007158	decreased histone H3 binding [has_severity] high	(Fig. 4B)
PMID:39094570	FYPO:0007159	decreased histone H4 binding [has_severity] high	(Fig. 4B)
PMID:39094570	FYPO:0007158	decreased histone H3 binding [has_severity] high	(Fig. 4B)
PMID:39094570	FYPO:0007159	decreased histone H4 binding [has_severity] high	(Fig. 4B)
PMID:39094570	FYPO:0007159	decreased histone H4 binding [has_severity] high	(Fig. 4B)
PMID:39094570	FYPO:0007159	decreased histone H4 binding [has_severity] high	(Fig. 4B)
PMID:39094570	FYPO:0007158	decreased histone H3 binding [has_severity] high	(Fig. 4B)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. 4C)
PMID:39094570	FYPO:0000963	normal growth on hydroxyurea	(Fig. 4C)
PMID:39094570	FYPO:0000963	normal growth on hydroxyurea	(Fig. 4C)
PMID:39094570	FYPO:0000963	normal growth on hydroxyurea	(Fig. 4C)
PMID:39094570	FYPO:0000963	normal growth on hydroxyurea	(Fig. 4C)
PMID:39094570	FYPO:0000963	normal growth on hydroxyurea	(Fig. 4C)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. 4C)
PMID:39094570	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] low	(Fig. 4C, Fig. S4G)
PMID:39094570	FYPO:0007478	decreased epigenetic heterochromatin inheritance [has_severity] medium	(Fig. 4C, Fig. S4G)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. 4C, Fig. S4G)
PMID:39094570	FYPO:0004745	abolished histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 4F)
PMID:39094570	FYPO:0004745	abolished histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 4F)
PMID:39094570	FYPO:0000888	decreased histone H3-K9 dimethylation at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 4F)
PMID:39094570	FYPO:0004745	abolished histone H3-K9 dimethylation at centromere outer repeat during vegetative growth	(Fig. 4F)
PMID:39094570	FYPO:0007472	abnormal histone exchange	(Fig. 5J)
PMID:39094570	FYPO:0007472	abnormal histone exchange	(Fig. 5J)
PMID:39094570	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. 6C)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. 6C)
PMID:39094570	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. 6C)
PMID:39094570	FYPO:0008454	decreased chromatin silencing at ectopic tethering site	(Fig. 6F)
PMID:39094570	FYPO:0008454	decreased chromatin silencing at ectopic tethering site	(Fig. 6F)
PMID:39094570	FYPO:0007598	abolished chromatin silencing at ectopic tethering site	(Fig. 6F)
PMID:39094570	FYPO:0007599	increased chromatin silencing at ectopic tethering site	(Fig. 6F)
PMID:39094570	FYPO:0008454	decreased chromatin silencing at ectopic tethering site	(Fig. 6F)
PMID:39094570	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC3H5.06c [assayed_protein] PomBase:SPBC609.05	(Fig. 6G)
PMID:39094570	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC3H5.06c [assayed_protein] PomBase:SPBP8B7.19	(Fig. 6G)
PMID:39094570	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC3H5.06c [assayed_protein] PomBase:SPBC609.05	(Fig. 6G)
PMID:39094570	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC3H5.06c [assayed_protein] PomBase:SPBP8B7.19	(Fig. 6G)
PMID:39094570	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC3H5.06c [assayed_protein] PomBase:SPBC609.05	(Fig. 6G)
PMID:39094570	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC3H5.06c [assayed_protein] PomBase:SPBP8B7.19	(Fig. 6G)
PMID:39094570	FYPO:0007158	decreased histone H3 binding	(Fig. 6H)
PMID:39094570	FYPO:0008273	normal histone H4 binding	(Fig. 6H)
PMID:39094570	FYPO:0008272	normal histone H3 binding	(Fig. 6H)
PMID:39094570	FYPO:0008272	normal histone H3 binding	(Fig. 6H)
PMID:39094570	FYPO:0008273	normal histone H4 binding	(Fig. 6H)
PMID:39094570	FYPO:0007159	decreased histone H4 binding	(Fig. 6H)
PMID:39094570	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC3H5.06c [assayed_protein] PomBase:SPAPB1E7.02c	(Fig. 6I)
PMID:39094570	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC3H5.06c [assayed_protein] PomBase:SPAPB1E7.02c	(Fig. 6I)
PMID:39094570	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC3H5.06c [assayed_protein] PomBase:SPAPB1E7.02c	(Fig. 6I)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. S1B)
PMID:39094570	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. S1B)
PMID:39094570	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. S1B)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. S1B)
PMID:39094570	FYPO:0007477	abnormal epigenetic heterochromatin inheritance	(Fig. S1B-D)
PMID:39094570	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. S1F)
PMID:39094570	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. S1F)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. S1F)
PMID:39094570	FYPO:0007376	abolished epigenetic heterochromatin inheritance	(Fig. S1F)
PMID:39094570	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. S1F)
PMID:39094570	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. S1F)
PMID:39094570	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. S1I)
PMID:39094570	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. S1I)
PMID:39094570	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. S1I)
PMID:39094570	FYPO:0000963	normal growth on hydroxyurea	(Fig. S1I)
PMID:39094570	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. S1I)
PMID:39094570	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. S1I)
PMID:39094570	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. S1I)
PMID:39094570	FYPO:0007479	normal epigenetic heterochromatin inheritance	(Fig. S1I)
PMID:39094570	GO:0000510	H3-H4 histone complex chaperone activity [part_of] DNA replication-dependent chromatin assembly	Mrc1/CLASPIN, as a histone H3-H4 tetramer chaperone required for heterochro- matin maintenance and efficient recycling of parental histones during DNA replication.
PMID:39096900	GO:0120262	negative regulation of heterochromatin organization	(Fig. 1)
PMID:39096900	GO:0120262	negative regulation of heterochromatin organization	(Fig. 1)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1C)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 1C)
PMID:39096900	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 1C)
PMID:39096900	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette [has_penetrance] 97.89	(Fig. 1C, 1D)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low [has_penetrance] 30.39	(Fig. 1C, 1D)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 1E, 1F)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 1E, 1F)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 1E, 1F)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 1E, 1F)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 1E, 1F)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 1E, 1F)
PMID:39096900	FYPO:0005154	decreased protein localization to heterochromatin at mat2P silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] medium	(Fig. 1G)
PMID:39096900	FYPO:0005154	decreased protein localization to heterochromatin at mat2P silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 1G)
PMID:39096900	FYPO:0005154	decreased protein localization to heterochromatin at mat2P silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] high	(Fig. 1G)
PMID:39096900	FYPO:0005154	decreased protein localization to heterochromatin at mat2P silent mating-type cassette [assayed_protein] PomBase:SPAC664.01c [has_severity] low	(Fig. 1G)
PMID:39096900	FYPO:0008327	increased histone H3-K9 trimethylation at heterochromatin island during vegetative growth	(Fig. 2A-C)
PMID:39096900	FYPO:0004749	increased spatial extent of subtelomeric heterochromatin assembly	(Fig. 2D)
PMID:39096900	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC1620.14c	(Fig. 3A, 3C)
PMID:39096900	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC1250.01	(Fig. 3B, 3D)
PMID:39096900	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC1620.14c	(Fig. 3C)
PMID:39096900	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC1620.14c	(Fig. 3C)
PMID:39096900	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC1250.01	(Fig. 3D)
PMID:39096900	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC1250.01	(Fig. 3D)
PMID:39096900	FYPO:0008416	increased histone exchange at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 3E)
PMID:39096900	FYPO:0008416	increased histone exchange at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 3E)
PMID:39096900	FYPO:0008416	increased histone exchange at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 3E)
PMID:39096900	FYPO:0008416	increased histone exchange at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 3E)
PMID:39096900	FYPO:0008416	increased histone exchange at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 3E)
PMID:39096900	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC17G8.13c	(Fig. 4B)
PMID:39096900	FYPO:0007633	increased histone H3-K14 acetylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 4C, 4H)
PMID:39096900	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC1620.14c	(Fig. 4D)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 4E, 4G)
PMID:39096900	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. 4F)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 4F)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 4F)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. 4G)
PMID:39096900	FYPO:0007633	increased histone H3-K14 acetylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 4H)
PMID:39096900	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC1620.14c	(Fig. 5B)
PMID:39096900	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPCC1620.14c	(Fig. 5B)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high [has_penetrance] 96.57	(Fig. 5C, 5F, 5H)
PMID:39096900	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette [has_penetrance] 98.90	(Fig. 5C, 5F, 5H)
PMID:39096900	FYPO:0005844	abolished histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth	(Fig. 5D, 5G)
PMID:39096900	FYPO:0005844	abolished histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth	(Fig. 5D, 5G)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low [has_penetrance] 5.17	(Fig. 5F, 5H)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] 5.18 [has_severity] low	(Fig. 5F, 5H)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_penetrance] 5.18 [has_severity] low	(Fig. 5F, 5H)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low [has_penetrance] 5.17	(Fig. 5F, 5H)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 5G)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 5G)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 5G)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] low	(Fig. 5G)
PMID:39096900	FYPO:0007002	normal histone exchange at silent mating-type cassette	(Fig. 5I)
PMID:39096900	FYPO:0007002	normal histone exchange at silent mating-type cassette	(Fig. 5I)
PMID:39096900	FYPO:0007002	normal histone exchange at silent mating-type cassette	(Fig. 5I)
PMID:39096900	FYPO:0007002	normal histone exchange at silent mating-type cassette	(Fig. 5I)
PMID:39096900	FYPO:0008416	increased histone exchange at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 5I)
PMID:39096900	FYPO:0008416	increased histone exchange at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. 5I)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. S1A)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. S1A)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. S1A)
PMID:39096900	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. S1B)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1B)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1B)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1B)
PMID:39096900	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. S1B)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1D)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. S1D)
PMID:39096900	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. S1D)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. S1E)
PMID:39096900	FYPO:0008364	normal histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth	(Fig. S1E)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. S1E)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] medium	(Fig. S1E)
PMID:39096900	FYPO:0005845	decreased histone H3-K9 trimethylation at silent mating-type cassette during vegetative growth [has_severity] high	(Fig. S1E)
PMID:39096900	FYPO:0008419	increased protein localization to heterochromatin island [assayed_protein] PomBase:SPAC664.01c	(Fig. S2)
PMID:39096900	FYPO:0004577	decreased histone H3-K9 trimethylation at subtelomeric heterochromatin during vegetative growth [has_severity] high	(Fig. S4B)
PMID:39096900	FYPO:0000883	decreased histone H3-K9 trimethylation at centromere during vegetative growth [has_severity] medium	(Fig. S5A)
PMID:39096900	FYPO:0004577	decreased histone H3-K9 trimethylation at subtelomeric heterochromatin during vegetative growth [has_severity] high	(Fig. S5B)
PMID:39096900	FYPO:0004577	decreased histone H3-K9 trimethylation at subtelomeric heterochromatin during vegetative growth [has_severity] high	(Fig. S5B)
PMID:39096900	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. S5E)
PMID:39096900	FYPO:0007336	abolished chromatin silencing at silent mating-type cassette	(Fig. S5E)
PMID:39096900	FYPO:0008417	increased epigenetic heterochromatin inheritance [has_severity] low	(Fig. S6)
PMID:39096900	FYPO:0008417	increased epigenetic heterochromatin inheritance [has_severity] high	(Fig. S6)
PMID:39096900	GO:0120262	negative regulation of heterochromatin organization	Deletion of rsc1 promotes epigenetic heterochromatin inheritance. (Fig. S6)
PMID:39096900	GO:0120262	negative regulation of heterochromatin organization	Deletion of snf22 promotes epigenetic heterochromatin inheritance. (Fig. S6)
PMID:39096900	FYPO:0007376	abolished epigenetic heterochromatin inheritance	Expression of Snf5-CDx2 fusion protein abolished epigenetic inheritance of ectopic heterochromatin. (Fig. 6C, 6D)
PMID:39096900	GO:0120262	negative regulation of heterochromatin organization	Targeting Mst2 to heterochromatin by expressing chromodomain-fused Mst2 (Mst2-CDx2) resulted in the loss of heterochromatin and gene silencing. (Fig. 4)
PMID:39096900	GO:0120262	negative regulation of heterochromatin organization	Targeting SWI/SNF to heterochromatin by expressing chromodomain-fused Snf5 (Snf5-CDx2) resulted in the loss of heterochromatin and gene silencing. (Fig. 5)
PMID:39096900	GO:0120262	negative regulation of heterochromatin organization	Targeting SWI/SNF to heterochromatin by expressing chromodomain-fused Snf59 (Snf59-CDx2) resulted in the loss of heterochromatin and gene silencing. (Fig. 5)
PMID:39105351	FYPO:0007500	abolished macroautophagy during sulfur starvation	(Figure 2a). However, in ΔSPCC417.09c cells, sulfur depletion did not induce the cleavage of GFP-Atg8, indicating that autophagy was not induced.
PMID:39105351	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC417.10	(Figure 3a). However, dal51+ is an adjacent gene to sdr1+ (Figure S1). Therefore, the increased expression of dal51+ in Δsdr1 cells was potentially due to the loss of the regulatory sequence of dal51+ expression rather than the deletion of the sdr1+.
PMID:39105351	FYPO:0007085	increased RNA level during cellular response to sulfur starvation [assayed_transcript] PomBase:SPAC19D5.01	Additionally, we confirmed gene expressions that showed significant differences due to the deletion of sdr1+ through a real-time polymerase chain reaction (PCR) assay (Figure 3a).
PMID:39105351	FYPO:0007085	increased RNA level during cellular response to sulfur starvation [assayed_transcript] PomBase:SPBC2F12.09c	Additionally, we confirmed gene expressions that showed significant differences due to the deletion of sdr1+ through a real-time polymerase chain reaction (PCR) assay (Figure 3a).
PMID:39105351	FYPO:0007085	increased RNA level during cellular response to sulfur starvation [assayed_transcript] PomBase:SPBC1289.14	Additionally, we confirmed gene expressions that showed significant differences due to the deletion of sdr1+ through a real-time polymerase chain reaction (PCR) assay (Figure 3a).
PMID:39105351	FYPO:0007085	increased RNA level during cellular response to sulfur starvation [assayed_transcript] PomBase:SPBC839.06	Additionally, we confirmed gene expressions that showed significant differences due to the deletion of sdr1+ through a real-time polymerase chain reaction (PCR) assay (Figure 3a).
PMID:39105351	FYPO:0007084	decreased RNA level during cellular response to sulfur starvation [assayed_transcript] PomBase:SPBC8E4.12c	Additionally, we confirmed gene expressions that showed significant differences due to the deletion of sdr1+ through a real-time polymerase chain reaction (PCR) assay (Figure 3a).
PMID:39105351	FYPO:0008320	abnormal cell morphology during sulphur deprivation	Although the morphological abnormalities of Δsdr1 cells under sulfur depletion were rectified by overexpressing sdr1+, those of Δecls cells were not (Figure 5).
PMID:39105351	FYPO:0008318	normal RNA level during sulfur starvation [assayed_transcript] PomBase:SPCC63.08c	Contrary to our prediction, the presence or absence of sdr1+ did not have significant effect on atg1+ and atg20+ induction by sulfur starvation.
PMID:39105351	FYPO:0008318	normal RNA level during sulfur starvation [assayed_transcript] PomBase:SPCC16A11.08	Contrary to our prediction, the presence or absence of sdr1+ did not have significant effect on atg1+ and atg20+ induction by sulfur starvation.
PMID:39105351	FYPO:0007085	increased RNA level during cellular response to sulfur starvation [assayed_transcript] PomBase:SPCC417.10	However, dal51+ is an adjacent gene to sdr1+ (Figure S1). Therefore, the increased expression of dal51+ in Δsdr1 cells was potentially due to the loss of the regulatory sequence of dal51+ expression rather than the deletion of the sdr1+.
PMID:39105351	FYPO:0008321	abolished sporulation during nitrogen starvation	In contrast, in Δsdr1 diploid cells, almost no sporulation occurred under nitrogen or sulfur starvation, and the sporulation rate during phosphate starvation was also significantly less.
PMID:39105351	FYPO:0007087	abolished sporulation during sulfur starvation	In contrast, in Δsdr1 diploid cells, almost no sporulation occurred under nitrogen or sulfur starvation, and the sporulation rate during phosphate starvation was also significantly less.
PMID:39105351	FYPO:0008317	loss of viability in stationary phase upon sulfur starvation [assayed_transcript] PomBase:SPBC8E4.12c	In this regard, we also confirmed that the sdr1+ deletion mutant exhibited a shorter CLS than the wild-type during the stationary phase in our assay system (Figure 6).
PMID:39105351	FYPO:0008319	normal macroautophagy during sulfur starvation	In Δfal1 cells, sulfur depletion induced the cleavage of GFP-Atg8, resulting in free-GFP, which confirms the occurrence of autophagy (Figure 2a).
PMID:39105351	FYPO:0001355	decreased vegetative cell population growth	The induction of sdr1+ expression, yeast cell growth was significantly suppressed (Figure 2d), indicating that excessive expression of sdr1+ plays an active role in suppressing yeast cell growth.
PMID:39105351	FYPO:0007085	increased RNA level during cellular response to sulfur starvation [assayed_transcript] PomBase:SPBC8E4.01c	These include mei2+, which encodes the master meiosis-regulator (Harigaya et al., 2006; Sugiyama et al., 2016), and phosphate depletion-responsive genes ecl3+, pho1+, and pho84+
PMID:39105351	FYPO:0007085	increased RNA level during cellular response to sulfur starvation [assayed_transcript] PomBase:SPBP4G3.02	These include mei2+, which encodes the master meiosis-regulator (Harigaya et al., 2006; Sugiyama et al., 2016), and phosphate depletion-responsive genes ecl3+, pho1+, and pho84+
PMID:39105351	FYPO:0007085	increased RNA level during cellular response to sulfur starvation [assayed_transcript] PomBase:SPAC27D7.03c	These include mei2+, which encodes the master meiosis-regulator (Harigaya et al., 2006; Sugiyama et al., 2016), and phosphate depletion-responsive genes ecl3+, pho1+, and pho84+
PMID:39105351	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	We found that, similar to a phosphate-depleted environment (Ohtsuka et al., 2023), the expression levels in Δpho7 cells were significantly reduced under sulfur- depleted conditions (Figure 4).
PMID:39105351	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.12c	We found that, similar to a phosphate-depleted environment (Ohtsuka et al., 2023), the expression levels in Δpho7 cells were significantly reduced under sulfur- depleted conditions (Figure 4).
PMID:39105351	FYPO:0007592	normal mitophagy during nitrogen starvation	autophagy was triggered in ΔSPCC417.09c cells under nitrogen depletion but not under sulfur depletion.
PMID:39105351	FYPO:0008320	abnormal cell morphology during sulphur deprivation	similar to sdr1+, overexpression of fal1+ did not rectify the morphological abnormalities of Δecl cells under sulfur depletion.
PMID:39110593	GO:0032541	cortical endoplasmic reticulum	(Figure 1C)
PMID:39110593	GO:0032541	cortical endoplasmic reticulum	(Figure 1C)
PMID:39110593	FYPO:0008077	decreased phosphatidylserine binding [has_severity] medium	(Figure 3D)
PMID:39110593	FYPO:0008077	decreased phosphatidylserine binding [has_severity] high	(Figure 3D)
PMID:39110593	GO:0001786	phosphatidylserine binding	(Figure 3D)
PMID:39110593	GO:0035091	phosphatidylinositol binding	(Figure 3D)
PMID:39110593	FYPO:0008328	decreased phosphatidylinositol binding [has_severity] medium	(Figure 3D)
PMID:39110593	FYPO:0008328	decreased phosphatidylinositol binding [assayed_protein] PomBase:SPBC16G5.05c [has_severity] high	(Figure 3D)
PMID:39110593	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering [has_severity] high	(Figure S3A) (left panel), ER-PM tethering is reduced in Scs2-2TA mutant at native locus
PMID:39110593	FYPO:0008294	normal plasma membrane-ER tethering	(Figure S3A) (left panel), ER-PM tethering is reduced in Scs2-2TA mutant at native locus
PMID:39110593	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering	(Figures 4B and S4B)
PMID:39110593	FYPO:0004085	decreased vegetative cell growth [has_severity] medium	(comment: CONDITION medium pH below 3.5)
PMID:39110593	FYPO:0004085	decreased vegetative cell growth [has_severity] medium	(comment: CONDITION medium pH below 3.5) (Figure 6)
PMID:39110593	FYPO:0004085	decreased vegetative cell growth [has_severity] high	(comment: CONDITION medium pH below 3.5) (Figure 6)
PMID:39110593	FYPO:0004085	decreased vegetative cell growth [has_severity] high	(comment: CONDITION medium pH below 3.5) (Figure 6)
PMID:39110593	FYPO:0004085	decreased vegetative cell growth [has_severity] high	(comment: CONDITION medium pH below 3.5) (Figure 6)
PMID:39110593	SO:0001527	peptide_localization_signal	(comment: FFAT-like motif that binds VAPs (scs2))
PMID:39110593	GO:0035091	phosphatidylinositol binding	(comment: liposome binding assay)
PMID:39110593	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering [has_severity] high	A previous study has shown that Scs2 plays a dominant role in ER-PM tethering over Scs22 in fission yeast,5 manifested by apparent ER-PM dissociation indicated by the luminal ER marker mCherry-ADEL18 in scs2D cells (see also Figure 1A).
PMID:39110593	FYPO:0008294	normal plasma membrane-ER tethering	ER-PM contact formation was however unaffected in pps1D (Figures 4B and S4B).
PMID:39110593	FYPO:0002151	inviable spore [has_penetrance] 100	Either the removal or genetic alterations of this presumed Scs2-interacting motif engendered inviable spores in S. pombe (Figure 6A), indicative of its necessity for Pma1 function.
PMID:39110593	FYPO:0002151	inviable spore [has_penetrance] 100	Either the removal or genetic alterations of this presumed Scs2-interacting motif engendered inviable spores in S. pombe (Figure 6A), indicative of its necessity for Pma1 function.
PMID:39110593	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering [has_severity] low	Fascinatingly, though not as fully efficient as WT, Scs2-PM was able to establish ER-PM contacts in a dose-dependent manner, which similarly required a functional MSP domain (Figure 3A).
PMID:39110593	FYPO:0008294	normal plasma membrane-ER tethering	However, no reduction of ER-PM contacts was seen in csr102Dpdr16Dpil1D cells, and Scs2 could still establish ER-PM contacts at cortical regions devoid of Pma1 in the background (Figure 2G)
PMID:39110593	GO:0035091	phosphatidylinositol binding	In fact, purified Scs2N-6His could bind both PI and PS liposomes. Such binding was enhanced with increased PI or PS concentration or by adding PI4P to respective liposomes (Figure S3C).
PMID:39110593	GO:0001786	phosphatidylserine binding	In fact, purified Scs2N-6His could bind both PI and PS liposomes. Such binding was enhanced with increased PI or PS concentration or by adding PI4P to respective liposomes (Figure S3C).
PMID:39110593	FYPO:0008329	phosphatidylserine absent from plasma membrane	Indeed, as previously shown,31 the PM pool of PS marked by GFP-Lact-C234 was absent in pps1D (Figure S4A).
PMID:39110593	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering	Interestingly, ER-PM association was compromised when the open reading frames of scs2 and scs22 were swapped at their genomic loci (asterisked in Figure S1A), implying that two VAPs may intrinsically differ in ER-PM tethering function.
PMID:39110593	FYPO:0002674	normal protein localization to plasma membrane [has_penetrance] 100 [has_severity] high [assayed_protein] PomBase:SPAC3H8.02	Likewise, the cortical recruitment of Csr102 was fully rescued by Scs2-PM but not Scs23KA-PM (Figure S3B).
PMID:39110593	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering [has_severity] high	Notably, mutations of three previously reported conserved lysine residues (K36/38/43A,20,21 hereafter referred to as 3KA) in the VAP consensus sequence (VCS) within the MSP domain of either Scs2 or Scs22 abolished their ER-PM tethering capacity (asterisked by large PM regions devoid of the cER in Figure 1C)
PMID:39110593	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering [has_severity] high	Notably, mutations of three previously reported conserved lysine residues (K36/38/43A,20,21 hereafter referred to as 3KA) in the VAP consensus sequence (VCS) within the MSP domain of either Scs2 or Scs22 abolished their ER-PM tethering capacity (asterisked by large PM regions devoid of the cER in Figure 1C)
PMID:39110593	FYPO:0006330	decreased endoplasmic reticulum-plasma membrane tethering [has_severity] high	Notably, mutations of three previously reported conserved lysine residues (K36/38/43A,20,21 hereafter referred to as 3KA) in the VAP consensus sequence (VCS) within the MSP domain of either Scs2 or Scs22 abolished their ER-PM tethering capacity (asterisked by large PM regions devoid of the cER in Figure 1C)
PMID:39110593	FYPO:0008077	decreased phosphatidylserine binding [has_severity] high [assayed_protein] PomBase:SPAC17C9.12	Scs2N bound specifically to PI and PS, and Scs2N2TA showed weaker binding to both, whereas Scs2N3KA exhibited significantly lower affinities for both (Figures 3C, S3D, and S3E). (Liposome binding assay)
PMID:39110593	FYPO:0008328	decreased phosphatidylinositol binding [has_severity] high	Scs2N bound specifically to PI and PS, and Scs2N2TA showed weaker binding to both, whereas Scs2N3KA exhibited significantly lower affinities for both (Figures 3C, S3D, and S3E). (liposome binding assay)
PMID:39110593	FYPO:0002128	abolished protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [has_penetrance] 100 [has_severity] high [assayed_protein] PomBase:SPAC3H8.02	Such interactions were required for its cortical localization, as Csr102 became cytosolic in the absence of both VAPs even when ER-PM contacts were artificially restored (Figures 2E and S2F).
PMID:39110593	FYPO:0006628	decreased phosphatidylinositol-4-phosphate level in plasma membrane [has_severity] high [has_penetrance] 100	Such reduction was enhanced when cells further lost either or both of csr102 and pdr16 in the background, whereas mutants with single or double deletion of csr102 and pdr16 remained WT-like (Figure 2D).
PMID:39110593	FYPO:0006628	decreased phosphatidylinositol-4-phosphate level in plasma membrane [has_severity] medium [has_penetrance] 100	Such reduction was enhanced when cells further lost either or both of csr102 and pdr16 in the background, whereas mutants with single or double deletion of csr102 and pdr16 remained WT-like (Figure 2D).
PMID:39110593	FYPO:0006628	decreased phosphatidylinositol-4-phosphate level in plasma membrane [has_penetrance] 100 [has_severity] high	Such reduction was enhanced when cells further lost either or both of csr102 and pdr16 in the background, whereas mutants with single or double deletion of csr102 and pdr16 remained WT-like (Figure 2D).
PMID:39110593	GO:0120010	intermembrane phospholipid transfer	Such reduction was enhanced when cells further lost either or both of csr102 and pdr16 in the background, whereas mutants with single or double deletion of csr102 and pdr16 remained WT-like (Figure 2D). No detectable change of phosphatidylinositol 4,5-bisphosphate (PI4,5P2) levels was seen in all these mutants (data not shown). These data suggest that Sec14 family proteins contribute to PI4P homeostasis in S. pombe.
PMID:39110593	GO:0120010	intermembrane phospholipid transfer	Such reduction was enhanced when cells further lost either or both of csr102 and pdr16 in the background, whereas mutants with single or double deletion of csr102 and pdr16 remained WT-like (Figure 2D). No detectable change of phosphatidylinositol 4,5-bisphosphate (PI4,5P2) levels was seen in all these mutants (data not shown). These data suggest that Sec14 family proteins contribute to PI4P homeostasis in S. pombe.
PMID:39110593	GO:0120010	intermembrane phospholipid transfer	Such reduction was enhanced when cells further lost either or both of csr102 and pdr16 in the background, whereas mutants with single or double deletion of csr102 and pdr16 remained WT-like (Figure 2D). No detectable change of phosphatidylinositol 4,5-bisphosphate (PI4,5P2) levels was seen in all these mutants (data not shown). These data suggest that Sec14 family proteins contribute to PI4P homeostasis in S. pombe.
PMID:39110593	FYPO:0006629	normal phosphatidylinositol-4-phosphate level in plasma membrane	Surprisingly, like WT (Figure S1F), Scs2-PM was able to restore the PM PI4P level in scs2Dscs22D cells, while Scs23KA-PM again lost the competence (Figure 3B).
PMID:39110593	GO:0005635	nuclear envelope	Unlike Scs22 where its nuclear envelope (NE) localization was obvious, the NE pool of Scs2 was barely visible, suggesting likely stronger affinity of Scs2 toward the cell cortex (Figure 1C).
PMID:39110593	FYPO:0008330	increased phosphatidylinositol-4-phosphate level in plasma membrane	We also saw augmented PM levels of PI4P and PI4,5P2 indicated by PHOsh2-GFP and PHNum1- GFP,5 respectively, in these cells (Figure S4A)
PMID:39110593	FYPO:0006628	decreased phosphatidylinositol-4-phosphate level in plasma membrane [has_penetrance] 100 [has_severity] medium	We found that both the PM and Golgi pools of PI4P decreased significantly in sec14D cells.
PMID:39110593	FYPO:0006628	decreased phosphatidylinositol-4-phosphate level in plasma membrane [has_penetrance] 100 [has_severity] medium	We found that both the PM and Golgi pools of PI4P decreased significantly in sec14D cells.
PMID:39110593	FYPO:0004085	decreased vegetative cell growth [has_severity] medium	medium pH below 3.5. In fact, scs2Dscs22D cells already showed compromised growth in highly acidic media, similarly to pma1-DCter cells that lacked the C-terminal R domain (Figure 6D).
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 1A and B)
PMID:39156640	FYPO:0007436	swollen elongated multiseptate vegetative cell [has_severity] high	(Fig. 1A and B)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 1A and B)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] medium	(Fig. 1A and C)
PMID:39156640	FYPO:0007436	swollen elongated multiseptate vegetative cell [has_severity] low	(Fig. 1A and C)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] medium	(Fig. 1A and C)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 1B)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 1B)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 1B)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 1B)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] low	(Fig. 1C)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] low	(Fig. 1C)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] medium	(Fig. 1C)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] medium	(Fig. 1C)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 1D)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] medium	(Fig. 1D)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] medium	(Fig. 1D)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 1D)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 1D)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 1D)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] low	(Fig. 1E)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] low	(Fig. 1E)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] low	(Fig. 1E)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] low	(Fig. 1E)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] low	(Fig. 1E)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] low	(Fig. 1E)
PMID:39156640	FYPO:0002719	decreased protein localization to septum [assayed_protein] PomBase:SPCC1281.01 [has_severity] medium	(Fig. 2A)
PMID:39156640	FYPO:0002871	decreased protein localization to growing cell tip [assayed_protein] PomBase:SPCC1840.02c [has_severity] medium	(Fig. 2A)
PMID:39156640	FYPO:0003317	decreased protein localization to growing cell tip, with protein distributed in plasma membrane or cortex [has_severity] high [assayed_protein] PomBase:SPCC1281.01	(Fig. 2B and C)
PMID:39156640	FYPO:0003317	decreased protein localization to growing cell tip, with protein distributed in plasma membrane or cortex [has_severity] high [assayed_protein] PomBase:SPCC1281.01	(Fig. 2B and C)
PMID:39156640	FYPO:0006220	abolished protein localization to septum [assayed_protein] PomBase:SPCC1281.01 [has_severity] medium	(Fig. 2B)
PMID:39156640	FYPO:0003317	decreased protein localization to growing cell tip, with protein distributed in plasma membrane or cortex [assayed_protein] PomBase:SPCC1840.02c [has_severity] high	(Fig. 2B)
PMID:39156640	FYPO:0003317	decreased protein localization to growing cell tip, with protein distributed in plasma membrane or cortex [assayed_protein] PomBase:SPCC1840.02c [has_severity] high	(Fig. 2B)
PMID:39156640	FYPO:0006220	abolished protein localization to septum [assayed_protein] PomBase:SPCC1281.01 [has_severity] medium	(Fig. 2B)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 3A)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 3A)
PMID:39156640	FYPO:0000646	swollen vegetative cell [has_severity] low	(Fig. 3A)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 3A)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 3A)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 3A)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 3A)
PMID:39156640	FYPO:0000674	normal cell population growth at high temperature	(Fig. 3B)
PMID:39156640	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 3B)
PMID:39156640	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 3B)
PMID:39156640	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 3B)
PMID:39156640	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 3B)
PMID:39156640	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 3B)
PMID:39156640	FYPO:0001357	normal vegetative cell population growth	(Fig. 3B)
PMID:39156640	FYPO:0001357	normal vegetative cell population growth	(Fig. 3B)
PMID:39156640	FYPO:0001357	normal vegetative cell population growth	(Fig. 3B)
PMID:39156640	FYPO:0000674	normal cell population growth at high temperature	(Fig. 3B)
PMID:39156640	FYPO:0000674	normal cell population growth at high temperature	(Fig. 3B)
PMID:39156640	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3B)
PMID:39156640	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3B)
PMID:39156640	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3B)
PMID:39156640	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3B)
PMID:39156640	FYPO:0000135	abnormal plasma membrane sterol distribution	(Fig. 4A)
PMID:39156640	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth	(Fig. 4A, 4B, Fig. S5B)
PMID:39156640	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth	(Fig. 5A)
PMID:39156640	FYPO:0000945	swollen spheroid vegetative cell [has_severity] high	(Fig. 5A)
PMID:39156640	FYPO:0002942	swollen spheroid cell during G0	(Fig. 5B)
PMID:39156640	FYPO:0002942	swollen spheroid cell during G0	(Fig. 5B)
PMID:39156640	FYPO:0002942	swollen spheroid cell during G0	(Fig. 5B)
PMID:39156640	FYPO:0002942	swollen spheroid cell during G0	(Fig. 5B)
PMID:39156640	FYPO:0007868	sensitive to actin polymerization inhibitor [has_severity] low	(Fig. 6A)
PMID:39156640	FYPO:0007868	sensitive to actin polymerization inhibitor [has_severity] high	(Fig. 6A)
PMID:39156640	FYPO:0007868	sensitive to actin polymerization inhibitor [has_severity] low	(Fig. 6A)
PMID:39156640	FYPO:0002652	excess intracellular endomembrane system present	(Fig. 6B)
PMID:39156640	FYPO:0002652	excess intracellular endomembrane system present [has_severity] high	(Fig. 6C, D and E)
PMID:39156640	FYPO:0000281	small vacuoles present in increased numbers during vegetative growth [has_severity] high	(Fig. 7A, C, D and E)
PMID:39156640	FYPO:0000281	small vacuoles present in increased numbers during vegetative growth [has_severity] high	(Fig. 7B, C and D)
PMID:39156640	FYPO:0000539	increased protein secretion during vegetative growth [assayed_protein] PomBase:SPAC19G12.10c [has_severity] high	(Fig. 7F and G)
PMID:39156640	FYPO:0000539	increased protein secretion during vegetative growth [assayed_protein] PomBase:SPAC19G12.10c [has_severity] medium	(Fig. 7F and G)
PMID:39156640	FYPO:0000539	increased protein secretion during vegetative growth [assayed_protein] PomBase:SPAC19G12.10c [has_severity] medium	(Fig. 7F and G)
PMID:39156640	FYPO:0000539	increased protein secretion during vegetative growth [assayed_protein] PomBase:SPAC19G12.10c [has_severity] low	(Fig. 7F and G)
PMID:39156640	GO:2000769	regulation of establishment or maintenance of cell polarity regulating cell shape	We show that Bgs1-synthetized linear b(1,3)glucan cooperates specifically with the Tea1-Tea4 complex, but not with the rest of polarisome proteins, and all together are essential for the control and maintenance of growth polarity and morphology (Figure 5C).
PMID:39174851	GO:0035861	site of double-strand break [exists_during] meiotic prophase I	(Fig. 1 and 5)
PMID:39174851	MOD:00696	phosphorylated residue [increased_during] meiotic prophase I [added_by] PomBase:SPBC11B10.09	(Fig. 1B and 2C)
PMID:39174851	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC644.14c [has_severity] high [assayed_protein] PomBase:SPBC28F2.07	(Fig. 3A)
PMID:39174851	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC644.14c [assayed_protein] PomBase:SPBC28F2.07	(Fig. 3A, Fig. EV1A)
PMID:39174851	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC644.14c [assayed_protein] PomBase:SPBC28F2.07	(Fig. 3A, Fig. EV1A)
PMID:39174851	FYPO:0002485	decreased intergenic meiotic recombination [has_severity] low	(Fig. 3B)
PMID:39174851	FYPO:0002485	decreased intergenic meiotic recombination [has_severity] medium	(Fig. 3B)
PMID:39174851	FYPO:0003891	normal intragenic meiotic recombination	(Fig. 3C)
PMID:39174851	FYPO:0003179	decreased intragenic meiotic recombination [has_severity] medium	(Fig. 3C)
PMID:39174851	FYPO:0006160	decreased number of Rad51 foci during meiotic prophase I [has_severity] high	(Fig. 4, Fig. EV2)
PMID:39174851	FYPO:0008301	decreased punctate nuclear protein localization during meiotic prophase I [assayed_protein] PomBase:SPBC28F2.07 [has_severity] high	(Fig. 4A, Fig. EV2 and EV3)
PMID:39174851	FYPO:0004910	normal punctate nuclear protein localization [assayed_protein] PomBase:SPBC28F2.07	(Fig. 4A, Fig. EV2 and EV3)
PMID:39174851	FYPO:0008303	normal number of Rad51 foci during meiotic prophase I	(Fig. 4A, Fig. EV2)
PMID:39174851	FYPO:0006160	decreased number of Rad51 foci during meiotic prophase I [has_severity] high	(Fig. 4A, Fig. EV2)
PMID:39174851	FYPO:0000478	normal meiosis	(Fig. 4A, Fig. S2)
PMID:39174851	FYPO:0000478	normal meiosis	(Fig. 4A, Fig. S2)
PMID:39174851	FYPO:0000478	normal meiosis	(Fig. 4A, Fig. S2)
PMID:39174851	FYPO:0004910	normal punctate nuclear protein localization [assayed_protein] PomBase:SPBC28F2.07	(Fig. 5)
PMID:39174851	FYPO:0008302	abolished punctate nuclear protein localization during meiotic prophase I [assayed_protein] PomBase:SPBC28F2.07	(Fig. 5)
PMID:39174851	FYPO:0008302	abolished punctate nuclear protein localization during meiotic prophase I [assayed_protein] PomBase:SPBC28F2.07	(Fig. 5)
PMID:39174851	FYPO:0008305	increased inter-sister chromatid meiotic recombination	(Fig. 6)
PMID:39174851	FYPO:0008305	increased inter-sister chromatid meiotic recombination	(Fig. 6)
PMID:39174851	FYPO:0000151	abnormal meiotic chromosome segregation [has_penetrance] 35 [has_severity] medium	(Fig. 7A)
PMID:39174851	FYPO:0000151	abnormal meiotic chromosome segregation [has_severity] medium [has_penetrance] 28	(Fig. 7A)
PMID:39174851	FYPO:0000151	abnormal meiotic chromosome segregation [has_severity] medium [has_penetrance] 28	(Fig. 7A)
PMID:39174851	FYPO:0000151	abnormal meiotic chromosome segregation [has_severity] medium [has_penetrance] 48	(Fig. 7A)
PMID:39174851	FYPO:0000151	abnormal meiotic chromosome segregation [has_severity] high [has_penetrance] 68	(Fig. 7A)
PMID:39174851	FYPO:0000151	abnormal meiotic chromosome segregation [has_severity] high [has_penetrance] 68	(Fig. 7A)
PMID:39174851	FYPO:0000151	abnormal meiotic chromosome segregation [has_severity] medium [has_penetrance] 24	(Fig. 7A)
PMID:39174851	FYPO:0000151	abnormal meiotic chromosome segregation [has_severity] medium [has_penetrance] 24	(Fig. 7A)
PMID:39174851	FYPO:0003176	normal meiotic chromosome segregation	(Fig. 7A)
PMID:39174851	FYPO:0003176	normal meiotic chromosome segregation	(Fig. 7A)
PMID:39174851	FYPO:0006419	increased duration of Rad51 focus presence during meiotic cell cycle [has_penetrance] low	(Fig. 7C)
PMID:39174851	FYPO:0006419	increased duration of Rad51 focus presence during meiotic cell cycle [has_penetrance] low	(Fig. 7C)
PMID:39174851	FYPO:0006419	increased duration of Rad51 focus presence during meiotic cell cycle [has_penetrance] high	(Fig. 7C)
PMID:39174851	FYPO:0006419	increased duration of Rad51 focus presence during meiotic cell cycle [has_penetrance] low	(Fig. 7C)
PMID:39174851	FYPO:0006419	increased duration of Rad51 focus presence during meiotic cell cycle [has_penetrance] low	(Fig. 7C)
PMID:39174851	FYPO:0000581	decreased spore germination frequency [has_severity] low	(Fig. 7D)
PMID:39174851	FYPO:0000581	decreased spore germination frequency [has_severity] low	(Fig. 7D)
PMID:39174851	FYPO:0000581	decreased spore germination frequency [has_severity] low	(Fig. 7D)
PMID:39174851	FYPO:0000581	decreased spore germination frequency [has_severity] high	(Fig. 7D)
PMID:39174851	FYPO:0000581	decreased spore germination frequency [has_severity] high	(Fig. 7D)
PMID:39174851	FYPO:0000581	decreased spore germination frequency [has_severity] medium	(Fig. 7D)
PMID:39174851	FYPO:0004993	normal spore germination frequency	(Fig. 7D)
PMID:39174851	FYPO:0004993	normal spore germination frequency	(Fig. 7D)
PMID:39174851	FYPO:0000581	decreased spore germination frequency [has_severity] low	(Fig. 7D)
PMID:39174851	FYPO:0000581	decreased spore germination frequency [has_severity] low	(Fig. 7D)
PMID:39174851	FYPO:0003611	increased protein level during meiosis [assayed_protein] PomBase:SPBC28F2.07	(Fig. EV4)
PMID:39174851	FYPO:0003611	increased protein level during meiosis [assayed_protein] PomBase:SPBC28F2.07	(Fig. EV4)
PMID:39174851	FYPO:0004634	normal protein level during meiosis [assayed_protein] PomBase:SPAC644.14c	(Fig. S3A and B)
PMID:39174851	FYPO:0004634	normal protein level during meiosis [assayed_protein] PomBase:SPAC644.14c	(Fig. S3A and B)
PMID:39174851	FYPO:0004634	normal protein level during meiosis [assayed_protein] PomBase:SPAC644.14c	(Fig. S3A and B)
PMID:39174851	FYPO:0004634	normal protein level during meiosis [assayed_protein] PomBase:SPAC644.14c	(Fig. S3C)
PMID:39174851	FYPO:0004634	normal protein level during meiosis [assayed_protein] PomBase:SPAC644.14c	(Fig. S3C)
PMID:39174851	FYPO:0004634	normal protein level during meiosis [assayed_protein] PomBase:SPAC644.14c	(Fig. S3C)
PMID:39174851	FYPO:0002485	decreased intergenic meiotic recombination [has_severity] high	(Fig. S4A)
PMID:39174851	FYPO:0008304	abolished protein localization to nucleus during meiosis [assayed_protein] PomBase:SPBC28F2.07	(Fig. S4B)
PMID:39174851	FYPO:0004634	normal protein level during meiosis [assayed_protein] PomBase:SPBC28F2.07	(Fig. S4C)
PMID:39174851	PomGeneEx:0000018	protein level increased [during] meiotic prophase I	EGFP-Sfr1 protein was clearly detected from the end of S-phase (2.5 h after meiotic induction) to the entry into the first chromosome segregation (meiosis I, 4.5 h), with the highest levels during meiotic prophase (Fig. 1A).
PMID:39174851	FYPO:0005577	decreased protein phosphorylation during meiotic cell cycle [has_severity] high [assayed_protein] PomBase:SPBC28F2.07	The mobility shift observed in Phos-tag gels was almost completely abolished in this EGFP-Sfr1-7A mutant protein, indicating that it was related to modifications in these residues of the protein (Fig. 1D).
PMID:39174851	FYPO:0005577	decreased protein phosphorylation during meiotic cell cycle [assayed_protein] PomBase:SPBC28F2.07 [has_severity] medium	This mobility shift was diminished in cells of the same culture treated in parallel with 1-NM- PP1, showing a 50% reduction in the slow-migrating band compared to DMSO-treated cells at 4 h after meiotic induction (n = 4, P value = 0.0337). This result suggests that Cdc2 is responsible for the phosphorylation of Sfr1 during meiotic prophase. (Fig. 2A)
PMID:39239853	FYPO:0008198	decreased protein localization to plasma membrane during vegetative growth [assayed_protein] PomBase:SPCC594.01	(comment: CHECK (check was normal protein localization to plasma membrane)) We found that Duc1-mNG PM localization along the lateral cell cortex was diminished by ~25% in efr3Δ cells compared to wild-type (Fig. 5A,B).
PMID:39239853	FYPO:0000782	mislocalized protein during vegetative growth [assayed_protein] PomBase:SPCC594.01	(comment: CHECK (mislocalized to division site).) As anticipated if these mutations successfully disrupted Duc1 association with Scs2 and Scs22, Duc1-Y374A,F375A-mNG localized at the division site (Fig. 4H).
PMID:39239853	FYPO:0007283	normal protein localization to lateral cell cortex during vegetative growth [assayed_protein] PomBase:SPCC594.01	(comment: CHECK check was plasma menbrane/) To dissect the contribution of each class of ER-PM contact to Duc1-mNG localization, we analyzed its distribution in hob2Δ, ltc2Δ, ist2Δ, and tcb1Δ tcb2Δ tcb3Δ strains. We found that Duc1-mNG was excluded from the cell division site in all four strains, as in wild-type cells (Fig. S2A).
PMID:39239853	GO:0016328	lateral plasma membrane	Also, Opy1 and Its3 displayed localization along the cortex consistently throughout the cell cycle whereas Duc1 accumulated at different cortical sites depending on the cell-cycle stage (Fig. 1E). These results indicate that Duc1 may be proximal to Its3 and Opy1 at the PM only at certain times. || In scs2Δ scs22Δ cells, Duc1-mNG remained along the cell cortex, confirming its PM localization (Fig. 2A).
PMID:39239853	FYPO:0001401	abnormal protein localization to cell division site [assayed_protein] PomBase:SPCC594.01	Analysis of Duc1-mNG localization showed that, unlike in wild-type cells, Duc1- mNG localized at the septum in scs2-T39A,T40A scs22Δ cells (Fig. 4F).
PMID:39239853	FYPO:0004780	decreased protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_protein] PomBase:SPCC594.01	Duc1-mNG levels were also reduced at the lateral PM in its3-1 cells at a semi-restrictive temperature compared to wild-type (Fig. 5A,B). These results are consistent with Duc1 requiring PM PI(4,5)P2 for its PM localization.
PMID:39239853	FYPO:0000339	mislocalized septum during vegetative growth	Further, we noticed that over-production of Duc1, like overproduction of Opy1 (Snider et al., 2020), resulted in cells with off-centered septation (Fig. 5E,F), consistent with both of these proteins associating with PI(4,5)P2 and out-competing CR anchoring proteins for a limiting amount of PI(4,5)P2.
PMID:39239853	FYPO:0005289	actomyosin contractile ring sliding	However, a quantification of the ratio of short-to-long duc1Δ cells at septation demonstrated a significant fraction of duc1Δ cells divided asymmetrically (Fig. 6A,B). Wildtype cells formed a medial CR that slid in 1/13 cells examined, but duc1Δ cells formed a medial CR that slid along the cortex towards one cell end in 12/15 cells observed (Fig. 6C). Thus, Duc1 promotes proper CR anchoring.
PMID:39239853	FYPO:0001401	abnormal protein localization to cell division site [assayed_protein] PomBase:SPCC594.01	In contrast to its exclusion from the division site in wild-type cells, Duc1- mNG localized along the septa in scs2Δ scs22Δ cells (Fig. 2A,B). This observation was confirmed by live-cell time-lapse imaging with CR and SPB markers (Fig. 2C). Thus, we conclude that Duc1 exclusion from the cell division site depends specifically on Scs2 and Scs22 and not ER-PM contact sites per se.
PMID:39239853	FYPO:0006625	decreased phosphatidylinositol-4,5-bisphosphate level in plasma membrane	In contrast, lateral PM and septum PI(4,5)P2 levels, indicated by the GFP-2xPHPlc biosensor, were 36% and 48%, respectively, in duc1Δ compared to wild-type (Fig. 6D-F).
PMID:39239853	FYPO:0003337	increased protein localization to septum [assayed_protein] PomBase:SPAC19G12.14	Its3-mNG was increased at the septum in scs2Δ scs22Δ cells compared to wild-type cells by ~50% without a change in the lateral cortex levels (Fig. 7A-C).
PMID:39239853	FYPO:0004780	decreased protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_protein] PomBase:SPCPB16A4.02c	Live-cell imaging revealed that over-production of Duc1 indeed reduced Opy1-mNG at the PM by ~35% (Fig. 5C,D).
PMID:39239853	FYPO:0004780	decreased protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_protein] PomBase:SPCC594.01	Live-cell imaging revealed that over-production of Duc1 indeed reduced Opy1-mNG at the PM by ~35% (Fig. 5C,D).
PMID:39239853	GO:0032541	cortical endoplasmic reticulum	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0140268	endoplasmic reticulum-plasma membrane contact site	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0140268	endoplasmic reticulum-plasma membrane contact site	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0140268	endoplasmic reticulum-plasma membrane contact site	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0140268	endoplasmic reticulum-plasma membrane contact site	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0032541	cortical endoplasmic reticulum	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0032541	cortical endoplasmic reticulum	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0032541	cortical endoplasmic reticulum	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	GO:0032541	cortical endoplasmic reticulum	Live-cell imaging revealed that they all localized either uniformly or in a punctate pattern along the lateral cell cortex and, all but Ist2 lacked any detectable localization at the cell division site (Fig. 3A)
PMID:39239853	FYPO:0007441	normal protein localization to endoplasmic reticulum-plasma membrane contact site [assayed_protein] PomBase:SPAC17C9.12	The localizations of Scs2-mNG, Scs22-mNG and mCherry-AHDL all appeared unchanged in duc1Δ cells compared to wild-type cells (Figure S4B).
PMID:39239853	FYPO:0007441	normal protein localization to endoplasmic reticulum-plasma membrane contact site [assayed_protein] PomBase:SPBC16G5.05c	The localizations of Scs2-mNG, Scs22-mNG and mCherry-AHDL all appeared unchanged in duc1Δ cells compared to wild-type cells (Figure S4B).
PMID:39239853	FYPO:0003414	normal protein localization to septum [assayed_protein] PomBase:SPAC19G12.14	There was no change in Its3-mNG septum intensity in duc1Δ cells compared to wild-type, as expected (Fig. S4E).
PMID:39239853	FYPO:0006629	normal phosphatidylinositol-4-phosphate level in plasma membrane	There was no significant change in lateral cortex or septum PI4P levels, as determined by the GFP-P4CSidC biosensor (Fig. 6D-F).
PMID:39239853	FYPO:0002674	normal protein localization to plasma membrane [assayed_protein] PomBase:SPCC594.01	To dissect the contribution of each class of ER-PM contact to Duc1-mNG localization, we analyzed its distribution in hob2Δ, ltc2Δ, ist2Δ, and tcb1Δ tcb2Δ tcb3Δ strains. We found that Duc1-mNG was excluded from the cell division site in all four strains, as in wild-type cells (Fig. S2A).
PMID:39239853	FYPO:0002674	normal protein localization to plasma membrane [assayed_protein] PomBase:SPCC594.01	To dissect the contribution of each class of ER-PM contact to Duc1-mNG localization, we analyzed its distribution in hob2Δ, ltc2Δ, ist2Δ, and tcb1Δ tcb2Δ tcb3Δ strains. We found that Duc1-mNG was excluded from the cell division site in all four strains, as in wild-type cells (Fig. S2A).
PMID:39239853	FYPO:0002674	normal protein localization to plasma membrane [assayed_protein] PomBase:SPCC594.01	We also examined if Scs2 or Scs22 alone was responsible for preventing Duc1 division site localization but, as in wild-type cells, Duc1- mNG was excluded from the cell division site in both single deletion strains (Fig. S2B).
PMID:39239853	FYPO:0002674	normal protein localization to plasma membrane [assayed_protein] PomBase:SPCC594.01	We also examined if Scs2 or Scs22 alone was responsible for preventing Duc1 division site localization but, as in wild-type cells, Duc1- mNG was excluded from the cell division site in both single deletion strains (Fig. S2B).
PMID:39239853	FYPO:0006626	increased phosphatidylinositol-4,5-bisphosphate level in plasma membrane	We confirmed a lack of change in lateral cortical PI(4,5)P2 signal but found that the PI(4,5)P2 signal was increased at the septum by ~20% in scs2Δ scs22Δ cells compared to wild-type (Fig. 7D-F).
PMID:39239853	FYPO:0002674	normal protein localization to plasma membrane [assayed_protein] PomBase:SPCC794.08	We detected no change in lateral cortex Efr3-mNG but a ~30% decrease in lateral cortex Its3-mNG in duc1Δ compared to wild-type cells (Fig 6G,H and Fig. S4C,D)
PMID:39239853	FYPO:0004780	decreased protein localization to plasma membrane, with protein mislocalized to cytoplasm, during vegetative growth [assayed_protein] PomBase:SPAC19G12.14	We detected no change in lateral cortex Efr3-mNG but a ~30% decrease in lateral cortex Its3-mNG in duc1Δ compared to wild-type cells (Fig 6G,H and Fig. S4C,D)
PMID:39239853	FYPO:0007283	normal protein localization to lateral cell cortex during vegetative growth [assayed_protein] PomBase:SPCC594.01	check was plasma membrane /To dissect the contribution of each class of ER-PM contact to Duc1-mNG localization, we analyzed its distribution in hob2Δ, ltc2Δ, ist2Δ, and tcb1Δ tcb2Δ tcb3Δ strains. We found that Duc1-mNG was excluded from the cell division site in all four strains, as in wild-type cells (Fig. S2A).
PMID:39289458	FYPO:0008291	increased cellular mtDNA level [has_severity] low	As shown in Fig. 5c, the mtDNA copy number is slightly increased in ∆shy1 cells compared to that of in WT strain, indicating the observed reduction in mitochondrial RNA is not attributed to a decrease in mtDNA levels.
PMID:39289458	GO:0005743	mitochondrial inner membrane	Collectively, our findings strongly indicate that Shy1 is affixed to the mitochondrial inner membrane./Fig. 6. Shy1 is localized in the mitochondrial inner membrane.
PMID:39289458	FYPO:0001164	normal growth on glucose carbon source	Conversely, the growth reduction was marginal when cultured in glucose medium, which supports fermentative growth and thus necessitates moderate respiratory activity43.
PMID:39289458	FYPO:0001940	decreased ubiquinol-cytochrome-c reductase activity	Our results revealed a slight decrease in complex III enzyme activity in ∆shy1 cells compared to WT cells (Supplementary Fig. S5 online), suggesting that shy1 affects complex III in ways other than its assembly.
PMID:39289458	FYPO:0003915	decreased mitochondrial protein level [assayed_transcript] PomBase:SPMIT.11	Our results showed that the expression of Cob1, Cox1, Cox2, Cox3, and Atp6 were greatly reduced in ∆shy1 cells (Fig. 5d).
PMID:39289458	FYPO:0003915	decreased mitochondrial protein level [assayed_transcript] PomBase:SPMIT.04	Our results showed that the expression of Cob1, Cox1, Cox2, Cox3, and Atp6 were greatly reduced in ∆shy1 cells (Fig. 5d).
PMID:39289458	FYPO:0003915	decreased mitochondrial protein level [assayed_transcript] PomBase:SPMIT.05	Our results showed that the expression of Cob1, Cox1, Cox2, Cox3, and Atp6 were greatly reduced in ∆shy1 cells (Fig. 5d).
PMID:39289458	FYPO:0003915	decreased mitochondrial protein level [assayed_transcript] PomBase:SPMIT.07	Our results showed that the expression of Cob1, Cox1, Cox2, Cox3, and Atp6 were greatly reduced in ∆shy1 cells (Fig. 5d).
PMID:39289458	FYPO:0003915	decreased mitochondrial protein level [assayed_transcript] PomBase:SPMIT.01	Our results showed that the expression of Cob1, Cox1, Cox2, Cox3, and Atp6 were greatly reduced in ∆shy1 cells (Fig. 5d).
PMID:39289458	FYPO:0003423	decreased mitochondrial RNA level [assayed_transcript] PomBase:SPMIT.01	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	FYPO:0003423	decreased mitochondrial RNA level [assayed_transcript] PomBase:SPMIT.08	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	FYPO:0003423	decreased mitochondrial RNA level [assayed_transcript] PomBase:SPMIT.04	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	FYPO:0003423	decreased mitochondrial RNA level [assayed_transcript] PomBase:SPRRNA.02	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	FYPO:0003423	decreased mitochondrial RNA level [assayed_transcript] PomBase:SPRRNA.01	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	FYPO:0003423	decreased mitochondrial RNA level [assayed_transcript] PomBase:SPMIT.10	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	FYPO:0003423	decreased mitochondrial RNA level [assayed_transcript] PomBase:SPMIT.09	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	FYPO:0003423	decreased mitochondrial RNA level [assayed_transcript] PomBase:SPMIT.07	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	FYPO:0003423	decreased mitochondrial RNA level [assayed_transcript] PomBase:SPMIT.11	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	FYPO:0003423	decreased mitochondrial RNA level [assayed_transcript] PomBase:SPMIT.05	Our results showed that the levels of cob1, cox1, cox2, cox3, atp6, atp8 and atp9 RNAs were reduced in ∆shy1 cells (Fig. 5b). Furthermore, the abundance of mt-rRNAs (rns and rnl) was also reduced in shy1 deletion cells compared to WT cells, suggesting that deletion of shy1 affects the overall levels of the expression of the mtDNA-encoded genes.
PMID:39289458	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] high	The cell growth of the ∆shy1 mutant exhibited a notable decline when cultivated in glycerol medium in comparison to the wild-type (WT) strain (Fig. 5a).
PMID:39289458	GO:0097250	mitochondrial respirasome assembly	The levels of supercomplexes III2IV2 and III2IV were found to be lower in ∆shy1 cells compared to WT cells, while the abundance of COA complexes increased (Fig. 7a), indicating that the formation of supercomplexes involving complex IV is influenced by deletion of shy1. In contrast, the abundance of III2 and V complexes was largely unchanged in ∆shy1 cells (Fig. 7a).
PMID:39289458	FYPO:0007624	decreased mitochondrial respiratory chain complex IV assembly	The levels of supercomplexes III2IV2 and III2IV were found to be lower in ∆shy1 cells compared to WT cells, while the abundance of COA complexes increased (Fig. 7a), indicating that the formation of supercomplexes involving complex IV is influenced by deletion of shy1. In contrast, the abundance of III2 and V complexes was largely unchanged in ∆shy1 cells (Fig. 7a).
PMID:39330407	FYPO:0003013	abnormal actomyosin contractile ring disassembly [has_penetrance] 70 [has_severity] high	(Figure 3) Contractile ring shedding is exaggerated and premature in ∆ain1 ∆myo51 cells.
PMID:39330407	FYPO:0003013	abnormal actomyosin contractile ring disassembly [has_penetrance] 70 [has_severity] high	(Figure 3) Contractile ring shedding is exaggerated and premature in ∆ain1 ∆myo51 cells.
PMID:39330407	GO:0120104	mitotic actomyosin contractile ring, proximal layer	3.4. Myo51 Localizes to the Inner Layer of the Contractile Ring during Constriction
PMID:39330407	FYPO:0003013	abnormal actomyosin contractile ring disassembly [has_penetrance] 24	During our investigation, we noticed that contractile ring shedding appeared premature and exaggerated in ∆ain1 ∆myo51 cells when compared to wild-type cells. In wild-type cells expressing mEGFP-Myo2p, shedding begins when the ring is 62% constricted (n = 38 cells), and the fragments that shed from the constricting contractile ring extend out along the septum without reaching the full width of the cell (Figures 2A and 3A-C)
PMID:39330407	FYPO:0004653	delayed onset of actomyosin contractile ring contraction	The onset of contractile ring constriction is delayed by ~10 min in ∆ain1 ∆myp2 cells.
PMID:39330407	FYPO:0000161	abnormal actomyosin contractile ring assembly [has_severity] low [has_penetrance] 43	We acquired timelapse micrographs of ∆ain1 ∆myp2 cells expressing mEGFP-Myo2p to measure the duration of clumping when the onset of constriction is delayed. Forty-four percent of ∆ain1 ∆myp2 cells (n = 87 cells) showed the ring clumping phenotype, similar to ∆ain1 cells (Figure 1D).
PMID:39330407	FYPO:0000729	delayed onset of actomyosin contractile ring assembly	We measured the duration of clumps in ∆ain1 ∆myp2 cells and found that as expected, clumps last ~7 min longer in those cells (Figure 1E).
PMID:39330407	FYPO:0007211	premature actomyosin contractile ring assembly [has_penetrance] 54	"node clumping, Myo2p marker Figure 1A-D ""The clumping phenotype suggests that nodes aggregate into clumps during contractile ring assembly in the absence of Ain1p."""
PMID:39333464	FYPO:0008332	decreased mRNA poly(A) tail uridylation [has_severity] high	(Fig. 3A and B and Fig. S4)
PMID:39333464	FYPO:0008336	abolished mRNA poly(A) tail uridylation	(Fig. 3A and B and Fig. S4B)
PMID:39333464	FYPO:0008336	abolished mRNA poly(A) tail uridylation	(Fig. 3A and B and Fig. S4B)
PMID:39333464	FYPO:0008337	decreased 3' end uridylation of non-polyadenylated RNA [has_severity] high	(Fig. 3C, Fig. S4)
PMID:39333464	FYPO:0008339	abolished 3' end uridylation of non-polyadenylated RNA	(Fig. 3C, Fig. S4B)
PMID:39333464	FYPO:0008339	abolished 3' end uridylation of non-polyadenylated RNA	(Fig. 3C, Fig. S4B)
PMID:39333464	FYPO:0008338	increased 3' end uridylation of non-polyadenylated RNA [has_severity] low	(Fig. 4A)
PMID:39333464	FYPO:0008332	decreased mRNA poly(A) tail uridylation [has_severity] low	(Fig. 4A)
PMID:39333464	FYPO:0008335	increased mRNA poly(A) tail uridylation [has_severity] medium	(Fig. 4A, 4F)
PMID:39333464	FYPO:0002930	decreased poly(A) tail length [has_severity] low	(Fig. 4B)
PMID:39333464	FYPO:0002930	decreased poly(A) tail length [has_severity] low	(Fig. 4B)
PMID:39333464	FYPO:0002930	decreased poly(A) tail length [has_severity] medium	(Fig. 4B, 4F)
PMID:39333464	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4C, 4D)
PMID:39333464	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4C, 4D)
PMID:39333464	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4C, 4D)
PMID:39333464	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4C, 4D)
PMID:39333464	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 4C, 4D)
PMID:39333464	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 4C, 4D)
PMID:39333464	FYPO:0008335	increased mRNA poly(A) tail uridylation [has_severity] medium	(Fig. 4F)
PMID:39333464	FYPO:0002930	decreased poly(A) tail length [has_severity] medium	(Fig. 4F)
PMID:39333464	FYPO:0008335	increased mRNA poly(A) tail uridylation [has_severity] medium	(Fig. 4F)
PMID:39333464	FYPO:0002930	decreased poly(A) tail length [has_severity] medium	(Fig. 4F)
PMID:39333464	FYPO:0008338	increased 3' end uridylation of non-polyadenylated RNA [has_severity] medium	(Fig. 5A)
PMID:39333464	FYPO:0008338	increased 3' end uridylation of non-polyadenylated RNA [has_severity] high	(Fig. 5A)
PMID:39333464	FYPO:0002930	decreased poly(A) tail length [has_severity] high	(Fig. 5B)
PMID:39333464	FYPO:0002930	decreased poly(A) tail length [has_severity] medium	(Fig. 5B)
PMID:39333464	FYPO:0002930	decreased poly(A) tail length [has_severity] low	(Fig. 5B)
PMID:39333464	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 5C)
PMID:39333464	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 5C)
PMID:39333464	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 5C)
PMID:39333464	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 5C)
PMID:39333464	FYPO:0001357	normal vegetative cell population growth	(Fig. 5C)
PMID:39333464	FYPO:0001357	normal vegetative cell population growth	(Fig. 5C)
PMID:39333464	FYPO:0001357	normal vegetative cell population growth	(Fig. 5C)
PMID:39333464	FYPO:0001357	normal vegetative cell population growth	(Fig. S5B)
PMID:39333464	FYPO:0001357	normal vegetative cell population growth	(Fig. S5B)
PMID:39333464	FYPO:0001357	normal vegetative cell population growth	(Fig. S5B)
PMID:39333464	GO:1990074	polyuridylation-dependent mRNA catabolic process	(comment: CHECK ******uridylation dependent 3'-5' mRNA decay******) (Fig. 5)
PMID:39333464	GO:1990074	polyuridylation-dependent mRNA catabolic process	(comment: CHECK ******uridylation dependent 3'-5' mRNA decay*******.) (Fig. 5)
PMID:39333464	GO:0050265	RNA uridylyltransferase activity [part_of] mitochondrial RNA catabolic process	The highest number of oligo(U) tailed reads were detected for mitochondrial transcripts (Supplementary Fig. 4a), therefore, oligouridylation of mtRNA seems to be a main function of Cid16.
PMID:39333464	GO:0000957	mitochondrial RNA catabolic process	The highest number of oligo(U) tailed reads were detected for mitochondrial transcripts (Supplementary Fig. 4a), therefore, oligouridylation of mtRNA seems to be a main function of Cid16.
PMID:39333464	GO:0036450	polyuridylation-dependent decapping of nuclear-transcribed mRNA	Under standard conditions, uridylation of short mRNA poly(A) tails by Cid1 helps to direct mRNA toward the 5’ to 3’ decay pathway by enhancing Lsm1-7 complex binding and protecting the 3’-end from extensive deadenylation.
PMID:39333464	FYPO:0002930	decreased poly(A) tail length	While the global tail profile did not change in the Δcid16 mutant, we noticed an increase in the fraction of short-tailed reads in Δcid1 and double deletion strains (Fig. 3e).
PMID:39333464	GO:0050265	RNA uridylyltransferase activity [part_of] polyuridylation-dependent mRNA catabolic process	mRNAs with shortened poly(A) tails are uridylated by Cid1, while completely deadenylated mRNAs are subjected to oligouridylation by Cid16. Cid1- mediated uridylation routes decay towards the 5’ to 3’ pathway, while Cid16-mediated oligouridylation facilitates 3’ to 5’ degradation.
PMID:39333464	GO:0050265	RNA uridylyltransferase activity [has_input] mRNA [part_of] polyuridylation-dependent decapping of nuclear-transcribed mRNA	mRNAs with shortened poly(A) tails are uridylated by Cid1, while completely deadenylated mRNAs are subjected to oligouridylation by Cid16. Cid1- mediated uridylation routes decay towards the 5’ to 3’ pathway, while Cid16-mediated oligouridylation facilitates 3’ to 5’ degradation.
PMID:39333464	GO:0060212	negative regulation of nuclear-transcribed mRNA poly(A) tail shortening	uridylation prevents excessive deadenylation which in turn protects mRNA from 3’ to 5’ exonucleolitic decay.
PMID:39333500	FYPO:0008299	decreased rate of protein exchange at plasma membrane [assayed_protein] PomBase:SPAC110.03 [has_severity] low	(Fig. 2B)
PMID:39333500	FYPO:0008299	decreased rate of protein exchange at plasma membrane [has_severity] medium [assayed_protein] PomBase:SPAC110.03	(Fig. 2B)
PMID:39333500	FYPO:0008299	decreased rate of protein exchange at plasma membrane [assayed_protein] PomBase:SPAC110.03 [has_severity] high	(Fig. 2B)
PMID:39333500	FYPO:0003317	decreased protein localization to growing cell tip, with protein distributed in plasma membrane or cortex [has_severity] high [assayed_protein] PomBase:SPAC110.03	(Fig. 2E and F)
PMID:39333500	FYPO:0003317	decreased protein localization to growing cell tip, with protein distributed in plasma membrane or cortex [has_severity] medium [assayed_protein] PomBase:SPAC110.03	(Fig. 2E and F)
PMID:39333500	FYPO:0000021	spheroid vegetative cell [has_severity] high	(Fig. 2E)
PMID:39333500	FYPO:0002059	inviable cell population	(Fig. 2G)
PMID:39333500	FYPO:0001387	loss of viability at high temperature [has_severity] high	(Fig. 2H)
PMID:39333500	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 2H)
PMID:39333500	FYPO:0002380	viable spheroid vegetative cell [has_severity] high	(Fig. 4C)
PMID:39358553	PomGeneEx:0000011	RNA level increased [during] cell quiescence	(Fig. 1)
PMID:39358553	FYPO:0005995	increased lncRNA level [assayed_transcript] PomBase:SPNCRNA.1530 [has_severity] low	(Fig. 1A)
PMID:39358553	FYPO:0005995	increased lncRNA level [assayed_transcript] PomBase:SPNCRNA.1530 [has_severity] medium	(Fig. 1A)
PMID:39358553	FYPO:0005995	increased lncRNA level [assayed_transcript] PomBase:SPNCRNA.1530 [has_severity] high	(Fig. 1A)
PMID:39358553	FYPO:0005995	increased lncRNA level [assayed_transcript] PomBase:SPNCRNA.1530 [has_severity] high	(Fig. 1A)
PMID:39358553	FYPO:0005995	increased lncRNA level [assayed_transcript] PomBase:SPNCRNA.1530 [has_severity] medium	(Fig. 1A)
PMID:39358553	FYPO:0005995	increased lncRNA level [assayed_transcript] PomBase:SPNCRNA.1530 [has_severity] medium	(Fig. 1A)
PMID:39358553	FYPO:0005995	increased lncRNA level [assayed_transcript] PomBase:SPNCRNA.1530 [has_severity] medium	(Fig. 1A)
PMID:39358553	FYPO:0005995	increased lncRNA level [assayed_transcript] PomBase:SPNCRNA.1530 [has_severity] medium	(Fig. 1A)
PMID:39358553	FYPO:0005995	increased lncRNA level [assayed_transcript] PomBase:SPNCRNA.1530 [has_severity] low	(Fig. 1A)
PMID:39358553	FYPO:0006523	loss of viability in stationary phase following entry from mitotic G2 phase [has_severity] medium	(Fig. 1C)
PMID:39358553	FYPO:0001309	increased viability in stationary phase [has_severity] medium	(Fig. 1C)
PMID:39358553	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(Fig. 1D)
PMID:39358553	FYPO:0002062	normal cell growth	(Fig. 1E)
PMID:39358553	FYPO:0004706	decreased cytosolic monomeric ribosome level	(Fig. 4A and C)
PMID:39358553	FYPO:0006036	increased cytosolic monomeric ribosome level	(Fig. 4B and C)
PMID:39358553	FYPO:0008324	decreased cytosolic ribosome content	(Fig. 4E and F)
PMID:39358553	FYPO:0008325	increased cytosolic ribosome content	(Fig. 4E and F)
PMID:39358553	FYPO:0007317	decreased cytoplasmic translation [has_severity] low	(Fig. 4G)
PMID:39358553	GO:0003729	mRNA binding [has_input] PomBase:SPBC56F2.02	(Fig. 5)
PMID:39358553	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC56F2.02	(Fig. 5D)
PMID:39358553	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC56F2.02	(Fig. 5D)
PMID:39358553	FYPO:0006523	loss of viability in stationary phase following entry from mitotic G2 phase [has_severity] medium	(Fig. 5F)
PMID:39358553	FYPO:0001309	increased viability in stationary phase [has_severity] medium	(Fig. 5F)
PMID:39358553	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. EV2)
PMID:39358553	GO:0005737	cytoplasm	This analysis revealed that aal1 RNAs predominantly localize in the cytoplasm in multiple foci (Fig. 2B).
PMID:39378339	GO:0061621	canonical glycolysis	As expected, fba1-KD caused an accumulation of its substrate, FBP, by 2.4-fold. (Fig. 5 D)
PMID:39378339	GO:0004332	fructose-bisphosphate aldolase activity [part_of] canonical glycolysis	As expected, fba1-KD caused an accumulation of its substrate, FBP, by 2.4-fold. (Fig. 5 D)
PMID:39378339	FYPO:0008446	increased cellular nicotinamide level	Given that Qns1 converts NaAD to NAD, amounts of these metabolites were expected to be altered in qns1-KD cells. Therefore, these metabolites were quantified in the qns1-KD strain. After induction of CRISPRi, qns1-KD and nonsense control cells were broken down in methanol, and their watersoluble metabolites were quantified by liquid chromatography with tandem mass spectrometry (LC-MS/MS) (Fig. 5 B). In qns1- KD cells, the amount of NAD was reduced to about one-fifth of that in control cells, whereas the amount of NaAD increased by 23.5-fold in a specific manner (Fig. S5 B), consistent with the predicted function of Qns1. NAD is consumed by enzymes and converted to nicotinamide (NAM), which is utilized to regenerate NAD through the Preiss-Handler pathway after conversion to NA (Castro-Portuguez and Sutphin, 2020; Preiss and Handler, 1958a, 1958b). NAM and NA also accumulated after the knockdown of qns1+ (Fig. 5 B)
PMID:39378339	FYPO:0008444	increased cellular nicotinic acid adenine dinucleotide level	Given that Qns1 converts NaAD to NAD, amounts of these metabolites were expected to be altered in qns1-KD cells. Therefore, these metabolites were quantified in the qns1-KD strain. After induction of CRISPRi, qns1-KD and nonsense control cells were broken down in methanol, and their watersoluble metabolites were quantified by liquid chromatography with tandem mass spectrometry (LC-MS/MS) (Fig. 5 B). In qns1- KD cells, the amount of NAD was reduced to about one-fifth of that in control cells, whereas the amount of NaAD increased by 23.5-fold in a specific manner (Fig. S5 B), consistent with the predicted function of Qns1. NAD is consumed by enzymes and converted to nicotinamide (NAM), which is utilized to regenerate NAD through the Preiss-Handler pathway after conversion to NA (Castro-Portuguez and Sutphin, 2020; Preiss and Handler, 1958a, 1958b). NAM and NA also accumulated after the knockdown of qns1+ (Fig. 5 B)
PMID:39378339	GO:0034355	NAD+ biosynthetic process via the salvage pathway	Given that Qns1 converts NaAD to NAD, amounts of these metabolites were expected to be altered in qns1-KD cells. Therefore, these metabolites were quantified in the qns1-KD strain. After induction of CRISPRi, qns1-KD and nonsense control cells were broken down in methanol, and their watersoluble metabolites were quantified by liquid chromatography with tandem mass spectrometry (LC-MS/MS) (Fig. 5 B). In qns1- KD cells, the amount of NAD was reduced to about one-fifth of that in control cells, whereas the amount of NaAD increased by 23.5-fold in a specific manner (Fig. S5 B), consistent with the predicted function of Qns1. NAD is consumed by enzymes and converted to nicotinamide (NAM), which is utilized to regenerate NAD through the Preiss-Handler pathway after conversion to NA (Castro-Portuguez and Sutphin, 2020; Preiss and Handler, 1958a, 1958b). NAM and NA also accumulated after the knockdown of qns1+ (Fig. 5 B)
PMID:39378339	GO:0003952	NAD+ synthase (glutamine-hydrolyzing) activity [part_of] NAD+ biosynthetic process via the salvage pathway	Given that Qns1 converts NaAD to NAD, amounts of these metabolites were expected to be altered in qns1-KD cells. Therefore, these metabolites were quantified in the qns1-KD strain. After induction of CRISPRi, qns1-KD and nonsense control cells were broken down in methanol, and their watersoluble metabolites were quantified by liquid chromatography with tandem mass spectrometry (LC-MS/MS) (Fig. 5 B). In qns1- KD cells, the amount of NAD was reduced to about one-fifth of that in control cells, whereas the amount of NaAD increased by 23.5-fold in a specific manner (Fig. S5 B), consistent with the predicted function of Qns1. NAD is consumed by enzymes and converted to nicotinamide (NAM), which is utilized to regenerate NAD through the Preiss-Handler pathway after conversion to NA (Castro-Portuguez and Sutphin, 2020; Preiss and Handler, 1958a, 1958b). NAM and NA also accumulated after the knockdown of qns1+ (Fig. 5 B)
PMID:39378339	FYPO:0008445	increased cellular nicotinic acid level	Given that Qns1 converts NaAD to NAD, amounts of these metabolites were expected to be altered in qns1-KD cells. Therefore, these metabolites were quantified in the qns1-KD strain. After induction of CRISPRi, qns1-KD and nonsense control cells were broken down in methanol, and their watersoluble metabolites were quantified by liquid chromatography with tandem mass spectrometry (LC-MS/MS) (Fig. 5 B). In qns1- KD cells, the amount of NAD was reduced to about one-fifth of that in control cells, whereas the amount of NaAD increased by 23.5-fold in a specific manner (Fig. S5 B), consistent with the predicted function of Qns1. NAD is consumed by enzymes and converted to nicotinamide (NAM), which is utilized to regenerate NAD through the Preiss-Handler pathway after conversion to NA (Castro-Portuguez and Sutphin, 2020; Preiss and Handler, 1958a, 1958b). NAM and NA also accumulated after the knockdown of qns1+ (Fig. 5 B)
PMID:39378339	FYPO:0007367	increased cellular fructose 1,6-bisphosphate level	However, contrary to expectations, fba1-KD did not reduce the level of the product, G3P (Fig. 5 D).
PMID:39378339	FYPO:0000284	large and small daughter nuclei, with unequal mitotic sister chromatid segregation [has_penetrance] 20	Similarly, 48 h after induction of CRISPRi, the mis6-KD strain produced unequally divided nuclei and lagging chromosomes, which were observed in the mis6 temperature-sensitive mutant cells (Saitoh et al., 1997) (Fig. 4 B). .
PMID:39378339	FYPO:0006715	large and small daughter nuclei [has_penetrance] 40-60	This phenotype was identical to that observed in fas2/lsd1 temperaturesensitive mutant cells (Saitoh et al., 1996) (Fig. 4 B).
PMID:39378339	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 5	This phenotype was identical to that observed in fas2/lsd1 temperaturesensitive mutant cells (Saitoh et al., 1996) (Fig. 4 B).
PMID:39379376	FYPO:0008333	normal ribosome hibernation during glucose starvation	We then examined whether cytosolic ribosomes still tethered to mitochondria in Δdnm1 cells after prolonged glucose depletion. In situ cryo-ET imaging of Δdnm1 cells revealed that mitochondria remained elongated throughout glucose depletion (Fig. 4b). However, this morphological change did not prevent the tethering of cytosolic ribosomes to the OMM, with 98% of the imaged mitochondria (n = 100) being fully decorated with ribosomes at day 7 of glucose depletion (Fig. 4b, c, Supplementary Fig. 10 and Supplementary Movie 2).
PMID:39379376	FYPO:0008334	abolished ribosome to mitochondrion tethering	We then used in situ cryo-ET to assess whether ribosomal tethering to mitochondria was affected in the Δcpc2 strain. The tomograms showed fragmented circular mitochondria, as observed in WT cells, while no ribosome tethering was observed after 7 days of cells growing at low glucose concentrations (Fig. 5c, d, Supplementary Fig. 10 and Supplementary Movie 3).
PMID:39379376	FYPO:0009007	decreased vegetative cell population viability	While Δcpc2 cells did not display discernible growth defects under nutrient-rich conditions, significant growth impairments were evident when these cells were cultivated in defined EMM media supplemented with either 2% or 0.5% glucose concentrations.
PMID:39387272	FYPO:0004709	increased number of Rad52 foci [has_penetrance] 20	(Fig. 1A)
PMID:39387272	FYPO:0004709	increased number of Rad52 foci [has_penetrance] 25	(Fig. 1A)
PMID:39387272	FYPO:0004709	increased number of Rad52 foci [has_penetrance] 25	(Fig. 1A)
PMID:39387272	FYPO:0004709	increased number of Rad52 foci [has_penetrance] 12	(Fig. 2B)
PMID:39387272	FYPO:0001122	elongated vegetative cell [has_severity] medium	(Fig. 2B)
PMID:39387272	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 2E)
PMID:39387272	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 2E)
PMID:39387272	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 2E)
PMID:39387272	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 2E)
PMID:39387272	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 2E)
PMID:39387272	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 2E)
PMID:39387272	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 2E)
PMID:39387272	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 2E)
PMID:39387272	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 2E)
PMID:39387272	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 2E)
PMID:39387272	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 2E)
PMID:39387272	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 2E)
PMID:39387272	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 2E)
PMID:39387272	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 2E)
PMID:39387272	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 2E)
PMID:39387272	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 2E)
PMID:39387272	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 2E)
PMID:39387272	FYPO:0003660	decreased double-strand break repair during vegetative growth [has_penetrance] 30	(Fig. 3B)
PMID:39387272	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_severity] medium	(Fig. 4A)
PMID:39387272	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_severity] high	(Fig. 4A)
PMID:39387272	FYPO:0003912	decreased double-strand break repair via homologous recombination [has_severity] medium	(Fig. 4A)
PMID:39387272	FYPO:0004287	decreased double-strand break repair via nonhomologous end joining [has_severity] low	(Fig. 4B)
PMID:39387272	FYPO:0004287	decreased double-strand break repair via nonhomologous end joining [has_severity] high	(Fig. 4B)
PMID:39387272	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 5D)
PMID:39387272	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 5D)
PMID:39387272	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 5E)
PMID:39387272	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5E)
PMID:39387272	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5E)
PMID:39387272	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 5E)
PMID:39387272	FYPO:0004709	increased number of Rad52 foci [has_penetrance] 11	(Fig. 5G)
PMID:39387272	FYPO:0004709	increased number of Rad52 foci [has_penetrance] 15	(Fig. 5G)
PMID:39387272	FYPO:0004287	decreased double-strand break repair via nonhomologous end joining [has_severity] medium	(Fig. 5H)
PMID:39387272	FYPO:0004287	decreased double-strand break repair via nonhomologous end joining [has_severity] medium	(Fig. 5H)
PMID:39387272	FYPO:0001122	elongated vegetative cell [has_severity] high	(Fig. S1B)
PMID:39387272	FYPO:0001122	elongated vegetative cell [has_severity] medium	(Fig. S1B)
PMID:39387272	FYPO:0001122	elongated vegetative cell [has_severity] medium	(Fig. S1B)
PMID:39387272	FYPO:0001122	elongated vegetative cell [has_severity] low	(Fig. S1B)
PMID:39387272	FYPO:0001122	elongated vegetative cell [has_severity] low	(Fig. S1B)
PMID:39387272	FYPO:0001122	elongated vegetative cell [has_severity] high	(Fig. S1B)
PMID:39387272	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S1C)
PMID:39387272	FYPO:0000674	normal cell population growth at high temperature	(Fig. S1C)
PMID:39387272	FYPO:0000674	normal cell population growth at high temperature	(Fig. S1C)
PMID:39387272	FYPO:0000674	normal cell population growth at high temperature	(Fig. S1C)
PMID:39387272	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S1C)
PMID:39387272	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S1C)
PMID:39387272	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S1C)
PMID:39387272	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S1C)
PMID:39387272	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. S1C)
PMID:39387272	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S1C)
PMID:39387272	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. S1C)
PMID:39387272	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. S1C)
PMID:39387272	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S1C)
PMID:39387272	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S1C)
PMID:39387272	FYPO:0001357	normal vegetative cell population growth	(Fig. S1C)
PMID:39387272	FYPO:0001357	normal vegetative cell population growth	(Fig. S1C)
PMID:39387272	FYPO:0001357	normal vegetative cell population growth	(Fig. S1C)
PMID:39387272	FYPO:0001357	normal vegetative cell population growth	(Fig. S1C)
PMID:39387272	FYPO:0001122	elongated vegetative cell [has_severity] low	(Fig. S1D)
PMID:39387272	FYPO:0001122	elongated vegetative cell [has_severity] low	(Fig. S1D)
PMID:39387272	FYPO:0001122	elongated vegetative cell [has_severity] medium	(Fig. S1D)
PMID:39387272	FYPO:0001122	elongated vegetative cell [has_severity] high	(Fig. S1D)
PMID:39387272	FYPO:0001122	elongated vegetative cell [has_severity] low	(Fig. S1D)
PMID:39387272	FYPO:0001122	elongated vegetative cell [has_severity] low	(Fig. S1D)
PMID:39387272	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. S2B)
PMID:39387272	FYPO:0001357	normal vegetative cell population growth	(Fig. S2B)
PMID:39387272	FYPO:0001357	normal vegetative cell population growth	(Fig. S2B)
PMID:39387272	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. S2B)
PMID:39387272	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. S2B)
PMID:39387272	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. S2B)
PMID:39387272	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. S2B)
PMID:39387272	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. S2B)
PMID:39387272	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	(Fig. S2B)
PMID:39387272	FYPO:0001690	normal growth on camptothecin	(Fig. S2B)
PMID:39387272	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. S2B)
PMID:39387272	FYPO:0004287	decreased double-strand break repair via nonhomologous end joining [has_severity] medium	(Fig. S2C)
PMID:39387272	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC23C4.12	These data strongly suggest that S60 is an additional Hhp1 and Hhp2 phosphorylation site, and that S60, S62, S75, and S87 are the primary sites on Arp8 that are targeted by Hhp1 and Hhp2.
PMID:39387272	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC23C4.12	These data strongly suggest that S60 is an additional Hhp1 and Hhp2 phosphorylation site, and that S60, S62, S75, and S87 are the primary sites on Arp8 that are targeted by Hhp1 and Hhp2.
PMID:39387272	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC23C4.12	These data strongly suggest that S60 is an additional Hhp1 and Hhp2 phosphorylation site, and that S60, S62, S75, and S87 are the primary sites on Arp8 that are targeted by Hhp1 and Hhp2.
PMID:39387272	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC23C4.12	These data strongly suggest that S60 is an additional Hhp1 and Hhp2 phosphorylation site, and that S60, S62, S75, and S87 are the primary sites on Arp8 that are targeted by Hhp1 and Hhp2.
PMID:39471327	GO:1905047	mitotic spindle pole body organization	(Figure 7)
PMID:39471327	FYPO:0007652	mononucleate vegetative cell with mislocalized septum and anucleate compartment [has_penetrance] medium	. A 2 portion of ppc89-4 cells at 36°C showed an additional abnormal phenotype - cells with 3 a septum but only one nucleus (Figure 1C,D).
PMID:39471327	FYPO:0000674	normal cell population growth at high temperature	... so we tested whether tethering Sid4 to 23 Pcp1-GFP would rescue ppc89-3 and if so, ppc89-4 as well. ppc89-3 was rescued when Sid4 was tethered to Pcp1-GFP, as it had been when tethered to Ppc89-3 directly 2 (Figure S3D)
PMID:39471327	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC1739.11c	As expected, Dma1- 22 mNG, Cdc11-GFP and Mto1-mNG were lost from SPBs in ppc89-3 and ppc89-4 cells at 23 restrictive temperature, but Mto1-mNG localized normally to SPBs in ppc89(1-707) cells (Figures 4A-G; S2B and C)
PMID:39471327	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC1739.11c	As expected, Dma1- 22 mNG, Cdc11-GFP and Mto1-mNG were lost from SPBs in ppc89-3 and ppc89-4 cells at 23 restrictive temperature, but Mto1-mNG localized normally to SPBs in ppc89(1-707) cells (Figures 4A-G; S2B and C)
PMID:39471327	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC417.07c	As expected, Dma1- 22 mNG, Cdc11-GFP and Mto1-mNG were lost from SPBs in ppc89-3 and ppc89-4 cells at 23 restrictive temperature, but Mto1-mNG localized normally to SPBs in ppc89(1-707) cells (Figures 4A-G; S2B and C)
PMID:39471327	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC17G8.10c	As expected, Dma1- 22 mNG, Cdc11-GFP and Mto1-mNG were lost from SPBs in ppc89-3 and ppc89-4 cells at 23 restrictive temperature, but Mto1-mNG localized normally to SPBs in ppc89(1-707) cells (Figures 4A-G; S2B and C)
PMID:39471327	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC17G8.10c	As expected, Dma1- 22 mNG, Cdc11-GFP and Mto1-mNG were lost from SPBs in ppc89-3 and ppc89-4 cells at 23 restrictive temperature, but Mto1-mNG localized normally to SPBs in ppc89(1-707) cells (Figures 4A-G; S2B and C)
PMID:39471327	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPCC417.07c	As expected, Dma1- 22 mNG, Cdc11-GFP and Mto1-mNG were lost from SPBs in ppc89-3 and ppc89-4 cells at 23 restrictive temperature, but Mto1-mNG localized normally to SPBs in ppc89(1-707) cells (Figures 4A-G; S2B and C)
PMID:39471327	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC244.01c	At 25°C, Sid4-GFP SPB intensity was reduced by 4 approximately 30% in ppc89-3 and 60% in ppc89-4 compared to wild-type (Figures 2A 5 and S2A). At 36°C, Sid4-GFP SPB intensity was further reduced by ~90% in ppc89-3 6 and ppc89-4 compared to wild-type (Figure 2A,B). These results indicate that the Sid4- 7 Ppc89 interaction is disrupted in both ppc89-3 and ppc89-4 cells at restrictive 8 temperatu re.
PMID:39471327	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC244.01c	At 25°C, Sid4-GFP SPB intensity was reduced by 4 approximately 30% in ppc89-3 and 60% in ppc89-4 compared to wild-type (Figures 2A 5 and S2A). At 36°C, Sid4-GFP SPB intensity was further reduced by ~90% in ppc89-3 6 and ppc89-4 compared to wild-type (Figure 2A,B). These results indicate that the Sid4- 7 Ppc89 interaction is disrupted in both ppc89-3 and ppc89-4 cells at restrictive 8 temperatu re.
PMID:39471327	FYPO:0003245	telophase nuclear clustering	At 36°C, ppc89-2 and ppc89-3 displayed an increased proportion of binucleate cells with “kissing” nuclei in which nuclei return to the cell center after a failed cytokinesis as well as cell lysis (Figure 1C,D)
PMID:39471327	FYPO:0000647	vegetative cell lysis	At 36°C, ppc89-2 and ppc89-3 displayed an increased proportion of binucleate cells with “kissing” nuclei in which nuclei return to the cell center after a failed cytokiness as well as cell lysis (Figure 1C,D)
PMID:39471327	FYPO:0000647	vegetative cell lysis	At 36°C, ppc89-2 and ppc89-3 displayed an increased proportion of binucleate cells with “kissing” nuclei in which nuclei return to the cell center after a failed cytokiness as well as cell lysis (Figure 1C,D)
PMID:39471327	FYPO:0003245	telophase nuclear clustering	At 36°C, ppc89-2 and ppc89-3 displayed an increased proportion of binucleate cells with “kissing” nuclei in which nuclei return to the cell center after a failed cytokiness as well as cell lysis (Figure 1C,D)
PMID:39471327	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC244.01c	Both Ppc89(1-707)-mNG and Sid4-RFP 8 localized to the SPB with comparable intensity to wild-type at both 25 ̊C and 36°C 9 (Figure 3D,E).
PMID:39471327	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC4H3.11c	Both Ppc89(1-707)-mNG and Sid4-RFP 8 localized to the SPB with comparable intensity to wild-type at both 25 ̊C and 36°C 9 (Figure 3D,E).
PMID:39471327	FYPO:0000082	decreased cell population growth at high temperature [has_severity] medium	Can grow at 32°C but not at 36°C | Sid4 tethered to 4 the SPB via Pcp1-GFP did not rescue growth of ppc89-4 cells at 36°C but the ppc89-4 5 pcp1-GFP sid4-mCherry strain grew at 32°C, and imaging confirmed that Sid4-GBP- 6 mCherry but not Sid4-mCherry was present at the SPB at 36 ̊C (Figures 5B and S4A).
PMID:39471327	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC4H3.11c	In contrast, Ppc89-4-mNG showed a ~50% reduction in SPB 12 fluorescence intensity at both temperatures compared to wild-type (Figures 1E, F and 13 S1A).
PMID:39471327	FYPO:0001475	fragmented mitotic spindle pole body	In ppc89-3 cells at the restrictive temperature, we noticed an increased proportion 14 of cells displaying 2 or 4 Ppc89-3-mNG and Sad1-mCherry foci, indicative of cytokinesis 15 failure (Figure 1G,H). In contrast, ppc89-4 cells displayed 3, 4, or ≥5 Ppc89-4-mNG and 16 Sad1-mCherry foci (Figure 1G,H), indicating that the integrity of the SPB as a whole is 17 disrupted in ppc89-4 cells whereas it appears to remain intact in ppc89-3 cells.
PMID:39471327	FYPO:0001475	fragmented mitotic spindle pole body	Interestingly we found that the additional foci of Ppc89-4, 11 observed in 169/280 cells that progressed through mitosis during the movies, always 12 formed during anaphase by splitting off from one of the two SPBs (Figure 7A). By 13 determining the intensity of the two SPBs before and after foci appeared, we confirmed 14 that the fragments originated from one SPB because the fluorescence intensity of that 15 SPB always diminished relative to the second SPB (Figure 7B).
PMID:39471327	FYPO:0007652	mononucleate vegetative cell with mislocalized septum and anucleate compartment	Moreover, we found that 5 ppc89(1-707)-mNG cells accumulated mononucleated, septated cells and anucleate cell 6 compartments (Figure 6C,D) as well as multiple Ppc89 foci (Figure 6E and S4B).
PMID:39471327	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC8D2.05c	Neither Sfi1-mCherry nor 7 Sad1-mCherry signal were reduced in ppc89-3 or ppc89-4 cells (Figure S3A,B).
PMID:39471327	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC8D2.05c	Neither Sfi1-mCherry nor 7 Sad1-mCherry signal were reduced in ppc89-3 or ppc89-4 cells (Figure S3A,B).
PMID:39471327	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC6G9.06c	Pcp1 showed ~50% 9 reduction in pcp89-4 cells (Figure S3C)
PMID:39471327	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPAC4H3.11c	Ppc89-3-mNG localized to the 10 SPB at both permissive and restrictive temperatures similarly to Ppc89-mNG (Figures 11 1E, F and S1A).
PMID:39471327	FYPO:0007652	mononucleate vegetative cell with mislocalized septum and anucleate compartment [has_penetrance] high	The addition of the tagged sid4 and pcp1 alleles 13 exacerbated the cell growth (Figures 5B and S3D) and cell division defects of the ppc89 14 ts alleles (Figures 1C,D and 5C,D) In contrast, ppc89-4 cells with Sid4 tethered to the SPB displayed a significant 17 percentage of uninucleate cells with an off-center septum and also multiple Ppc89-4 foci 18 (Figures 5C,D and S4).
PMID:39471327	FYPO:0007742	premature actomyosin contractile ring assembly during mitotic interphase	We also determined 16 that the rarer off-center septum phenotype (9 of 280 cells) arose because a second 17 cytokinetic ring formed at the new cell end of one daughter cell after its birth (Figure 18 7C). In these cells, the cytokinetic ring appeared not to fully disassemble and one 19 daughter inherited this cortical material. Then, a second cytokinetic ring formed at 20 variable times relative to completion of the previous division where the first cytokinetic 21 ring remnants were located (Figure 7C).
PMID:39471327	FYPO:0000082	decreased cell population growth at high temperature	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0000082	decreased cell population growth at high temperature	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0002150	inviable spore population	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0002150	inviable spore population	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0000082	decreased cell population growth at high temperature	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0000082	decreased cell population growth at high temperature	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0000082	decreased cell population growth at high temperature	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0000082	decreased cell population growth at high temperature	We found 22 that ppc89-3 was synthetically lethal with sid4-SA1 and synthetically sick with spg1-106, 23 mob1-R4, and plo1-25 (Figure S1B,C).
PMID:39471327	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	ppc89(1-707)-mNG cells were 7 viable but temperature-sensitive (Figure 3C).
PMID:39471327	FYPO:0000082	decreased cell population growth at high temperature	ppc89-2, ppc89-3 and ppc89-4 grow 19 similarly to wild-type at 25°C but do not form colonies at 36°C (Figure 1B
PMID:39471327	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	ppc89-2, ppc89-3 and ppc89-4 grow 19 similarly to wild-type at 25°C but do not form colonies at 36°C (Figure 1B
PMID:39471327	FYPO:0000082	decreased cell population growth at high temperature	ppc89-2, ppc89-3 and ppc89-4 grow 19 similarly to wild-type at 25°C but do not form colonies at 36°C (Figure 1B
PMID:39471327	FYPO:0002150	inviable spore population	ppc89-4 was also synthetically lethal with sid4- 12 Downloaded from https://academic.oup.com/g3journal/advance-article/doi/10.1093/g3journal/jkae249/7848890 by guest on 01 November 2024 1 SA1 (Figure S1C)
PMID:39471327	FYPO:0002150	inviable spore population	ppc89-4 was also synthetically lethal with sid4- 12 Downloaded from https://academic.oup.com/g3journal/advance-article/doi/10.1093/g3journal/jkae249/7848890 by guest on 01 November 2024 1 SA1 (Figure S1C)
PMID:39471327	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	ppc89-L756P,I770V was 3 temperature-sensitive and accumulated cells with one nucleus and a septum (Figure 4 6B-D), reminiscent of what we observed in ppc89-4 cells
PMID:39471327	FYPO:0007652	mononucleate vegetative cell with mislocalized septum and anucleate compartment	ppc89-L756P,I770V was 3 temperature-sensitive and accumulated cells with one nucleus and a septum (Figure 4 6B-D), reminiscent of what we observed in ppc89-4 cells| Moreover, we found that 5 ppc89(1-707)-mNG cells accumulated mononucleated, septated cells and anucleate cell 6 compartments (Figure 6C,D) as well as multiple Ppc89 foci (Figure 6E and S4B).
PMID:39471327	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC902.06	we also observed a reduction 3 in Mto2-mNG SPB signal at 36 ̊C in ppc89-3 and ppc89-4 compared to wild-type (Figure 4 S2D,E).
PMID:39471327	FYPO:0000940	decreased protein localization to mitotic spindle pole body [assayed_protein] PomBase:SPBC902.06	we also observed a reduction 3 in Mto2-mNG SPB signal at 36 ̊C in ppc89-3 and ppc89-4 compared to wild-type (Figure 4 S2D,E).
PMID:39473973	PomGeneEx:0000018	protein level increased [during] cellular response to heat	(Fig. 1D)
PMID:39473973	PomGeneEx:0000018	protein level increased [in_presence_of] L-canavanine	(Fig. 1F)
PMID:39473973	FYPO:0004545	decreased proteasomal ubiquitin-dependent protein degradation	(Fig. 2)
PMID:39473973	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 2A and B)
PMID:39473973	FYPO:0004545	decreased proteasomal ubiquitin-dependent protein degradation	(Fig. 2D)
PMID:39473973	FYPO:0004808	increased cellular protein aggregate level during cellular response to heat [assayed_protein] PomBase:SPBC106.16	(Fig. 2E)
PMID:39473973	FYPO:0004056	decreased protein localization to nucleus, with protein mislocalized to cytoplasm [assayed_protein] PomBase:SPBP19A11.03c	(Fig. 2G)
PMID:39473973	FYPO:0005382	delayed exit from meiosis	(Fig. 3A)
PMID:39473973	PomGeneEx:0000018	protein level increased [in_presence_of] bortezomib	(Fig. 4A)
PMID:39473973	FYPO:0006606	abnormal dynamic protein localization pattern [assayed_protein] PomBase:SPAC2E12.02	(Fig. 4B)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPBC16D10.08c [has_severity] high	(Fig. 4C and Fig. S4A)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPAC13G7.02c	(Fig. 4D)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPAC13G7.02c	(Fig. 4E)
PMID:39473973	FYPO:0006100	decreased protein localization to cytoplasm, with protein mislocalized to nucleus [assayed_protein] PomBase:SPBP19A11.03c [has_severity] medium	(Fig. 5A)
PMID:39473973	FYPO:0004056	decreased protein localization to nucleus, with protein mislocalized to cytoplasm [assayed_protein] PomBase:SPBP19A11.03c	(Fig. 5A)
PMID:39473973	FYPO:0006100	decreased protein localization to cytoplasm, with protein mislocalized to nucleus [assayed_protein] PomBase:SPBP19A11.03c	(Fig. 5A)
PMID:39473973	FYPO:0006606	abnormal dynamic protein localization pattern [assayed_protein] PomBase:SPAC2E12.02	(Fig. 5B)
PMID:39473973	FYPO:0006606	abnormal dynamic protein localization pattern [assayed_protein] PomBase:SPAC2E12.02	(Fig. 5B)
PMID:39473973	FYPO:0006606	abnormal dynamic protein localization pattern [assayed_protein] PomBase:SPAC2E12.02	(Fig. 5B)
PMID:39473973	FYPO:0006606	abnormal dynamic protein localization pattern [assayed_protein] PomBase:SPAC2E12.02	(Fig. 5B)
PMID:39473973	FYPO:0006606	abnormal dynamic protein localization pattern [assayed_protein] PomBase:SPAC2E12.02	(Fig. 5B)
PMID:39473973	FYPO:0000021	spheroid vegetative cell	(Fig. S2A)
PMID:39473973	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S2B and C)
PMID:39473973	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S2C)
PMID:39473973	FYPO:0000229	cut [has_penetrance] 8.1	(Fig. S2E)
PMID:39473973	FYPO:0002774	increased level of ubiquitinated protein in cell during vegetative growth	(Fig. S2G)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPBC16D10.08c	(Fig. S3B)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPBC16D10.08c	(Fig. S3D)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPBC16D10.08c	(Fig. S3D)
PMID:39473973	FYPO:0000099	sensitive to canavanine [has_severity] low	(Fig. S3E)
PMID:39473973	FYPO:0000099	sensitive to canavanine [has_severity] high	(Fig. S3E)
PMID:39473973	FYPO:0004056	decreased protein localization to nucleus, with protein mislocalized to cytoplasm [assayed_protein] PomBase:SPAC2E12.02	(Fig. S3F)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPAC13G7.02c	(Fig. S3G)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPAC13G7.02c	(Fig. S3G)
PMID:39473973	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S3H)
PMID:39473973	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S3H)
PMID:39473973	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S3H)
PMID:39473973	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S3H)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPBC16D10.08c [has_severity] medium	(Fig. S4A)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPBC16D10.08c [has_severity] low	(Fig. S4A)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPBC16D10.08c [has_severity] low	(Fig. S4A)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPBC16D10.08c [has_severity] medium	(Fig. S4A)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPBC16D10.08c [has_severity] medium	(Fig. S4A)
PMID:39473973	FYPO:0000836	increased protein level [assayed_protein] PomBase:SPBC16D10.08c [has_severity] medium	(Fig. S4A)
PMID:39473973	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S4B)
PMID:39473973	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S4B)
PMID:39473973	GO:0080129	proteasome core complex assembly	The increased proteasome activity correlates with the upregulation of the 20S CP assembly chaperone Ump1 and with an increase in proteasome assembly. Ump1 inactivation compromises 20S proteasome assembly, resulting in a drop in mature 26S/30S proteasomes.
PMID:39476757	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B and E)
PMID:39476757	FYPO:0002141	normal cell population growth at low temperature	(Fig. 1B)
PMID:39476757	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 1B)
PMID:39476757	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 1D, E and F)
PMID:39476757	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC8E4.01c	(Table S1)
PMID:39476757	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC1198.14c	(Table S1)
PMID:39476757	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC16D10.06	(Table S1)
PMID:39476757	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC24B10.18	(Table S1)
PMID:39476757	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC144.04c	(Table S1)
PMID:39476757	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC543.07	(Table S1)
PMID:39476757	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC609.04	(Table S1)
PMID:39476757	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC4B4.08	(Table S1)
PMID:39476757	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC30D11.11	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC17G6.13	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC2D10.20	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC576.15c	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC1235.14	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC4F6.17c	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC16D10.08c	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC513.07	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC3B9.01	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC13G7.05	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC887.15c	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC19C7.04c	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC1289.14	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC550.06c	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC1271.05c	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCC18B5.01c	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBP4G3.03	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC186.05c	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPCPB16A4.05c	(Table S1)
PMID:39476757	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPBC8E4.03	(Table S1)
PMID:39477503	FYPO:0005547	decreased protein targeting to vacuole, with protein secreted	1 showed that the signal peptide and the transmembrane including DUF3844 domain were 2 essential for this function (Fig. 4A).
PMID:39477503	FYPO:0001423	normal protein targeting to vacuole	1 showed that the signal peptide and the transmembrane including DUF3844 domain were 2 essential for this function (Fig. 4A).
PMID:39477503	FYPO:0001423	normal protein targeting to vacuole	1 showed that the signal peptide and the transmembrane including DUF3844 domain were 2 essential for this function (Fig. 4A).
PMID:39477503	FYPO:0005547	decreased protein targeting to vacuole, with protein secreted	1 showed that the signal peptide and the transmembrane including DUF3844 domain were 2 essential for this function (Fig. 4A).
PMID:39477503	FYPO:0005547	decreased protein targeting to vacuole, with protein secreted	1 showed that the signal peptide and the transmembrane including DUF3844 domain were 2 essential for this function (Fig. 4A).
PMID:39477503	FYPO:0001423	normal protein targeting to vacuole [assayed_protein] PomBase:SPAC1006.01	Although the Vps3844 protein is important for the transport of 26 CPY into the vacuole, Isp6-GFP and Psp3-GFP were found to localize in the vacuolar lumen 27 in vps3844Δ cells (Fig. S5).
PMID:39477503	FYPO:0001423	normal protein targeting to vacuole [assayed_protein] PomBase:SPAC4A8.04	Although the Vps3844 protein is important for the transport of 26 CPY into the vacuole, Isp6-GFP and Psp3-GFP were found to localize in the vacuolar lumen 27 in vps3844Δ cells (Fig. S5).
PMID:39477503	FYPO:0000080	decreased cell population growth at low temperature	Growth of the vps3844Δ strain was significantly inhibited at low temperature (Fig. 2B).
PMID:39477503	FYPO:0005547	decreased protein targeting to vacuole, with protein secreted	To confirm that SPBC1709.03 is a VPS gene, extracellular leakage of CPY was assessed 17 by colony blot assay (Fig. 1C). Relative to wild type (WT), the SPBC1709.03 deletion strain 18 showed higher chemiluminescence intensity of CPY, indicating an increased occurrence of 19 CPY mis-sorting to the cell surface.
PMID:39485795	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:39485795	GO:0110134	meiotic drive	(Fig. 1C and D)
PMID:39485795	FYPO:0000579	normal spore germination	(Fig. 1C)
PMID:39485795	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] high	(Fig. 2B and C)
PMID:39485795	FYPO:0000579	normal spore germination	(Fig. 3B and C)
PMID:39485795	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 4C)
PMID:39485795	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 4C)
PMID:39485795	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 4D)
PMID:39485795	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 4D)
PMID:39485795	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 4D)
PMID:39485795	FYPO:0006790	meiotic drive suppression [has_severity] high	(Fig. 4E)
PMID:39485795	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 4K)
PMID:39485795	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 4K)
PMID:39485795	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 4K)
PMID:39485795	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 4K)
PMID:39485795	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 4K)
PMID:39485795	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 4K)
PMID:39485795	FYPO:0001571	increased protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 5C)
PMID:39485795	FYPO:0001571	increased protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 5C)
PMID:39485795	FYPO:0001571	increased protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. 5C)
PMID:39485795	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 5D)
PMID:39485795	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 5D)
PMID:39485795	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 5D)
PMID:39485795	FYPO:0000141	abnormal mitotic sister chromatid segregation [has_severity] high	(Fig. 5E and F)
PMID:39485795	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S10A)
PMID:39485795	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S10A)
PMID:39485795	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S10A)
PMID:39485795	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S10A)
PMID:39485795	FYPO:0001571	increased protein-protein interaction [assayed_protein] PomBase:SPCC1450.02 [assayed_protein] PomBase:SPCC330.04c	(Fig. S10B)
PMID:39485795	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC330.04c [assayed_protein] PomBase:SPAC631.02	(Fig. S9C)
PMID:39485795	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC330.04c [assayed_protein] PomBase:SPAC631.02	(Fig. S9D)
PMID:39485795	GO:0140463	chromatin-protein adaptor activity [has_input] PomBase:SPCC330.04c [part_of] meiotic drive	These results suggest that the only role of Bdf1 in Tdk1-mediated killing is to bridge an association between Tdk1 and acetylated histones, leading to the attachment of Tdk1 to chromosomes. (Fig. 6)
PMID:39485800	GO:0005654	nucleoplasm [exists_during] single-celled organism vegetative growth phase	(Fig. 2A)
PMID:39485800	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC330.04c [assayed_protein] PomBase:SPCC1450.02	(Fig. 3A)
PMID:39485800	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC330.04c [assayed_protein] PomBase:SPCC1450.02	(Fig. 3A)
PMID:39485800	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC330.04c [assayed_protein] PomBase:SPCC1450.02	(Fig. 3A)
PMID:39485800	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC330.04c [assayed_protein] PomBase:SPCC1450.02	(Fig. 3A)
PMID:39485800	FYPO:0005116	increased punctate nuclear protein localization [assayed_protein] PomBase:SPCC330.04c	(Fig. 3B)
PMID:39485800	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3E)
PMID:39485800	FYPO:0002150	inviable spore population	(Fig. 6A and B)
PMID:39502420	FYPO:0002271	growth auxotrophic for glutamine [has_penetrance] high [has_severity] high	Arginine, glutamic acid, or proline weakly support growth with an ammonium nitrogen source. The mutant grows normally when these amino acids are used as the sole nitrogen source. The mutant cannot utilize aspartic acid and asparagine as the sole nitrogen source.
PMID:39502420	GO:0015139	alpha-ketoglutarate transmembrane transporter activity [part_of] mitochondrial alpha-ketoglutarate transmembrane transport	In addition to glu1/maa1, the yhm2 gene (SPBC83.13) is a multicopy weak suppressor of the growth defect in the glu1-NS176 mutant. The glu1 mutant harboring the multicopy yhm2+ plasmid grew slower than the glu1-corrected, wild-type strain (maa1+ (integrated); Figure 1B). The Yhm2 homolog in Saccharomyces cerevisiae is a mitochondrial carrier protein that imports 2-oxoglutarate into the mitochondria (Castegna et al., 2010). Therefore, increasing the 2-oxoglutarate concentration in mitochondria may alleviate the ammonium utilization defect in the glu1-NS176 mutant. The yhm2∆ strain showed no growth defects under all medium conditions examined, whereas the glu1 and yhm2∆ mutations had an additive effect. The glu1-NS176 yhm2∆ double mutant grew slower than each single mutant in yeast extract medium (Figure 1F). The S. pombe glu1-NS176 yhm2∆ double mutant grew when amino acids, except aspartate and asparagine, were used as the sole nitrogen source (Figure 1F). Interestingly, all the tested amino acids, including glutamine, did not support the growth of double mutant in the presence of ammonium. S. cerevisiae mutants, which lack all mitochondrial 2-oxoglutarate carriers including Yhm2, cannot grow when ammonium is the sole nitrogen source, and importantly, this growth defect is rescued by the addition of glutamate (Palmieri et al., 2001, Castegna et al., 2010, Scarcia et al., 2017).
PMID:39502420	FYPO:0001357	normal vegetative cell population growth	Interestingly, glutamine efficiently rescues the growth defect of the glu1 mutant compared to glutamate, even in the presence of ammonium (Figure 1F, Barel and MacDonald 1993).
PMID:39502420	GO:0004069	L-aspartate:2-oxoglutarate transaminase activity [part_of] L-glutamate biosynthetic process [happens_during] cellular response to nitrogen starvation	It catalyzes the transamination between oxaloacetate and glutamate, leading to the formation of aspartate and 2-oxoglutarate (Figure 1A). phenotypes support glutamate production. evidence also supports that this ebzyme would normally be other direction? on rich nitrogen source
PMID:39502420	FYPO:0000249	decreased cell population growth on ammonia nitrogen source [has_severity] high	The glu1 mutant grew when glutamate was used as the sole nitrogen source, although glutamate poorly supported its growth in the presence of ammonium (Figures 1B and F). ( In general, their availability is regulated by nitrogen catabolite repression; thus, it is greatly affected by the presence of ammonium, a high-quality nitrogen source.)
PMID:39502420	FYPO:0000242	normal growth on ammonia nitrogen source [has_severity] high	The glu1-NS176 mutation was rescued by sup3-5 (Figure 1E), a tRNASer (SPATRNASER.03) suppressor mutation that suppresses the TGAopal nonsense codon (Hottinger et al., 1982, Niwa et al., 1989). This is direct proof that the observed growth defect in the ammonium medium is caused by the maa1 gene nonsense mutation in the glu1- NS176 strain.
PMID:39502420	FYPO:0000242	normal growth on ammonia nitrogen source [has_severity] high	The glu1-NS176 mutation was rescued by sup3-5 (Figure 1E), a tRNASer (SPATRNASER.03) suppressor mutation that suppresses the TGAopal nonsense codon (Hottinger et al., 1982, Niwa et al., 1989). This is direct proof that the observed growth defect in the ammonium medium is caused by the maa1 gene nonsense mutation in the glu1- NS176 strain.
PMID:39502420	FYPO:0000249	decreased cell population growth on ammonia nitrogen source [has_severity] high	yhm2+ works as a dosage suppressor of auxotrophic growth defect in the maa1 (glu1) mutant.
PMID:39502420	FYPO:0000249	decreased cell population growth on ammonia nitrogen source [has_severity] high	yhm2+ works as a dosage suppressor of auxotrophic growth defect in the maa1 (glu1) mutant.
PMID:39509469	FYPO:0007450	decreased maintenance of protein location in cell cortex of cell tip [assayed_protein] PomBase:SPBC1706.01	(Fig. 1A, B and F)
PMID:39509469	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [assayed_protein] PomBase:SPCC1223.06	(Fig. 1C)
PMID:39509469	FYPO:0007182	decreased cytoplasmic microtubule depolymerization at plus end at cell tip	(Fig. 1G)
PMID:39509469	FYPO:0004511	long curved interphase microtubules [has_severity] medium	(Fig. 1H)
PMID:39509469	FYPO:0004511	long curved interphase microtubules [has_severity] high	(Fig. 1H)
PMID:39509469	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [has_severity] medium [assayed_protein] PomBase:SPBC1706.01	(Fig. 2A)
PMID:39509469	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [assayed_protein] PomBase:SPBC1706.01 [has_severity] high	(Fig. 2A)
PMID:39509469	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 80	(Fig. 2B)
PMID:39509469	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 55	(Fig. 2B)
PMID:39509469	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 80	(Fig. 2B)
PMID:39509469	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 85	(Fig. 2B)
PMID:39509469	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 65	(Fig. 2B)
PMID:39509469	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 65	(Fig. 2B)
PMID:39509469	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 55	(Fig. 2B)
PMID:39509469	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 55	(Fig. 2B)
PMID:39509469	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 70	(Fig. 2B)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 18	(Fig. 2C)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 23	(Fig. 2C)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 20	(Fig. 2C)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 18	(Fig. 2C)
PMID:39509469	FYPO:0006776	decreased phosphatidylinositol-4-phosphate binding [assayed_protein] PomBase:SPCC645.07	(Fig. 3E)
PMID:39509469	GO:0070273	phosphatidylinositol-4-phosphate binding	(Fig. 3E)
PMID:39509469	FYPO:0000929	decreased protein localization to cell cortex during vegetative growth [assayed_protein] PomBase:SPCC645.07	(Fig. 3F)
PMID:39509469	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [assayed_protein] PomBase:SPCC645.07	(Fig. 3G)
PMID:39509469	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPCC645.07	(Fig. 3H)
PMID:39509469	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC645.07 [has_severity] medium	(Fig. 3H)
PMID:39509469	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [assayed_protein] PomBase:SPBC1706.01	(Fig. 4A)
PMID:39509469	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [assayed_protein] PomBase:SPBC1706.01	(Fig. 4A)
PMID:39509469	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [assayed_protein] PomBase:SPBC1706.01	(Fig. 4A)
PMID:39509469	FYPO:0001529	decreased GTP binding [assayed_protein] PomBase:SPAC1F7.04 [has_severity] medium	(Fig. 4B)
PMID:39509469	FYPO:0001529	decreased GTP binding [assayed_protein] PomBase:SPAC1F7.04 [has_severity] medium	(Fig. 4B)
PMID:39509469	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPCC645.07 [assayed_protein] PomBase:SPBC1706.01	(Fig. 4C)
PMID:39509469	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPCC645.07 [assayed_protein] PomBase:SPBC1706.01	(Fig. 4D)
PMID:39509469	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 45	(Fig. 4E)
PMID:39509469	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 60	(Fig. 4E)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 65	(Fig. 5B)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 50	(Fig. 5C)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 5	(Fig. 5C)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 48	(Fig. 5C)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 48	(Fig. 5C)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 50	(Fig. 5C)
PMID:39509469	PomGeneEx:0000019	protein level decreased [in_presence_of] potassium chloride	(Fig. 5E)
PMID:39509469	PomGeneEx:0000019	protein level decreased [during] cellular response to heat	(Fig. 5E)
PMID:39509469	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [assayed_protein] PomBase:SPCC1223.06	(Fig. S1D)
PMID:39509469	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [assayed_protein] PomBase:SPCC1223.06	(Fig. S2A)
PMID:39509469	FYPO:0001529	decreased GTP binding [assayed_protein] PomBase:SPAC1F7.04 [has_severity] medium	(Fig. S4C)
PMID:39509469	FYPO:0000929	decreased protein localization to cell cortex during vegetative growth [has_severity] high	(Fig. S4D)
PMID:39509469	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [assayed_protein] PomBase:SPBC1706.01	(Fig. S4E)
PMID:39509469	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 50	(Fig. S4G)
PMID:39509469	FYPO:0002848	T-shaped cell during recovery from stationary phase [has_penetrance] 50	(Fig. S4G)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 25	(Fig. S5B)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 40	(Fig. S5B)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 33	(Fig. S5B)
PMID:39509469	FYPO:0000801	abnormal actin cytoskeleton organization during vegetative growth	(Fig. S5C)
PMID:39509469	PomGeneEx:0000019	protein level decreased [in_presence_of] latrunculin A	(Fig. S5D)
PMID:39509469	FYPO:0001789	normal protein localization to nucleus during cellular response to oxidative stress [assayed_protein] PomBase:SPAC24B11.06c	(Fig. S5G)
PMID:39509469	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPBC29B5.01	(Fig. S5H)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 50	(Fig. S5J)
PMID:39509469	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 50	(Fig. S5J)
PMID:39509469	GO:0061245	establishment or maintenance of bipolar cell polarity	Through Rho1 activation, Rgf1 stabilizes Tea4 at the cell ends, promoting its accumulation. Additionally, we described an alternative actin-dependent mechanism, driven by Rgf1 and Rho1, for marking the poles independently to the known MT- and Tea-dependent pathway.
PMID:39520300	GO:0140693	molecular condensate scaffold activity	(Figure 1)
PMID:39520300	GO:0140693	molecular condensate scaffold activity	(Figure 1)
PMID:39520300	GO:0140693	molecular condensate scaffold activity	(Figure 2)
PMID:39520300	GO:0140693	molecular condensate scaffold activity	(Figure 2)
PMID:39520300	GO:0140693	molecular condensate scaffold activity	(Figure 2)
PMID:39540318	FYPO:0001885	decreased protein phosphorylation during salt stress [has_severity] medium [assayed_protein] PomBase:SPBC119.08	(Fig. 1A and Fig. 4A)
PMID:39540318	FYPO:0001885	decreased protein phosphorylation during salt stress [assayed_protein] PomBase:SPBC119.08 [has_severity] low	(Fig. 1B)
PMID:39540318	FYPO:0002376	decreased protein phosphorylation during cellular response to osmotic stress [has_severity] medium [assayed_protein] PomBase:SPBC119.08	(Fig. 1C)
PMID:39540318	FYPO:0002376	decreased protein phosphorylation during cellular response to osmotic stress [assayed_protein] PomBase:SPBC119.08 [has_severity] high	(Fig. 1D)
PMID:39540318	FYPO:0002290	normal protein phosphorylation during cellular response to osmotic stress [assayed_protein] PomBase:SPBC119.08	(Fig. 1E)
PMID:39540318	FYPO:0004450	normal protein phosphorylation during cellular response to calcium ion [assayed_protein] PomBase:SPBC119.08	(Fig. 1G)
PMID:39540318	FYPO:0004422	normal protein phosphorylation [assayed_protein] PomBase:SPBC119.08	(Fig. 1H)
PMID:39540318	FYPO:0004154	normal protein phosphorylation during cellular response to heat [assayed_protein] PomBase:SPBC119.08	(Fig. 1I)
PMID:39540318	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39540318	FYPO:0001473	resistance to tacrolimus during salt stress [has_severity] high	(Fig. 2B)
PMID:39540318	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39540318	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39540318	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39540318	FYPO:0001357	normal vegetative cell population growth	(Fig. 2B)
PMID:39540318	FYPO:0001473	resistance to tacrolimus during salt stress [has_severity] high	(Fig. 2B)
PMID:39540318	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPBC119.08 [has_severity] low	(Fig. 2D)
PMID:39540318	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08 [has_severity] high	(Fig. 2D)
PMID:39540318	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPBC119.08 [has_severity] medium	(Fig. 2D)
PMID:39540318	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08 [has_severity] high	(Fig. 2D)
PMID:39540318	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPBC119.08 [has_severity] high	(Fig. 2D)
PMID:39540318	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPBC119.08 [has_severity] low	(Fig. 2D)
PMID:39540318	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_protein] PomBase:SPCC645.07	(Fig. 3A)
PMID:39540318	FYPO:0004468	decreased protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPCC645.07 [has_penetrance] 60 [has_severity] high	(Fig. 3A)
PMID:39540318	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. 3B)
PMID:39540318	FYPO:0004468	decreased protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c [has_severity] high [has_penetrance] 70	(Fig. 3B)
PMID:39540318	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_protein] PomBase:SPAC1F3.02c	(Fig. 3C)
PMID:39540318	FYPO:0004468	decreased protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPAC1F3.02c [has_penetrance] 40	(Fig. 3C)
PMID:39540318	FYPO:0008376	abolished protein localization to cell cortex of cell tip during cellular response to osmotic stress [assayed_protein] PomBase:SPBC12D12.04c [has_penetrance] 50	(Fig. 4C)
PMID:39540318	FYPO:0008376	abolished protein localization to cell cortex of cell tip during cellular response to osmotic stress [assayed_protein] PomBase:SPBC12D12.04c [has_penetrance] 30	(Fig. 4C)
PMID:39540318	FYPO:0008376	abolished protein localization to cell cortex of cell tip during cellular response to osmotic stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. 4C)
PMID:39540318	FYPO:0008376	abolished protein localization to cell cortex of cell tip during cellular response to osmotic stress [assayed_protein] PomBase:SPBC12D12.04c [has_penetrance] 30	(Fig. 5A and 5C)
PMID:39540318	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPBC119.08 [has_severity] high	(Fig. 5B)
PMID:39540318	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [has_severity] medium [assayed_protein] PomBase:SPBC119.08	(Fig. 5B)
PMID:39540318	FYPO:0008370	increased protein localization to cell surface during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c [has_penetrance] 10	(Fig. 5C)
PMID:39540318	FYPO:0008370	increased protein localization to cell surface during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c [has_penetrance] 20	(Fig. 5C)
PMID:39540318	FYPO:0008371	decreased protein localization to cell surface during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c [has_penetrance] 15	(Fig. 5C)
PMID:39540318	FYPO:0008370	increased protein localization to cell surface during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c [has_penetrance] 10	(Fig. 5C)
PMID:39540318	FYPO:0008370	increased protein localization to cell surface during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c [has_penetrance] 10	(Fig. 5C)
PMID:39540318	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [has_severity] low [assayed_protein] PomBase:SPBC119.08	(Fig. 5E)
PMID:39540318	FYPO:0001885	decreased protein phosphorylation during salt stress [assayed_protein] PomBase:SPBC119.08 [has_severity] low	(Fig. 5E)
PMID:39540318	FYPO:0008376	abolished protein localization to cell cortex of cell tip during cellular response to osmotic stress [assayed_protein] PomBase:SPCC645.07 [has_penetrance] 40	(Fig. 5F)
PMID:39540318	FYPO:0008371	decreased protein localization to cell surface during cellular response to salt stress [assayed_protein] PomBase:SPAC1F3.02c [has_penetrance] 40	(Fig. 5F)
PMID:39540318	FYPO:0004467	normal protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. 5G)
PMID:39540318	FYPO:0004467	normal protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. 5G)
PMID:39540318	FYPO:0004467	normal protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. 5G)
PMID:39540318	FYPO:0001266	normal protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPBC119.08	(Fig. 5H)
PMID:39540318	FYPO:0001885	decreased protein phosphorylation during salt stress [has_severity] medium [assayed_protein] PomBase:SPBC119.08	(Fig. 5H)
PMID:39540318	FYPO:0008376	abolished protein localization to cell cortex of cell tip during cellular response to osmotic stress [assayed_protein] PomBase:SPAC1F3.02c [has_penetrance] 45	(Fig. 5I)
PMID:39540318	FYPO:0004467	normal protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPCC645.07	(Fig. 5I)
PMID:39540318	FYPO:0008375	increased phosphatidylinositol-4-phosphate level in the Golgi [has_severity] medium	(Fig. 6B and Fig. 7G)
PMID:39540318	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC22E12.16c	(Fig. 6C and D)
PMID:39540318	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_protein] PomBase:SPAC22E12.16c	(Fig. 6D)
PMID:39540318	FYPO:0004467	normal protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. 6E)
PMID:39540318	FYPO:0004467	normal protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. 6E)
PMID:39540318	FYPO:0004467	normal protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. 6E)
PMID:39540318	FYPO:0001885	decreased protein phosphorylation during salt stress [has_severity] medium [assayed_protein] PomBase:SPBC119.08	(Fig. 7A)
PMID:39540318	FYPO:0001885	decreased protein phosphorylation during salt stress [has_severity] medium [assayed_protein] PomBase:SPBC119.08	(Fig. 7A)
PMID:39540318	FYPO:0008377	abnormal protein distribution along cell tip [assayed_protein] PomBase:SPBC12D12.04c	(Fig. 7D)
PMID:39540318	FYPO:0008373	normal protein localization to cell surface during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. 7E)
PMID:39540318	FYPO:0008373	normal protein localization to cell surface during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. 7E)
PMID:39540318	FYPO:0001885	decreased protein phosphorylation during salt stress [has_severity] medium [assayed_protein] PomBase:SPBC119.08	(Fig. 7F)
PMID:39540318	FYPO:0001885	decreased protein phosphorylation during salt stress [has_severity] high [assayed_protein] PomBase:SPBC119.08	(Fig. 7F)
PMID:39540318	FYPO:0008133	decreased phosphatidylinositol-4-phosphate level in the Golgi [has_severity] medium	(Fig. 7G)
PMID:39540318	FYPO:0008374	normal phosphatidylinositol-4-phosphate level in the Golgi	(Fig. 7G)
PMID:39540318	FYPO:0008133	decreased phosphatidylinositol-4-phosphate level in the Golgi [has_severity] medium	(Fig. 7G)
PMID:39540318	FYPO:0008374	normal phosphatidylinositol-4-phosphate level in the Golgi	(Fig. 7G)
PMID:39540318	FYPO:0008374	normal phosphatidylinositol-4-phosphate level in the Golgi	(Fig. 7G)
PMID:39540318	FYPO:0006637	decreased protein localization to cell cortex of cell tip, with protein distributed in cortex [has_severity] medium [assayed_protein] PomBase:SPBC12D12.04c	(Fig. S10A)
PMID:39540318	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [has_severity] high [assayed_protein] PomBase:SPBC119.08	(Fig. S1A)
PMID:39540318	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [has_severity] medium [assayed_protein] PomBase:SPBC119.08	(Fig. S1A)
PMID:39540318	FYPO:0001266	normal protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPAC24B11.06c	(Fig. S1B)
PMID:39540318	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_protein] PomBase:SPBC1685.01	(Fig. S1C)
PMID:39540318	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_protein] PomBase:SPBC1685.01	(Fig. S1C)
PMID:39540318	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [assayed_protein] PomBase:SPBC119.08 [has_severity] high	(Fig. S1D)
PMID:39540318	FYPO:0007526	increased protein phosphorylation during cellular response to salt stress [has_severity] medium [assayed_protein] PomBase:SPBC119.08	(Fig. S1D)
PMID:39540318	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPBC30B4.01c	(Fig. S2A)
PMID:39540318	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPBC30B4.01c	(Fig. S2A)
PMID:39540318	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPAC11G7.01	(Fig. S2B)
PMID:39540318	FYPO:0008376	abolished protein localization to cell cortex of cell tip during cellular response to osmotic stress [assayed_protein] PomBase:SPBC12D12.04c [has_penetrance] 60	(Fig. S2B)
PMID:39540318	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPAC11G7.01	(Fig. S2B)
PMID:39540318	FYPO:0004468	decreased protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. S2C)
PMID:39540318	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPAC16.01	(Fig. S4B)
PMID:39540318	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPAC16.01	(Fig. S4B)
PMID:39540318	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_protein] PomBase:SPAC16.01	(Fig. S4D)
PMID:39540318	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPBC119.08	(Fig. S5)
PMID:39540318	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPBC119.08	(Fig. S5)
PMID:39540318	FYPO:0005168	normal protein level during cellular response to salt stress [assayed_protein] PomBase:SPBC119.08	(Fig. S5C)
PMID:39540318	FYPO:0006625	decreased phosphatidylinositol-4,5-bisphosphate level in plasma membrane [has_severity] low	(Fig. S6A)
PMID:39540318	FYPO:0006626	increased phosphatidylinositol-4,5-bisphosphate level in plasma membrane [has_severity] low	(Fig. S6A)
PMID:39540318	FYPO:0006626	increased phosphatidylinositol-4,5-bisphosphate level in plasma membrane [has_severity] low	(Fig. S6A)
PMID:39540318	FYPO:0003136	excess plasma membrane present [has_penetrance] 25	(Fig. S6B)
PMID:39540318	FYPO:0003136	excess plasma membrane present [has_penetrance] 30	(Fig. S6B)
PMID:39540318	FYPO:0006616	viable vegetative cell with increased cell diameter [has_severity] low	(Fig. S7A)
PMID:39540318	FYPO:0006616	viable vegetative cell with increased cell diameter [has_penetrance] medium	(Fig. S7A)
PMID:39540318	FYPO:0006616	viable vegetative cell with increased cell diameter [has_severity] variable severity	(Fig. S7A)
PMID:39540318	FYPO:0006616	viable vegetative cell with increased cell diameter [has_severity] variable severity	(Fig. S7A)
PMID:39540318	FYPO:0004467	normal protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. S8A)
PMID:39540318	FYPO:0004467	normal protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. S8A)
PMID:39540318	FYPO:0008375	increased phosphatidylinositol-4-phosphate level in the Golgi [has_penetrance] medium	(Fig. S8B)
PMID:39540318	FYPO:0004467	normal protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. S8C)
PMID:39540318	FYPO:0004467	normal protein localization to cell tip during cellular response to salt stress [assayed_protein] PomBase:SPBC12D12.04c	(Fig. S8C)
PMID:39540318	FYPO:0008330	increased phosphatidylinositol-4-phosphate level in plasma membrane [has_severity] low	(Fig. S9A)
PMID:39540318	FYPO:0006626	increased phosphatidylinositol-4,5-bisphosphate level in plasma membrane [has_severity] high	(Fig. S9B)
PMID:39540318	FYPO:0001505	increased cellular phosphatidylserine level [has_severity] variable severity	(Fig. S9C)
PMID:39540318	FYPO:0001505	increased cellular phosphatidylserine level [has_severity] variable severity	(Fig. S9C)
PMID:39540318	FYPO:0008375	increased phosphatidylinositol-4-phosphate level in the Golgi [has_severity] high	(Fig. S9D)
PMID:39601909	FYPO:0000062	abnormal nuclear morphology during vegetative growth	(Fig. 3) Tunicamycin exposure leads to apoptotic cell death and aberrant nuclear morphology.
PMID:39601909	GO:0034976	response to endoplasmic reticulum stress	Based on these results we speculate a protective role of Bsd1 in response to tunicamycin-induced ER stress.
PMID:39601909	FYPO:0008365	sensitive to 2-deoxyglucose	Furthermore, we checked the growth of S. pombe cells in the presence of 2-deoxy-glucose and observed the concentration-dependent sensitivity of bsd1delta
PMID:39601909	FYPO:0000368	abnormal vacuolar morphology during vegetative growth	Interestingly, unlike wild type cells, the bsd1Δ cells showed punctate FM4-64 staining after tunicamycin exposure (Fig. 4), reminiscent of endosome like intermediate compartment previously has been reported in vps28 mutant cells that exhibit a defect in protein sorting process in budding yeast [34].
PMID:39601909	GO:0005789	endoplasmic reticulum membrane	The confocal microscopic analysis using GFP tagged Bsd1 suggests a typical endoplasmic reticulum membranous localization of Bsd1-GFP (Fig. 2b, left panel) [32]. Interestingly, in the presence of tunicamycin, the Bsd1-GFP localization was more pronounced (Fig. 2b, right pane
PMID:39601909	FYPO:0001457	sensitive to tunicamycin [has_severity] high	The epistatic interaction analysis between bsd1Δ and ire1Δ cells revealed a relative increase in tunicamycin sensitivity in bsd1Δ ire1Δ double mutant as compared to each single mutant (Fig. 5a).
PMID:39601909	FYPO:0001457	sensitive to tunicamycin [has_severity] high	The epistatic interaction analysis between bsd1Δ and ire1Δ cells revealed a relative increase in tunicamycin sensitivity in bsd1Δ ire1Δ double mutant as compared to each single mutant (Fig. 5a).
PMID:39601909	FYPO:0001457	sensitive to tunicamycin [has_severity] medium	The spotting assay analysis revealed that the bsd1Δ cells exhibit sensitivity against tunicamycin (Fig. 1c)
PMID:39652606	FYPO:0000229	cut [has_penetrance] 11 [has_severity] high	(Fig. 1)
PMID:39652606	FYPO:0000229	cut [has_penetrance] 14 [has_severity] high	(Fig. 1)
PMID:39652606	FYPO:0000229	cut [has_penetrance] 12 [has_severity] high	(Fig. 1)
PMID:39652606	FYPO:0000164	abnormal cell separation after cytokinesis	(Fig. 1A)
PMID:39652606	FYPO:0000164	abnormal cell separation after cytokinesis	(Fig. 1A)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1235.02 [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1B3.16c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBP4H10.11c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC22A12.06c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBP4H10.11c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC18H10.02 [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1281.06c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC56E4.04c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1235.02 [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC22A12.06c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC4A8.11c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1281.06c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1B3.16c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC18H10.02 [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC4A8.11c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1235.02 [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBP4H10.11c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC22A12.06c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC56E4.04c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1B3.16c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC18H10.02 [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC56E4.04c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1281.06c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC4A8.11c [has_severity] medium	(Fig. 2A, 2B)
PMID:39652606	FYPO:0005995	increased lncRNA level	(Fig. 2E)
PMID:39652606	FYPO:0005995	increased lncRNA level	(Fig. 2E)
PMID:39652606	FYPO:0005995	increased lncRNA level	(Fig. 2E)
PMID:39652606	FYPO:0008362	variable cellular lipid droplet content	(Fig. 3)
PMID:39652606	FYPO:0002552	lipid droplets present in decreased numbers [has_severity] low	(Fig. 3)
PMID:39652606	FYPO:0002552	lipid droplets present in decreased numbers [has_severity] medium	(Fig. 3)
PMID:39652606	FYPO:0008362	variable cellular lipid droplet content	(Fig. 3)
PMID:39652606	FYPO:0002552	lipid droplets present in decreased numbers [has_severity] medium	(Fig. 3)
PMID:39652606	FYPO:0006791	lipid droplets present in normal numbers	(Fig. 3)
PMID:39652606	FYPO:0006791	lipid droplets present in normal numbers	(Fig. 3)
PMID:39652606	FYPO:0006791	lipid droplets present in normal numbers	(Fig. 3)
PMID:39652606	FYPO:0008362	variable cellular lipid droplet content	(Fig. 3)
PMID:39652606	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. 4)
PMID:39652606	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 4)
PMID:39652606	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. 4)
PMID:39652606	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4)
PMID:39652606	FYPO:0001357	normal vegetative cell population growth	(Fig. 4)
PMID:39652606	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 4)
PMID:39652606	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 4)
PMID:39652606	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	(Fig. 4)
PMID:39652606	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 4)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [has_severity] high [assayed_protein] PomBase:SPAC26H5.05 [assayed_region] PomBase:SPCC1281.06c	(Fig. 5B)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [has_severity] medium [assayed_protein] PomBase:SPCC736.08 [assayed_region] PomBase:SPCC1281.06c	(Fig. 5B)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [assayed_region] PomBase:SPAC56E4.04c [has_severity] high [assayed_protein] PomBase:SPAC26H5.05	(Fig. 5B)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [assayed_region] PomBase:SPAC56E4.04c [has_severity] medium [assayed_protein] PomBase:SPCC736.08	(Fig. 5B)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC926.09c [has_severity] medium	(Fig. S2)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1786.01c [has_severity] low	(Fig. S2)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1450.16c [has_severity] medium	(Fig. S2)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1450.16c [has_severity] medium	(Fig. S2)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1786.01c [has_severity] medium	(Fig. S2)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC926.09c [has_severity] medium	(Fig. S2)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPCC1450.16c [has_severity] medium	(Fig. S2)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC1786.01c [has_severity] medium	(Fig. S2)
PMID:39652606	FYPO:0004880	decreased level of lipid metabolism gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC926.09c [has_severity] medium	(Fig. S2)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [has_severity] medium [assayed_protein] PomBase:SPCC736.08 [assayed_region] PomBase:SPBP4H10.11c	(Fig. S6A)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [has_severity] medium [assayed_protein] PomBase:SPCC736.08 [assayed_region] PomBase:SPAC22A12.06c	(Fig. S6A)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [has_severity] high [assayed_protein] PomBase:SPAC26H5.05 [assayed_region] PomBase:SPBP4H10.11c	(Fig. S6A)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [has_severity] high [assayed_protein] PomBase:SPAC26H5.05 [assayed_region] PomBase:SPCC1450.16c	(Fig. S6A)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [has_severity] high [assayed_protein] PomBase:SPAC26H5.05 [assayed_region] PomBase:SPAC22A12.06c	(Fig. S6A)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [has_severity] high [assayed_protein] PomBase:SPAC26H5.05 [assayed_region] PomBase:SPAC1B3.16c	(Fig. S6A)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPAC26H5.05 [assayed_region] PomBase:SPAC1786.01c [has_severity] medium	(Fig. S6B)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [has_severity] high [assayed_protein] PomBase:SPAC26H5.05 [assayed_region] PomBase:SPBC18H10.02	(Fig. S6B)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPCC736.08 [has_severity] high [assayed_region] PomBase:SPBC18H10.02	(Fig. S6B)
PMID:39652606	FYPO:0008249	decreased protein localization to chromatin at protein coding gene [assayed_protein] PomBase:SPCC736.08 [has_severity] high [assayed_region] PomBase:SPAC1786.01c	(Fig. S6B)
PMID:39660919	FYPO:0001357	normal vegetative cell population growth	(Fig. 3A)
PMID:39660919	FYPO:0001357	normal vegetative cell population growth	(Fig. 3A)
PMID:39660919	FYPO:0006657	abolished acid phosphatase activity during cellular response to phosphate starvation	(Fig. 3C) (comment: Assayed activity using medium supernatant)
PMID:39660919	FYPO:0008352	abolished CMP 5'-nucleotidase activity	(Fig. 4C)
PMID:39660919	FYPO:0008350	abolished GMP 5'-nucleotidase activity	(Fig. 4C)
PMID:39660919	FYPO:0008353	abolished UMP 5'-nucleotidase activity	(Fig. 4C)
PMID:39660919	FYPO:0008351	abolished AMP 5'-nucleotidase activity	(Fig. 4C)
PMID:39660919	FYPO:0008357	decreased GMP 5'-nucleotidase activity	(Fig. 5)
PMID:39660919	FYPO:0008355	decreased AMP 5'-nucleotidase activity	(Fig. 5)
PMID:39660919	FYPO:0008356	decreased CMP 5'-nucleotidase activity	(Fig. 5)
PMID:39660919	FYPO:0008354	decreased UMP 5'-nucleotidase activity	(Fig. 5)
PMID:39660919	FYPO:0008357	decreased GMP 5'-nucleotidase activity	(Fig. 5)
PMID:39660919	FYPO:0008355	decreased AMP 5'-nucleotidase activity	(Fig. 5)
PMID:39660919	FYPO:0008356	decreased CMP 5'-nucleotidase activity	(Fig. 5)
PMID:39660919	FYPO:0008354	decreased UMP 5'-nucleotidase activity	(Fig. 5)
PMID:39660919	FYPO:0001310	normal viability in stationary phase	(Fig. 6) We conclude that Pho1 acid phosphatase and extracellular 5'-nucleotidase activities, which are induced during acute phosphate starvation, are not important for survival during chronic phosphate starvation. It is likely that the lifespan-shortening effects of ablating Pho7 reflect its role in promoting the expression of several hundred other fission yeast genes (8).
PMID:39660919	GO:0008253	5'-nucleotidase activity [happens_during] cellular response to phosphate starvation [occurs_in] extracellular region	(Figure 5) It is apparent that Efn1 contributes a greater share of secreted 5'-nucleotidase activity against AMP, GMP, and UMP compared to Efn2.
PMID:39660919	GO:0008253	5'-nucleotidase activity [happens_during] cellular response to phosphate starvation [occurs_in] extracellular region	(Figure 5) The Efn1:Efn2 activity ratio is 5.0 for AMP, 6.3 for GMP, and 4.1 for UMP (Fig. 5) However, the Efn1:Efn2 activity ratio for CMP hydrolysis is 1.3, suggesting that Efn2 displays a greater selectivity for CMP than does Efn1.
PMID:39660919	GO:0005576	extracellular region [exists_during] cellular response to phosphate starvation	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	GO:0005576	extracellular region [exists_during] cellular response to phosphate starvation	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	GO:0005576	extracellular region [exists_during] cellular response to phosphate starvation	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	GO:0005576	extracellular region [exists_during] cellular response to phosphate starvation	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	GO:0005576	extracellular region [exists_during] cellular response to phosphate starvation	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	GO:0005576	extracellular region [exists_during] cellular response to phosphate starvation	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	GO:0005576	extracellular region [exists_during] cellular response to phosphate starvation	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	GO:0005576	extracellular region [exists_during] cellular response to phosphate starvation	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	GO:0005576	extracellular region [exists_during] cellular response to phosphate starvation	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	GO:0005576	extracellular region [exists_during] cellular response to phosphate starvation	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	GO:0005576	extracellular region [exists_during] cellular response to phosphate starvation	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	GO:0005576	extracellular region [exists_during] cellular response to phosphate starvation	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	GO:0005576	extracellular region [exists_during] cellular response to phosphate starvation	A list of the 13 most abundant secreted proteins detected in the medium of phosphate-starved fission yeast cells is compiled in Fig. 2A
PMID:39660919	PomGeneEx:0000018	protein level increased [during] cellular response to phosphate starvation	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PomGeneEx:0000018	protein level increased [during] cellular response to phosphate starvation	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PomGeneEx:0000018	protein level increased [during] cellular response to phosphate starvation	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PomGeneEx:0000018	protein level increased [during] cellular response to phosphate starvation	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PomGeneEx:0000018	protein level increased [during] cellular response to phosphate starvation	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PomGeneEx:0000018	protein level increased [during] cellular response to phosphate starvation	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PomGeneEx:0000018	protein level increased [during] cellular response to phosphate starvation	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PomGeneEx:0000018	protein level increased [during] cellular response to phosphate starvation	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PomGeneEx:0000018	protein level increased [during] cellular response to phosphate starvation	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PomGeneEx:0000018	protein level increased [during] cellular response to phosphate starvation	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PomGeneEx:0000018	protein level increased [during] cellular response to phosphate starvation	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PomGeneEx:0000018	protein level increased [during] cellular response to phosphate starvation	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	PomGeneEx:0000018	protein level increased [during] cellular response to phosphate starvation	Protein content of supernant medium from wild-type cells that were starved for phosphate for 12 hours was analyzed by UHPLC-MS
PMID:39660919	FYPO:0001357	normal vegetative cell population growth	we generated a pho1∆ pho4∆ strain that grew as well as wild-type on YES agar medium (Fig. 3A).
PMID:39666777	FYPO:0002060	viable vegetative cell population	(Fig. 4A)
PMID:39666777	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC19G7.05c	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAPJ760.03c	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPAC2F7.03c	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC4F6.12	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPBC646.06c	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	FYPO:0000826	decreased RNA level [assayed_transcript] PomBase:SPAC14C4.09	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC29B5.01	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC11C11.05	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	FYPO:0001890	increased RNA level [assayed_transcript] PomBase:SPBC19G7.06	(Fig. 7) Nup211 regulates the expression of several genes involved in cytokinesis.
PMID:39666777	FYPO:0000134	branched, elongated, multiseptate cell	(Figure 3B) Some cells appeared abnormally round, curved, bulged, or branched, indicating that Nup211 plays a role in maintaining proper cell shape (Fig 3B). Interestingly, nup211 shut-off cells also showed severe defects in septation and cytokinesis. These defects varied widely: some cells failed to develop a septum during division (Fig 3B- a), while others developed thicker (Fig 3B-b), misplaced (Fig 3B-c), or multiple septa (Fig 3B- d). Furthermore, septa were sometimes seen in shorter cells (Fig 3B-c), while other phenotypes like bulging (Fig 3B-c, 3B-e), branching (Fig 3B-e), curving, and swelling (Fig 3B-f) were also observed.
PMID:39666777	FYPO:0002563	normal protein localization to nuclear periphery [assayed_protein] PomBase:SPCC162.08c	(Figure 5C)
PMID:39666777	FYPO:0001406	increased septum thickness	Compared with wild type cells, a higher percentage of nup211 shut-off cells contained multiple and/or thicker septa (Fig 3C).
PMID:39666777	FYPO:0002060	viable vegetative cell population	Exogenous expression of Nup211, Nup2111-863, or Nup2111-655 restored cell viability; however, expression of Nup2111-1033 only led to a partial recovery (Fig 4A)
PMID:39666777	FYPO:0002060	viable vegetative cell population	Exogenous expression of Nup211, Nup2111-863, or Nup2111-655 restored cell viability; however, expression of Nup2111-1033 only led to a partial recovery (Fig 4A)
PMID:39666777	FYPO:0000950	elongated aseptate vegetative cell	some cells failed to develop a septum during division (Fig 3B- a)
PMID:39705284	FYPO:0000413	abolished cell fusion during mating [has_penetrance] 80	(Fig. 1D)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [assayed_protein] PomBase:SPAC13G6.07c [has_severity] low	(Fig. 5C)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [assayed_protein] PomBase:SPAC13G6.07c [has_severity] low	(Fig. 5C)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [assayed_protein] PomBase:SPAPB1E7.12 [has_severity] low	(Fig. 5C)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [assayed_protein] PomBase:SPAPB1E7.12 [has_severity] low	(Fig. 5C)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [assayed_protein] PomBase:SPCC4G3.08 [has_severity] high	(Fig. 5C)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [has_severity] high [assayed_protein] PomBase:SPAC13G6.07c	(Fig. 5D)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [assayed_protein] PomBase:SPAPB1E7.12 [has_severity] high	(Fig. 5D)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [assayed_protein] PomBase:SPAPB1E7.12 [has_severity] high	(Fig. 5D)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [has_severity] high [assayed_protein] PomBase:SPAC13G6.07c	(Fig. 5D)
PMID:39705284	FYPO:0000573	normal shmoo formation	(Fig. 6A)
PMID:39705284	FYPO:0004670	abnormal macroautophagy during nitrogen starvation	(Fig. 6C)
PMID:39705284	FYPO:0006295	abolished macroautophagy during nitrogen starvation	(Fig. 6C)
PMID:39705284	FYPO:0006294	normal macroautophagy during nitrogen starvation	(Fig. 6D)
PMID:39705284	FYPO:0000573	normal shmoo formation	(Fig. 6E)
PMID:39705284	FYPO:0000573	normal shmoo formation	(Fig. 6E)
PMID:39705284	FYPO:0000708	decreased mating efficiency [has_severity] high	(Fig. 7A)
PMID:39705284	FYPO:0000708	decreased mating efficiency [has_severity] high	(Fig. 7A)
PMID:39705284	FYPO:0000280	sterile [has_penetrance] complete	(Fig. 7A)
PMID:39705284	FYPO:0000280	sterile [has_penetrance] complete	(Fig. 7A)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [assayed_protein] PomBase:SPAPB1E7.12	(Fig. 7B)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [assayed_protein] PomBase:SPAC13G6.07c	(Fig. 7B)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [assayed_protein] PomBase:SPCC4G3.08	(Fig. 7B)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [assayed_protein] PomBase:SPAPB1E7.12	(Fig. 7B)
PMID:39705284	FYPO:0008411	decreased protein phosphorylation during mating [assayed_protein] PomBase:SPAC13G6.07c	(Fig. 7B)
PMID:39705284	FYPO:0000708	decreased mating efficiency [has_severity] medium	(Fig. 7C)
PMID:39705284	FYPO:0000581	decreased spore germination frequency [has_severity] high	(Fig. 7F and G)
PMID:39705284	FYPO:0000581	decreased spore germination frequency	(Fig. 7F)
PMID:39705284	FYPO:0000708	decreased mating efficiency [has_severity] low	(Fig. 7H)
PMID:39705284	FYPO:0008412	abolished protein phosphorylation during mating [assayed_protein] PomBase:SPAPB1E7.12	(Figure 5)
PMID:39705284	FYPO:0008412	abolished protein phosphorylation during mating [assayed_protein] PomBase:SPAPB1E7.12	(Figure 5)
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [part_of] regulation of gene expression [occurs_in] euchromatin	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [part_of] regulation of gene expression [occurs_in] euchromatin	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [part_of] regulation of gene expression [occurs_in] euchromatin	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [part_of] regulation of gene expression [occurs_in] euchromatin	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [part_of] regulation of gene expression [occurs_in] euchromatin	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [part_of] regulation of gene expression [occurs_in] euchromatin	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [part_of] regulation of gene expression [occurs_in] euchromatin	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [part_of] regulation of gene expression [occurs_in] euchromatin	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [part_of] positive regulation of heterochromatin formation [occurs_in] mating-type region heterochromatin	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [part_of] positive regulation of heterochromatin formation [occurs_in] mating-type region heterochromatin	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [part_of] regulation of gene expression [occurs_in] euchromatin	(comment: ChIP-Seq data showed binding to euchromatin.)
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_in] mating-type region heterochromatin	"(comment: vw: changed. ""GO:0140297 DNA-binding transcription factor BINDING"" to RNA polymerase II cis-regulatory region sequence-specific DNA binding. DNA-binding transcription factor binding is a term for proteins which bind transcription factors) We next investigated whether Php2 and Php3 bind at the het- erochromatic regions where Php5 is found. ChIP-seq analyses revealed that both proteins co-localized with Php5 at the cenH and dh repeats adjacent to siRNA hotspots, and this result was confirmed by ChIP- qPCR (Fig. 2c–f)."
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_in] pericentric heterochromatin	"(comment: vw: changed. ""GO:0140297 DNA-binding transcription factor BINDING"" to RNA polymerase II cis-regulatory region sequence-specific DNA binding. DNA-binding transcription factor binding is a term for proteins which bind transcription factors) We next investigated whether Php2 and Php3 bind at the het- erochromatic regions where Php5 is found. ChIP-seq analyses revealed that both proteins co-localized with Php5 at the cenH and dh repeats adjacent to siRNA hotspots, and this result was confirmed by ChIP- qPCR (Fig. 2c–f)."
PMID:39747188	FYPO:0008424	decreased silent mating-type cassette transcript-derived siRNA level [has_severity] low	A temperature-sensitive mutation in the conserved spliceosome component Cwf10EFTUD2 (cwf10-1)56 alone caused only a modest defect in the production of siRNAs that map to cenH (Sup- plementary Fig. 7c).
PMID:39747188	FYPO:0008246	normal cenH-derived RNA level [has_severity] low	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	FYPO:0008246	normal cenH-derived RNA level [has_severity] low	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	FYPO:0004689	increased cenH-derived RNA level [has_severity] low	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	FYPO:0004689	increased cenH-derived RNA level [has_severity] low	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	FYPO:0004689	increased cenH-derived RNA level [has_severity] low	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	FYPO:0004689	increased cenH-derived RNA level [has_severity] high	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	FYPO:0004689	increased cenH-derived RNA level [has_severity] low	As expected, we observed increased cenH transcript levels in clr4Δ26 (Fig. 5a, b and Supplementary Fig. 6a, b). Interestingly, the lack of PhpC significantly decreased cenH transcript levels in clr4Δ (Fig. 5a, b).
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_in] pericentric heterochromatin	By using this method, we confirmed that Php5 and Moc3 were indeed enriched at both cenH and dh loci (Fig. 1d and Supplementary Fig. 1b). These results indicate that TFs can access repeat elements located within repressive het- erochromatin domains.
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_in] pericentric heterochromatin	By using this method, we confirmed that Php5 and Moc3 were indeed enriched at both cenH and dh loci (Fig. 1d and Supplementary Fig. 1b). These results indicate that TFs can access repeat elements located within repressive het- erochromatin domains.
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_in] mating-type region heterochromatin	By using this method, we confirmed that Php5 and Moc3 were indeed enriched at both cenH and dh loci (Fig. 1d and Supplementary Fig. 1b). These results indicate that TFs can access repeat elements located within repressive het- erochromatin domains.
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_in] mating-type region heterochromatin	By using this method, we confirmed that Php5 and Moc3 were indeed enriched at both cenH and dh loci (Fig. 1d and Supplementary Fig. 1b). These results indicate that TFs can access repeat elements located within repressive het- erochromatin domains.
PMID:39747188	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPAC23C11.08	Consistent with the fact that Php2/3/5 forms a complex, loss of Php3 localization at cenH and dh elements was observed in the absence of php2 or php5 (Fig. 3a, b, and Supplementary Fig. 3a).
PMID:39747188	FYPO:0003074	abolished protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC23C11.08	Consistent with the fact that Php2/3/5 forms a complex, loss of Php3 localization at cenH and dh elements was observed in the absence of php2 or php5 (Fig. 3a, b, and Supplementary Fig. 3a).
PMID:39747188	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPAC23C11.08	Consistent with the fact that Php2/3/5 forms a complex, loss of Php3 localization at cenH and dh elements was observed in the absence of php2 or php5 (Fig. 3a, b, and Supplementary Fig. 3a).
PMID:39747188	FYPO:0003074	abolished protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC23C11.08	Consistent with the fact that Php2/3/5 forms a complex, loss of Php3 localization at cenH and dh elements was observed in the absence of php2 or php5 (Fig. 3a, b, and Supplementary Fig. 3a).
PMID:39747188	GO:0016602	CCAAT-binding factor complex	For this, we performed immuno-affinity purification of GFP-tagged Php5 (Fig. 2a) and analyzed the purified fraction by mass spectroscopy. In addition to Php5, these analyses identified NF-YA and NF-YB orthologs, Php2 and Php3, respectively (Fig. 2b). Therefore, Php5 associates with Php3NF-YB and Php2NF-YA to form the Php complex (PhpC), as observed in other yeasts and humans.
PMID:39747188	GO:0016602	CCAAT-binding factor complex	For this, we performed immuno-affinity purification of GFP-tagged Php5 (Fig. 2a) and analyzed the purified fraction by mass spectroscopy. In addition to Php5, these analyses identified NF-YA and NF-YB orthologs, Php2 and Php3, respectively (Fig. 2b). Therefore, Php5 associates with Php3NF-YB and Php2NF-YA to form the Php complex (PhpC), as observed in other yeasts and humans.
PMID:39747188	GO:0016602	CCAAT-binding factor complex	For this, we performed immuno-affinity purification of GFP-tagged Php5 (Fig. 2a) and analyzed the purified fraction by mass spectroscopy. In addition to Php5, these analyses identified NF-YA and NF-YB orthologs, Php2 and Php3, respectively (Fig. 2b). Therefore, Php5 associates with Php3NF-YB and Php2NF-YA to form the Php complex (PhpC), as observed in other yeasts and humans.
PMID:39747188	GO:0005721	pericentric heterochromatin	Furthermore, the genome-wide distribution of Php3 and Moc3 remained largely unchanged in mitotic-arrested cells (Supplementary Data 4), indi- cating that PhpC and Moc3 maintain their association with hetero- chromatin outside of S-phase.
PMID:39747188	GO:0005721	pericentric heterochromatin	Furthermore, the genome-wide distribution of Php3 and Moc3 remained largely unchanged in mitotic-arrested cells (Supplementary Data 4), indi- cating that PhpC and Moc3 maintain their association with hetero- chromatin outside of S-phase.
PMID:39747188	GO:0031934	mating-type region heterochromatin	Furthermore, the genome-wide distribution of Php3 and Moc3 remained largely unchanged in mitotic-arrested cells (Supplementary Data 4), indi- cating that PhpC and Moc3 maintain their association with hetero- chromatin outside of S-phase.
PMID:39747188	GO:0031934	mating-type region heterochromatin	Furthermore, the genome-wide distribution of Php3 and Moc3 remained largely unchanged in mitotic-arrested cells (Supplementary Data 4), indi- cating that PhpC and Moc3 maintain their association with hetero- chromatin outside of S-phase.
PMID:39747188	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPAC821.07c	Interestingly, we also observed that Moc3 occupancy at both cenH and dh heterochromatic regions was contingent upon PhpC (Fig. 3a, c and Supplementary Fig. 3d).
PMID:39747188	FYPO:0003074	abolished protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC821.07c	Interestingly, we also observed that Moc3 occupancy at both cenH and dh heterochromatic regions was contingent upon PhpC (Fig. 3a, c and Supplementary Fig. 3d).
PMID:39747188	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPAC23C11.08	Moreover, the localization of PhpC subunits was compro- mised in moc3Δ cells (Fig. 3a, b and Supplementary Fig. 3b, c).
PMID:39747188	FYPO:0003074	abolished protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC23C11.08	Moreover, the localization of PhpC subunits was compro- mised in moc3Δ cells (Fig. 3a, b and Supplementary Fig. 3b, c).
PMID:39747188	FYPO:0008424	decreased silent mating-type cassette transcript-derived siRNA level [has_penetrance] high	On the other hand, loss of Swi6HP1, which causes an increase in heterochromatic repeat transcription (Supplementary Fig. 7a), showed a corresponding increase in cenH siRNAs.
PMID:39747188	FYPO:0006110	increased silent mating-type cassette transcript-derived siRNA level [has_penetrance] high	On the other hand, loss of Swi6HP1, which causes an increase in heterochromatic repeat transcription (Supplementary Fig. 7a), showed a corresponding increase in cenH siRNAs.
PMID:39747188	FYPO:0008424	decreased silent mating-type cassette transcript-derived siRNA level [has_penetrance] high	On the other hand, loss of Swi6HP1, which causes an increase in heterochromatic repeat transcription (Supplementary Fig. 7a), showed a corresponding increase in cenH siRNAs.
PMID:39747188	FYPO:0007505	decreased protein localization to chromatin at promoter [assayed_protein] PomBase:SPAC23C11.08 [has_severity] low	On the other hand, the global binding of Php3 at gene promoters, lncRNAs, and other ncRNAs, was reduced but not abolished in HFD mutant cells (Supplementary Fig. 5d, e, Supplemen- tary Data 4).
PMID:39747188	FYPO:0008424	decreased silent mating-type cassette transcript-derived siRNA level [has_severity] high	On the other hand, when cwf10-1 was combined with swi6Δ, the double mutant cells showed a dramatic reduction in cenH siRNAs (Supplementary Fig. 7c).
PMID:39747188	FYPO:0008423	increased spatial extent of protein localization to heterochromatin [assayed_protein] PomBase:SPAC23C11.08	PhpC and Moc3 peaks at cenH and dh elements were mostly unchanged in cells lacking Clr4Suv39h (Fig. 4a–d and Supplementary Fig. 4a, b).
PMID:39747188	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC23C11.08	PhpC and Moc3 peaks at cenH and dh elements were mostly unchanged in cells lacking Clr4Suv39h (Fig. 4a–d and Supplementary Fig. 4a, b).
PMID:39747188	FYPO:0004378	normal protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPAC821.07c	PhpC and Moc3 peaks at cenH and dh elements were mostly unchanged in cells lacking Clr4Suv39h (Fig. 4a–d and Supplementary Fig. 4a, b).
PMID:39747188	FYPO:0008154	normal protein localization to centromeric heterochromatin [assayed_protein] PomBase:SPAC821.07c	PhpC and Moc3 peaks at cenH and dh elements were mostly unchanged in cells lacking Clr4Suv39h (Fig. 4a–d and Supplementary Fig. 4a, b).
PMID:39747188	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC28F2.12 [has_severity] low	RNAPII occu- pancy increased at cenH in clr4Δ (Fig. 5e, f and Supplementary Fig. 6c). Removal of PhpC or Moc3, or the introduction of CCAATmut mutation in clr4Δ cells, resulted in a considerable reduction in RNAPII levels at cenH (Fig. 5e, f).
PMID:39747188	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC28F2.12 [has_severity] low	RNAPII occu- pancy increased at cenH in clr4Δ (Fig. 5e, f and Supplementary Fig. 6c). Removal of PhpC or Moc3, or the introduction of CCAATmut mutation in clr4Δ cells, resulted in a considerable reduction in RNAPII levels at cenH (Fig. 5e, f).
PMID:39747188	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [has_severity] high [assayed_protein] PomBase:SPBC28F2.12	RNAPII occu- pancy increased at cenH in clr4Δ (Fig. 5e, f and Supplementary Fig. 6c). Removal of PhpC or Moc3, or the introduction of CCAATmut mutation in clr4Δ cells, resulted in a considerable reduction in RNAPII levels at cenH (Fig. 5e, f).
PMID:39747188	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC28F2.12 [has_severity] low	RNAPII occu- pancy increased at cenH in clr4Δ (Fig. 5e, f and Supplementary Fig. 6c). Removal of PhpC or Moc3, or the introduction of CCAATmut mutation in clr4Δ cells, resulted in a considerable reduction in RNAPII levels at cenH (Fig. 5e, f).
PMID:39747188	FYPO:0004377	increased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBC28F2.12 [has_severity] low	RNAPII occu- pancy increased at cenH in clr4Δ (Fig. 5e, f and Supplementary Fig. 6c). Removal of PhpC or Moc3, or the introduction of CCAATmut mutation in clr4Δ cells, resulted in a considerable reduction in RNAPII levels at cenH (Fig. 5e, f).
PMID:39747188	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] high [assayed_protein] PomBase:SPBC3B8.02	Remarkably, we observed that in both mutants, the binding of PhpC subunits Php3 and Php5 at cenH and dh heterochromatic repeats was drastically reduced (Fig. 4e–g, Supplementary Fig. 5b),....... Indeed, site- specific ChIP-qPCR analysis revealed a ~ 90% reduction in Php3 and a ~ 80% reduction in Php5 in HFD mutants compared to WT (Fig. 4g, Supplementary Fig. 5b).
PMID:39747188	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [assayed_protein] PomBase:SPAC23C11.08 [has_severity] high	Remarkably, we observed that in both mutants, the binding of PhpC subunits Php3 and Php5 at cenH and dh heterochromatic repeats was drastically reduced (Fig. 4e–g, Supplementary Fig. 5b)...... Indeed, site- specific ChIP-qPCR analysis revealed a ~ 90% reduction in Php3 and a ~ 80% reduction in Php5 in HFD mutants compared to WT (Fig. 4g, Supplementary Fig. 5b).
PMID:39747188	FYPO:0004689	increased cenH-derived RNA level [has_severity] low	Similar changes were observed in moc3Δ (Fig. 5a and Supplementary Fig. 6b)52.
PMID:39747188	GO:0140185	siRNA-mediated silent mating type cassette region heterochromatin formation	Small RNA sequencing data indicated that Swi6 is necessary for siRNA production, irrespective of PhpC and Moc3.
PMID:39747188	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] low [assayed_protein] PomBase:SPAC821.07c	Specifically, we assessed TF localization in cells lacking the RSC subunit Rsc1, the SWI/SNF ATP-dependent chromatin remodeler Snf22 and/or bearing a mutation in the ATPase domain of Ino80 (i.e., ino80K873A). In all cases, we observed that Php3 and Moc3 binding to cenH and dh regions were only marginally reduced but nevertheless not abolished (Supplementary Fig. 4f–i).
PMID:39747188	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] low [assayed_protein] PomBase:SPAC23C11.08	Specifically, we assessed TF localization in cells lacking the RSC subunit Rsc1, the SWI/SNF ATP-dependent chromatin remodeler Snf22 and/or bearing a mutation in the ATPase domain of Ino80 (i.e., ino80K873A). In all cases, we observed that Php3 and Moc3 binding to cenH and dh regions were only marginally reduced but nevertheless not abolished (Supplementary Fig. 4f–i).
PMID:39747188	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] low [assayed_protein] PomBase:SPAC821.07c	Specifically, we assessed TF localization in cells lacking the RSC subunit Rsc1, the SWI/SNF ATP-dependent chromatin remodeler Snf22 and/or bearing a mutation in the ATPase domain of Ino80 (i.e., ino80K873A). In all cases, we observed that Php3 and Moc3 binding to cenH and dh regions were only marginally reduced but nevertheless not abolished (Supplementary Fig. 4f–i).
PMID:39747188	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] low [assayed_protein] PomBase:SPAC23C11.08	Specifically, we assessed TF localization in cells lacking the RSC subunit Rsc1, the SWI/SNF ATP-dependent chromatin remodeler Snf22 and/or bearing a mutation in the ATPase domain of Ino80 (i.e., ino80K873A). In all cases, we observed that Php3 and Moc3 binding to cenH and dh regions were only marginally reduced but nevertheless not abolished (Supplementary Fig. 4f–i).
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_in] mating-type region heterochromatin	We next investigated whether Php2 and Php3 bind at the het- erochromatic regions where Php5 is found. ChIP-seq analyses revealed that both proteins co-localized with Php5 at the cenH and dh repeats adjacent to siRNA hotspots, and this result was confirmed by ChIP- qPCR (Fig. 2c–f).
PMID:39747188	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding [occurs_in] pericentric heterochromatin	We next investigated whether Php2 and Php3 bind at the het- erochromatic regions where Php5 is found. ChIP-seq analyses revealed that both proteins co-localized with Php5 at the cenH and dh repeats adjacent to siRNA hotspots, and this result was confirmed by ChIP- qPCR (Fig. 2c–f).
PMID:39747188	GO:0140185	siRNA-mediated silent mating type cassette region heterochromatin formation	positive regulation? (comment: I removed GO:0031453 positive regulation of heterochromatin formation and GO:0010964 regulation of regulatory ncRNA-mediated heterochromatin formation, because if we make a positive regulation term it will cover both i.e the other terms will be ancestors ) Mutations in the php5 gene or its binding site, the CCAAT box located at cenH when combine with Swi6, result in a significant decrease in siRNA production at the mating type locus.
PMID:39747188	GO:0140185	siRNA-mediated silent mating type cassette region heterochromatin formation	positive regulation? (comment: vw: I removed GO:0031453 positive regulation of heterochromatin formation and GO:0010964 regulation of regulatory ncRNA-mediated heterochromatin formation, because if we make a positive regulation term it will cover both i.e the other terms will be ancestors ) Mutations in the Php3 gene or its binding site, the CCAAT box located at cenH, result in a significant decrease in siRNA production at the mating type locus.
PMID:39747188	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] low [assayed_protein] PomBase:SPAC821.07c	we investigated the dis- tribution of Php3 and Moc3 in cells devoid of both Gcn5, a subunit of the SAGA complex, and Mst2, a MYST acetyltransferase. Interestingly, we found that in those cells, both TFs can still localize to cenH and dh heterochromatic repeat elements, albeit with a slight reduction (Sup- plementary Fig. 4d, e).
PMID:39747188	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] low [assayed_protein] PomBase:SPAC23C11.08	we investigated the dis- tribution of Php3 and Moc3 in cells devoid of both Gcn5, a subunit of the SAGA complex, and Mst2, a MYST acetyltransferase. Interestingly, we found that in those cells, both TFs can still localize to cenH and dh heterochromatic repeat elements, albeit with a slight reduction (Sup- plementary Fig. 4d, e).
PMID:39747188	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] low [assayed_protein] PomBase:SPAC821.07c	we investigated the dis- tribution of Php3 and Moc3 in cells devoid of both Gcn5, a subunit of the SAGA complex, and Mst2, a MYST acetyltransferase. Interestingly, we found that in those cells, both TFs can still localize to cenH and dh heterochromatic repeat elements, albeit with a slight reduction (Sup- plementary Fig. 4d, e).
PMID:39747188	FYPO:0002386	decreased protein localization to pericentric heterochromatin at centromere outer repeat region [has_severity] low [assayed_protein] PomBase:SPAC23C11.08	we investigated the dis- tribution of Php3 and Moc3 in cells devoid of both Gcn5, a subunit of the SAGA complex, and Mst2, a MYST acetyltransferase. Interestingly, we found that in those cells, both TFs can still localize to cenH and dh heterochromatic repeat elements, albeit with a slight reduction (Sup- plementary Fig. 4d, e).
PMID:39747188	FYPO:0000838	normal protein localization to nucleus during vegetative growth [has_severity] high [assayed_protein] PomBase:SPBC3B8.02	while the nuclear localization of both TFs was preserved (Fig. 4h, Supplementary Fig. 5c)
PMID:39747188	FYPO:0000838	normal protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPAC23C11.08 [has_severity] high	while the nuclear localization of both TFs was preserved (Fig. 4h, Supplementary Fig. 5c)
PMID:39761853	PomGeneEx:0000012	RNA level decreased [during] cellular response to zinc ion starvation	(Fig. 1)
PMID:39761853	FYPO:0006830	normal RNA level during cellular response to replete zinc [assayed_transcript] PomBase:SPAC821.10c	(Fig. 1A)
PMID:39761853	FYPO:0001547	increased RNA level during cellular response to zinc ion starvation [assayed_transcript] PomBase:SPAC821.10c [has_severity] low	(Fig. 1A)
PMID:39761853	FYPO:0006829	normal RNA level during cellular response to zinc ion starvation [assayed_transcript] PomBase:SPAC821.10c	(Fig. 1B)
PMID:39761853	FYPO:0006830	normal RNA level during cellular response to replete zinc [assayed_transcript] PomBase:SPAC821.10c	(Fig. 1B)
PMID:39761853	FYPO:0006830	normal RNA level during cellular response to replete zinc [assayed_transcript] PomBase:SPAC821.10c	(Fig. 1B)
PMID:39761853	FYPO:0006830	normal RNA level during cellular response to replete zinc [assayed_transcript] PomBase:SPAC821.10c	(Fig. 1B)
PMID:39761853	FYPO:0006829	normal RNA level during cellular response to zinc ion starvation [assayed_transcript] PomBase:SPAC821.10c	(Fig. 1B)
PMID:39761853	FYPO:0006829	normal RNA level during cellular response to zinc ion starvation [assayed_transcript] PomBase:SPAC821.10c	(Fig. 1B)
PMID:39761853	FYPO:0005291	increased RNA level during cellular response to zinc ion [assayed_transcript] PomBase:SPAC821.10c [has_severity] medium	(Fig. 3A)
PMID:39761853	FYPO:0001547	increased RNA level during cellular response to zinc ion starvation [assayed_transcript] PomBase:SPAC821.10c [has_severity] medium	(Fig. 3A)
PMID:39761853	FYPO:0005291	increased RNA level during cellular response to zinc ion [has_severity] high [assayed_transcript] PomBase:SPAC821.10c	(Fig. 3A)
PMID:39761853	FYPO:0001547	increased RNA level during cellular response to zinc ion starvation [has_severity] high [assayed_transcript] PomBase:SPAC821.10c	(Fig. 3A)
PMID:39761853	FYPO:0006829	normal RNA level during cellular response to zinc ion starvation [assayed_transcript] PomBase:SPAC821.10c	(Fig. 3B)
PMID:39761853	GO:0010629	negative regulation of gene expression [happens_during] cellular response to zinc ion starvation	(Fig. 4)
PMID:39761853	GO:0010629	negative regulation of gene expression [happens_during] cellular response to zinc ion starvation	(Fig. 4)
PMID:39761853	PomGeneEx:0000019	protein level decreased [during] cellular response to zinc ion starvation	(Fig. 4A)
PMID:39761853	FYPO:0001551	increased protein level during cellular response to zinc ion starvation [has_severity] high [assayed_protein] PomBase:SPAC821.10c	(Fig. 4B)
PMID:39761853	FYPO:0001551	increased protein level during cellular response to zinc ion starvation [has_severity] high [assayed_protein] PomBase:SPAC821.10c	(Fig. 4B)
PMID:39761853	FYPO:0007054	normal protein level during cellular response to zinc ion starvation [assayed_protein] PomBase:SPAC821.10c	(Fig. 4B)
PMID:39761853	FYPO:0008441	normal protein level during cellular response to replete zinc [assayed_protein] PomBase:SPAC821.10c	(Fig. 4B)
PMID:39761853	FYPO:0008441	normal protein level during cellular response to replete zinc [assayed_protein] PomBase:SPAC821.10c	(Fig. 4B)
PMID:39761853	FYPO:0008441	normal protein level during cellular response to replete zinc [assayed_protein] PomBase:SPAC821.10c	(Fig. 4B)
PMID:39761853	FYPO:0006830	normal RNA level during cellular response to replete zinc [has_severity] high [assayed_transcript] PomBase:SPAC821.10c	(Fig. 5)
PMID:39761853	FYPO:0001547	increased RNA level during cellular response to zinc ion starvation [has_severity] high [assayed_transcript] PomBase:SPAC821.10c	(Fig. 5)
PMID:39761853	FYPO:0001551	increased protein level during cellular response to zinc ion starvation [assayed_protein] PomBase:SPAC821.10c [has_severity] low	(Fig. 5)
PMID:39761853	FYPO:0001551	increased protein level during cellular response to zinc ion starvation [assayed_protein] PomBase:SPAC821.10c [has_severity] high	(Fig. 5)
PMID:39761853	FYPO:0006829	normal RNA level during cellular response to zinc ion starvation [assayed_transcript] PomBase:SPAC821.10c	(Fig. 7)
PMID:39761853	FYPO:0000116	sensitive to zinc	(Fig. 8A)
PMID:39761853	FYPO:0007928	sensitive to ethylenediaminetetraacetic acid	(Fig. 8A)
PMID:39761853	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 8A)
PMID:39761853	FYPO:0008442	normal growth on ethylenediaminetetraacetic acid	(Fig. 8C)
PMID:39761853	FYPO:0007928	sensitive to ethylenediaminetetraacetic acid [has_severity] medium	(Fig. 8C)
PMID:39761853	FYPO:0007928	sensitive to ethylenediaminetetraacetic acid [has_severity] medium	(Fig. 8C)
PMID:39761853	FYPO:0003507	normal growth on zinc	(Fig. 8C)
PMID:39761853	FYPO:0003507	normal growth on zinc	(Fig. 8C)
PMID:39761853	FYPO:0003507	normal growth on zinc	(Fig. 8C)
PMID:39786922	FYPO:0002778	decreased protein sumoylation during vegetative growth [has_severity] high	(Fig. 2A)
PMID:39786922	FYPO:0000443	abnormal protein localization during vegetative growth [assayed_protein] PomBase:SPBC3D6.11c	(Fig. 2B and C)
PMID:39786922	FYPO:0000443	abnormal protein localization during vegetative growth [assayed_protein] PomBase:SPBC3D6.11c	(Fig. 2B and C)
PMID:39786922	FYPO:0000443	abnormal protein localization during vegetative growth [assayed_protein] PomBase:SPBC3D6.11c	(Fig. 2B, C and D)
PMID:39786922	FYPO:0002339	decreased protein localization to nuclear periphery [has_severity] medium	(Fig. 4)
PMID:39786922	GO:0031934	mating-type region heterochromatin [exists_during] single-celled organism vegetative growth phase	(Fig. 5)
PMID:39786922	FYPO:0000644	normal protein localization during vegetative growth [assayed_protein] PomBase:SPBC3D6.11c	(Fig. 6)
PMID:39786922	FYPO:0000443	abnormal protein localization during vegetative growth [assayed_protein] PomBase:SPBC3D6.11c	(Fig. 6)
PMID:39786922	FYPO:0000443	abnormal protein localization during vegetative growth [assayed_protein] PomBase:SPBC3D6.11c	(Fig. 6)
PMID:39786922	FYPO:0003411	decreased chromatin silencing at centromere inner repeat [has_severity] low	(Fig. 7A)
PMID:39786922	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. 7A)
PMID:39786922	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase [has_severity] low [assayed_protein] PomBase:SPBC1105.17 [has_penetrance] 5	(Fig. 7B and C)
PMID:39786922	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase [has_severity] low [assayed_protein] PomBase:SPBC1105.17 [has_penetrance] 5	(Fig. 7B and C)
PMID:39786922	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase [assayed_protein] PomBase:SPBC1105.17 [has_penetrance] 3 [has_severity] medium	(Fig. 7B and C)
PMID:39786922	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase [assayed_protein] PomBase:SPBC1105.17 [has_severity] medium [has_penetrance] 35	(Fig. 7B and C)
PMID:39786922	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase [assayed_protein] PomBase:SPBC1105.17 [has_severity] low [has_penetrance] 10	(Fig. 7B and C)
PMID:39786922	FYPO:0006800	decreased centromere clustering at nuclear periphery during mitotic interphase [assayed_protein] PomBase:SPBC1105.17 [has_severity] medium [has_penetrance] 33	(Fig. 7B and C)
PMID:39786922	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. S1A)
PMID:39786922	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. S1A)
PMID:39786922	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. S1A)
PMID:39786922	GO:0034399	nuclear periphery [exists_during] single-celled organism vegetative growth phase	Sl8-GFP colocalizes with nuclear periphery labeled by Cut11-mCherry (Fig. 4A)
PMID:39786922	GO:0000775	chromosome, centromeric region [exists_during] single-celled organism vegetative growth phase	Slx8-GFP colocalizes wih Mis6-RFP (Fig. 5)
PMID:39786922	GO:0044732	mitotic spindle pole body [exists_during] single-celled organism vegetative growth phase	Slx8-GFP colocalizes with Sid4-RFP (Fig. 5)
PMID:39789818	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPBC530.14c	(Figure 4) (comment: Dsk1 phosphorylates Rad52 in vitro and in vivo).
PMID:39789818	FYPO:0006437	normal mitotic DNA damage checkpoint during cellular response to methyl methanesulfonate	Additionally, there were few septa when both dsk1+ and dsk1Δ were treated with MMS, and their number of septa was similarly increased after MMS release (Figure S2d). This result indicates that the cell cycle progression of dsk1Δ under MMS is arrested by functional checkpoints. To further support it biochemically, we tagged Chk1 with 3HA as we had no antibody against S. pombe Chk1. We found that the 3HA tag did not influence the genotoxic phenotype of chk1+ (Figure S2e). Immunoblots showed that Chk1-3HA in dsk1Δ was normally phosphorylated after MMS treatment (Figure S2f). Therefore, we conclude that dsk1Δ does not influence checkpoints activation.
PMID:39789818	FYPO:0006567	abnormal DNA repair	After CPT release, the percentage of Rad52 foci in dsk1Δ decreased more slowly than that in dsk1+ (Figures 2a and S3a,b), indicating a compromised HR repair in dsk1Δ. Second, we exploited a transformation-based genetic system (Figure 2b)
PMID:39789818	FYPO:0003912	decreased double-strand break repair via homologous recombination	As expected, the HR frequency of leu1 integration in rad51Δ cells was too low to be displayed. We also found that the HR frequency of leu1 integration in dsk1Δ cells was significantly reduced (Figure 2c), suggesting that Dsk1 may regulate the Rad52- and Rad51-dependent gene conversion sub-pathway of HR.
PMID:39789818	FYPO:0000829	resistance to cisplatin	Consistent with the phenotypes of deficiency of SKY1 and SRPKs, dsk1Δ also exhibited cisPt resistance.........(Figure 1a and Figure S1c).
PMID:39789818	GO:0005634	nucleus [exists_during] DNA damage response	Consistent with the previous study (Hayashi et al. 2009), Dsk1-GFP localized in both the nucleus and cytoplasm. After CPT treatment, the percentage of Dsk1-GFP translocated from cytoplasm to nucleus was increased, and dominantly accumulated in the nucleus (Figures 3a and S3c).
PMID:39789818	GO:0005737	cytoplasm	Consistent with the previous study (Hayashi et al. 2009), Dsk1-GFP localized in both the nucleus and cytoplasm. After CPT treatment, the percentage of Dsk1-GFP translocated from cytoplasm to nucleus was increased, and dominantly accumulated in the nucleus (Figures 3a and S3c).
PMID:39789818	FYPO:0004709	increased number of Rad52 foci [has_severity] medium	Furthermore, a high percentage of spontaneous Rad52-YFP foci was observed in rad52-S365D-YFP, but not in rad52-YFP and rad52-S365A-YFP, suggesting genomic instability of rad52- S365D-YFP.
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] high	However, dsk1Δ combined with mutations of DNA damage checkpoint effector chk1Δ and replication checkpoint effector cds1Δ, exhibited synergistic CPT and HU sensitivities (Figure S2b,c).
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] high	However, dsk1Δ combined with mutations of DNA damage checkpoint effector chk1Δ and replication checkpoint effector cds1Δ, exhibited synergistic CPT and HU sensitivities (Figure S2b,c).
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] high	However, dsk1Δ combined with mutations of DNA damage checkpoint effector chk1Δ and replication checkpoint effector cds1Δ, exhibited synergistic CPT and HU sensitivities (Figure S2b,c).
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] high	However, dsk1Δ combined with mutations of DNA damage checkpoint effector chk1Δ and replication checkpoint effector cds1Δ, exhibited synergistic CPT and HU sensitivities (Figure S2b,c).
PMID:39789818	FYPO:0007074	normal growth on mycophenolic acid	However, dsk1Δ was not sensitive to Bleomycin (Bleo), Phleomycin (Phleo), and UV irradiation, which directly break DNA, as well as 6-Azauracil (6-AU) and Mycophenolic acid (MPA), which impair transcription (Figure S1d).
PMID:39789818	FYPO:0000969	normal growth during cellular response to UV	However, dsk1Δ was not sensitive to Bleomycin (Bleo), Phleomycin (Phleo), and UV irradiation, which directly break DNA, as well as 6-Azauracil (6-AU) and Mycophenolic acid (MPA), which impair transcription (Figure S1d).
PMID:39789818	FYPO:0005517	normal growth on 6-azauracil	However, dsk1Δ was not sensitive to Bleomycin (Bleo), Phleomycin (Phleo), and UV irradiation, which directly break DNA, as well as 6-Azauracil (6-AU) and Mycophenolic acid (MPA), which impair transcription (Figure S1d).
PMID:39789818	FYPO:0003906	normal growth on bleomycin	However, dsk1Δ was not sensitive to Bleomycin (Bleo), Phleomycin (Phleo), and UV irradiation, which directly break DNA, as well as 6-Azauracil (6-AU) and Mycophenolic acid (MPA), which impair transcription (Figure S1d).
PMID:39789818	FYPO:0003183	normal growth on phleomycin	However, dsk1Δ was not sensitive to Bleomycin (Bleo), Phleomycin (Phleo), and UV irradiation, which directly break DNA, as well as 6-Azauracil (6-AU) and Mycophenolic acid (MPA), which impair transcription (Figure S1d).
PMID:39789818	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	In addition, dsk1Δ was consistently but marginally sensitive to HU. .........(Figure 1a and Figure S1c).
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] medium	In line with this, the spacer truncation mutant was also sensitive to CPT (Figure 1e).
PMID:39789818	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	Interestingly, we found that dsk1Δ was highly sensitive to replication-associated DNA break agents like camptothecin (CPT), which is a topoisomerase I inhibitor, and was slightly sensitive to methyl methanesulfonate (MMS), which alkylates and breaks DNA during replication (Figure 1a and Figure S1c).
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] low	Interestingly, we found that dsk1Δ was highly sensitive to replication-associated DNA break agents like camptothecin (CPT), which is a topoisomerase I inhibitor, and was slightly sensitive to methyl methanesulfonate (MMS), which alkylates and breaks DNA during replication (Figure 1a and Figure S1c).
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] low	Interestingly, we found that dsk1Δ was highly sensitive to replication-associated DNA break agents like camptothecin (CPT), which is a topoisomerase I inhibitor, and was slightly sensitive to methyl methanesulfonate (MMS), which alkylates and breaks DNA during replication (Figure 1a and Figure S1c).
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] high	Interestingly, we found that dsk1Δ was highly sensitive to replication-associated DNA break agents like camptothecin (CPT), which is a topoisomerase I inhibitor, and was slightly sensitive to methyl methanesulfonate (MMS), which alkylates and breaks DNA during replication (Figure 1a and Figure S1c).
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] medium	It showed CPT sensitivity compared with its isogenic dsk1-5FLAG control, but not as severe as dsk1Δ (Figure 1d). To avoid the negative effects of the FLAG tag, we created a dsk1-K110A mutant without the tag, and it also showed the sensitivity of CPT (Figure S1e)
PMID:39789818	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	Moreover, the rad52-S365D/E-YFP displayed higher sensitivities to HU, CPT, and MMS rather than cisPt (Figure 5a).
PMID:39789818	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	Moreover, the rad52-S365D/E-YFP displayed higher sensitivities to HU, CPT, and MMS rather than cisPt (Figure 5a).
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] medium	Moreover, the rad52-S365D/E-YFP displayed higher sensitivities to HU, CPT, and MMS rather than cisPt (Figure 5a).
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] medium	Moreover, the rad52-S365D/E-YFP displayed higher sensitivities to HU, CPT, and MMS rather than cisPt (Figure 5a).
PMID:39789818	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	Moreover, the rad52-S365D/E-YFP displayed higher sensitivities to HU, CPT, and MMS rather than cisPt (Figure 5a).
PMID:39789818	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	Moreover, the rad52-S365D/E-YFP displayed higher sensitivities to HU, CPT, and MMS rather than cisPt (Figure 5a).
PMID:39789818	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	Moreover, we found that dsk1Δ together with mutations of PRR genes rhp18Δ (translesion synthesis) (Figure S2g) and ubc13Δ (template switching) (Figure S2h) were additively defective in response to CPT and MMS treatments, suggesting that Dsk1 and PRR are in parallel and distinct pathways in response to replication stress.
PMID:39789818	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	Moreover, we found that dsk1Δ together with mutations of PRR genes rhp18Δ (translesion synthesis) (Figure S2g) and ubc13Δ (template switching) (Figure S2h) were additively defective in response to CPT and MMS treatments, suggesting that Dsk1 and PRR are in parallel and distinct pathways in response to replication stress.
PMID:39789818	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	Moreover, we found that dsk1Δ together with mutations of PRR genes rhp18Δ (translesion synthesis) (Figure S2g) and ubc13Δ (template switching) (Figure S2h) were additively defective in response to CPT and MMS treatments, suggesting that Dsk1 and PRR are in parallel and distinct pathways in response to replication stress.
PMID:39789818	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	Moreover, we found that dsk1Δ together with mutations of PRR genes rhp18Δ (translesion synthesis) (Figure S2g) and ubc13Δ (template switching) (Figure S2h) were additively defective in response to CPT and MMS treatments, suggesting that Dsk1 and PRR are in parallel and distinct pathways in response to replication stress.
PMID:39789818	FYPO:0000482	decreased mitotic recombination	On the contrary, dsk1Δ cells displayed about a fivefold reduction in spontaneous recombination rate, mainly in the aspect of gene conversion rather than gene deletion (Figure 2g).
PMID:39789818	FYPO:0000957	normal growth on methyl methanesulfonate	The rad52-S365A-YFP was slightly sensitive to HU and CPT, but not to MMS and cisPt.
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] low	The rad52-S365A-YFP was slightly sensitive to HU and CPT, but not to MMS and cisPt.
PMID:39789818	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	The rad52-S365A-YFP was slightly sensitive to HU and CPT, but not to MMS and cisPt.
PMID:39789818	FYPO:0001023	normal growth on cisplatin	The rad52-S365A-YFP was slightly sensitive to HU and CPT, but not to MMS and cisPt.
PMID:39789818	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	The results of spot assays revealed that rad52Δ strain as a positive control grew slowly and exhibited pronounced sensitivities to all tested drugs. FIGURE 5 | The defective genotoxic and HR phenotypes of Rad52-Ser365 phosphorylation-defective and -mimicking mutants
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] high	The results of spot assays revealed that rad52Δ strain as a positive control grew slowly and exhibited pronounced sensitivities to all tested drugs. FIGURE 5 | The defective genotoxic and HR phenotypes of Rad52-Ser365 phosphorylation-defective and -mimicking mutants
PMID:39789818	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	The results of spot assays revealed that rad52Δ strain as a positive control grew slowly and exhibited pronounced sensitivities to all tested drugs. FIGURE 5 | The defective genotoxic and HR phenotypes of Rad52-Ser365 phosphorylation-defective and -mimicking mutants
PMID:39789818	FYPO:0000102	sensitive to cisplatin [has_severity] high	The results of spot assays revealed that rad52Δ strain as a positive control grew slowly and exhibited pronounced sensitivities to all tested drugs. FIGURE 5 | The defective genotoxic and HR phenotypes of Rad52-Ser365 phosphorylation-defective and -mimicking mutants
PMID:39789818	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC30D11.10 [part_of] positive regulation of double-strand break repair via homologous recombination	We also purified 6His-Rad52-S365A and 6His-Rad52-S367A proteins and found that the abundance of the phosphorylated peptide of Rad52-S367A was significantly higher than that of Rad52-S365A when incubated with GST- Dsk1 (Figure 4f,g). Together, these in vitro data strongly indicate that Dsk1 directly phosphorylates Rad52-Ser365. Together, these results suggest that Dsk1-mediated Rad52-Ser365 phosphorylation is probably one of the mechanisms for Dsk1 regulating HR repair.
PMID:39789818	FYPO:0004466	increased number of Rad52 foci during cellular response to camptothecin	We exploited the YFP-tagged Rad52 strain and found that the percentage (45%) of Rad52-YFP fluorescent foci in dsk1Δ cells was elevated almost 100-fold relative to the percentage (0.5%) of that in WT cells under physiological conditions, suggesting more spontaneous DNA damage induced by dsk1Δ.
PMID:39789818	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC644.14c [assayed_protein] PomBase:SPAC30D11.10 [has_severity] low	We found that the association affinity between Rad52-YFP and Rad51 was marginally affected by dsk1Δ (Figure S7b).
PMID:39789818	FYPO:0002679	decreased protein phosphorylation [assayed_protein] PomBase:SPAC30D11.10	We found that the levels of the indicated phosphorylated peptide of Rad52-YFP were substantially reduced in dsk1Δ, whereas no differences in the levels of unmodified peptides (Figure 4h). The remaining Rad52 phosphorylation in dsk1Δ suggests that there are redundant kinases of Rad52 in vivo. Moreover, Ser319 was predicted as the major phosphorylated residue in this indicated Rad52 peptide (Figure 4h).
PMID:39789818	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	We then overexpressed dsk1+ from the constitutive adh21 promoter with medium strength at the lys1 locus of S. pombe genome (Chen et al. 2017). This made the cells highly sensitive to CPT and marginally sensitive to MMS (Figure 1g).
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] high	We then overexpressed dsk1+ from the constitutive adh21 promoter with medium strength at the lys1 locus of S. pombe genome (Chen et al. 2017). This made the cells highly sensitive to CPT and marginally sensitive to MMS (Figure 1g).
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] high	When combined with dsk1Δ, obviously synthetic effects were observed for CPT treatment, and slightly additive effects were observed for HU and MMS treatment (Figure 5a)
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] high	When combined with dsk1Δ, obviously synthetic effects were observed for CPT treatment, and slightly additive effects were observed for HU and MMS treatment (Figure 5a)
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] high	When combined with dsk1Δ, obviously synthetic effects were observed for CPT treatment, and slightly additive effects were observed for HU and MMS treatment (Figure 5a)
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] high	When combined with dsk1Δ, obviously synthetic effects were observed for CPT treatment, and slightly additive effects were observed for HU and MMS treatment (Figure 5a)
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] high	When combined with dsk1Δ, obviously synthetic effects were observed for CPT treatment, and slightly additive effects were observed for HU and MMS treatment (Figure 5a)
PMID:39789818	FYPO:0000085	sensitive to camptothecin [has_severity] high	When combined with dsk1Δ, obviously synthetic effects were observed for CPT treatment, and slightly additive effects were observed for HU and MMS treatment (Figure 5a)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:39878217	FYPO:0002061	inviable vegetative cell population	(Fig. 1B)
PMID:39878217	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1E)
PMID:39878217	FYPO:0000085	sensitive to camptothecin	(Fig. 1E)
PMID:39878217	FYPO:0001690	normal growth on camptothecin	(Fig. 1E)
PMID:39878217	FYPO:0001690	normal growth on camptothecin	(Fig. 1E)
PMID:39878217	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1E)
PMID:39878217	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1E)
PMID:39878217	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1E)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. 1E)
PMID:39878217	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 1E)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. 1E)
PMID:39878217	FYPO:0000085	sensitive to camptothecin	(Fig. 1E)
PMID:39878217	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 1E)
PMID:39878217	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1E)
PMID:39878217	FYPO:0000085	sensitive to camptothecin	(Fig. 1E)
PMID:39878217	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 1E)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. 1E)
PMID:39878217	FYPO:0000089	sensitive to methyl methanesulfonate	(Fig. 1E)
PMID:39878217	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1E, Fig. 6A, 6E)
PMID:39878217	FYPO:0004240	decreased histone H3-K56 acetylation during vegetative growth [has_severity] high	(Fig. 1F)
PMID:39878217	FYPO:0004240	decreased histone H3-K56 acetylation during vegetative growth [has_severity] high	(Fig. 1F)
PMID:39878217	FYPO:0004240	decreased histone H3-K56 acetylation during vegetative growth [has_severity] high	(Fig. 1F)
PMID:39878217	FYPO:0008160	normal histone H3-K56 acetylation during vegetative growth	(Fig. 1F)
PMID:39878217	FYPO:0004240	decreased histone H3-K56 acetylation during vegetative growth [has_severity] high	(Fig. 1F)
PMID:39878217	GO:0042393	histone binding [has_input] PomBase:SPBC8D2.03c	(Fig. 2)
PMID:39878217	GO:0042393	histone binding [has_input] PomBase:SPBC1105.11c	(Fig. 2)
PMID:39878217	GO:0042393	histone binding [has_input] PomBase:SPAC1834.04	(Fig. 2)
PMID:39878217	GO:0042393	histone binding [has_input] PomBase:SPBC8D2.04	(Fig. 2)
PMID:39878217	GO:0042393	histone binding [has_input] PomBase:SPBC1105.12	(Fig. 2)
PMID:39878217	GO:0042393	histone binding [has_input] PomBase:SPAC1834.03c	(Fig. 2)
PMID:39878217	FYPO:0003247	abolished histone H3 binding	(Fig. 2E)
PMID:39878217	FYPO:0007158	decreased histone H3 binding	(Fig. 2E)
PMID:39878217	FYPO:0007158	decreased histone H3 binding	(Fig. 2E)
PMID:39878217	FYPO:0008272	normal histone H3 binding	(Fig. 2E)
PMID:39878217	FYPO:0008272	normal histone H3 binding	(Fig. 2E)
PMID:39878217	FYPO:0003247	abolished histone H3 binding	(Fig. 2E)
PMID:39878217	FYPO:0003247	abolished histone H3 binding	(Fig. 2E)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. 3I)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 3I)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. 4A)
PMID:39878217	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC1071.09c [assayed_protein] PomBase:SPBC8D2.04 [has_severity] medium	(Fig. 4C, 4D)
PMID:39878217	FYPO:0001645	decreased protein-protein interaction [has_severity] high [assayed_protein] PomBase:SPAC1071.09c [assayed_protein] PomBase:SPBC8D2.04	(Fig. 4C, 4D)
PMID:39878217	FYPO:0008392	normal level of histone H4 in cell	(Fig. 5A)
PMID:39878217	FYPO:0005336	normal level of histone H3 in cell	(Fig. 5A)
PMID:39878217	FYPO:0007324	decreased level of histone H4 in cell	(Fig. 5A)
PMID:39878217	FYPO:0004578	decreased level of histone H3 in cell	(Fig. 5A)
PMID:39878217	FYPO:0008392	normal level of histone H4 in cell	(Fig. 5A)
PMID:39878217	FYPO:0005336	normal level of histone H3 in cell	(Fig. 5A)
PMID:39878217	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 5E)
PMID:39878217	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 5E)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 5F)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 5F)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 5F)
PMID:39878217	FYPO:0008390	increased level of histone H3 in cell	(Fig. 6B)
PMID:39878217	FYPO:0008391	increased level of histone H4 in cell	(Fig. 6B)
PMID:39878217	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 6E)
PMID:39878217	FYPO:0000963	normal growth on hydroxyurea	(Fig. 6E)
PMID:39878217	FYPO:0000963	normal growth on hydroxyurea	(Fig. 6E)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 7A)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 7A)
PMID:39878217	FYPO:0000674	normal cell population growth at high temperature	(Fig. S1E)
PMID:39878217	FYPO:0000674	normal cell population growth at high temperature	(Fig. S1E)
PMID:39878217	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S1E)
PMID:39878217	FYPO:0000674	normal cell population growth at high temperature	(Fig. S1E)
PMID:39878217	FYPO:0000674	normal cell population growth at high temperature	(Fig. S1E)
PMID:39878217	FYPO:0000674	normal cell population growth at high temperature	(Fig. S1E)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. S1E)
PMID:39878217	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC1071.09c [assayed_protein] PomBase:SPAC13G7.02c	(Fig. S1G)
PMID:39878217	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC1071.09c [assayed_protein] PomBase:SPAC13G7.02c	(Fig. S1G)
PMID:39878217	FYPO:0007158	decreased histone H3 binding	(Fig. S3A)
PMID:39878217	FYPO:0003247	abolished histone H3 binding	(Fig. S3B)
PMID:39878217	FYPO:0003247	abolished histone H3 binding	(Fig. S3B)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. S3C, S3D)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. S3C, S3D)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S3C, S3D)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. S3C, S3D)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. S3C, S3D)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S3D)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. S3D)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. S3D)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. S3D)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. S3D)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. S3D)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. S3D)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. S3D)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. S3D)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S3D)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. S5E)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S5E, S5F)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S5F)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S5F)
PMID:39878217	FYPO:0000088	sensitive to hydroxyurea	(Fig. S6A)
PMID:39878217	FYPO:0000088	sensitive to hydroxyurea	(Fig. S6A)
PMID:39878217	FYPO:0006993	decreased chromatin silencing at centromere otr1R [has_severity] high	(Fig. S7A)
PMID:39878217	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. S7A)
PMID:39878217	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. S7A)
PMID:39878217	FYPO:0006992	normal chromatin silencing at centromere otr1R	(Fig. S7A)
PMID:39878217	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. S7B)
PMID:39878217	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. S7B)
PMID:39878217	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. S7B)
PMID:39878217	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] medium	(Fig. S7B)
PMID:39878217	FYPO:0005751	normal growth on Zeocin	(Fig. S7D)
PMID:39878217	FYPO:0005750	sensitive to Zeocin	(Fig. S7D)
PMID:39878217	FYPO:0000674	normal cell population growth at high temperature	(Fig. S7E)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. S7E)
PMID:39878217	FYPO:0001357	normal vegetative cell population growth	(Fig. S7E)
PMID:39878217	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S7E)
PMID:39878217	FYPO:0004481	abolished cell population growth at high temperature	(Fig. S7E)
PMID:39878217	FYPO:0000674	normal cell population growth at high temperature	(Fig. S7E)
PMID:39878217	FYPO:0005751	normal growth on Zeocin	(Fig. S7G)
PMID:39878217	FYPO:0005751	normal growth on Zeocin	(Fig. S7G)
PMID:39878217	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. S7G)
PMID:39878217	FYPO:0001690	normal growth on camptothecin	(Fig. S7G)
PMID:39878217	FYPO:0001690	normal growth on camptothecin	(Fig. S7G)
PMID:39878217	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. S7G)
PMID:39878217	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. S7G)
PMID:39878217	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. S7G)
PMID:39878217	FYPO:0005750	sensitive to Zeocin [has_severity] high	(Fig. S7G)
PMID:39878217	GO:0036205	histone catabolic process	Our study reveals that as a binding protein for the histone H3-H4 dimer, Djc9 acts with Hsp70 to promote the proteasomal degradation of excess histones. Its activity is restrained by the competitive binding of H3-H4 by Asf1, whose essential function in fission yeast is restricting histone degradation by Djc9. (Fig. 5 and Fig. 6)
PMID:39880258	GO:0016929	deSUMOylase activity [has_input] PomBase:SPBC365.06	(kcat) was computed as 9.08 s-1. The Michaelis-Menten constant, KM was determined as 0.65 × 101 μM with a maximum velocity (Vmax) of 0.045 μM/s. The substrate specificity ratio, kcat/KM was calculated to be 1.39 × 106 M-1 s-1.
PMID:39910760	GO:0030291	protein serine/threonine kinase inhibitor activity [has_input] PomBase:SPBC216.07c [part_of] negative regulation of TORC1 signaling	Ecl1, which physically interacts with Mip1, reduces TORC1 activity regardless of Thr7 mutation
PMID:39910760	FYPO:0000280	sterile [has_penetrance] complete	First, we investigated the conjugation rate in the stationary phase. Overexpression of wild-type Ecl1 and Ecl1-22D, but not the empty vector or Ecl1-7D, rescued the conjugation defect in the stationary phase of Δecls cells (Figure 3b), suggesting a significant loss of activity in Ecl1-7D.
PMID:39910760	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	Furthermore, the Ecl1-overexpression reduced TORC1 activity regardless of the presence or absence of sulfur (Figure 5e,f). In other words, even during the logarithmic growth phase, when Thr7 is phosphorylated and Ecl function is suppressed, Ecl1 overexpression sufficiently reduces TORC1 activity. These results indicated that phosphorylation of the N-terminus of Ecl1 had little effect on TORC1 repression and that the expression of Ecl1, rather than starvation conditions, was important for TORC1 repression.
PMID:39910760	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	Furthermore, the Ecl1-overexpression reduced TORC1 activity regardless of the presence or absence of sulfur (Figure 5e,f). In other words, even during the logarithmic growth phase, when Thr7 is phosphorylated and Ecl function is suppressed, Ecl1 overexpression sufficiently reduces TORC1 activity. These results indicated that phosphorylation of the N-terminus of Ecl1 had little effect on TORC1 repression and that the expression of Ecl1, rather than starvation conditions, was important for TORC1 repression.
PMID:39910760	FYPO:0001309	increased viability in stationary phase	Furthermore, the overexpression of the Ecl1 fusion protein using this plasmid led to CLS extension, suggesting that the protein was functional (Figure 1c).
PMID:39910760	MOD:00046	O-phospho-L-serine [decreased_during] cellular response to sulfur starvation	GST protein purified from cultures under each condition revealed the phosphorylation of Thr7, Ser22, Ser61, Thr63, and Thr69 of Ecl1 protein in the nutrient-rich environment (Figure 1d; Figure S1). Under conditions of sulfur or metal starvation,...... but those of Thr7 and Ser22 (situated near the N-terminus) decreased.
PMID:39910760	MOD:00047	O-phospho-L-threonine [decreased_during] cellular response to sulfur starvation	GST protein purified from cultures under each condition revealed the phosphorylation of Thr7, Ser22, Ser61, Thr63, and Thr69 of Ecl1 protein in the nutrient-rich environment (Figure 1d; Figure S1). Under conditions of sulfur or metal starvation,...... but those of Thr7 and Ser22 (situated near the N-terminus) decreased.
PMID:39910760	FYPO:0001309	increased viability in stationary phase [has_severity] low	If CLS extension by Ecl1 is mediated by the same pathway as TORC1, no additive CLS extension would be observed if Ecl1 was overexpressed in a TORC1 subunit-deficient cell. Although wat1+ deletion or ecl1+ overexpression extended the CLS, overexpression of ecl1+ in the wat1-deficient cells did not result in further CLS extension, suggesting that Ecl1 and Wat1 function in CLS extension through the same pathway.
PMID:39910760	FYPO:0001309	increased viability in stationary phase [has_severity] medium	If CLS extension by Ecl1 is mediated by the same pathway as TORC1, no additive CLS extension would be observed if Ecl1 was overexpressed in a TORC1 subunit-deficient cell. Although wat1+ deletion or ecl1+ overexpression extended the CLS, overexpression of ecl1+ in the wat1-deficient cells did not result in further CLS extension, suggesting that Ecl1 and Wat1 function in CLS extension through the same pathway.
PMID:39910760	FYPO:0001309	increased viability in stationary phase [has_severity] medium	If CLS extension by Ecl1 is mediated by the same pathway as TORC1, no additive CLS extension would be observed if Ecl1 was overexpressed in a TORC1 subunit-deficient cell. Although wat1+ deletion or ecl1+ overexpression extended the CLS, overexpression of ecl1+ in the wat1-deficient cells did not result in further CLS extension, suggesting that Ecl1 and Wat1 function in CLS extension through the same pathway. (However, because Wat1 is a component of TORC1 and TORC2 (Ahamad et al., 2018), further experiments are required to clarify whether Ecl1-induced CLS extension is exclusively mediated by TORC1)
PMID:39910760	FYPO:0004085	decreased vegetative cell growth	In addition, Ecl1 fusion protein overexpression slowed the growth rate, similar to a previous report of Ecl1- overexpression (Ohtsuka et al., 2024a) (Figure 1c).
PMID:39910760	FYPO:0004085	decreased vegetative cell growth	In addition, Ecl1 fusion protein overexpression slowed the growth rate, similar to a previous report of Ecl1- overexpression (Ohtsuka et al., 2024a) (Figure 1c).
PMID:39910760	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC4G3.08	TORC1 activity was reported to decrease in an ecl gene-dependent manner under conditions of sulfur or phosphate starvation (Ohtsuka et al., 2022a, 2023c) (Figure 5a).
PMID:39910760	FYPO:0005097	abnormal cell cycle arrest in mitotic G1 phase	The number of cells in the G1 phase was considerably reduced in cells harboring pE- cl1-DD (Figure 2e)..
PMID:39910760	FYPO:0000644	normal protein localization during vegetative growth [has_penetrance] complete [assayed_protein] PomBase:SPCC70.12c	This suggested that phosphorylation of the N-terminus of Ecl1 was unlikely to significantly affect the intracellular localization of Ecl1.
PMID:39910760	FYPO:0000644	normal protein localization during vegetative growth [has_penetrance] complete [assayed_protein] PomBase:SPCC70.12c	This suggested that phosphorylation of the N-terminus of Ecl1 was unlikely to significantly affect the intracellular localization of Ecl1.
PMID:39910760	FYPO:0000708	decreased mating efficiency	This suggested that the Ecl1-AA mutant protein activity was comparable to that of the wild-type Ecl1 protein. Meanwhile, when Ecl1-DD was expressed, the recovery was low, and the degree of recovery was significantly lower than that of Ecl1 and Ecl1-AA. This suggested that the activity or stability of the Ecl1-DD mutant protein, which mimics the phosphorylation of Thr7 and Ser22, was reduced compared with the wild-type Ecl1 protein. (comment: (vw: there was no WT assay, but compared to WT in the same background))
PMID:39910760	FYPO:0000708	decreased mating efficiency	This suggested that the Ecl1-AA mutant protein activity was comparable to that of the wild-type Ecl1 protein. Meanwhile, when Ecl1-DD was expressed, the recovery was low, and the degree of recovery was significantly lower than that of Ecl1 and Ecl1-AA. This suggested that the activity or stability of the Ecl1-DD mutant protein, which mimics the phosphorylation of Thr7 and Ser22, was reduced compared with the wild-type Ecl1 protein. (comment: (vw: there was no WT assay, but compared to WT in the same background))
PMID:39910760	FYPO:0000708	decreased mating efficiency [has_severity] high	This suggested that the Ecl1-AA mutant protein activity was comparable to that of the wild-type Ecl1 protein. Meanwhile, when Ecl1-DD was expressed, the recovery was low, and the degree of recovery was significantly lower than that of Ecl1 and Ecl1-AA. This suggested that the activity or stability of the Ecl1-DD mutant protein, which mimics the phosphorylation of Thr7 and Ser22, was reduced compared with the wild-type Ecl1 protein. (comment: (vw: there was no WT assay, but compared to WT in the same background))
PMID:39910760	GO:0005737	cytoplasm	To investigate this, we observed the intracellular localization of the Ecl1-GFP fusion protein (Figure 4a). Regardless of mutations at Thr7 and Ser22, the Ecl1-GFP fusion protein was mainly localized in the nucleus during logarithmic growth and was also observed in the cytoplasm.
PMID:39910760	GO:0005634	nucleus	To investigate this, we observed the intracellular localization of the Ecl1-GFP fusion protein (Figure 4a). Regardless of mutations at Thr7 and Ser22, the Ecl1-GFP fusion protein was mainly localized in the nucleus during logarithmic growth and was also observed in the cytoplasm.
PMID:39910760	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC57A7.11 [assayed_protein] PomBase:SPCC70.12c	We investigated the effect of phosphorylation mutations of Ecl1 on the binding of TORC1 subunit Mip1 to Ecl1 (Figure 5i). Mip1-HA protein did not coprecipitate with GFP but did coprecipitate wild-type Ecl1 and with Ecl1 proteins with mutations at Thr7 or Ser22.
PMID:39910760	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC57A7.11 [assayed_protein] PomBase:SPCC70.12c	We investigated the effect of phosphorylation mutations of Ecl1 on the binding of TORC1 subunit Mip1 to Ecl1 (Figure 5i). Mip1-HA protein did not coprecipitate with GFP but did coprecipitate wild-type Ecl1 and with Ecl1 proteins with mutations at Thr7 or Ser22.
PMID:39910760	FYPO:0000280	sterile [has_penetrance] complete	When Δecls cells were cultured in EMM, mating did not occur, not even in the stationary phase, but this defect was restored by the expression of wild-type Ecl1 or Ecl1-AA proteins by plasmids (Figure 2b).
PMID:39916665	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1C)
PMID:39916665	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1C)
PMID:39916665	FYPO:0001357	normal vegetative cell population growth	(Fig. 1C)
PMID:39916665	FYPO:0001357	normal vegetative cell population growth	(Fig. 1C)
PMID:39916665	FYPO:0001357	normal vegetative cell population growth	(Fig. 1C)
PMID:39916665	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1C)
PMID:39916665	FYPO:0009007	decreased vegetative cell population viability	(Fig. 2A)
PMID:39916665	FYPO:0003166	monoseptate vegetative cell with binucleate and anucleate compartments [has_penetrance] 9.7	(Fig. 3C, 3D)
PMID:39916665	FYPO:0004562	binucleate aseptate vegetative cell [has_penetrance] 20	(Fig. 3C, 3D)
PMID:39916665	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 30	(Fig. 4C, 4D)
PMID:39916665	FYPO:0003241	unequal mitotic sister chromatid segregation [has_penetrance] 25	(Fig. 4C, 4D)
PMID:39916665	FYPO:0001357	normal vegetative cell population growth	(Fig. S1A)
PMID:39916665	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S1A)
PMID:39916665	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S1A)
PMID:39916665	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. S1A)
PMID:39916665	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. S1A)
PMID:39916665	FYPO:0001357	normal vegetative cell population growth	(Fig. S1A)
PMID:39916665	FYPO:0004710	increased number of Rad52 foci during G0 to G1 transition	(Fig. S2)
PMID:39916665	FYPO:0001127	abnormal cell size [has_penetrance] 22	(Fig. S3)
PMID:39916665	FYPO:0002090	lagging chromosomes [has_penetrance] 12	(Fig. S3)
PMID:39945308	FYPO:0001132	abolished protein localization to heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC622.16c	(Fig. 1C)
PMID:39945308	FYPO:0001645	decreased protein-protein interaction [assayed_protein] PomBase:SPAC664.01c [assayed_protein] PomBase:SPCC622.16c	(Fig. 1D)
PMID:39945308	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] low	(Fig. 1F)
PMID:39945308	FYPO:0007334	abolished chromatin silencing at centromere outer repeat	(Fig. 1F)
PMID:39945308	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_penetrance] low	(Fig. 1F)
PMID:39945308	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 4C and 4E)
PMID:39945308	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] low	(Fig. 4C and 4E)
PMID:39945308	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 4C and 4E)
PMID:39945308	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 4C, 4D and 4E)
PMID:39945308	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 4D and 4E)
PMID:39945308	FYPO:0002336	normal chromatin silencing at silent mating-type cassette	(Fig. 4D and 4E)
PMID:39945308	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [has_severity] high	(Fig. 4D and 4E)
PMID:39945308	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPBP35G2.10	(Fig. 4F)
PMID:39945308	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBP35G2.10 [has_severity] medium	(Fig. 4F)
PMID:39945308	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBP35G2.10 [has_severity] medium	(Fig. 4F)
PMID:39945308	FYPO:0003573	decreased protein localization to heterochromatin at silent mating-type cassette [assayed_protein] PomBase:SPBP35G2.10 [has_severity] high	(Fig. 4F)
PMID:39945308	FYPO:0008153	abolished protein localization to heterochromatin at  silent mating-type cassette during vegetative growth [assayed_protein] PomBase:SPBP35G2.10	(Fig. 4F)
PMID:39945308	FYPO:0001132	abolished protein localization to heterochromatin during vegetative growth [assayed_protein] PomBase:SPCC622.16c	(Fig. S1E)
PMID:40015273	FYPO:0001352	abnormal chromatin organization during vegetative growth [assayed_region] PomBase:SPAC1002.16c	(Figure 7) (comment: CHECK decreased localization of chromatin region to nuclear periphery)
PMID:40015273	FYPO:0001352	abnormal chromatin organization during vegetative growth [assayed_region] PomBase:SPAC1002.16c	(Figure 7) (comment: CHECK decreased localization of chromatin region to nuclear periphery)
PMID:40015273	GO:0031491	nucleosome binding	Although histones were abundantly pulled down in all low stringency IPs, including the untagged control, this interaction was uniquely preserved for Pap1 and the heterodimeric TFs Atf1 and Pcr1 amongst TFs investigated under high stringency conditions (Figure 5C, Figure S5C)
PMID:40015273	GO:0031491	nucleosome binding	Although histones were abundantly pulled down in all low stringency IPs, including the untagged control, this interaction was uniquely preserved for Pap1 and the heterodimeric TFs Atf1 and Pcr1 amongst TFs investigated under high stringency conditions (Figure 5C, Figure S5C)
PMID:40015273	GO:0031491	nucleosome binding	Although histones were abundantly pulled down in all low stringency IPs, including the untagged control, this interaction was uniquely preserved for Pap1 and the heterodimeric TFs Atf1 and Pcr1 amongst TFs investigated under high stringency conditions (Figure 5C, Figure S5C)
PMID:40015273	GO:0140311	protein sequestering activity [has_input] PomBase:SPBC27B12.11c	Notably, Rad24 is known to negatively regulate Pho7- dependent pho1+ expression, with its deletion resulting in increased pho1+ levels even under phosphate-replete conditions82-84. Mechanistically, Rad24 has been linked to the regulation of an upstream long non-coding RNA (lncRNA), which is known to interfere with pho1+ expression in the absence of stress84,85. Our data suggests an alternative mechanism where Rad24, and potentially Rad25, directly interact with and negatively regulate Pho7, which would explain the de-repression of pho1+ in rad24Δ mutants. We identified two optimal 14-3-3 binding motifs78 in Pho7, corresponding to phosphorylated serine and threonine residues (RVCSAP (pS230) and RSFTNP (pT463))86-89 (Figure 6B). These motifs flank the Pho7 DBD, indicating that Rad24/Rad25 interactions could interfere with Pho7 DNA binding, similar to the mechanism proposed for the mammalian TF FOXO4
PMID:40015273	GO:0140311	protein sequestering activity [has_input] PomBase:SPBC27B12.11c	Notably, Rad24 is known to negatively regulate Pho7- dependent pho1+ expression, with its deletion resulting in increased pho1+ levels even under phosphate-replete conditions82-84. Mechanistically, Rad24 has been linked to the regulation of an upstream long non-coding RNA (lncRNA), which is known to interfere with pho1+ expression in the absence of stress84,85. Our data suggests an alternative mechanism where Rad24, and potentially Rad25, directly interact with and negatively regulate Pho7, which would explain the de-repression of pho1+ in rad24Δ mutants. We identified two optimal 14-3-3 binding motifs78 in Pho7, corresponding to phosphorylated serine and threonine residues (RVCSAP (pS230) and RSFTNP (pT463))86-89 (Figure 6B). These motifs flank the Pho7 DBD, indicating that Rad24/Rad25 interactions could interfere with Pho7 DNA binding, similar to the mechanism proposed for the mammalian TF FOXO4
PMID:40063661	GO:0034063	stress granule assembly	(Fig 4D and 4E). Hence like their human orthologs, Cpn1 and Nxt3 are required to promote stress granule formation.
PMID:40063661	GO:0034063	stress granule assembly	(Fig 4D and 4E). Hence like their human orthologs, Cpn1 and Nxt3 are required to promote stress granule formation.
PMID:40063661	FYPO:0008413	increased establishment of chromatin silencing at centromere outer repeat region [has_severity] high [has_penetrance] 50	(Fig. 1E)
PMID:40063661	FYPO:0008413	increased establishment of chromatin silencing at centromere outer repeat region [has_penetrance] 10 [has_severity] low	(Fig. 1E)
PMID:40063661	FYPO:0008413	increased establishment of chromatin silencing at centromere outer repeat region [has_severity] low [has_penetrance] 10	(Fig. 1E)
PMID:40063661	FYPO:0007223	decreased establishment of chromatin silencing at centromere outer repeat region [has_severity] high [has_penetrance] 20	(Fig. 1F)
PMID:40063661	FYPO:0007223	decreased establishment of chromatin silencing at centromere outer repeat region [has_severity] high [has_penetrance] 75	(Fig. 1F)
PMID:40063661	FYPO:0007223	decreased establishment of chromatin silencing at centromere outer repeat region [has_severity] medium [has_penetrance] 80	(Fig. 1F)
PMID:40063661	FYPO:0007223	decreased establishment of chromatin silencing at centromere outer repeat region [has_severity] high [has_penetrance] 80	(Fig. 2A, 2C, 2D)
PMID:40063661	FYPO:0004744	normal heterochromatin maintenance involved in chromatin silencing at centromere outer repeat	(Fig. 2A, 3E)
PMID:40063661	FYPO:0003101	decreased heterochromatin assembly at protein coding gene [assayed_region] PomBase:SPCC1442.04c	(Fig. 2G)
PMID:40063661	FYPO:0003101	decreased heterochromatin assembly at protein coding gene [assayed_region] PomBase:SPCC1442.04c	(Fig. 2G)
PMID:40063661	FYPO:0003101	decreased heterochromatin assembly at protein coding gene [assayed_region] PomBase:SPCC1442.04c	(Fig. 2G)
PMID:40063661	FYPO:0003101	decreased heterochromatin assembly at protein coding gene [assayed_region] PomBase:SPCC1442.04c	(Fig. 2G)
PMID:40063661	FYPO:0007224	decreased heterochromatin assembly at centromere outer repeat during vegetative growth [has_severity] low	(Fig. 2H)
PMID:40063661	FYPO:0007224	decreased heterochromatin assembly at centromere outer repeat during vegetative growth [has_severity] low	(Fig. 2H)
PMID:40063661	FYPO:0007224	decreased heterochromatin assembly at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 2H)
PMID:40063661	FYPO:0007224	decreased heterochromatin assembly at centromere outer repeat during vegetative growth [has_severity] medium	(Fig. 2H)
PMID:40063661	FYPO:0007224	decreased heterochromatin assembly at centromere outer repeat during vegetative growth [has_severity] high	(Fig. 2H)
PMID:40063661	FYPO:0007223	decreased establishment of chromatin silencing at centromere outer repeat region [has_severity] low	(Fig. 2H, 3F)
PMID:40063661	FYPO:0004744	normal heterochromatin maintenance involved in chromatin silencing at centromere outer repeat	(Fig. 3E)
PMID:40063661	FYPO:0004744	normal heterochromatin maintenance involved in chromatin silencing at centromere outer repeat	(Fig. 3E)
PMID:40063661	FYPO:0004744	normal heterochromatin maintenance involved in chromatin silencing at centromere outer repeat	(Fig. 3E)
PMID:40063661	FYPO:0008413	increased establishment of chromatin silencing at centromere outer repeat region [has_severity] low [has_penetrance] 15	(Fig. 3F)
PMID:40063661	FYPO:0007223	decreased establishment of chromatin silencing at centromere outer repeat region [has_severity] high [has_penetrance] 25	(Fig. 3F)
PMID:40063661	FYPO:0004024	normal protein localization to cytoplasmic stress granule [assayed_protein] PomBase:SPAC12G12.07c	(Fig. 4A)
PMID:40063661	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to glucose starvation	(Fig. 4A)
PMID:40063661	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to heat	(Fig. 4A)
PMID:40063661	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to heat	(Fig. 4B)
PMID:40063661	GO:0010494	cytoplasmic stress granule [exists_during] cellular response to heat	(Fig. 4B)
PMID:40063661	FYPO:0007323	normal stress granule assembly during cellular response to heat	(Fig. 4D, 4E)
PMID:40063661	FYPO:0007323	normal stress granule assembly during cellular response to heat	(Fig. 4D, 4E)
PMID:40063661	FYPO:0007322	decreased stress granule assembly during cellular response to heat	(Fig. 4D, 4E)
PMID:40063661	FYPO:0007322	decreased stress granule assembly during cellular response to heat	(Fig. 4D, 4E)
PMID:40063661	FYPO:0007322	decreased stress granule assembly during cellular response to heat	(Fig. 4D, 4E)
PMID:40063661	FYPO:0007320	increased stress granule assembly during vegetative growth [has_severity] low [has_penetrance] 4	(Fig. 5A, 5B, 5E)
PMID:40063661	FYPO:0007320	increased stress granule assembly during vegetative growth [has_severity] high [has_penetrance] 15	(Fig. 5A, 5B, 5E)
PMID:40063661	FYPO:0007320	increased stress granule assembly during vegetative growth [has_severity] high [has_penetrance] 5	(Fig. 5A, 5B, 5E)
PMID:40063661	FYPO:0007320	increased stress granule assembly during vegetative growth [has_penetrance] 4	(Fig. 5B)
PMID:40063661	FYPO:0002350	normal stress granule assembly during vegetative growth	(Fig. 5B)
PMID:40063661	FYPO:0002350	normal stress granule assembly during vegetative growth	(Fig. 5B)
PMID:40063661	FYPO:0007320	increased stress granule assembly during vegetative growth [has_penetrance] 4	(Fig. 5B)
PMID:40063661	FYPO:0007322	decreased stress granule assembly during cellular response to heat	(Fig. 5D, 5E)
PMID:40063661	FYPO:0007322	decreased stress granule assembly during cellular response to heat	(Fig. 5D, 5E)
PMID:40063661	FYPO:0007322	decreased stress granule assembly during cellular response to heat	(Fig. 5D, 5E)
PMID:40063661	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPAC57A7.04c	(Fig. 6C)
PMID:40063661	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPAC12G12.07c	(Fig. 6D)
PMID:40063661	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] medium	(Fig. 7A, 7B)
PMID:40063661	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	(Fig. 7A, 7B)
PMID:40063661	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	(Fig. 7A, 7B)
PMID:40063661	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	(Fig. 7A, 7B)
PMID:40063661	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	(Fig. 7A, 7B)
PMID:40063661	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	(Fig. 7C)
PMID:40063661	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] medium	(Fig. 7C)
PMID:40063661	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	(Fig. 7C)
PMID:40063661	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] low	(Fig. 7C)
PMID:40063661	FYPO:0007227	increased number of R-loops at centromere [has_severity] medium	(Fig. 7D)
PMID:40063661	FYPO:0007227	increased number of R-loops at centromere [has_severity] high	(Fig. 7D)
PMID:40063661	FYPO:0007223	decreased establishment of chromatin silencing at centromere outer repeat region [has_severity] high [has_penetrance] 35	(Fig. 7E)
PMID:40063661	FYPO:0008415	abnormal centromeric outer repeat transcript localization to the cytoplasm	(Fig. 7F)
PMID:40063661	FYPO:0007226	normal chromatin silencing at heterochromatin island	(Fig. S2A)
PMID:40063661	FYPO:0004749	increased spatial extent of subtelomeric heterochromatin assembly	(Fig. S4)
PMID:40063661	FYPO:0008414	normal stress granule assembly during glucose starvation	(Fig. S7B, S7C)
PMID:40063661	FYPO:0008414	normal stress granule assembly during glucose starvation	(Fig. S7B, S7C)
PMID:40063661	FYPO:0008414	normal stress granule assembly during glucose starvation	(Fig. S7B, S7C)
PMID:40063661	FYPO:0001130	increased protein localization to nucleus during vegetative growth [assayed_protein] PomBase:SPAC57A7.04c	(Fig. S8A)
PMID:40063661	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	(Fig. S8B, S8C)
PMID:40063661	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	(Fig. S8B, S8C)
PMID:40063661	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] high	(Fig. S8D)
PMID:40063661	FYPO:0000220	increased centromeric outer repeat transcript level [has_severity] medium	(Fig. S8D)
PMID:40063661	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC12G12.08	(Table S1)
PMID:40063661	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC15F9.01c	(Table S1)
PMID:40063661	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPCC663.06c	(Table S1)
PMID:40063661	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1241	(Table S1)
PMID:40063661	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPRRNA.05	(Table S1)
PMID:40063661	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC3E7.02c	(Table S1)
PMID:40063661	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.774	(Table S1)
PMID:40063661	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.232	(Table S1)
PMID:40063661	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.362	(Table S1)
PMID:40063661	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1271	(Table S1)
PMID:40063661	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.230	(Table S1)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC750.07c	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBCPT2R1.06c	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC212.08c	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB21E7.07	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC23G7.10c	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB2B2.06c	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.388	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC8E4.12c	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB8B6.04c	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC460.04c	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.1487	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB10D8.03	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBPB21E7.01c	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBP4G3.02	(Table S2)
PMID:40063661	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC212.12	(Table S2)
PMID:40093821	FYPO:0001309	increased viability in stationary phase	(Fig. 1A-D)
PMID:40093821	FYPO:0007469	increased histone H3-K9 trimethylation during G0 [has_severity] high	(Fig. 1E)
PMID:40093821	FYPO:0000879	increased histone H3-K9 trimethylation during vegetative growth [has_severity] low	(Fig. 1F)
PMID:40124504	FYPO:0008406	abnormal protein localization to endoplasmic reticulum with cytoplasmic aggregation [assayed_protein] PomBase:SPAP4C9.02	(comment: CHECK XXXXXX CHANGE TO ABOLISHED XXXXXXX) As shown in Figure 1C, depletion of Oca3 leads to loss of Emc3, aggregation of Emc5, and normal ER localization, but reduced fluorescence levels of EMC6, revealing the requirement of Oca3 for the assembly of a functional EMC complex.
PMID:40124504	GO:0005789	endoplasmic reticulum membrane	As expected for an EMC component, in vivo fluorescence microscopy shows that Oca3-mCherry localizes to the ER (Figure 1A), co-localizing with the ER-reporter ADEL-GFP.
PMID:40124504	FYPO:0008409	resistance to ketoconazole	As expected for the observed ergosterol overaccumulation (Figures 4A and 4B), the growth of Oca3/Emc2-depleted cells is sensitive to nystatin and resistant to ketoconazole (Figure 4C).
PMID:40124504	FYPO:0008408	sensitive to nystatin	As expected for the observed ergosterol overaccumulation (Figures 4A and 4B), the growth of Oca3/Emc2-depleted cells is sensitive to nystatin and resistant to ketoconazole (Figure 4C).
PMID:40124504	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPCC1020.11c	As shown in Figure 1C, depletion of Oca3 leads to loss of Emc3, aggregation of Emc5, and normal ER localization, but reduced fluorescence levels of EMC6, revealing the requirement of Oca3 for the assembly of a functional EMC complex.
PMID:40124504	FYPO:0008405	abolished protein localization to endoplasmic reticulum [assayed_protein] PomBase:SPBC1711.03	As shown in Figure 1C, depletion of Oca3 leads to loss of Emc3, aggregation of Emc5, and normal ER localization, but reduced fluorescence levels of EMC6, revealing the requirement of Oca3 for the assembly of a functional EMC complex.
PMID:40124504	GO:0044233	mitochondria-associated endoplasmic reticulum membrane contact site	As shown in Figure 3, Mdm34-GFP co-localizes with mitochondrial membrane markers in wild-type cells, enriched at the ERMES ER-mitochondrial contact sites.
PMID:40124504	FYPO:0002321	decreased cellular ergosterol level	As shown in Figure 4A, loss of EMC results in a marked increase in the ergosterol content in the oca3D mutant strain at both temperatures when compared to levels in wild-type cells.
PMID:40124504	GO:0044233	mitochondria-associated endoplasmic reticulum membrane contact site	In agreement with its localization in ER-PM and ER-vesicles previously described in fission yeast,17 Ltc1-GFP localizes to cortical and internal dots in the ER in wild-type cells (arrows in Figure 3), but MitoHealth co-localization indicates that this protein is also associated to ER-Mitochondrial contact sites in S. pombe cells (Figures 3 and S2), as reported in S. cerevisiae cells.24
PMID:40124504	GO:0140268	endoplasmic reticulum-plasma membrane contact site	In agreement with its localization in ER-PM and ER-vesicles previously described in fission yeast,17 Ltc1-GFP localizes to cortical and internal dots in the ER in wild-type cells (arrows in Figure 3), but MitoHealth co-localization indicates that this protein is also associated to ER-Mitochondrial contact sites in S. pombe cells (Figures 3 and S2), as reported in S. cerevisiae cells.24
PMID:40124504	FYPO:0005838	symmetric mitochondrial aggregation	In comparison to wild-type cells, Oca3/Emc2 depletion results in a condensed mitochondrial structure that co-localize with abnormal mtDNA aggregations (Figure 2C).
PMID:40124504	FYPO:0008407	decreased protein localization to endoplasmic reticulum-mitochondrial contact site with increased localization to mitochondrial matrix [assayed_protein] PomBase:SPBC20F10.07	In contrast to Mdm34-GFP, Ltc1-GFP lacks its normal ER-PM and ER-mitochondria localization (see Figure 3). This result indicates that Ltc1 localization is fully dependent on EMC activity.
PMID:40124504	FYPO:0008410	increased endoplasmic reticulum unfolded protein response	In contrast, BiP1-driven expression of mCherry-ADEL is greatly induced in Oca3/Emc2-depleted cells. The UPR senses the protein folding capacity of the ER,45 suggesting that EMC dysfunction may provoke the accumulation of ER-unfolded proteins in S. pombe cells (ER stressed cells).
PMID:40124504	FYPO:0008407	decreased protein localization to endoplasmic reticulum-mitochondrial contact site with increased localization to mitochondrial matrix [assayed_protein] PomBase:SPAP4C9.02	In oca3D cells, most of the Mdm34-GFP is delocalized into the abnormal mitochondria, indicating that EMC disfunction may interfere the assembly of ERMES components.
PMID:40124504	GO:0005789	endoplasmic reticulum membrane	Like Oca3, localization of fluorescently tagged constructs of the putative orthologous S. pombe Emc3 (Pombase: ID SPBC1711.03), Emc5 (Pombase: ID SPAP4C9.02) and Emc6 (Pombase: ID SPCC1020.11c) is consistent with the ER structure in all these EMC subunits.
PMID:40124504	GO:0005789	endoplasmic reticulum membrane	Like Oca3, localization of fluorescently tagged constructs of the putative orthologous S. pombe Emc3 (Pombase: ID SPBC1711.03), Emc5 (Pombase: ID SPAP4C9.02) and Emc6 (Pombase: ID SPCC1020.11c) is consistent with the ER structure in all these EMC subunits.
PMID:40124504	GO:0005789	endoplasmic reticulum membrane	Like Oca3, localization of fluorescently tagged constructs of the putative orthologous S. pombe Emc3 (Pombase: ID SPBC1711.03), Emc5 (Pombase: ID SPAP4C9.02) and Emc6 (Pombase: ID SPCC1020.11c) is consistent with the ER structure in all these EMC subunits.
PMID:40124504	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	Likewise, the deletion of genes encoding the above predicted components of the S. pombe EMC (emc3D, emc5D and emc6D) renders a cold- sensitive phenotype too (Figure 1D).
PMID:40124504	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	Likewise, the deletion of genes encoding the above predicted components of the S. pombe EMC (emc3D, emc5D and emc6D) renders a cold- sensitive phenotype too (Figure 1D).
PMID:40124504	FYPO:0000080	decreased cell population growth at low temperature	Likewise, the deletion of genes encoding the above predicted components of the S. pombe EMC (emc3D, emc5D and emc6D) renders a cold- sensitive phenotype too (Figure 1D).
PMID:40124504	FYPO:0006378	normal protein localization to endoplasmic reticulum during vegetative growth [assayed_protein] PomBase:SPBC1539.04	Localization of the Tts1-mCherry construct, enriched in the tubular structure of the ER14 indicates that the ER, ER-associated plasma membrane (PM) and nuclear membrane remain unaltered in oca3-null cells (the oca3D deletion strain) (Figure 1B).
PMID:40124504	FYPO:0003769	decreased cellular mtDNA level	Quantitative PCR analysis of target mtDNA sequences determined a 28% reduction in mtDNA molecules per cell in the mutant strain at 30C, exacerexacerbated at low temperature (37% reduction at 20C) (Figure 2B).
PMID:40124504	GO:0032977	membrane insertase activity [has_input] PomBase:SPBC20F10.07	Since Ltc1 requires EMC for its localization and function at ER-Plasma membrane and ER-mitochondria contact sites (Figure 3), we conclude that EMC regulates ergosterol homeostasis through the ER-assisted biogenesis of the sterol transfer protein Ltc1.
PMID:40124504	GO:0032977	membrane insertase activity [has_input] PomBase:SPBC20F10.07	Since Ltc1 requires EMC for its localization and function at ER-Plasma membrane and ER-mitochondria contact sites (Figure 3), we conclude that EMC regulates ergosterol homeostasis through the ER-assisted biogenesis of the sterol transfer protein Ltc1. ........These observations lead us to conclude that EMC assists membrane protein folding and insertion by direct action on client proteins (i.e., Ltc1), but also may facilitate the biogenesis of some other membrane proteins by providing optimal membrane fluidity (i.e., ERMES components).
PMID:40124504	FYPO:0003004	increased cellular reactive oxygen species level during vegetative growth	The accumulation of reactive oxygen species (ROS) is associated to mitochondrial dysfunctions.18 Remarkably, proliferating Oca3-depleted cells (at 30C) reach ROS levels similar to those found in wild-type cells subjected to oxidative stress (H2O2 treatment), indicating that EMC-deficient cells suffer mitochondrial stress (Figures S1A and S1B).
PMID:40124504	FYPO:0000080	decreased cell population growth at low temperature [has_severity] high	The oca3D strain produces compromised cells that can grow at 30°C but fail to grow at lower temperatures (routinely assessed at 20°C) (Figure 1D), a cold-sensitive phenotype that may reflect the loss of membrane lipid homeostasis,16,17 energy homeostasis,18,19 or other adaptive mechanisms required for growth at these environmental conditions.
PMID:40124504	GO:0055092	sterol homeostasis	Thus, as previously reported in S. cerevisiae cells,24 this protein may also facilitate ergosterol transfer from the ER to the mitochondria. Since Ltc1 depletion leads to ergosterol overaccumulation in S. pombe cells,17 it is likely that sterol transport from the PM to the ER and from the ER to the mitochondria by this protein is required to drain ergosterol excess in these cells.
PMID:40124504	FYPO:0003766	aggregated mtDNA	however, clumps of mitochondrial DNA (mtDNA) were present in the cytoplasm of these mutant cells (Figure 2A).
PMID:40132111	FYPO:0004009	decreased rRNA transcription [assayed_transcript] cytosolic_28S_rRNA	(Fig. 1B)
PMID:40132111	FYPO:0004009	decreased rRNA transcription [has_severity] high [assayed_transcript] cytosolic_18S_rRNA	(Fig. 1B, Fig. 3D)
PMID:40132111	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC4C3.05c [has_severity] high	(Fig. 1C, Fig. 3E)
PMID:40132111	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPCC306.03c	(Fig. 1E)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [has_severity] high [assayed_protein] PomBase:SPAC1834.04	(Fig. 2A, Fig. 3F)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [has_severity] high [assayed_protein] PomBase:SPBC8D2.04	(Fig. 2A, Fig. 3F)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [has_severity] high [assayed_protein] PomBase:SPBC1105.11c	(Fig. 2A, Fig. 3F)
PMID:40132111	FYPO:0004824	normal rDNA copy number	(Fig. 2B)
PMID:40132111	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] PomBase:SPAC1834.04	(Fig. 2D)
PMID:40132111	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] PomBase:SPBC1105.11c	(Fig. 2D)
PMID:40132111	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] PomBase:SPBC8D2.04	(Fig. 2D)
PMID:40132111	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] PomBase:SPBC1105.11c	(Fig. 2D)
PMID:40132111	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] PomBase:SPAC1834.04	(Fig. 2D)
PMID:40132111	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] PomBase:SPBC8D2.04	(Fig. 2D)
PMID:40132111	FYPO:0006077	increased histone H3-K9 methylation at rDNA during vegetative growth [has_severity] high	(Fig. 3A, 3B)
PMID:40132111	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. 3C)
PMID:40132111	FYPO:0006079	increased chromatin silencing at rDNA	(Fig. 3C)
PMID:40132111	FYPO:0004009	decreased rRNA transcription [has_severity] low [assayed_transcript] cytosolic_18S_rRNA	(Fig. 3D)
PMID:40132111	FYPO:0004009	decreased rRNA transcription [has_severity] low [assayed_transcript] cytosolic_18S_rRNA	(Fig. 3D)
PMID:40132111	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC4C3.05c [has_severity] low	(Fig. 3E)
PMID:40132111	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC4C3.05c [has_severity] high	(Fig. 3E)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [has_severity] high [assayed_protein] PomBase:SPBC1105.11c	(Fig. 3F)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [has_severity] high [assayed_protein] PomBase:SPBC8D2.04	(Fig. 3F)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [has_severity] high [assayed_protein] PomBase:SPAC1834.04	(Fig. 3F)
PMID:40132111	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] rpb1/Phos(CTD-S2)	(Fig. 4A)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [assayed_protein] rpb1/Phos(CTD-S2) [has_severity] high	(Fig. 4A)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [assayed_protein] rpb1/Phos(CTD-S2) [has_severity] high	(Fig. 4A)
PMID:40132111	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] rpb1/Phos(CTD-S2)	(Fig. 4A)
PMID:40132111	FYPO:0005866	normal histone H3-K9 methylation at rDNA during vegetative growth	(Fig. 4B)
PMID:40132111	FYPO:0005866	normal histone H3-K9 methylation at rDNA during vegetative growth	(Fig. 4B)
PMID:40132111	FYPO:0005866	normal histone H3-K9 methylation at rDNA during vegetative growth	(Fig. 4B)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPAC18G6.02c	(Fig. 4C)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPAC6F12.09 [has_severity] low	(Fig. 4D)
PMID:40132111	FYPO:0005866	normal histone H3-K9 methylation at rDNA during vegetative growth	(Fig. 4E)
PMID:40132111	FYPO:0005866	normal histone H3-K9 methylation at rDNA during vegetative growth	(Fig. 4E)
PMID:40132111	FYPO:0006077	increased histone H3-K9 methylation at rDNA during vegetative growth [has_severity] low	(Fig. 4E)
PMID:40132111	FYPO:0006077	increased histone H3-K9 methylation at rDNA during vegetative growth [has_severity] low	(Fig. 4E)
PMID:40132111	FYPO:0006077	increased histone H3-K9 methylation at rDNA during vegetative growth [has_severity] low	(Fig. 4E)
PMID:40132111	FYPO:0006077	increased histone H3-K9 methylation at rDNA during vegetative growth [has_severity] low	(Fig. 4E)
PMID:40132111	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC1105.11c	(Fig. 4F)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [has_severity] high [assayed_protein] PomBase:SPBC1105.11c	(Fig. 4F)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [has_severity] high [assayed_protein] PomBase:SPBC8D2.04	(Fig. 4F)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [has_severity] high [assayed_protein] PomBase:SPAC1834.04	(Fig. 4F)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [has_severity] high [assayed_protein] PomBase:SPBC1105.11c	(Fig. 4F)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [has_severity] high [assayed_protein] PomBase:SPBC8D2.04	(Fig. 4F)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [has_severity] high [assayed_protein] PomBase:SPAC1834.04	(Fig. 4F)
PMID:40132111	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC8D2.04	(Fig. 4F)
PMID:40132111	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPAC1834.04	(Fig. 4F)
PMID:40132111	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] PomBase:SPBC1105.11c	(Fig. 4F)
PMID:40132111	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] PomBase:SPBC8D2.04	(Fig. 4F)
PMID:40132111	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] PomBase:SPAC1834.04	(Fig. 4F)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [assayed_protein] rpb1/Phos(CTD-S2) [has_severity] high	(Fig. 4G)
PMID:40132111	FYPO:0004032	increased protein localization to chromatin at rDNA [assayed_protein] rpb1/Phos(CTD-S2) [has_severity] high	(Fig. 4G)
PMID:40132111	PomGeneEx:0000020	protein level unchanged [during] cellular response to glucose starvation	(Fig. 5B)
PMID:40132111	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC1105.04c	(Fig. 5C)
PMID:40132111	FYPO:0007467	increased histone H3-K9 methylation during G0 [has_severity] high	(Fig. 5D)
PMID:40132111	FYPO:0003340	decreased re-entry into mitotic cell cycle during recovery from stationary phase [has_penetrance] 40	(Fig. 5F)
PMID:40132111	FYPO:0007634	increased histone H3-K14 acetylation at rDNA during vegetative growth [has_severity] high	(Fig. S2A)
PMID:40132111	FYPO:0007634	increased histone H3-K14 acetylation at rDNA during vegetative growth [has_severity] high	(Fig. S2A)
PMID:40132111	FYPO:0005866	normal histone H3-K9 methylation at rDNA during vegetative growth	(Fig. S2B)
PMID:40132111	FYPO:0005866	normal histone H3-K9 methylation at rDNA during vegetative growth	(Fig. S2B)
PMID:40132111	FYPO:0005866	normal histone H3-K9 methylation at rDNA during vegetative growth	(Fig. S2B)
PMID:40132111	FYPO:0005866	normal histone H3-K9 methylation at rDNA during vegetative growth	(Fig. S2B)
PMID:40132111	FYPO:0005866	normal histone H3-K9 methylation at rDNA during vegetative growth	(Fig. S2B)
PMID:40132111	FYPO:0005866	normal histone H3-K9 methylation at rDNA during vegetative growth	(Fig. S2B)
PMID:40132111	FYPO:0007655	increased nucleosome occupancy [assayed_region] rRNA_gene	MNase-qPCR (Fig. 2C)
PMID:40132111	GO:0061188	negative regulation of rDNA heterochromatin formation	Our findings demonstrated that loss of Abp1 leads to increased nucleosome occupancy and a decrease in RNAPI recruitment at rDNA repeats.
PMID:40185772	FYPO:0003700	increased snoRNA primary transcript level [assayed_transcript] PomBase:SPNCRNA.1715 [has_severity] high	(Fig. 1)
PMID:40185772	FYPO:0003700	increased snoRNA primary transcript level [assayed_transcript] PomBase:SPNCRNA.1715 [has_severity] high	(Fig. 1, Fig. 2D)
PMID:40185772	FYPO:0003040	decreased RNA splicing, via splicosome [assayed_transcript] PomBase:SPNCRNA.1715 [has_severity] high	(Fig. 1B and C)
PMID:40185772	FYPO:0003040	decreased RNA splicing, via splicosome [assayed_transcript] PomBase:SPNCRNA.1715 [has_severity] high	(Fig. 1B)
PMID:40185772	FYPO:0003700	increased snoRNA primary transcript level [has_severity] high [assayed_transcript] PomBase:SPSNORNA.21	(Fig. 1B)
PMID:40185772	FYPO:0003700	increased snoRNA primary transcript level [has_severity] high [assayed_transcript] PomBase:SPSNORNA.21	(Fig. 1B)
PMID:40185772	FYPO:0003700	increased snoRNA primary transcript level [has_severity] high [assayed_transcript] PomBase:SPSNORNA.21	(Fig. 1B)
PMID:40185772	FYPO:0003040	decreased RNA splicing, via splicosome [assayed_transcript] PomBase:SPNCRNA.1715 [has_severity] high	(Fig. 1B)
PMID:40185772	FYPO:0003040	decreased RNA splicing, via splicosome [assayed_transcript] PomBase:SPNCRNA.1715 [has_severity] medium	(Fig. 1B)
PMID:40185772	FYPO:0003040	decreased RNA splicing, via splicosome [assayed_transcript] PomBase:SPNCRNA.1715 [has_severity] high	(Fig. 1B, 1C)
PMID:40185772	GO:0031428	box C/D methylation guide snoRNP complex	(Fig. 2C)
PMID:40185772	FYPO:0003058	normal RNA localization [assayed_transcript] PomBase:SPSNORNA.55	(Fig. 2D)
PMID:40185772	FYPO:0002933	increased mature snoRNA level [assayed_transcript] PomBase:SPSNORNA.55	(Fig. 2D)
PMID:40185772	GO:0030562	rRNA 2'-O-ribose methylation guide activity [modified_residue] G2483 [has_input] PomBase:SPRRNA.48	(Fig. 3)
PMID:40185772	FYPO:0003720	snoRNA guided rRNA 2'-O-methylation abolished at specific site [assayed_transcript] PomBase:SPRRNA.48	(Fig. 3A and C)
PMID:40185772	FYPO:0003720	snoRNA guided rRNA 2'-O-methylation abolished at specific site [assayed_transcript] PomBase:SPRRNA.48	(Fig. 3A, 3C)
PMID:40185772	FYPO:0003720	snoRNA guided rRNA 2'-O-methylation abolished at specific site [assayed_transcript] PomBase:SPRRNA.48	(Fig. 3A, 3C)
PMID:40185772	FYPO:0008436	snoRNA guided rRNA 2'-O-methylation level decreased at specific site [assayed_transcript] PomBase:SPRRNA.48 [has_severity] medium	(Fig. 3C)
PMID:40185772	FYPO:0003720	snoRNA guided rRNA 2'-O-methylation abolished at specific site [assayed_transcript] PomBase:SPRRNA.48	(Fig. 3C)
PMID:40185772	FYPO:0008436	snoRNA guided rRNA 2'-O-methylation level decreased at specific site [assayed_transcript] PomBase:SPRRNA.48 [has_severity] low	(Fig. 3C)
PMID:40185772	FYPO:0008435	abnormal cytosolic ribosomal large subunit assembly [has_severity] high	(Fig. 3D)
PMID:40185772	FYPO:0008435	abnormal cytosolic ribosomal large subunit assembly [has_severity] medium	(Fig. 3D)
PMID:40185772	FYPO:0008435	abnormal cytosolic ribosomal large subunit assembly [has_severity] medium	(Fig. 3D)
PMID:40185772	FYPO:0008435	abnormal cytosolic ribosomal large subunit assembly [has_severity] medium	(Fig. 3D)
PMID:40185772	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c [has_severity] low	(Fig. 4B)
PMID:40185772	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c	(Fig. 4B)
PMID:40185772	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c [has_severity] high	(Fig. 4B)
PMID:40185772	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c [has_severity] medium	(Fig. 4B, D and E)
PMID:40185772	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c	(Fig. 4D)
PMID:40185772	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c [has_severity] medium	(Fig. 4D)
PMID:40185772	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c	(Fig. 4D)
PMID:40185772	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c [has_severity] medium	(Fig. 4D)
PMID:40185772	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c [has_severity] low	(Fig. 4D)
PMID:40185772	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c	(Fig. 4E)
PMID:40185772	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c [has_severity] medium	(Fig. 4E)
PMID:40185772	FYPO:0001327	increased protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c [has_severity] medium	(Fig. 4E)
PMID:40185772	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c	(Fig. 4E)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC27D7.13c	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02 [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02 [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPBC32H8.11	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPAC27D7.13c	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPBC216.02	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [has_severity] high [assayed_transcript] PomBase:SPNCRNA.103	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPNCRNA.103	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPNCRNA.103 [has_severity] medium	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPNCRNA.103 [has_severity] medium	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPNCRNA.103	(Fig. 4F)
PMID:40185772	FYPO:0008146	increased ncRNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.103 [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0008146	increased ncRNA level during vegetative growth [assayed_transcript] PomBase:SPNCRNA.103 [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC27D7.13c	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC27D7.13c	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC32H8.11	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC32H8.11	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC27D7.13c [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC27D7.13c [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPNCRNA.103	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC27D7.13c	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC32H8.11	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC32H8.11 [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC32H8.11 [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPNCRNA.103 [has_severity] medium	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPNCRNA.103 [has_severity] medium	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02 [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02 [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC32H8.11 [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC32H8.11 [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC27D7.13c [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC32H8.11 [has_severity] medium	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC27D7.13c [has_severity] medium	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC216.02 [has_severity] medium	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC27D7.13c [has_severity] low	(Fig. 4F)
PMID:40185772	FYPO:0002960	increased level of DSR-containing meiotic gene mRNA during vegetative growth [has_severity] high [assayed_transcript] PomBase:SPNCRNA.103	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC32H8.11	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPBC32H8.11	(Fig. 4F)
PMID:40185772	FYPO:0003747	normal level of DSR-containing meiotic gene mRNA during vegetative growth [assayed_transcript] PomBase:SPAC27D7.13c	(Fig. 4F)
PMID:40185772	FYPO:0006976	normal RNA level during meiotic cell cycle [assayed_transcript] PomBase:SPAC27D7.13c	(Fig. 5C)
PMID:40185772	FYPO:0005120	increased RNA level during meiotic cell cycle [assayed_transcript] PomBase:SPBC216.02	(Fig. 5C)
PMID:40185772	FYPO:0005120	increased RNA level during meiotic cell cycle [assayed_transcript] PomBase:SPAC27D7.13c	(Fig. 5C)
PMID:40185772	FYPO:0006976	normal RNA level during meiotic cell cycle [assayed_transcript] PomBase:SPBC216.02	(Fig. 5C)
PMID:40185772	FYPO:0005120	increased RNA level during meiotic cell cycle [assayed_transcript] PomBase:SPBC216.02	(Fig. 5D)
PMID:40185772	FYPO:0006976	normal RNA level during meiotic cell cycle [assayed_transcript] PomBase:SPBC216.02	(Fig. 5D)
PMID:40185772	FYPO:0005120	increased RNA level during meiotic cell cycle [assayed_transcript] PomBase:SPAC27D7.13c	(Fig. 5D)
PMID:40185772	FYPO:0005120	increased RNA level during meiotic cell cycle [assayed_transcript] PomBase:SPAC27D7.13c	(Fig. 5D)
PMID:40185772	FYPO:0003579	normal RNA level during meiosis [assayed_transcript] PomBase:SPAC27D7.13c	(Fig. 5E)
PMID:40185772	FYPO:0003579	normal RNA level during meiosis [assayed_transcript] PomBase:SPBC216.02	(Fig. 5E)
PMID:40185772	FYPO:0005120	increased RNA level during meiotic cell cycle [assayed_transcript] PomBase:SPAC27D7.13c	(Fig. 5E)
PMID:40185772	FYPO:0005120	increased RNA level during meiotic cell cycle [assayed_transcript] PomBase:SPAC27D7.13c	(Fig. 5E, 5F)
PMID:40185772	FYPO:0005120	increased RNA level during meiotic cell cycle [assayed_transcript] PomBase:SPBC216.02	(Fig. 5E, 5F)
PMID:40185772	FYPO:0005120	increased RNA level during meiotic cell cycle [assayed_transcript] PomBase:SPBC216.02	(Fig. 5F)
PMID:40185772	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPCC736.12c [assayed_transcript] PomBase:SPSNORNA.55	(Fig. 6C)
PMID:40185772	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPAC27D7.03c [assayed_transcript] PomBase:SPSNORNA.55	(Fig. 6D)
PMID:40185772	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPCC736.12c [assayed_transcript] PomBase:SPSNORNA.55	(Fig. 6E)
PMID:40185772	FYPO:0002357	normal protein-RNA interaction [assayed_protein] PomBase:SPCC736.12c [assayed_transcript] PomBase:SPSNORNA.55	(Fig. 6E)
PMID:40185772	FYPO:0002133	abolished protein-RNA interaction [assayed_protein] PomBase:SPAC27D7.03c [assayed_transcript] PomBase:SPSNORNA.55	(Fig. 6F)
PMID:40185772	FYPO:0002357	normal protein-RNA interaction [assayed_transcript] PomBase:SPSNORNA.55 [assayed_protein] PomBase:SPAC27D7.03c	(Fig. 6F)
PMID:40185772	FYPO:0002133	abolished protein-RNA interaction [assayed_transcript] PomBase:SPSNORNA.55 [assayed_protein] PomBase:SPBC2D10.10c	(Fig. 6G)
PMID:40185772	FYPO:0002357	normal protein-RNA interaction [assayed_transcript] PomBase:SPSNORNA.55 [assayed_protein] PomBase:SPBC2D10.10c	(Fig. 6G)
PMID:40185772	FYPO:0002357	normal protein-RNA interaction [assayed_protein] PomBase:SPAC23G3.06 [assayed_transcript] PomBase:SPSNORNA.55	(Fig. 6H)
PMID:40185772	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPAC23G3.06 [assayed_transcript] PomBase:SPSNORNA.55	(Fig. 6H)
PMID:40185772	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPSNORNA.55	(Fig. S1A)
PMID:40185772	FYPO:0001979	increased lariat intron level [assayed_transcript] PomBase:SPSNORNA.55 [has_severity] high	(Fig. S1A)
PMID:40185772	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPSNORNA.55	(Fig. S1A)
PMID:40185772	FYPO:0003700	increased snoRNA primary transcript level [assayed_transcript] PomBase:SPSNORNA.21	(Fig. S2D)
PMID:40185772	FYPO:0003700	increased snoRNA primary transcript level [assayed_transcript] PomBase:SPSNORNA.55	(Fig. S2D)
PMID:40185772	FYPO:0003700	increased snoRNA primary transcript level [assayed_transcript] PomBase:SPSNORNA.55 [has_severity] low	(Fig. S2E)
PMID:40185772	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPSNORNA.55 [has_severity] low	(Fig. S2E)
PMID:40185772	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPSNORNA.55 [has_severity] low	(Fig. S2E)
PMID:40185772	FYPO:0001135	increased 35S rRNA precursor level	(Fig. S3C)
PMID:40185772	FYPO:0001135	increased 35S rRNA precursor level	(Fig. S3C)
PMID:40185772	FYPO:0001135	increased 35S rRNA precursor level	(Fig. S3C)
PMID:40185772	FYPO:0001135	increased 35S rRNA precursor level	(Fig. S3C)
PMID:40185772	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPSNORNA.55	(Fig. S3E)
PMID:40185772	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPSNORNA.55	(Fig. S3E)
PMID:40185772	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPSNORNA.55	(Fig. S3E)
PMID:40185772	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPSNORNA.55	(Fig. S3E)
PMID:40185772	FYPO:0003058	normal RNA localization [assayed_transcript] PomBase:SPSNORNA.55	(Fig. S3F)
PMID:40185772	FYPO:0003058	normal RNA localization [assayed_transcript] PomBase:SPSNORNA.55	(Fig. S3F)
PMID:40185772	FYPO:0003058	normal RNA localization [assayed_transcript] PomBase:SPSNORNA.55	(Fig. S3F)
PMID:40185772	FYPO:0001357	normal vegetative cell population growth	(Fig. S3G)
PMID:40185772	FYPO:0001357	normal vegetative cell population growth	(Fig. S3G)
PMID:40185772	FYPO:0001357	normal vegetative cell population growth	(Fig. S3G)
PMID:40185772	FYPO:0001357	normal vegetative cell population growth	(Fig. S3G)
PMID:40185772	FYPO:0001357	normal vegetative cell population growth	(Fig. S3G)
PMID:40185772	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPSNORNA.55 [has_severity] medium	(Fig. S4B)
PMID:40185772	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPSNORNA.55 [has_severity] high	(Fig. S4B)
PMID:40185772	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPSNORNA.55 [has_severity] low	(Fig. S4B)
PMID:40185772	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPSNORNA.55 [has_severity] medium	(Fig. S4B)
PMID:40185772	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPSNORNA.55 [has_severity] high	(Fig. S4B)
PMID:40185772	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c	(Fig. S4C)
PMID:40185772	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. S4D)
PMID:40185772	FYPO:0008435	abnormal cytosolic ribosomal large subunit assembly [has_severity] high	(Fig. S4E)
PMID:40185772	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC27D7.03c	(Fig. S4F)
PMID:40185772	FYPO:0000590	normal sporulation	(Fig. S5F)
PMID:40185772	FYPO:0000590	normal sporulation	(Fig. S5F)
PMID:40185772	FYPO:0002357	normal protein-RNA interaction [assayed_protein] PomBase:SPBC2D10.10c [assayed_transcript] PomBase:SPSNORNA.55	(Fig. S6A)
PMID:40185772	FYPO:0002357	normal protein-RNA interaction [assayed_protein] PomBase:SPBC2D10.10c [assayed_transcript] PomBase:SPSNORNA.21	(Fig. S6B)
PMID:40185772	FYPO:0002357	normal protein-RNA interaction [assayed_protein] PomBase:SPBC2D10.10c [assayed_transcript] PomBase:SPSNORNA.21	(Fig. S6B)
PMID:40185772	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC2D10.10c [assayed_protein] PomBase:SPCC736.12c	(Fig. S6C)
PMID:40185772	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC2D10.10c [assayed_protein] PomBase:SPCC736.12c	(Fig. S6C)
PMID:40185772	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC2D10.10c [assayed_protein] PomBase:SPAC27D7.03c	(Fig. S6D)
PMID:40185772	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPBC2D10.10c [assayed_protein] PomBase:SPAC27D7.03c	(Fig. S6D)
PMID:40185772	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPCC736.12c [assayed_transcript] PomBase:SPSNORNA.21	(Fig. S6E)
PMID:40185772	FYPO:0002134	decreased protein-RNA interaction [assayed_protein] PomBase:SPAC27D7.03c [assayed_transcript] PomBase:SPSNORNA.21	(Fig. S6F)
PMID:40185772	GO:0000451	rRNA 2'-O-methylation	(comment: vw: added because this seems to be multi step and the process is in the title)
PMID:40185772	FYPO:0008437	RNA mislocalized to nucleolus during vegetative growth [has_penetrance] high [has_severity] high [assayed_transcript] PomBase:SPNCRNA.1715	5’&3’SSmut cells also exhibited a strong increase in signal intensity and a redistribution of the lncRNA to the nucleolus, as determined by fluorescence overlap with the nucleolar marker Nop56 (Fig. 1d, e)
PMID:40185772	GO:0000027	ribosomal large subunit assembly	From these experiments, we concluded that snR107 mediates 25S rRNA G2483 2’-O-Me and contributes to pre-rRNA processing and 60S subunit biogenesis in a Gm2483-independent fashion.
PMID:40185772	GO:0005730	nucleolus	We further carried out smFISH analyses and found that snR107, as opposed to mamRNA 5’ exon, accumulated specifically in the nucleolus in wild type cells (Fig. 2d, e).
PMID:40193710	FYPO:0000964	normal growth on thiabendazole	(Fig. 2A)
PMID:40193710	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 2A)
PMID:40193710	FYPO:0001861	increased minichromosome loss upon segregation during vegetative growth [has_severity] high	(Fig. 2B)
PMID:40193710	FYPO:0000228	lagging mitotic chromosomes	(Fig. 2C and D)
PMID:40193710	FYPO:0001355	decreased vegetative cell population growth	(Fig. 2E)
PMID:40193710	FYPO:0001355	decreased vegetative cell population growth	(Fig. 2E)
PMID:40193710	FYPO:0004827	inviable vegetative cell with cell death during mitosis [has_penetrance] 48	(Fig. 2E)
PMID:40193710	FYPO:0004827	inviable vegetative cell with cell death during mitosis [has_penetrance] 21	(Fig. 2E)
PMID:40193710	FYPO:0004827	inviable vegetative cell with cell death during mitosis [has_penetrance] 71	(Fig. 2E)
PMID:40193710	FYPO:0004827	inviable vegetative cell with cell death during mitosis [has_penetrance] 71	(Fig. 2E)
PMID:40193710	FYPO:0004827	inviable vegetative cell with cell death during mitosis [has_penetrance] 12	(Fig. 2E)
PMID:40193710	FYPO:0001355	decreased vegetative cell population growth	(Fig. 2E)
PMID:40193710	FYPO:0004827	inviable vegetative cell with cell death during mitosis [has_penetrance] 48	(Fig. 2E)
PMID:40193710	FYPO:0001355	decreased vegetative cell population growth	(Fig. 2E)
PMID:40193710	FYPO:0005555	decreased mitotic cohesin loading [has_severity] high [assayed_protein] PomBase:SPCC338.17c	(Fig. 3A and B)
PMID:40193710	FYPO:0005555	decreased mitotic cohesin loading [assayed_protein] PomBase:SPCC338.17c [has_penetrance] 54	(Fig. 3C)
PMID:40193710	FYPO:0000415	decreased mitotic sister chromatid segregation [has_penetrance] 38	(Fig. 3D)
PMID:40193710	FYPO:0004742	normal chromatin silencing at centromere outer repeat	(Fig. 3E)
PMID:40193710	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC9G1.08c	(Fig. 4H and I)
PMID:40193710	FYPO:0001645	decreased protein-protein interaction [has_severity] medium [assayed_protein] PomBase:SPCC338.17c [assayed_protein] PomBase:SPAC1250.01	(Fig. 5A)
PMID:40193710	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC9G1.08c [assayed_protein] PomBase:SPCC338.17c	(Fig. 5C)
PMID:40193710	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC31A2.05c	(Fig. 5D and F)
PMID:40193710	FYPO:0004380	increased protein localization to pericentric heterochromatin during vegetative growth [assayed_protein] PomBase:SPAC1687.18c	(Fig. 5E and F)
PMID:40193710	FYPO:0006599	decreased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPCC338.17c	(Fig. 5F)
PMID:40193710	FYPO:0008154	normal protein localization to centromeric heterochromatin [assayed_protein] PomBase:SPAC664.01c	(Fig. 5F)
PMID:40193710	FYPO:0008154	normal protein localization to centromeric heterochromatin [assayed_protein] PomBase:SPAC1250.01	(Fig. 5F)
PMID:40193710	GO:0030674	protein-macromolecule adaptor activity [part_of] establishment of mitotic sister chromatid cohesion	our study suggested that Phi1 was a part of the cohesin loading machinery (Fig. 5)
PMID:40193710	GO:0034087	establishment of mitotic sister chromatid cohesion	our study suggested that Phi1 was a part of the cohesin loading machinery (Fig. 5)
PMID:40385371	FYPO:0003440	cell lysis during cytokinesis	A percentage of lysed cells were also detected for mob1-N1 and mob1-R4 (Figure 1C-D).
PMID:40385371	FYPO:0003440	cell lysis during cytokinesis	A percentage of lysed cells were also detected for mob1-N1 and mob1-R4 (Figure 1C-D).
PMID:40385371	FYPO:0002049	elongated multinucleate aseptate vegetative cell	At 36°C, mob1-1 cells were multinucleated with no septum present (Figure 1C), as has been previously reported (Hou et al., 2000).
PMID:40385371	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	mob1-1 grew less well than wildtype at 32°C and 36°C and mob1-N1 grew less well than wildtype at 36°C (Figure 1B).
PMID:40385371	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	mob1-N1 grew less well than wildtype at 36°C (Figure 1B).
PMID:40385371	FYPO:0000080	decreased cell population growth at low temperature [has_severity] low	mob1-R4 grew slightly less well than wildtype at both high (32°C and 36°C) and low (25°C) temperatures (Figure 1B).
PMID:40385371	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	mob1-R4 grew slightly less well than wildtype at both high (32°C and 36°C) and low (25°C) temperatures (Figure 1B).
PMID:40395999	FYPO:0008429	normal protein level during cellular response to sulfur starvation [assayed_protein] PomBase:SPBC11B10.09	Cdc13 is degraded during sulfur depletion, but the levels of its binding partner Cdc2 did not change (Fig. 1F and 1G), suggesting autophagy selectively degrades Cdc13 but not Cdc2 in this condition.
PMID:40395999	FYPO:0008427	increased protein level during cellular response to sulfur starvation [assayed_protein] PomBase:SPBC582.03	Cdc13 levels declined in wild-type cells in response to sulfur depletion, but not in ecls∆ cells (Fig. 1F), suggesting that the abnormal morphology of ecls∆ cells during sulfur depletion is attributable to the failure of normal cyclin degradation.
PMID:40395999	FYPO:0008428	increased protein phosphorylation during sulfur starvation [assayed_protein] PomBase:SPCC4G3.08	Sulfur deficiency decreased the phosphorylation of the TORC1- phosphorylation site of Psk1. Conversely, in the absence of Ecl1-family genes, remarkable phosphorylation was observed with or without sulfur.
PMID:40395999	FYPO:0007086	elongated vegetative cell during sulfur starvation	Sulfur depletion results in Ecl1-family gene-dependent reduction of the cell size of S. pombe [12] (Fig. 1A and 1B). ecl1∆ ecl2∆ ecl3∆ (ecls∆) cells do not exhibit reduced cell size and develop abnormal deposits stained with aniline blue that stains the septum [28,29] (Fig. 1C).
PMID:40395999	GO:0004860	protein kinase inhibitor activity [part_of] negative regulation of TORC1 signaling	TORC1 activity of the ecls∆ cells was much higher than that of control cells even in the logarithmic growth phase (0 hour), suggesting that Ecl1-family proteins also partially inhibit TORC1 activity in this minimum medium condition.
PMID:40395999	GO:0004860	protein kinase inhibitor activity [part_of] negative regulation of TORC1 signaling	TORC1 activity of the ecls∆ cells was much higher than that of control cells even in the logarithmic growth phase (0 hour), suggesting that Ecl1-family proteins also partially inhibit TORC1 activity in this minimum medium condition.
PMID:40395999	GO:0004860	protein kinase inhibitor activity [part_of] negative regulation of TORC1 signaling	TORC1 activity of the ecls∆ cells was much higher than that of control cells even in the logarithmic growth phase (0 hour), suggesting that Ecl1-family proteins also partially inhibit TORC1 activity in this minimum medium condition.
PMID:40395999	FYPO:0008427	increased protein level during cellular response to sulfur starvation [assayed_protein] PomBase:SPBC582.03	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	FYPO:0008427	increased protein level during cellular response to sulfur starvation [assayed_protein] PomBase:SPBC582.03	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	FYPO:0008427	increased protein level during cellular response to sulfur starvation [assayed_protein] PomBase:SPBC582.03	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	FYPO:0008427	increased protein level during cellular response to sulfur starvation [assayed_protein] PomBase:SPBC582.03	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	FYPO:0008427	increased protein level during cellular response to sulfur starvation [assayed_protein] PomBase:SPBC582.03	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	FYPO:0008427	increased protein level during cellular response to sulfur starvation [assayed_protein] PomBase:SPBC582.03	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	FYPO:0008427	increased protein level during cellular response to sulfur starvation [assayed_protein] PomBase:SPBC582.03	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	FYPO:0008427	increased protein level during cellular response to sulfur starvation [assayed_protein] PomBase:SPBC582.03	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	FYPO:0008427	increased protein level during cellular response to sulfur starvation [assayed_protein] PomBase:SPBC582.03	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	FYPO:0008427	increased protein level during cellular response to sulfur starvation [assayed_protein] PomBase:SPBC582.03	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40395999	FYPO:0008427	increased protein level during cellular response to sulfur starvation [assayed_protein] PomBase:SPBC582.03	We investigated the levels of Cdc13 in these mutants under sulfur depletion, as with ecls∆ cells, 11 single- gene deletion mutants that did not display proper degradation were identi- fied (Fig. 1G). Interestingly, nine of these genes were Atg genes, suggesting that autophagy is required for Cdc13 degradation.
PMID:40402811	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 1A)
PMID:40402811	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:40402811	FYPO:0000095	sensitive to bleomycin [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0002344	sensitive to phleomycin [has_severity] medium	(Fig. 1A)
PMID:40402811	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 1A)
PMID:40402811	FYPO:0000084	sensitive to 6-azauracil [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1A)
PMID:40402811	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1A)
PMID:40402811	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0003906	normal growth on bleomycin	(Fig. 1A)
PMID:40402811	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0005517	normal growth on 6-azauracil	(Fig. 1A)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:40402811	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:40402811	FYPO:0005517	normal growth on 6-azauracil	(Fig. 1A)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:40402811	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:40402811	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1A)
PMID:40402811	FYPO:0001690	normal growth on camptothecin	(Fig. 1A)
PMID:40402811	FYPO:0003906	normal growth on bleomycin	(Fig. 1A)
PMID:40402811	FYPO:0003183	normal growth on phleomycin	(Fig. 1A)
PMID:40402811	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0005517	normal growth on 6-azauracil	(Fig. 1A)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:40402811	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0003906	normal growth on bleomycin	(Fig. 1A)
PMID:40402811	FYPO:0000084	sensitive to 6-azauracil [has_severity] medium	(Fig. 1A)
PMID:40402811	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1A)
PMID:40402811	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:40402811	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0000085	sensitive to camptothecin [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0000095	sensitive to bleomycin [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0002344	sensitive to phleomycin [has_severity] medium	(Fig. 1A)
PMID:40402811	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 1A)
PMID:40402811	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:40402811	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1A)
PMID:40402811	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:40402811	FYPO:0000095	sensitive to bleomycin [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0002344	sensitive to phleomycin [has_severity] medium	(Fig. 1A)
PMID:40402811	FYPO:0002578	resistance to hydroxyurea	(Fig. 1A)
PMID:40402811	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1A)
PMID:40402811	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 1A)
PMID:40402811	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1A)
PMID:40402811	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 1A)
PMID:40402811	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 1A)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:40402811	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1A)
PMID:40402811	FYPO:0002578	resistance to hydroxyurea	(Fig. 1A)
PMID:40402811	FYPO:0005517	normal growth on 6-azauracil	(Fig. 1A)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1A)
PMID:40402811	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1B)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:40402811	FYPO:0005517	normal growth on 6-azauracil	(Fig. 1B)
PMID:40402811	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 1B)
PMID:40402811	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1B)
PMID:40402811	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1B)
PMID:40402811	FYPO:0003183	normal growth on phleomycin	(Fig. 1B)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:40402811	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1B)
PMID:40402811	FYPO:0000084	sensitive to 6-azauracil [has_severity] low	(Fig. 1B)
PMID:40402811	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 1B)
PMID:40402811	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1B)
PMID:40402811	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1B)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:40402811	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(Fig. 1B)
PMID:40402811	FYPO:0005517	normal growth on 6-azauracil	(Fig. 1B)
PMID:40402811	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1B)
PMID:40402811	FYPO:0001690	normal growth on camptothecin	(Fig. 1B)
PMID:40402811	FYPO:0003906	normal growth on bleomycin	(Fig. 1B)
PMID:40402811	FYPO:0004752	resistance to phleomycin	(Fig. 1B)
PMID:40402811	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1B)
PMID:40402811	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1B)
PMID:40402811	FYPO:0005517	normal growth on 6-azauracil	(Fig. 1B)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1B)
PMID:40402811	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1B)
PMID:40402811	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1B)
PMID:40402811	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 1B)
PMID:40402811	FYPO:0001690	normal growth on camptothecin [has_severity] low	(Fig. 1B)
PMID:40402811	FYPO:0003906	normal growth on bleomycin	(Fig. 1B)
PMID:40402811	FYPO:0003183	normal growth on phleomycin	(Fig. 1B)
PMID:40402811	FYPO:0003906	normal growth on bleomycin	(Fig. 1B)
PMID:40402811	FYPO:0001690	normal growth on camptothecin	(Fig. 1B)
PMID:40402811	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1B)
PMID:40402811	FYPO:0000095	sensitive to bleomycin [has_severity] low	(Fig. 1B)
PMID:40402811	FYPO:0001690	normal growth on camptothecin	(Fig. 1B)
PMID:40402811	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(Fig. 1B)
PMID:40402811	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 1B)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1C)
PMID:40402811	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1C)
PMID:40402811	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1C)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1C)
PMID:40402811	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1C)
PMID:40402811	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1C)
PMID:40402811	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1C)
PMID:40402811	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 1C)
PMID:40402811	FYPO:0003906	normal growth on bleomycin	(Fig. 1C)
PMID:40402811	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 1C)
PMID:40402811	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1C)
PMID:40402811	FYPO:0005517	normal growth on 6-azauracil	(Fig. 1C)
PMID:40402811	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. 1C)
PMID:40402811	FYPO:0000082	decreased cell population growth at high temperature [has_severity] high	(Fig. 1C)
PMID:40402811	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1C)
PMID:40402811	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 1C)
PMID:40402811	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 1C)
PMID:40402811	FYPO:0003906	normal growth on bleomycin	(Fig. 1C)
PMID:40402811	FYPO:0002344	sensitive to phleomycin [has_severity] medium	(Fig. 1C)
PMID:40402811	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 1C)
PMID:40402811	FYPO:0000084	sensitive to 6-azauracil [has_severity] medium	(Fig. 1C)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1C)
PMID:40402811	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1C)
PMID:40402811	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 1C)
PMID:40402811	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 1C)
PMID:40402811	FYPO:0001690	normal growth on camptothecin	(Fig. 1C)
PMID:40402811	FYPO:0003906	normal growth on bleomycin	(Fig. 1C)
PMID:40402811	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 1C)
PMID:40402811	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1C)
PMID:40402811	FYPO:0005517	normal growth on 6-azauracil	(Fig. 1C)
PMID:40402811	FYPO:0003906	normal growth on bleomycin	(Fig. 1C)
PMID:40402811	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 1C)
PMID:40402811	FYPO:0000969	normal growth during cellular response to UV	(Fig. 1C)
PMID:40402811	FYPO:0005517	normal growth on 6-azauracil	(Fig. 1C)
PMID:40402811	FYPO:0001032	resistance to camptothecin [has_severity] medium	(Fig. 1C)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 1C)
PMID:40402811	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1C)
PMID:40402811	FYPO:0000963	normal growth on hydroxyurea	(Fig. 1C)
PMID:40402811	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 1C)
PMID:40402811	FYPO:0000085	sensitive to camptothecin [has_severity] medium	(Fig. 1C)
PMID:40402811	FYPO:0003906	normal growth on bleomycin	(Fig. 1C)
PMID:40402811	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 1C)
PMID:40402811	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(Fig. 1C)
PMID:40402811	FYPO:0005517	normal growth on 6-azauracil	(Fig. 1C)
PMID:40402811	FYPO:0000674	normal cell population growth at high temperature	(Fig. 1C)
PMID:40402811	FYPO:0002922	abolished histone H2B-K119 ubiquitination during vegetative growth	(Fig. 2)
PMID:40402811	FYPO:0007386	decreased histone H2B-K119 ubiquitination during vegetative growth [has_severity] medium	(Fig. 2A)
PMID:40402811	FYPO:0007386	decreased histone H2B-K119 ubiquitination during vegetative growth [has_severity] low	(Fig. 2A)
PMID:40402811	FYPO:0007386	decreased histone H2B-K119 ubiquitination during vegetative growth [has_severity] high	(Fig. 2A)
PMID:40402811	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 2A)
PMID:40402811	FYPO:0007386	decreased histone H2B-K119 ubiquitination during vegetative growth [has_severity] low	(Fig. 2A)
PMID:40402811	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 2A)
PMID:40402811	FYPO:0008439	increased histone H2B-K119 ubiquitination during vegetative growth [has_severity] low	(Fig. 2B)
PMID:40402811	FYPO:0008439	increased histone H2B-K119 ubiquitination during vegetative growth [has_severity] medium	(Fig. 2B)
PMID:40402811	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 2B)
PMID:40402811	FYPO:0007386	decreased histone H2B-K119 ubiquitination during vegetative growth [has_severity] medium	(Fig. 2B)
PMID:40402811	FYPO:0008439	increased histone H2B-K119 ubiquitination during vegetative growth [has_severity] low	(Fig. 2B)
PMID:40402811	FYPO:0002923	normal histone H2B-K119 ubiquitination during vegetative growth	(Fig. 2C)
PMID:40402811	FYPO:0007386	decreased histone H2B-K119 ubiquitination during vegetative growth [has_severity] medium	(Fig. 2C)
PMID:40402811	FYPO:0008439	increased histone H2B-K119 ubiquitination during vegetative growth [has_severity] medium	(Fig. 2C)
PMID:40402811	FYPO:0008439	increased histone H2B-K119 ubiquitination during vegetative growth [has_severity] medium	(Fig. 2C)
PMID:40402811	FYPO:0008439	increased histone H2B-K119 ubiquitination during vegetative growth [has_severity] medium	(Fig. 2C)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPAC110.01	(Fig. 4A)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] medium	(Fig. 4A)
PMID:40402811	FYPO:0000825	increased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPAC821.09	(Fig. 4A)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09 [has_severity] low	(Fig. 4A)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] low [assayed_transcript] PomBase:SPBC887.17	(Fig. 4A)
PMID:40402811	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] high	(Fig. 4A)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 4A)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC887.17	(Fig. 4A)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC887.17	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] high [assayed_transcript] PomBase:SPAC110.01	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] high	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] high [assayed_transcript] PomBase:SPAC821.09	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC887.17 [has_severity] low	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] high	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] high	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC887.17 [has_severity] medium	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01 [has_severity] medium	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] high [assayed_transcript] PomBase:SPBC887.17	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC887.17 [has_severity] low	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPBC887.17	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [has_severity] medium [assayed_transcript] PomBase:SPAC110.01	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09 [has_severity] medium	(Fig. 4B)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC887.17 [has_severity] medium	(Fig. 4B)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 4C)
PMID:40402811	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] high	(Fig. 4C)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c	(Fig. 4C)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01 [has_severity] low	(Fig. 4C)
PMID:40402811	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] high	(Fig. 4C)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 4C)
PMID:40402811	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] low	(Fig. 4D)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c	(Fig. 4D)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 4D)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 4D)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 4D)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] low	(Fig. 4D)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 4E)
PMID:40402811	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] medium	(Fig. 4E)
PMID:40402811	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] medium	(Fig. 4E)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 4E)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 4E)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c	(Fig. 4E)
PMID:40402811	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC359.03c [has_severity] high	(Fig. 4F)
PMID:40402811	FYPO:0001984	protein absent from cell during vegetative growth [assayed_protein] PomBase:SPBC359.03c	(Fig. 4F)
PMID:40402811	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC359.03c [has_severity] medium	(Fig. 4F)
PMID:40402811	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAC821.09	(Fig. 4G)
PMID:40402811	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC821.09 [has_severity] medium	(Fig. 4G)
PMID:40402811	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC821.09 [has_severity] medium	(Fig. 4G)
PMID:40402811	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAC110.01	(Fig. 4H)
PMID:40402811	FYPO:0001324	decreased protein level during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAC110.01	(Fig. 4H)
PMID:40402811	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC110.01 [has_severity] medium	(Fig. 4H)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c	(Fig. 5G)
PMID:40402811	FYPO:0000825	increased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c [has_severity] low	(Fig. 5G)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09	(Fig. 5G)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 5G)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 5G)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC887.17	(Fig. 5G)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC887.17	(Fig. 5G)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09	(Fig. 5G)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPBC359.03c	(Fig. 5G)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 5G)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 5G)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC887.17 [has_severity] low	(Fig. 5G)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC887.17 [has_severity] low	(Fig. 5G)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 5G)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC110.01	(Fig. 5G)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09	(Fig. 5G)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC887.17 [has_severity] low	(Fig. 5G)
PMID:40402811	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPBC887.17 [has_severity] low	(Fig. 5G)
PMID:40402811	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPAC821.09	(Fig. 5G)
PMID:40402811	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC28F2.12 [has_severity] high [assayed_region] PomBase:SPAC821.09	(Fig. 6B)
PMID:40402811	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC28F2.12 [has_severity] high [assayed_region] PomBase:SPBC887.17	(Fig. 6B)
PMID:40402811	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC28F2.12 [has_severity] high [assayed_region] PomBase:SPBC887.17	(Fig. 6B)
PMID:40402811	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_region] PomBase:SPBC359.03c [assayed_protein] PomBase:SPBC28F2.12 [has_severity] high	(Fig. 6B)
PMID:40402811	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC28F2.12 [has_severity] high [assayed_region] PomBase:SPBC887.17	(Fig. 6B)
PMID:40402811	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC28F2.12 [has_severity] high [assayed_region] PomBase:SPAC821.09	(Fig. 6B)
PMID:40402811	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC28F2.12 [has_severity] high [assayed_region] PomBase:SPBC887.17	(Fig. 6B)
PMID:40402811	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC28F2.12 [has_severity] high [assayed_region] PomBase:SPAC821.09	(Fig. 6B)
PMID:40402811	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_protein] PomBase:SPBC28F2.12 [has_severity] high [assayed_region] PomBase:SPAC821.09	(Fig. 6B)
PMID:40402811	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_region] PomBase:SPBC359.03c [assayed_protein] PomBase:SPBC28F2.12 [has_severity] high	(Fig. 6B)
PMID:40402811	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_region] PomBase:SPBC359.03c [assayed_protein] PomBase:SPBC28F2.12 [has_severity] high	(Fig. 6B)
PMID:40402811	FYPO:0004161	decreased protein localization to chromatin at RNA polymerase II-transcribed genes during vegetative growth [assayed_region] PomBase:SPBC359.03c [assayed_protein] PomBase:SPBC28F2.12 [has_severity] high	(Fig. 6B)
PMID:40402811	FYPO:0000095	sensitive to bleomycin [has_severity] low	(Fig. 6C)
PMID:40402811	FYPO:0004752	resistance to phleomycin [has_severity] low	(Fig. 6C)
PMID:40402811	FYPO:0002344	sensitive to phleomycin [has_severity] medium	(Fig. 6C)
PMID:40402811	FYPO:0002344	sensitive to phleomycin [has_severity] low	(Fig. 6C)
PMID:40402811	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 6C)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 6C)
PMID:40402811	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 6C)
PMID:40402811	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. 6C)
PMID:40402811	FYPO:0000085	sensitive to camptothecin [has_severity] high	(Fig. 6C)
PMID:40402811	FYPO:0001032	resistance to camptothecin [has_severity] medium	(Fig. 6C)
PMID:40402811	FYPO:0003906	normal growth on bleomycin	(Fig. 6C)
PMID:40402811	FYPO:0001032	resistance to camptothecin [has_severity] low	(Fig. 6C)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 6C)
PMID:40402811	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 6C)
PMID:40402811	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(Fig. 6C)
PMID:40402811	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 6C)
PMID:40402811	FYPO:0001357	normal vegetative cell population growth	(Fig. 6C)
PMID:40402811	FYPO:0009031	resistance to bleomycin [has_severity] low	(Fig. 6C)
PMID:40406582	FYPO:0003216	decreased chromatin silencing at rDNA	For this, we monitored for de-repression of the ura4+ reporter gene that had been integrated into the normally silenced rDNA repeats (Jin et al., 2007; Thon and Verhein-Hansen, 2000). Depression of the ura4+ reporter in this context leads to enhanced growth on plates lacking exogenous uracil and increased sensitivity to 5-fluoroorotic acid (5-FOA). By this assay, we found that rDNA silencing was partially relieved in nsk1∆ cells (Figure 1A) and to the same extent as in dnt1∆ cells (Jin et al., 2007).
PMID:40406582	FYPO:0002965	normal protein localization to nucleolus [assayed_protein] PomBase:SPAC140.02	Gar2-GFP, a nucleolar marker and ortholog of human nucleolin (Gulli et al., 1995; Rutherford et al., 2024), localized normally within the nucleolus of nsk1∆ cells, as did two other nucleolar proteins, Nop2, a rRNA methyltransferase involved in ribosome biogenesis (Rutherford et al., 2024), and Nuc1 (Hirano et al., 1989) (Figure 1D).
PMID:40406582	FYPO:0002965	normal protein localization to nucleolus [assayed_protein] PomBase:SPBC4C3.05c	Gar2-GFP, a nucleolar marker and ortholog of human nucleolin (Gulli et al., 1995; Rutherford et al., 2024), localized normally within the nucleolus of nsk1∆ cells, as did two other nucleolar proteins, Nop2, a rRNA methyltransferase involved in ribosome biogenesis (Rutherford et al., 2024), and Nuc1 (Hirano et al., 1989) (Figure 1D).
PMID:40406582	FYPO:0002965	normal protein localization to nucleolus [assayed_protein] PomBase:SPBP8B7.20c	Gar2-GFP, a nucleolar marker and ortholog of human nucleolin (Gulli et al., 1995; Rutherford et al., 2024), localized normally within the nucleolus of nsk1∆ cells, as did two other nucleolar proteins, Nop2, a rRNA methyltransferase involved in ribosome biogenesis (Rutherford et al., 2024), and Nuc1 (Hirano et al., 1989) (Figure 1D).
PMID:40406582	FYPO:0004329	normal mitotic rDNA separation [assayed_protein] PomBase:SPBP8B7.20c	Time-lapse imaging of 21 nsk1+ and 42 nsk1∆ cells showed that Gar2-GFP segregated equally and without lagging in all cells (Figure 1E).
PMID:40427588	FYPO:0001357	normal vegetative cell population growth	Compared to wild-type cells, the growth of mti2∆insertion and ∆mti2 cells was only marginally reduced in glucose media but was significantly impaired in glycerol media (Figure 2b).
PMID:40427588	FYPO:0000684	decreased cell population growth on glycerol carbon source	Compared to wild-type cells, the growth of mti2∆insertion and ∆mti2 cells was only marginally reduced in glucose media but was significantly impaired in glycerol media (Figure 2b).
PMID:40427588	FYPO:0001357	normal vegetative cell population growth	Compared to wild-type cells, the growth of mti2∆insertion and ∆mti2 cells was only marginally reduced in glucose media but was significantly impaired in glycerol media (Figure 2b). This result suggests that mitochondrial respiration is similarly inhibited in both mutants.
PMID:40427588	FYPO:0000684	decreased cell population growth on glycerol carbon source	Compared to wild-type cells, the growth of mti2∆insertion and ∆mti2 cells was only marginally reduced in glucose media but was significantly impaired in glycerol media (Figure 2b). This result suggests that mitochondrial respiration is similarly inhibited in both mutants.
PMID:40427588	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPMIT.07	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	FYPO:0001324	decreased protein level during vegetative growth [assayed_transcript] PomBase:SPMIT.05	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPMIT.11	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	FYPO:0001324	decreased protein level during vegetative growth [assayed_transcript] PomBase:SPMIT.05	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPMIT.01	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPMIT.11	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPMIT.04	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPMIT.07	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPMIT.04	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPMIT.01	Furthermore, both mti2∆insertion and ∆mti2 cells showed nearly abolished expression of the corresponding OXPHOS-related proteins (Figure 2d).
PMID:40427588	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.08	However, the RNA level of var1, which encodes a mitochondrial ribosomal protein, remained stable in both mutants (Figure 2c)
PMID:40427588	FYPO:0001317	normal RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.08	However, the RNA level of var1, which encodes a mitochondrial ribosomal protein, remained stable in both mutants (Figure 2c).
PMID:40427588	FYPO:0008434	abnormal mitochondrial ribosome assembly	Moreover, the deletion significantly reduced the association with assembled mitoribosomes and impaired mitoribosome assembly. Specifically, a distinct mitoribosome peak was observed in fraction 11 in the wild-type cells (Figure 4a) but was markedly diminished in the mti2∆insertion cells (Figure 4b), indicating a defect in mitoribosome assembly.
PMID:40427588	FYPO:0008434	abnormal mitochondrial ribosome assembly	Moreover, the deletion significantly reduced the association with assembled mitoribosomes and impaired mitoribosome assembly. Specifically, a distinct mitoribosome peak was observed in fraction 11 in the wild-type cells (Figure 4a) but was markedly diminished in the mti2∆insertion cells (Figure 4b), indicating a defect in mitoribosome assembly. This phenotype is similar Biomolecules 2025, 15, x FOR PEER REVIEW 11 of 16 to that observed in ∆mti2 cells (Figure 4c).
PMID:40427588	FYPO:0007525	decreased ribosome binding [assayed_protein] PomBase:SPBC18E5.13	Notably, deletion of the insertion domain resulted in a greatly decreased associ- ation of the translation initiation factors Mti2 and Mti3 with the mtSSU.
PMID:40427588	FYPO:0007525	decreased ribosome binding [assayed_protein] PomBase:SPBC1271.15c	Notably, deletion of the insertion domain resulted in a greatly decreased associ- ation of the translation initiation factors Mti2 and Mti3 with the mtSSU.
PMID:40427588	GO:0070124	mitochondrial translational initiation	These findings indicate that, similar to MTIF2 in humans, the insertion domain in S. pombe Mti2 promotes the efficiency of translation initiation by facilitating the association of initiation factors with the mitochondrial ribosome.
PMID:40427588	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPBC18E5.13 [part_of] mitochondrial translational initiation	These findings indicate that, similar to MTIF2 in humans, the insertion domain in S. pombe Mti2 promotes the efficiency of translation initiation by facilitating the association of initiation factors with the mitochondrial ribosome.
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.07	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.10	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.09	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.07	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.04	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.11	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.01	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.05	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPRRNA.01	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPRRNA.02	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.10	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.09	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.04	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.11	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.01	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPRRNA.01	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPRRNA.02	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes,
PMID:40427588	FYPO:0001117	decreased RNA level during vegetative growth [assayed_transcript] PomBase:SPMIT.05	We found that mti2∆insertion cells, similar to ∆mti2 cells, showed significantly reduced RNA levels of core subunits of respiratory chain complexes, including cob1 (complex III), cox1, cox2 and cox3 (complex IV) and atp6, atp8 and atp9 (ATP synthase).
PMID:40452482	GO:1990916	Isp3 layer of spore wall	Isp3 is the major component of the outermost spore wall layer in S. pombe and is required for the surface hydrophobicity of mature spores.
PMID:40452482	FYPO:0000175	abnormal ascospore wall assembly	The isp3Δ mutant spores fail to partition into the hydrophobic polyethylene glycol (PEG) phase in aqueous two-phase systems (ATPSs), suggesting that Isp3 is required for proper spore wall assembly and surface hydrophobicity.
PMID:40452482	GO:0042244	spore wall assembly	The isp3Δ mutant spores fail to partition into the hydrophobic polyethylene glycol (PEG) phase in aqueous two-phase systems (ATPSs), suggesting that Isp3 is required for proper spore wall assembly and surface hydrophobicity.
PMID:40484900	GO:0008553	P-type proton-exporting transporter activity	(comment: Pma1 is a direct target of inhibitors Si01 and Si04) Next, P-type ATPase activitiy of whole cell was ana- lyzed to test whether Si01 inhibits it in fission yeast (Fig. 1D) and budding yeast (Fig. 1E).
PMID:40484900	GO:0120029	proton export across plasma membrane	The results showed that Si01 treatment suppressed the acidification of the medium in a concentration-dependent manner. This result suggests that Si01 inhibits ­ H+ efflux activity.
PMID:40484900	FYPO:0001310	normal viability in stationary phase	The results showed that the addition of Si01 to L18 did not have an additive effect on lifespan extension (Fig. 5A). This suggested that the lifespan extension effect of Si01 is mediated through the same path- way as that of L18 mutant.
PMID:40526720	FYPO:0003480	queuosine absent from tRNA	In contrast, in the qtp1∆ strain, tRNAAsp showed no Q modification of the tRNA even at the higher q concentration. Similarly, the qtp1∆ strain showed no Q modification of tRNAAsp when provided with the Q nucleoside, whereas the WT strain showed full modification.
PMID:40526720	GO:0160286	queuosine transmembrane transporter activity	SLC35F2 Homologs Are the Sole q/Q Transporters in S. pombe and T. brucei.
PMID:40526720	GO:0160283	queuine transmembrane transporter activity	SLC35F2 Homologs Are the Sole q/Q Transporters in S. pombe and T. brucei.
PMID:40526720	GO:0160284	queuine import across plasma membrane	To test whether Qtp1 transports q and/or Q in  S. pombe , a qtp1∆ strain was constructed, and Q levels analyzed via APB Northerns in tRNAAsp extracted from cells grown in medium supplemented with either q or Q ( Fig. 3D ). In the pres- ence of 10 nM q, WT cells showed partial Q modification of tRNAAsp , and 100 nM q resulted in full modification, as deter- mined by APB Northern blotting. In contrast, in the qtp1∆ strain, tRNAAsp showed no Q modification of the tRNA even at the higher q concentration. Similarly, the qtp1∆ strain showed no Q modification of tRNAAsp when provided with the Q nucleoside, whereas the WT strain showed full modification.
PMID:40526720	FYPO:0001357	normal vegetative cell population growth	ot a principal effect of q/Q deficiency. Growth of the T. brucei or S. pombe Qtp1 deficient strains was not affected (SI Appendix, Fig. S7 D and E ), in agreement with the fact that Q in tRNA is not essential for growth in these organ- isms ( 4 , 10 , 19 , 22 – 26 ).
PMID:40629316	FYPO:0008456	normal plasma membrane hypoosmotic expansion during vegetative growth	Among them, Tcb2 is functionally unrelated, as tcb2Δ protoplasts exhibited normal Ca2+-dependent hypotonic PM expansion (Fig. 3B).
PMID:40629316	FYPO:0008456	normal plasma membrane hypoosmotic expansion during vegetative growth	Curiously, protoplasts lacking the only putative water channel Aqp1 (encoded by SPAC977.17) exhibited normal Ca2+ influx and WT- like hypoosmotic PM expansion (Additional file 1: Fig. S1E).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] medium	Furthermore, our domain analysis using truncation mutants manifest that the TM, SMP, and C2A domains of either E-Syts, as well as the C2C domain of Tcb1, are crucial for hypotonic PM expansion (Fig. 3E and Addi- tional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] high	Furthermore, our domain analysis using truncation mutants manifest that the TM, SMP, and C2A domains of either E-Syts, as well as the C2C domain of Tcb1, are crucial for hypotonic PM expansion (Fig. 3E and Addi- tional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] high	Furthermore, our domain analysis using truncation mutants manifest that the TM, SMP, and C2A domains of either E-Syts, as well as the C2C domain of Tcb1, are crucial for hypotonic PM expansion (Fig. 3E and Addi- tional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] medium	Furthermore, our domain analysis using truncation mutants manifest that the TM, SMP, and C2A domains of either E-Syts, as well as the C2C domain of Tcb1, are crucial for hypotonic PM expansion (Fig. 3E and Addi- tional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] low	Furthermore, our domain analysis using truncation mutants manifest that the TM, SMP, and C2A domains of either E-Syts, as well as the C2C domain of Tcb1, are crucial for hypotonic PM expansion (Fig. 3E and Addi- tional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] low	Furthermore, our domain analysis using truncation mutants manifest that the TM, SMP, and C2A domains of either E-Syts, as well as the C2C domain of Tcb1, are crucial for hypotonic PM expansion (Fig. 3E and Addi- tional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] high	Furthermore, our domain analysis using truncation mutants manifest that the TM, SMP, and C2A domains of either E-Syts, as well as the C2C domain of Tcb1, are crucial for hypotonic PM expansion (Fig. 3E and Addi- tional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] high	Furthermore, our domain analysis using truncation mutants manifest that the TM, SMP, and C2A domains of either E-Syts, as well as the C2C domain of Tcb1, are crucial for hypotonic PM expansion (Fig. 3E and Addi- tional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] high	Furthermore, our domain analysis using truncation mutants manifest that the TM, SMP, and C2A domains of either E-Syts, as well as the C2C domain of Tcb1, are crucial for hypotonic PM expansion (Fig. 3E and Addi- tional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] high	Furthermore, our domain analysis using truncation mutants manifest that the TM, SMP, and C2A domains of either E-Syts, as well as the C2C domain of Tcb1, are crucial for hypotonic PM expansion (Fig. 3E and Addi- tional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] high	Furthermore, our domain analysis using truncation mutants manifest that the TM, SMP, and C2A domains of either E-Syts, as well as the C2C domain of Tcb1, are crucial for hypotonic PM expansion (Fig. 3E and Addi- tional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] medium	Furthermore, our domain analysis using truncation mutants manifest that the TM, SMP, and C2A domains of either E-Syts, as well as the C2C domain of Tcb1, are crucial for hypotonic PM expansion (Fig. 3E and Addi- tional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] low	However, unlike the previous study showing limited expansion of eisosome-deficient pil1Δ protoplasts after mild hypoosmotic shocks (ΔC=−0.4 M or−0.2 M sorbitol) [5], we found pil1Δ protoplasts exhibited WT-like hypotonic PM expansion, with only a minor reduction in cell surface area increment (Addi- tional file 1: Fig. S2B).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] high	In contrast, both tcb1Δ and tcb3Δ single mutants showed compromised PM expansion similar to tcb1Δtcb3Δ double mutant under acute hypoosmotic shock (Fig. 3B), implying that they may function together.
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] high	In contrast, both tcb1Δ and tcb3Δ single mutants showed compromised PM expansion similar to tcb1Δtcb3Δ double mutant under acute hypoosmotic shock (Fig. 3B), implying that they may function together.
PMID:40629316	GO:0160219	cortical endoplasmic reticulum membrane	In fact, unlike a previous study that showed their ER localization via immunostaining [13], C-terminally GFP-tagged Msy1 and Msy2 expressed from native loci, mainly localized to the cell cortex in both walled cells and protoplasts (Additional file 1: Fig. S1C and Fig. 1E).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] high	Instead, our screening for Ca2+-effectors involved in hypotonic PM expansion revealed that tcb1Δtcb3Δ protoplasts lacking two fis- sion yeast E-Syts barely survived such PM injury and ruptured quickly after Ca2+ influx with limited PM expansion (Fig. 2E).
PMID:40629316	FYPO:0003016	cell lysis during cellular response to non-ionic osmotic stress [has_severity] high	Instead, our screening for Ca2+-effectors involved in hypotonic PM expansion revealed that tcb1Δtcb3Δ protoplasts lacking two fis- sion yeast E-Syts barely survived such PM injury and ruptured quickly after Ca2+ influx with limited PM expansion (Fig. 2E).
PMID:40629316	FYPO:0008198	decreased protein localization to plasma membrane during vegetative growth [assayed_protein] PomBase:SPAPYUK71.03c	Interestingly, the accumulation of Tcb1 and Tcb3 at ER-PM contacts is mutually depend- ent: Tcb3 delocalized to the perinuclear ER in tcb1Δ, while Tcb1 levels in the cortical ER decreased in tcb3Δ. Their localization remained unchanged in tcb2Δ (Fig. 3C and Additional file 1: Fig. S3A).
PMID:40629316	FYPO:0008198	decreased protein localization to plasma membrane during vegetative growth [assayed_protein] PomBase:SPCC962.01	Interestingly, the accumulation of Tcb1 and Tcb3 at ER-PM contacts is mutually depend- ent: Tcb3 delocalized to the perinuclear ER in tcb1Δ, while Tcb1 levels in the cortical ER decreased in tcb3Δ. Their localization remained unchanged in tcb2Δ (Fig. 3C and Additional file 1: Fig. S3A).
PMID:40629316	FYPO:0008456	normal plasma membrane hypoosmotic expansion during vegetative growth	Moreover, both Ync13 and Git1, the S. pombe homologs of Munc13 family which is one core......were dispensable for substantial hypotonic PM expansion (Additional file 1: Fig. S2E).
PMID:40629316	FYPO:0008456	normal plasma membrane hypoosmotic expansion during vegetative growth	Moreover, both Ync13 and Git1, the S. pombe homologs of Munc13 family which is one core......were dispensable for substantial hypotonic PM expansion (Additional file 1: Fig. S2E).
PMID:40629316	FYPO:0008456	normal plasma membrane hypoosmotic expansion during vegetative growth	Moreover, none of other putative non-essen- tial stretch-activated ion channels [29] or organellar Ca2+-ATPase [30] appeared to be crucial for control- ling Ca2+ flux or for acute hypotonic protoplast expan- sion (Additional file 1: Fig. S1E).
PMID:40629316	FYPO:0008456	normal plasma membrane hypoosmotic expansion during vegetative growth	Moreover, none of other putative non-essen- tial stretch-activated ion channels [29] or organellar Ca2+-ATPase [30] appeared to be crucial for control- ling Ca2+ flux or for acute hypotonic protoplast expan- sion (Additional file 1: Fig. S1E).
PMID:40629316	FYPO:0008456	normal plasma membrane hypoosmotic expansion during vegetative growth	Moreover, none of other putative non-essen- tial stretch-activated ion channels [29] or organellar Ca2+-ATPase [30] appeared to be crucial for control- ling Ca2+ flux or for acute hypotonic protoplast expan- sion (Additional file 1: Fig. S1E).
PMID:40629316	FYPO:0008456	normal plasma membrane hypoosmotic expansion during vegetative growth	Moreover, none of other putative non-essen- tial stretch-activated ion channels [29] or organellar Ca2+-ATPase [30] appeared to be crucial for control- ling Ca2+ flux or for acute hypotonic protoplast expan- sion (Additional file 1: Fig. S1E).
PMID:40629316	FYPO:0008456	normal plasma membrane hypoosmotic expansion during vegetative growth	Other potential Ca2+-effectors, including putative Rab GTPases Gyp2 and Gyp4, which are implicated in vesi- cle trafficking, were also not required for hypotonic PM expansion (Additional file 1: Fig. S2E).
PMID:40629316	FYPO:0008456	normal plasma membrane hypoosmotic expansion during vegetative growth	Other potential Ca2+-effectors, including putative Rab GTPases Gyp2 and Gyp4, which are implicated in vesi- cle trafficking, were also not required for hypotonic PM expansion (Additional file 1: Fig. S2E).
PMID:40629316	FYPO:0001953	abnormal calcium import [has_severity] high	Remarkably, protoplasts lacking both MscS-like mechanosensitive channels (Msy1 and Msy2) showed no apparent Ca2+ influx after hypoosmotic shock regardless of Ca2+ in the medium (Fig. 1D).
PMID:40629316	FYPO:0003016	cell lysis during cellular response to non-ionic osmotic stress [has_severity] high	Similar to WT protoplasts treated with Ca2+-free hypotonic buffer, both msy1Δmsy2Δ and msy2Δ cells exhibited limited PM expansion (~10%) before quick rupturing, independently of external Ca2+ (Fig. 1D and Additional file 1: Fig. S1B).
PMID:40629316	FYPO:0003016	cell lysis during cellular response to non-ionic osmotic stress [has_severity] high	Similar to WT protoplasts treated with Ca2+-free hypotonic buffer, both msy1Δmsy2Δ and msy2Δ cells exhibited limited PM expansion (~10%) before quick rupturing, independently of external Ca2+ (Fig. 1D and Additional file 1: Fig. S1B).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] high	Similar to WT protoplasts treated with Ca2+-free hypotonic buffer, both msy1Δmsy2Δ and msy2Δ cells exhibited limited PM expansion (~10%) before quick rupturing, independently of external Ca2+ (Fig. 1D and Additional file 1: Fig. S1B).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] high	Similar to WT protoplasts treated with Ca2+-free hypotonic buffer, both msy1Δmsy2Δ and msy2Δ cells exhibited limited PM expansion (~10%) before quick rupturing, independently of external Ca2+ (Fig. 1D and Additional file 1: Fig. S1B).
PMID:40629316	FYPO:0008456	normal plasma membrane hypoosmotic expansion during vegetative growth	Such hypothetical PM repair does not require Ca2+-dependent ESCRT-III/Vps4 machinery [44], as no apparent defects were seen in hypotonic PM expansion in protoplasts lacking related key play- ers (Additional file 1: Fig. S2E).
PMID:40629316	GO:0015275	stretch-activated, monoatomic cation-selective, calcium channel activity [happens_during] cellular hypotonic response	Taken together, our results suggest that extracellular Ca2+influx controlled by MscS-like mechanosensitive channels is
PMID:40629316	GO:0071476	cellular hypotonic response	Taken together, our results suggest that extracellular Ca2+influx controlled by MscS-like mechanosensitive channels is
PMID:40629316	GO:0071476	cellular hypotonic response	Taken together, our results suggest that extracellular Ca2+influx controlled by MscS-like mechanosensitive channels is
PMID:40629316	GO:0015275	stretch-activated, monoatomic cation-selective, calcium channel activity [happens_during] cellular hypotonic response	Taken together, our results suggest that extracellular Ca2+influx controlled by MscS-like mechanosensitive channels is
PMID:40629316	GO:0140268	endoplasmic reticulum-plasma membrane contact site	Tcb1 and Tcb3 were mainly enriched at ER-PM contacts in both protoplasts and walled cells. (Fig. 3C and Addi- tional file 1: Fig. S3A)
PMID:40629316	GO:0140268	endoplasmic reticulum-plasma membrane contact site	Tcb1 and Tcb3 were mainly enriched at ER-PM contacts in both protoplasts and walled cells. (Fig. 3C and Addi- tional file 1: Fig. S3A)
PMID:40629316	GO:0120013	lipid transfer activity [happens_during] cellular hypotonic response	The reduced PM sur- face increase in tcb1wwtcb3www background implies that Tcb1/3-mediated lipid transfer may also contribute to expanding the PM. In line with this, raising the amount of Tcb1/3 resulted in a ~ 5% more PM surface area expan- sion and a~18.2% higher survival rate during the shock (Fig. 3F and Additional file 1: Fig. S3D).
PMID:40629316	GO:0120013	lipid transfer activity [happens_during] cellular hypotonic response	The reduced PM sur- face increase in tcb1wwtcb3www background implies that Tcb1/3-mediated lipid transfer may also contribute to expanding the PM. In line with this, raising the amount of Tcb1/3 resulted in a ~ 5% more PM surface area expan- sion and a~18.2% higher survival rate during the shock (Fig. 3F and Additional file 1: Fig. S3D).
PMID:40629316	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPAPYUK71.03c	These mutations did not affect protein locali- zation but indeed led to compromised hypotonic PM expansion (Fig. 3F and Additional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] medium	These mutations did not affect protein locali- zation but indeed led to compromised hypotonic PM expansion (Fig. 3F and Additional file 1: Fig. S3C).
PMID:40629316	FYPO:0008455	decreased plasma membrane hypoosmotic expansion during vegetative growth [has_severity] medium	These mutations did not affect protein locali- zation but indeed led to compromised hypotonic PM expansion (Fig. 3F and Additional file 1: Fig. S3C).
PMID:40629316	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPCC962.01	These mutations did not affect protein locali- zation but indeed led to compromised hypotonic PM expansion (Fig. 3F and Additional file 1: Fig. S3C).
PMID:40629316	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPAPYUK71.03c	These mutations did not affect protein locali- zation but indeed led to compromised hypotonic PM expansion (Fig. 3F and Additional file 1: Fig. S3C).
PMID:40629316	FYPO:0003627	normal protein localization [assayed_protein] PomBase:SPCC962.01	These mutations did not affect protein locali- zation but indeed led to compromised hypotonic PM expansion (Fig. 3F and Additional file 1: Fig. S3C).
PMID:40629316	GO:0005886	plasma membrane	Using scs2Δscs22Δ background where the cortical ER (cER) indicated by the luminal ER marker mCherry-ADEL [28] is largely detached from the PM [16], we confirmed that a considerable portion of Msy2 and Msy1 localized to the PM of the protoplasts (Fig. 1E).
PMID:40629316	GO:0005886	plasma membrane [exists_during] cellular hypotonic response	Using scs2Δscs22Δ background where the cortical ER (cER) indicated by the luminal ER marker mCherry-ADEL [28] is largely detached from the PM [16], we confirmed that a considerable portion of Msy2 and Msy1 localized to the PM of the protoplasts (Fig. 1E). We also performed membrane fractiona- tion by sucrose density gradient centrifugation in the same background where the PM and the cortical are separable, and confirmed that Msy2-GFP was indeed enriched in the light membrane fractions containing the PM-resident protein Pma1 but not the ER-resident protein TM-GFP [17] (Additional file 1: Fig. S1D).
PMID:40668835	FYPO:0002946	abnormal cell wall	*****More rigid cell wall****** Figure 6
PMID:40668835	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells [has_penetrance] high	Almost every aah1∆ aah3∆ cell also contained at least one septum, and the cells tended to form clumps (Fig. 2A). These observations were confirmed by fixing and staining the cells with DAPI and methyl blue to mark the DNA and the cell wall, respectively, and quan- tifying the number of nucleated cell compartments per clump or cell (Fig. 2 C and D)
PMID:40668835	FYPO:0001035	increased cell wall thickness during vegetative growth	Despite the apparent lack of an outer GM layer, the width of aah1∆ aah3∆ cell walls were more variable compared to wildtype cell walls and generally the walls were thicker (Fig. 3 A–C),
PMID:40668835	FYPO:0006117	multiseptate spheroid vegetative cell	Figure 2
PMID:40668835	FYPO:0002265	decreased cell wall galactomannan level	Figure 5 and S2
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Figure S1
PMID:40668835	FYPO:0001357	normal vegetative cell population growth [has_severity] high	Figure S1
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Figure S1
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Figure S1
PMID:40668835	FYPO:0000080	decreased cell population growth at low temperature	Figure S1
PMID:40668835	FYPO:0000080	decreased cell population growth at low temperature	Figure S1
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Figure S4
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Figure S4
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Figure S4
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Figure S4
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Figure S4
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Figure S4
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	Figure S4
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Figure S4
PMID:40668835	FYPO:0001081	decreased cell wall alpha-glucan level	In comparison, the aah1∆ aah3∆ mutant exhibited a significantly reduced α-1,3-glucan con- tent, with the Aa1 peak diminished to one-third of its original intensity and the Ab1 peak completely absent (Fig. 4C, Fig 5).....Consequently, the overall α-1,3-glucan content declined markedly, from 44% in wildtype rigid cell walls to 11% in the aah1∆ aah3∆ mutant
PMID:40668835	FYPO:0004103	viable spherical vegetative cell	Last, aah1∆ aah3∆ cells were spherical rather than rod-shaped resulting in a ratio of sep- tated cell length-to-width nearing one (Fig. 2 A and B).
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Of the double mutant strains, only aah1∆ aah3∆ cells showed an enhanced growth defect at all temperatures tested (SI Appendix, Fig. S1).
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Of the double mutant strains, only aah1∆ aah3∆ cells showed an enhanced growth defect at all temperatures tested (SI Appendix, Fig. S1).
PMID:40668835	FYPO:0001357	normal vegetative cell population growth	Of the double mutant strains, only aah1∆ aah3∆ cells showed an enhanced growth defect at all temperatures tested (SI Appendix, Fig. S1).
PMID:40668835	FYPO:0001357	normal vegetative cell population growth	Of the double mutant strains, only aah1∆ aah3∆ cells showed an enhanced growth defect at all temperatures tested (SI Appendix, Fig. S1).
PMID:40668835	FYPO:0001357	normal vegetative cell population growth	Of the double mutant strains, only aah1∆ aah3∆ cells showed an enhanced growth defect at all temperatures tested (SI Appendix, Fig. S1).
PMID:40668835	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Of the double mutant strains, only aah1∆ aah3∆ cells showed an enhanced growth defect at all temperatures tested (SI Appendix, Fig. S1).
PMID:40668835	FYPO:0001357	normal vegetative cell population growth	The aah1∆, aah2∆, and aah4∆ cells grew like wildtype at all temperatures tested, and aah3∆ cells were cold- sensitive (SI Appendix, Fig. S1).
PMID:40668835	FYPO:0000080	decreased cell population growth at low temperature	The aah1∆, aah2∆, and aah4∆ cells grew like wildtype at all temperatures tested, and aah3∆ cells were cold- sensitive (SI Appendix, Fig. S1).
PMID:40668835	FYPO:0001357	normal vegetative cell population growth	The aah1∆, aah2∆, and aah4∆ cells grew like wildtype at all temperatures tested, and aah3∆ cells were cold- sensitive (SI Appendix, Fig. S1).
PMID:40668835	FYPO:0001357	normal vegetative cell population growth	The aah1∆, aah2∆, and aah4∆ cells grew like wildtype at all temperatures tested, and aah3∆ cells were cold- sensitive (SI Appendix, Fig. S1).
PMID:40668835	FYPO:0004860	increased cell wall beta-glucan level	The total β-1,3-glucan content increased from 55% in the wildtype to 89% in the mutant (Fig. 4D) (Figure 5 and S4)
PMID:40668835	FYPO:0000673	normal septum assembly	Thus, septum formation did not appear to be aberrant in aah1∆ aah3∆ cells.
PMID:40668835	FYPO:0001036	delaminated cell wall during vegetative growth	We also observed that the outermost layers of aah1∆ aah3∆ cell walls appeared to be abnormally shedding from the cell, a pheno- type not observed in wildtype cells and possibly explaining the reduction of FITC-Concanavalin A staining (Fig. 3A).
PMID:40668835	FYPO:0002151	inviable spore	We found that pck2Δ aah1Δ aah3Δ and pmk1Δ aah1Δ aah3Δ combinations were synthetically lethal (SI Appendix, Fig. S4F). These data suggest that there is a require- ment for sufficient β-glucan synthesis mediated by the CIP when the α-glucan network is disrupted. (Figure S4)
PMID:40668835	FYPO:0002151	inviable spore	We found that pck2Δ aah1Δ aah3Δ and pmk1Δ aah1Δ aah3Δ combinations were synthetically lethal (SI Appendix, Fig. S4F). These data suggest that there is a require- ment for sufficient β-glucan synthesis mediated by the CIP when the α-glucan network is disrupted. (Figure S4)
PMID:40668835	FYPO:0003133	galactomannan absent from cell wall	We further probed the observation that many aah1∆ aah3∆ cells lacked an outermost layer, typically composed of GMs, by staining cells with the Concanavalin A lectin labeled with fluorescein isothiocyanate (FITC).
PMID:40668835	FYPO:0001120	pear-shaped vegetative cell	aah3∆ cells were abnormally pear-shaped and had a lower length-to-width ratio (Fig. 2 A and B) consistent with published work (29, 39)
PMID:40668835	FYPO:0002104	viable vegetative cell with normal cell shape	cells had an average length-to-width ratio of ~4.5 indicative of their rod shape (Fig. 2 A and B).
PMID:40829803	GO:0160147	tRNA pseudouridine(38-40) synthase activity	Deg1,whichisthedirecthomolog of Deg1/Pus3 from S. cerevisiae and humans, modifies posi- tions 38,39,and40 in the anticodon stem
PMID:40829803	GO:0106029	tRNA pseudouridine synthase activity	Pus1 modifies positions 25 and 27 in the D arm of tRNAs [28,29] .The newly identified 22 site in the D arm is modified by Pus1. (comment: Pus1 pseudouridinylates positions 25/ 27, and position 22 in tRNA-Leu (AAG), tRNA-Leu (CAA), tRNA-Leu (CAG) and tRNA-Leu (TAG))
PMID:40829803	GO:0106029	tRNA pseudouridine synthase activity	Pus2 modifies position 1 in three tRNAs
PMID:40829803	GO:0106029	tRNA pseudouridine synthase activity	Pus3 pseudouridinylates position 1 of selected cytoplasmic tRNAs
PMID:40829803	GO:0160148	tRNA pseudouridine(55) synthase activity	Pus4 modifies U55
PMID:40829803	GO:0160150	tRNA pseudouridine(13) synthase activity	Pus7 modifies positions 6, 8, and 13 in S. pombe. For position 13 in the D arm, this is consistent with prior knowledge of Pus7 (comment: Pus7 pseudouridinylates position 13 in several tRNAs and positions 6 and 8 in tRNA-Val (TAC))
PMID:40829803	GO:0160151	tRNA pseudouridine(32) synthase activity	Pus9 modifies position 32 in the anticodon loop
PMID:40829803	FYPO:0008449	abnormal tRNA modification at postion U34	Raw signal intensities as well as Dorado probability scores showedclearlydistinguishablepatternsbetweenwtandelp6Δ at U34 (Fig. 4A and B; see Supplementary Fig. S15 for base- calling errors wt/elp6Δ)
PMID:40829803	FYPO:0008451	abnormal tRNA modification at postion A58	The m6A model resulted in elevated KL divergence at i6A37 positions in wt/tit1Δ (Fig. 5A) and at m1A58 in wt/trm6Δ (Fig.5B),t
PMID:40829803	FYPO:0008450	abnormal tRNA modification at postion A37	The m6A model resulted in elevated KL divergence at i6A37 positions in wt/tit1Δ (Fig. 5A) and at m1A58 in wt/trm6Δ (Fig.5B),t
PMID:40899782	FYPO:0008453	abolished Golgi cisternae stacking [has_penetrance] high	For WT and spap27g11.12 isolates, a stacked GA-like structure with multiple cisternae was clearly visible and corresponded to previous re- ports (Osumi 2012, Eckler et al. 2013). In contrast, no stacked GA structure was observed in cells of spac17a5.16 isolates and the onlycorrespondingstructurewasasingle,enlargedandelongated structure with associated vesicles. This single structure was not observed in BP90 or spap27g11.12 isolates.
PMID:40899782	FYPO:0000067	resistance to brefeldin A	Treating with increasing concentrations of Brefeldin A (BFA) led to an increase in GT for BP90 from a median time of 3.8–4.3 h, but not for either spac17a5.16 or spap27g11.12 (Fig.4A).
PMID:40899782	FYPO:0000127	increased sensitivity to chemical during vegetative growth [has_severity] high	Treatment with Golgicide A (GCA) resulted in increased GTs for all strains with spac17a5.16 being most profoundly affected (Fig. 4B). The median GT for spac17a5.16 increased by about 6 h compared to around 2 h for both BP90 and spap27g11.12.Again, the GT for spac17a5.16 under nontreated conditions was about 2 h longer than that for BP90.
PMID:40899782	FYPO:0000127	increased sensitivity to chemical during vegetative growth [has_severity] low	Treatment with Golgicide A (GCA) resulted in increased GTs for all strains with spac17a5.16 being most profoundly affected (Fig. 4B). The median GT for spac17a5.16 increased by about 6 h compared to around 2 h for both BP90 and spap27g11.12.Again, the GT for spac17a5.16 under nontreated conditions was about 2 h longer than that for BP90.
PMID:40931936	GO:0030674	protein-macromolecule adaptor activity [part_of] establishment of cell polarity [has_input] PomBase:SPAC3G9.05	5C). Thus, we propose that the S. pombe Spa2 SHD domain similarly recruits Gyp3 to sites of polarized growth and division
PMID:40931936	GO:0030674	protein-macromolecule adaptor activity [part_of] establishment of cell polarity [has_input] PomBase:SPCC4G3.09c	5C). Thus, we propose that the S. pombe Spa2 SHD domain similarly recruits Gyp3 to sites of polarized growth and division
PMID:40931936	FYPO:0001339	abnormal cellular response to starvation during vegetative growth	After nitrogen starvation at 32°C for 48 h, wild-type and spa2Δ cells arrested growth at the same short size (Fig. 7A,B). Upon re-feeding at 32°C, we observed that wildtype cells began to adopt a typical cylindrical shape by 6 h. In contrast, spa2Δ cells maintained a shorter, rounded morphology for significantly longer before resuming cylindrical growth by 24 h (Fig. 7A,B).
PMID:40931936	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_protein] PomBase:SPAC3G9.05	Although the C-terminal truncation mutants Spa2(1–500) and Spa2(1–360) localized to cell tips and septa like full-length Spa2, they were both reduced in intensity by 3-fold and 1.5-fold relative to full-length Spa2 at tips and the division site, respectively (Fig. 1D–F; Fig. S2A,B).
PMID:40931936	FYPO:0006221	decreased protein localization to cell division site, with protein mislocalized to cytoplasm [assayed_protein] PomBase:SPAC3G9.05	Although the C-terminal truncation mutants Spa2(1–500) and Spa2(1–360) localized to cell tips and septa like full-length Spa2, they were both reduced in intensity by 3-fold and 1.5-fold relative to full-length Spa2 at tips and the division site, respectively (Fig. 1D–F; Fig. S2A,B).
PMID:40931936	FYPO:0003209	abolished protein localization to cell tip, with protein mislocalized to cytoplasm [assayed_protein] PomBase:SPCC4G3.09c	Gyp3–mNG localization to cell tips and division sites was lost in spa2Δ cells (Fig. 5A),
PMID:40931936	FYPO:0000703	normal protein-protein interaction [assayed_protein] PomBase:SPAC3G9.05 [assayed_protein] PomBase:SPAC16E8.08	In accord with this model, a spa2 construct encoding residues 305–360 [spa2(305–360)] supported pos1 interaction in a yeast two-hybrid assay (Fig. 3C)
PMID:40931936	FYPO:0006221	decreased protein localization to cell division site, with protein mislocalized to cytoplasm [assayed_protein] PomBase:SPAC3G9.05	Pos1 directly binds Spa2 and promotes Spa2 localization
PMID:40931936	FYPO:0006221	decreased protein localization to cell division site, with protein mislocalized to cytoplasm [assayed_protein] PomBase:SPAC3G9.05 [has_severity] low	Spa2 lacking CC1 was reduced in abundance at the cell division site by ∼12%and at cell tips by ∼25%compared to levels of wild-type Spa2 (Fig. 2E,F; Fig. S2F).
PMID:40931936	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_protein] PomBase:SPAC3G9.05 [has_severity] low	Spa2 lacking CC1 was reduced in abundance at the cell division site by ∼12%and at cell tips by ∼25%compared to levels of wild-type Spa2 (Fig. 2E,F; Fig. S2F).
PMID:40931936	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_protein] PomBase:SPAC3G9.05 [has_severity] high	Spa2 lacking CC2 was more significantly reduced in abundance at both the cell division site (∼60%) and cell tips (∼67%) (Fig. 2E,F; Fig. S2F).
PMID:40931936	FYPO:0006221	decreased protein localization to cell division site, with protein mislocalized to cytoplasm [assayed_protein] PomBase:SPAC3G9.05	Spa2 lacking CC2 was more significantly reduced in abundance at both the cell division site (∼60%) and cell tips (∼67%) (Fig. 2E,F; Fig. S2F).
PMID:40931936	FYPO:0000835	decreased protein level [assayed_protein] PomBase:SPAC3G9.05	Spa2 lacking FAT1 did not have a change in cell division site localization but was decreased in abundance at cell tips by ∼32% compared to levels of wild-type Spa2 (Fig. 2E,F; Fig. S2F).
PMID:40931936	FYPO:0001586	decreased protein localization to cell tip during vegetative growth [assayed_protein] PomBase:SPAC3G9.05	Spa2 lacking FAT1 did not have a change in cell division site localization but was decreased in abundance at cell tips by ∼32% compared to levels of wild-type Spa2 (Fig. 2E,F; Fig. S2F).
PMID:40931936	FYPO:0003209	abolished protein localization to cell tip, with protein mislocalized to cytoplasm [assayed_protein] PomBase:SPAC3G9.05	Spa2(R58A, R59A)–GFP formed puncta and did not localize to the PM (Fig. 2D).
PMID:40931936	FYPO:0001584	abnormal protein localization to cell tip during vegetative growth [assayed_protein] PomBase:SPAC15A10.16	Therefore, we expected the tip distribution of Bud6–GFP3 to mirror that of Exo70–mNG and Sec3–mNG and to be broader in spa2Δ cells. This is what we observed (Fig. 6C,D),
PMID:40931936	FYPO:0001880	abolished protein localization to cell division site [assayed_protein] PomBase:SPAC3G9.05	Truncating the C terminus further to the predicted CC1 region (amino acid 305) abolished plasma membrane (PM) localization (Fig. 1D).
PMID:40931936	FYPO:0001584	abnormal protein localization to cell tip during vegetative growth [assayed_protein] PomBase:SPAC17G8.12	We found that not only were the Exo70–mNG and Sec3–mNG distributions broader in spa2Δ cells than in wild-type cells, but Exo70–mNG and Sec3–mNG lacked the medial peak of focused localization observed in wild-type cells (Fig. 6C,D).
PMID:40931936	FYPO:0001584	abnormal protein localization to cell tip during vegetative growth [assayed_protein] PomBase:SPBC106.20	We found that not only were the Exo70–mNG and Sec3–mNG distributions broader in spa2Δ cells than in wild-type cells, but Exo70–mNG and Sec3–mNG lacked the medial peak of focused localization observed in wild-type cells (Fig. 6C,D).
PMID:41068765	FYPO:0000684	decreased cell population growth on glycerol carbon source [has_severity] high	Both mutants grow normally in glucose-rich media. However, while mts4L636P mutants show normal growth in glycerol respiratory media, the atp3R282C mutant exhibited very slow growth (Fig. 3A).
PMID:41068765	FYPO:0001409	normal growth on glycerol carbon source	Both mutants grow normally in glucose-rich media. However, while mts4L636P mutants show normal growth in glycerol respiratory media, the atp3R282C mutant exhibited very slow growth (Fig. 3A).
PMID:41068765	FYPO:0004944	decreased mitochondrial membrane potential [has_severity] high	But the mts4L636P/atp2-R4-3 double mutant remained petite- positive, albeit yielding lower frequencies of ρ0 colonies upon EtBr treatment. ρ0 cells derived from this double mutant showed ­ DiOC6 staining levels similar to those of mts4L636P ρ0 cells Fig. 3F, Additional file 9), indicating that the atp2-R4-3 mutation does not further decrease ∆Ψ. Figure 3F
PMID:41068765	FYPO:0003881	mtDNA absent from cell [has_penetrance] high	Figure 1D D ρ0 growth assay after CRISPR mutagenesis to revert and induce the mts4L636P mutation. In the ptp1-1 and mts4L636P plates a section of each plate is amplified to show the growth of petite colonies.
PMID:41068765	FYPO:0005142	decreased proteasome core complex binding	Figure 2D
PMID:41068765	FYPO:0003881	mtDNA absent from cell [has_penetrance] high	Figure 3C ρ0 growth assay in combination with Δαtp2 mutation. .....and the atg43-1 single mutant was petite- negative (Additional file 6: Fig. S2).
PMID:41068765	FYPO:0004944	decreased mitochondrial membrane potential [has_severity] medium	Figure 3D
PMID:41068765	FYPO:0000359	abnormal mitochondrial morphology	Figure 3D
PMID:41068765	FYPO:0004944	decreased mitochondrial membrane potential [has_severity] high	Figure 3D
PMID:41068765	FYPO:0004944	decreased mitochondrial membrane potential [has_severity] medium	Figure 3D
PMID:41068765	FYPO:0004085	decreased vegetative cell growth [has_severity] low	Figure 3E
PMID:41068765	FYPO:0000359	abnormal mitochondrial morphology	Figure 3F
PMID:41068765	FYPO:0000637	increased cell population growth rate on glucose carbon source	Furthermore, ρ0 strains derived from mts4L636P/atp3R282C double mutants showed faster growth than ρ0 strains derived from either single mutant (Fig. 3B) (AND WILD-TYP)
PMID:41068765	FYPO:0002061	inviable vegetative cell population	Interest- ingly, both mutants lost petite-positivity after knockout of atp2, indicating that the mts4L636P mutation requires a functional ­ F1-ATPase for survival in the absence of mtDNA (Fig. 3C).
PMID:41068765	FYPO:0002061	inviable vegetative cell population	Interest- ingly, both mutants lost petite-positivity after knockout of atp2, indicating that the mts4L636P mutation requires a functional ­ F1-ATPase for survival in the absence of mtDNA (Fig. 3C).Figure 3C
PMID:41068765	FYPO:0002060	viable vegetative cell population	Supplementary Figure 2
PMID:41068765	FYPO:0007629	normal viability during G0	Surprisingly, the viability of the mts4L636P mutants did not decrease even after pro- longed culture and exceeded the viability of the WT after very long exposure to media without nitrogen.
PMID:41068765	FYPO:0004344	increased viability upon nitrogen starvation	Surprisingly, the viability of the mts4L636P mutants did not decrease even after pro- longed culture and exceeded the viability of the WT after very long exposure to media without nitrogen.
PMID:41068765	FYPO:0002061	inviable vegetative cell population	The atp3R282C mutant became petite-neg- ative in combination with atp2-R4-3, consistent with a dependence on ­ F1-ATPase activity to rescue ∆Ψ.
PMID:41068765	FYPO:0000668	decreased peptidase activity [assayed_enzyme] proteasome complex	These experiments revealed a consistent and sig- nificant (p < 0.01, Student’s t test) decrease in MG132- sensitive peptidase activity of between 30 and 40% in the mts4L636P mutant extracts, both in rich media (Fig. 2A, Additional file 1) and in EtBr media (Fig. 2B, Additional file 2).
PMID:41068765	FYPO:0000668	decreased peptidase activity [assayed_enzyme] proteasome complex	These experiments revealed a consistent and sig- nificant (p < 0.01, Student’s t test) decrease in MG132- sensitive peptidase activity of between 30 and 40% in the mts4L636P mutant extracts, both in rich media (Fig. 2A, Additional file 1) and in EtBr media (Fig. 2B, Additional file 2).
PMID:41144523	FYPO:0006880	increased protein localization to center of cell division site [assayed_protein] PomBase:SPCC1281.01	As previously reported [58], compared to WT cells, in ync13Δ cells, Ags1 and Bgs4 were more concentrated at cell center during septum maturation (from the end of ring constriction until daughter-cell separation), but Bgs1 was less affected (Fig 4A–4C).
PMID:41144523	FYPO:0006880	increased protein localization to center of cell division site [assayed_protein] PomBase:SPCC1840.02c	As previously reported [58], compared to WT cells, in ync13Δ cells, Ags1 and Bgs4 were more concentrated at cell center during septum maturation (from the end of ring constriction until daughter-cell separation), but Bgs1 was less affected (Fig 4A–4C).
PMID:41144523	FYPO:0003213	explosive cytokinetic cell separation resulting in vegetative cell lysis	Because many more ync13Δ cells lyse when grown in YE5S rich medium than in the EMM5S minimal medium, we observed septum morphology after shifting cells from YE5S with sorbitol to YE5S by electron microscopy.
PMID:41144523	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPCC1840.02c	Bgs4 levels at the division site decreased in sec1-M2 and trs120-ts1 mutants after ring constriction (S6D and S6E Fig).
PMID:41144523	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPCC1840.02c	Bgs4 levels at the division site decreased in sec1-M2 and trs120-ts1 mutants after ring constriction (S6D and S6E Fig).
PMID:41144523	FYPO:0002061	inviable vegetative cell population	C. The rga7Δ ync13-19 mutant could not be tested because it was inviable even at 25°C, which is the permissive temperature for ync13-19 [58].
PMID:41144523	FYPO:0004651	decreased secondary cell septum thickness	Compared to ync13+, the septa in ync13Δ cells were distorted, curved, wavy, uneven, and/or thinner (Fig 7A and 7B),
PMID:41144523	FYPO:0003212	kinked septum	Compared to ync13+, the septa in ync13Δ cells were distorted, curved, wavy, uneven, and/or thinner (Fig 7A and 7B),
PMID:41144523	FYPO:0003203	curved septum	Compared to ync13+, the septa in ync13Δ cells were distorted, curved, wavy, uneven, and/or thinner (Fig 7A and 7B),
PMID:41144523	FYPO:0004478	protein mislocalized to mitochondrion [assayed_protein] PomBase:SPBC30D10.17c	Consistently, Rga7 mistargeted tdTomato-tagged Smi1, which is an adaptor for Bgs4 [13], to mitochondria in cells expressing Tom20-GBP Rga7-mEGFP (Fig 1F).
PMID:41144523	FYPO:0000705	abolished protein-protein interaction [assayed_protein] PomBase:SPAC688.07c [assayed_protein] PomBase:SPAC11E3.02c	Except Rng10-(1-200) (S4D Fig), all other Rga7 and Rng10 truncations, even the Rng10 C-terminal (751-1038) could mistarget Ync13-tdTomato to mitochondria (S4 Fig),
PMID:41144523	FYPO:0004478	protein mislocalized to mitochondrion [assayed_protein] PomBase:SPCC584.05	In addition, Ync13 was still able to mistarget Sec1 to mitochondria without Rng10 (S2G Fig).
PMID:41144523	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPAC6G10.05c	In rga7Δ, rng10Δ, and rga7Δ rng10Δ (shifting from medium with sorbitol to the one without sorbitol) cells, Trs120 intensity at division site decreased significantly, while it increased in ync13Δ cells (Fig 5A and 5B; arrowheads), consistent with the Bgs4 intensity (Fig 4F and 4G).
PMID:41144523	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPAC6G10.05c	In rga7Δ, rng10Δ, and rga7Δ rng10Δ (shifting from medium with sorbitol to the one without sorbitol) cells, Trs120 intensity at division site decreased significantly, while it increased in ync13Δ cells (Fig 5A and 5B; arrowheads), consistent with the Bgs4 intensity (Fig 4F and 4G).
PMID:41144523	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] low	Mild overexpression of Ync13, but not expressing Pmo25-GBP alone, reduced cell lysis of rga7Δ cells from 78% to 51% at 36°C and promoted more growth at both 25 and 36°C (Fig 6A–6D, compare strains 1, 5, and 6).
PMID:41144523	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] low	Mild overexpression of Ync13, but not expressing Pmo25-GBP alone, reduced cell lysis of rga7Δ cells from 78% to 51% at 36°C and promoted more growth at both 25 and 36°C (Fig 6A–6D, compare strains 1, 5, and 6).
PMID:41144523	FYPO:0004478	protein mislocalized to mitochondrion [assayed_protein] PomBase:SPAC6G10.05c	Rga7-mEGFP and Rng10-mEGFP recruited tdTomato-tagged Trs120, which is a TRAPP-II-specific subunit [94,95], but not the exocyst subunit Sec3 [6,42,96], to mitochondria (Figs 1C and S3A). These data suggest that Rga7 and Rng10 selectively interact with the TRAPP-II complex to promote vesicle tethering during exocytosis along the cleavage furrow, rather than the exocyst complex, which is more concentrated at the rim of the division plane [6,42,96].
PMID:41144523	FYPO:0004478	protein mislocalized to mitochondrion [assayed_protein] PomBase:SPAC6G10.05c	Rga7-mEGFP and Rng10-mEGFP recruited tdTomato-tagged Trs120, which is a TRAPP-II-specific subunit [94,95], but not the exocyst subunit Sec3 [6,42,96], to mitochondria (Figs 1C and S3A). These data suggest that Rga7 and Rng10 selectively interact with the TRAPP-II complex to promote vesicle tethering during exocytosis along the cleavage furrow, rather than the exocyst complex, which is more concentrated at the rim of the division plane [6,42,96].
PMID:41144523	FYPO:0004478	protein mislocalized to mitochondrion [assayed_protein] PomBase:SPCC1840.02c	Similarly, mECitrine-Ync13 could mistarget Bgs4 and Ags1 to mitochondria (S3B Fig).
PMID:41144523	FYPO:0004478	protein mislocalized to mitochondrion [assayed_protein] PomBase:SPCC1281.01	Similarly, mECitrine-Ync13 could mistarget Bgs4 and Ags1 to mitochondria (S3B Fig).
PMID:41144523	FYPO:0004478	protein mislocalized to mitochondrion [assayed_protein] PomBase:SPAC11E3.02c	The ectopically targeted Rga7 and Rng10 were both able to recruit Ync13-tdTomato to the mitochondria (Fig 1B and Table 1).
PMID:41144523	GO:0030674	protein-macromolecule adaptor activity [part_of] exocytosis [has_input] PomBase:SPAC11E3.02c [happens_during] mitotic anaphase	The ectopically targeted Rga7 and Rng10 were both able to recruit Ync13-tdTomato to the mitochondria (Fig 1B and Table 1).
PMID:41144523	GO:0030674	protein-macromolecule adaptor activity [part_of] exocytosis [has_input] PomBase:SPAC11E3.02c	The ectopically targeted Rga7 and Rng10 were both able to recruit Ync13-tdTomato to the mitochondria (Fig 1B and Table 1).
PMID:41144523	GO:0006887	exocytosis	The ectopically targeted mECitrine-Ync13 was able to recruit the Sec1/Munc18 (SM) family protein Sec1-tdTomato to the mitochondria (S2B Fig), suggesting Ync13 may function as a priming factor for SNARE complex assembly and/or vesicle tether during exocytosis similar to its animal homologs Munc13/UNC-13 [53–55,88–92]
PMID:41144523	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPCC1840.02c	The time-lapse movies showed that the Bgs4 intensity at division site was significantly reduced in rng10Δ and rng10Δ ync13-19 cells, and Bgs4 did not accumulate in the center of the division plane compared to ync13-19 cells (Fig 4F). Consistently, Bgs4 levels at the division site were significantly lower in rga7Δ, rng10Δ, and rng10Δ rga7Δ cells (Fig 4G).
PMID:41144523	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPCC1840.02c	The time-lapse movies showed that the Bgs4 intensity at division site was significantly reduced in rng10Δ and rng10Δ ync13-19 cells, and Bgs4 did not accumulate in the center of the division plane compared to ync13-19 cells (Fig 4F). Consistently, Bgs4 levels at the division site were significantly lower in rga7Δ, rng10Δ, and rng10Δ rga7Δ cells (Fig 4G).
PMID:41144523	FYPO:0004655	increased protein localization to cell division site [assayed_protein] PomBase:SPBC23G7.08c	The total Rga7 amount at the division site increased in ync13Δ cells under fluorescence microscopy, although Rga7 and Rng10 global protein levels were not obviously affected in ync13Δ cells (slightly increased in 3nmt1-ync13 cells) in Western blotting (Figs 3D, 3E, S6B and S6C).
PMID:41144523	FYPO:0006880	increased protein localization to center of cell division site [assayed_protein] PomBase:SPAC6G10.05c	Trs120 was also more concentrated at the center of the division plane in ync13Δ cells (Fig 5A), confirmed the earlier report [58].
PMID:41144523	GO:0043495	protein-membrane adaptor activity	Trs120 was also more concentrated at the center of the division plane in ync13Δ cells (Fig 5A), confirmed the earlier report [58]. The accumulation of Trs120-3GFP outside of the division site in cells with a nearly closed or closed septa was more frequently detected in the sum projection images of 2-min continuous movies in rga7Δ, rng10Δ, and rga7Δ rng10Δ than in WT cells, suggesting membrane tethering defect at the division site in the mutants (S8A Fig, arrowheads).
PMID:41144523	GO:0030674	protein-macromolecule adaptor activity [has_input] PomBase:SPAC6G10.05c [part_of] vesicle tethering involved in exocytosis [occurs_in] cleavage furrow [happens_during] mitotic anaphase	We next tested if Rga7 or Rng10 can mistarget TRAPP-II vesicle tether and secretory cargos to mitochondria by Tom20-GBP. Both Rga7-mEGFP and Rng10-mEGFP recruited tdTomato-tagged Trs120, which is a TRAPP-II-specific subunit [94,95], but not the exocyst subunit Sec3 [6,42,96], to mitochondria (Figs 1C and S3A). These data suggest that Rga7 and Rng10 selectively interact with the TRAPP-II complex to promote vesicle tethering during exocytosis along the cleavage furrow, rather than the exocyst complex, which is more concentrated at the rim of the division plane [6,42,96].
PMID:41144523	GO:0051285	cell cortex of cell tip	We started with Ync13, Rga7, and Rng10 because they perfectly colocalized on the plasma membrane at cell tips and the division site (Fig 1A)
PMID:41144523	GO:0051285	cell cortex of cell tip	We started with Ync13, Rga7, and Rng10 because they perfectly colocalized on the plasma membrane at cell tips and the division site (Fig 1A)
PMID:41144523	GO:0051285	cell cortex of cell tip	We started with Ync13, Rga7, and Rng10 because they perfectly colocalized on the plasma membrane at cell tips and the division site (Fig 1A)
PMID:41144523	GO:0032153	cell division site	We started with Ync13, Rga7, and Rng10 because they perfectly colocalized on the plasma membrane at cell tips and the division site (Fig 1A)
PMID:41144523	GO:0032153	cell division site	We started with Ync13, Rga7, and Rng10 because they perfectly colocalized on the plasma membrane at cell tips and the division site (Fig 1A)
PMID:41144523	GO:0032153	cell division site	We started with Ync13, Rga7, and Rng10 because they perfectly colocalized on the plasma membrane at cell tips and the division site (Fig 1A)
PMID:41144523	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPAC11E3.02c	Ync13 levels at the division site measured by fluorescence intensity were significantly reduced (>85%) in both rga7Δ and rng10Δ cells (Fig 3A and 3B),
PMID:41144523	FYPO:0002869	decreased protein localization to cell division site [assayed_protein] PomBase:SPAC11E3.02c	Ync13 levels at the division site measured by fluorescence intensity were significantly reduced (>85%) in both rga7Δ and rng10Δ cells (Fig 3A and 3B),
PMID:41144523	FYPO:0002442	normal protein localization to cell division site [assayed_protein] PomBase:SPBC23G7.08c	mutants. Neither Rga7 nor Rng10 localization showed defects in bgs4 temperature-sensitive mutants cwg1-1 and cwg1-2 (S6F and S6G Fig),
PMID:41144523	FYPO:0002442	normal protein localization to cell division site [assayed_protein] PomBase:SPAC688.07c	mutants. Neither Rga7 nor Rng10 localization showed defects in bgs4 temperature-sensitive mutants cwg1-1 and cwg1-2 (S6F and S6G Fig),
PMID:41144523	FYPO:0002442	normal protein localization to cell division site [assayed_protein] PomBase:SPAC688.07c	mutants. Neither Rga7 nor Rng10 localization showed defects in bgs4 temperature-sensitive mutants cwg1-1 and cwg1-2 (S6F and S6G Fig),
PMID:41144523	FYPO:0002442	normal protein localization to cell division site [assayed_protein] PomBase:SPBC23G7.08c	mutants. Neither Rga7 nor Rng10 localization showed defects in bgs4 temperature-sensitive mutants cwg1-1 and cwg1-2 (S6F and S6G Fig),
PMID:41144523	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] high	rga7Δ cells had severe lysis and negligible growth on plates with Phloxine B (a red dye accumulated in lysed or unhealthy cells because they cannot pump it out) at both 25 and 36°C (Fig 6A–6D).
PMID:41144523	FYPO:0003440	cell lysis during cytokinesis [has_penetrance] high	rga7Δ cells had severe lysis and negligible growth on plates with Phloxine B (a red dye accumulated in lysed or unhealthy cells because they cannot pump it out) at both 25 and 36°C (Fig 6A–6D).
PMID:41154583	FYPO:0000245	loss of viability in stationary phase [has_severity] low	CAP-treated cells of all three strains, on the other hand, showed markedly reduced viability at later times of culturing (36 h and 48 h), with ∆rst2 showing slightly higher viability and ∆scr1 slightly lower viability compared to wild-type cells (Figure 4b).
PMID:41154583	FYPO:0001309	increased viability in stationary phase [has_severity] low	CAP-treated cells of all three strains, on the other hand, showed markedly reduced viability at later times of culturing (36 h and 48 h), with ∆rst2 showing slightly higher viability and ∆scr1 slightly lower viability compared to wild-type cells (Figure 4b).
PMID:41154583	FYPO:0001310	normal viability in stationary phase	In untreated cells, deletion of either rst2 or scr1 did not significantly affect cell viability at any time points compared to wild type (Figure 4b).
PMID:41154583	FYPO:0001310	normal viability in stationary phase	In untreated cells, deletion of either rst2 or scr1 did not significantly affect cell viability at any time points compared to wild type (Figure 4b).
PMID:41154583	FYPO:0000637	increased cell population growth rate on glucose carbon source [has_severity] low	With CAP treatment, all three strains exhibited reduced overall growth patterns, but with the same relative differences of increased growth patterns in ∆rst2 and decreased growth patterns in ∆scr1 compared to wild-type cells (Figure 4a).
PMID:41154583	FYPO:0000637	increased cell population growth rate on glucose carbon source [has_severity] low	Without CAP treatment, ∆rst2 cells showed a slightly faster growth rate, shorter lag phase, and higher final cell mass compared to wild-type cells, (Figure 4a)
PMID:41154583	FYPO:0001407	decreased cell population growth on glucose carbon source [has_severity] low	e ∆scr1 cells showed a slower growth rate, prolonged lag phase, and lower final cell mass (Figure 4a)
PMID:41171630	FYPO:0003213	explosive cytokinetic cell separation resulting in vegetative cell lysis	(Table 2)
PMID:41171630	FYPO:0003213	explosive cytokinetic cell separation resulting in vegetative cell lysis	(Table 2)
PMID:41171630	FYPO:0003213	explosive cytokinetic cell separation resulting in vegetative cell lysis	(Table 2)
PMID:41171630	FYPO:0001370	abnormal protein localization [assayed_protein] PomBase:SPAC4F10.11	At the restrictive temperature, although Spn1 localized as a ring at the division site before septation, a fraction of Spn1 abnormally spread onto the division plane following furrow ingression in sec3-913 and sec8-1 mutants (Figure 1F, red boxes; and Figure 1—figure supplement 1B, middle focal plane).
PMID:41171630	FYPO:0001370	abnormal protein localization [assayed_protein] PomBase:SPAC4F10.11	At the restrictive temperature, although Spn1 localized as a ring at the division site before septation, a fraction of Spn1 abnormally spread onto the division plane following furrow ingression in sec3-913 and sec8-1 mutants (Figure 1F, red boxes; and Figure 1—figure supplement 1B, middle focal plane).
PMID:41171630	FYPO:0006880	increased protein localization to center of cell division site [assayed_protein] PomBase:SPCC622.10c	Both Sec15 and Sec5 spread more or less to the whole division plane in ~50% of spn2Δ cells with obvious septa (Figure 5A–D). Unlike in spn1Δ or spn4Δ cells, a fraction of Sec15 and Sec5 still localized to the rim in spn2Δ cells with a septum (Figure 5A, C).
PMID:41171630	FYPO:0006880	increased protein localization to center of cell division site [assayed_protein] PomBase:SPCC1183.01	Both Sec15 and Sec5 spread more or less to the whole division plane in ~50% of spn2Δ cells with obvious septa (Figure 5A–D). Unlike in spn1Δ or spn4Δ cells, a fraction of Sec15 and Sec5 still localized to the rim in spn2Δ cells with a septum (Figure 5A, C).
PMID:41171630	FYPO:0006880	increased protein localization to center of cell division site [assayed_protein] PomBase:SPAC6G9.11	Consistently, secretory vesicle markers Rab11 GTPase Ypt3 and vSNARE Syb1 accumulated more in the center of the division plane but diminished from the rim in spn1Δ cells (Figure 6C, D).
PMID:41171630	FYPO:0006880	increased protein localization to center of cell division site [assayed_protein] PomBase:SPAC18G6.03	Consistently, secretory vesicle markers Rab11 GTPase Ypt3 and vSNARE Syb1 accumulated more in the center of the division plane but diminished from the rim in spn1Δ cells (Figure 6C, D).
PMID:41171630	FYPO:0006880	increased protein localization to center of cell division site [assayed_protein] PomBase:SPCC970.09	During and after septum formation, the levels of all three exocyst components were significantly reduced at the division site (except Exo70 in cells with forming septum) and almost absent at the rim in spn1Δ cells (Figure 2A, B; Figure 2—figure supplement 1A–C). These results were confirmed in cells expressed Sec8-GFP and myosin light chain Rlc1 as a contractile ring marker (Figure 2D, E).
PMID:41171630	FYPO:0006880	increased protein localization to center of cell division site [assayed_protein] PomBase:SPAC17G8.12	During septation, however, the exocyst spread across the division plane as a disk in spn1Δ cells while it remained at the rim in WT cells (Figure 2A, Figure 2—figure supplement 1A, B, red boxes).
PMID:41171630	FYPO:0002088	exocytic vesicles present in increased numbers at septum during septum assembly [has_severity] low	During septum formation, seven- and twofold more secretory vesicles accumulated at the division site in sec8-1 and spn1Δ cells, respectively, compared to WT (Figure 6A, B
PMID:41171630	FYPO:0002088	exocytic vesicles present in increased numbers at septum during septum assembly [has_severity] high	During septum formation, seven- and twofold more secretory vesicles accumulated at the division site in sec8-1 and spn1Δ cells, respectively, compared to WT (Figure 6A, B
PMID:41171630	GO:0051285	cell cortex of cell tip	Sec3 and Exo70, but not Spn1, also concentrated at cell tips (Figure 1C, D).
PMID:41171630	GO:0051285	cell cortex of cell tip	Sec3 and Exo70, but not Spn1, also concentrated at cell tips (Figure 1C, D).
PMID:41171630	GO:0032153	cell division site	Spn1 and Sec3 colocalized at the division site as a single ring first, and later as double rings during septum formation (Figure 1A, B).
PMID:41171630	GO:0032153	cell division site	Spn1 and Sec3 colocalized at the division site as a single ring first, and later as double rings during septum formation (Figure 1A, B).
PMID:41171630	FYPO:0006880	increased protein localization to center of cell division site [assayed_protein] PomBase:SPCC1183.01	the deletion of spn1 or spn4 led to mislocalization of Sec15 on the division plane in ~75% of cells with a septum while Sec15 in ~90% of WT cells
PMID:41171630	FYPO:0006880	increased protein localization to center of cell division site [assayed_protein] PomBase:SPCC1183.01	the deletion of spn1 or spn4 led to mislocalization of Sec15 on the division plane in ~75% of cells with a septum while Sec15 in ~90% of WT cells
PMID:41184513	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC1687.22c [part_of] negative regulation of nuclear-transcribed mRNA poly(A) tail shortening	Increased phosphorylation of Puf3 does not affect RNA-binding capacity but reduces the ability of Puf3 to stimu- late Ccr4–Not deadenylase activity (Fig. 4f and Extended Data Fig. 8). This reduction occurs in a graded manner where more phosphorylation results in slower deadenylation rates.
PMID:41184513	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening [has_severity] high	Individual substitutions of hydrophobic residues, either alone or in combination, also resulted in modest changes in the ability of Puf3 to stimulate Ccr4–Not (Extended Data Fig. 3b–d).
PMID:41184513	FYPO:0006809	decreased nuclear-transcribed mRNA poly(A) tail shortening	Individual substitutions of hydrophobic residues, either alone or in combination, also resulted in modest changes in the ability of Puf3 to stimulate Ccr4–Not (Extended Data Fig. 3b–d).
PMID:41184513	FYPO:0003822	decreased ribonuclease activity [assayed_enzyme] CCR4-NOT complex	N-terminal and C-terminal truncations of the N-terminal IDR in Puf3 lead to progressive decreases in activity and the first 258 residues of the IDR are necessary for efficient stimulation of deadenylation (Fig. 1b).
PMID:41184513	FYPO:0003822	decreased ribonuclease activity [assayed_enzyme] CCR4-NOT complex	N-terminal and C-terminal truncations of the N-terminal IDR in Puf3 lead to progressive decreases in activity and the first 258 residues of the IDR are necessary for efficient stimulation of deadenylation (Fig. 1b).
PMID:41184513	GO:0170054	ribonuclease activator activity	Not. Puf3 promotes targeted deadenylation in a reconstituted in vitro assay with Ccr4–Not and stimulates deadenyla- tion ~50-fold17 (Fig. 1a,b and Extended Data Fig. 1b–d).
PMID:41184513	FYPO:0003591	abnormal protein complex binding [assayed_enzyme] CCR4-NOT complex [has_severity] high [assayed_protein] PomBase:SPAC1687.22c	Notably, a construct spanning amino acids 109–258 shows higher fractional binding than 109–208 or 158–258. Overall, these data support a model where extensive regions of the Puf3-IDR contribute to the interaction with Ccr4–Not.
PMID:41184513	FYPO:0003591	abnormal protein complex binding [assayed_enzyme] CCR4-NOT complex [has_severity] medium [assayed_protein] PomBase:SPAC1687.22c	Notably, a construct spanning amino acids 109–258 shows higher fractional binding than 109–208 or 158–258. Overall, these data support a model where extensive regions of the Puf3-IDR contribute to the interaction with Ccr4–Not.
PMID:41184513	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC1687.22c [part_of] negative regulation of nuclear-transcribed mRNA poly(A) tail shortening	Time-resolved NMR experiments with Puf3-IDR1–258 (Extended Data Fig. 7c) and intact MS (Fig. 4b,c) with Puf3-IDR1–376 showed that Puf3 is sequentially phosphorylated by Sck1 and Pdk1 kinases.
PMID:41184513	FYPO:0003822	decreased ribonuclease activity [assayed_enzyme] CCR4-NOT complex [has_severity] high	To test the interaction between Puf3 and Not9, we designed substitu- tions of surface residues that would disrupt the conserved interac- tion sites (Extended Data Fig. 5e), incorporated them into Ccr4–Not and assayed the ability of Puf3 to stimulate deadenylation activity. Mutations impacting the Not9-binding sites reduced the ability of Ccr4–Not to accelerate deadenylation (~1.5–2-fold reduction) (Fig. 3d and Extended Data Fig. 6).
PMID:41184513	FYPO:0003822	decreased ribonuclease activity [assayed_enzyme] CCR4-NOT complex [has_severity] low	To test the interaction between Puf3 and Not9, we designed substitu- tions of surface residues that would disrupt the conserved interac- tion sites (Extended Data Fig. 5e), incorporated them into Ccr4–Not and assayed the ability of Puf3 to stimulate deadenylation activity. Mutations impacting the Not9-binding sites reduced the ability of Ccr4–Not to accelerate deadenylation (~1.5–2-fold reduction) (Fig. 3d and Extended Data Fig. 6).
PMID:41184513	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC1B9.02c	We assigned five peaks with comparable signal intensities to the remainder of the spectrum as phosphoserine (pS42, pS156, pS207, pS226 and pS241) (Extended Data Fig. 7b).
PMID:41184513	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC1B9.02c	We assigned five peaks with comparable signal intensities to the remainder of the spectrum as phosphoserine (pS42, pS156, pS207, pS226 and pS241) (Extended Data Fig. 7b).
PMID:41184513	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC1B9.02c	We assigned five peaks with comparable signal intensities to the remainder of the spectrum as phosphoserine (pS42, pS156, pS207, pS226 and pS241) (Extended Data Fig. 7b).
PMID:41184513	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC1B9.02c	We assigned five peaks with comparable signal intensities to the remainder of the spectrum as phosphoserine (pS42, pS156, pS207, pS226 and pS241) (Extended Data Fig. 7b).
PMID:41184513	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPAC1B9.02c	We assigned five peaks with comparable signal intensities to the remainder of the spectrum as phosphoserine (pS42, pS156, pS207, pS226 and pS241) (Extended Data Fig. 7b).
PMID:41201383	FYPO:0002907	circularized chromosome during mitotic G1 phase	Accordingly, chromosome end fusions occur in rap1∆ cells arrested in G1 phase under ni- trogen starvation (Figure 6).
PMID:41201383	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores	Consistently, the rap1∆ mutant frequently formed abnormal numbers (one to three) of spores, whereas al- most all wild-­ type and poz1∆ strains produced four spores under nitrogen starvation (Figure 7A,B).
PMID:41201383	FYPO:0000590	normal sporulation	Elimination of all introns from rap1+ or poz1+ had no impact on spore formation; these strains produced spores normally, as did wild-­ type cells (Figure 7C).
PMID:41201383	FYPO:0000121	abnormal sporulation	Elimination of all introns from rap1+ or poz1+ had no impact on spore formation; these strains produced spores normally, as did wild-­ type cells (Figure 7C).
PMID:41201383	FYPO:0000590	normal sporulation	Elimination of all introns from rap1+ or poz1+ had no impact on spore formation; these strains produced spores normally, as did wild-­ type cells (Figure 7C).
PMID:41201383	FYPO:0000121	abnormal sporulation [has_severity] high	In contrast, the tls1∆cay1∆ double mutant displayed severe sporulation defects similar to those of rap1∆ cells (Figure 7A,B).
PMID:41201383	FYPO:0000121	abnormal sporulation [has_severity] medium	In contrast, tls1∆cay1∆ cells expressing intron-­ less poz1+ showed severe sporulation defects, whereas tls1∆cay1∆ cells expressing intron-less rap1+ exhibited only moderate defects, less severe than those in tls1∆cay1∆ cells with intact rap1+ introns (Figure 7C).
PMID:41201383	FYPO:0000121	abnormal sporulation [has_severity] high	In contrast, tls1∆cay1∆ cells expressing intron-­ less poz1+ showed severe sporulation defects, whereas tls1∆cay1∆ cells expressing intron-less rap1+ exhibited only moderate defects, less severe than those in tls1∆cay1∆ cells with intact rap1+ introns (Figure 7C).
PMID:41201383	FYPO:0002687	normal telomere length during vegetative growth	In contrast, tls1∆cay1∆ cells lacking introns in both rap1+ and poz1+ ex- hibited telomere lengths comparable to those in wild-­ type cells (Figure 5B),
PMID:41201383	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC1778.02	Notably, the pro- tein levels of Rap1 and Poz1 were markedly reduced in tls1∆ cells, as previously reported (Anil et al. 2022; Lorenzi et al. 2015; Wang et al. 2014). In contrast, those of Taz1, Pot1, Tpz1, Ccq1, Rif1, and Sgo2 (a shugoshin family protein, used here as a negative control) remained unchanged (Figure 2, lanes 1 and 2).
PMID:41201383	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC19G12.13c	Notably, the pro- tein levels of Rap1 and Poz1 were markedly reduced in tls1∆ cells, as previously reported (Anil et al. 2022; Lorenzi et al. 2015; Wang et al. 2014). In contrast, those of Taz1, Pot1, Tpz1, Ccq1, Rif1, and Sgo2 (a shugoshin family protein, used here as a negative control) remained unchanged (Figure 2, lanes 1 and 2).
PMID:41201383	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPBC1778.02	Notably, the protein levels of Rap1 and Poz1 were reduced in cay1∆ cells to a greater extent than those in tls1∆ cells, whereas those of Taz1, Pot1, Tpz1, Ccq1, Rif1, and Sgo2 remained un- changed (Figure 2, lane 3).
PMID:41201383	FYPO:0001324	decreased protein level during vegetative growth [assayed_protein] PomBase:SPAC19G12.13c	Notably, the protein levels of Rap1 and Poz1 were reduced in cay1∆ cells to a greater extent than those in tls1∆ cells, whereas those of Taz1, Pot1, Tpz1, Ccq1, Rif1, and Sgo2 remained un- changed (Figure 2, lane 3).
PMID:41201383	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] high	The cay1∆ mutant exhibited substantially longer telomeres than the tls1∆ mutant, and the tls1∆cay1∆ double mutant showed even greater telomere elongation than cay1∆ alone (Figure 5A).
PMID:41201383	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC1778.02	The intron-­ less rap1+ and poz1+ constructs produced Rap1 and Poz1 proteins at levels comparable to those observed in wild-­ type cells, and deletion of tls1+, cay1+, or both no longer resulted in a reduction of Rap1 or Poz1 protein levels (Figure 3A,B).
PMID:41201383	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPBC1778.02	The intron-­ less rap1+ and poz1+ constructs produced Rap1 and Poz1 proteins at levels comparable to those observed in wild-­ type cells, and deletion of tls1+, cay1+, or both no longer resulted in a reduction of Rap1 or Poz1 protein levels (Figure 3A,B).
PMID:41201383	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC19G12.13c	The intron-­ less rap1+ and poz1+ constructs produced Rap1 and Poz1 proteins at levels comparable to those observed in wild-­ type cells, and deletion of tls1+, cay1+, or both no longer resulted in a reduction of Rap1 or Poz1 protein levels (Figure 3A,B).
PMID:41201383	FYPO:0000833	normal protein level during vegetative growth [assayed_protein] PomBase:SPAC19G12.13c	The intron-­ less rap1+ and poz1+ constructs produced Rap1 and Poz1 proteins at levels comparable to those observed in wild-­ type cells, and deletion of tls1+, cay1+, or both no longer resulted in a reduction of Rap1 or Poz1 protein levels (Figure 3A,B).
PMID:41201383	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] medium	The resulting tls1∆ strain exhibited moderately elongated telomere DNA (~400 bp) compared with the wild type (~300 bp) (Figure 1B),
PMID:41201383	FYPO:0000590	normal sporulation	The tls1∆ and cay1∆ single mutants showed only mild sporula- tion defects
PMID:41201383	FYPO:0000590	normal sporulation	The tls1∆ and cay1∆ single mutants showed only mild sporula- tion defects
PMID:41227381	FYPO:0002989	increased level of transmembrane transport gene mRNA during vegetative growth	3.2. The Protein-Coding Genes Affected by cwf14 Mutation Are Often Involved in Transport Processes, Encode Enzymes, and Rarely Contain Introns To find out what molecular processes lie behind the observed phenotypic changes, we selected the protein-coding genes (log2 value +/−1.5) affected by cwf14 mutation from the genes identified by Kallgren [17] and determined the GO categories to which they belong (Table S4) (PomBase database) [30]. Unexpectedly, most genes were upregulated (106 out of 117 genes; 90%), and many of them encoded proteins with oxidoreductase, transferase, hydrolase, and transporter activity (Tables S4 and 1). The genes involved in transport processes were also supported by GO enrich- ment analysis, which primarily highlighted genes related to urea (GO:0015840) (Num- Cells 2025, 14, 1736 10 of 23 ber of genes/pathway genes: 3/3) and putrescine transport (GO:0015847) (Number of genes/pathway genes: 3/3).
PMID:41227381	FYPO:0001492	viable elongated vegetative cell [has_severity] high	Figure 1. Phenotype of the mutant strain (cwf14−). Morphology: The mutant strain produced elongated cells at 37◦C (YEA) (2-1480) (a)
PMID:41227381	FYPO:0009007	decreased vegetative cell population viability	In a long-term survival assay, four-week-old cwf14 mutant cells showed reduced colony-forming ability (57%) compared to the wild-type strain (99%), indicating a decrease in viability of mutant cells.
PMID:41227381	FYPO:0000960	normal growth on ethanol	Our results revealed that the presence of S. pombe tor1, tor2, and fhl1 genes improved the growth on ethanol-containing medium in the mutant (cwf14 disrupted) cells, compared to the control cells (transformed with empty pREP81, or pREP3X vectors) (Figure 3a).
PMID:41227381	FYPO:0000960	normal growth on ethanol	Our results revealed that the presence of S. pombe tor1, tor2, and fhl1 genes improved the growth on ethanol-containing medium in the mutant (cwf14 disrupted) cells, compared to the control cells (transformed with empty pREP81, or pREP3X vectors) (Figure 3a).
PMID:41227381	FYPO:0000960	normal growth on ethanol	Our results revealed that the presence of S. pombe tor1, tor2, and fhl1 genes improved the growth on ethanol-containing medium in the mutant (cwf14 disrupted) cells, compared to the control cells (transformed with empty pREP81, or pREP3X vectors) (Figure 3a).
PMID:41227381	FYPO:0000960	normal growth on ethanol	Our results revealed that the presence of S. pombe tor1, tor2, and fhl1 genes improved the growth on ethanol-containing medium in the mutant (cwf14 disrupted) cells, compared to the control cells (transformed with empty pREP81, or pREP3X vectors) (Figure 3a).
PMID:41227381	FYPO:0000960	normal growth on ethanol	Our results revealed that the presence of S. pombe tor1, tor2, and fhl1 genes improved the growth on ethanol-containing medium in the mutant (cwf14 disrupted) cells, compared to the control cells (transformed with empty pREP81, or pREP3X vectors) (Figure 3a).
PMID:41227381	FYPO:0000960	normal growth on ethanol	Our results revealed that the presence of S. pombe tor1, tor2, and fhl1 genes improved the growth on ethanol-containing medium in the mutant (cwf14 disrupted) cells, compared to the control cells (transformed with empty pREP81, or pREP3X vectors) (Figure 3a).
PMID:41227381	FYPO:0003031	mating without nitrogen starvation	Similarly, the sporulation of the cwf14 deleted h90 strain (2-1532) was also altered, and cells showed an increased tendency to sporulate. That is, the mutant cells conjugated and produced asci both on nutrient-rich (YEA) and minimal (EMMA-nitrogen) media after only 1 day, in contrast to the wild-type h90 strain, which at that time contained only vegetative cells (Figure S2).
PMID:41227381	FYPO:0000097	sensitive to caffeine during vegetative growth	Stress response assays also demonstrated that the cwf14− mutant strains (2-1532, 2-1480) are sensitive to rapamycin, ethanol, and caffeine (Figure 1h–j), confirming previous results [60,61]
PMID:41227381	FYPO:0000111	sensitive to rapamycin	Stress response assays also demonstrated that the cwf14− mutant strains (2-1532, 2-1480) are sensitive to rapamycin, ethanol, and caffeine (Figure 1h–j), confirming previous results [60,61]
PMID:41227381	FYPO:0000842	sensitive to ethanol during vegetative growth	Stress response assays also demonstrated that the cwf14− mutant strains (2-1532, 2-1480) are sensitive to rapamycin, ethanol, and caffeine (Figure 1h–j), confirming previous results [60,61]
PMID:41227381	FYPO:0001355	decreased vegetative cell population growth	The growth of cells (cwf14−: 2-1542; WT: 0-3) was tested at 30◦C (d) and 25◦C (SMA) (e), showing slower growth of mutant cells.
PMID:41227381	FYPO:0001122	elongated vegetative cell	The size of the cells was also measured at 30◦C (SMA) and was found to be significantly longer in the mutant than in the wild-type strain (f).
PMID:41227381	FYPO:0000134	branched, elongated, multiseptate cell [has_severity] high	and multiseptated morphology on caffeine-containing medium (YEA + 10 mM caffeine, 37◦C) (2-1480) (b),
PMID:41236477	FYPO:0004964	actin cortical patches present in decreased numbers	Phalloidin staining in the wt background visually revealed a decrease in the area occupied by actin patches in the REEact1 strain as opposed to the MEEEact1 strain (Fig. 4 D). To analyze patches in greater detail, we generated fimbrin-GFP strains that mark patches but not cables or rings. The patches were counted manually in 3D. This analysis showed that the number of patches in the REEact1 strain is less than that in the MEEEact1 strain per cell (Fig. 4 E (i)).
PMID:41236477	FYPO:0001365	decreased rate of actomyosin contractile ring contraction	The ring constriction took longer in the REEact1 strain, reflecting the reduced average rate of constriction (ring diameter divided by the time for constriction). Overall, the total time taken for cytokinesis from node appearance to the end of CAR constriction was increased in the REEact1 strain. (Fig. 5A, 5B)
PMID:41236477	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] low [has_penetrance] 80	There was no obvious difference in the viability of REEact1 and MEEEact1 strains in spot assays (Fig. 4 A). To test if there were any size differences between the strains, we analyzed septated cells. The REEact1 cells were shorter and wider with lower volumes and surface area (Fig. 4 C).
PMID:41236477	FYPO:0002151	inviable spore	We were unable to find any viable colony that contained both REEact1 and myo2-E1, although all other combinations were observed (Fig. 5 C).
PMID:41236477	FYPO:0002151	inviable spore	We were unable to find any viable colony that contained both REEact1 and myo2-E1, although all other combinations were observed (Fig. 5 C).
PMID:41258116	GO:0030874	nucleolar chromatin [exists_during] single-celled organism vegetative growth phase	(Fig. 4A)
PMID:41258116	FYPO:0001309	increased viability in stationary phase [has_severity] low	(Fig. 5f)
PMID:41258116	FYPO:0006074	increased histone H3-K9 dimethylation at rDNA during vegetative growth [has_severity] medium	(Fig. S5)
PMID:41258116	FYPO:0003601	decreased rRNA precursor level	Additionally, the abundance of ITS2-containing precursor rRNA was also decreased. (Fig. 1E)
PMID:41258116	FYPO:0003601	decreased rRNA precursor level	Additionally, the abundance of ITS2-containing precursor rRNA was also decreased. (Fig. 1E)
PMID:41258116	FYPO:0003601	decreased rRNA precursor level	Additionally, the abundance of ITS2-containing precursor rRNA was also decreased. (Fig. 1E)
PMID:41258116	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPCC24B10.07	Additionally, the enrichment of Gad8-FLAG in the rDNA region was reduced in the tor1Δ mutant despite total Gad8-FLAG protein levels remaining unchanged, indicating that TORC2 is required for Gad8 locali- zation in the rDNA region (Fig. 3c, d)
PMID:41258116	FYPO:0004032	increased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPAC664.01c	Furthermore, ChIP-qPCR revealed that rDNA fragments were more frequently immunoprecipitated with GFP-Swi6 in the tor1Δ mutant than in the wild-type (Fig. 2h).
PMID:41258116	FYPO:0003601	decreased rRNA precursor level	Furthermore, rRNA levels in the leo1Δ mutant were reduced relative to those in the wild- type (Fig. 4e).
PMID:41258116	FYPO:0006470	decreased mature rRNA level	Furthermore, rRNA levels in the leo1Δ mutant were reduced relative to those in the wild- type (Fig. 4e).
PMID:41258116	FYPO:0010028	abolished histone H3-K9 dimethylation at rDNA during vegetative growth	In the clr4Δ single mutant, H3K9 methylation in the rDNA region was completely abolished in nutrient-rich conditions, yet viability over time was comparable to that of the wild-type (Supplementary Fig. 5c, d).
PMID:41258116	FYPO:0001310	normal viability in stationary phase	In the clr4Δ single mutant, H3K9 methylation in the rDNA region was completely abolished in nutrient-rich conditions, yet viability over time was comparable to that of the wild-type (Supplementary Fig. 5c, d).
PMID:41258116	FYPO:0004009	decreased rRNA transcription	In the tor1Δ mutant, the amount of nascent rRNA was substantially lower than that in the wild-type (Fig. 1f).
PMID:41258116	FYPO:0001309	increased viability in stationary phase [has_severity] high	Intriguingly, culturing the tor1Δ mutant in the presence of rapa- mycin led to a further but moderate improvement in the maintenance of viability in quiescence (Fig. 5e).
PMID:41258116	GO:0030874	nucleolar chromatin [exists_during] single-celled organism vegetative growth phase	Like Tor1-FLAG, Gad8-FLAG was enriched across the entire rDNA region, particularly in the 18S, 5.8S, and 28S regions. (Fig. 3A)
PMID:41258116	FYPO:0006074	increased histone H3-K9 dimethylation at rDNA during vegetative growth [has_severity] high	Notably, the tor1Δ tor2-287 double mutant exhibited the greatest increase in H3K9 methylation and the most pro- nounced reduction in rRNA levels among all strains tested, surpassing the effects observed in either single mutant (Supplementary Fig. 5a, b).
PMID:41258116	FYPO:0006074	increased histone H3-K9 dimethylation at rDNA during vegetative growth [has_severity] high	Notably, the tor1Δ tor2-287 double mutant exhibited the greatest increase in H3K9 methylation and the most pro- nounced reduction in rRNA levels among all strains tested, surpassing the effects observed in either single mutant (Supplementary Fig. 5a, b).
PMID:41258116	GO:0061188	negative regulation of rDNA heterochromatin formation	Our findings uncover a pathway by which TORC2 inactivation induces heterochromatin formation at rDNA loci and represses rRNA transcription independently of TORC1 signaling. Mechanistically, the dissociation of Gad8, recruited to rDNA by TORC2, facilitates the release of the Paf1 complex, a key regulator of histone turnover44,45. This, in turn, promotes the accumulation of H3K9 methylation mediated by the RNAi-dependent pathway, thereby driving heterochromatin assembly.
PMID:41258116	FYPO:0006077	increased histone H3-K9 methylation at rDNA during vegetative growth	Our results showed that H3K9me2 and H3K9me3 levels were elevated across the entire rDNA region in the tor1Δ mutant (Fig. 2a, b).
PMID:41258116	FYPO:0006470	decreased mature rRNA level	The partial inactivation of the tor2-287 single mutant exhibited little or no increase in H3K9 methylation but exhibited reduced rRNA levels in the glucose-rich conditions. (Fig. S5)
PMID:41258116	FYPO:0010029	normal histone H3-K9 dimethylation at rDNA during vegetative growth	The partial inactivation of the tor2-287 single mutant exhibited little or no increase in H3K9 methylation. (Fig. S5)
PMID:41258116	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] PomBase:SPBC29B5.01	The results revealed that the localization of Atf1 and Gcn5-HA in the rDNA remained largely unchanged among the wild-type, tor1Δ, and gad8Δ mutant strains (Supplementary Fig. 4).
PMID:41258116	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] PomBase:SPBC29B5.01	The results revealed that the localization of Atf1 and Gcn5-HA in the rDNA remained largely unchanged among the wild-type, tor1Δ, and gad8Δ mutant strains (Supplementary Fig. 4).
PMID:41258116	FYPO:0002625	normal protein localization to chromatin rDNA [assayed_protein] PomBase:SPAC1952.05	The results revealed that the localization of Atf1 and Gcn5-HA in the rDNA remained largely unchanged among the wild-type, tor1Δ, and gad8Δ mutant strains (Supplementary Fig. 4).
PMID:41258116	FYPO:0006494	decreased rDNA copy number during vegetative growth [has_severity] low	The tor1Δ mutant exhibited an approximately 20% reduction in rDNA copy number compared to the wild-type (Supplemen- tary Fig. 2).
PMID:41258116	GO:0061188	negative regulation of rDNA heterochromatin formation	This study demonstrates that TORC2, acting independently of TORC1, contributes to the control of ribosome biogenesis by regulating rRNA transcription through heterochromatin formation in the rDNA region.
PMID:41258116	GO:0030874	nucleolar chromatin [exists_during] single-celled organism vegetative growth phase	Tor1-FLAG was broadly enri- ched across the rDNA unit, spanning the 18S, 5.8S, 28S, and 3’ETS (Fig. 1b).
PMID:41258116	FYPO:0006077	increased histone H3-K9 methylation at rDNA during vegetative growth	We found a significant increase in H3K9me2 and H3K9me3 levels in the 18S, 5.8S, and 28S rDNA regions in the leo1Δ mutant compared to the wild-type (Fig. 4c, d).
PMID:41258116	FYPO:0001309	increased viability in stationary phase [has_severity] medium	We found that the tor1Δ mutant exhibited prolonged maintenance of viability during quiescence compared to the wild-type, although the overall effect was moderate (Fig. 5e).
PMID:41258116	FYPO:0006077	increased histone H3-K9 methylation at rDNA during vegetative growth [has_severity] high	rapamycin treatment of tor1Δ cells induced much denser heterochromatin in the rDNA region and further suppressed rRNA tran- scription than in rapamycin-untreated tor1Δ cells (Fig. 5a–c).
PMID:41258116	FYPO:0004009	decreased rRNA transcription [has_severity] high	rapamycin treatment of tor1Δ cells induced much denser heterochromatin in the rDNA region and further suppressed rRNA tran- scription than in rapamycin-untreated tor1Δ cells (Fig. 5a–c).
PMID:41258116	FYPO:0002391	decreased protein localization to chromatin at rDNA [assayed_protein] PomBase:SPBC13E7.08c	the accumulation of Leo1-FLAG in rDNA was reduced in the gad8Δ mutant (Fig. 4b).
PMID:41258116	FYPO:0006470	decreased mature rRNA level	the gad8Δ mutant exhibited increased H3K9me2/me3 levels in the rDNA and decreased rRNA transcription (Fig. 3e–g).
PMID:41258116	FYPO:0006077	increased histone H3-K9 methylation at rDNA during vegetative growth	the gad8Δ mutant exhibited increased H3K9me2/me3 levels in the rDNA and decreased rRNA transcription (Fig. 3e–g).
PMID:41258116	FYPO:0003601	decreased rRNA precursor level	the gad8Δ mutant exhibited increased H3K9me2/me3 levels in the rDNA and decreased rRNA transcription (Fig. 3e–g).
PMID:41258116	FYPO:0006470	decreased mature rRNA level	the tor1Δ tor2-287 double mutant exhibited the greatest increase in H3K9 methylation and the most pro- nounced reduction in rRNA levels among all strains tested, surpassing the effects observed in either single mutant (Supplementary Fig. 5a, b).
PMID:41258116	FYPO:0001309	increased viability in stationary phase [has_severity] low	the viability extension observed in the tor1Δ mutant treated with rapamycin was largely diminished in the tor1Δ clr4Δ double mutant (Fig. 5f).
PMID:41258116	FYPO:0001309	increased viability in stationary phase [has_severity] low	the viability extension observed in the tor1Δ mutant treated with rapamycin was largely diminished in the tor1Δ clr4Δ double mutant (Fig. 5f).
PMID:41258116	FYPO:0006470	decreased mature rRNA level	we performed RT-qPCR to assess rRNA abundance in mutants lacking each TORC2 component, including Tor1, Wat1/Lst8, Sin1, and Ste20/Rictor29,35,36 (Fig. 1d). Our analysis revealed that 18S, 5.8S, and 28S rRNA levels were reduced in all these mutants. (Fig. 1E)
PMID:41258116	FYPO:0006470	decreased mature rRNA level	we performed RT-qPCR to assess rRNA abundance in mutants lacking each TORC2 component, including Tor1, Wat1/Lst8, Sin1, and Ste20/Rictor29,35,36 (Fig. 1d). Our analysis revealed that 18S, 5.8S, and 28S rRNA levels were reduced in all these mutants. (Fig. 1E)
PMID:41258116	FYPO:0006470	decreased mature rRNA level	we performed RT-qPCR to assess rRNA abundance in mutants lacking each TORC2 component, including Tor1, Wat1/Lst8, Sin1, and Ste20/Rictor29,35,36 (Fig. 1d). Our analysis revealed that 18S, 5.8S, and 28S rRNA levels were reduced in all these mutants. (Fig. 1E)
PMID:41259369	FYPO:0010034	abolished nuclear pore clustering during cellular response to hydroxyurea [has_penetrance] 100	(Fig. 6A, 6B)
PMID:41259369	FYPO:0010034	abolished nuclear pore clustering during cellular response to hydroxyurea [has_penetrance] 100	(Fig. 6A, 6B)
PMID:41259369	FYPO:0008139	dilated endoplasmic reticulum lumen	(Fig. S1E)
PMID:41259369	FYPO:0010034	abolished nuclear pore clustering during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC1786.03 [has_penetrance] 50	(Fig. S2H) Percentage of cells with N-Cap phenotype goes from 60% in WT to 10% in lem2D and vps4D.
PMID:41259369	FYPO:0010034	abolished nuclear pore clustering during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC1786.03 [has_penetrance] 50	(Fig. S2H) Percentage of cells with N-Cap phenotype goes from 60% in WT to 10% in lem2D and vps4D.
PMID:41259369	FYPO:0010035	normal nuclear pore clustering during cellular response to hydroxyurea	(Fig. S6B)
PMID:41259369	FYPO:0000805	abnormal endoplasmic reticulum organization [has_penetrance] 25	As expected, the addition of HU to cells deleted for lem2, cmp7 or vps4 resulted in perinuclear ER fragmentation (S2G, S2H Fig; for results, see S1 Data).
PMID:41259369	FYPO:0000805	abnormal endoplasmic reticulum organization [has_penetrance] 80	As expected, the addition of HU to cells deleted for lem2, cmp7 or vps4 resulted in perinuclear ER fragmentation (S2G, S2H Fig; for results, see S1 Data).
PMID:41259369	FYPO:0000805	abnormal endoplasmic reticulum organization [has_penetrance] 80	As expected, the addition of HU to cells deleted for lem2, cmp7 or vps4 resulted in perinuclear ER fragmentation (S2G, S2H Fig; for results, see S1 Data).
PMID:41259369	FYPO:0000355	normal endoplasmic reticulum morphology	Clustered NPCs in nup120Δ cells showed an apparently normal perinuclear ER morphology (Fig 1G)
PMID:41259369	FYPO:0010034	abolished nuclear pore clustering during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC1786.03 [has_penetrance] 100	Consistent, pgr1Δ also fully prevented ER expansion under DIA treatment, while the incidence of the HU-induced ER expansion phenotype was significantly reduced in this mutant (Fig 6C).
PMID:41259369	FYPO:0010034	abolished nuclear pore clustering during cellular response to hydroxyurea [has_penetrance] 60	Consistent, pgr1Δ also fully prevented ER expansion under DIA treatment, while the incidence of the HU-induced ER expansion phenotype was significantly reduced in this mutant (Fig 6C).
PMID:41259369	FYPO:0000843	sensitive to dithiothreitol	Consistently, whereas ire1Δ cells were hypersensitive to DTT, they showed a sensitivity to DIA similar to wild-type cells (S6C Fig).
PMID:41259369	FYPO:0001240	normal growth on diamide	Consistently, whereas ire1Δ cells were hypersensitive to DTT, they showed a sensitivity to DIA similar to wild-type cells (S6C Fig).
PMID:41259369	PomGeneEx:0000018	protein level increased [in_presence_of] hydroxyurea	Furthermore, we analyzed whether DIA and HU were also engaging cytoplasmic chaperones. Indeed, we found that both treatments led to an increase in the levels of Hsp70/Ssa1-YFP, Hsp16-GFP, and the disaggregase Hsp104-GFP and their accumulation in cytoplasmic foci, suggesting defective folding in this compartment (Fig 4D–4F; for results, see S1 Data).
PMID:41259369	PomGeneEx:0000018	protein level increased [in_presence_of] hydroxyurea	Furthermore, we analyzed whether DIA and HU were also engaging cytoplasmic chaperones. Indeed, we found that both treatments led to an increase in the levels of Hsp70/Ssa1-YFP, Hsp16-GFP, and the disaggregase Hsp104-GFP and their accumulation in cytoplasmic foci, suggesting defective folding in this compartment (Fig 4D–4F; for results, see S1 Data).
PMID:41259369	PomGeneEx:0000018	protein level increased [in_presence_of] hydroxyurea	Furthermore, we analyzed whether DIA and HU were also engaging cytoplasmic chaperones. Indeed, we found that both treatments led to an increase in the levels of Hsp70/Ssa1-YFP, Hsp16-GFP, and the disaggregase Hsp104-GFP and their accumulation in cytoplasmic foci, suggesting defective folding in this compartment (Fig 4D–4F; for results, see S1 Data).
PMID:41259369	PomGeneEx:0000018	protein level increased [in_presence_of] hydroxyurea	Furthermore, we analyzed whether DIA and HU were also engaging cytoplasmic chaperones. Indeed, we found that both treatments led to an increase in the levels of Hsp70/Ssa1-YFP, Hsp16-GFP, and the disaggregase Hsp104-GFP and their accumulation in cytoplasmic foci, suggesting defective folding in this compartment (Fig 4D–4F; for results, see S1 Data).
PMID:41259369	PomGeneEx:0000018	protein level increased [in_presence_of] hydroxyurea	Furthermore, we analyzed whether DIA and HU were also engaging cytoplasmic chaperones. Indeed, we found that both treatments led to an increase in the levels of Hsp70/Ssa1-YFP, Hsp16-GFP, and the disaggregase Hsp104-GFP and their accumulation in cytoplasmic foci, suggesting defective folding in this compartment (Fig 4D–4F; for results, see S1 Data).
PMID:41259369	PomGeneEx:0000018	protein level increased [in_presence_of] hydroxyurea	Furthermore, we analyzed whether DIA and HU were also engaging cytoplasmic chaperones. Indeed, we found that both treatments led to an increase in the levels of Hsp70/Ssa1-YFP, Hsp16-GFP, and the disaggregase Hsp104-GFP and their accumulation in cytoplasmic foci, suggesting defective folding in this compartment (Fig 4D–4F; for results, see S1 Data).
PMID:41259369	PomGeneEx:0000018	protein level increased [in_presence_of] 1,1'-azobis(N,N-dimethylformamide)	Furthermore, we analyzed whether DIA and HU were also engaging cytoplasmic chaperones. Indeed, we found that both treatments led to an increase in the levels of Hsp70/Ssa1-YFP, Hsp16-GFP, and the disaggregase Hsp104-GFP and their accumulation in cytoplasmic foci, suggesting defective folding in this compartment (Fig 4D–4F; for results, see S1 Data).
PMID:41259369	PomGeneEx:0000018	protein level increased [in_presence_of] 1,1'-azobis(N,N-dimethylformamide)	Furthermore, we analyzed whether DIA and HU were also engaging cytoplasmic chaperones. Indeed, we found that both treatments led to an increase in the levels of Hsp70/Ssa1-YFP, Hsp16-GFP, and the disaggregase Hsp104-GFP and their accumulation in cytoplasmic foci, suggesting defective folding in this compartment (Fig 4D–4F; for results, see S1 Data).
PMID:41259369	PomGeneEx:0000018	protein level increased [in_presence_of] 1,1'-azobis(N,N-dimethylformamide)	Furthermore, we analyzed whether DIA and HU were also engaging cytoplasmic chaperones. Indeed, we found that both treatments led to an increase in the levels of Hsp70/Ssa1-YFP, Hsp16-GFP, and the disaggregase Hsp104-GFP and their accumulation in cytoplasmic foci, suggesting defective folding in this compartment (Fig 4D–4F; for results, see S1 Data).
PMID:41259369	PomGeneEx:0000018	protein level increased [in_presence_of] 1,1'-azobis(N,N-dimethylformamide)	Furthermore, we analyzed whether DIA and HU were also engaging cytoplasmic chaperones. Indeed, we found that both treatments led to an increase in the levels of Hsp70/Ssa1-YFP, Hsp16-GFP, and the disaggregase Hsp104-GFP and their accumulation in cytoplasmic foci, suggesting defective folding in this compartment (Fig 4D–4F; for results, see S1 Data).
PMID:41259369	PomGeneEx:0000018	protein level increased [in_presence_of] 1,1'-azobis(N,N-dimethylformamide)	Furthermore, we analyzed whether DIA and HU were also engaging cytoplasmic chaperones. Indeed, we found that both treatments led to an increase in the levels of Hsp70/Ssa1-YFP, Hsp16-GFP, and the disaggregase Hsp104-GFP and their accumulation in cytoplasmic foci, suggesting defective folding in this compartment (Fig 4D–4F; for results, see S1 Data).
PMID:41259369	PomGeneEx:0000018	protein level increased [in_presence_of] 1,1'-azobis(N,N-dimethylformamide)	Furthermore, we analyzed whether DIA and HU were also engaging cytoplasmic chaperones. Indeed, we found that both treatments led to an increase in the levels of Hsp70/Ssa1-YFP, Hsp16-GFP, and the disaggregase Hsp104-GFP and their accumulation in cytoplasmic foci, suggesting defective folding in this compartment (Fig 4D–4F; for results, see S1 Data).
PMID:41259369	FYPO:0010035	normal nuclear pore clustering during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC1786.03	HU-dependent NPC clustering could be induced in G2/M blocked cells (by inacti- vation of cdc25-22, a thermosensitive allele of the mitotic activator Cdc25) (S1E Fig).
PMID:41259369	FYPO:0010034	abolished nuclear pore clustering during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC1786.03 [has_penetrance] 100	Inactivation of Cdc22R1 by using a thermo- sensitive cdc22-M45 mutant strain and keeping it at restrictive temperature for over four hours [33,34] did not result in NPC clustering (S1D Fig).
PMID:41259369	FYPO:0000355	normal endoplasmic reticulum morphology	Moreover, ire1Δ cells expanded the perinuclear ER under DIA treatment with the same frequency and timing as wild-type cells (S6B Fig; for results, see S1 Data)
PMID:41259369	FYPO:0010035	normal nuclear pore clustering during cellular response to hydroxyurea [assayed_protein] PomBase:SPAC1786.03	The appearance of clustered NPCs was unrelated to the differential nucleocytoplasmic compartmentalization of the two RNR subunits, as deletion of spd1, which results in both subunits constitutively localizing in the cytoplasm [32], did not alter the frequency of NPC clustering (S1C Fig).
PMID:41259369	PomGeneEx:0000020	protein level unchanged [in_presence_of] 1,1'-azobis(N,N-dimethylformamide)	upon HU or DIA treatments, Bip1-GFP cortical foci decreased their number and intensity concomitantly with an increase of Bip1-GFP signal at the expanded perinuclear ER (Fig 4A), whereas the protein levels of Bip1 did not signifi- cantly change (Fig 4B).
PMID:41259369	PomGeneEx:0000020	protein level unchanged [in_presence_of] hydroxyurea	upon HU or DIA treatments, Bip1-GFP cortical foci decreased their number and intensity concomitantly with an increase of Bip1-GFP signal at the expanded perinuclear ER (Fig 4A), whereas the protein levels of Bip1 did not signifi- cantly change (Fig 4B).
PMID:41259369	FYPO:0000354	abnormal endoplasmic reticulum morphology	we found that perinuclear ER expansion was suppressed in the absence of Gcs1, and the gsa1Δ mutant strain also fully sup- pressed N-Cap appearance in DIA and significantly reduced its frequency in HU.
PMID:41259369	FYPO:0010034	abolished nuclear pore clustering during cellular response to hydroxyurea [has_penetrance] 100	we found that perinuclear ER expansion was suppressed in the absence of Gcs1, and the gsa1Δ mutant strain also fully sup- pressed N-Cap appearance in DIA and significantly reduced its frequency in HU.
PMID:41259369	FYPO:0010034	abolished nuclear pore clustering during cellular response to hydroxyurea [has_penetrance] 100	we found that perinuclear ER expansion was suppressed in the absence of Gcs1, and the gsa1Δ mutant strain also fully sup- pressed N-Cap appearance in DIA and significantly reduced its frequency in HU.
PMID:41298081	FYPO:0003056	Mei2 nuclear dot absent from cell	(Fig. 2G)
PMID:41298081	FYPO:0010003	abolished protein export from nucleus during mating [assayed_protein] PomBase:SPAC27D7.03c	(Fig. 2H)
PMID:41298081	FYPO:0010000	abnormal protein export from nucleus during mating [assayed_protein] PomBase:SPAC27D7.03c	(Fig. 2I)
PMID:41298081	FYPO:0002151	inviable spore	(Fig. 3G)
PMID:41298081	FYPO:0008321	abolished sporulation during nitrogen starvation [has_penetrance] 100	(Fig. 4B)
PMID:41298081	FYPO:0008321	abolished sporulation during nitrogen starvation [has_penetrance] 100	(Fig. 4B)
PMID:41298081	FYPO:0008321	abolished sporulation during nitrogen starvation [has_penetrance] 100	(Fig. 4B)
PMID:41298081	FYPO:0002052	normal sporulation frequency	(Fig. 4B)
PMID:41298081	FYPO:0003056	Mei2 nuclear dot absent from cell	(Fig. 4C)
PMID:41298081	FYPO:0000474	abolished meiosis	(Fig. 6B-D)
PMID:41298081	GO:0000932	P-body [exists_during] conjugation with cellular fusion	(Fig. 7A, 7B). These results suggest that mamRNA localizes to P-bodies in zygotes.
PMID:41298081	GO:0000932	P-body [exists_during] conjugation with cellular fusion	(Fig. 7A, 7B). These results suggest that mamRNA localizes to P-bodies in zygotes.
PMID:41298081	GO:0046831	regulation of RNA export from nucleus [happens_during] meiotic S phase	(Fig. 7A, Fig. S7A-B)
PMID:41298081	GO:2000766	negative regulation of cytoplasmic translation [happens_during] meiotic S phase	(Fig. 7D-7G) Taken together, our results suggest that Mei2 represses transla- tion of mRNAs that it physically binds and that this re- quires RRM1, but not RRM3 or Mei3, expression.
PMID:41298081	FYPO:0008321	abolished sporulation during nitrogen starvation [has_penetrance] 100	(Fig. S1I)
PMID:41298081	FYPO:0008321	abolished sporulation during nitrogen starvation [has_penetrance] 100	(Fig. S1I)
PMID:41298081	FYPO:0000913	abnormal sporulation resulting in formation of ascus containing non-uniform spores	(Fig. S6A-B)
PMID:41298081	FYPO:0000913	abnormal sporulation resulting in formation of ascus containing non-uniform spores	(Fig. S6A-B)
PMID:41298081	FYPO:0000913	abnormal sporulation resulting in formation of ascus containing non-uniform spores	(Fig. S6A-B)
PMID:41298081	FYPO:0001355	decreased vegetative cell population growth	Although Pat1-NLS-3sfGFP was upregulated (Supplemen- tal Fig. S2A–C), this strain had reduced population growth (Fig. 3C).
PMID:41298081	FYPO:0010008	decreased protein localization to P-bodies during mating [assayed_protein] PomBase:SPAC27D7.03c	Both Mei2-sfGFP and Mei2F239A - sfGFP produced a diffuse cytosolic signal in gametes, but wild-type Mei2 formed cytosolic foci in zygotes that were absent from the F239A mutant (Fig. 4C).
PMID:41298081	FYPO:0003612	viable spore population	Consistent with this idea, genetic crosses showed that the pat1Δ mutant lethality (Bähler et al. 1991; Kita- mura et al. 2001; Cipak et al. 2012) is suppressed by the nucleus-targeted Mei2-NLS-3mCherry allele (Fig. 3G, purple arrowheads; Supplemental Fig. S3E).
PMID:41298081	FYPO:0003612	viable spore population	Consistent with this idea, genetic crosses showed that the pat1Δ mutant lethality (Bähler et al. 1991; Kita- mura et al. 2001; Cipak et al. 2012) is suppressed by the nucleus-targeted Mei2-NLS-3mCherry allele (Fig. 3G, purple arrowheads; Supplemental Fig. S3E).
PMID:41298081	FYPO:0001357	normal vegetative cell population growth	Deleting the mei2 gene rescued the proliferation of the pat1-NLS-3sfGFP strain (Supplemental Fig. S3A)
PMID:41298081	FYPO:0001357	normal vegetative cell population growth	Deleting the mei2 gene rescued the proliferation of the pat1-NLS-3sfGFP strain (Supplemental Fig. S3A)
PMID:41298081	FYPO:0003612	viable spore population	Deleting the ste13 gene rescued the lethality of pat1Δ mutants (Supplemental Fig. S6E)
PMID:41298081	FYPO:0003612	viable spore population	Deleting the ste13 gene rescued the lethality of pat1Δ mutants (Supplemental Fig. S6E)
PMID:41298081	FYPO:0007147	normal Mei2 nuclear dot formation	Deletion of Rad24, which binds only phosphorylated Mei2 (Sato et al. 2002), did not affect the nucleocytoplasmic distribu- tion of Mei2-sfGFP and Mei2-NLS-sfGFP (Supplemental Fig. S1G,H; Supplemental Movie S3).
PMID:41298081	FYPO:0000474	abolished meiosis	However, Mei2-NES- 3mCherry zygotes arrested ahead of meiotic divisions and completely failed to induce sporulation (Fig. 3H).
PMID:41298081	FYPO:0001357	normal vegetative cell population growth	Importantly, the slow growth and precocious meiosis of pat1-NLS-3sfGFP cells were also rescued when Mei2 was targeted to the nucleus with two NLS motifs flanking either sfGFP or 3mCherry (Fig. 3D–F; Supplemental Fig. S3A,B).
PMID:41298081	FYPO:0001357	normal vegetative cell population growth	Importantly, the slow growth and precocious meiosis of pat1-NLS-3sfGFP cells were also rescued when Mei2 was targeted to the nucleus with two NLS motifs flanking either sfGFP or 3mCherry (Fig. 3D–F; Supplemental Fig. S3A,B).
PMID:41298081	FYPO:0006185	decreased protein localization to nucleus during prophase I [assayed_protein] PomBase:SPBC19C2.05 [has_severity] high	In contrast, Pat1-3sfGFP failed to accumulate in the nucleus upon fusion between mei3Δ mutant gametes (Fig. 1E,F; Supplemental Movie S1).
PMID:41298081	FYPO:0002958	abnormal protein localization to Mei2 nuclear dot [assayed_protein] PomBase:SPAC27D7.03c	In mei3Δ zygotes, Mei2-sfGFP nuclear dots were unstable, disap- pearing and reappearing over the course of imaging (Supplemental Movie S2). (Fig. 2C)
PMID:41298081	FYPO:0001897	P-bodies present in decreased numbers during vegetative growth [has_severity] high	In ste13Δ mutants, the P-body marker Edc3-mCherry showed a se- verely reduced number of puncta, but their assembly was not completely abolished (Fig. 6A; Supplemental Fig. S6D).
PMID:41298081	FYPO:0000479	premature meiosis [has_severity] high	Indeed, Pat1-NLS-3sfGFP haploid gametes entered meiosis, and 22.9% ± 1% of gam- etes contained spores (Fig. 3A,B).
PMID:41298081	FYPO:0007147	normal Mei2 nuclear dot formation	Indeed, nuclear Mei2 dots formed in paired gametes that were unable to fuse due to the deletion of the formin fus1 (Petersen et al. 1995) and in cells lacking the mei3 gene, where Pat1 activity re- mains high (Fig. 2B,C; Supplemental Movie S2).
PMID:41298081	GO:0000932	P-body [exists_during] karyogamy involved in conjugation with cellular fusion	Mei2- sfGFP cytosolic foci extensively colocalized with mCherry-tagged P-body components Edc3 and Dcp2 in zy- gotes (87% ± 6% and 79% ± 11% of Mei2-sfGFP foci colo- calized with Edc3 and Dcp2, respectively; n = 10 zygotes) (Fig. 4E; Supplemental Fig. S4G; Supplemental Movie S9; Wang et al. 2017). We did not observe Mei2-sfGFP re- cruitment to Edc3- and Dcp2-labeled P-bodies in gametes even though Edc3 and Dcp2 puncta were clearly visible (Fig. 4E; Supplemental Fig. S4G). We conclude that Mei2 is recruited to P-bodies specifically in zygotes.
PMID:41298081	FYPO:0007147	normal Mei2 nuclear dot formation	Mei2-NES-3mCherry failed to form a nuclear dot, which we observed with Mei2-NLS-3mCherry and Mei2-NES-NLS-3mCherry (Fig. 3F [insets], I; Supplemen- tal Movie S7).
PMID:41298081	FYPO:0005992	decreased protein localization to P-bodies [assayed_protein] PomBase:SPAC27D7.03c	Mei2-sfGFP cytosolic foci failed to form in the mei3Δ mutant (Fig. 5A), showing that Mei3 triggers Mei2 recruitment to P-bodies.
PMID:41298081	GO:0005634	nucleus [exists_during] karyogamy involved in conjugation with cellular fusion	Mei3-sfGFP signal was undetect- able in gametes but then quickly increased upon fusion and localized predominantly to the zygotic nucleus (Fig. 1B,C)
PMID:41298081	GO:0005634	nucleus [exists_during] karyogamy involved in conjugation with cellular fusion	Mei3-sfGFP signal was undetect- able in gametes but then quickly increased upon fusion and localized predominantly to the zygotic nucleus (Fig. 1B,C)
PMID:41298081	GO:0005634	nucleus [exists_during] karyogamy involved in conjugation with cellular fusion	Pat1-3sfGFP showed a dif- fuse nucleocytoplasmic signal in gametes, and gamete fu- sion led to its rapid accumulation in the nucleus of zygotes (Fig. 1E, bottom panel).
PMID:41298081	FYPO:0010020	abolished protein localization to P-bodies during mating [assayed_protein] PomBase:SPAC27D7.03c	The fusion-deficient fus1Δ mutants, which arrest as mated pairs, did not form cytosolic Mei2 foci, and we could only detect the Mei2 nuclear dot (Fig. 4D; Supple- mental Movie S8).
PMID:41298081	FYPO:0003056	Mei2 nuclear dot absent from cell	Third, Mei2-NES-3mCherry failed to in- duce transcriptional elongation of meiRNA at the nuclear dot (Yamashita et al. 2012; Shichino et al. 2014) and thus failed to produce the long meiRNAL transcript (Fig. 3I,J; Supplemental Movie S7).
PMID:41298081	FYPO:0010010	decreased protein localization to nucleus, with protein mislocalized to cytoplasm during mating [assayed_protein] PomBase:SPBC19C2.05	This Pat1- NES-3sfGFP was induced in gametes and largely excluded from the nucleus, yet we did not observe defects in sexual reproduction or mitotic proliferation of this strain (Fig. 3A–C; Supplemental Fig. S2A,B).
PMID:41298081	FYPO:0003797	normal conjugation frequency	This Pat1- NES-3sfGFP was induced in gametes and largely excluded from the nucleus, yet we did not observe defects in sexual reproduction or mitotic proliferation of this strain (Fig. 3A–C; Supplemental Fig. S2A,B).
PMID:41298081	FYPO:0004795	normal zygotic meiosis	This Pat1- NES-3sfGFP was induced in gametes and largely excluded from the nucleus, yet we did not observe defects in sexual reproduction or mitotic proliferation of this strain (Fig. 3A–C; Supplemental Fig. S2A,B).
PMID:41298081	FYPO:0001357	normal vegetative cell population growth	This Pat1- NES-3sfGFP was induced in gametes and largely excluded from the nucleus, yet we did not observe defects in sexual reproduction or mitotic proliferation of this strain (Fig. 3A–C; Supplemental Fig. S2A,B).
PMID:41298081	FYPO:0010019	increased protein localization to nucleus in gametes [assayed_protein] PomBase:SPAC27D7.03c [has_severity] high	To test this possibility, we fused Mei2 with two NLS motifs flanking sfGFP, which did not impair Mei2 function and resulted in expectedly strong nuclear enrichment of Mei2-NLS-sfGFP in gametes (Fig. 2D; Supplemental Fig. S1A; Supplemental Movie S3).
PMID:41298081	FYPO:0010006	decreased RNA localization to P-bodies during mating [has_severity] high [assayed_transcript] PomBase:SPNCRNA.1715	Upon mutating RRM1 and RRM3 of Mei2, mamRNA remained strongly nuclear in both gametes and zygotes (Fig. 7A; Supplemental Fig. S7A–C),
PMID:41298081	FYPO:0010006	decreased RNA localization to P-bodies during mating [has_severity] high [assayed_transcript] PomBase:SPNCRNA.1715	Upon mutating RRM1 and RRM3 of Mei2, mamRNA remained strongly nuclear in both gametes and zygotes (Fig. 7A; Supplemental Fig. S7A–C),
PMID:41298081	FYPO:0001357	normal vegetative cell population growth	We did not observe defects in strains where nucleus-tar- geted Mei2 was segregated from cytosol-restricted Pat1 (Fig. 3D, mei2-NLS pat1-NES; Supplemental Fig. S3D; Supplemental Movie S5).
PMID:41298081	FYPO:0010015	increased protein localization to nucleus during mating [has_severity] high [assayed_protein] PomBase:SPBC19C2.05	We targeted Pat1 to the nucleus by fusing it with two NLS motifs flanking the 3sfGFP, which resulted in expect- edly low cytoplasmic levels and a strong nuclear accumula- tion of Pat1-NLS-3sfGFP (Fig. 3A; Supplemental Fig. S2C).
PMID:41298081	FYPO:0010006	decreased RNA localization to P-bodies during mating [has_severity] low [assayed_transcript] PomBase:SPNCRNA.1715	mamRNA cytosolic targeting was also partially impaired in mei3Δ mutant zygotes (Fig.7A; Supplemental Fig. S7A,B).
PMID:41298081	FYPO:0002052	normal sporulation frequency	sporulation was fully restored when we forced Mei2 bidirectional nucleocytoplasmic shuttling by ex- changing one of the two NES motifs in Mei2-NES- 3mCherry for an NLS motif (Mei2-NES-NLS-3mCherry) (Fig. 3F,H; Supplemental Fig. S3G; Supplemental Movie S5).
PMID:41298081	FYPO:0006541	decreased protein level during mating [assayed_protein] PomBase:SPAC27D7.03c [has_severity] high	ste13Δ mutants severely downregulated Mei2 (Supplemental Fig. S6F).
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Fig. 2A)
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat	(Fig. 2A)
PMID:41316862	FYPO:0010018	increased histone H3-K36 trimethylation at centromere outer repeat during vegetative growth	(Fig. 2D)
PMID:41316862	FYPO:0006369	increased histone H3-K9 dimethylation at heterochromatin domain during vegetative growth	(Fig. 3A)
PMID:41316862	FYPO:0006369	increased histone H3-K9 dimethylation at heterochromatin domain during vegetative growth	(Fig. 3A). Interestingly, elp1 loss restored H3K9me2 at HOOD-23 in m203 cells.
PMID:41316862	FYPO:0007009	decreased heterochromatin assembly by small RNA [has_severity] low	(Fig. 4)
PMID:41316862	FYPO:0007009	decreased heterochromatin assembly by small RNA [has_severity] low	(Fig. 4)
PMID:41316862	FYPO:0007009	decreased heterochromatin assembly by small RNA [has_severity] high	(Fig. 4)
PMID:41316862	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] high	(Fig. 4A)
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	(Fig. 5A)
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	(Fig. 5A)
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] low	(Fig. 6C)
PMID:41316862	FYPO:0005843	abolished histone H3-K9 trimethylation at centromere outer repeat during vegetative growth	By H3K9me3 ChIP analyses, we also found that overexpression of tRNALys UUU, but not tRNALys CUU, in m203 elp1Δ cells dramatically reduced H3K9me3 at the otr1R::ura4+ locus (Fig. 7b).
PMID:41316862	FYPO:0008199	normal histone H3-K9 trimethylation at centromere outer repeat during vegetative growth	By H3K9me3 ChIP analyses, we also found that overexpression of tRNALys UUU, but not tRNALys CUU, in m203 elp1Δ cells dramatically reduced H3K9me3 at the otr1R::ura4+ locus (Fig. 7b).
PMID:41316862	FYPO:0004742	normal chromatin silencing at centromere outer repeat	Cells in which Rpb2-Asn44 was substituted with glutamine (Glu, Q), whose side-chain is most similar to that of Asn, grew similarly to wild-type in the presence of 5-FOA (Fig. 1b).
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	Cells where Rpb2-Asn44 was substituted with phenylalanine (Phe, F), which has a bulky side-chain similar to Tyr, grew as poorly as rpb2-N44Y (m203) cells on media with 5-FOA (Fig. 1b).
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	Cells where Rpb2-Asn44 was substituted with phenylalanine (Phe, F), which has a bulky side-chain similar to Tyr, grew as poorly as rpb2-N44Y (m203) cells on media with 5-FOA (Fig. 1b).
PMID:41316862	FYPO:0010032	normal histone H3-K36 trimethylation at centromere outer repeat during vegetative growth	ChIP-qPCR confirmed that elp1Δ increased heterochromatic H3K9me3 and decreased euchromatic H3K36me3 at our reporter locus in m203 cells (Fig. 2c and d).
PMID:41316862	FYPO:0010032	normal histone H3-K36 trimethylation at centromere outer repeat during vegetative growth	ChIP-qPCR confirmed that elp1Δ increased heterochromatic H3K9me3 and decreased euchromatic H3K36me3 at our reporter locus in m203 cells (Fig. 2c and d).
PMID:41316862	FYPO:0008199	normal histone H3-K9 trimethylation at centromere outer repeat during vegetative growth	ChIP-qPCR confirmed that elp1Δ increased heterochromatic H3K9me3 and decreased euchromatic H3K36me3 at our reporter locus in m203 cells (Fig. 2c and d).
PMID:41316862	FYPO:0008199	normal histone H3-K9 trimethylation at centromere outer repeat during vegetative growth	ChIP-qPCR confirmed that elp1Δ increased heterochromatic H3K9me3 and decreased euchromatic H3K36me3 at our reporter locus in m203 cells (Fig. 2c and d).
PMID:41316862	FYPO:0000087	sensitive to hydrogen peroxide	Due to the lack of tRNA modification capability, the elp3-CC mutant was hypersensitive to H2O2-induced oxidative stress (Supplementary Fig. 4b)
PMID:41316862	FYPO:0008199	normal histone H3-K9 trimethylation at centromere outer repeat during vegetative growth	Furthermore, there was still H3K9me3 enrichment at otr1R::ura4+ in the rpb2-N44S variant (Fig. 1c).
PMID:41316862	FYPO:0004742	normal chromatin silencing at centromere outer repeat	In contrast, the empty vector or overexpression of tRNALys CUU showed far less suppressive effects (Fig. 7a).
PMID:41316862	FYPO:0000890	decreased histone H3-K9 trimethylation at centromere outer repeat during vegetative growth [has_severity] medium	Interestingly, knocking out both Elp1 and Elp3 in m203 cells (m203 elp1Δ elp3Δ) reduced H3K9me3 enrichment at the otr1R::ura4+ reporter, relative to m203 elp1Δ cells (Fig. 5b).
PMID:41316862	FYPO:0004742	normal chromatin silencing at centromere outer repeat	Lastly, we confirmed that elp1Δ in rpb2-N44F mutant cells also robustly grew on 5-FOA media (Supplementary Fig. 2b).
PMID:41316862	FYPO:0004742	normal chromatin silencing at centromere outer repeat	Lastly, we confirmed that elp1Δ in rpb2-N44F mutant cells also robustly grew on 5-FOA media (Supplementary Fig. 2b).
PMID:41316862	FYPO:0003218	abolished tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridine biosynthesis	Next, we performed mass spectrometry of total tRNAs to confirm that elp3-CC cells completely lost mcm5s2 tRNA modifications (Fig. 6b),
PMID:41316862	FYPO:0000890	decreased histone H3-K9 trimethylation at centromere outer repeat during vegetative growth [has_severity] high	There was also minor restoration of H3K9me3 at the reporter locus in cells m203 ctu1Δ (Fig. 6f).
PMID:41316862	FYPO:0000890	decreased histone H3-K9 trimethylation at centromere outer repeat during vegetative growth [has_severity] medium	These phenotypes correlated with partial increases in H3K9me3 at the otr1R::ura4 + reporter in m203 cells lacking elp3, compared to a higher H3K9me3 restoration in m203 elp1Δ cells (Fig. 5b),
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	Using 20 μM of cycloheximide, there was no restoration of m203 cell growth on 5-FOA media (Supplementary Fig. 5).
PMID:41316862	FYPO:0000890	decreased histone H3-K9 trimethylation at centromere outer repeat during vegetative growth [has_severity] high	Validating this finding, H3K9me3 ChIP-qPCR analysis showed that elp3-CC only slightly restored H3K9me3 at otr1R::ura4 + in m203 cells (Fig. 6d).
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	We also deleted the ctu1 gene (ctu1Δ), which encodes for the Ctu2 tRNA thiolase that is required for adding the sulfur group (s2) within the mcm5s2 tRNA modification (Dewez et al. 2008), and found weak growth of m203 ctu1Δ cells on 5-FOA media (Fig. 6e).
PMID:41316862	FYPO:0004742	normal chromatin silencing at centromere outer repeat	We discovered that loss of elp1 (elp1Δ) in m203 cells enabled strong growth in the presence of 5-FOA, similar to wild-type cells (Fig. 2a and Supplementary Fig. 2a).
PMID:41316862	FYPO:0004742	normal chromatin silencing at centromere outer repeat	We discovered that loss of elp1 (elp1Δ) in m203 cells enabled strong growth in the presence of 5-FOA, similar to wild-type cells (Fig. 2a and Supplementary Fig. 2a).
PMID:41316862	FYPO:0004742	normal chromatin silencing at centromere outer repeat	We found that cells with rpb2-N44A and rpb2-N44S variants proliferated similarly to wild- type cells in the presence of 5-FOA (Fig. 1b).
PMID:41316862	FYPO:0004742	normal chromatin silencing at centromere outer repeat	We found that cells with rpb2-N44A and rpb2-N44S variants proliferated similarly to wild- type cells in the presence of 5-FOA (Fig. 1b).
PMID:41316862	FYPO:0004201	decreased centromeric outer repeat transcript-derived siRNA level [has_severity] medium	We found that elp1Δ increases pericentromeric siRNAs in m203 cells (Fig. 4a).
PMID:41316862	FYPO:0010033	normal histone H3-K9 dimethylation at heterochromatin domain during vegetative growth	We found that m203 reduced H3K9me2 at one HOOD known as HOOD-23, which encompasses the pho1 gene (Fig. 3a)
PMID:41316862	FYPO:0010033	normal histone H3-K9 dimethylation at heterochromatin domain during vegetative growth	We found that m203 reduced H3K9me2 at one HOOD known as HOOD-23, which encompasses the pho1 gene (Fig. 3a)
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	We found that tRNALys UUU overexpression re- sensitized m203 elp1Δ cells to 5-FOA (Fig. 7a).
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	We found that the loss of ago1, dcr1, or rdp1 reverted cells to the 5-FOA-sensitive state, suggesting that elp1Δ depends on the RNAi pathway to repress the otr1R::ura4+ reporter (Fig. 4b).
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	We found that the loss of ago1, dcr1, or rdp1 reverted cells to the 5-FOA-sensitive state, suggesting that elp1Δ depends on the RNAi pathway to repress the otr1R::ura4+ reporter (Fig. 4b).
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	We found that the loss of ago1, dcr1, or rdp1 reverted cells to the 5-FOA-sensitive state, suggesting that elp1Δ depends on the RNAi pathway to repress the otr1R::ura4+ reporter (Fig. 4b).
PMID:41316862	FYPO:0005843	abolished histone H3-K9 trimethylation at centromere outer repeat during vegetative growth	We further validated by chromatin immunoprecipitation with quantitative PCR (ChIP-qPCR) that both rpb2-N44Y and rpb2-N44F mutants decreased the levels of heterochromatic H3K9me3 at the otr1R::ura4+ reporter (Fig. 1c).
PMID:41316862	FYPO:0005843	abolished histone H3-K9 trimethylation at centromere outer repeat during vegetative growth	We further validated by chromatin immunoprecipitation with quantitative PCR (ChIP-qPCR) that both rpb2-N44Y and rpb2-N44F mutants decreased the levels of heterochromatic H3K9me3 at the otr1R::ura4+ reporter (Fig. 1c).
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	elp3-CC did not strongly restore growth of m203 cells on 5-FOA media (Fig. 6c).
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	m203 cells lacking elp3 or elp5 only had modest growth (Fig. 5a).
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	m203 cells lacking elp3 or elp5 only had modest growth (Fig. 5a).
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	m203 cells lacking elp3 or elp5 only had modest growth (Fig. 5a).
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] medium	m203 cells lacking elp3 or elp5 only had modest growth (Fig. 5a).
PMID:41316862	FYPO:0003412	decreased chromatin silencing at centromere outer repeat [has_severity] high	m203 elp1Δ cells reverted to hypersensitivity on 5-FOA-containing media after the loss of the clr4 gene (which encodes for the sole H3K9 methyltransferase) (Fig. 2e).
PMID:41330900	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] 35	(Fig. 1B)
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 3C)
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Fig. 3C)
PMID:41330900	MOD:01149	sumoylated lysine	(Fig. 5)
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 6A)
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 6A)
PMID:41330900	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 6A)
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 6A)
PMID:41330900	FYPO:0000957	normal growth on methyl methanesulfonate	(Fig. 6A)
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	(Fig. 6A)
PMID:41330900	FYPO:0000964	normal growth on thiabendazole	(Fig. 6A)
PMID:41330900	FYPO:0000964	normal growth on thiabendazole	(Fig. 6A)
PMID:41330900	FYPO:0000964	normal growth on thiabendazole	(Fig. 6A)
PMID:41330900	FYPO:0000964	normal growth on thiabendazole	(Fig. 6A)
PMID:41330900	FYPO:0005226	decreased level of ubiquitinated protein in cell [assayed_protein] PomBase:SPBC16D10.09	(Fig. 6C)
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] low	(Fig. 7D)
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	(Fig. 7D)
PMID:41330900	FYPO:0007328	normal number of Rad52 foci during vegetative growth	(Fig. 7F)
PMID:41330900	FYPO:0001357	normal vegetative cell population growth	(Fig. S14B)
PMID:41330900	FYPO:0001357	normal vegetative cell population growth	(Fig. S14C)
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. S14C)
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. S2A)
PMID:41330900	FYPO:0000268	sensitive to UV during vegetative growth	(Fig. S2A)
PMID:41330900	FYPO:0002344	sensitive to phleomycin	(Fig. S2A)
PMID:41330900	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. S2A)
PMID:41330900	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. S3A)
PMID:41330900	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. S3A)
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. S3A)
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. S3A)
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. S3B)
PMID:41330900	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. S3B)
PMID:41330900	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. S3B)
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	(Fig. S3B)
PMID:41330900	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. S3B)
PMID:41330900	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(Fig. S7B)
PMID:41330900	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. S7B)
PMID:41330900	FYPO:0001355	decreased vegetative cell population growth [has_severity] low	(Fig. S7B)
PMID:41330900	FYPO:0010023	increased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC644.14c	ChIP analysis con rmed elevated binding of Rad52- YFP and Rad51 to centromere cores in the SUMO-KallR mutant (Fig. 3a, b).
PMID:41330900	FYPO:0010023	increased protein localization to centromeric chromatin during vegetative growth [assayed_protein] PomBase:SPAC30D11.10	ChIP analysis con rmed elevated binding of Rad52- YFP and Rad51 to centromere cores in the SUMO-KallR mutant (Fig. 3a, b).
PMID:41330900	FYPO:0000614	increased duration of mitotic S phase	Flow cytometry analysis of cell cycle from samples taken in parallel to PFGE revealed that SUMO-KallR mutant progressed more slowly through S phase compared to WT (Supplementary Fig. 2e, red arrows).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	In contrast, deletion of TLS poly- merases, Rev1 or Rev3, did not suppress SUMO-KallR TBZ sensitivity (Fig. 6a).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	In contrast, deletion of TLS poly- merases, Rev1 or Rev3, did not suppress SUMO-KallR TBZ sensitivity (Fig. 6a).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] low	Introduction of rad52-Schain to SUMO-KallR mutant partially suppressed its TBZ sensitivity (Fig. 7d).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] low	Introduction of rad52-Schain to SUMO-KallR mutant partially suppressed its TBZ sensitivity (Fig. 7d).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	Loss of SUMO chains also enhanced TBZ sensitivity in SUMO- KallR rad51Δ and SUMO-KallR rad52Δ double mutants compared to single mutants (Fig. 3c).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] high	Loss of SUMO chains also enhanced TBZ sensitivity in SUMO- KallR rad51Δ and SUMO-KallR rad52Δ double mutants compared to single mutants (Fig. 3c).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	Loss of SUMO chains also enhanced TBZ sensitivity in SUMO- KallR rad51Δ and SUMO-KallR rad52Δ double mutants compared to single mutants (Fig. 3c).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] high	Loss of SUMO chains also enhanced TBZ sensitivity in SUMO- KallR rad51Δ and SUMO-KallR rad52Δ double mutants compared to single mutants (Fig. 3c).
PMID:41330900	FYPO:0000969	normal growth during cellular response to UV	Loss of SUMO chains leads to sensitivity to RS-generating drugs (methyl methanesulfonate (MMS) and hydroxyurea (HU)) but not to phleomycin-induced DSBs or UV-mediated DNA damage (Supple- mentary Fig. 2a).
PMID:41330900	FYPO:0003183	normal growth on phleomycin	Loss of SUMO chains leads to sensitivity to RS-generating drugs (methyl methanesulfonate (MMS) and hydroxyurea (HU)) but not to phleomycin-induced DSBs or UV-mediated DNA damage (Supple- mentary Fig. 2a).
PMID:41330900	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	Loss of SUMO chains leads to sensitivity to RS-generating drugs (methyl methanesulfonate (MMS) and hydroxyurea (HU)) but not to phleomycin-induced DSBs or UV-mediated DNA damage (Supple- mentary Fig. 2a).
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	Loss of SUMO chains leads to sensitivity to RS-generating drugs (methyl methanesulfonate (MMS) and hydroxyurea (HU)) but not to phleomycin-induced DSBs or UV-mediated DNA damage (Supple- mentary Fig. 2a).
PMID:41330900	FYPO:0002573	increased number of Ssb1 foci [has_penetrance] 60	Loss of SUMO chains led to elevated Ssb3-YFP (RPA) foci in untreated SUMO-KallR cells, though less than in SUMOΔ (Fig. 1a and Supplementary Fig. 1d).
PMID:41330900	FYPO:0002573	increased number of Ssb1 foci [has_penetrance] 20	Loss of SUMO chains led to elevated Ssb3-YFP (RPA) foci in untreated SUMO-KallR cells, though less than in SUMOΔ (Fig. 1a and Supplementary Fig. 1d).
PMID:41330900	FYPO:0004516	decreased number of Rad52 foci during vegetative growth	Notably, immuno uorescence on rad52-Schain showed that it can reduce formation of Rad52 foci compared to WT and suppress excessive formation of repair foci in the absence of SUMO chains (Fig. 7f and Supplementary Fig. 13c).
PMID:41330900	FYPO:0003410	increased spatial extent of CENP-A containing chromatin assembly	On all three chromosomes, SUMO-KallR cells showed excessive Cnp1 binding to the central centromeric domain and spreading into the entire otr region (Fig. 2g and Supplementary Fig. 5c, d, compare blue signal of SUMO-KallR vs red corresponding to WT; green line marks untagged control).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] high	On the other hand, rad52-Schain markedly increased the sensitivity of pcn1-K164R mutant on MMS and TBZ (Supplementary Fig. 14b).
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	On the other hand, rad52-Schain markedly increased the sensitivity of pcn1-K164R mutant on MMS and TBZ (Supplementary Fig. 14b).
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	On the other hand, rad52-Schain markedly increased the sensitivity of pcn1-K164R mutant on MMS and TBZ (Supplementary Fig. 14b).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] high	On the other hand, rad52-Schain markedly increased the sensitivity of pcn1-K164R mutant on MMS and TBZ (Supplementary Fig. 14b).
PMID:41330900	FYPO:0005619	increased level of sumoylated protein in cell [assayed_protein] PomBase:SPBC16D10.09	Pcn1-K164R-HF showed a markedly reduced ubiquitin signal, but slightly increased SUMOylation com- pared to Pcn1-HF (Fig. 5b).
PMID:41330900	FYPO:0005226	decreased level of ubiquitinated protein in cell [has_severity] high [assayed_protein] PomBase:SPBC16D10.09	Pcn1-K164R-HF showed a markedly reduced ubiquitin signal, but slightly increased SUMOylation com- pared to Pcn1-HF (Fig. 5b).
PMID:41330900	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC1259.13	SUMO mutants showed auto- phosphorylation of Chk1 kinase (Fig. 1c).
PMID:41330900	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC1259.13	SUMO mutants showed auto- phosphorylation of Chk1 kinase (Fig. 1c).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] medium	SUMO- KallR mutant showed increased TBZ sensitivity compared to WT (Fig. 2c).
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	SUMO-KallR allele was increasing sensitivity of pcn1-K164R upon global RS induced by MMS. (Fig. 6A)
PMID:41330900	FYPO:0010024	increased mitotic recombination at centromere	SUMO-KallR cells showed a signi cantly elevated recombination frequency at cen- tromeres (Fig. 3e).
PMID:41330900	FYPO:0001357	normal vegetative cell population growth	SUMO-KallR mutation did not impair growth com- pared to the SUMO-devoid strain (pmt3ΔSUMOΔ, Supplementary Fig. 1b).
PMID:41330900	FYPO:0005630	decreased cellular HMW SUMO conjugate level	SUMO-KallR variant exhibited a reduction in high molecular weight (HMW) SUMO conjugates. (Fig. S1C)
PMID:41330900	FYPO:0010026	abolished mitotic recombination at centromere	Strikingly, Rad52-Schain abolished centromeric recombination in both WT and SUMO-KallR backgrounds (Fig. 7e).
PMID:41330900	FYPO:0010027	normal mitotic recombination frequency at centromere	The pcn1-K164R mutation reduced the elevated recombination seen in SUMO-KallR cells (Fig. 6d)
PMID:41330900	FYPO:0010027	normal mitotic recombination frequency at centromere	The pcn1-K164R mutation reduced the elevated recombination seen in SUMO-KallR cells (Fig. 6d)
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] low	The rad52-Schain mutant exhibited milder sensitivity to MMS than rad52Δ mutant. (Fig. 7D)
PMID:41330900	FYPO:0005226	decreased level of ubiquitinated protein in cell [assayed_protein] PomBase:SPBC16D10.09	This hyper-ubiquitination depended on Rad8 activity, as shown by analysis of Pcn1-HF in rad8Δ SUMO-KallR (Fig. 6c and Supplementary Fig. 12b).
PMID:41330900	FYPO:0005226	decreased level of ubiquitinated protein in cell [assayed_protein] PomBase:SPBC16D10.09	This hyper-ubiquitination depended on Rad8 activity, as shown by analysis of Pcn1-HF in rad8Δ SUMO-KallR (Fig. 6c and Supplementary Fig. 12b).
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	Upon shift to the restrictive temperature (34 °C), slx8-29 cells accumulated HMW SUMO conjugates, showed reduced viability, and became hyper- sensitive to HU, MMS, and TBZ, in a manner dependent on SUMO chains (Supplementary Fig. 7a, b).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] high	Upon shift to the restrictive temperature (34 °C), slx8-29 cells accumulated HMW SUMO conjugates, showed reduced viability, and became hyper- sensitive to HU, MMS, and TBZ, in a manner dependent on SUMO chains (Supplementary Fig. 7a, b).
PMID:41330900	FYPO:0005629	increased cellular HMW SUMO conjugate level	Upon shift to the restrictive temperature (34 °C), slx8-29 cells accumulated HMW SUMO conjugates, showed reduced viability, and became hyper- sensitive to HU, MMS, and TBZ, in a manner dependent on SUMO chains (Supplementary Fig. 7a, b).
PMID:41330900	FYPO:0005630	decreased cellular HMW SUMO conjugate level	Upon shift to the restrictive temperature (34 °C), slx8-29 cells accumulated HMW SUMO conjugates, showed reduced viability, and became hyper- sensitive to HU, MMS, and TBZ, in a manner dependent on SUMO chains (Supplementary Fig. 7a, b).
PMID:41330900	FYPO:0005630	decreased cellular HMW SUMO conjugate level	Upon shift to the restrictive temperature (34 °C), slx8-29 cells accumulated HMW SUMO conjugates, showed reduced viability, and became hyper- sensitive to HU, MMS, and TBZ, in a manner dependent on SUMO chains (Supplementary Fig. 7a, b).
PMID:41330900	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	Upon shift to the restrictive temperature (34 °C), slx8-29 cells accumulated HMW SUMO conjugates, showed reduced viability, and became hyper- sensitive to HU, MMS, and TBZ, in a manner dependent on SUMO chains (Supplementary Fig. 7a, b).
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	Upon shift to the restrictive temperature (34 °C), slx8-29 cells accumulated HMW SUMO conjugates, showed reduced viability, and became hyper- sensitive to HU, MMS, and TBZ, in a manner dependent on SUMO chains (Supplementary Fig. 7a, b).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] high	Upon shift to the restrictive temperature (34 °C), slx8-29 cells accumulated HMW SUMO conjugates, showed reduced viability, and became hyper- sensitive to HU, MMS, and TBZ, in a manner dependent on SUMO chains (Supplementary Fig. 7a, b).
PMID:41330900	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	Upon shift to the restrictive temperature (34 °C), slx8-29 cells accumulated HMW SUMO conjugates, showed reduced viability, and became hyper- sensitive to HU, MMS, and TBZ, in a manner dependent on SUMO chains (Supplementary Fig. 7a, b).
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] medium	Upon shift to the restrictive temperature (34 °C), slx8-29 cells accumulated HMW SUMO conjugates, showed reduced viability, and became hyper- sensitive to HU, MMS, and TBZ, in a manner dependent on SUMO chains (Supplementary Fig. 7a, b).
PMID:41330900	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	Upon shift to the restrictive temperature (34 °C), slx8-29 cells accumulated HMW SUMO conjugates, showed reduced viability, and became hyper- sensitive to HU, MMS, and TBZ, in a manner dependent on SUMO chains (Supplementary Fig. 7a, b).
PMID:41330900	FYPO:0010021	increased duration of double-strand break repair via homologous recombination	WT completed genome duplication during the course of the experiment, whereas the SUMO-KallR mutant displayed delayed resolution of replication intermediates (Supplementary Fig. 2b, c).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] high	We also found that the triple mutant pcn1-K164R rad52-Schain SUMO-KallR was exhibiting the same pheno- type as the rad52-Schain pcn1-K164R strain on TBZ plates (Supplemen- tary Fig. 14c).
PMID:41330900	FYPO:0006282	decreased mitotic recombination at chromosome arms	We also measured the rate of mitotic recombi- nation on chromosome arm using the ade6-L469-his3-ade6-M375 assay (Fig. 3f)41. Strikingly, we found a decreased rate of intrachro- mosomal recombination in SUMO-KallR compared to WT cells (Fig. 3g).
PMID:41330900	FYPO:0000972	increased number of Rad52 foci during vegetative growth [has_penetrance] 10	We also noticed accumulation of Rad52 foci in SUMO-KallR mutant, indicating increased spontaneous DNA damage or compromised disassembly of protein complexes at DNA damage foci (Fig. 1b and Supplementary Fig. 1e).
PMID:41330900	FYPO:0002774	increased level of ubiquitinated protein in cell during vegetative growth [assayed_protein] PomBase:SPBC16D10.09	We then examined PCNA modi cation by Ni-NTA pulldown in WT and SUMO-KallR strains and found that loss of SUMO chains in SUMO-KallR led to increased polyubiquitination of Pcn1-HF (Fig. 6b and Supplementary Fig. 12a).
PMID:41330900	FYPO:0010022	normal number of Rad52 foci during cellular response to methyl methanesulfonate	While SUMO- KallR cells showed more Rad52 foci in logarithmic culture, MMS exposure equalized foci numbers between WT and mutant (Supple- mentary Fig. 3c).
PMID:41330900	FYPO:0000091	sensitive to thiabendazole [has_severity] high	While the SUMOΔ strain was inviable on TBZ. (Fig. 2C)
PMID:41330900	FYPO:0000089	sensitive to methyl methanesulfonate [has_severity] high	deletion of rad8 + E3 ubiquitin ligase, which is required for TS activation, suppressed SUMO-KallR TBZ sensitivity similarly to pcn1-K164R, but increased sensitivity of rad8Δ to MMS. (Fig. 6A)
PMID:41330900	FYPO:0000964	normal growth on thiabendazole	deletion of rad8 + E3 ubiquitin ligase, which is required for TS activation, suppressed SUMO-KallR TBZ sensitivity similarly to pcn1-K164R. (Fig. 6A)
PMID:41330900	FYPO:0000964	normal growth on thiabendazole	deletion of rad8 + E3 ubiquitin ligase, which is required for TS activation, suppressed SUMO-KallR TBZ sensitivity similarly to pcn1-K164R. (Fig. 6A)
PMID:41330900	FYPO:0005630	decreased cellular HMW SUMO conjugate level [assayed_protein] PomBase:SPBC16D10.09 [has_severity] high	the appearance of higher-molecular-weight bands depended on Pli1, not Nse2. These higher SUMO-conjugated forms were absent in extracts from SUMO-KallR and pli1Δ mutants, suggesting attachment of SUMO chains to PCNA. (Fig. 5A)
PMID:41330900	FYPO:0005630	decreased cellular HMW SUMO conjugate level [assayed_protein] PomBase:SPBC16D10.09 [has_severity] low	the appearance of higher-molecular-weight bands depended on Pli1, not Nse2. These higher SUMO-conjugated forms were absent in extracts from SUMO-KallR and pli1Δ mutants, suggesting attachment of SUMO chains to PCNA. (Fig. 5A)
PMID:41330900	FYPO:0005630	decreased cellular HMW SUMO conjugate level [assayed_protein] PomBase:SPBC16D10.09 [has_severity] high	the appearance of higher-molecular-weight bands depended on Pli1, not Nse2. These higher SUMO-conjugated forms were absent in extracts from SUMO-KallR and pli1Δ mutants, suggesting attachment of SUMO chains to PCNA. (Fig. 5A)
PMID:41330900	FYPO:0000964	normal growth on thiabendazole	under TBZ exposure, pcn1-K164R muta- tion was bene cial for cells devoid of SUMO chains (Fig. 6a).
PMID:41330900	FYPO:0000964	normal growth on thiabendazole	under TBZ exposure, pcn1-K164R muta- tion was bene cial for cells devoid of SUMO chains (Fig. 6a).
PMID:41330900	FYPO:0002574	normal protein localization to centromere during vegetative growth	we monitored Rad52-GFP colocaliza- tion with the centromere marker Mis6-RFP and found that enhanced Rad52-centromeres interaction in SUMO-KallR was reduced in the pcn1-K164R SUMO-KallR double mutant (Fig. 6e and Supplementary Fig. 12c).
PMID:41330900	FYPO:0007295	increased protein localization to CENP-A containing chromatin [has_penetrance] 13 [assayed_protein] PomBase:SPCC23B6.05c	we observed a twofold increase in RPA-centromere colocali- zation in SUMO-KallR mutant (~ 25% of cells) compared to WT (~ 12% of cells, Fig. 2b).
PMID:41330900	FYPO:0002151	inviable spore	we observed by tetrad dissection, that all the double mutants supposed to bear rad52Δ pcn1-K164R mutations were not able to ger- minate (Supplementary Fig. 14a).
PMID:41330900	FYPO:0006992	normal chromatin silencing at centromere otr1R	we showed that intro- duction of SUMO-KallR into the swi6Δ background (abolished het- erochromatin formation35) or WT did not affect the growth on 5-FOA and selective media (Supplementary Fig. 4b, c).
PMID:41335110	GO:1990819	mating projection actin fusion focus	(comment distal to Myo52) In contrast, exocyst components Exo70, Exo84, and Sec6, as well as the secretory vesicle– associated Rab GTPases Ypt2 and Ypt3 (Craighead et al., 1993; Cheng et al., 2002), all initially localized close to Myo52, with clear overlap in traces at times 60–100 min before fusion (Fig. S2 B).
PMID:41335110	GO:1990819	mating projection actin fusion focus	(comment: colocalized with Fus1) In contrast, exocyst components Exo70, Exo84, and Sec6, as well as the secretory vesicle– associated Rab GTPases Ypt2 and Ypt3 (Craighead et al., 1993; Cheng et al., 2002), all initially localized close to Myo52, with clear overlap in traces at times 60–100 min before fusion (Fig. S2 B).
PMID:41335110	GO:1990819	mating projection actin fusion focus	(comment: colocalized with Myo52) In contrast, exocyst components Exo70, Exo84, and Sec6, as well as the secretory vesicle– associated Rab GTPases Ypt2 and Ypt3 (Craighead et al., 1993; Cheng et al., 2002), all initially localized close to Myo52, with clear overlap in traces at times 60–100 min before fusion (Fig. S2 B).
PMID:41335110	FYPO:0006503	abnormal protein localization to actin fusion focus [assayed_protein] PomBase:SPCC1919.10c	(comment: colocalized with Myo52) In contrast, in fus1Δ cells, Myo52 decorated a wide region at the fusion site (Fig. 4 A) (Dudin et al., 2015).
PMID:41335110	GO:1990819	mating projection actin fusion focus	(comment: distal to Myo52) In contrast, exocyst components Exo70, Exo84, and Sec6, as well as the secretory vesicle– associated Rab GTPases Ypt2 and Ypt3 (Craighead et al., 1993; Cheng et al., 2002), all initially localized close to Myo52, with clear overlap in traces at times 60–100 min before fusion (Fig. S2 B).
PMID:41335110	GO:1990819	mating projection actin fusion focus	(comment: distal to Myo52) In contrast, exocyst components Exo70, Exo84, and Sec6, as well as the secretory vesicle– associated Rab GTPases Ypt2 and Ypt3 (Craighead et al., 1993; Cheng et al., 2002), all initially localized close to Myo52, with clear overlap in traces at times 60–100 min before fusion (Fig. S2 B).
PMID:41335110	GO:1990819	mating projection actin fusion focus	(comment: distal to Myo52) In contrast, exocyst components Exo70, Exo84, and Sec6, as well as the secretory vesicle– associated Rab GTPases Ypt2 and Ypt3 (Craighead et al., 1993; Cheng et al., 2002), all initially localized close to Myo52, with clear overlap in traces at times 60–100 min before fusion (Fig. S2 B).
PMID:41335110	GO:1990819	mating projection actin fusion focus	(comment: distal to Myo52) In contrast, exocyst components Exo70, Exo84, and Sec6, as well as the secretory vesicle– associated Rab GTPases Ypt2 and Ypt3 (Craighead et al., 1993; Cheng et al., 2002), all initially localized close to Myo52, with clear overlap in traces at times 60–100 min before fusion (Fig. S2 B).
PMID:41335110	GO:1990819	mating projection actin fusion focus	(comment: distal to Myo52, progressively more compact) etails of the map in h+ cells only. The distal localization of Myo51 was mirrored by that of tropomyosin Cdc8, which decorates linear actin filaments (Fig. 2 B) (Hatano et al., 2022)
PMID:41335110	GO:1990819	mating projection actin fusion focus	(comment: membrane-proximal relative to Myo52) In the zone proximal to the partner cell, we located the transmembrane proteins Dni1 and Dni2, involved in membrane merging, in addition to Scd2 and Prm1 (Fig. 2 C)
PMID:41335110	GO:1990819	mating projection actin fusion focus	(comment: membrane-proximal relative to Myo52) In the zone proximal to the partner cell, we located the transmembrane proteins Dni1 and Dni2, involved in membrane merging, in addition to Scd2 and Prm1 (Fig. 2 C)
PMID:41335110	GO:1990819	mating projection actin fusion focus	(comment: membrane-proximal relative to Myo52) In the zone proximal to the partner cell, we located the transmembrane proteins Dni1 and Dni2, involved in membrane merging, in addition to Scd2 and Prm1 (Fig. 2 C)
PMID:41335110	GO:1990819	mating projection actin fusion focus	(comment: membrane-proximal relative to Myo52) In the zone proximal to the partner cell, we located the transmembrane proteins Dni1 and Dni2, involved in membrane merging, in addition to Scd2 and Prm1 (Fig. 2 C)
PMID:41335110	FYPO:0006503	abnormal protein localization to actin fusion focus [assayed_protein] PomBase:SPBC106.20	(comment: wide signal and membrane-proximal relative to Myo52) In myo52Δtail cells, like in myo52AID , the Exo70-GFP remained localized to cell poles ....However, both its centroid position and distribution width were distinct from that in WT cells. In WT cells, Exo70 was cell-internal relative to Myo52 (Fig. 3 F)
PMID:41335110	GO:1990819	mating projection actin fusion focus	(distal to Myo52, progressively more compact) We confirmed this function by measuring the lateral distribution of Fus1 along the cell–cell contact area (perpendicular to the fusion axis), which was indeed wider in myo51Δ than WT cells (see below Fig. 6, A and B).
PMID:41335110	FYPO:0007683	wide actin fusion focus [has_severity] high	Myo52 depletion also led to a wider Fus1 distribution in a myo51Δ mutant background, indicating both myosins contribute to focus condensation through distinct pathways.
PMID:41335110	GO:0000146	microfilament motor activity [has_input] PomBase:SPAC20G4.02c [part_of] protein transport to mating projection actin fusion focus [occurs_in] mating projection tip	Myo52 transports Fus1, Together, the association of Fus1 with Myo52, their overlapping localizations, and the Myo52-dependent long-range movement of Fus1 demonstrate that the formin is a cargo of the myosin V.
PMID:41335110	FYPO:0007096	decreased protein localization to actin fusion focus [has_severity] high [assayed_protein] PomBase:SPBC106.20	Similar to Ypt3, Exo70 still localized at the fusion site, albeit weakly, in myo52AID cells (Fig. 3 D)
PMID:41335110	FYPO:0006503	abnormal protein localization to actin fusion focus [assayed_protein] PomBase:SPAC20G4.02c	Similarly, in cells in which Fus1 fails to condense due to deletion of its IDR (fus1ΔIDR) (Billault- Chaumartin et al., 2022b), Fus1 and Myo52 exhibited similarly wider distributions (Fig. 4, B and C).
PMID:41335110	FYPO:0006503	abnormal protein localization to actin fusion focus [assayed_protein] PomBase:SPCC1919.10c	Similarly, in cells in which Fus1 fails to condense due to deletion of its IDR (fus1ΔIDR) (Billault- Chaumartin et al., 2022b), Fus1 and Myo52 exhibited similarly wider distributions (Fig. 4, B and C).
PMID:41335110	FYPO:0007875	normal protein localization to actin fusion focus [assayed_protein] PomBase:SPCC1919.10c	Thus, the organization of the actin fusion focus is not grossly altered in myo52Δtail mutant cells, even though these mutants fail to concentrate cell wall digestive enzymes and are largely fusion-deficient (Dudin et al., 2015)
PMID:41335110	GO:0000146	microfilament motor activity [part_of] Golgi to plasma membrane transport [occurs_in] mating projection tip	Together, these data indicate that exocyst and vesicles can be captured at the plasma membrane in the absence of functional Myo52, but that binding of the myosin V Myo52 to secretory vesicles promotes their early transport to the fusion site and their concentration on the fusion focus.
PMID:41335110	FYPO:0007096	decreased protein localization to actin fusion focus [has_severity] high [assayed_protein] PomBase:SPAC18G6.03	Upon Myo52 depletion, Ypt3 did not accumulate at the fusion focus (Fig. 3 C).
PMID:41335110	FYPO:0007683	wide actin fusion focus [has_severity] medium	Upon Myo52AID depletion, Fus1 occupied a wider region than in WT cells (Fig. 6, A and B), in agreement with previous measurement of Fus1 in myo52Δ cells (in which both partner cells were mutant)
PMID:41354344	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_enzyme] PomBase:SPAC23C4.12	A kinase-dead mutant, Hhp2-K41R (39), was also phosphorylated in mitotically-arrested cells, although not as extensively as wild type Hhp2, indicating that Hhp2 is both autophosphorylated and phosphorylated by another kinase(s).
PMID:41354344	FYPO:0001838	decreased protein phosphorylation during vegetative growth [has_severity] high	Almost all slower mobility bands were abolished in both the 3A and 7A mutants, with a few up-shifted bands remaining in the 3A mutant (denoted with dots) that were absent in the 7A mutant (Fig. 3C).
PMID:41354344	FYPO:0004318	abolished mitotic spindle assembly checkpoint	Consistent with Hhp2’s required function in the Dma1-dependent checkpoint (36, 39), catalytically inactive nda3-KM311 hhp2-K41R-7A cells were not able to hold the checkpoint arrest as long as nda3-KM311 cells (Fig. 4A).
PMID:41354344	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPAC23C4.12 [happens_during] mitotic M phase	Hhp2 auto- phosphorylates at four residues and is phosphorylated by the cyclin-dependent kinase Cdk1 at three additional sites.
PMID:41354344	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPAC23C4.12 [happens_during] mitotic M phase	Hhp2 auto- phosphorylates at four residues and is phosphorylated by the cyclin-dependent kinase Cdk1 at three additional sites. ...A kinase-dead mutant, Hhp2-K41R (39), was also phosphorylated in mitotically-arrested cells, although not as extensively as wild type Hhp2, indicating that Hhp2 is both autophosphorylated and phosphorylated by another kinase(s).
PMID:41354344	FYPO:0002638	increased activation of mitotic spindle assembly checkpoint	In contrast, nda3-KM311 hhp2-7A cells held the arrest longer than nda3-KM311 cells (Fig. 4A).
PMID:41354344	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C4.12 [present_during] mitotic M phase	In contrast, we found that Hhp2-HA 3 -TAP was highly phosphorylated in both mitotically-arrested strains, as detected by the slower mobility forms on SDS-PAGE, but slower mobility forms were barely detectable in asynchronously growing cells that are primarily in interphase (Fig. 1A). Using information annotated from global phosphoproteomic screens of S. pombe (60), and phosphopeptide mapping of individual and combination alanine site mutants, we determined that the major auto- phosphorylation sites were S307, T309, T329, and S381 (Fig. 2A and S2, B and C).
PMID:41354344	FYPO:0001838	decreased protein phosphorylation during vegetative growth [has_severity] high [assayed_protein] PomBase:SPAC23C4.12	Inhibition of Cdk1/Cdc2 activity signifi- cantly reduced Hhp2 phosphorylation (Fig. 3E), confirming that Cdk1 is responsible for the majority of Hhp2 mitotic phosphorylation.
PMID:41354344	FYPO:0001357	normal vegetative cell population growth	Of note, the hhp2-3A and hhp2-7A strains grew comparably to wildtype at a range of temperatures (Fig. S3A), and there was no effect on protein levels or cellular localization of any of these endoge- nous phosphosite mutations when they were tagged with either FLAG 3 or mNeonGreen at their C-terminus (Fig.3D and S3D).
PMID:41354344	FYPO:0000833	normal protein level during vegetative growth	The abundance of the Hhp2-4A mutant protein was also comparable to that of wildtype Hhp2 (Fig. 2B).
PMID:41354344	FYPO:0006490	decreased duration of mitotic M phase	Unexpectedly, the duration of mitosis and cytokinesis (from SPB separation that indicates the onset of mitotic spindle formation to the completion of CR constriction) was accelerated in hhp2-7A compared to the wildtype (9 min, 1.24-fold faster) (Fig. 4, B and C), although hhp2Δ showed similar kinetics to wild- type.
PMID:41354344	FYPO:0002085	normal vegetative cell growth	Unlike for hhp1, we did not observe any differences in growth between the hhp2 4A and 4N mutants and used the strains interchangeably; they also both grew similarly to wild-type cells and were not sen- sitive to the DNA-damaging agent, hydroxyurea, as are hhp2Δ cells (Fig. S3A).
PMID:41354344	FYPO:0002085	normal vegetative cell growth	Unlike for hhp1, we did not observe any differences in growth between the hhp2 4A and 4N mutants and used the strains interchangeably; they also both grew similarly to wild-type cells and were not sen- sitive to the DNA-damaging agent, hydroxyurea, as are hhp2Δ cells (Fig. S3A).
PMID:41354344	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C4.12 [present_during] mitotic M phase	Using information annotated from global phosphoproteomic screens of S. pombe (60), and phosphopeptide mapping of individual and combination alanine site mutants, we determined that the major auto- phosphorylation sites were S307, T309, T329, and S381 (Fig. 2A and S2, B and C).
PMID:41354344	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C4.12 [present_during] mitotic M phase	Using information annotated from global phosphoproteomic screens of S. pombe (60), and phosphopeptide mapping of individual and combination alanine site mutants, we determined that the major auto- phosphorylation sites were S307, T309, T329, and S381 (Fig. 2A and S2, B and C).
PMID:41354344	MOD:00696	phosphorylated residue [added_by] PomBase:SPAC23C4.12 [present_during] mitotic M phase	Using information annotated from global phosphoproteomic screens of S. pombe (60), and phosphopeptide mapping of individual and combination alanine site mutants, we determined that the major auto- phosphorylation sites were S307, T309, T329, and S381 (Fig. 2A and S2, B and C).
PMID:41354344	FYPO:0006822	viable small vegetative cell with normal cell growth rate	We also found that the cell length of septated hhp2-7A cells was �1 μm shorter than that of wildtype cells (Fig. 4D), suggesting a shortened G2 phase in hhp2-7A cells. These observations indicate that Hhp2 promotes cell proliferation, particularly when it is relieved of mitotic inhibition.
PMID:41354344	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC23C4.12	We found thatin the individual T345A and S358A mutants, the lowest mobility bands were significantly decreased, and the doublemutant was even less phosphorylated (Fig. S3C), indicatingthat T345 and S358 are mitotic Hhp2 phosphorylation sites targeted by another kinase(s).
PMID:41354344	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPAC23C4.12	We found thatin the individual T345A and S358A mutants, the lowest mobility bands were significantly decreased, and the doublemutant was even less phosphorylated (Fig. S3C), indicatingthat T345 and S358 are mitotic Hhp2 phosphorylation sites targeted by another kinase(s).
PMID:41354344	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	We observed a negative genetic interaction between hhp2Δ and the temperature-sensitive plo1-ts35 allele Furthermore, hhp2-7A suppressed the temperature sensitivity of plo1-ts35 at 34 ◦ C (Fig. 4E). at 32 ◦ C, the semi- restrictive temperature (Fig. S4C).
PMID:41354344	FYPO:0000082	decreased cell population growth at high temperature [has_severity] low	We observed a negative genetic interaction between hhp2Δ and the temperature-sensitive plo1-ts35 allele Furthermore, hhp2-7A suppressed the temperature sensitivity of plo1-ts35 at 34 ◦ C (Fig. 4E). at 32 ◦ C, the semi- restrictive temperature (Fig. S4C).
PMID:41354344	FYPO:0002700	increased protein kinase activity	When these residues were all mutated to alanines to generate Hhp2-4A, the major phos- phopeptides were abolished (Fig. S2B, middle panel). As anticipated, MBP-Hhp2-4A showed enhanced kinase activity (Fig. S2D), to approximately the same extent as dephos- phorylated endogenous Hhp2 (Fig. 1C).
PMID:4154968	GO:0004354	L-glutamate dehydrogenase (NADP+) activity	"(comment: well this is a slight fudge. The activity was assayed and present. We know this is glutamate dehydrogenase...so sone and will make ""published"")"
PMID:41850284	GO:0045324	late endosome to vacuole transport	(comment: blocked by the CK-666 inhibitor) (By contrast, upon CK666 treatment 4 min after FM4-64 addition, effectively blocking Arp2/3 function as FM4- 64 reaching endosomes, FM4-64 did not progress to the vacu- ole and remained associated with endosomes (Figure 4B).)
PMID:41850284	GO:0045324	late endosome to vacuole transport	(comment: blocked by the CK-666 inhibitor) (By contrast, upon CK666 treatment 4 min after FM4-64 addition, effectively blocking Arp2/3 function as FM4- 64 reaching endosomes, FM4-64 did not progress to the vacu- ole and remained associated with endosomes (Figure 4B).)
PMID:41850284	GO:0005768	endosome	colocalization with FM4-64
PMID:41850284	GO:0005768	endosome	colocalization with Syb1
PMID:41850284	GO:0005768	endosome	transient localization
PMID:4309177	GO:0003938	IMP dehydrogenase activity	(comment: activated by ATP)
PMID:4698209	GO:0004794	threonine deaminase activity	(comment: CHECK inhibited_by CHEBI:17191)
PMID:4698210	GO:0003984	acetolactate synthase activity	(comment: CHECK inhibited_by CHEBI:27266)
PMID:4708672	GO:0004019	adenylosuccinate synthase activity	The enzyme is strongly inhibited by AMP and GMP. Whereas GMP seems to act by a direct competition for the GTP binding site, AMP appears as an allosteric effector, showing at non-saturating substrate concentrations a homotropic effect as well as a heterotropic effect upon the GTP and aspartate binding
PMID:4708672	GO:0016208	AMP binding	The enzyme is strongly inhibited by AMP and GMP. Whereas GMP seems to act by a direct competition for the GTP binding site, AMP appears as an allosteric effector, showing at non-saturating substrate concentrations a homotropic effect as well as a heterotropic effect upon the GTP and aspartate binding
PMID:4708672	GO:0019002	GMP binding	The enzyme is strongly inhibited by AMP and GMP. Whereas GMP seems to act by a direct competition for the GTP binding site, AMP appears as an allosteric effector, showing at non-saturating substrate concentrations a homotropic effect as well as a heterotropic effect upon the GTP and aspartate binding
PMID:4821071	GO:0003984	acetolactate synthase activity	(comment: CHECK activated_by FAD , inhibited_by L-valine)
PMID:6094012	FYPO:0000134	branched, elongated, multiseptate cell	(comment: CHECK actually this only occurs in 30% of cells.. I don't know if it is viable or inviable)
PMID:6094012	FYPO:0001972	abnormal cell separation after cytokinesis resulting in septated cell	(comment: CHECK parent child relationship with term above requested)
PMID:6526818	GO:0051009	O-acetylhomoserine sulfhydrylase activity [part_of] L-homocysteine biosynthetic process	(comment: CHECK inhibited by methionine)
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A)
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	"(Fig. 1A) (comment: EXP) The transition point for cdc1 is not advanced in a cdc1.7 cdc2-1w mutant (0.64). An asynchronous population of a cdc1-7cdc2-1w mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the cdc1 gene and the number of cells that went on to divide was similar to a cdc1-7 mutant. The transition point for cdc1 (0.58) is not advanced in a cdc1.7 cdc2-2w mutant (comment: cdc2-2w is the same change as cdc2-1w, but also consider comment transferred from duplicate annotation: ""I think this allele cdc2-2w maybe a typo or a changed annotation since this paper was published and is actually cdc2-3w"")."
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A) The cdc1 gene has a execution point of ~0.62 which means its function is completed just before entry into mitosis. An asynchronous population of the cdc1-7 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the gene and the number of cells that went on to divide was measured
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A) The cdc1 gene has a execution point of ~0.65 which means its function is completed just before entry into mitosis. An asynchronous population of the cdc1-7 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the gene and the number of cells that went on to divide was measured
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A) The transition point for cdc2 (0.68) is not advanced using a cdc2.M63 wee1.6 mutant
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A) The transition point for cdc2 (0.74) is not advanced using a cdc2.M35 wee1.6 mutant
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A) The transition point for cdc2 is 0.65 using cdc2.33
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A) The transition point for cdc2 is 0.65 using cdc2.M26
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A) The transition point for cdc2 is 0.65 using cdc2.M55
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A) The transition point for cdc2 is 0.66 using cdc2.M35
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A) The transition point for cdc2 is 0.68 using cdc2.L7
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A) The transition point for cdc2 is 0.70 using cdc2.M63
PMID:6828164	FYPO:0003449	abnormal cell cycle arrest at mitotic G1/S phase transition	(Fig. 1A) The transition point for cdc2 is advanced from 0.69 to 0.48 using a cdc2.33 wee1 [more...]
PMID:6828164	FYPO:0003449	abnormal cell cycle arrest at mitotic G1/S phase transition	(Fig. 1A) The transition point for cdc27 is advanced from 0.63 to 0.22 in a cdc27-K3 wee1.6 mutant. An asynchronous population of a cdc1-7 wee1.6 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the cdc27 gene and the number of cells that went on to divide was increased compared to a cdc27-K3 mutant
PMID:6828164	FYPO:0003449	abnormal cell cycle arrest at mitotic G1/S phase transition	(Fig. 1A) The transition point s advanced from 0.68 to 0.29 in a cdc1.7 wee1.6 mutant. An asynchronous population of a cdc1-7 wee1.6 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the cdc1 gene and the number of cells that went on to divide was increased compared to a cdc1-7 mutant
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A, Table 1) cdc13 transition point (0.78) is not advanced in a cdc13-117 wee1.6 mutant
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A, Table 1) cdc13 transition point is 0.69 using a cdc13-117 mutant
PMID:6828164	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(Fig. 1A, Table 1) cdc27 transition point is 0.62 using a cdc27.K3 mutant
PMID:6828164	FYPO:0002516	premature mitotic G2/M phase transition	(comment: ???)
PMID:6828164	FYPO:0002516	premature mitotic G2/M phase transition	(comment: TP. 0.33)
PMID:6828164	FYPO:0001492	viable elongated vegetative cell [has_severity] medium	(comment: cell size at separation is 16.7µm compared to 12.8µm for wild type)
PMID:6828164	FYPO:0001492	viable elongated vegetative cell [has_severity] high	(comment: cell size at separation is 22.4µm compared to 12.8µm for wild type)
PMID:6828164	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(comment: cell size at septation is 10.3µm)
PMID:6828164	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(comment: cell size at septation is 8.4µm)
PMID:6828164	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(comment: cell size at septation is 8.5µm)
PMID:6828164	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(comment: cell size at septation is 8.7µm)
PMID:6828164	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(comment: cell size at septation is 8.9µm)
PMID:6828164	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(comment: cell size at septation is 8.9µm)
PMID:6828164	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(comment: cell size at septation is 9.6µm)
PMID:6828164	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(commnet; cell size at septation is 9.5µm in cdc2-1w (9.7µm in cdc2-2w))
PMID:6828164	FYPO:0003449	abnormal cell cycle arrest at mitotic G1/S phase transition	The transition point for cdc1 is advanced in a cdc1.P13 wee1.6 mutant from 0.62 to 0.33. An asynchronous population of a cdc1-P13 wee1.6 mutant was shifted from 25°C to the restrictive temperature of 36°C to inactivate the cdc1 gene and the number of cells that went on to divide was increased compared to a cdc1-7 mutant
PMID:6828164	FYPO:0003449	abnormal cell cycle arrest at mitotic G1/S phase transition	The transition point for cdc2 is advanced from 0.65 to 0.53 using a cdc2.M26 wee1.6 mutant
PMID:6828164	FYPO:0003449	abnormal cell cycle arrest at mitotic G1/S phase transition	The transition point for cdc2 is advanced from 0.68 to 0.47 using a cdc2.L7 wee1.6 mutant
PMID:689088	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(comment: CHECK at division)
PMID:6943408	FYPO:0003485	abolished DNA synthesis	(comment: After release from HU block, cells can undergo one round of division without DNA replication)
PMID:6943408	FYPO:0003485	abolished DNA synthesis	(comment: After release from HU block, cells can undergo one round of division without DNA replication)
PMID:6943408	FYPO:0003485	abolished DNA synthesis	(comment: After release from HU block, cells can undergo one round of division without DNA replication)
PMID:6943408	FYPO:0003738	abnormal mitotic cell cycle arrest with condensed chromosomes	(comment: All nuclei took on a granular appearance and in some nuclei this granularity was clearly resolvable into three densely staining bodies resembling condensed chromosomes) (Fig. 3)
PMID:6943408	FYPO:0001248	abnormal regulation of mitotic DNA replication initiation	(comment: CHECK abolished)
PMID:6943408	FYPO:0000608	abnormal cell cycle arrest in mitotic M phase	(comment: Cells able to undergo normal DNA replication and enter cell division, but fail to divide.)
PMID:6943408	FYPO:0000608	abnormal cell cycle arrest in mitotic M phase	(comment: Cells able to undergo normal DNA replication and enter cell division, but fail to divide.)
PMID:6943408	FYPO:0001982	decreased rate of DNA replication during vegetative growth	(comment: Cells unable to divide, even after DNA replication is completed)
PMID:6943408	FYPO:0001982	decreased rate of DNA replication during vegetative growth	(comment: Cells unable to divide, even after DNA replication is completed)
PMID:6943408	FYPO:0003485	abolished DNA synthesis	(comment: DNA synthesis and cell number increase were rapidly inhibited (data not given but similar to the mitotic mutant cdc 2 in Fig. 5 of Nurse et al. 1976))
PMID:6943408	FYPO:0003485	abolished DNA synthesis	(comment: DNA synthesis and cell number increase were rapidly inhibited (data not given but similar to the mitotic mutant cdc 2 in Fig. 5 of Nurse et al. 1976))
PMID:6943408	FYPO:0003485	abolished DNA synthesis	(comment: DNA synthesis and cell number increase were rapidly inhibited (data not given but similar to the mitotic mutant cdc2 in Fig. 5 of Nurse et al. 1976))
PMID:6943408	FYPO:0003485	abolished DNA synthesis	After release from HU block, cells can undergo one round of division without DNA replication)
PMID:6943408	FYPO:0003485	abolished DNA synthesis	DNA synthesis and cell number increase were rapidly inhibited (data not given but similar to the mitotic mutant cdc 2 in Fig. 5 of Nurse et al. 1976)
PMID:6961452	GO:0004070	aspartate carbamoyltransferase activity	(comment: This was really IGI complemetnation of E-coli pyrB)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: Cells divide at 65% of wild type diploid cell length)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high [has_penetrance] complete	(comment: This mutation is probably allelic with cdc2-56. Cells divide at 10.0 µm. I think it is useful to have it annotated as it is in old literature and people may wonder what it is)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cdc2-1w was previously called wee2-1)
PMID:7262540	FYPO:0001492	viable elongated vegetative cell [has_penetrance] complete [has_severity] high	(comment: cells divide at 10% longer than wild diploid cells at division)
PMID:7262540	FYPO:0001492	viable elongated vegetative cell [has_penetrance] complete [has_severity] high	(comment: cells divide at 10% longer than wild diploid cells at division)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells divide at 10.2µm at 25°C)
PMID:7262540	FYPO:0001492	viable elongated vegetative cell [has_penetrance] complete [has_severity] high	(comment: cells divide at 11% longer than wild diploid cells at division)
PMID:7262540	FYPO:0001492	viable elongated vegetative cell [has_penetrance] complete [has_severity] high	(comment: cells divide at 11% longer than wild diploid cells at division)
PMID:7262540	FYPO:0001492	viable elongated vegetative cell [has_penetrance] complete [has_severity] high	(comment: cells divide at 12% longer than wild diploid cells at division)
PMID:7262540	FYPO:0001492	viable elongated vegetative cell [has_penetrance] complete [has_severity] high	(comment: cells divide at 16.7µm at 25°C)
PMID:7262540	FYPO:0001492	viable elongated vegetative cell [has_severity] high [has_penetrance] complete	(comment: cells divide at 22.4µm at 25°C)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells divide at 51% of control cell length at division)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells divide at 56% of the size at division of wild type diploids)
PMID:7262540	FYPO:0001492	viable elongated vegetative cell [has_penetrance] complete [has_severity] medium	(comment: cells divide at 6% longer than wild diploid cells at division)
PMID:7262540	FYPO:0001492	viable elongated vegetative cell [has_penetrance] high [has_severity] medium	(comment: cells divide at 7% longer than wild diploid cells at division)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells divide at 75% of wild type diploid cell length at division at 25°C)
PMID:7262540	FYPO:0001492	viable elongated vegetative cell [has_penetrance] complete [has_severity] medium	(comment: cells divide at 8% longer than wild diploid cells at division)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells divide at 82% of wild diploid size at division)
PMID:7262540	FYPO:0001492	viable elongated vegetative cell [has_penetrance] complete [has_severity] medium	(comment: cells divide at 9% longer than wild diploid cells at division)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells septate at 52% of wild type diploid length)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells septate at 54% of wild type diploid length)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells septate at 56% of wild type diploid length)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells septate at 58% of wild type diploid length)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells septate at 58% of wild type diploid length)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells septate at 77% of wild type diploid length)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells septate at 81% of wild type diploid length)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells septate at 82% of wild type diploid length)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells septate at 85% of wild type diploid length)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] complete [has_severity] high	(comment: cells septate at 87% of wild type diploid length)
PMID:7262540	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] low	(comment: small cell size at division is partially suppressed in the presence of sup3-5 an opal nonsense suppressor mutation in the sup3 tRNA gene. Cells divide at 89% of control cell length at division so are not really normal size)
PMID:7498507	GO:0004725	protein tyrosine phosphatase activity	(comment: CHECK activated_by(CHEBI:16356))
PMID:7501024	FYPO:0001490	inviable elongated vegetative cell	(comment: CHECK salt stress)
PMID:7501024	FYPO:0001490	inviable elongated vegetative cell	(comment: CHECK salt stress)
PMID:7501024	FYPO:0001490	inviable elongated vegetative cell	(comment: CONDITION non-ionic osmotic stress)
PMID:7501454	MOD:00046	O-phospho-L-serine	(comment: CHECK hyperphosphorylated in late S phase; phosphorylated on different sites in S versus G2/M)
PMID:7501454	GO:0003887	DNA-directed DNA polymerase activity	(comment: constant throughout cell cycle)
PMID:7501454	GO:0003697	single-stranded DNA binding	(comment: higher affinity during S phase than G2/M)
PMID:7559598	FYPO:0000280	sterile	data not shown
PMID:7559598	FYPO:0001152	decreased RNA level during nitrogen starvation [assayed_using] PomBase:SPBP4H10.04	data not shown
PMID:7596817	FYPO:0003696	increased cytosolic large ribosomal subunit level	(comment: polysome profile)
PMID:7596817	FYPO:0003695	decreased cytosolic small ribosomal subunit level	(comment: polysome profile)
PMID:7622618	FYPO:0000280	sterile	(comment: evidence is essentially IC, as I inferred sterility from the lack of shmoo formation (h- cells))
PMID:7626804	FYPO:0007761	normal protein phosphorylation during mitotic G2/M transition [assayed_using] PomBase:SPBC11B10.09	(Fig. 1A)
PMID:7626804	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09	(Fig. 1B, C and D) (comment: x = a small phospho peptide of T14Y15. T14 phosphorylation only occurs when wee1 is overexpressed)
PMID:7626804	MOD:00047	O-phospho-L-threonine	(Fig. 1D) peptide 2
PMID:7626804	MOD:00047	O-phospho-L-threonine	(Fig. 1D) peptide 3
PMID:7626804	MOD:00048	O4'-phospho-L-tyrosine [added_by] PomBase:SPCC18B5.03	(Fig. 1D) peptide 3 and peptide1
PMID:7626804	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09	(Fig. 3) (comment: chk1 is not required for T14 phosphorylation by wee1)
PMID:7626804	FYPO:0000648	viable small vegetative cell [has_severity] medium	(Fig. 4A) (comment: cells average size 11.6µm)
PMID:7626804	FYPO:0001492	viable elongated vegetative cell [has_severity] medium	(Fig. 4A) (comment: cells average size 16.6µm)
PMID:7626804	FYPO:0000776	normal protein phosphorylation during vegetative growth [has_severity] medium [assayed_using] PomBase:SPBC11B10.09	(Fig. 4B)
PMID:7626804	FYPO:0002033	abolished protein phosphorylation during vegetative growth [has_severity] medium [assayed_using] PomBase:SPBC11B10.09	(Fig. 4B)
PMID:7626804	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09 [has_penetrance] high	(Fig. 4B)
PMID:7626804	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09 [has_penetrance] high	(Fig. 4B)
PMID:7626804	FYPO:0000648	viable small vegetative cell [has_severity] high	(Fig. 5B) (comment: wee1 is necessary for T14 phosphorylation no peptide 3 is observed when wee1 is deleted)
PMID:7626804	FYPO:0004423	normal protein threonine phosphorylation [assayed_using] PomBase:SPBC11B10.09	(Fig. 7A, B)
PMID:7626804	FYPO:0002678	abolished protein phosphorylation [assayed_using] PomBase:SPBC11B10.09	(Fig. 7A, B)
PMID:7626804	FYPO:0001706	normal mitotic DNA damage checkpoint during cellular response to ionizing radiation	(Fig. 8)
PMID:7626804	FYPO:0002102	normal mitotic DNA damage checkpoint during cellular response to UV	(Fig. 8)
PMID:7626804	FYPO:0002176	viable vegetative cell with normal cell size	(Table 2)
PMID:7626804	FYPO:0000648	viable small vegetative cell [has_severity] medium	(Table 2) (comment: cdc2-T14A is present on multicopy plasmid cells are viable but have a semi wee phenotype)
PMID:7626804	FYPO:0000012	mitotic G2/M phase transition delay [has_severity] medium	data not shown
PMID:7651412	FYPO:0003735	altered DNA binding specificity	(comment: switches specificity from direct repeats to inverted repeats)
PMID:7651414	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPMTR.02	(comment: matmi and matpi)
PMID:7651414	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC23G7.17c	(comment: matmi and matpi)
PMID:7651414	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPMTR.02	(comment: matmi and matpi)
PMID:7651414	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC23G7.17c	(comment: matmi and matpi)
PMID:7651414	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC119.04	(comment: matmi and matpi)
PMID:7657164	FYPO:0004062	increased duration of protein phosphorylation during cellular response to salt stress [assayed_using] PomBase:SPAC24B11.06c	(comment: residue not determined, but probably Y173)
PMID:7687541	GO:0005737	cytoplasm	(Fig. 4)
PMID:7706287	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition	(comment: arrest point determined by H1 kinase activity peak)
PMID:7706287	FYPO:0002522	decreased poly(A)+ mRNA export from nucleus	(comment: assayed for bulk poly(A)+ RNA)
PMID:7706287	FYPO:0000911	increased nuclear RNA level during vegetative growth	(comment: assayed for bulk poly(A)+ RNA)
PMID:7739540	FYPO:0001430	abnormal mitotic cell cycle arrest with unreplicated DNA	(Figure 3b)
PMID:7739540	FYPO:0001430	abnormal mitotic cell cycle arrest with unreplicated DNA	(Figure 3b)
PMID:7739540	FYPO:0001430	abnormal mitotic cell cycle arrest with unreplicated DNA	(Figure 3b)
PMID:7773104	FYPO:0005472	abolished glutamate dehydrogenase (NADP+) activity	(comment: NADP-GDH-defective)
PMID:7774573	FYPO:0001933	abnormal mitotic cell cycle regulation during cellular response to hydroxyurea [has_penetrance] 24	(comment: 24% cells enter mitosis compared to 2% when cdc2+ is not over expressed but they did not say that it was a cut phenotype)
PMID:7774573	FYPO:0000117	abnormal septum assembly [has_penetrance] 76 [has_severity] variable severity	(comment: CHECK Abnormal septum phenotype include misplace septum, multi septa and partially formed septa)
PMID:7774573	FYPO:0000411	normal mitotic cell cycle [has_penetrance] complete	(comment: CHECK cdc2+ is expressed from its own promoter on a multi copy plasmid)
PMID:7774573	FYPO:0003758	mitotic spindle elongation without chromosome separation [has_penetrance] 70	(comment: CHECK child term of abnormal regulation of mitotic metaphase/anaphase transition.)
PMID:7774573	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(comment: CHECK pIRT2suc1 multi copy plasmid partially rescues the pREP5cdc2-DL41 integrant mitotic arrest phenotype and allows formation of micro colonies) (comment: CHECK cdc2-DL45 is also partially rescued)
PMID:7774573	FYPO:0001046	premature mitosis [has_penetrance] high	(comment: CHECK pREP41-DL50 is integrated)
PMID:7774573	FYPO:0000411	normal mitotic cell cycle [has_penetrance] complete	(comment: CHECK pREP5-DL45 is integrated. cdc2+ is expressed from its own promoter on a multi copy plasmid)
PMID:7774573	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase [has_penetrance] 30	(comment: CHECK pREP5cdc2-DL41 is integrated)
PMID:7774573	FYPO:0000446	cell cycle arrest at mitotic G2/M phase transition [has_penetrance] high	(comment: CHECK pRIP45DL45 is integrated). (Figure 6B) (comment: CHECK the 20% of cells that are in mitosis are probably cells that were in mitosis when the culture was shifted to the restrictive temperature)
PMID:7774573	FYPO:0001929	normal cell cycle regulation during cellular response to hydroxyurea [has_penetrance] high	About 75% of cells do not enter mitosis in presence of HU Figure 6A, showing that this mutant does not disrupt normal controls regulating entry into mitosis. pRIP45cdc2-DL45 is integrated cdc2-DL41 has same phenotype but it is not clear if it is under the same conditions
PMID:7774573	FYPO:0000411	normal mitotic cell cycle [has_penetrance] high	DNS
PMID:7774573	FYPO:0000411	normal mitotic cell cycle [has_penetrance] high	DNS
PMID:7774573	FYPO:0000337	abnormal mitosis [has_penetrance] high	DNS
PMID:7774573	FYPO:0000337	abnormal mitosis [has_penetrance] high	DNS
PMID:7774573	FYPO:0005710	abnormal negative regulation of DNA replication initiation resulting in complete rereplication, with mitotic cell cycle arrest [has_penetrance] 20	abnormal mitotic arrest with 4C DNA content Cells undergo an extra round of DNA replication without undergoing cytokinesis.
PMID:7796804	FYPO:0000445	cell cycle arrest in mitotic G1 phase [has_penetrance] high	(Fig. 5A)
PMID:7796804	FYPO:0003449	abnormal cell cycle arrest at mitotic G1/S phase transition [has_penetrance] medium	(Fig. 5A)
PMID:7796804	FYPO:0003449	abnormal cell cycle arrest at mitotic G1/S phase transition [has_penetrance] medium	(Fig. 5A)
PMID:7796804	FYPO:0005933	decreased protein level during mitotic G1 phase [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 5B) (comment: CHECK cdc10-129 cells blocked in G1)
PMID:7796804	FYPO:0004083	normal protein level [assayed_using] PomBase:SPBC582.03	(Fig. 5B) (comment: CHECK cdc22-M45 blocked in G1/S)
PMID:7796804	FYPO:0004083	normal protein level [assayed_using] PomBase:SPBC582.03	(Fig. 5B) (comment: CHECK cdc22-M45 blocks in G1/S)
PMID:7796804	FYPO:0005711	decreased cyclin B1-CDK1 complex level [assayed_using] PomBase:SPBC582.03 [has_severity] high	(Fig. 5C) cyclin cdc13 cdc2 complex are not detected when cells are blocked in G1 with cdc10-129 mutant complex precipitated with p13 beads
PMID:7796804	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] high	(Fig. 6 bottom panels Fig7B panel 6) cells examined 7 hour after refeeding with nitrogen
PMID:7796804	FYPO:0001491	viable vegetative cell [has_penetrance] high	(Fig. 6 middle panels Fig7B panel 3) cells examined 7 hour after refeeding with nitrogen
PMID:7796804	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] high	(Fig. 6 middle panels Fig7B panel 4) cells examined 7 hour after refeeding with nitrogen
PMID:7796804	FYPO:0001052	cut, small cell [has_penetrance] high	(Fig. 6 top panels, Fig7B panel 1) cells examined 7 hour after refeeding with nitrogen
PMID:7796804	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] high	(Fig. 6 top panels, Fig7B panel 2) cells examined 7 hour after refeeding with nitrogen After 7 hour the cdc10-V50 cells start to leak through and this allows the mik1D wee1-50 cells to start entering mitosis
PMID:7796804	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] high	(Fig. 6, Fig 7B panel 8)
PMID:7796804	FYPO:0004321	altered DNA level during vegetative growth [has_penetrance] high	(Fig. 7A panel 1)
PMID:7796804	FYPO:0000445	cell cycle arrest in mitotic G1 phase [has_penetrance] high	(Fig. 7A panel 2)
PMID:7796804	FYPO:0001383	normal DNA content [has_penetrance] high	(Fig. 7A panel 3)
PMID:7796804	FYPO:0000445	cell cycle arrest in mitotic G1 phase [has_penetrance] high	(Fig. 7A panel 4)
PMID:7796804	FYPO:0001383	normal DNA content [has_penetrance] high	(Fig. 7A panel 5)
PMID:7796804	FYPO:0000445	cell cycle arrest in mitotic G1 phase [has_penetrance] high	(Fig. 7A panel 6)
PMID:7796804	FYPO:0000445	cell cycle arrest in mitotic G1 phase [has_penetrance] high	(Fig. 7A,8)
PMID:7796804	FYPO:0003151	decreased protein level during cellular response to heat [assayed_using] PomBase:SPBC11B10.09	(Fig. 7B) It is the soluble form (upper panel) that disappears not the insoluble form (lower panel) which has implications for which form is allowing replication. I don't know whether to leave this annotation out
PMID:7796804	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication [assayed_using] PomBase:SPBC11B10.09	(Fig. 7C)
PMID:7796804	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication [has_penetrance] high	(Fig. 7C)
PMID:7796804	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication [has_penetrance] high	(Fig. 7C)
PMID:7796804	MOD:00696	phosphorylated residue [absent_during] mitotic G1 phase	(Figure 1, 4,5)
PMID:7796804	MOD:00696	phosphorylated residue [present_during] mitotic S phase	(Figure 1, 4,5)
PMID:7796804	MOD:00696	phosphorylated residue [present_during] mitotic G2 phase	(Figure 1, 4,5)
PMID:7796804	MOD:00696	phosphorylated residue [present_during] mitotic prophase	(Figure 1, 4,5)
PMID:7796804	FYPO:0006286	normal cyclin B1-CDK1 complex level [assayed_using] PomBase:SPBC582.03	(comment: CHECK fypo/issues/3164) Fig 5C the cyclin cdc13 cdc2 complex are detected when cells are blocked at G1/S with cdc20-M10 mutant, complex precipitated with p13 beads
PMID:7796804	FYPO:0006286	normal cyclin B1-CDK1 complex level [assayed_using] PomBase:SPBC582.03	(comment: CHECK fypo/issues/3164) Fig 5C the cyclin cdc13 cdc2 complex are detected when cells are blocked at G1/S with cdc20-M45 mutant, complex precipitated with p13 beads
PMID:7798319	FYPO:0003166	monoseptate vegetative cell with binucleate and anucleate compartments	Consistently, the phenotype of cut9-T98 was indistinguishable from that of cut9-665
PMID:7798319	FYPO:0002303	inviable mononucleate monoseptate vegetative cell with anucleate compartment	Consistently, the phenotype of cut9-T98 was indistinguishable from that of cut9-665
PMID:7798319	FYPO:0003165	cut with abnormal chromosome segregation	Consistently, the phenotype of cut9-T98 was indistinguishable from that of cut9-665
PMID:7813446	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPCC18B5.03	(comment: higher than wee1 not overexp, but lower than wee1-50 overexp in wt bkg)
PMID:7813446	FYPO:0001355	decreased vegetative cell population growth	(comment: not arrested like wee1+ overexp alone)
PMID:7813446	FYPO:0001355	decreased vegetative cell population growth	(comment: not arrested like wee1-50 overexp alone)
PMID:7813446	FYPO:0001355	decreased vegetative cell population growth	(comment: not arrested like wee1-50 overexp alone)
PMID:7859738	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:7859738	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:7859738	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:7859738	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:7859738	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:7859738	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:7859738	FYPO:0002060	viable vegetative cell population	(Figure 4)
PMID:7876257	MOD:00006	N-glycosylated residue	(comment: endoglycosidase-H cleaves N-linked glycosylation)
PMID:7883794	FYPO:0005710	abnormal negative regulation of DNA replication initiation resulting in complete rereplication, with mitotic cell cycle arrest [has_penetrance] high [has_severity] high	(Fig. 1B)
PMID:7883794	FYPO:0005440	swollen elongated cell with enlarged nucleus [has_penetrance] high	(Figure 1A)
PMID:7883794	FYPO:0001001	abnormal cell cycle arrest at mitotic G2/M phase transition during nitrogen starvation [has_penetrance] high	(Figure 2B)
PMID:7883794	FYPO:0000603	decreased duration of mitotic G1 phase [has_penetrance] high	(Figure 2C)
PMID:7883794	FYPO:0003165	cut [has_penetrance] high	(Figure 3A)
PMID:7883794	FYPO:0006728	abolished mitotic DNA replication initiation [has_penetrance] high	(Figure 3B)
PMID:7883794	FYPO:0005773	elongated mononucleate aseptate vegetative cell	Data not shown
PMID:7883794	FYPO:0006031	delayed onset of mitotic DNA replication initiation [has_penetrance] high	Table 1, Figure 1B appearance of IC peak at early timepoint
PMID:7883794	FYPO:0003498	premature mitotic DNA replication initiation [has_penetrance] high	Table 1, Figure 2C
PMID:7889932	GO:0000287	magnesium ion binding	(comment: crystal structure)
PMID:7903653	FYPO:0000249	decreased cell population growth on ammonia nitrogen source	(comment: CHECK ABOLISHED)
PMID:7903653	FYPO:0000249	decreased cell population growth on ammonia nitrogen source	(comment: CHECK ABOLISHED)
PMID:7903653	FYPO:0000249	decreased cell population growth on ammonia nitrogen source	(comment: CHECK ABOLISHED)
PMID:7909513	FYPO:0001443	abolished transcription during vegetative growth [assayed_using] PomBase:SPAPB2B4.03	(comment: 3 kb transcript)
PMID:7909513	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPAPB2B4.03	the basal level of the 3.2 kb transcript was lower than that in h90 wild type cells, but the 3 kb transcript was properly induced upon nitrogen starvation
PMID:7916658	FYPO:0001492	viable elongated vegetative cell	(comment: constitutive cdc18+ expression)
PMID:7916658	FYPO:0000012	mitotic G2/M phase transition delay	(comment: constitutive cdc18+ expression)
PMID:7916658	FYPO:0001355	decreased vegetative cell population growth	(comment: constitutive cdc18+ expression)
PMID:7916658	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC14C8.07c	(comment: inferred from combination of phenotype shown in this paper with background knowledge)
PMID:7923372	GO:0043539	protein serine/threonine kinase activator activity [directly_positively_regulates] PomBase:SPBC1D7.05 [part_of] positive regulation of pheromone response MAPK cascade	(comment: they interacted in the Y2H experiment, so inferring this relationship)
PMID:7957097	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPBC776.02c	(comment: CHECK inhibits)
PMID:7957097	FYPO:0004922	inviable elongated mononucleate aseptate cell with cell cycle arrest at mitotic G2/M phase transition	(comment: no mitotic spindle)
PMID:7957098	FYPO:0000848	abnormal chromosome morphology during vegetative growth [has_severity] low	(comment: CHECK same as cdc10-129 alone)
PMID:7957098	FYPO:0001916	elongated mononucleate vegetative cell	(comment: CHECK same as cdc13-117 alone)
PMID:7957098	FYPO:0001916	elongated mononucleate vegetative cell	(comment: CHECK same as cdc2-33 alone)
PMID:7957098	FYPO:0001916	elongated mononucleate vegetative cell	(comment: CHECK same as cdc25-22 alone)
PMID:7957098	FYPO:0001933	abnormal mitotic cell cycle regulation during cellular response to hydroxyurea	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	abnormal mitotic cell cycle regulation during cellular response to hydroxyurea	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	abnormal mitotic cell cycle regulation during cellular response to hydroxyurea	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	abnormal mitotic cell cycle regulation during cellular response to hydroxyurea	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	abnormal mitotic cell cycle regulation during cellular response to hydroxyurea	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	abnormal mitotic cell cycle regulation during cellular response to hydroxyurea	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	abnormal mitotic cell cycle regulation during cellular response to hydroxyurea	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	abnormal mitotic cell cycle regulation during cellular response to hydroxyurea	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7957098	FYPO:0001933	abnormal mitotic cell cycle regulation during cellular response to hydroxyurea	(comment: CHECK same as rad4 cut5 allele alone)
PMID:7975894	FYPO:0005662	increased transcription from TR box [assayed_using] PomBase:SPMTR.02	(comment: CHECK increased transcription from TR box SO:0001858)
PMID:7983142	FYPO:0001357	normal vegetative cell population growth	(comment: CONDITION 33 degrees) (comment: may be standard for them)
PMID:7983142	FYPO:0003610	branched, elongated cell with branch forming adjacent to septum [has_severity] medium [has_penetrance] low	(comment: CONDITION 33 degrees) (comment: may be standard for them)
PMID:7983142	FYPO:0001253	elongated multinucleate multiseptate vegetative cell, single septa between nuclei [has_penetrance] low	(comment: CONDITION 33 degrees) (comment: may be standard for them)
PMID:7983142	FYPO:0000280	sterile	(comment: CONDITION 33 degrees) (comment: may be standard for them)
PMID:7983142	FYPO:0001253	elongated multinucleate multiseptate vegetative cell, single septa between nuclei	(comment: CONDITION 33 degrees) (comment: may be standard for them)
PMID:7983142	FYPO:0001253	elongated multinucleate multiseptate vegetative cell, single septa between nuclei	(comment: CONDITION 33 degrees) (comment: may be standard for them)
PMID:7983142	FYPO:0000021	spheroid vegetative cell	(comment: CONDITION 33 degrees) (comment: may be standard for them); (comment: CHECK morphology same as ppe1delta alone)
PMID:8006074	FYPO:0001043	increased mating efficiency	(Fig. 8)
PMID:8006074	FYPO:0000477	delayed onset of meiosis	(Fig. 8)
PMID:8006074	FYPO:0000477	delayed onset of meiosis	(Fig. 8)
PMID:8006074	FYPO:0000479	premature meiosis	(Fig. 8)
PMID:8026462	FYPO:0001384	abolished protein kinase activity	(comment: CHECK assayed using casein)
PMID:8087848	FYPO:0000252	increased spontaneous diploidization [has_penetrance] 99	(Table 1)
PMID:8087848	FYPO:0000252	increased spontaneous diploidization [has_penetrance] 99	(Table 1)
PMID:8087848	FYPO:0000252	increased spontaneous diploidization [has_penetrance] 85	(Table 1)
PMID:8087848	FYPO:0004596	abnormal negative regulation of DNA replication initiation during mitotic G2 phase resulting in complete rereplication [has_penetrance] high	FACS analysis of germinating haploid cdc13delta spores. Up to 32C DNA content was observed by 19 hour after referring spores to allow germination Figure 2
PMID:8087848	FYPO:0001052	cut, small cell [has_penetrance] 60	cdc10-129 cells blocked in G1 over expressing cdc2 from integrated pREP5cdc2 and cdc13 from episomal pREP41-cdc13. The nmt1 promoter is derepressed Figure 4
PMID:8087848	FYPO:0003449	abnormal cell cycle arrest at mitotic G1/S phase transition [has_penetrance] high	cdc10-129 cells blocked in G1 over expressing cdc2 from integrated pREP5cdc2 and cdc13 from episomal pREP41-cdc13. The nmt1 promoter is derepressed Figure 4
PMID:8087848	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication [has_penetrance] high	cdc13delete cells were kept alive by episomal pSM2 cdc13. Cell phenotype was observed after plasmid loss. Figure 2C
PMID:8087848	FYPO:0002083	inviable swollen elongated cell with enlarged nucleus [has_penetrance] high	germinating haploid cdc13delta spores, observed by 14 hour after spores allowed to germination (Figure 2b). cdc13delete cells kept alive by a multicopy plasmid, pSM2-cdc13. Cell phenotype was observed after plasmid loss same phenotype as in Figure 2b
PMID:8087848	FYPO:0005711	decreased cyclin B1-CDK1 complex level	p34cdc2 cdc13-9 complex was pulled down using p13suc1 beads and then western blotted using anti cdc13 antibody SP4 to show reduced levels of Cdc13 complexed with cdc2 compared to the wild type control
PMID:8121488	FYPO:0002083	inviable swollen elongated cell with enlarged nucleus [has_penetrance] high	(Fig. 1A) Overreplicating haploid cells become highly enlarged (Fig. la, left)
PMID:8121488	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication	(Fig. 1B) (comment: they give a pulse of rum1)
PMID:8121488	FYPO:0003345	abolished cell cycle arrest in mitotic G1 phase in response to nitrogen starvation [has_penetrance] high	(Fig. 2B) (comment: prestart)
PMID:8121488	FYPO:0000280	sterile [has_penetrance] high [has_severity] low	(Fig. 3a)
PMID:8121488	FYPO:0001053	cut, normal size cell [has_penetrance] high [has_severity] high	(Fig. 4A, B) In cdc10-129 rum1 delta strain cells fail to activate the DNA replication checkpoint in the absence of DNA replication and
PMID:8121488	FYPO:0000453	DNA content decreased during vegetative growth [has_penetrance] high [has_severity] high	(Fig. 4E,G) In cdc10-129 rum1 delta strain cells at 36 fail to activate the DNA replication checkpoint in the absence of rum1 and cells proceed into mitosis in the presence of HU and enter mitosis with reduced DNA content
PMID:8121488	FYPO:0005097	abnormal cell cycle arrest in mitotic G1 phase	(Fig. 4a) elongated cell, cells do not replicate DNA (never enter S phase), but keep growing
PMID:8121488	FYPO:0000453	DNA content decreased during vegetative growth [has_penetrance] high [has_severity] high	(Fig. 4d, f) In cdc10-129 rum1 delta strain cells fail to activate the DNA replication checkpoint in the absence of rum1 and cells proceed into mitosis in the absence of DNA replication and enter mitosis with reduced DNA content proce of DNA replication and
PMID:8121488	FYPO:0000398	premature mitotic G1/S phase transition [has_penetrance] high [has_severity] low	(Table 1)
PMID:8121488	GO:0004861	cyclin-dependent protein serine/threonine kinase inhibitor activity [has_input] PomBase:SPBC11B10.09	(comment: CHECK in vitro assay) data not shown
PMID:8121488	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication [has_penetrance] high	(comment: transient expression) (Fig 1b)
PMID:8121488	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication	At both temperatures the DNA content per cell continued to increase, demonstrating that the G2-arrested cells were able to undergo further rounds of S phase (Fig. 2c and d, right) .
PMID:8121488	GO:0031568	mitotic G1 cell size control checkpoint signaling [happens_during] mitotic G1 phase [happens_during] cellular response to nitrogen starvation	Expression results in a small delay of S phase onset until cells attain a higher mass, suggesting the rum1 gene product may act as a transient inhibitor of progression through GI into S phase. The appearance of a small population of IC cells at 16 h is consistent with this interpretation (Fig. lb).
PMID:8121488	GO:0031568	mitotic G1 cell size control checkpoint signaling [happens_during] mitotic G1 phase [happens_during] cellular response to nitrogen starvation	Expression results in a small delay of S phase onset until cells attain a higher mass, suggesting the rum1 gene product may act as a transient inhibitor of progression through GI into S phase. The appearance of a small population of IC cells at 16 h is consistent with this interpretation (Fig. lb).
PMID:8121488	GO:0007089	traversing start control point of mitotic cell cycle [happens_during] mitotic G1 phase [happens_during] cellular response to nitrogen starvation	Expression results in a small delay of S phase onset until cells attain a higher mass, suggesting the rum1 gene product may act as a transient inhibitor of progression through GI into S phase. The appearance of a small population of IC cells at 16 h is consistent with this interpretation (Fig. lb).
PMID:8121488	FYPO:0000333	mitotic G1/S phase transition delay [has_penetrance] high [has_severity] medium	Table 1 (comment: CHECK increased cell size required for the G1/S transition.)
PMID:8121488	FYPO:0007476	decreased duration of cell cycle arrest in mitotic G1 phase	data not shown, cells become arrest in G2
PMID:8163505	GO:0004674	protein serine/threonine kinase activity	(comment: based on phenotype this annotation is possible)
PMID:8187760	FYPO:0001382	decreased protein kinase activity	(comment: assayed in vitro using casein)
PMID:8187760	FYPO:0004105	abolished polar cell growth	(comment: grows in three dimensions instead of just at cell ends)
PMID:8187760	FYPO:0000839	inviable elongated mononucleate aseptate cell	(comment: same as cdc2-33 alone)
PMID:8187760	FYPO:0000839	inviable elongated mononucleate aseptate cell	(comment: same as cdc25-22 alone)
PMID:8223442	FYPO:0007564	normal DNA binding at MCB	(Fig. 1)
PMID:8223442	FYPO:0007565	abolished DNA binding at MCB	(Fig. 1)
PMID:8227198	FYPO:0001665	decreased cellular cAMP level during cellular response to glucose stimulus	(comment: response curve differs from wt and other git mutants)
PMID:8264625	GO:0043539	protein serine/threonine kinase activator activity	(comment: casein substrate (vw changed from GO:0004674 with contributes to))
PMID:8264625	GO:0004674	protein serine/threonine kinase activity	(comment: casein substrate)
PMID:8292390	FYPO:0001387	loss of viability at high temperature [has_severity] medium	(comment: CHECK same as cps8-185 alone)
PMID:8299169	FYPO:0002068	growth auxotrophic for histidine	(comment: CHECK C868T (nt))
PMID:8319772	MOD:00046	O-phospho-L-serine	(comment: present throughout cell cycle)
PMID:8413241	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC31G5.09c	(comment: tyrosine; residue not determined)
PMID:8413241	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC31G5.09c	(comment: tyrosine; residue not determined)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	(Fig. 4) (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(Fig. 4) (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	(Fig. 4, Table 1) (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(Fig. 4, Table 1) (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0000446	cell cycle arrest at mitotic G2/M phase transition [has_penetrance] high	(Fig. 5) (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0000446	cell cycle arrest at mitotic G2/M phase transition [has_penetrance] high	(Fig. 5) (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0000446	cell cycle arrest at mitotic G2/M phase transition [has_penetrance] high	(Fig. 5) (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0000333	mitotic G1/S phase transition delay [has_penetrance] high	(Fig. 5) increased duration of G1 phase
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	(comment: Cdc2 is only mildly over expressed as it is expressed from a multi copy plasmid pIRT2. This is much lower over expression than from the nmt1 promoter and for all the other annotations were the cdc2 mutant is expressed from pIRT2 I have said 'unknown' for expression level)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(comment: Cdc2 is only mildly over expressed as it is expressed from a multi copy plasmid pIRT2. This is much lower over expression than from the nmt1 promoter and for all the other annotations were the cdc2 mutant is expressed from pIRT2 I have said 'unknown' for expression level)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(comment: mutant expressed from multi copy plasmid has dominant negative phenotype) Table 1
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	(comment: mutant expressed from multi copy plasmid has dominant negative phenotype) Table 1
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(comment: mutant expressed from multi copy plasmid has dominant negative phenotype) Table 1
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(comment: mutant expressed from multi copy plasmid has dominant negative phenotype) Table 1
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	(comment: mutant expressed from multi copy plasmid has dominant negative phenotype) Table 1
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	(comment: mutant expressed from multi copy plasmid has dominant negative phenotype) Table 1
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	(comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	(comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	(comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	(comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0000082	decreased cell population growth at high temperature	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	(comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant expressed from multi copy plasmid has dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant expressed from multi copy plasmid has dominant negative phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant expressed from multi copy plasmid pIRT2)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype)
PMID:8437586	FYPO:0001122	elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not supress the ts phenotype)
PMID:8437586	FYPO:0002060	viable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 give partial suppression)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has a dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 has dominant negative phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 no suppression)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 no suppression)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 no suppression)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 no suppression)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 no suppression)
PMID:8437586	FYPO:0001234	slow vegetative cell population growth	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 partially suppresses the ts phenotype)
PMID:8437586	FYPO:0000082	decreased cell population growth at high temperature	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype)
PMID:8437586	FYPO:0000082	decreased cell population growth at high temperature	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype)
PMID:8437586	FYPO:0001492	viable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 partially supresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	FYPO:0001122	elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 supresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2 surpresses the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001234	slow vegetative cell population growth	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] medium	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0000082	decreased cell population growth at high temperature	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table 1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	Table 1, Fig 2 (comment: mutant gene expressed from multicopy plasmid pIRT2 suppresses the ts phenotype)
PMID:8437586	FYPO:0001512	branched, elongated cell [has_penetrance] high	Table 1, Fig 2 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8437586	FYPO:0001052	cut, small cell [has_penetrance] high	Table 1, Fig 4 (comment: CHECK nmt1 ON)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table 1, Fig 4 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0001490	inviable elongated vegetative cell [has_penetrance] high	Table 1, Fig 4 (comment: CHECK nmt1 promoter ON)
PMID:8437586	FYPO:0001492	viable elongated vegetative cell [has_penetrance] high [has_severity] variable severity	Table 1, Fig2 (comment: mutant gene expressed from multicopy plasmid pIRT2 partially suppresses the ts phenotype)
PMID:8437586	FYPO:0002061	inviable vegetative cell population	Table1 (comment: mutant gene expressed from multicopy plasmid pIRT2 does not suppress the ts phenotype)
PMID:8437586	FYPO:0002085	normal vegetative cell growth [has_penetrance] high	Table1 (comment: mutant gene expressed from multicopy plasmid pIRT2)
PMID:8463273	GO:0004699	diacylglycerol-dependent, calcium-independent serine/threonine kinase activity	(comment: kinase assay, and hybridization with S. cerevisiae PKC)
PMID:8485317	FYPO:0002060	viable vegetative cell population	(comment: like dis1-288 alone)
PMID:8485317	FYPO:0002061	inviable vegetative cell population	(comment: like dis1-288 alone)
PMID:8496185	GO:0004017	AMP kinase activity	(comment: CHECK inhibited by P(1),P(5)-bis(5'-adenosyl) pentaphosphate(5-)?)
PMID:8497322	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 2a)
PMID:8497322	FYPO:0001128	decreased septation index [has_severity] high	(Fig. 2a) (comment: DROPS TO ZERO)
PMID:8497322	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(Fig. 2c)
PMID:8497322	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] medium	(Fig. 2c)
PMID:8497322	FYPO:0001387	loss of viability at high temperature [has_severity] high	(Fig. 2c)
PMID:8497322	FYPO:0005705	loss of viability following cellular response to UV [has_severity] high	(Fig. 2c)
PMID:8497322	FYPO:0002061	inviable vegetative cell population	(Fig. 3)
PMID:8497322	FYPO:0001046	premature mitosis	(Fig. 3) (comment: CHECK fypo/issues/2818)
PMID:8497322	FYPO:0006822	viable small vegetative cell with normal cell growth rate	(Fig. 3) (comment: CHECK fypo/issues/2818)
PMID:8497322	FYPO:0001971	abnormal cell separation after cytokinesis resulting in chained cells	(Fig. 3) cells fail to separate and are clupmed together, multiple rounds of nuclear division
PMID:8497322	FYPO:0002060	viable vegetative cell population	(Fig. 3a)
PMID:8497322	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 4)
PMID:8497322	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] low	(comment: partial rescue of chk1) (Fig. 2b)
PMID:8497322	FYPO:0002061	inviable vegetative cell population	data not shown
PMID:8515818	FYPO:0002060	viable vegetative cell population	(Fig. 1b bottom R panel , bottom R)
PMID:8515818	FYPO:0001491	viable vegetative cell [has_penetrance] high	(Fig. 1b bottom R panel , bottom R)
PMID:8515818	FYPO:0001489	inviable vegetative cell [has_penetrance] high	(Fig. 1b bottom R panel, bottom L)
PMID:8515818	FYPO:0002061	inviable vegetative cell population	(Fig. 1b bottom R panel, bottom L)
PMID:8515818	FYPO:0002061	inviable vegetative cell population	(Fig. 1b bottom R panel, top)
PMID:8515818	FYPO:0001489	inviable vegetative cell [has_penetrance] high	(Fig. 1b bottom R panel, top)
PMID:8515818	FYPO:0001489	inviable vegetative cell [has_penetrance] high	(Fig. 1b top R panel bottom L)
PMID:8515818	FYPO:0002061	inviable vegetative cell population	(Fig. 1b top R panel bottom L)
PMID:8515818	FYPO:0002060	viable vegetative cell population	(Fig. 1b top R panel bottom R)
PMID:8515818	FYPO:0001491	viable vegetative cell [has_penetrance] high	(Fig. 1b top R panel bottom R)
PMID:8515818	FYPO:0002061	inviable vegetative cell population	(Fig. 1b top R panel, top)
PMID:8515818	FYPO:0001489	inviable vegetative cell [has_penetrance] high	(Fig. 1b top R panel, top)
PMID:8515818	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC18B5.03 [has_penetrance] medium	(Fig. 2a lane 1)
PMID:8515818	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPCC18B5.03 [has_penetrance] medium	(Fig. 2a lane 3)
PMID:8515818	MOD:00047	O-phospho-L-threonine	(Fig. 2b)
PMID:8515818	MOD:00047	O-phospho-L-threonine	(Fig. 2b)
PMID:8515818	MOD:00046	O-phospho-L-serine	(Fig. 2b)
PMID:8515818	MOD:00046	O-phospho-L-serine	(Fig. 2b)
PMID:8515818	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPCC18B5.03 [part_of] mitotic G2 cell size control checkpoint signaling	(Fig. 4a,b, Fig. 2,3)
PMID:8515818	FYPO:0006822	viable small vegetative cell with normal cell growth rate	data not shown
PMID:8521469	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication	(comment: CHECK same as cdc18+ oe alone)
PMID:8521469	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication	(comment: CHECK same as cdc18+ oe alone)
PMID:8521500	FYPO:0004319	increased cyclin-dependent protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 1) (comment: Histone H1 used as substrate)
PMID:8521500	FYPO:0006560	decreased protein kinase activity during mitotic G1 phase [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 1) (comment: Histone H1 used as substrate)
PMID:8521500	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition [has_penetrance] high	(Fig. 2C) (comment: rum1+ driven by nmt1 promoter in pREP6X is integrated)
PMID:8521500	FYPO:0005933	decreased protein level during mitotic G1 phase [assayed_using] PomBase:SPBC582.03 [has_penetrance] high	(Fig. 3A)
PMID:8521500	FYPO:0004108	increased protein level during mitotic G1 phase [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 3A)
PMID:8521500	FYPO:0005926	normal protein level during mitotic G1 phase [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Fig. 3A)
PMID:8521500	FYPO:0005926	normal protein level during mitotic G1 phase [has_penetrance] high [assayed_using] PomBase:SPBC11B10.09	(Fig. 3A)
PMID:8521500	FYPO:0004108	increased protein level during mitotic G1 phase [has_penetrance] high [assayed_using] PomBase:SPBC32F12.09	(Fig. 3A)
PMID:8521500	FYPO:0006506	normal RNA level during mitotic G1 phase [has_penetrance] high [assayed_using] PomBase:SPBC32F12.09	(Fig. 3B)
PMID:8521500	FYPO:0006506	normal RNA level during mitotic G1 phase [assayed_using] PomBase:SPBC582.03 [has_penetrance] high	(Fig. 3B)
PMID:8521500	FYPO:0004193	decreased protein level during mitotic S phase [assayed_using] PomBase:SPBC32F12.09 [has_penetrance] high	(Fig. 3C)
PMID:8521500	FYPO:0006288	decreased protein level during mitotic G2 phase [assayed_using] PomBase:SPBC32F12.09 [has_penetrance] high	(Fig. 3C)
PMID:8521500	FYPO:0006561	normal CDK-cyclin complex binding during mitotic G1 phase [assayed_using] PomBase:SPBC32F12.09 [assayed_using] PomBase:SPBC582.03	(Fig. 4) (comment: rum1HA pulldown brings down both cdc13 and cdc2 to form rum1-cdc13-cdc2 complex. so I really need to add 3 proteins not two in the annotation extensions)
PMID:8521500	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPBC582.03 [assayed_using] PomBase:SPBC32F12.09	(Fig. 5A)
PMID:8521500	FYPO:0001571	increased protein-protein interaction [assayed_using] PomBase:SPBC32F12.09 [assayed_using] PomBase:SPBC11B10.09	(Fig. 5A)
PMID:8521500	FYPO:0003436	decreased protein kinase activity during mitotic G2 phase [assayed_enzyme] PomBase:SPBC582.03	(Fig. 5B) over expression abolishes cdc13 associated kinase activity even in absence of added rum1 protein
PMID:8521500	FYPO:0003436	decreased protein kinase activity during mitotic G2 phase [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 5B) over expression reduces cdc2 kinase activity even in absence of added rum1 protein
PMID:8521500	GO:0061575	cyclin-dependent protein serine/threonine kinase activator activity [part_of] mitotic cell cycle process	(Fig. 6) cdc2-cig1 complex is insensitive to inhibition by rum1. There is ~100% activity in the presence of 26nM rum
PMID:8521500	GO:0004861	cyclin-dependent protein serine/threonine kinase inhibitor activity [has_input] PomBase:SPAPB2B4.03 [has_input] PomBase:SPBC11B10.09 [part_of] negative regulation of G1/S transition of mitotic cell cycle [happens_during] mitotic interphase	(comment: CHECK [ move to specific cyclin]) Fig6 2.6nM rum1 inhibits cig2 associated cdc2 kinase activity by ~50%
PMID:8521500	GO:0004861	cyclin-dependent protein serine/threonine kinase inhibitor activity [has_input] PomBase:SPBC582.03 [has_input] PomBase:SPBC11B10.09 [part_of] negative regulation of mitotic cell cycle [happens_during] mitotic G1 phase	(comment: CHECK [MOVE 'occurs at' TO M-PHASE CYCLIN]) Fig1 and 2B 0.26nM pRum1 inhibits in vitro cdc2-cdc13 kinase activity by ~80%, Fig3C ig5B,C, D addition of 2.6nM rum1 reduces cdc2 associated kinase activity
PMID:8522609	FYPO:0000839	inviable elongated mononucleate aseptate cell	(comment: same as cdc2-33 alone)
PMID:8522609	FYPO:0001018	abolished NETO	(comment: same as orb2-34 alone)
PMID:8522609	FYPO:0001018	abolished NETO	(comment: same as orb2-34 alone)
PMID:8522609	FYPO:0001418	abnormal microtubule cytoskeleton morphology during vegetative growth	(comment: same as orb3-167 alone)
PMID:8522609	FYPO:0002021	dispersed actin cortical patch localization during vegetative growth	(comment: same as orb3-167 alone)
PMID:8522609	FYPO:0000647	vegetative cell lysis	(comment: same as orb3-167 alone)
PMID:8552670	GO:0043565	sequence-specific DNA binding [occurs_at] ARS_consensus_sequence	(comment: CHECK activated_by(CHEBI:18420))
PMID:8557036	GO:0004693	cyclin-dependent protein serine/threonine kinase activity	(comment: assayed in S. cerevisiae cell extracts, with S.c. CDK2 substrate)
PMID:8557036	GO:0008353	RNA polymerase II CTD heptapeptide repeat kinase activity	(comment: assayed in S. cerevisiae cell extracts, with S.c. CTD substrate)
PMID:8557037	GO:0004693	cyclin-dependent protein serine/threonine kinase activity	(comment: CHECK activated_by(CHEBI:63041))
PMID:8569679	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:8569679	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:8569679	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:8569679	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:8569679	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:8569679	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:8569679	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:8569679	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:8590464	GO:0004043	L-aminoadipate-semialdehyde dehydrogenase [NAD(P)+] activity [part_of] L-lysine biosynthetic process	(comment: CHECK inhibited_by L-lysine)
PMID:8590474	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(comment: CHECK partial rescuie)
PMID:8599928	FYPO:0001124	normal vegetative cell size	Microscopic examination failed to detect any difference in cell size or morphology between wis2+-deleted cels (wis2A) and wild-type cels,over a range oftemperatures from 20 to 36°C.
PMID:8599928	FYPO:0002060	viable vegetative cell population	Tetrad analysis showed that all four haploid spores of the heterozygous diploid produced colonies at 28°C, indicating that the wis2+ gene is non-essential for viability under normal growth conditions.
PMID:8618924	GO:0033260	nuclear DNA replication [happens_during] mitotic S phase	(comment: also inferred from orthology to all other Orc1s in the world)
PMID:8621436	FYPO:0000158	DNA content increased during vegetative growth	(comment: they show it is not abnormal regulation of rereplication in cdc25 double mutant expts)
PMID:8621436	FYPO:0000158	DNA content increased during vegetative growth	(comment: they show it is not abnormal regulation of rereplication in cdc25 double mutant expts)
PMID:8621436	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	(comment: transient phenotype, they then attempt to divide without segregation)
PMID:8621436	FYPO:0002303	inviable mononucleate monoseptate vegetative cell with anucleate compartment	(comment: transient phenotype, they then attempt to divide without segregation)
PMID:8621436	FYPO:0002303	inviable mononucleate monoseptate vegetative cell with anucleate compartment	(comment: transient phenotype, they then attempt to divide without segregation)
PMID:8621436	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	(comment: transient phenotype, they then attempt to divide without segregation)
PMID:8649397	FYPO:0001122	elongated vegetative cell	(comment: Can't say if they are viable vegetative because it is in a pyp2+ background)
PMID:8654750	GO:0043409	negative regulation of MAPK cascade [occurs_in] H minus	(comment: PHEROMONE)
PMID:8668131	GO:0006744	ubiquinone biosynthetic process	(comment: functionally complements S cerevisiae ABC1)
PMID:8688826	GO:0034399	nuclear periphery	(comment: vw: changed from nuclear lumen to nuclear periphery)
PMID:872890	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(Fig. 1) data not shown cdc2-1w is called wee 2-1 in this paper. Wee cells enter mitosis at a small cell size compared to wild type cells and thus daughter cells are born smaller than wild type cells. Wee cells have similar cell cycle timing (doubling time) to wild type cells
PMID:872890	FYPO:0006906	normal mitotic G2 cell size control checkpoint	(Fig. 2) This shows that wee1-50 has a direct effect on the G2-M transition because cells now at the permissive temperature (active wee1) detect that they are too small to enter mitosis and the G2/M transition is inhibited
PMID:872890	FYPO:0006905	normal mitotic G1 cell size control checkpoint	(Fig. 2) This suggests that wee1-50 only has an indirect effect on the G1-S transition because when wee1-50 is shifted to the permissive temperature cells are still small, this is not affected by the presence of active wee1 and cells enter S-phase at the same size as they did at the restrictive temperature
PMID:872890	FYPO:0006908	normal mitotic G1 cell size control checkpoint following spore germination [has_penetrance] high	(Fig. 4, Table 2) cell size measure by protein content per cell, cells need to reach ~7pg/cell. This measurement is also the same for wild type cells which are small after spore germination (Fig3)
PMID:872890	FYPO:0006907	normal mitotic G1 cell size control checkpoint following nitrogen starvation-induced arrest in G1 phase [has_penetrance] high	(Fig. 6, Table 2) cell size measure by protein content per cell, cells need to reach ~7pg/cell. This measurement is also the same for wild type cells which are small after nitrogen starvation (Fig5)
PMID:872890	FYPO:0006909	mitotic G1/S phase transition at small cell size	(Table 1)
PMID:872890	FYPO:0006909	mitotic G1/S phase transition at small cell size	Table 1, DNA replication initiated at low protein content
PMID:872890	FYPO:0006031	delayed onset of mitotic DNA replication initiation [has_penetrance] high	Table 1, Fig1
PMID:872890	FYPO:0006031	delayed onset of mitotic DNA replication initiation	Table 1, Fig1
PMID:8799335	PomGeneEx:0000014	RNA present [during] single-celled organism vegetative growth phase	(comment: present with ammonium, allantoin, or proline nitrogen source)
PMID:8799851	FYPO:0004189	increased protein level during cellular response to hydroxyurea [assayed_using] PomBase:SPBC582.03 [has_penetrance] high	(Fig. 10)
PMID:8799851	FYPO:0006758	protein absent from cell during mitotic G1 phase [assayed_using] PomBase:SPBC582.03 [has_penetrance] high	(Fig. 9)
PMID:8799851	FYPO:0000835	decreased protein level [assayed_using] PomBase:SPBC582.03	Data not shown cdc13 protein level in asynchronous culture of wee1-50 cells at restrictive temperature is reduced by 40% compared to asynchronous culture of WT cells
PMID:8799851	FYPO:0006758	protein absent from cell during mitotic G1 phase [assayed_using] PomBase:SPBC582.03	Uses elutriation synchrony. Fig5 cdc13 protein level in synchronous culture of wee1-50 cells at restrictive temperature is absent during longer G1 phase
PMID:8811082	GO:0000703	oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity	(comment: CHECK thymine glycols, urea)
PMID:8811082	GO:0140078	class I DNA-(apurinic or apyrimidinic site) endonuclease activity	The capacity of Nth-Spo to generate strand breaks in a variety of damaged plasmid DNA substrates was investigated. Figure 4shows the activity of Nth-Spo and Nth-Eco in incising supercoiled damaged DNA. None of the proteins caused breaks in undamaged DNA.
PMID:8824588	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC19D5.01	(comment: also has AP1 binding site)
PMID:8834798	FYPO:0000117	abnormal septum assembly	abnormal septum forms on the surface from one side of the cell and then extends in a disorganized manner into the interior
PMID:8876193	FYPO:0003811	asymmetric mitochondrial aggregation [has_penetrance] 77	(Fig. 1) 77% asymmetric distribution by 5 hours, aggregation observed after 1 hour
PMID:8876193	FYPO:0006102	interphase microtubules absent from cell [has_penetrance] 88	(Fig. 2)
PMID:8876193	FYPO:0000732	short bipolar mitotic spindle [has_penetrance] 1	(Fig. 2) 1% of cells still have a short mitotic spindle after 5h at restrictive temperature
PMID:8876193	FYPO:0005838	symmetric mitochondrial aggregation [has_penetrance] 91	(Fig. 3)
PMID:8876193	FYPO:0003811	asymmetric mitochondrial aggregation [has_penetrance] 22	(Fig. 3)
PMID:8876193	GO:0048311	mitochondrion distribution	(Fig. 4)
PMID:8876193	FYPO:0006747	asymmetric mitochondrial aggregation at old end [has_penetrance] 73	(comment: 73% asymmetric distribution at old end by 5 hours asymmetric mitochondrial aggregation at old cell end)
PMID:8876193	FYPO:0005838	symmetric mitochondrial aggregation [has_penetrance] >90	data not shown
PMID:8876193	FYPO:0005838	symmetric mitochondrial aggregation [has_penetrance] 80	data not shown, cells blocked at G1/S, cells need to complete cell cycle to observe asymmetry
PMID:8876193	FYPO:0005838	symmetric mitochondrial aggregation [has_penetrance] 80	data not shown, cells blocked at G2/M, cells need to complete cell cycle to observe asymmetry
PMID:8876193	FYPO:0005838	symmetric mitochondrial aggregation [has_penetrance] 80	data not shown, cells blocked in S phase, cells need to complete cell cycle to observe asymmetry
PMID:8876193	FYPO:0005838	symmetric mitochondrial aggregation [has_penetrance] 80	data not shown, cells blocked in absence of septation, cells need to complete cell cycle to observe asymmetry
PMID:8898110	FYPO:0006144	decreased cellular gluconate level	(Fig. 6)
PMID:8898110	FYPO:0006144	decreased cellular gluconate level	(Fig. 6)
PMID:8918598	FYPO:0005112	decreased ubiquitin-specific protease activity	(comment: ubiquitin conjugate)
PMID:8918598	FYPO:0005112	decreased ubiquitin-specific protease activity	(comment: ubiquitin conjugate)
PMID:8918880	FYPO:0002060	viable vegetative cell population	(Fig. 1)
PMID:8918880	FYPO:0002060	viable vegetative cell population	(Fig. 1)
PMID:8918880	FYPO:0002060	viable vegetative cell population	(Fig. 1)
PMID:8918880	FYPO:0002061	inviable vegetative cell population	(Fig. 1)
PMID:8918880	GO:0005680	anaphase-promoting complex	(Fig. 5)
PMID:8943330	GO:0000196	cell integrity MAPK cascade	(comment: CHECK not sure this annotation is 100% supported, can revise later if needed.)
PMID:8943330	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: tyrosine; position(s) not determined)
PMID:8946912	FYPO:0003210	mislocalized, misoriented septum	(Fig. 2a)
PMID:8946912	FYPO:0001007	normal mitosis	(Fig. 2a)
PMID:8946912	FYPO:0002070	normal nucleus location	(Fig. 2a)
PMID:8946912	FYPO:0001234	slow vegetative cell population growth	(Fig. 3)
PMID:8978670	FYPO:0002023	abnormal septum morphology during vegetative growth	(Figure 1)
PMID:8978670	FYPO:0001008	actomyosin contractile ring absent	(Figure 1)
PMID:8978670	FYPO:0000417	abolished cytokinesis	(Figure 1)
PMID:8978670	FYPO:0002024	inviable elongated multinucleate aseptate vegetative cell	(Figure 1)
PMID:8978687	FYPO:0001368	normal actomyosin contractile ring assembly	(Fig. 4b)
PMID:8978687	FYPO:0004648	delayed onset of mitotic spindle assembly	(Fig. 6a)
PMID:8978687	FYPO:0000729	delayed onset of actomyosin contractile ring assembly	(Fig. 6a)
PMID:8978687	FYPO:0003758	mitotic spindle elongation without chromosome separation	(Fig. 6a)
PMID:8978687	FYPO:0005716	delayed negative regulation of protein kinase activity during mitosis [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 6c)
PMID:8978687	FYPO:0005393	progressively decreasing vegetative cell population growth rate	(Fig. 7)
PMID:8978687	FYPO:0002049	elongated multinucleate aseptate vegetative cell	(Fig. 7)
PMID:8978687	FYPO:0002060	viable vegetative cell population	(Figure 1a)
PMID:8978687	FYPO:0002060	viable vegetative cell population	(Figure 2)
PMID:8978687	FYPO:0002018	mitotic spindle absent from cell	(Figure 5)
PMID:8978687	FYPO:0004474	normal mitotic cell cycle DNA replication checkpoint	(Figure 5)
PMID:8978687	FYPO:0001705	normal mitotic DNA damage checkpoint	(Figure 5)
PMID:8978687	FYPO:0002018	mitotic spindle absent from cell	(Figure 5)
PMID:8978687	FYPO:0005371	increased linear minichromosome loss during vegetative growth	(Figure 6)
PMID:8978689	FYPO:0007664	mononucleate monoseptate vegetative cell with anucleate compartment	(Figure 3A)
PMID:8978689	FYPO:0004022	abnormal cell cycle arrest in mitotic metaphase with long polar microtubules	(Figure 3A) However, dis2-11 displayed an allele-specific mitotic phenotype with spindle elongation (Ohkura et al., 1989; see Figure 3A).
PMID:8978689	FYPO:0007664	mononucleate monoseptate vegetative cell with anucleate compartment	(Figure 3A) abnormal cell cycle arrest in mitotic metaphase, condend chrosmosmes
PMID:8978689	FYPO:0002061	inviable vegetative cell population	(Figure 3A) abnormal cell cycle arrest in mitotic metaphase, condend chrosmosmes
PMID:8978689	FYPO:0007303	abnormal cell cycle arrest in mitotic metaphase with condensed chromosomes	(Figure 3A) because the spindle elongates in the absence of sister chromatid separation.
PMID:8978689	FYPO:0002061	inviable vegetative cell population	(Figure ID, -Thi, Dis2),which allows for colony formation. Cells producing the mutant T316A protein under the strong promoter, on the other hand, severely blocked colony formation (Figure ID,-Thi,Dis2T316A)
PMID:8978689	FYPO:0002060	viable vegetative cell population	A multicopy plasmid which conferred the ability to suppress ts sds22-181 was isolated.
PMID:8978689	FYPO:0002060	viable vegetative cell population	A multicopy plasmid which conferred the ability to suppress ts sds22-181 was isolated.
PMID:8978689	MOD:00047	O-phospho-L-threonine [increased_during] mitotic M phase	A temperature shift (G2 block and release) experiment using the cdc25-22 mutant showed that the level of T316-phosphorylated Dis2 peaked in mitosis(Figure2A).
PMID:8978689	FYPO:0002061	inviable vegetative cell population	Heterozygous diploids verified by Southern hybridization (lower panel) yielded four viable spores at 26 or 33°C with Ade+ segregating 2+:2-, indicating that the sds23+ gene was not essential for viability. Colonies were not formed at 22 or 36°C, however (Figure 6B), indicating that the gene-disrupted Asds23 causes cold and temperature sensitivity.
PMID:8978689	FYPO:0002060	viable vegetative cell population	Heterozygous diploids verified by Southern hybridization (lower panel) yielded four viable spores at 26 or 33°C with Ade+ segregating 2+:2-, indicating that the sds23+ gene was not essential for viability. Colonies were not formed at 22 or 36°C, however (Figure 6B), indicating that the gene-disrupted Asds23 causes cold and temperature sensitivity.
PMID:8978689	FYPO:0002061	inviable vegetative cell population	Heterozygous diploids verified by Southern hybridization (lower panel) yielded four viable spores at 26 or 33°C with Ade+ segregating 2+:2-, indicating that the sds23+ gene was not essential for viability. Colonies were not formed at 22 or 36°C, however (Figure 6B), indicating that the gene-disrupted Asds23 causes cold and temperature sensitivity.
PMID:8978689	FYPO:0007303	abnormal cell cycle arrest in mitotic metaphase with condensed chromosomes	In parallel with the increase in plasmid loss, cells containing condensed chromosomes with a short metaphase spindle dramatically increased (Figure 3C). After transferring the culture from selective to non-selective medium at 33°C, the fraction of these metaphase-arrested cells increased about nine times within 20 h (from 2 to 19%). We concluded, therefore, that the complete absence of PPI in fission yeast leads to the metaphase arrest, which is strikingly similar to the phenotype of sds22 mutants. More than 90% of the cells examined contained condensed chromosomes (Figure 3B, upper panel).
PMID:8978689	FYPO:0006821	slow vegetative cell growth	The cell division rates of Asds23 at the permissive temperatures were exceedingly slow.The generation times in rich YPD medium were 5.7(3.3) and 4.3(2.2) h at2 6 and 33°C, respectively; the values in parenthesis are the generation times for the wild-type strain.)
PMID:8978689	FYPO:0000133	elongated multinucleate vegetative cell	The cell division rates of Asds23 at the permissive temperatures were exceedingly slow.The generation times in rich YPD medium were 5.7(3.3) and 4.3(2.2) h at2 6 and 33°C, respectively; the values in parenthesis are the generation times for the wild-type strain.)
PMID:9024682	FYPO:0000303	decreased conjugation frequency [has_severity] high	(comment: severe when both cells are cpb1delta)
PMID:9034194	FYPO:0001420	normal vegetative cell population growth rate	- haploids grow vegetatively at the same rate as cells containing wild-type tazl+. A complete deletion of tazl + was also constructed and found not to affect viability.
PMID:9034194	GO:0000723	telomere maintenance	Digestion of wild-type DNA with Apal gave a broad distribution of telomeric fragments centred around 300 base pairs. In DNA from cells carrying the tazl disruption, the telomere band was shifted to a smear of ~ 2.5 -4.5 kilo bases. This striking increase in the abundance of telomeric DNA is further underscored by the greater intensity of telomeric hybridiz- ation relative to the signal for wild-type telomeric DNA. A similar increase in the intensity of hybridization to the rDNA-adjacent telomeres on chromosome III, which do not contain telomere- proximal Apal sites, was also observed (Fig. 3 );
PMID:9034194	FYPO:0003066	abnormal sporulation resulting in formation of ascus with fewer than four spores [has_penetrance] 95	Most tazl- asci con- tained fewer than four distinct spores (open arrows in Fig. 5, right), which were often shaped aberrantly. Occasionally, tazl- asci con- tained four spores of normal appearance (filled arrow in Fig. 5, right), and some cells in the tazl+ mixture may have corresponded to aberrant asci. Of the spores that did form in tazl - homozygous crosses, spore viability was only ~5o/o of that measured for tazl+ crosses.
PMID:9034194	FYPO:0002019	elongated telomeres during vegetative growth [has_severity] high	Telomere length increased dramatically when tazl + was disrupted (Fig. 3)
PMID:9034194	GO:0042162	telomeric repeat DNA binding	a one-hybrid screen18 was used to identify proteins that bind specifically to the S. pombe telomere DNA sequence (Fig. la). This screen had.... ; Fig. lb) ..S. pombe proteins that bind to the telomeric target sequence recruit the GAL4 activation- domain fusion to the promoter, thereby activating transcription of the lacZ reporter gene and yielding a blue colony upon exposure to X-gal. Of over a million colonies screened, four blue colonies were identified; these harboured distinct cDNAs, but all four contained the gene tazl+. The Tazl fusion protein did not activate lacZ transcription when a scrambled version of the telomeric sequence was used as a target (Fig. lb), indicating the specificity ofTazlp for telomeric repeats.
PMID:9034337	MOD:00048	O4'-phospho-L-tyrosine [present_during] mitotic G2 DNA damage checkpoint signaling	(Fig. 1)
PMID:9034337	FYPO:0001575	abolished vegetative cell population growth	(Fig. 2A)
PMID:9034337	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 2B) (comment: Histone H1 used as cdc2 substrate Chk2 expressed from nmt1 promoter)
PMID:9034337	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 2C)
PMID:9034337	FYPO:0000444	abnormal mitotic cell cycle arrest with replicated DNA	(Fig. 2D)
PMID:9034337	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 2D)
PMID:9034337	FYPO:0002060	viable vegetative cell population	(Fig. 3A)
PMID:9034337	FYPO:0001234	slow vegetative cell population growth [has_severity] medium	(Fig. 3B)
PMID:9034337	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 3B)
PMID:9034337	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_penetrance] high	(Fig. 3C) cell elongation as a result of chk1 over expression is dependent on wee1+
PMID:9034337	FYPO:0001974	increased number of cells with 1C DNA content	(Fig. 3C) wee cell phenotype cell cycle distribution FACS profile of vegetatively growing wee cells show a cell cycle distribution with increased number of cells with a 1C DNA content compared to wild type cells. Note the increase in the G1 peak depends on the size of the cell and semi-wee cells do not always shown an increased G1 peak
PMID:9034337	MOD:00000	protein modification [added_by] PomBase:SPCC1259.13 [occupancy] ~50 [added_during] DNA damage response	(Fig. 4)
PMID:9034337	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC1259.13 [added_during] DNA damage response	(Fig. 5, 6)
PMID:9034337	MOD:00048	O4'-phospho-L-tyrosine [added_by] PomBase:SPCC18B5.03	(Fig. 6) GST wee1 has been phosphorylated in vitro by chk1. This assay shows that phosphorylation of wee1 by chk1 does not affect wee1 kinase activity
PMID:9034337	FYPO:0002085	normal vegetative cell growth	Data not shown chk1+ over expression phenotype is suppressed by over expressing cdc25+ independently of cdr1
PMID:9042863	GO:0072435	response to mitotic G2 DNA damage checkpoint signaling	(comment: Activity inhibited in response to mitotic G2 DNA damage checkpoint)
PMID:9042863	MOD:00048	O4'-phospho-L-tyrosine [present_during] cellular response to ionizing radiation [removed_by] PomBase:SPAC24H6.05	(comment: dephosphorylation of Cdc2 Y15 by Cdc25 delayed in response to ionising radiation)
PMID:9042863	FYPO:0001046	premature mitosis	(comment: temperature permissive for wee1-50; un-irradiated)
PMID:9042863	FYPO:0007248	decreased duration of mitotic G2 DNA damage checkpoint during cellular response to ionizing radiation	(comment: temperature restrictive for wee1-50)
PMID:9055078	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [assayed_transcript] PomBase:SPBC1711.02	(Fig. 7A)
PMID:9055078	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [assayed_transcript] PomBase:SPBC1711.02	(Fig. 7A)
PMID:9055078	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [assayed_transcript] PomBase:SPBC1711.02	(Fig. 7A)
PMID:9055078	FYPO:0002827	decreased chromatin silencing at silent mating-type cassette [assayed_transcript] PomBase:SPBC1711.02	(Fig. 7A)
PMID:9062192	GO:0051728	cell cycle switching, mitotic to meiotic cell cycle	(comment: mei2 promotes g1 arrest, premeiotic dna replication and meiosis I)
PMID:9078390	FYPO:0002967	normal protein localization to mitotic spindle pole body [assayed_using] PomBase:SPCC736.14	(Fig. 2C)
PMID:9078390	FYPO:0003186	abolished protein localization to mitotic spindle [assayed_using] PomBase:SPCC736.14	(Fig. 2C)
PMID:9078390	FYPO:0002825	decreased protein localization to mitotic spindle [assayed_using] PomBase:SPCC736.14	(Fig. 2C)
PMID:9078390	FYPO:0002956	abnormal protein localization to nucleus [assayed_using] PomBase:SPCC736.14	(Fig. 2C)
PMID:9078390	FYPO:0003186	abolished protein localization to mitotic spindle [assayed_using] PomBase:SPCC736.14	(Fig. 2C)
PMID:9078390	FYPO:0002956	abnormal protein localization to nucleus [assayed_using] PomBase:SPCC736.14	(Fig. 2C)
PMID:9078390	FYPO:0001512	branched, elongated cell [has_penetrance] high	(Fig. 3a)
PMID:9078390	FYPO:0002061	inviable vegetative cell population	(Fig. 3a)
PMID:9078390	FYPO:0001512	branched, elongated cell [has_penetrance] high	(Fig. 3a)
PMID:9078390	FYPO:0002061	inviable vegetative cell population	(Fig. 3a)
PMID:9078390	FYPO:0002061	inviable vegetative cell population	(Fig. 3a)
PMID:9090050	GO:0005358	high-affinity D-glucose:proton symporter activity [part_of] D-glucose import across plasma membrane	(comment: inhibition by CCCP and DCCD)
PMID:9092661	FYPO:0002550	sensitive to UV [has_severity] low	(Figure 2) ...The uvde gene disruption made cells only mildly sensitive to UV, even after high doses.
PMID:9092661	FYPO:0004031	decreased UV-damage excision repair [has_severity] medium	(Figure 4)
PMID:9092661	FYPO:0004031	decreased UV-damage excision repair [has_severity] medium	(Figure 4)
PMID:9092661	FYPO:0004031	decreased UV-damage excision repair [has_severity] high	(Figure 4) The rad13d uvded double mutant cells were unable to remove either type of damage, even during 3 h post-UV incubation.
PMID:9092661	FYPO:0004031	decreased UV-damage excision repair [has_severity] medium	(Figure 5)
PMID:9092661	FYPO:0002550	sensitive to UV [has_severity] medium	(comment: Cell survival assay)
PMID:9092661	FYPO:0002550	sensitive to UV [has_severity] high	(comment: Cell survival assay)
PMID:9092661	FYPO:0002550	sensitive to UV [has_severity] high	(comment: Cell survival assay)
PMID:9092661	FYPO:0002550	sensitive to UV [has_severity] medium	(comment: Cell survival assay)
PMID:9092661	FYPO:0004031	decreased UV-damage excision repair [has_severity] high	Furthermore, a rad13d uvded rad2d triple disruptant had the same UV sensitivity as the rad13d uvded double disruptant.
PMID:9092661	FYPO:0002550	sensitive to UV [has_severity] low	We found that the double mutant uvded rad2d was more resistant than a rad2d single mutant (Fig. 3).
PMID:9092661	FYPO:0002550	sensitive to UV [has_severity] low	We found that the double mutant uvded rad2d was more resistant than a rad2d single mutant (Fig. 3).
PMID:9092661	GO:0070914	UV-damage excision repair	We found that the double mutant uvded rad2d was more resistant than a rad2d single mutant (Fig. 3). This implies that the Rad2 protein is very important for processing nicks introduced by UVDE..........These results show that the Rad2 protein is involved only in the UVDE-mediated second pathway and that there are both rad2-dependent and rad2-independent components of the UVDE-mediated repair pathway.
PMID:9105045	FYPO:0003289	abnormal protein localization to medial cortical node [assayed_using] PomBase:SPAC1F5.04c	(comment: cdc12 froms a cortical spot)
PMID:9111307	FYPO:0003241	unequal mitotic sister chromatid segregation	(comment: CHECK not sure if this is the right term, sent a question)
PMID:9125114	FYPO:0002118	decreased transporter activity [assayed_using] PomBase:SPCC1795.03	(comment: CHECK also increased (WT overexppression)) (comment: CHECK normal (WT))
PMID:9135147	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC119.08	(comment: yrosine; residue not determined)
PMID:9135148	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC11B10.09	(comment: inferring that residue is Y15, though not shown experimentally)
PMID:9136929	GO:1900745	positive regulation of p38MAPK cascade [part_of] cellular response to oxidative stress	(comment: not annotated to other stresses as subsequent papers show it is critical for assembly of signaling MAPKKK-MAPKKmodule)
PMID:9153313	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: same as crb2delta alone)
PMID:9153313	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: same as rad26delta alone)
PMID:9153313	FYPO:0000268	sensitive to UV during vegetative growth [has_severity] high	(comment: same as rad3delta alone)
PMID:9154834	FYPO:0004254	abnormal mitotic cell cycle regulation during cellular response to UV	(comment: doesn't resume normally)
PMID:9154834	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC24B11.06c	(comment: residue not determined, but probably Y173)
PMID:9154834	FYPO:0002033	abolished protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC24B11.06c	(comment: residue not determined, but probably Y173)
PMID:9154838	FYPO:0003875	inviable elongated cell with mitotic G2/M transition delay and cell cycle arrest in M phase [has_penetrance] 6	(comment: has condensed chromosomes)
PMID:9177184	GO:0004693	cyclin-dependent protein serine/threonine kinase activity [has_input] PomBase:SPBC14C8.07c	(comment: as cyclin-CDK complex with Cdc13 or Cig2)
PMID:9182664	FYPO:0003413	inviable branched, elongated, multiseptate vegetative cell	(comment: CHECK swollen)
PMID:9182664	FYPO:0002462	inviable branched, elongated vegetative cell	(comment: CHECK swollen)
PMID:9182664	FYPO:0002845	inviable swollen elongated septated vegetative cell	(comment: this might be dumbbell ask Jacky)
PMID:9200612	FYPO:0002060	viable vegetative cell population [has_penetrance] 30	(Fig. 1C ii)
PMID:9200612	FYPO:0002215	viable curved elongated vegetative cell [has_penetrance] 30	(Fig. 1C ii)
PMID:9200612	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 20	(Fig. 1C iii)
PMID:9200612	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [has_penetrance] 20	(Fig. 1C iii)
PMID:9200612	FYPO:0004700	bent vegetative cell [has_penetrance] 35	(Fig. 1C iii)
PMID:9200612	GO:0035838	growing cell tip [exists_during] mitotic G1 phase [exists_during] mitotic S phase [exists_during] mitotic G2 phase	(Fig. 2B, 2C)
PMID:9200612	GO:0035839	non-growing cell tip [exists_during] mitotic G1 phase [exists_during] mitotic S phase [exists_during] mitotic G2 phase	(Fig. 2B, 2C)
PMID:9200612	FYPO:0001587	normal protein localization to cell tip during vegetative growth	(Fig. 2C) Protein localised to both cell tips during monopolar growth
PMID:9200612	FYPO:0001587	normal protein localization to cell tip during vegetative growth	(Fig. 2C) protein localised to both cell tips
PMID:9200612	FYPO:0001587	normal protein localization to cell tip during vegetative growth	(Fig. 2D) Protein localised to both cell tips during monopolar growth
PMID:9200612	FYPO:0001677	increased protein localization to medial cortex during vegetative growth [assayed_using] PomBase:SPCC1223.06	(Fig. 3A)
PMID:9200612	FYPO:0004700	bent vegetative cell [assayed_using] PomBase:SPCC1223.06	(Fig. 3A)
PMID:9200612	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPCC1223.06	(Fig. 4A)
PMID:9200612	FYPO:0001587	normal protein localization to cell tip during vegetative growth [assayed_using] PomBase:SPCC1223.06	(Fig. 4A)
PMID:9200612	FYPO:0000190	abnormal actin cortical patch localization during vegetative growth [has_penetrance] high	(Fig. 4A)
PMID:9200612	FYPO:0000190	abnormal actin cortical patch localization during vegetative growth [has_penetrance] high	(Fig. 4A)
PMID:9200612	GO:1904511	cytoplasmic microtubule plus-end [exists_during] mitotic interphase	(Fig. 5) (comment: shown using TBZ treatment and wash out and by cold shock and relocalization)
PMID:9200612	FYPO:0006102	interphase microtubules absent from cell [has_penetrance] high	(Fig. 5C)
PMID:9200612	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPCC1223.06 [has_penetrance] high [has_severity] high	(Fig. 5C)
PMID:9200612	FYPO:0005798	decreased protein localization to cell cortex of cell tip during vegetative growth [assayed_using] PomBase:SPCC1223.06	(Fig. 5C)
PMID:9200612	FYPO:0006102	interphase microtubules absent from cell [has_penetrance] high	(Fig. 5C) (comment: cells blocked in mitosis so have no interphase MTs)
PMID:9200612	FYPO:0006103	short interphase microtubules [has_penetrance] high	(Fig. 6D)
PMID:9200612	FYPO:0005880	long interphase microtubules curved around cell end [has_penetrance] 10-15	(Fig. 6D)
PMID:9200612	FYPO:0004700	bent vegetative cell [has_penetrance] 70	data not shown
PMID:9200612	FYPO:0004700	bent vegetative cell [has_penetrance] 95	data not shown. 95% of cells re bent or T shaped but don't say the different percentages so I've left it as bent
PMID:9200612	FYPO:0002177	viable vegetative cell with normal cell morphology	data not shown. tea1 on multi copy plasmid -R2 suppresses the cell shape defect of tea1 delta
PMID:9201720	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC19F5.01c [part_of] positive regulation of G1/S transition of mitotic cell cycle	(comment: not shown that it is ser/thr kinase activity, just that it is kinase activity)
PMID:9202173	FYPO:0001682	normal alpha,alpha-trehalase activity increase during cellular response to salt stress	(Fig. 5)
PMID:9202173	FYPO:0003458	alpha,alpha-trehalase activity increase abolished during cellular response to salt stress	(Fig. 6)
PMID:9202173	FYPO:0003458	alpha,alpha-trehalase activity increase abolished during cellular response to salt stress	(Fig. 6)
PMID:9202173	FYPO:0003265	normal alpha,alpha-trehalase activity increase during cellular response to heat stress	(Fig. 7)
PMID:9202173	FYPO:0003265	normal alpha,alpha-trehalase activity increase during cellular response to heat stress	(Fig. 7)
PMID:9211982	FYPO:0003698	abnormal dense body present in nucleolus	truncated Gar2 accumulates in this dense body
PMID:9252327	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	Cell growth rate is reduced in later generation due to telomere shortening. In early generation, cells growth rate is not distingushiable from trt1+ cells.
PMID:9252327	FYPO:0001490	inviable elongated vegetative cell [has_severity] high	Cells look normal in early generation, but show many elongated cells in later generation due to telomere shortening.
PMID:9252327	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] high	Cells show progressive telomere shortening.
PMID:9252327	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	This allele removes motif B' through E in reverse transcriptase domain of telomerase catalytic subunit. This allele showed similar delayed grow defect phenotype as trt1∆::his3+ allele that remove 99% of ORF.
PMID:9252327	FYPO:0001490	inviable elongated vegetative cell [has_severity] high	This allele removes motif B' through E in reverse transcriptase domain of telomerase catalytic subunit. This allele showed similar extent of delayed cell elongation phenotype as trt1∆::his3+ allele that remove 99% of ORF.
PMID:9252327	FYPO:0002239	shortened telomeres during vegetative growth [has_severity] high	This allele removes motif B' through E in reverse transcriptase domain of telomerase catalytic subunit. This allele showed similar rate of telomere shortening as trt1∆::his3+ allele that remove 99% of ORF.
PMID:9278510	FYPO:0004259	abolished mitotic G2 DNA damage checkpoint	(Fig. 1)
PMID:9278510	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] low	(Fig. 2b)
PMID:9278510	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry [has_penetrance] low	(Fig. 2b)
PMID:9285594	GO:0000796	condensin complex	(Fig. 1)
PMID:9285594	GO:0000796	condensin complex	(Fig. 1)
PMID:9285594	FYPO:0005439	decreased DNA/DNA annealing activity [assayed_enzyme] condensin complex	(comment: CHECK in vitro)
PMID:9301023	FYPO:0005717	normal protein kinase activity during mitosis [assayed_enzyme] PomBase:SPBC11B10.09	(Figure 2a)
PMID:9301023	FYPO:0002519	abolished response to mitotic G2/M transition checkpoint signaling	(Figure 2b)
PMID:9303310	FYPO:0005993	normal cytoplasmic translation [assayed_using] PomBase:SPBC582.03 [has_penetrance] high	(Fig. 1) (comment: exponentially growing cells mainly in G2)
PMID:9303310	FYPO:0005993	normal cytoplasmic translation [assayed_using] PomBase:SPBC582.03 [has_penetrance] high	(Fig. 1) cells blocked in G1 at the restrictive temp
PMID:9303310	FYPO:0004200	increased protein degradation during mitotic G1 phase [assayed_using] PomBase:SPBC582.03	(Fig. 2)
PMID:9303310	FYPO:0006519	decreased protein degradation during mitotic G1 phase [assayed_using] PomBase:SPBC582.03	(Fig. 2)
PMID:9303310	FYPO:0004108	increased protein level during mitotic G1 phase [assayed_using] PomBase:SPBC582.03	(Fig. 2, Fig. 3)
PMID:9303310	FYPO:0005933	decreased protein level during mitotic G1 phase [assayed_using] PomBase:SPBC582.03	(Fig. 2, Fig. 3)
PMID:9303310	GO:0004861	cyclin-dependent protein serine/threonine kinase inhibitor activity [has_input] PomBase:SPBC582.03 [part_of] regulation of protein stability [part_of] negative regulation of mitotic cell cycle [happens_during] mitotic G1 phase	(Fig. 5)
PMID:9303310	FYPO:0000333	mitotic G1/S phase transition delay	(Fig. 7A)
PMID:9303310	FYPO:0004108	increased protein level during mitotic G1 phase [assayed_using] PomBase:SPBC32F12.09 [has_penetrance] high	(Fig. 7B)
PMID:9303310	MOD:00696	phosphorylated residue [added_by] PomBase:SPCC4E9.02	(Fig. 8) (comment: added by cig1 associated CDK1)
PMID:9303312	FYPO:0006506	normal RNA level during mitotic G1 phase [assayed_using] PomBase:SPBC14C8.07c	(Fig. 1A, C) (comment: cdc18 transcription is not dependent on cdc2 function)
PMID:9303312	FYPO:0003437	abolished protein kinase activity during mitotic G1 phase [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 1B) (comment: cdc2-M26 has no detectable kinase activity in G1 at restrictive temperature)
PMID:9303312	FYPO:0003449	abnormal cell cycle arrest at mitotic G1/S phase transition [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 1D) (comment: cdc2-M26 does not enter S phase even though cdc18 transcription is presence)
PMID:9303312	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC14C8.07c	(Fig. 2A) cells do not undergo re replication at restrictive temperature but cdc18 transcript increases
PMID:9303312	FYPO:0006506	normal RNA level during mitotic G1 phase [assayed_using] PomBase:SPBC14C8.07c	(Fig. 2B)
PMID:9303312	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition [has_penetrance] high	(Fig. 2B)
PMID:9303312	FYPO:0004596	abnormal negative regulation of DNA replication initiation during mitotic G2 phase resulting in complete rereplication [has_penetrance] high	(Fig. 2B)
PMID:9303312	FYPO:0006158	normal RNA level during mitotic S phase [assayed_using] PomBase:SPBC14C8.07c	(Fig. 2B)
PMID:9303312	FYPO:0000400	abnormal cell cycle arrest at mitotic G2/M phase transition [has_penetrance] high	(Fig. 2B) cells do not undergo re replication at restrictive temperature
PMID:9303312	FYPO:0000840	normal RNA level [assayed_using] PomBase:SPBC14C8.07c	(Fig. 3A) cdc18 transcript accumulates in absence of cdc13
PMID:9303312	FYPO:0000840	normal RNA level [assayed_using] PomBase:SPBC14C8.07c	(Fig. 3A) cdc18 transcript accumulates in absence of cig1, cig2 and cdc13
PMID:9303312	FYPO:0000836	increased protein level [assayed_using] PomBase:SPBC14C8.07c	(Fig. 3B) cdc18 protein accumulates in absence of cig1, cig2 and cdc13
PMID:9303312	FYPO:0003165	cut with abnormal chromosome segregation [has_penetrance] medium	(Fig. 3C) Abnormal DNA replication with cut DNA replication in absence cig1, cig2 and cdc13 promoter ON some cells have a cut phenotype. (comment: NOT sure the data warrants an annotation)
PMID:9303312	FYPO:0001343	abnormal mitotic DNA replication [has_penetrance] medium	(Fig. 3C) Abnormal DNA replication with cut DNA replication in absence cig1, cig2 and cdc13 promoter ON some cells have a cut phenotype. (comment: NOT sure the data warrants an annotation)
PMID:9303312	FYPO:0004629	normal mitotic DNA replication [has_penetrance] high	(Fig. 3C) DNA replication in presence of cig1 and cig2
PMID:9303312	FYPO:0003485	abolished DNA synthesis [has_penetrance] high	(Fig. 3C) no DNA replication in absence of all 3 cyclins
PMID:9303312	FYPO:0004242	decreased protein kinase activity during mitotic S phase [assayed_enzyme] PomBase:SPBC11B10.09 [has_severity] high	(Fig. 3C, D) Absence of cdc2 kinase activity in absence cig1, cig2 and cdc13
PMID:9303312	FYPO:0003332	normal protein kinase activity during mitotic interphase [has_penetrance] medium	(Fig. 3C, D) cdc13 promoter ON cdc2 kinase activity acts after the accumulation of cdc18 protein to bring about the G1/S transition
PMID:9303312	PomGeneEx:0000017	RNA level fluctuates [during] single-celled organism vegetative growth phase	(Fig. 4B)
PMID:9303312	FYPO:0004235	normal RNA level oscillation during mitotic cell cycle [assayed_using] PomBase:SPBC14C8.07c	(Fig. 4C) Cdc18 transcript is low during G2
PMID:9303312	FYPO:0004235	normal RNA level oscillation during mitotic cell cycle [assayed_using] PomBase:SPBC14C8.07c	(Fig. 4C) Cdc18 transcript is low during G2
PMID:9303312	FYPO:0000840	normal RNA level [assayed_using] PomBase:SPBC14C8.07c	(Fig. 4C) Cdc2 not required for active cdc10 dependent transcription during S phase
PMID:9303312	FYPO:0003246	normal mitotic S phase progression	(Fig. 4D)
PMID:9303312	FYPO:0003246	normal mitotic S phase progression	(Fig. 4D)
PMID:9303312	GO:0001227	DNA-binding transcription repressor activity, RNA polymerase II-specific [happens_during] mitotic G2 phase [part_of] negative regulation of transcription by RNA polymerase II	(Fig. 5, 6, 7)
PMID:9303312	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [happens_during] mitotic G1 phase [part_of] positive regulation of transcription by RNA polymerase II	(Fig. 5, 6, 7)
PMID:9303312	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPBC14C8.07c	(Fig. 5A) decreased cdc18 transcript in HU block and on release
PMID:9303312	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPBC14C8.07c	(Fig. 5A, B) decreased cdc18 transcript in HU block and on release
PMID:9303312	FYPO:0000826	decreased RNA level [assayed_using] PomBase:SPBC14C8.07c	(Fig. 5A, B) decreased cdc18 transcript in HU block and on release
PMID:9303312	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC14C8.07c	(Fig. 5A, B) level of cdc18 transcript does not decreased after release from HU block
PMID:9303312	FYPO:0004235	normal RNA level oscillation during mitotic cell cycle	(Fig. 5C)
PMID:9303312	FYPO:0001890	increased RNA level [assayed_using] PomBase:SPBC14C8.07c	(Fig. 5C) rep2delta has no effect on cdc18 transcript levels in the absence of res2
PMID:9303312	FYPO:0004988	abnormal RNA level oscillation during mitotic cell cycle [assayed_using] PomBase:SPBC14C8.07c	(Fig. 6B)
PMID:9303312	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC14C8.07c	(Fig. 6B)
PMID:9303312	FYPO:0004988	abnormal RNA level oscillation during mitotic cell cycle [assayed_using] PomBase:SPBC14C8.07c	(Fig. 6C)
PMID:9303312	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC14C8.07c	(Fig. 6C)
PMID:9303312	FYPO:0004988	abnormal RNA level oscillation during mitotic cell cycle [assayed_using] PomBase:SPBC14C8.07c	(Fig. 6D)
PMID:9303312	FYPO:0001117	decreased RNA level during vegetative growth [assayed_using] PomBase:SPBC14C8.07c	(Fig. 6D)
PMID:9303312	FYPO:0000780	increased transcription during vegetative growth [assayed_using] PomBase:SPBC14C8.07c	(Fig. 7)
PMID:9303312	FYPO:0000825	increased RNA level during vegetative growth [assayed_using] PomBase:SPBC14C8.07c	(Fig. 7) (comment: CHECK res1 on multi copy pREP3X ON)
PMID:9303312	FYPO:0006562	increased RNA level during mitotic G2 phase [assayed_using] PomBase:SPBC14C8.07c	(Fig. 7) (comment: CHECK res1 on multi copy pREP3X ON)
PMID:9303312	FYPO:0004988	abnormal RNA level oscillation during mitotic cell cycle [assayed_using] PomBase:SPBC14C8.07c	(Fig. 7) (comment: CHECK res1 on multi copy pREP3X ON)
PMID:9303312	FYPO:0004235	normal RNA level oscillation during mitotic cell cycle [assayed_using] PomBase:SPBC14C8.07c	(Fig. 7) (comment: CHECK res2 on multi copy pREP3X ON)
PMID:9303312	FYPO:0004235	normal RNA level oscillation during mitotic cell cycle [assayed_using] PomBase:SPBC14C8.07c	(Fig. 7) (comment: CHECK res2 on multi copy pREP3X ON)
PMID:9303312	FYPO:0000659	abolished DNA binding [assayed_using] MCB [assayed_using] MBF transcription complex	(Fig. 8) (comment: DSC1 is now called MBF)
PMID:9303312	FYPO:0000659	abolished DNA binding [assayed_using] MCB [assayed_using] MBF transcription complex	(Fig. 8) (comment: DSC1 is now called MBF)
PMID:9303312	GO:0030907	MBF transcription complex [exists_during] mitotic G2 phase	(Fig. 8) Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	GO:0030907	MBF transcription complex [exists_during] mitotic G2 phase	(Fig. 8) Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	GO:0030907	MBF transcription complex [exists_during] mitotic G2 phase	(Fig. 8) Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	GO:0030907	MBF transcription complex [exists_during] mitotic G2 phase	(Fig. 8) Presence of MBF is correlated with cdc10 dependent transcription repression during G2
PMID:9303312	FYPO:0000659	abolished DNA binding [assayed_using] MCB [assayed_using] MBF transcription complex	(Fig. 8B) (comment: DSC1 is now called MBF)
PMID:9303312	FYPO:0000659	abolished DNA binding [assayed_using] MCB [assayed_using] MBF transcription complex	(Fig. 8B) (comment: DSC1 is now called MBF)
PMID:9303312	FYPO:0006563	abolished MBF complex assembly during mitotic G1 phase [has_penetrance] high	(Fig. 8C)
PMID:9303312	FYPO:0003436	decreased protein kinase activity during mitotic G2 phase [assayed_using] PomBase:SPBC14C8.07c	Cdc2 kinase activity is low during G2 data not shown
PMID:9303312	FYPO:0004235	normal RNA level oscillation during mitotic cell cycle [assayed_using] PomBase:SPBC14C8.07c	Data not shown
PMID:9312055	FYPO:0002060	viable vegetative cell population	(Fig. 1b)
PMID:9312055	FYPO:0002061	inviable vegetative cell population	(Fig. 1b)
PMID:9312055	FYPO:0002061	inviable vegetative cell population	(Fig. 1b)
PMID:9312055	FYPO:0002061	inviable vegetative cell population	(Fig. 1b)
PMID:9312055	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 1b)
PMID:9312055	FYPO:0001946	abolished mitotic sister chromatid separation	(Fig. 1c)
PMID:9312055	FYPO:0003165	cut with abnormal chromosome segregation	(Fig. 1c)
PMID:9312055	FYPO:0001946	abolished mitotic sister chromatid separation	(Fig. 1c)
PMID:9312055	FYPO:0003165	cut with abnormal chromosome segregation	(Fig. 1c)
PMID:9312055	FYPO:0001946	abolished mitotic sister chromatid separation	(Fig. 1c)
PMID:9312055	FYPO:0003165	cut with abnormal chromosome segregation	(Fig. 1c)
PMID:9312055	FYPO:0002061	inviable vegetative cell population	(Fig. 2)
PMID:9312055	FYPO:0002060	viable vegetative cell population	(Fig. 2) (comment: CHECK synthetic rescue)
PMID:9312055	FYPO:0002060	viable vegetative cell population	(Fig. 2) (comment: CHECK synthetic rescue)
PMID:9312055	FYPO:0002061	inviable vegetative cell population	(Fig. 3b)
PMID:9312055	FYPO:0002061	inviable vegetative cell population	(Fig. 3b)
PMID:9312055	FYPO:0002061	inviable vegetative cell population	(Fig. 3b)
PMID:9312055	FYPO:0002061	inviable vegetative cell population	(Fig. 3b) (comment: CHECK rescue)
PMID:9312055	FYPO:0002060	viable vegetative cell population	(Fig. 3b) (comment: CHECK rescue)
PMID:9312055	FYPO:0004157	increased protein level during mitosis [assayed_using] PomBase:SPBC582.03	(Fig. 4)
PMID:9312055	FYPO:0004157	increased protein level during mitosis [assayed_using] PomBase:SPBC14C8.01c	(Fig. 4)
PMID:9312055	FYPO:0005925	normal protein level during mitosis [assayed_using] PomBase:SPBC582.03	(Fig. 4a)
PMID:9312055	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase [has_penetrance] 45	(Fig. 4b-d)
PMID:9312055	FYPO:0005933	decreased protein level during mitotic G1 phase [assayed_using] PomBase:SPBC11B10.09	(Fig. 6)
PMID:9312055	FYPO:0004108	increased protein level during mitotic G1 phase [assayed_using] PomBase:SPBC582.03	(Fig. 6)
PMID:9312055	MOD:00696	phosphorylated residue [added_during] mitotic M phase	(Fig. 7)
PMID:9312055	FYPO:0005928	abolished protein polyubiquitination during vegetative growth [assayed_using] PomBase:SPBC14C8.01c	(Fig. 9)
PMID:9312055	FYPO:0005927	normal protein monoubiquitination during vegetative growth [assayed_using] PomBase:SPBC14C8.01c	(Fig. 9)
PMID:9312055	MOD:01148	ubiquitinylated lysine	(comment: poly...)
PMID:9315645	GO:0062038	positive regulation of pheromone response MAPK cascade	"(comment: This one comes in ""from the side"", see Ladds, Bond post 2010 publication summary)"
PMID:9321395	FYPO:0000082	decreased cell population growth at high temperature	(Figure 4)
PMID:9321395	FYPO:0000271	sensitive to salt stress	(Figure 4)
PMID:9321395	FYPO:0001492	viable elongated vegetative cell	(Figure 4)
PMID:9321395	FYPO:0001492	viable elongated vegetative cell	(Figure 4)
PMID:9321395	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC24B11.06c	(Figure 5)
PMID:9321395	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC24B11.06c	(Figure 5)
PMID:9321395	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC24B11.06c	(Figure 5)
PMID:9321395	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC24B11.06c	(Figure 5)
PMID:9321395	GO:0038066	p38MAPK cascade	An increased level of phosphotyrosine was detected on Spc1 in wis1+ cells overexpressing Wis4∆N, but not in wis1∆ cells, indicating that the action of Wis4 is Wis1- dependent.
PMID:9321395	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC24B11.06c	data not shown
PMID:9321395	FYPO:0002177	viable vegetative cell with normal cell morphology	data not shown
PMID:9325108	GO:0008821	crossover junction DNA endonuclease activity	(comment: CHECK activated_by(CHEBI:18420)| activated_by(CHEBI:29035))
PMID:9325304	FYPO:0006477	abnormal mitotic metaphase/anaphase transition	Figure 3B
PMID:9325304	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	Figure 3B
PMID:9325316	GO:0003899	DNA-directed RNA polymerase activity [part_of] transcription by RNA polymerase II	(comment: vw: author intent)
PMID:9325316	GO:0003899	DNA-directed RNA polymerase activity [part_of] transcription by RNA polymerase II	(comment: vw: author intent)
PMID:9325316	GO:0003899	DNA-directed RNA polymerase activity [part_of] transcription by RNA polymerase II	(comment: vw: author intent)
PMID:9325316	GO:0003899	DNA-directed RNA polymerase activity [part_of] transcription by RNA polymerase II	(comment: vw: author intent)
PMID:9325316	GO:0003677	DNA binding	(comment: vw: binds DNA in complex (2,3,11))
PMID:9325316	GO:0003677	DNA binding	(comment: vw: binds DNA in complex (2,3,11))
PMID:9325316	GO:0003677	DNA binding	(comment: vw: binds DNA in complex (2,3,11))
PMID:9325316	GO:0003677	DNA binding	(comment: vw: binds DNA on its own)
PMID:9371883	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC146.07 [assayed_using] PomBase:SPBC1289.02c	(comment: two-hybrid assay)
PMID:9371883	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC146.07 [assayed_using] PomBase:SPBC1289.02c	(comment: two-hybrid assay)
PMID:9371883	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC146.07 [assayed_using] PomBase:SPBC1289.02c	(comment: two-hybrid assay)
PMID:9371883	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC146.07 [assayed_using] PomBase:SPBC1289.02c	(comment: two-hybrid assay)
PMID:9372936	FYPO:0000838	normal protein localization to nucleus during vegetative growth	(comment: assayed using SV40 NLS-GFP-LacZ reporter protein)
PMID:9372936	FYPO:0000838	normal protein localization to nucleus during vegetative growth	(comment: assayed using SV40 NLS-GFP-LacZ reporter protein)
PMID:9372936	FYPO:0001355	decreased vegetative cell population growth	(comment: same as rae1-167 single mutant)
PMID:9372936	FYPO:0001355	decreased vegetative cell population growth	(comment: same as rae1-167 single mutant)
PMID:9398669	FYPO:0001425	abnormal negative regulation of mitotic DNA replication initiation resulting in complete rereplication	(Fig. 5a)
PMID:9398669	FYPO:0000280	sterile [has_penetrance] 80	(Fig. 5c) (comment: switched from conjugtion freqeuncy to sterility as can only capture penetance on cell phenotypes)
PMID:9398669	FYPO:0000303	decreased conjugation frequency	(comment: CHECK add penetrance?)
PMID:9398669	FYPO:0005409	normal protein level during cell cycle arrest in mitotic G1 phase in response to nitrogen starvation [assayed_using] PomBase:SPAPB2B4.03	(comment: G1 phase nitrogen induced arrest)
PMID:9398669	GO:0031568	mitotic G1 cell size control checkpoint signaling [happens_during] cellular response to nitrogen starvation	(comment: because slp1 can bypass wee1 it must independently inhibit cdc2)
PMID:9398669	GO:0031568	mitotic G1 cell size control checkpoint signaling [happens_during] cellular response to nitrogen starvation	(comment: because slp1 can bypass wee1 it must independently inhibit cdcs)
PMID:9398669	FYPO:0005401	increased protein level during mitotic G1 cell cycle arrest in response to nitrogen starvation [assayed_using] PomBase:SPBC582.03	(comment: nitrogen induced arrest)
PMID:9420333	GO:0004674	protein serine/threonine kinase activity [part_of] septation initiation signaling [occurs_in] new mitotic spindle pole body [happens_during] mitotic anaphase B	"(Fig. 1) (comment: vw interpretation for ""active form"")"
PMID:9420333	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPBC21.06c	(Fig. 2A) loss of cdc16 function does not affect cdc7 kinase activity
PMID:9420333	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPBC21.06c	(Fig. 2A) loss of spg1 function does not affect cdc7 kinase activity
PMID:9420333	GO:0044732	mitotic spindle pole body [exists_during] mitotic metaphase	(Fig. 3A,C) spg1-HA observed at SPB throughout the mitotic cell cycle
PMID:9420333	GO:0044732	mitotic spindle pole body [exists_during] mitotic interphase	(Fig. 3A,C) spg1-HA observed at SPB throughout the mitotic cell cycle
PMID:9420333	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_using] PomBase:SPBC21.06c [has_penetrance] high	(Fig. 5A)
PMID:9420333	FYPO:0006825	abolished protein localization to mitotic spindle pole body during mitosis [assayed_using] PomBase:SPBC21.06c [has_penetrance] high	(Fig. 5A)
PMID:9420333	FYPO:0002967	normal protein localization to mitotic spindle pole body [has_penetrance] high [assayed_using] PomBase:SPAC1565.06c	(Fig. 5B)
PMID:9420333	FYPO:0001876	decreased asymmetric protein localization, with protein localized to both mitotic spindle pole bodies during anaphase [has_penetrance] high [assayed_using] PomBase:SPBC21.06c	(Fig. 6A) in late anaphase cdc7 is normally localized only one SPB
PMID:9420333	FYPO:0001876	decreased asymmetric protein localization, with protein localized to both mitotic spindle pole bodies during anaphase [assayed_protein] PomBase:SPBC21.06c	(Fig. 6C) in late anaphase cdc7 is normally localized only one SPB
PMID:9420333	GO:0071958	new mitotic spindle pole body [exists_during] mitotic anaphase B	(comment: From this paper we don't actuallyyet know that it's the new one, that comes later, but ..)cdc7 is associated with both SPBs when a short spindle is present)
PMID:9420333	GO:0035591	signaling adaptor activity [has_input] PomBase:SPBC21.06c [part_of] septation initiation signaling [happens_during] mitotic metaphase [occurs_in] old mitotic spindle pole body	(comment: GTP bound)
PMID:9420333	GO:0035591	signaling adaptor activity [has_input] PomBase:SPBC21.06c [part_of] septation initiation signaling [occurs_in] new mitotic spindle pole body [happens_during] mitotic metaphase	(comment: GTP bound)
PMID:9420333	GO:0035591	signaling adaptor activity [has_input] PomBase:SPBC21.06c [part_of] septation initiation signaling [occurs_in] new mitotic spindle pole body [happens_during] mitotic anaphase B	(comment: GTP bound)
PMID:9428701	GO:0004722	protein serine/threonine phosphatase activity	(comment: MBP substrate),(comment: CHECK activated_by(CHEBI:29035))
PMID:9430640	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC32F12.09 [has_penetrance] high [has_severity] high	(Fig. 10)
PMID:9430640	PomGeneEx:0000019	protein level decreased [during] mitotic S phase	(Fig. 1B)
PMID:9430640	PomGeneEx:0000021	protein present [during] mitotic G1 phase	(Fig. 1B)
PMID:9430640	PomGeneEx:0000018	protein level increased [during] mitotic anaphase	(Fig. 1B)
PMID:9430640	PomGeneEx:0000017	RNA level fluctuates [during] mitotic G2 phase	(Fig. 1C) Peaks at the end of G2 40 min before peak of rum1 protein
PMID:9430640	FYPO:0000836	increased protein level [assayed_using] PomBase:SPBC32F12.09	(Fig. 2)
PMID:9430640	MOD:01148	ubiquitinylated lysine	(Fig. 2)
PMID:9430640	FYPO:0001122	elongated vegetative cell [has_severity] medium	(Fig. 3) (comment: data not shown phenotype similar to rum+OP)
PMID:9430640	FYPO:0001234	slow vegetative cell population growth [has_severity] high	(Fig. 3B) (comment: CHECK: similar to rum1+OP more severe than either single mutant expressed from muliticopy plasmid. Colonies were integrants)
PMID:9430640	MOD:00047	O-phospho-L-threonine	(Fig. 3C)
PMID:9430640	FYPO:0000158	DNA content increased during vegetative growth [has_penetrance] high	(Fig. 3C) (comment: integrated copy)
PMID:9430640	GO:0004861	cyclin-dependent protein serine/threonine kinase inhibitor activity [has_input] PomBase:SPBC11B10.09 [has_input] PomBase:SPAPB2B4.03	(Fig. 4B) (comment: inhibitory for cdc2/cdc13 and cdc2/cig2 but not cdc2/cig1. Both Rum1+ and Rum1-A58A62 can inhibit cdk1 activity)
PMID:9430640	GO:0004861	cyclin-dependent protein serine/threonine kinase inhibitor activity [has_input] PomBase:SPBC11B10.09 [has_input] PomBase:SPBC582.03	(Fig. 4B) (comment: inhibitory for cdc2/cdc13 and cdc2/cig2 but not cdc2/cig1. Both Rum1+ and Rum1-A58A62 can inhibit cdk1 activity)
PMID:9430640	GO:2000134	negative regulation of G1/S transition of mitotic cell cycle [happens_during] mitotic G1 phase	(Fig. 5)
PMID:9430640	FYPO:0007766	abolished protein level oscillation during mitotic cell cycle [has_penetrance] high [assayed_using] PomBase:SPBC32F12.09	(Fig. 5B)
PMID:9430640	FYPO:0000333	mitotic G1/S phase transition delay [has_severity] medium	(Fig. 6)
PMID:9430640	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC11B10.09 [added_by] PomBase:SPCC4E9.02	(Fig. 7,8) cdc2-cig1 complex efficiently phosphorylates rum1 T58T62 residues in vivo . Phosphorylation by cdc2-cig2 or cdc2-cdc13 only observed after a very long exposure
PMID:9430640	MOD:00047	O-phospho-L-threonine [added_by] PomBase:SPBC11B10.09 [added_by] PomBase:SPCC4E9.02	(Fig. 7,8) cdc2-cig1 complex efficiently phosphorylates rum1 T58T62 residues in vivo . Phosphorylation by cdc2-cig2 or cdc2-cdc13 only observed after a very long exposure
PMID:9430640	FYPO:0002033	abolished protein phosphorylation during vegetative growth [has_penetrance] high [assayed_using] PomBase:SPBC32F12.09	(Fig. 7B) rum1 A58A62 mutant protein is unable to be phosphorylated by cdc2/cig1
PMID:9430640	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process [has_input] PomBase:SPBC32F12.09	(comment: this isn't quite the right way to capture this target, still thinking)
PMID:9430640	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process [has_input] PomBase:SPBC32F12.09	(comment: this isn't quite the right way to capture this target, still thinking)
PMID:9450991	FYPO:0002061	inviable vegetative cell population	(Fig. 4A)
PMID:9450991	FYPO:0000016	curved vegetative cell	(Figure 1A)
PMID:9450991	FYPO:0003166	monoseptate vegetative cell with binucleate and anucleate compartments	(Figure 1A)
PMID:9450991	FYPO:0003166	monoseptate vegetative cell with binucleate and anucleate compartments	(Figure 1A)
PMID:9450991	FYPO:0002071	mislocalized nucleus during vegetative growth [has_penetrance] 80	(Figure 1A)
PMID:9450991	FYPO:0000013	T-shaped vegetative cell with normal cell length [has_penetrance] 6	(Figure 1A)
PMID:9450991	FYPO:0004702	cytoplasmic microtubules absent from cell	(Figure 2A,B)
PMID:9450991	FYPO:0001490	inviable elongated vegetative cell	(Figure 4B)
PMID:9450991	FYPO:0001418	abnormal microtubule cytoskeleton morphology during vegetative growth	30x Figure 4B
PMID:9459302	FYPO:0002455	abnormal septum during vegetative growth [has_penetrance] 59	(comment: CHECK is this OK? its aseptate?)
PMID:9468529	GO:0008444	CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity	(comment: CHECK inhibited_by CHEBI:29035)
PMID:9488736	GO:0004674	protein serine/threonine kinase activity [has_input] PomBase:SPBC146.07	(comment: looks very likely it is a ser/thr kinase, but if anything comes up that contradicts it this annotation can be made less specific)
PMID:9491802	FYPO:0002061	inviable vegetative cell population	(comment: expressed Clostridium botulinum C3 protein to ADP-ribosylate Rho proteins including Rho1)
PMID:9524127	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC20G4.04c	(Fig. 3)
PMID:9524127	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC20G4.04c [assayed_using] PomBase:SPAC1952.07	(Fig. 3a)
PMID:9524127	FYPO:0001324	decreased protein level during vegetative growth [assayed_using] PomBase:SPAC20G4.04c	(Fig. 3a)
PMID:9524127	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC20G4.04c [assayed_using] PomBase:SPAC1952.07	(Fig. 3a)
PMID:9524127	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC20G4.04c [assayed_using] PomBase:SPAC1952.07	(Fig. 3a)
PMID:9524127	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC20G4.04c [assayed_using] PomBase:SPAC1952.07	(Fig. 3a)
PMID:9524127	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC20G4.04c [assayed_using] PomBase:SPAC1952.07	(Fig. 3a)
PMID:9524127	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPAC20G4.04c [assayed_using] PomBase:SPAC1952.07	(Fig. 3a)
PMID:9524127	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPAC20G4.04c [assayed_using] PomBase:SPAC1952.07	(Fig. 3a)
PMID:9531532	FYPO:0002061	inviable vegetative cell population	(comment: over 25)
PMID:9531532	FYPO:0000276	monopolar mitotic spindle	(comment: over 25)
PMID:9531532	FYPO:0002060	viable vegetative cell population	(comment: over 25)
PMID:9531532	FYPO:0002061	inviable vegetative cell population	(comment: over 25)
PMID:9531532	FYPO:0002061	inviable vegetative cell population	(comment: over 35)
PMID:9535817	FYPO:0005288	decreased negative regulation of transcription by glucose	(comment: inferred from FYPO:0000825, FYPO:0001117, FYPO:0005743, FYPO:0007674 phenotypes (including conditions))
PMID:9552380	GO:0000307	cyclin-dependent protein kinase holoenzyme complex	(comment: cig2-cdc2)
PMID:9560390	FYPO:0001122	elongated vegetative cell	(comment: CHECK osmotic stress)
PMID:9560390	FYPO:0001122	elongated vegetative cell	(comment: CHECK osmotic stress)
PMID:9571240	FYPO:0000398	premature mitotic G1/S phase transition	(Fig. 3)
PMID:9571240	FYPO:0001054	cut, elongated cell	(Figure 4e)
PMID:9571240	FYPO:0003012	mitosis with unreplicated DNA	(Figure 4e)
PMID:9571240	GO:2000134	negative regulation of G1/S transition of mitotic cell cycle	Ste9 was indispensable for the growth of the wee1 cells, which had to lengthen the pre-Start G1 period to restrain DNA synthesis until the critical size to override Start control was attained....Ste9 might be required for maintenance of the Cdc2 kinase in a pre-Start form, suggested by the fact that overexpression of Ste9 induced rereplication of the genome due to reduction of the mitotic kinase activity of the Cdc13/Cdc2 complex, and rereplication in the cdc2ts strain was prevented by the ste9 mutation.
PMID:9572736	MOD:00696	phosphorylated residue [increased_in_presence_of] hydroxyurea [added_during] mitotic S phase	(Fig. 1C)
PMID:9572736	FYPO:0000776	normal protein phosphorylation during vegetative growth [assayed_protein] PomBase:SPCC18B5.03	(Fig. 1C)
PMID:9572736	FYPO:0004353	increased protein phosphorylation during mitotic S phase [assayed_protein] PomBase:SPCC18B5.03	(Fig. 1C)
PMID:9572736	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPCC18B5.03	(Fig. 2A)
PMID:9572736	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPCC18B5.03	(Fig. 2A)
PMID:9572736	FYPO:0002098	decreased protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPCC18B5.03	(Fig. 2A)
PMID:9572736	FYPO:0002096	increased protein phosphorylation during cellular response to hydroxyurea [assayed_protein] PomBase:SPCC18B5.03	(Fig. 2B)
PMID:9572736	MOD:00696	phosphorylated residue [added_by] PomBase:SPCC18B5.11c [increased_in_presence_of] hydroxyurea	(Fig. 3B)
PMID:9572736	FYPO:0004194	decreased protein level during cellular response to hydroxyurea [assayed_protein] PomBase:SPBC660.14	(Fig. 3C)
PMID:9572736	PomGeneEx:0000018	protein level increased [in_presence_of] hydroxyurea	(Fig. 3C)
PMID:9572736	FYPO:0004194	decreased protein level during cellular response to hydroxyurea [assayed_protein] PomBase:SPBC660.14	(Fig. 3C)
PMID:9572736	FYPO:0000088	sensitive to hydroxyurea	(Fig. 3D)
PMID:9572736	FYPO:0001492	viable elongated vegetative cell	(Fig. 4)
PMID:9572736	FYPO:0001492	viable elongated vegetative cell	(Fig. 4)
PMID:9572736	FYPO:0003503	normal vegetative cell length	(Fig. 4)
PMID:9572736	FYPO:0003503	normal vegetative cell length	(Fig. 4)
PMID:9572736	FYPO:0003503	normal vegetative cell length	(Fig. 4)
PMID:9572736	FYPO:0001492	viable elongated vegetative cell	(Fig. 4)
PMID:9572736	FYPO:0003503	normal vegetative cell length	(Fig. 4)
PMID:9572736	FYPO:0003503	normal vegetative cell length	(Fig. 4)
PMID:9572736	FYPO:0003503	normal vegetative cell length	(Fig. 4)
PMID:9572736	FYPO:0005189	abnormal re-entry into mitotic cell cycle after arrest in response to hydroxyurea	(Fig. 5A)
PMID:9572736	FYPO:0005189	abnormal re-entry into mitotic cell cycle after arrest in response to hydroxyurea	(Fig. 5A)
PMID:9572736	FYPO:0005189	abnormal re-entry into mitotic cell cycle after arrest in response to hydroxyurea	(Fig. 5A)
PMID:9572736	FYPO:0000963	normal growth on hydroxyurea	(Fig. 5B)
PMID:9572736	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 5B)
PMID:9572736	FYPO:0000088	sensitive to hydroxyurea [has_severity] high	(Fig. 5B)
PMID:9572736	FYPO:0000088	sensitive to hydroxyurea [has_severity] medium	(Fig. 5B)
PMID:9585506	FYPO:0001490	inviable elongated vegetative cell	(comment: CHECK salt stress)
PMID:9585506	FYPO:0001490	inviable elongated vegetative cell	(comment: CHECK salt stress)
PMID:9585506	FYPO:0001490	inviable elongated vegetative cell	(comment: CHECK salt stress)
PMID:9585506	FYPO:0001490	inviable elongated vegetative cell	(comment: CHECK salt stress)
PMID:9585506	GO:0005515	protein binding	(comment: western but we know this happens and I wanted to capture the extension)
PMID:9585506	GO:0005515	protein binding	(comment: western but we know this happens and I wanted to capture the extension)
PMID:9601094	FYPO:0002303	inviable mononucleate monoseptate vegetative cell with anucleate compartment [has_penetrance] 44	(Fig. 2D)
PMID:9601094	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase [has_penetrance] 15	(Fig. 3C) (comment: CHECK at metaphase/anaphase transiton)
PMID:9601094	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	(Fig. 3C) (comment: CHECK at metaphase/anaphase transiton)
PMID:9601094	FYPO:0003903	loss of viability at low temperature	(Fig. 4B)
PMID:9601094	FYPO:0000229	cut [has_penetrance] ~14	(Fig. 4B)
PMID:9601094	FYPO:0002303	inviable mononucleate monoseptate vegetative cell with anucleate compartment [has_penetrance] ~14	(Fig. 4B)
PMID:9601094	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase [has_penetrance] 60	(Fig. 4D)
PMID:9601094	FYPO:0000091	sensitive to thiabendazole [has_severity] high	(Figure 4A)
PMID:9601094	FYPO:0001399	normal mitotic spindle	(Figure 6)
PMID:9601094	FYPO:0001399	normal mitotic spindle	(Figure 6)
PMID:9601094	FYPO:0001357	normal vegetative cell population growth	(Figure 6)
PMID:9601094	FYPO:0001357	normal vegetative cell population growth	(comment: medium level of mph1 OEX (high is lethal))
PMID:9601094	FYPO:0000964	normal growth on thiabendazole	dph1∆ cells were not hypersensitive to TBZ, compared to wild-type cells (Fig. 6C)
PMID:9606213	FYPO:0000573	normal shmoo formation	(Fig. 1)
PMID:9606213	FYPO:0000573	normal shmoo formation	(Fig. 1)
PMID:9606213	FYPO:0000573	normal shmoo formation	(Fig. 1)
PMID:9606213	FYPO:0003626	normal protein localization to shmoo tip [assayed_using] PomBase:SPAC4A8.15c	(Fig. 7)
PMID:9606213	FYPO:0006505	abolished protein localization to shmoo tip [assayed_using] PomBase:SPBC32H8.12c [has_penetrance] 70	(comment: DNS actin distributed in cytoplasm)
PMID:9606213	FYPO:0001366	normal actin cytoskeleton organization [has_penetrance] 82 [assayed_using] PomBase:SPBC32H8.12c	(commment: polarization, in shmoo DNS)
PMID:9606213	FYPO:0003626	normal protein localization to shmoo tip [assayed_using] PomBase:SPAC20G4.02c	(slightly increased- In fact, more cells had staining at their tips than wild-type cells, probably indicating a prolonged attempt to conjugate, after which the protein delocalizes)
PMID:9606213	FYPO:0003626	normal protein localization to shmoo tip [assayed_using] PomBase:SPAC20G4.02c	(slightly increased- In fact, more cells had staining at their tips than wild-type cells, probably indicating a prolonged attempt to conjugate, after which the protein delocalizes)
PMID:9606213	GO:0043332	mating projection tip	By immunofluorescence, these antibodies stained a single dot at the very tip of each cell in wild-type pre-zygotes (Fig. 2, C and D).
PMID:9606213	FYPO:0003626	normal protein localization to shmoo tip [assayed_using] PomBase:SPAC20G4.02c	In fact, more cells had staining at their tips than wild-type cells, probably indicating a prolonged attempt to conjugate, after which the protein delocalizes
PMID:9606213	FYPO:0006505	abolished protein localization to shmoo tip [assayed_using] PomBase:SPAC20G4.02c	Therefore, in a h90 mam2 strain, the P cells will attempt mating, but the M cells will be unable to respond due to the lack of the P-factor receptor and so the cells will fail to initiate fusion
PMID:9606213	FYPO:0001366	normal actin cytoskeleton organization [has_penetrance] 82 [assayed_using] PomBase:SPBC32H8.12c	polarization, during conjugation, in shmoo Fig1. We interpret the data as indicating that F-actin is first correctly localized to the tip in all fus1 mutants, but is then redistributed after a defective attempt to fuse. Thus, it is likely that Fus1 is required for the correct organization and stabilization of polarized F-actin at the tip, but is no
PMID:9614176	FYPO:0000531	abolished mitotic cell cycle arrest in response to pheromone [has_penetrance] high	(Fig. 1A)
PMID:9614176	GO:0031568	mitotic G1 cell size control checkpoint signaling	(Fig. 2B) after addition of P factor to nitrogen starved G1 arrested cells P factor does not further increase rum1 protein level. It is inferred that rum1 is required to maintain G1 arrest rather than bring it about.
PMID:9614176	FYPO:0006571	increased cyclin-dependent protein kinase activity during cellular response to pheromone [assayed_using] PomBase:SPBC582.03 [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 3A) In absence of rum1 cdc2-cdc13 kinase activity remains high in presence of P factor
PMID:9614176	FYPO:0000531	abolished mitotic cell cycle arrest in response to pheromone [has_penetrance] high	(Fig. 3D) loss of cig2 does not restore P factor induced G1 arrest
PMID:9614176	FYPO:0006574	normal RNA level during cellular response to pheromone [assayed_using] PomBase:SPBC582.03	(Fig. 4)
PMID:9614176	FYPO:0006572	abolished protein degradation during cellular response to pheromone [assayed_using] PomBase:SPBC582.03 [has_penetrance] high	(Fig. 4) (comment: sows proteasome involvment as well)
PMID:9614176	FYPO:0000532	decreased mitotic cell cycle arrest in response to pheromone [has_penetrance] high	(Fig. 5A)
PMID:9614176	FYPO:0006571	increased cyclin-dependent protein kinase activity during cellular response to pheromone [assayed_using] PomBase:SPAPB2B4.03 [assayed_enzyme] PomBase:SPBC11B10.09 [has_severity] high	(Fig. 5B)
PMID:9614176	FYPO:0006573	normal protein level during cellular response to pheromone [has_penetrance] high [assayed_using] PomBase:SPAPB2B4.03	(Fig. 5C)
PMID:9614176	FYPO:0001220	increased protein level during cellular response to pheromone [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 5C)
PMID:9614176	FYPO:0001220	increased protein level during cellular response to pheromone [assayed_using] PomBase:SPAPB2B4.03	(Fig. 5C)
PMID:9614176	FYPO:0001220	increased protein level during cellular response to pheromone [has_penetrance] high [assayed_using] PomBase:SPBC582.03	(Fig. 5C)
PMID:9614176	FYPO:0003426	decreased RNA level during cellular response to pheromone [assayed_using] PomBase:SPBC23G7.17c	(Fig. 6A) (comment: CHECK transcript assayed was Mat1-Mm)
PMID:9614178	FYPO:0006232	abolished protein phosphorylation during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC24B11.06c	(comment: residue not determined experimentally, but probably Y173)
PMID:9614178	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC24B11.06c	(comment: residue not determined experimentally, but probably Y173)
PMID:9614178	FYPO:0002130	abolished protein phosphorylation during cellular response to heat [assayed_using] PomBase:SPAC24B11.06c	(comment: residue not determined experimentally, but probably Y173)
PMID:9614178	FYPO:0002130	abolished protein phosphorylation during cellular response to heat [assayed_using] PomBase:SPAC24B11.06c	(comment: residue not determined experimentally, but probably Y173)
PMID:9614178	FYPO:0002129	increased protein phosphorylation during cellular response to heat [assayed_using] PomBase:SPAC24B11.06c	(comment: residue not determined experimentally, but probably Y173)
PMID:9614178	FYPO:0006232	abolished protein phosphorylation during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC24B11.06c	(comment: residue not determined experimentally, but probably Y173)
PMID:9622480	FYPO:0001825	increased sodium export [has_severity] low	(comment: CHECK very mild as shown in xp)
PMID:9635190	FYPO:0001645	decreased protein-protein interaction [assayed_using] PomBase:SPCC5E4.04 [assayed_using] PomBase:SPBC14C8.01c	(Fig. 1i)
PMID:9635190	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPCC5E4.04 [assayed_using] PomBase:SPBC14C8.01c	(Fig. 1i)
PMID:9635190	FYPO:0005000	protein mislocalized to nucleus during mitotic interphase	(Fig. 5) (comment: CHECK during interphase)
PMID:9635190	FYPO:0000783	protein mislocalized to cytoplasm during vegetative growth	(Fig. 5) (comment: CHECK during mitosis)
PMID:9635190	FYPO:0000783	protein mislocalized to cytoplasm during vegetative growth	(Fig. 5) (comment: CHECK during mitotic M-phase)
PMID:9635190	FYPO:0000783	protein mislocalized to cytoplasm during vegetative growth	(Fig. 5) (comment: CHECK during mitotic M-phase)
PMID:9635190	FYPO:0004754	abolished protein localization to mitotic spindle during mitosis	(Fig. 5) (comment: CHECK during mitotic M-phase)
PMID:9635190	FYPO:0000783	protein mislocalized to cytoplasm during vegetative growth	(Fig. 5) (comment: CHECK during mitotic M-phase)
PMID:9635190	FYPO:0000783	protein mislocalized to cytoplasm during vegetative growth	(Fig. 5) (comment: CHECK during mitotic M-phase)
PMID:9635190	FYPO:0000783	protein mislocalized to cytoplasm during vegetative growth	(Fig. 5) (comment: CHECK during mitotic M-phase)
PMID:9635190	FYPO:0001327	increased protein level during vegetative growth [assayed_using] PomBase:SPBC14C8.01c	(Figure 2a)
PMID:9635190	FYPO:0000840	normal RNA level [assayed_using] PomBase:SPBC14C8.01c	(Figure 2b)
PMID:9635190	FYPO:0000833	normal protein level during vegetative growth [assayed_using] PomBase:SPBC14C8.01c	(Figure 2c)
PMID:9635190	FYPO:0004412	abolished protein localization to mitotic spindle midzone during anaphase [has_penetrance] high	(Figure 4b)
PMID:9635190	FYPO:0001179	abolished protein localization during vegetative growth	(comment: CHECK cytoplasm during interphase with nuclear localization)
PMID:9635190	FYPO:0001179	abolished protein localization during vegetative growth	(comment: cytoplasm in interphase) (Figure 4a, I)
PMID:9636183	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high	(comment: same severity as wee1-50 alone)
PMID:9649518	FYPO:0003165	cut with abnormal chromosome segregation	At 36° both mutant strains displayed the classical “cut” phenotype, like that seen in the TPCK-sensitive strain cut1-206
PMID:9649518	FYPO:0003241	unequal mitotic sister chromatid segregation	Often the chromosomes remained unseparated, despite the presence of a septum (Figure 4C, open triangles; Figure 4D, panel d), a phenotype also seen in nuc2-663ts
PMID:9649518	FYPO:0003165	cut with abnormal chromosome segregation	Often the chromosomes remained unseparated, despite the presence of a septum (Figure 4C, open triangles; Figure 4D, panel d), a phenotype also seen in nuc2-663ts
PMID:9649518	FYPO:0001490	inviable elongated vegetative cell	Slightly elongated cells with condensed chromosomes (Figure 4D, panel b) peaked at about 4 hr, followed by a peak in cells that had a septum but in which nuclear division had been abnormal (Figure 4D, panels c–g).
PMID:9649518	FYPO:0002061	inviable vegetative cell population	Strains containing the tsm1-512 mutation failed to grow at 36° on YES medium but could grow, albeit slowly, on minimal medium with supplements (data not shown). This phenotype is also exhibited by two other mitotic mutants of S. pombe: cut2-364 and cut4-533
PMID:9658208	FYPO:0002060	viable vegetative cell population	(comment: just to get the allele details of -P in the database)
PMID:9660817	FYPO:0000708	decreased mating efficiency	data not shown
PMID:9660817	FYPO:0001147	normal mating efficiency	data not shown
PMID:9660817	FYPO:0000708	decreased mating efficiency [has_severity] low	data not shown
PMID:9660818	FYPO:0000708	decreased mating efficiency [has_severity] low	(comment: same severity when crossed with wild type or shk1delta)
PMID:9660818	FYPO:0000708	decreased mating efficiency [has_severity] high	(comment: when crossed with partner overexpressing shk1-deltaN; normal in cross with wild type)
PMID:9660818	FYPO:0000708	decreased mating efficiency [has_severity] high	(comment: when crossed with shk1delta overexpressing shk2+ or wild type)
PMID:9679144	FYPO:0007377	protein mislocalized to medial cortex during mitotic interphase [assayed_using] PomBase:SPAC22H10.07	(Fig. 11) absence of microtubules
PMID:9679144	FYPO:0007377	protein mislocalized to medial cortex during mitotic interphase [assayed_using] PomBase:SPAC22H10.07	(Fig. 11) in the absence of microtubules and actin
PMID:9679144	FYPO:0007380	elongated T-shaped vegetative cell [has_penetrance] 35-40	(Fig. 1F,H) cells were pre NETO after temperature block
PMID:9679144	FYPO:0007380	elongated T-shaped vegetative cell [has_penetrance] high	(Fig. 2A) cdc25-22 arrest released cells ie post NETO do not branch
PMID:9679144	FYPO:0007380	elongated T-shaped vegetative cell [has_penetrance] 25	(Fig. 2B) cells were pre NETO after temperature block
PMID:9679144	FYPO:0007380	elongated T-shaped vegetative cell [has_penetrance] 20	(Fig. 2B) cells were pre NETO after temperature block
PMID:9679144	FYPO:0007380	elongated T-shaped vegetative cell [has_penetrance] 35-40	(Fig. 2B) cells were pre NETO after temperature block
PMID:9679144	FYPO:0000013	T-shaped vegetative cell [has_penetrance] 10	(Fig. 2C) arrest released cells are pre NETO but only branch at low level.
PMID:9679144	FYPO:0000672	normal cell morphology	(Fig. 2C) arrest released cells have NETO defect and do not branch.
PMID:9679144	FYPO:0007379	T-shaped vegetative cell [has_penetrance] 40	(Fig. 2C) cells were pre NETO after temperature block about 5% cells are already branched at release
PMID:9679144	FYPO:0007379	T-shaped vegetative cell [has_penetrance] 40	(Fig. 2C) cells were pre NETO after temperature block about 5% cells are already branched at release
PMID:9679144	FYPO:0001492	viable elongated vegetative cell [has_penetrance] high	(Fig. 3A-C) pre NETO blocked cells do not branch if TBZ is added at shift down
PMID:9679144	FYPO:0001492	viable elongated vegetative cell [has_penetrance] high	(Fig. 3C) cell length does not affect branching showing its not because cells are longer at high temp
PMID:9679144	FYPO:0006103	short interphase microtubules [has_penetrance] high [has_severity] high	(Fig. 4) Short interphase microtubules located in the cell centre
PMID:9679144	FYPO:0000069	resistance to thiabendazole [has_severity] high	(Fig. 5 C,D)
PMID:9679144	FYPO:0003627	normal protein localization [has_severity] high [assayed_using] PomBase:SPAC22H10.07	(Fig. 5 C,D, Fig. 12) Normal protein localisation in presence of TBZ
PMID:9679144	FYPO:0003988	mislocalized actin cortical patches during vegetative growth [has_penetrance] high	(Fig. 6) F-actin localised to branch site in presence of TBZ
PMID:9679144	FYPO:0007379	T-shaped vegetative cell	(Fig. 6) abnormal septum in branched cell
PMID:9679144	FYPO:0001398	monopolar actin cortical patch localization to either end [has_penetrance] high	(Fig. 8A-D) Actin relocalisation to old or new cell end after microtubule disruption
PMID:9679144	FYPO:0006876	normal protein localization to cell cortex of cell tip [assayed_using] PomBase:SPCC1223.06 [has_penetrance] medium	(Fig. 9) tea1 can relocalise to cell ends in absence of microtubules
PMID:9693363	FYPO:0003694	decreased mature 18S rRNA level	(comment: increased 25S/18S ratio)
PMID:9693384	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC24B11.06c	(comment: probably Y173, but not determined experimentally)
PMID:9693384	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC24B11.06c	(comment: probably Y173, but not determined experimentally)
PMID:9693384	FYPO:0001038	increased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPAC24B11.06c	(comment: probably Y173, but not determined experimentally)
PMID:9718372	FYPO:0004173	decreased protein phosphorylation during cellular response to heat [assayed_using] PomBase:SPAC24B11.06c	(comment: probably Y173, but not determined experimentally)
PMID:9718372	FYPO:0002130	abolished protein phosphorylation during cellular response to heat [assayed_using] PomBase:SPAC24B11.06c	(comment: probably Y173, but not determined experimentally)
PMID:9718372	FYPO:0002446	decreased protein phosphorylation during cellular response to hydrogen peroxide [assayed_using] PomBase:SPAC24B11.06c	(comment: probably Y173, but not determined experimentally)
PMID:9722643	FYPO:0002060	viable vegetative cell population	Fig. 1
PMID:9722643	FYPO:0000472	normal mating type switching	Fig. 2
PMID:9722643	FYPO:0000228	lagging mitotic chromosomes [has_penetrance] 7.8	Fig. 3
PMID:9722643	GO:0005634	nucleus	Fig. 4
PMID:9722643	FYPO:0000091	sensitive to thiabendazole	Fig. 5
PMID:9722643	FYPO:0001840	increased minichromosome loss during vegetative growth	Table 2
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] high	(Fig. 2A) (comment: cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 2A) (comment: cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] high	(Fig. 2A) (comment: cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] high	(Fig. 2A) (comment: cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] high	(Fig. 2A) (comment: cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	FYPO:0000216	abnormal negative regulation of mitotic DNA replication initiation [has_penetrance] high	(Fig. 2B) (comment: cdc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	FYPO:0004757	abnormal negative regulation of DNA replication initiation [has_penetrance] >40	(Fig. 2B) (comment: dc18 expressed from pREP3X and assayed after 20 hours after removal of thiamine at 32°C)
PMID:9739083	FYPO:0000836	increased protein level [assayed_using] PomBase:SPBC32F12.09	(Fig. 3) (comment: cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C)
PMID:9739083	FYPO:0000836	increased protein level [assayed_using] PomBase:SPBC32F12.09	(Fig. 3) (comment: cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C)
PMID:9739083	FYPO:0004083	normal protein level [assayed_using] PomBase:SPBC32F12.09	(Fig. 3) (comment: cdc18 expressed from pREP3X and assayed for 20 hours after removal of thiamine at 32°C)
PMID:9739083	FYPO:0000705	abolished protein-protein interaction [assayed_using] PomBase:SPBC11B10.09 [assayed_using] PomBase:SPBC14C8.07c	(Fig. 3) (comment: not strictly a co-immunoprecitation experiment as they used suc1 beads to pull down cdc2 then a western blot)
PMID:9739083	FYPO:0000703	normal protein-protein interaction [assayed_using] PomBase:SPBC11B10.09 [assayed_using] PomBase:SPBC14C8.07c	(Fig. 3) (comment: not strictly a co-immunoprecitation experiment as they used suc1 beads to pull down cdc2 then a western blot)
PMID:9739083	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 3) (comment: the kinase assay substrate used is Histone H1)
PMID:9739083	FYPO:0001382	decreased protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	(Fig. 3) (comment: the kinase assay substrate used is Histone H1)
PMID:9739083	FYPO:0000402	increased mitotic G2/M phase transition	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0001122	elongated vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	increased mitotic G2/M phase transition	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0001052	cut, small cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	increased mitotic G2/M phase transition	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	increased mitotic G2/M phase transition	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	increased mitotic G2/M phase transition	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	increased mitotic G2/M phase transition	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	increased mitotic G2/M phase transition	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0000402	increased mitotic G2/M phase transition	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0001052	cut, small cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0001122	elongated vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0001122	elongated vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell	(Fig. 4) (comment: cdc18 expressed from nmt1 on multi copy plasmid)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 50	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 60	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 40	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 50	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] 60	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	FYPO:0000402	increased mitotic G2/M phase transition [has_penetrance] high	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 65	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	FYPO:0000402	increased mitotic G2/M phase transition [has_penetrance] high	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 70	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 50	(Fig. 5) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. Cells grown in absence of thiamine for 20 hours then shifted to 25°C or 36°C and followed for 3 generations)
PMID:9739083	FYPO:0001052	cut, small cell [has_penetrance] 60	(Fig. 6) (comment: and cell phenotype data not shown. cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] 50	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 40	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 50	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] 80	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] 60	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] 60	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0001052	cut, small cell [has_penetrance] high	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] 60	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0005773	elongated mononucleate aseptate vegetative cell [has_penetrance] 75	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 65	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 70	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 60	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 50	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal)
PMID:9739083	FYPO:0001122	elongated vegetative cell [has_penetrance] 60	(Fig. 6) (comment: cdc18 expressed from nmt1 promoter on multi copy plasmid. cells examined after 20 h after thiamine removal.)
PMID:9739083	FYPO:0002061	inviable vegetative cell population	(comment: cdc1-577 (NTP) when expressed on multi copy plasmid does not rescue cdc18-K46)
PMID:9739083	FYPO:0002061	inviable vegetative cell population	(comment: cdc18-1-141 when expressed on multi copy plasmid does not rescue cdc18-K46)
PMID:9739083	FYPO:0002061	inviable vegetative cell population	(comment: cdc18-150-577 when expressed on multi copy plasmid does not rescue cdc18-K46)
PMID:9739083	FYPO:0002061	inviable vegetative cell population	(comment: cdc18-150-577(T374A) when expressed on multi copy plasmid does not rescue cdc18-K46)
PMID:9739083	FYPO:0002519	abolished response to mitotic G2/M transition checkpoint signaling	Data not shown (comment: Cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0002995	normal regulation of DNA replication	Data not shown (comment: Cdc18 expressed from nmt1 promoter on multi copy plasmid)
PMID:9739083	FYPO:0003075	normal protein kinase activity [assayed_enzyme] PomBase:SPBC11B10.09	data not shown (comment: the kinase assay substrate used is Histone H1)
PMID:9740803	FYPO:0004121	normal protein import into nucleus during vegetative growth [assayed_using] PomBase:SPBC146.03c	(comment: also assayed with GFP-NLS construct)
PMID:9740803	GO:0008139	nuclear localization sequence binding	(comment: can't use IPI because we don't have identifiers for human importin alpha or the GST-NLS construct)
PMID:9745017	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC26H8.07c	(comment: inferred from decreased nda3 mRNA level)
PMID:9745017	FYPO:0003029	decreased mRNA splicing, via spliceosome [assayed_using] PomBase:SPBC26H8.07c	(comment: inferred from decreased nda3 mRNA level)
PMID:9755169	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC14C8.07c [happens_during] mitotic G1 phase	(Fig. 2C) cdc10 dependent transcription occurs during mitotic exit
PMID:9755169	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPBC428.18 [happens_during] mitotic G1 phase	(Fig. 2C) cdc10 dependent transcription occurs during mitotic exit
PMID:9755169	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific [has_input] PomBase:SPAC1F7.05 [happens_during] mitotic G1 phase	(Fig. 2C) cdc10 dependent transcription occurs during mitotic exit
PMID:9755169	FYPO:0006544	decreased transcription during mitosis [assayed_using] PomBase:SPBC14C8.07c	(Fig. 3A) cdc10 is a cdc18 transcriptional regulator see Fig2C
PMID:9755169	FYPO:0006544	decreased transcription during mitosis [assayed_using] PomBase:SPBC14C8.07c	(Fig. 3B)
PMID:9755169	FYPO:0006544	decreased transcription during mitosis [assayed_using] PomBase:SPBC14C8.07c	(Fig. 3B) cdc10 is a cdc18 transcriptional regulator see Fig2C
PMID:9755169	FYPO:0006543	increased protein level during mitotic metaphase [assayed_using] PomBase:SPBC14C8.07c	(Fig. 4C) (comment: cd18 N term deletion can accumulate in a metaphase arrest)
PMID:9755169	FYPO:0006543	increased protein level during mitotic metaphase [assayed_using] PomBase:SPBC14C8.07c	(Fig. 4C) cd18 N term deletion can accumulate in a metaphase arrest
PMID:9755169	FYPO:0006543	increased protein level during mitotic metaphase [assayed_using] PomBase:SPBC14C8.07c	(Fig. 4E) cdc18 lacking cdc2 phosphorylation sites accumulates immediately as cells progress into mitosis
PMID:9755169	FYPO:0001838	decreased protein phosphorylation during vegetative growth [assayed_using] PomBase:SPBC14C8.07c	(Fig. 5B)
PMID:9755169	FYPO:0006543	increased protein level during mitotic metaphase [assayed_using] PomBase:SPBC14C8.07c	(Fig. 5C)
PMID:9755169	FYPO:0006543	increased protein level during mitotic metaphase [assayed_using] PomBase:SPBC14C8.07c	(Fig. 5D)
PMID:9771717	FYPO:0000678	unequal homologous chromosome segregation	data not shown
PMID:9774107	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC1259.13	(Fig. 2)
PMID:9774107	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC1259.13	(Fig. 2)
PMID:9774107	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC18B5.11c	(Fig. 2)
PMID:9774107	MOD:00046	O-phospho-L-serine [added_by] PomBase:SPCC18B5.11c	(Fig. 2)
PMID:9774107	GO:0004674	protein serine/threonine kinase activity [directly_negatively_regulates] PomBase:SPAC24H6.05	(Fig. 2e)
PMID:9774107	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPAC24H6.05	(Fig. 2e)
PMID:9774107	FYPO:0002679	decreased protein phosphorylation [assayed_using] PomBase:SPAC24H6.05	(Fig. 2e)
PMID:9774107	FYPO:0000229	cut [has_penetrance] 37.8	(Fig. 4a)
PMID:9774107	FYPO:0000229	cut [has_penetrance] 19	(Fig. 4a)
PMID:9774107	GO:0004674	protein serine/threonine kinase activity [directly_negatively_regulates] PomBase:SPAC24H6.05	data not shown
PMID:9778252	GO:0005634	nucleus [exists_during] conjugation with cellular fusion	Precise observation revealed that Mei2p dots could be visible in conjugating cells that completed cell fusion but did not undergo karyogamy yet.
PMID:9786952	FYPO:0006556	inviable elongated tetranucleate triseptate vegetative cell, single septa between nuclei [has_penetrance] 10	(Fig. 2A)
PMID:9786952	FYPO:0001406	increased septum thickness	(Fig. 2B)
PMID:9786952	FYPO:0005870	incomplete septum	(Fig. 2B)
PMID:9786952	FYPO:0006802	dispersed filamentous actin	(Fig. 2E)
PMID:9786952	FYPO:0003500	viable branched, elongated, multiseptate vegetative cell	(Fig. 4a)
PMID:9786952	FYPO:0001254	multinucleate multiseptate vegetative cell, septa grouped	(Fig. 4a)
PMID:9786952	FYPO:0000339	mislocalized septum during vegetative growth [has_penetrance] 10	(Fig. 4a,b)
PMID:9786952	FYPO:0001369	mislocalized actomyosin contractile ring [has_penetrance] 10	(Fig. 4d,e)
PMID:9786952	FYPO:0003013	abnormal actomyosin contractile ring disassembly [has_penetrance] 10	(Fig. 6)
PMID:9794798	FYPO:0004387	decreased positive regulation of DNA-directed DNA polymerase activity [assayed_using] PomBase:SPBC336.04 [assayed_using] PomBase:SPBC16D10.09	mutant Cdc6 is not positively regulated by PCNA to the same extent as Cdc6+
PMID:9794798	FYPO:0004387	decreased positive regulation of DNA-directed DNA polymerase activity [assayed_using] PomBase:SPBC336.04 [assayed_using] PomBase:SPBC16D10.09	mutant Cdc6 is not positively regulated by PCNA to the same extent as Cdc6+
PMID:9802907	GO:0044732	mitotic spindle pole body [exists_during] mitotic M phase	((comment: included because different/new method) To observe the SPB in living cells, GFP-tagged Sad1 (designated hereafter Sad1-GFP) was expressed and found to be bound to the SPB throughout the cell cycle (Figure 1A), identical to immunolocalization data (Hagan and Yanagida, 1995)
PMID:9802907	GO:0044732	mitotic spindle pole body [exists_during] mitotic interphase	((comment: included because different/new method) To observe the SPB in living cells, GFP-tagged Sad1 (designated hereafter Sad1–GFP) was expressed and found to be bound to the SPB throughout the cell cycle (Figure 1A), identical to immunolocalization data (Hagan and Yanagida, 1995)
PMID:9802907	FYPO:0002639	increased interkinetochore distance before mitotic anaphase	A striking feature in dis1 mutant cells was that the back-and-forth cen1 DNA movements seen in phase 2 of wild-type cells were entirely absent. After spindle elongation (the SPB distance, 􏰆8 􏰈m), the cen1 signals were fused again and moved to one of the SPBs. Such prolonged centromere splitting while the spindle was elongating was never seen in wild-type or any of the other mutant cells examined so far.
PMID:9808627	FYPO:0000619	abnormal cell cycle arrest in mitotic anaphase [has_penetrance] 50	(Fig. 2D)
PMID:9808627	FYPO:0003241	unequal mitotic sister chromatid segregation	(comment: G1 block)
PMID:9808627	FYPO:0005069	unequal mitotic sister chromatid segregation following normal mitosis [has_penetrance] 50	(comment: G2 block)
PMID:9832516	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(comment: severity estimated because wt (i.e. not overexpressing cdc25) not shown)
PMID:9832516	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(comment: severity estimated because wt (i.e. not overexpressing cdc25) not shown)
PMID:9832516	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(comment: severity estimated because wt (i.e. not overexpressing cdc25) not shown)
PMID:9832516	FYPO:0000088	sensitive to hydroxyurea [has_severity] low	(comment: severity estimated because wt (i.e. not overexpressing cdc25) not shown)
PMID:9839953	GO:0031278	alpha-1,2-galactosyltransferase activity [part_of] protein O-linked glycosylation	(comment: at the second position (Gal-Man-O))
PMID:9839953	GO:0031278	alpha-1,2-galactosyltransferase activity [part_of] protein N-linked glycosylation	(comment: at the second position (Gal-Man-O))
PMID:9839953	GO:0031278	alpha-1,2-galactosyltransferase activity [part_of] protein N-linked glycosylation	(comment: low activity)
PMID:9843572	FYPO:0001490	inviable elongated vegetative cell [has_severity] high	(Figure 1)
PMID:9843572	FYPO:0000712	delayed onset of cell cycle arrest in mitotic G1 phase in response to nitrogen starvation	(Figure 3A,B)
PMID:9843572	FYPO:0000711	decreased cell cycle arrest in mitotic G1 phase in response to nitrogen starvation	(Figure 3A,B)
PMID:9843572	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Figure 3B)
PMID:9843572	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Figure 3B)
PMID:9843572	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Figure 3B)
PMID:9843572	FYPO:0003481	viable elongated vegetative cell, elongated upon mitotic entry	(Figure 3B)
PMID:9843572	FYPO:0000711	decreased cell cycle arrest in mitotic G1 phase in response to nitrogen starvation [has_severity] high	(Figure 3B) (comment: additive)
PMID:9843572	FYPO:0001124	normal vegetative cell size	(Figure 6A)
PMID:9843572	FYPO:0001491	viable vegetative cell	(Figure 6B)
PMID:9843572	FYPO:0001492	viable elongated vegetative cell [has_severity] high	(Figure 7A)
PMID:9843572	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high [has_penetrance] high	(Figure 8)
PMID:9843572	FYPO:0006822	viable small vegetative cell with normal cell growth rate [has_severity] high [has_penetrance] high	(Figure 8)
PMID:9843572	FYPO:0001382	decreased protein kinase activity [has_severity] high [assayed_substrate] PomBase:SPAC57A10.02	(Figure 9A)
PMID:9843577	FYPO:0007137	small multinucleate vegetative cell	(comment: single micrograph, so can't tell if they're viable)
PMID:9843577	FYPO:0007136	small mononucleate vegetative cell	(comment: single micrograph, so can't tell if they're viable)
PMID:9843966	FYPO:0003785	aseptate mononucleate vegetative cell [has_penetrance] high	(comment: neutral wrt viability because data not shown, so don't know if aseptate mononucleate cells are the same ones that manage to survive and eventually divide)
PMID:9857040	GO:0000403	Y-form DNA binding	(comment: physiologically relevant?)
PMID:9857040	GO:0070336	flap-structured DNA binding	(comment: physiologically relevant?)
PMID:9862966	FYPO:0000229	cut [has_penetrance] 3	(Fig. 3C, D)
PMID:9862966	FYPO:0002303	inviable mononucleate monoseptate vegetative cell with anucleate compartment [has_penetrance] 3	(comment: CHECK https://github.com/pombase/fypo/issues/3931)
PMID:9864354	FYPO:0000229	cut	(Fig. 2D)
PMID:9864354	FYPO:0007125	mitotic sister chromatid separation in absence of mitotic spindle	(Fig. 2E)
PMID:9864354	FYPO:0007125	mitotic sister chromatid separation in absence of mitotic spindle	(Fig. 2E)
PMID:9864354	FYPO:0000620	abnormal cell cycle arrest in mitotic metaphase	indicated by high level of H1 kinase activity
PMID:9872416	GO:0004802	transketolase activity [part_of] pentose-phosphate shunt, non-oxidative branch	(Figure 2)
PMID:9872416	GO:0004616	phosphogluconate dehydrogenase (decarboxylating) activity [part_of] pentose-phosphate shunt, oxidative branch	(Figure 2)
PMID:9872416	GO:0017057	6-phosphogluconolactonase activity [part_of] pentose-phosphate shunt, oxidative branch	(Figure 2)
PMID:9872416	GO:0046316	gluconokinase activity	(Figure 2)
PMID:9872416	GO:0004750	D-ribulose-phosphate 3-epimerase activity [part_of] pentose-phosphate shunt, non-oxidative branch	(Figure 2)
PMID:9872416	GO:0004751	ribose-5-phosphate isomerase activity [part_of] pentose-phosphate shunt, non-oxidative branch	(Figure 2)
PMID:9872416	GO:0004801	transaldolase activity [part_of] pentose-phosphate shunt, non-oxidative branch	(Figure 2)
PMID:9891039	FYPO:0001355	decreased vegetative cell population growth	(comment: worse than cdc24-M38 alone -wt not shown)
PMID:9891039	FYPO:0001355	decreased vegetative cell population growth	(comment: worse than cdc24-M38 alone -wt not shown)
PMID:9891039	FYPO:0001355	decreased vegetative cell population growth	(comment: worse than cdc24-M38 alone -wt not shown)
PMID:9891039	FYPO:0001355	decreased vegetative cell population growth	(comment: worse than cdc24-M38 alone -wt not shown)
PMID:9891047	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] low	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] medium	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	FYPO:0002061	inviable vegetative cell population	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	FYPO:0001355	decreased vegetative cell population growth [has_severity] medium	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] medium	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] low	(comment: temperature permissive for single mutant without cds1delta)
PMID:9891047	FYPO:0002061	inviable vegetative cell population	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0002061	inviable vegetative cell population	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0002061	inviable vegetative cell population	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0002061	inviable vegetative cell population	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0002061	inviable vegetative cell population	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0002061	inviable vegetative cell population	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0002061	inviable vegetative cell population	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0001355	decreased vegetative cell population growth [has_severity] high	(comment: temperature permissive for single mutant without rad26delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] medium	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] medium	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] medium	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] medium	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] low	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] low	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] medium	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] medium	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] medium	(comment: temperature permissive for single mutant without rad2delta)
PMID:9891047	FYPO:0000256	mutator [has_severity] medium	(comment: temperature permissive for single mutant without rad2delta)
PMID:9950674	FYPO:0003165	cut with abnormal chromosome segregation	(Fig. 9)
PMID:9950674	FYPO:0002061	inviable vegetative cell population	(Fig. 9)
PMID:9973368	FYPO:0001357	normal vegetative cell population growth	(comment: non-flocculating cells)