YEAST:PP12

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	GLC7 (synonyms: CID1, DIS2)
Protein Name(s)	Serine/threonine-protein phosphatase PP1-2
External Links
UniProt	P32598
EMBL	M77175 M27070 U18916 BK006939
PIR	S32595
RefSeq	NP_011059.3
ProteinModelPortal	P32598
SMR	P32598
BioGrid	36877
DIP	DIP-1336N
IntAct	P32598
MINT	MINT-384176
iPTMnet	P32598
MaxQB	P32598
PeptideAtlas	P32598
PRIDE	P32598
EnsemblFungi	YER133W
GeneID	856870
KEGG	sce:YER133W
EuPathDB	FungiDB:YER133W
SGD	S000000935
GeneTree	ENSGT00530000062911
HOGENOM	HOG000172697
InParanoid	P32598
KO	K06269
OMA	KKPRYPP
OrthoDB	EOG79KPQ9
BioCyc	YEAST:YER133W-MONOMER
PRO	PR:P32598
Proteomes	UP000002311
GO	GO:0005935 GO:0000778 GO:0001400 GO:0005847 GO:0005730 GO:0005634 GO:0000164 GO:0005816 GO:0046872 GO:0004722 GO:0030437 GO:0007114 GO:0006873 GO:0007059 GO:0070940 GO:0000077 GO:0000076 GO:0005977 GO:0016576 GO:0007126 GO:0007067 GO:0007094 GO:0006397 GO:0035307 GO:0006470 GO:0034501 GO:0006109 GO:0051726 GO:0000903 GO:0007346 GO:0031297 GO:0009408 GO:0006986 GO:0006364 GO:0030847 GO:0030846 GO:0061587
Gene3D	3.60.21.10
InterPro	IPR004843 IPR029052 IPR006186 IPR031675
Pfam	PF00149 PF16891
PRINTS	PR00114
SMART	SM00156
SUPFAM	SSF56300
PROSITE	PS00125

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005816	spindle pole body	PMID:10747092^[1]	ECO:0000314			C		The fluorescent marked Glc7 protein was found to localize at the spindle pole bodies in early anaphase as well as in late mitosis (Figures 8 and 7 respectively).	complete CACAO 12171
Colocalizes with	GO:0000142	cellular bud neck contractile ring	PMID:10747092^[1]	ECO:0000314			C		Time lapse florescence imaging revealed that the Glc7 protein colocalizes with the actomyosin contractile ring in the cellular bud neck in late mitosis (Figure 9).	complete CACAO 12172
	GO:0005634	nucleus	PMID:23418575^[2]	ECO:0000314			C		Glc7 is found to be in the nucleus. Fig7e-f. Serine/threonine-protein phosphatase PP1-2 Saccharomyces cerevisiae	complete CACAO 12725
involved_in	GO:0000723	telomere maintenance	PMID:29529242^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000000479	P		Seeded From UniProt	complete
involved_in	GO:2000370	positive regulation of clathrin-dependent endocytosis	PMID:12356757^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000005856	P		Seeded From UniProt	complete
involved_in	GO:1901901	regulation of protein localization to cell division site involved in cytokinesis	PMID:26771880^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(UniProtKB:P40450)\|has_input:(UniProtKB:P41832)	Seeded From UniProt	complete
involved_in	GO:0006470	protein dephosphorylation	PMID:26771880^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(UniProtKB:P40450)	Seeded From UniProt	complete
involved_in	GO:1903501	positive regulation of mitotic actomyosin contractile ring assembly	PMID:26771880^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0000164	protein phosphatase type 1 complex	PMID:19948764^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q03898	C		Seeded From UniProt	complete
part_of	GO:0032153	cell division site	PMID:26771880^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006470	protein dephosphorylation	PMID:26582391^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(SGD:S000006011)\|has_input:(SGD:S000000385)	Seeded From UniProt	complete
involved_in	GO:0006986	response to unfolded protein	PMID:25730376^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070940	dephosphorylation of RNA polymerase II C-terminal domain	PMID:24413056^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061587	transfer RNA gene-mediated silencing	PMID:23707796^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051726	regulation of cell cycle	PMID:10072380^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051726	regulation of cell cycle	PMID:9584086^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051726	regulation of cell cycle	PMID:7891699^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051726	regulation of cell cycle	PMID:8164671^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035307	positive regulation of protein dephosphorylation	PMID:23418575^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034501	protein localization to kinetochore	PMID:19948764^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031297	replication fork processing	PMID:19884341^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030847	termination of RNA polymerase II transcription, exosome-dependent	PMID:12819204^[16]	ECO:0000353	physical interaction evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030846	termination of RNA polymerase II transcription, poly(A)-coupled	PMID:12819204^[16]	ECO:0000353	physical interaction evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030437	ascospore formation	PMID:9584086^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016576	histone dephosphorylation	PMID:19884341^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016576	histone dephosphorylation	PMID:10975519^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016576	histone dephosphorylation	PMID:19884341^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:10207049^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007346	regulation of mitotic cell cycle	PMID:23418575^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051321	meiotic cell cycle	PMID:8754819^[19]	ECO:0000353	physical interaction evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007114	cell budding	PMID:10639337^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007094	mitotic spindle assembly checkpoint	PMID:10072380^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007059	chromosome segregation	PMID:10072383^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006873	cellular ion homeostasis	PMID:11973298^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006470	protein dephosphorylation	PMID:1660885^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006364	rRNA processing	PMID:12837249^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006109	regulation of carbohydrate metabolic process	PMID:12167649^[25]	ECO:0000353	physical interaction evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006109	regulation of carbohydrate metabolic process	PMID:12167649^[25]	ECO:0000316	genetic interaction evidence used in manual assertion		P		Seeded From UniProt	Missing: with/from
involved_in	GO:0005977	glycogen metabolic process	PMID:1660885^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005935	cellular bud neck	PMID:11412094^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005847	mRNA cleavage and polyadenylation specificity factor complex	PMID:12819204^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005816	spindle pole body	PMID:10747092^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:11412094^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:23418575^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004722	protein serine/threonine phosphatase activity	PMID:1660885^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0001400	mating projection base	PMID:10747092^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008360	regulation of cell shape	PMID:12477789^[27]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000000069	P	happens_during:(GO:0072690)	Seeded From UniProt	complete
part_of	GO:0000778	condensed nuclear chromosome kinetochore	PMID:19948764^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000164	protein phosphatase type 1 complex	PMID:8289829^[28]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000077	DNA damage checkpoint	PMID:19884341^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000076	DNA replication checkpoint	PMID:19884341^[15]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000000099 SGD:S000002633 SGD:S000006074	P		Seeded From UniProt	complete
involved_in	GO:0000076	DNA replication checkpoint	PMID:19884341^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051726	regulation of cell cycle	PMID:21873635^[29]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000911503 PomBase:SPBC776.02c SGD:S000000935 UniProtKB:Q59N42	P		Seeded From UniProt	complete
involved_in	GO:0007346	regulation of mitotic cell cycle	PMID:21873635^[29]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000911503 PomBase:SPBC776.02c SGD:S000000935	P		Seeded From UniProt	complete
involved_in	GO:0007059	chromosome segregation	PMID:21873635^[29]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000911503 PomBase:SPBC776.02c SGD:S000000935 UniProtKB:P20654	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[29]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003140 MGI:MGI:103016 MGI:MGI:104871 MGI:MGI:104872 PANTHER:PTN000185232 PomBase:SPAC57A7.08 PomBase:SPBC776.02c PomBase:SPCC31H12.05c RGD:3375 RGD:3376 RGD:3377 SGD:S000000935 TAIR:locus:2024507 UniProtKB:P36873 UniProtKB:P62136 UniProtKB:P62140 UniProtKB:Q57YU1 UniProtKB:Q583K6 WB:WBGene00001748 WB:WBGene00020187 WB:WBGene00021113	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[29]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003140 FB:FBgn0025573 MGI:MGI:103016 PANTHER:PTN000185231 PomBase:SPBC776.02c PomBase:SPCC31H12.05c RGD:3375 SGD:S000000935 SGD:S000004478 TAIR:locus:2024507 TAIR:locus:2063942 TAIR:locus:2825042 UniProtKB:P20654 UniProtKB:Q583K6 UniProtKB:Q585J4 UniProtKB:Q59N42 WB:WBGene00001748 WB:WBGene00020187 WB:WBGene00021113	C		Seeded From UniProt	complete
enables	GO:0004722	protein serine/threonine phosphatase activity	PMID:21873635^[29]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0000711 FB:FBgn0003132 FB:FBgn0003140 FB:FBgn0004103 MGI:MGI:103016 MGI:MGI:104871 MGI:MGI:104872 PANTHER:PTN000185232 PomBase:SPAC57A7.08 PomBase:SPBC776.02c SGD:S000000935 SGD:S000004478 TAIR:locus:2024507 TAIR:locus:2043122 TAIR:locus:2063942 TAIR:locus:2078087 TAIR:locus:2102762 TAIR:locus:2128258 TAIR:locus:2168484 TAIR:locus:2180330 TAIR:locus:2825042 UniProtKB:P36873 UniProtKB:P62207 UniProtKB:Q57YU1 UniProtKB:Q59U06 WB:WBGene00001748	F		Seeded From UniProt	complete
part_of	GO:0000164	protein phosphatase type 1 complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR037981	C		Seeded From UniProt	complete
enables	GO:0004722	protein serine/threonine phosphatase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR037981	F		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004843 InterPro:IPR006186	F		Seeded From UniProt	complete
enables	GO:0004721	phosphoprotein phosphatase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.3.16	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
involved_in	GO:0007049	cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0131	P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
involved_in	GO:0005977	glycogen metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0321	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
enables	GO:0004721	phosphoprotein phosphatase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0904	F		Seeded From UniProt	complete
involved_in	GO:0006397	mRNA processing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0507	P		Seeded From UniProt	complete
involved_in	GO:0051301	cell division	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0132	P		Seeded From UniProt	complete
involved_in	GO:0005975	carbohydrate metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0119	P		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Bloecher, A & Tatchell, K (2000) Dynamic localization of protein phosphatase type 1 in the mitotic cell cycle of Saccharomyces cerevisiae. J. Cell Biol. 149 125-40 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Böhm, S & Buchberger, A (2013) The budding yeast Cdc48(Shp1) complex promotes cell cycle progression by positive regulation of protein phosphatase 1 (Glc7). PLoS ONE 8 e56486 PubMed GONUTS page
↑ Kedziora, S et al. (2018) Rif1 acts through Protein Phosphatase 1 but independent of replication timing to suppress telomere extension in budding yeast. Nucleic Acids Res. 46 3993-4003 PubMed GONUTS page
↑ Chang, JS et al. (2002) Protein phosphatase-1 binding to scd5p is important for regulation of actin organization and endocytosis in yeast. J. Biol. Chem. 277 48002-8 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Orii, M et al. (2016) PP1-Dependent Formin Bnr1 Dephosphorylation and Delocalization from a Cell Division Site. PLoS ONE 11 e0146941 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Akiyoshi, B et al. (2009) Quantitative proteomic analysis of purified yeast kinetochores identifies a PP1 regulatory subunit. Genes Dev. 23 2887-99 PubMed GONUTS page
↑ Yerlikaya, S et al. (2016) TORC1 and TORC2 work together to regulate ribosomal protein S6 phosphorylation in Saccharomyces cerevisiae. Mol. Biol. Cell 27 397-409 PubMed GONUTS page
↑ Ferrer-Dalmau, J et al. (2015) Protein kinase Snf1 is involved in the proper regulation of the unfolded protein response in Saccharomyces cerevisiae. Biochem. J. 468 33-47 PubMed GONUTS page
↑ Schreieck, A et al. (2014) RNA polymerase II termination involves C-terminal-domain tyrosine dephosphorylation by CPF subunit Glc7. Nat. Struct. Mol. Biol. 21 175-9 PubMed GONUTS page
↑ Good, PD et al. (2013) Silencing near tRNA genes is nucleosome-mediated and distinct from boundary element function. Gene 526 7-15 PubMed GONUTS page
↑ ^11.0 ^11.1 Bloecher, A & Tatchell, K (1999) Defects in Saccharomyces cerevisiae protein phosphatase type I activate the spindle/kinetochore checkpoint. Genes Dev. 13 517-22 PubMed GONUTS page
↑ ^12.0 ^12.1 Ramaswamy, NT et al. (1998) Regulation of yeast glycogen metabolism and sporulation by Glc7p protein phosphatase. Genetics 149 57-72 PubMed GONUTS page
↑ Zhang, S et al. (1995) The Saccharomyces SHP1 gene, which encodes a regulator of phosphoprotein phosphatase 1 with differential effects on glycogen metabolism, meiotic differentiation, and mitotic cell cycle progression. Mol. Cell. Biol. 15 2037-50 PubMed GONUTS page
↑ Hisamoto, N et al. (1994) The Glc7 type 1 protein phosphatase of Saccharomyces cerevisiae is required for cell cycle progression in G2/M. Mol. Cell. Biol. 14 3158-65 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 Bazzi, M et al. (2010) Dephosphorylation of gamma H2A by Glc7/protein phosphatase 1 promotes recovery from inhibition of DNA replication. Mol. Cell. Biol. 30 131-45 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Nedea, E et al. (2003) Organization and function of APT, a subcomplex of the yeast cleavage and polyadenylation factor involved in the formation of mRNA and small nucleolar RNA 3'-ends. J. Biol. Chem. 278 33000-10 PubMed GONUTS page
↑ Hsu, JY et al. (2000) Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. Cell 102 279-91 PubMed GONUTS page
↑ Lin, JT & Lis, JT (1999) Glycogen synthase phosphatase interacts with heat shock factor to activate CUP1 gene transcription in Saccharomyces cerevisiae. Mol. Cell. Biol. 19 3237-45 PubMed GONUTS page
↑ Tu, J et al. (1996) Protein phosphatase type 1 interacts with proteins required for meiosis and other cellular processes in Saccharomyces cerevisiae. Mol. Cell. Biol. 16 4199-206 PubMed GONUTS page
↑ Andrews, PD & Stark, MJ (2000) Type 1 protein phosphatase is required for maintenance of cell wall integrity, morphogenesis and cell cycle progression in Saccharomyces cerevisiae. J. Cell. Sci. 113 ( Pt 3) 507-20 PubMed GONUTS page
↑ Sassoon, I et al. (1999) Regulation of Saccharomyces cerevisiae kinetochores by the type 1 phosphatase Glc7p. Genes Dev. 13 545-55 PubMed GONUTS page
↑ Williams-Hart, T et al. (2002) Protein phosphatase type 1 regulates ion homeostasis in Saccharomyces cerevisiae. Genetics 160 1423-37 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 Feng, ZH et al. (1991) The yeast GLC7 gene required for glycogen accumulation encodes a type 1 protein phosphatase. J. Biol. Chem. 266 23796-801 PubMed GONUTS page
↑ Peng, WT et al. (2003) A panoramic view of yeast noncoding RNA processing. Cell 113 919-33 PubMed GONUTS page
↑ ^25.0 ^25.1 Young, ET et al. (2002) Snf1 protein kinase regulates Adr1 binding to chromatin but not transcription activation. J. Biol. Chem. 277 38095-103 PubMed GONUTS page
↑ ^26.0 ^26.1 Wu, X & Tatchell, K (2001) Mutations in yeast protein phosphatase type 1 that affect targeting subunit binding. Biochemistry 40 7410-20 PubMed GONUTS page
↑ Cullen, PJ & Sprague, GF Jr (2002) The Glc7p-interacting protein Bud14p attenuates polarized growth, pheromone response, and filamentous growth in Saccharomyces cerevisiae. Eukaryotic Cell 1 884-94 PubMed GONUTS page
↑ Stuart, JS et al. (1994) The mutant type 1 protein phosphatase encoded by glc7-1 from Saccharomyces cerevisiae fails to interact productively with the GAC1-encoded regulatory subunit. Mol. Cell. Biol. 14 896-905 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 ^29.3 ^29.4 ^29.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:10747092-1] 1.0 ^1.1 ^1.2 ^1.3 Bloecher, A & Tatchell, K (2000) Dynamic localization of protein phosphatase type 1 in the mitotic cell cycle of Saccharomyces cerevisiae. J. Cell Biol. 149 125-40 PubMed GONUTS page

[PMID:23418575-2] 2.0 ^2.1 ^2.2 ^2.3 Böhm, S & Buchberger, A (2013) The budding yeast Cdc48(Shp1) complex promotes cell cycle progression by positive regulation of protein phosphatase 1 (Glc7). PLoS ONE 8 e56486 PubMed GONUTS page

[PMID:29529242-3] Kedziora, S et al. (2018) Rif1 acts through Protein Phosphatase 1 but independent of replication timing to suppress telomere extension in budding yeast. Nucleic Acids Res. 46 3993-4003 PubMed GONUTS page

[PMID:12356757-4] Chang, JS et al. (2002) Protein phosphatase-1 binding to scd5p is important for regulation of actin organization and endocytosis in yeast. J. Biol. Chem. 277 48002-8 PubMed GONUTS page

[PMID:26771880-5] 5.0 ^5.1 ^5.2 ^5.3 Orii, M et al. (2016) PP1-Dependent Formin Bnr1 Dephosphorylation and Delocalization from a Cell Division Site. PLoS ONE 11 e0146941 PubMed GONUTS page

[PMID:19948764-6] 6.0 ^6.1 ^6.2 Akiyoshi, B et al. (2009) Quantitative proteomic analysis of purified yeast kinetochores identifies a PP1 regulatory subunit. Genes Dev. 23 2887-99 PubMed GONUTS page

[PMID:26582391-7] Yerlikaya, S et al. (2016) TORC1 and TORC2 work together to regulate ribosomal protein S6 phosphorylation in Saccharomyces cerevisiae. Mol. Biol. Cell 27 397-409 PubMed GONUTS page

[PMID:25730376-8] Ferrer-Dalmau, J et al. (2015) Protein kinase Snf1 is involved in the proper regulation of the unfolded protein response in Saccharomyces cerevisiae. Biochem. J. 468 33-47 PubMed GONUTS page

[PMID:24413056-9] Schreieck, A et al. (2014) RNA polymerase II termination involves C-terminal-domain tyrosine dephosphorylation by CPF subunit Glc7. Nat. Struct. Mol. Biol. 21 175-9 PubMed GONUTS page

[PMID:23707796-10] Good, PD et al. (2013) Silencing near tRNA genes is nucleosome-mediated and distinct from boundary element function. Gene 526 7-15 PubMed GONUTS page

[PMID:10072380-11] 11.0 ^11.1 Bloecher, A & Tatchell, K (1999) Defects in Saccharomyces cerevisiae protein phosphatase type I activate the spindle/kinetochore checkpoint. Genes Dev. 13 517-22 PubMed GONUTS page

[PMID:9584086-12] 12.0 ^12.1 Ramaswamy, NT et al. (1998) Regulation of yeast glycogen metabolism and sporulation by Glc7p protein phosphatase. Genetics 149 57-72 PubMed GONUTS page

[PMID:7891699-13] Zhang, S et al. (1995) The Saccharomyces SHP1 gene, which encodes a regulator of phosphoprotein phosphatase 1 with differential effects on glycogen metabolism, meiotic differentiation, and mitotic cell cycle progression. Mol. Cell. Biol. 15 2037-50 PubMed GONUTS page

[PMID:8164671-14] Hisamoto, N et al. (1994) The Glc7 type 1 protein phosphatase of Saccharomyces cerevisiae is required for cell cycle progression in G2/M. Mol. Cell. Biol. 14 3158-65 PubMed GONUTS page

[PMID:19884341-15] 15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 Bazzi, M et al. (2010) Dephosphorylation of gamma H2A by Glc7/protein phosphatase 1 promotes recovery from inhibition of DNA replication. Mol. Cell. Biol. 30 131-45 PubMed GONUTS page

[PMID:12819204-16] 16.0 ^16.1 ^16.2 Nedea, E et al. (2003) Organization and function of APT, a subcomplex of the yeast cleavage and polyadenylation factor involved in the formation of mRNA and small nucleolar RNA 3'-ends. J. Biol. Chem. 278 33000-10 PubMed GONUTS page

[PMID:10975519-17] Hsu, JY et al. (2000) Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. Cell 102 279-91 PubMed GONUTS page

[PMID:10207049-18] Lin, JT & Lis, JT (1999) Glycogen synthase phosphatase interacts with heat shock factor to activate CUP1 gene transcription in Saccharomyces cerevisiae. Mol. Cell. Biol. 19 3237-45 PubMed GONUTS page

[PMID:8754819-19] Tu, J et al. (1996) Protein phosphatase type 1 interacts with proteins required for meiosis and other cellular processes in Saccharomyces cerevisiae. Mol. Cell. Biol. 16 4199-206 PubMed GONUTS page

[PMID:10639337-20] Andrews, PD & Stark, MJ (2000) Type 1 protein phosphatase is required for maintenance of cell wall integrity, morphogenesis and cell cycle progression in Saccharomyces cerevisiae. J. Cell. Sci. 113 ( Pt 3) 507-20 PubMed GONUTS page

[PMID:10072383-21] Sassoon, I et al. (1999) Regulation of Saccharomyces cerevisiae kinetochores by the type 1 phosphatase Glc7p. Genes Dev. 13 545-55 PubMed GONUTS page

[PMID:11973298-22] Williams-Hart, T et al. (2002) Protein phosphatase type 1 regulates ion homeostasis in Saccharomyces cerevisiae. Genetics 160 1423-37 PubMed GONUTS page

[PMID:1660885-23] 23.0 ^23.1 ^23.2 Feng, ZH et al. (1991) The yeast GLC7 gene required for glycogen accumulation encodes a type 1 protein phosphatase. J. Biol. Chem. 266 23796-801 PubMed GONUTS page

[PMID:12837249-24] Peng, WT et al. (2003) A panoramic view of yeast noncoding RNA processing. Cell 113 919-33 PubMed GONUTS page

[PMID:12167649-25] 25.0 ^25.1 Young, ET et al. (2002) Snf1 protein kinase regulates Adr1 binding to chromatin but not transcription activation. J. Biol. Chem. 277 38095-103 PubMed GONUTS page

[PMID:11412094-26] 26.0 ^26.1 Wu, X & Tatchell, K (2001) Mutations in yeast protein phosphatase type 1 that affect targeting subunit binding. Biochemistry 40 7410-20 PubMed GONUTS page

[PMID:12477789-27] Cullen, PJ & Sprague, GF Jr (2002) The Glc7p-interacting protein Bud14p attenuates polarized growth, pheromone response, and filamentous growth in Saccharomyces cerevisiae. Eukaryotic Cell 1 884-94 PubMed GONUTS page

[PMID:8289829-28] Stuart, JS et al. (1994) The mutant type 1 protein phosphatase encoded by glc7-1 from Saccharomyces cerevisiae fails to interact productively with the GAC1-encoded regulatory subunit. Mol. Cell. Biol. 14 896-905 PubMed GONUTS page

[PMID:21873635-29] 29.0 ^29.1 ^29.2 ^29.3 ^29.4 ^29.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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