Reviewed, UniProtKB/Swiss-Prot P32598 (PP12_YEAST)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein phosphatase PP1-2
    EC=3.1.3.16

Gene names

Name:	GLC7
Synonyms:	CID1, DIS2
Ordered Locus Names:	YER133W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in control of glycogen metabolism, meiosis, translation, chromosome segregation, cell polarity and G2/M cell cycle progression. PP1 may act in opposition to the IPL1 protein kinase in regulating chromosome segregation by dephosphorylating H3S10ph. The BUD14-GLC7 complex is necessary to regulate microtubule dynamics at the cortex and may function as a specific activator of the dynein complex. Ref.5 Ref.9 Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation. Ref.5 Ref.9
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Subunit structure	Probably complexed with regulatory or targeting subunits. Interacts with BUD14. Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Component of the APT complex, which is a subcomplex of CPF, and is composed of PTI1, SYC1, SSU72, GLC7, REF2, PTA1 and SWD2. Ref.9 Ref.6
Subcellular location	Cytoplasm. Nucleus.
Miscellaneous	Present with 14600 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell cycle Cell division Glycogen metabolism Mitosis mRNA processing
Cellular component	Cytoplasm Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ascospore formation Inferred from mutant phenotype. Source: SGD cell budding Inferred from mutant phenotype. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW cell morphogenesis during vegetative growth Ref.6 Inferred from genetic interaction. Source: SGD cellular ion homeostasis Inferred from mutant phenotype. Source: SGD chromosome segregation Inferred from mutant phenotype. Source: SGD glycogen metabolic process Ref.1 Inferred from mutant phenotype. Source: SGD histone dephosphorylation Ref.5 Inferred from mutant phenotype. Source: SGD mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW meiosis Inferred from physical interaction. Source: SGD mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle spindle assembly checkpoint Inferred from mutant phenotype. Source: SGD rRNA processing Inferred from mutant phenotype. Source: SGD regulation of carbohydrate metabolic process Inferred from genetic interaction. Source: SGD response to heat Inferred from mutant phenotype. Source: SGD termination of RNA polymerase II transcription, poly(A)-coupled Ref.7 Inferred from physical interaction. Source: SGD termination of RNA polymerase II transcription, poly(A)-independent Ref.7 Inferred from physical interaction. Source: SGD
Cellular component	cellular bud neck Inferred from direct assay. Source: SGD mRNA cleavage and polyadenylation specificity factor complex Ref.7 Inferred from physical interaction. Source: SGD mating projection base Inferred from direct assay. Source: SGD nucleolus Inferred from direct assay. Source: SGD protein phosphatase type 1 complex Inferred from direct assay. Source: SGD spindle pole body Inferred from direct assay. Source: SGD
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine phosphatase activity Ref.1 Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q12276	1	EBI-13715,EBI-35056
BUD14	P27637	3	EBI-13715,EBI-20747
GIP1	P38229	2	EBI-13715,EBI-7604
GIP4	P39732	1	EBI-13715,EBI-20636
GLC8	P41818	1	EBI-13715,EBI-7629
MHP1	P43638	1	EBI-13715,EBI-10880
PEX31	P53203	1	EBI-13715,EBI-23069
SDS22	P36047	1	EBI-13715,EBI-16783
SOL1	P50278	1	EBI-13715,EBI-17675

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 312	312	Serine/threonine-protein phosphatase PP1-2		PRO_0000058820
Sites
	Active site	124	1	Proton donor By similarity
	Metal binding	63	1	Iron By similarity
	Metal binding	65	1	Iron By similarity
	Metal binding	91	1	Iron By similarity
	Metal binding	91	1	Manganese By similarity
	Metal binding	123	1	Manganese By similarity
	Metal binding	172	1	Manganese By similarity
	Metal binding	247	1	Manganese By similarity
Amino acid modifications
	Modified residue	176	1	Phosphoserine Ref.10
Experimental info
	Mutagenesis	73	1	R → C in GLC7-1; decreased glycogen accumulation. Ref.3
	Sequence conflict	137	1	D → H in AAA34570. Ref.2
	Sequence conflict	273	1	G → V in AAA34570. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P32598-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 71B20E3A4ED93235	FASTA	312	35,907
	10 20 30 40 50 60 MDSQPVDVDN IIDRLLEVRG SKPGQQVDLE ENEIRYLCSK ARSIFIKQPI LLELEAPIKI 70 80 90 100 110 120 CGDIHGQYYD LLRLFEYGGF PPESNYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFIL 130 140 150 160 170 180 RGNHECASIN RIYGFYDECK RRYNIKLWKT FTDCFNCLPI AAIIDEKIFC MHGGLSPDLN 190 200 210 220 230 240 SMEQIRRVMR PTDIPDVGLL CDLLWSDPDK DIVGWSENDR GVSFTFGPDV VNRFLQKQDM 250 260 270 280 290 300 ELICRAHQVV EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAQK 310 SLPRQAGGRK KK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The yeast GLC7 gene required for glycogen accumulation encodes a type 1 protein phosphatase." Feng Z.H., Wilson S.E., Peng Z.Y., Schlender K.K., Reimann E.M., Trumbly R.J. J. Biol. Chem. 266:23796-23801(1991) [PubMed: 1660885] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The fission yeast dis2+ gene required for chromosome disjoining encodes one of two putative type 1 protein phosphatases." Ohkura H., Kinoshita N., Miyatani S., Toda T., Yanagida M. Cell 57:997-1007(1989) [PubMed: 2544298] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Characterization of glycogen-deficient glc mutants of Saccharomyces cerevisiae." Cannon J.F., Pringle J.R., Fiechter A., Khalil M. Genetics 136:485-503(1994) [PubMed: 8150278] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF ARG-73.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	"Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes." Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K., Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R., Smith M.M., Allis C.D. Cell 102:279-291(2000) [PubMed: 10975519] [Abstract] Cited for: FUNCTION.
[6]	"The Glc7p-interacting protein Bud14p attenuates polarized growth, pheromone response, and filamentous growth in Saccharomyces cerevisiae." Cullen P.J., Sprague G.F. Jr. Eukaryot. Cell 1:884-894(2002) [PubMed: 12477789] [Abstract] Cited for: INTERACTION WITH BUD14.
[7]	"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." Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T., Buratowski S., Moore C.L., Greenblatt J. J. Biol. Chem. 278:33000-33010(2003) [PubMed: 12819204] [Abstract] Cited for: IDENTIFICATION IN THE CPF COMPLEX, COMPOSITION OF THE APT COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"The Bud14p-Glc7p complex functions as a cortical regulator of dynein in budding yeast." Knaus M., Cameroni E., Pedruzzi I., Tatchell K., De Virgilio C., Peter M. EMBO J. 24:3000-3011(2005) [PubMed: 16107882] [Abstract] Cited for: INTERACTION WITH BUD14, FUNCTION OF THE BUD14-GLC7 COMPLEX.
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M77175 Genomic DNA. Translation: AAB59322.1. M27070 Genomic DNA. Translation: AAA34570.1. U18916 Genomic DNA. Translation: AAC03231.1.
PIR	S32595.
RefSeq	NP_011059.1.
3D structure databases
SMR	P32598. Positions 6-298.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1336N.
IntAct	P32598. 90 interactions.
STRING	P32598.
Proteomic databases
PeptideAtlas	P32598.
PRIDE	P32598.
Genome annotation databases
Ensembl	YER133W; YER133W; YER133W; Saccharomyces cerevisiae. [Genome view]
GeneID	856870.
KEGG	sce:YER133W.
NMPDR	fig|4932.3.peg.2135.
Organism-specific databases
CYGD	YER133w.
SGD	S000000935. GLC7.
Phylogenomic databases
HOGENOM	P32598.
OMA	VGWSEND
OrthoDB	EOG9S1VQB
Enzyme and pathway databases
BRENDA	3.1.3.16. 250.
Gene expression databases
ArrayExpress	P32598.
Genevestigator	P32598.
GermOnline	YER133W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004843. M-pesterase. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
PANTHER	PTHR11668. T_phtase_apaH. 1 hit.
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	983240.

Entry information

Entry name

PP12_YEAST

Accession

Primary (citable) accession number: P32598

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 24, 2009
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)