Serine/threonine-protein phosphatase PP1-2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32598 (PP12_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 139. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
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.6 Ref.10 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.6 Ref.10
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.7 Ref.8 Ref.10
Subcellular location	Cytoplasm. Nucleus Ref.8.
Miscellaneous	Present with 14600 molecules/cell in log phase SD medium.
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 Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage checkpoint Inferred from mutant phenotype PubMed 19884341. Source: SGD DNA replication checkpoint Inferred from mutant phenotype PubMed 19884341. Source: SGD ascospore formation Inferred from mutant phenotype PubMed 9584086. Source: SGD cell budding Inferred from mutant phenotype PubMed 10639337. Source: SGD cellular ion homeostasis Inferred from mutant phenotype PubMed 11973298. Source: SGD chromosome segregation Inferred from mutant phenotype PubMed 10072383. Source: SGD glycogen metabolic process Inferred from mutant phenotype Ref.1. Source: SGD histone dephosphorylation Inferred from direct assay PubMed 19884341. Source: SGD mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW meiosis Inferred from physical interaction PubMed 8754819. Source: SGD mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic spindle assembly checkpoint Inferred from mutant phenotype PubMed 10072380. Source: SGD protein localization to kinetochore Inferred from mutant phenotype PubMed 19948764. Source: SGD rRNA processing Inferred from mutant phenotype PubMed 12837249. Source: SGD regulation of carbohydrate metabolic process Inferred from genetic interaction PubMed 12167649. Source: SGD regulation of cell shape during vegetative growth phase Inferred from genetic interaction Ref.7. Source: SGD replication fork processing Inferred from mutant phenotype PubMed 19884341. Source: SGD response to heat Inferred from physical interaction PubMed 10207049. Source: SGD termination of RNA polymerase II transcription, exosome-dependent Inferred from physical interaction Ref.8. Source: SGD termination of RNA polymerase II transcription, poly(A)-coupled Inferred from physical interaction Ref.8. Source: SGD
Cellular_component	cellular bud neck Inferred from direct assay PubMed 11412094. Source: SGD condensed nuclear chromosome kinetochore Inferred from direct assay PubMed 19948764. Source: SGD mRNA cleavage and polyadenylation specificity factor complex Inferred from direct assay Ref.8. Source: SGD mating projection base Inferred from direct assay PubMed 10747092. Source: SGD nucleolus Inferred from direct assay PubMed 11412094. Source: SGD protein phosphatase type 1 complex Inferred from direct assay PubMed 8289829. Source: SGD spindle pole body Inferred from direct assay PubMed 10747092. Source: SGD
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay Ref.1. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
BNI4	P53858	4	EBI-13715,EBI-3704
BUD14	P27637	7	EBI-13715,EBI-20747
FIN1	Q03898	3	EBI-13715,EBI-32941
GIP4	P39732	4	EBI-13715,EBI-20636
GLC8	P41818	8	EBI-13715,EBI-7629
HER1	Q12276	4	EBI-13715,EBI-35056
MHP1	P43638	6	EBI-13715,EBI-10880
REF2	P42073	7	EBI-13715,EBI-14915
SCD5	P34758	4	EBI-13715,EBI-16685
SDS22	P36047	10	EBI-13715,EBI-16783
SOL1	P50278	3	EBI-13715,EBI-17675
YPI1	P43587	6	EBI-13715,EBI-22913

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

Proton donor By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Manganese By similarity

Metal binding

123

Manganese By similarity

Metal binding

172

Manganese By similarity

Metal binding

247

Manganese By similarity

Amino acid modifications

Modified residue

176

Phosphoserine Ref.11

Experimental info

Mutagenesis

R → C in GLC7-1; decreased glycogen accumulation. Ref.3

Sequence conflict

137

D → H in AAA34570. Ref.2

Sequence conflict

273

G → V in AAA34570. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P32598 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 71B20E3A4ED93235
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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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BUD14.
[8]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE CPF COMPLEX, COMPOSITION OF THE APT COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[9]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BUD14, FUNCTION OF THE BUD14-GLC7 COMPLEX.
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M77175 Genomic DNA. Translation: AAB59322.1. M27070 Genomic DNA. Translation: AAA34570.1. U18916 Genomic DNA. Translation: AAC03231.1. BK006939 Genomic DNA. Translation: DAA07793.1.
PIR	S32595.
RefSeq	NP_011059.3. NM_001179023.3.
3D structure databases
ProteinModelPortal	P32598.
SMR	P32598. Positions 6-298.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1336N.
IntAct	P32598. 155 interactions.
MINT	MINT-384176.
STRING	4932.YER133W.
Proteomic databases
PaxDb	P32598.
PeptideAtlas	P32598.
PRIDE	P32598.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER133W; YER133W; YER133W.
GeneID	856870.
KEGG	sce:YER133W. sce:YER138C.
Organism-specific databases
CYGD	YER133w.
SGD	S000000935. GLC7.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00530000062911.
HOGENOM	HOG000172697.
KO	K06269.
OMA	APNYCNE.
OrthoDB	EOG4MGWH2.
Gene expression databases
Genevestigator	P32598.
GermOnline	YER133W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
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
NextBio	983240.

Entry information

Entry name

PP12_YEAST

Accession

Primary (citable) accession number: P32598
Secondary accession number(s): D3DM39

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents