Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P32598 (PP12_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PP1-2

EC=3.1.3.16
Gene names
Name:GLC7
Synonyms:CID1, DIS2
Ordered Locus Names:YER133W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 manganese ions 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 processCarbohydrate metabolism
Cell cycle
Cell division
Glycogen metabolism
Mitosis
mRNA processing
   Cellular componentCytoplasm
Nucleus
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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

dephosphorylation of RNA polymerase II C-terminal domain

Inferred from direct assay PubMed 24413056. 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

meiotic nuclear division

Inferred from physical interaction PubMed 8754819. Source: SGD

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic spindle assembly checkpoint

Inferred from mutant phenotype PubMed 10072380. Source: SGD

positive regulation of protein dephosphorylation

Inferred from mutant phenotype PubMed 23418575. Source: SGD

protein dephosphorylation

Inferred from direct assay Ref.1. 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 cycle

Inferred from mutant phenotype PubMed 10072380PubMed 7891699PubMed 8164671PubMed 9584086. Source: SGD

regulation of cell shape during vegetative growth phase

Inferred from genetic interaction Ref.7. Source: SGD

regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 23418575. Source: SGD

replication fork processing

Inferred from mutant phenotype PubMed 19884341. Source: SGD

response to heat

Inferred from mutant phenotype 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

transfer RNA gene-mediated silencing

Inferred from mutant phenotype PubMed 23707796. Source: SGD

   Cellular_componentcellular 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

nucleus

Inferred from direct assay PubMed 23418575. 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_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 10688190PubMed 11805826PubMed 14660704PubMed 14690591Ref.10PubMed 16429126PubMed 16537909PubMed 20489023PubMed 21179020. Source: IntAct

protein serine/threonine phosphatase activity

Inferred from direct assay Ref.1. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Serine/threonine-protein phosphatase PP1-2
PRO_0000058820

Sites

Active site1241Proton donor By similarity
Metal binding631Manganese 1 By similarity
Metal binding651Manganese 1 By similarity
Metal binding911Manganese 1 By similarity
Metal binding911Manganese 2 By similarity
Metal binding1231Manganese 2 By similarity
Metal binding1721Manganese 2 By similarity
Metal binding2471Manganese 2 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11

Experimental info

Mutagenesis731R → C in GLC7-1; decreased glycogen accumulation. Ref.3
Sequence conflict1371D → H in AAA34570. Ref.2
Sequence conflict2731G → V in AAA34570. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P32598 [UniParc].

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

FASTA31235,907
        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' 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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS32595.
RefSeqNP_011059.3. NM_001179023.3.

3D structure databases

ProteinModelPortalP32598.
SMRP32598. Positions 6-298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36877. 548 interactions.
DIPDIP-1336N.
IntActP32598. 149 interactions.
MINTMINT-384176.
STRING4932.YER133W.

Proteomic databases

MaxQBP32598.
PaxDbP32598.
PeptideAtlasP32598.
PRIDEP32598.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER133W; YER133W; YER133W.
GeneID856870.
KEGGsce:YER133W.

Organism-specific databases

CYGDYER133w.
SGDS000000935. GLC7.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000062911.
HOGENOMHOG000172697.
KOK06269.
OMAGSKPGQQ.
OrthoDBEOG79KPQ9.

Enzyme and pathway databases

BioCycYEAST:YER133W-MONOMER.

Gene expression databases

GenevestigatorP32598.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio983240.

Entry information

Entry namePP12_YEAST
AccessionPrimary (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: June 11, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

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

Yeast

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

SIMILARITY comments

Index of protein domains and families