Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P32598

- PP12_YEAST

UniProt

P32598 - PP12_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serine/threonine-protein phosphatase PP1-2

Gene

GLC7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.
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.

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Manganese 1By similarity
Metal bindingi65 – 651Manganese 1By similarity
Metal bindingi91 – 911Manganese 1By similarity
Metal bindingi91 – 911Manganese 2By similarity
Metal bindingi123 – 1231Manganese 2By similarity
Active sitei124 – 1241Proton donorBy similarity
Metal bindingi172 – 1721Manganese 2By similarity
Metal bindingi247 – 2471Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein serine/threonine phosphatase activity Source: SGD

GO - Biological processi

  1. ascospore formation Source: SGD
  2. cell budding Source: SGD
  3. cellular ion homeostasis Source: SGD
  4. chromosome segregation Source: SGD
  5. dephosphorylation of RNA polymerase II C-terminal domain Source: SGD
  6. DNA damage checkpoint Source: SGD
  7. DNA replication checkpoint Source: SGD
  8. glycogen metabolic process Source: SGD
  9. histone dephosphorylation Source: SGD
  10. meiotic nuclear division Source: SGD
  11. mitotic nuclear division Source: UniProtKB-KW
  12. mitotic spindle assembly checkpoint Source: SGD
  13. mRNA processing Source: UniProtKB-KW
  14. positive regulation of protein dephosphorylation Source: SGD
  15. protein dephosphorylation Source: SGD
  16. protein localization to kinetochore Source: SGD
  17. regulation of carbohydrate metabolic process Source: SGD
  18. regulation of cell cycle Source: SGD
  19. regulation of cell shape during vegetative growth phase Source: SGD
  20. regulation of mitotic cell cycle Source: SGD
  21. replication fork processing Source: SGD
  22. response to heat Source: SGD
  23. rRNA processing Source: SGD
  24. termination of RNA polymerase II transcription, exosome-dependent Source: SGD
  25. termination of RNA polymerase II transcription, poly(A)-coupled Source: SGD
  26. transfer RNA gene-mediated silencing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism, Mitosis, mRNA processing

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YER133W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1-2 (EC:3.1.3.16)
Gene namesi
Name:GLC7
Synonyms:CID1, DIS2
Ordered Locus Names:YER133W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome V

Organism-specific databases

CYGDiYER133w.
SGDiS000000935. GLC7.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cellular bud neck Source: SGD
  2. condensed nuclear chromosome kinetochore Source: SGD
  3. mating projection base Source: SGD
  4. mRNA cleavage and polyadenylation specificity factor complex Source: SGD
  5. nucleolus Source: SGD
  6. nucleus Source: SGD
  7. protein phosphatase type 1 complex Source: SGD
  8. spindle pole body Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731R → C in GLC7-1; decreased glycogen accumulation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 312312Serine/threonine-protein phosphatase PP1-2PRO_0000058820Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP32598.
PaxDbiP32598.
PeptideAtlasiP32598.
PRIDEiP32598.

Expressioni

Gene expression databases

GenevestigatoriP32598.

Interactioni

Subunit structurei

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 SWD2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BNI4P538584EBI-13715,EBI-3704
BUD14P276377EBI-13715,EBI-20747
GIP4P397324EBI-13715,EBI-20636
GLC8P418183EBI-13715,EBI-7629
MHP1P436383EBI-13715,EBI-10880
REF2P420737EBI-13715,EBI-14915
SCD5P347583EBI-13715,EBI-16685
SDS22P360476EBI-13715,EBI-16783
SOL1P502783EBI-13715,EBI-17675
YPI1P435874EBI-13715,EBI-22913

Protein-protein interaction databases

BioGridi36877. 548 interactions.
DIPiDIP-1336N.
IntActiP32598. 149 interactions.
MINTiMINT-384176.
STRINGi4932.YER133W.

Structurei

3D structure databases

ProteinModelPortaliP32598.
SMRiP32598. Positions 6-298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000172697.
InParanoidiP32598.
KOiK06269.
OMAiGSKPGQQ.
OrthoDBiEOG79KPQ9.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32598 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDSQPVDVDN IIDRLLEVRG SKPGQQVDLE ENEIRYLCSK ARSIFIKQPI
60 70 80 90 100
LLELEAPIKI CGDIHGQYYD LLRLFEYGGF PPESNYLFLG DYVDRGKQSL
110 120 130 140 150
ETICLLLAYK IKYPENFFIL RGNHECASIN RIYGFYDECK RRYNIKLWKT
160 170 180 190 200
FTDCFNCLPI AAIIDEKIFC MHGGLSPDLN SMEQIRRVMR PTDIPDVGLL
210 220 230 240 250
CDLLWSDPDK DIVGWSENDR GVSFTFGPDV VNRFLQKQDM ELICRAHQVV
260 270 280 290 300
EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAQK
310
SLPRQAGGRK KK
Length:312
Mass (Da):35,907
Last modified:October 1, 1993 - v1
Checksum:i71B20E3A4ED93235
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371D → H in AAA34570. (PubMed:2544298)Curated
Sequence conflicti273 – 2731G → V in AAA34570. (PubMed:2544298)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77175 Genomic DNA. Translation: AAB59322.1.
M27070 Genomic DNA. Translation: AAA34570.1.
U18916 Genomic DNA. Translation: AAC03231.1.
BK006939 Genomic DNA. Translation: DAA07793.1.
PIRiS32595.
RefSeqiNP_011059.3. NM_001179023.3.

Genome annotation databases

EnsemblFungiiYER133W; YER133W; YER133W.
GeneIDi856870.
KEGGisce:YER133W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77175 Genomic DNA. Translation: AAB59322.1 .
M27070 Genomic DNA. Translation: AAA34570.1 .
U18916 Genomic DNA. Translation: AAC03231.1 .
BK006939 Genomic DNA. Translation: DAA07793.1 .
PIRi S32595.
RefSeqi NP_011059.3. NM_001179023.3.

3D structure databases

ProteinModelPortali P32598.
SMRi P32598. Positions 6-298.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36877. 548 interactions.
DIPi DIP-1336N.
IntActi P32598. 149 interactions.
MINTi MINT-384176.
STRINGi 4932.YER133W.

Proteomic databases

MaxQBi P32598.
PaxDbi P32598.
PeptideAtlasi P32598.
PRIDEi P32598.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YER133W ; YER133W ; YER133W .
GeneIDi 856870.
KEGGi sce:YER133W.

Organism-specific databases

CYGDi YER133w.
SGDi S000000935. GLC7.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00530000062911.
HOGENOMi HOG000172697.
InParanoidi P32598.
KOi K06269.
OMAi GSKPGQQ.
OrthoDBi EOG79KPQ9.

Enzyme and pathway databases

BioCyci YEAST:YER133W-MONOMER.

Miscellaneous databases

NextBioi 983240.

Gene expression databases

Genevestigatori P32598.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. 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. 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. 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].

Entry informationi

Entry nameiPP12_YEAST
AccessioniPrimary (citable) accession number: P32598
Secondary accession number(s): D3DM39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 29, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 14600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3