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P32598

- PP12_YEAST

UniProt

P32598 - PP12_YEAST

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
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    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 binding Source: IntAct
    3. 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

    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

    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.
    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.

    P32598-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSQPVDVDN IIDRLLEVRG SKPGQQVDLE ENEIRYLCSK ARSIFIKQPI    50
    LLELEAPIKI CGDIHGQYYD LLRLFEYGGF PPESNYLFLG DYVDRGKQSL 100
    ETICLLLAYK IKYPENFFIL RGNHECASIN RIYGFYDECK RRYNIKLWKT 150
    FTDCFNCLPI AAIIDEKIFC MHGGLSPDLN SMEQIRRVMR PTDIPDVGLL 200
    CDLLWSDPDK DIVGWSENDR GVSFTFGPDV VNRFLQKQDM ELICRAHQVV 250
    EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAQK 300
    SLPRQAGGRK KK 312
    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.
    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

    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 1, 2014
    This is version 152 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