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P63087

- PP1G_MOUSE

UniProt

P63087 - PP1G_MOUSE

Protein

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Gene

Ppp1cc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (13 Sep 2004)
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    Functioni

    Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E.2 Publications

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Enzyme regulationi

    Inactivated by binding to URI1.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi64 – 641Manganese 1By similarity
    Metal bindingi66 – 661Manganese 1By similarity
    Metal bindingi92 – 921Manganese 1By similarity
    Metal bindingi92 – 921Manganese 2By similarity
    Metal bindingi124 – 1241Manganese 2By similarity
    Active sitei125 – 1251Proton donorBy similarity
    Metal bindingi173 – 1731Manganese 2By similarity
    Metal bindingi248 – 2481Manganese 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. circadian regulation of gene expression Source: UniProtKB
    4. entrainment of circadian clock by photoperiod Source: UniProtKB
    5. glycogen metabolic process Source: UniProtKB-KW
    6. protein dephosphorylation Source: UniProtKB
    7. regulation of circadian rhythm Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Biological rhythms, Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.
    REACT_215733. Downregulation of TGF-beta receptor signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (EC:3.1.3.16)
    Short name:
    PP-1G
    Alternative name(s):
    Protein phosphatase 1C catalytic subunit
    Gene namesi
    Name:Ppp1cc
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:104872. Ppp1cc.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Cleavage furrow By similarity. Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity. Chromosomecentromerekinetochore By similarity. Nucleus speckle By similarity. Midbody By similarity. Mitochondrion By similarity
    Note: Rapidly exchanges between the nucleolar, nucleoplasmic and cytoplasmic compartments. Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleolus to nuclear speckles. Shows a dynamic targeting to specific sites throughout the cell cycle. Highly concentrated in nucleoli of interphase cells and localizes at kinetochores early in mitosis. Relocalization to chromosome-containing regions occurs at the transition from early to late anaphase. Also accumulates at the cleavage furrow and midbody by telophase. Colocalizes with SPZ1 in the nucleus. Colocalizes with URI1 at mitochondrion By similarity.By similarity

    GO - Cellular componenti

    1. cleavage furrow Source: UniProtKB-SubCell
    2. condensed chromosome kinetochore Source: UniProtKB-SubCell
    3. midbody Source: UniProtKB-SubCell
    4. mitochondrion Source: UniProtKB-SubCell
    5. MLL5-L complex Source: Ensembl
    6. nuclear speck Source: UniProtKB-SubCell
    7. nucleolus Source: UniProtKB-SubCell
    8. PTW/PP1 phosphatase complex Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Kinetochore, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 323322Serine/threonine-protein phosphatase PP1-gamma catalytic subunitPRO_0000058788Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei307 – 3071PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylated by NEK2.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP63087.
    PaxDbiP63087.
    PRIDEiP63087.

    PTM databases

    PhosphoSiteiP63087.

    Expressioni

    Gene expression databases

    BgeeiP63087.
    GenevestigatoriP63087.

    Interactioni

    Subunit structurei

    PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R3B, PPP1R7 and CDCA2 By similarity. Isoform gamma-2 interacts with SPZ1. This interaction can prevent SPZ1 binding to the E-box and inhibits PPP1CC activity. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with IKFZ1; the interaction targets PPP1CC to pericentromeric heterochromatin, dephosphorylates IKAROS, stabilizes it and prevents it from degradation. Interacts with NOM1 and PPP1R8. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with NEK2. Interacts with NEK2. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner By similarity. Isoform 2 interacts with PPP1R42; the interaction is direct.By similarity5 Publications

    Protein-protein interaction databases

    BioGridi202337. 34 interactions.
    IntActiP63087. 22 interactions.
    MINTiMINT-4591330.

    Structurei

    3D structure databases

    ProteinModelPortaliP63087.
    SMRiP63087. Positions 6-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00530000062911.
    HOGENOMiHOG000172697.
    HOVERGENiHBG000216.
    KOiK06269.
    OMAiPRSMITK.
    OrthoDBiEOG7TJ3K3.
    PhylomeDBiP63087.
    TreeFamiTF354243.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Gamma-1 (identifier: P63087-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MADIDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP    50
    ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS 100
    LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK 150
    TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL 200
    LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV 250
    VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE 300
    KKKPNATRPV TPPRGMITKQ AKK 323
    Length:323
    Mass (Da):36,984
    Last modified:September 13, 2004 - v1
    Checksum:i4E28412C16898615
    GO
    Isoform Gamma-2 (identifier: P63087-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         315-323: GMITKQAKK → VGSGLNPSIQKASNYRNNTVLYE

    Show »
    Length:337
    Mass (Da):38,504
    Checksum:iE6F271155E0E67D7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti316 – 3172MI → IV in AAC53383. (PubMed:9339378)Curated
    Sequence conflicti316 – 3172MI → IV in AAC53384. (PubMed:9339378)Curated
    Sequence conflicti316 – 3172MI → IV in BAA19729. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei315 – 3239GMITKQAKK → VGSGLNPSIQKASNYRNNTV LYE in isoform Gamma-2. 2 PublicationsVSP_005095

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27071 mRNA. Translation: AAA37526.1.
    U53456 mRNA. Translation: AAC53383.1.
    U53276
    , U53271, U53272, U53273, U53275 Genomic DNA. Translation: AAC53384.1.
    U53276
    , U53271, U53272, U53273, U53275 Genomic DNA. Translation: AAC53385.1.
    D85137 mRNA. Translation: BAA19729.1.
    BC010613 mRNA. Translation: AAH10613.1.
    BC021646 mRNA. Translation: AAH21646.1.
    BC085496 mRNA. Translation: AAH85496.1.
    CCDSiCCDS19643.1. [P63087-1]
    PIRiC32550.
    RefSeqiNP_038664.2. NM_013636.3. [P63087-1]
    XP_006508478.1. XM_006508415.1. [P63087-2]
    XP_006530263.1. XM_006530200.1. [P63087-2]
    XP_006544330.1. XM_006544267.1. [P63087-2]
    UniGeneiMm.280784.
    Mm.334198.

    Genome annotation databases

    EnsembliENSMUST00000086294; ENSMUSP00000083474; ENSMUSG00000004455. [P63087-2]
    ENSMUST00000102528; ENSMUSP00000099587; ENSMUSG00000004455. [P63087-1]
    GeneIDi19047.
    434233.
    KEGGimmu:19047.
    mmu:434233.
    UCSCiuc008zks.1. mouse. [P63087-1]
    uc008zkt.1. mouse. [P63087-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    The things we forget - Issue 32 of March 2003

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27071 mRNA. Translation: AAA37526.1 .
    U53456 mRNA. Translation: AAC53383.1 .
    U53276
    , U53271 , U53272 , U53273 , U53275 Genomic DNA. Translation: AAC53384.1 .
    U53276
    , U53271 , U53272 , U53273 , U53275 Genomic DNA. Translation: AAC53385.1 .
    D85137 mRNA. Translation: BAA19729.1 .
    BC010613 mRNA. Translation: AAH10613.1 .
    BC021646 mRNA. Translation: AAH21646.1 .
    BC085496 mRNA. Translation: AAH85496.1 .
    CCDSi CCDS19643.1. [P63087-1 ]
    PIRi C32550.
    RefSeqi NP_038664.2. NM_013636.3. [P63087-1 ]
    XP_006508478.1. XM_006508415.1. [P63087-2 ]
    XP_006530263.1. XM_006530200.1. [P63087-2 ]
    XP_006544330.1. XM_006544267.1. [P63087-2 ]
    UniGenei Mm.280784.
    Mm.334198.

    3D structure databases

    ProteinModelPortali P63087.
    SMRi P63087. Positions 6-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202337. 34 interactions.
    IntActi P63087. 22 interactions.
    MINTi MINT-4591330.

    PTM databases

    PhosphoSitei P63087.

    Proteomic databases

    MaxQBi P63087.
    PaxDbi P63087.
    PRIDEi P63087.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000086294 ; ENSMUSP00000083474 ; ENSMUSG00000004455 . [P63087-2 ]
    ENSMUST00000102528 ; ENSMUSP00000099587 ; ENSMUSG00000004455 . [P63087-1 ]
    GeneIDi 19047.
    434233.
    KEGGi mmu:19047.
    mmu:434233.
    UCSCi uc008zks.1. mouse. [P63087-1 ]
    uc008zkt.1. mouse. [P63087-2 ]

    Organism-specific databases

    CTDi 5501.
    MGIi MGI:104872. Ppp1cc.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00530000062911.
    HOGENOMi HOG000172697.
    HOVERGENi HBG000216.
    KOi K06269.
    OMAi PRSMITK.
    OrthoDBi EOG7TJ3K3.
    PhylomeDBi P63087.
    TreeFami TF354243.

    Enzyme and pathway databases

    Reactomei REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.
    REACT_215733. Downregulation of TGF-beta receptor signaling.

    Miscellaneous databases

    ChiTaRSi PPP1CC. mouse.
    NextBioi 295513.
    PROi P63087.
    SOURCEi Search...

    Gene expression databases

    Bgeei P63087.
    Genevestigatori P63087.

    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 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 [MRNA] (ISOFORM GAMMA-2).
      Tissue: Brain.
    2. "Genomic organization and functional analysis of the murine protein phosphatase 1c gamma (Ppp1cc) gene."
      Okano K., Heng H., Trevisanato S., Tyers M., Varmuza S.
      Genomics 45:211-215(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS GAMMA-1 AND GAMMA-2), ALTERNATIVE SPLICING.
      Strain: 129 and CD-1.
      Tissue: Embryo.
    3. "Tertially complex among Pim-1 kinase, protein phosphatase 1 gamma, and PAP-1."
      Harada Y., Sato E., Izumi F., Imamura Y., Ariga H., Iguchi-Ariga S.
      Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-1).
      Tissue: Brain.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-1).
      Strain: C57BL/6, C57BL/6J and NOD.
      Tissue: Brain and Thymus.
    5. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 61-74 AND 114-122, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    6. "Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells."
      Jousse C., Oyadomari S., Novoa I., Lu P., Zhang Y., Harding H.P., Ron D.
      J. Cell Biol. 163:767-775(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R15B.
    7. "Identification of the spermatogenic zip protein Spz1 as a putative protein phosphatase-1 (PP1) regulatory protein that specifically binds the PP1cgamma2 splice variant in mouse testis."
      Hrabchak C., Varmuza S.
      J. Biol. Chem. 279:37079-37086(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPZ1.
    8. "Nck in a complex containing the catalytic subunit of protein phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling and cell survival to endoplasmic reticulum stress."
      Latreille M., Larose L.
      J. Biol. Chem. 281:26633-26644(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
    9. "TLRR (lrrc67) interacts with PP1 and is associated with a cytoskeletal complex in the testis."
      Wang R., Kaul A., Sperry A.O.
      Biol. Cell 102:173-189(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R42.
    10. "Ikaros stability and pericentromeric localization are regulated by protein phosphatase 1."
      Popescu M., Gurel Z., Ronni T., Song C., Hung K.Y., Payne K.J., Dovat S.
      J. Biol. Chem. 284:13869-13880(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IKFZ1.
    11. "Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock."
      Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.
      PLoS ONE 6:E21325-E21325(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN CLOCK.
    12. "The period of the circadian oscillator is primarily determined by the balance between casein kinase 1 and protein phosphatase 1."
      Lee H.M., Chen R., Kim H., Etchegaray J.P., Weaver D.R., Lee C.
      Proc. Natl. Acad. Sci. U.S.A. 108:16451-16456(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN CLOCK.

    Entry informationi

    Entry nameiPP1G_MOUSE
    AccessioniPrimary (citable) accession number: P63087
    Secondary accession number(s): O09186
    , O09189, P37139, Q64679
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: September 13, 2004
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3