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P63088

- PP1G_RAT

UniProt

P63088 - PP1G_RAT

Protein

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Gene

Ppp1cc

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (13 Sep 2004)
      Previous versions | rss
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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 By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.

    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 21 Publication
    Metal bindingi124 – 1241Manganese 21 Publication
    Active sitei125 – 1251Proton donorBy similarity
    Metal bindingi173 – 1731Manganese 21 Publication
    Metal bindingi248 – 2481Manganese 21 Publication

    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: UniProtKB

    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. neuron differentiation Source: MGI
    7. protein dephosphorylation Source: UniProtKB
    8. 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_194641. Downregulation of TGF-beta receptor signaling.
    REACT_194781. Separation of Sister Chromatids.
    REACT_198611. Resolution of Sister Chromatid Cohesion.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 12

    Organism-specific databases

    RGDi3377. 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. cytosol Source: Reactome
    4. dendritic spine Source: RGD
    5. midbody Source: UniProtKB-SubCell
    6. mitochondrion Source: UniProtKB
    7. nuclear speck Source: UniProtKB-SubCell
    8. nucleolus Source: UniProtKB-SubCell
    9. 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_0000058789Add
    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

    PaxDbiP63088.
    PRIDEiP63088.

    PTM databases

    PhosphoSiteiP63088.

    Expressioni

    Gene expression databases

    GenevestigatoriP63088.

    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 sliver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. 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. Isoform gamma-2 interacts with SPZ1. 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 By similarity. Interacts with NEK2. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Grm1P2338515EBI-80049,EBI-4410410
    Grm5P3142419EBI-80049,EBI-2902734
    Grm7P354004EBI-80049,EBI-6936416
    Grm7Q6333711EBI-80049,EBI-6935714
    Ppp1r9aO358672EBI-80049,EBI-7092421
    Ppp1r9bO352743EBI-80049,EBI-80022

    Protein-protein interaction databases

    IntActiP63088. 7 interactions.
    MINTiMINT-4591365.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 179
    Turni18 – 214
    Helixi32 – 4817
    Beta strandi51 – 555
    Beta strandi57 – 626
    Helixi69 – 7911
    Beta strandi87 – 893
    Beta strandi94 – 985
    Helixi100 – 11314
    Turni115 – 1173
    Beta strandi118 – 1203
    Helixi128 – 1314
    Helixi136 – 1438
    Helixi146 – 15611
    Beta strandi162 – 1654
    Turni166 – 1683
    Beta strandi169 – 1746
    Helixi183 – 1875
    Beta strandi197 – 1993
    Helixi200 – 2067
    Beta strandi214 – 2185
    Beta strandi222 – 2276
    Helixi229 – 23911
    Beta strandi242 – 2465
    Beta strandi253 – 2586
    Turni259 – 2624
    Beta strandi263 – 2675
    Helixi272 – 2743
    Beta strandi279 – 2857
    Beta strandi290 – 2967

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O8AX-ray2.61A/B2-323[»]
    2O8GX-ray2.50A/B2-323[»]
    ProteinModelPortaliP63088.
    SMRiP63088. Positions 6-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP63088.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172697.
    HOVERGENiHBG000216.
    KOiK06269.
    OMAiPRSMITK.
    OrthoDBiEOG7TJ3K3.
    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: P63088-1) [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: P63088-2) [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
    Isoform Gamma-2 (identifier: P63088-2)
    Sequence conflicti214 – 2141L → F in BAA14197. (PubMed:2177460)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei315 – 3239GMITKQAKK → VGSGLNPSIQKASNYRNNTV LYE in isoform Gamma-2. 1 PublicationVSP_011566

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90165 mRNA. Translation: BAA14196.1.
    D90166 mRNA. Translation: BAA14197.1.
    PIRiI76572.
    I76573.
    RefSeqiNP_071943.1. NM_022498.2. [P63088-1]
    UniGeneiRn.1495.
    Rn.234216.

    Genome annotation databases

    EnsembliENSRNOT00000048851; ENSRNOP00000047912; ENSRNOG00000001269. [P63088-2]
    GeneIDi24669.
    KEGGirno:24669.
    UCSCiRGD:3377. rat. [P63088-1]

    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
    D90165 mRNA. Translation: BAA14196.1 .
    D90166 mRNA. Translation: BAA14197.1 .
    PIRi I76572.
    I76573.
    RefSeqi NP_071943.1. NM_022498.2. [P63088-1 ]
    UniGenei Rn.1495.
    Rn.234216.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2O8A X-ray 2.61 A/B 2-323 [» ]
    2O8G X-ray 2.50 A/B 2-323 [» ]
    ProteinModelPortali P63088.
    SMRi P63088. Positions 6-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P63088. 7 interactions.
    MINTi MINT-4591365.

    PTM databases

    PhosphoSitei P63088.

    Proteomic databases

    PaxDbi P63088.
    PRIDEi P63088.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000048851 ; ENSRNOP00000047912 ; ENSRNOG00000001269 . [P63088-2 ]
    GeneIDi 24669.
    KEGGi rno:24669.
    UCSCi RGD:3377. rat. [P63088-1 ]

    Organism-specific databases

    CTDi 5501.
    RGDi 3377. Ppp1cc.

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172697.
    HOVERGENi HBG000216.
    KOi K06269.
    OMAi PRSMITK.
    OrthoDBi EOG7TJ3K3.
    TreeFami TF354243.

    Enzyme and pathway databases

    Reactomei REACT_194641. Downregulation of TGF-beta receptor signaling.
    REACT_194781. Separation of Sister Chromatids.
    REACT_198611. Resolution of Sister Chromatid Cohesion.

    Miscellaneous databases

    EvolutionaryTracei P63088.
    NextBioi 295513.
    PROi P63088.

    Gene expression databases

    Genevestigatori P63088.

    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. "Identification of members of the protein phosphatase 1 gene family in the rat and enhanced expression of protein phosphatase 1 alpha gene in rat hepatocellular carcinomas."
      Sasaki K., Shima H., Kitagawa Y., Irino S., Sugimura T., Nagao M.
      Jpn. J. Cancer Res. 81:1272-1280(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GAMMA-1 AND GAMMA-2), ALTERNATIVE SPLICING.
    2. Erratum
      Sasaki K., Shima H., Kitagawa Y., Irino S., Sugimura T., Nagao M.
      Jpn. J. Cancer Res. 82:873-873(1991) [PubMed] [Europe PMC] [Abstract]
    3. "Regulation of neurabin I interaction with protein phosphatase 1 by phosphorylation."
      McAvoy T., Allen P.B., Obaishi H., Nakanishi H., Takai Y., Greengard P., Nairn A.C., Hemmings H.C. Jr.
      Biochemistry 38:12943-12949(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 42-58 AND 212-234, INTERACTION WITH PPP1R9A.
      Strain: Sprague-Dawley.
    4. "Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography."
      Moorhead G., MacKintosh C., Morrice N., Cohen P.
      FEBS Lett. 362:101-105(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R3B.
    5. "Identification of the separate domains in the hepatic glycogen-targeting subunit of protein phosphatase 1 that interact with phosphorylase a, glycogen and protein phosphatase 1."
      Armstrong C.G., Doherty M.J., Cohen P.T.W.
      Biochem. J. 336:699-704(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R3B.
    6. "Brain actin-associated protein phosphatase 1 holoenzymes containing spinophilin, neurabin, and selected catalytic subunit isoforms."
      MacMillan L.B., Bass M.A., Cheng N., Howard E.F., Tamura M., Strack S., Wadzinski B.E., Colbran R.J.
      J. Biol. Chem. 274:35845-35854(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    7. "Structural basis for regulation of protein phosphatase 1 by inhibitor-2."
      Hurley T.D., Yang J., Zhang L., Goodwin K.D., Zou Q., Cortese M., Dunker A.K., DePaoli-Roach A.A.
      J. Biol. Chem. 282:28874-28883(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-323 IN COMPLEX WITH MANGANESE AND M.MUSCULUS INHIBITOR PPP1R2.

    Entry informationi

    Entry nameiPP1G_RAT
    AccessioniPrimary (citable) accession number: P63088
    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 108 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    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