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P36873

- PP1G_HUMAN

UniProt

P36873 - PP1G_HUMAN

Protein

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Gene

PPP1CC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 174 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      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.3 Publications

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

    Cofactori

    Binds 2 manganese ions per subunit.2 Publications

    Enzyme regulationi

    Inactivated by binding to URI1. The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi64 – 641Manganese 12 Publications
    Metal bindingi66 – 661Manganese 12 Publications
    Metal bindingi92 – 921Manganese 12 Publications
    Metal bindingi92 – 921Manganese 22 Publications
    Metal bindingi124 – 1241Manganese 22 Publications
    Active sitei125 – 1251Proton donor
    Metal bindingi173 – 1731Manganese 22 Publications
    Metal bindingi248 – 2481Manganese 22 Publications
    Sitei273 – 2731Inhibition by microcystin toxin binding

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphatase activity Source: UniProtKB
    3. phosphoprotein phosphatase activity Source: Reactome
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein kinase binding Source: UniProtKB
    7. protein N-terminus binding Source: MGI
    8. protein serine/threonine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. cell division Source: UniProtKB-KW
    2. circadian regulation of gene expression Source: UniProtKB
    3. entrainment of circadian clock by photoperiod Source: UniProtKB
    4. glycogen metabolic process Source: UniProtKB-KW
    5. mitotic cell cycle Source: Reactome
    6. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
    7. protein dephosphorylation Source: UniProtKB
    8. regulation of circadian rhythm Source: UniProtKB
    9. regulation of nucleocytoplasmic transport Source: Ensembl
    10. small molecule metabolic process Source: Reactome
    11. transforming growth factor beta receptor signaling pathway Source: Reactome
    12. triglyceride catabolic process Source: Reactome

    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_120727. Downregulation of TGF-beta receptor signaling.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
    REACT_682. Mitotic Prometaphase.
    SignaLinkiP36873.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9283. PPP1CC.

    Subcellular locationi

    Cytoplasm. Nucleus. Nucleusnucleolus. Nucleusnucleoplasm. Nucleus speckle. Chromosomecentromerekinetochore. Cleavage furrow. Midbody. Mitochondrion
    Note: Colocalizes with SPZ1 in the nucleus By similarity. Colocalizes with URI1 at mitochondrion. 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.By similarity

    GO - Cellular componenti

    1. cleavage furrow Source: UniProtKB-SubCell
    2. condensed chromosome kinetochore Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB
    4. cytosol Source: Reactome
    5. midbody Source: UniProtKB-SubCell
    6. mitochondrial outer membrane Source: Ensembl
    7. mitochondrion Source: UniProtKB
    8. MLL5-L complex Source: UniProtKB
    9. nuclear speck Source: UniProtKB-SubCell
    10. nucleolus Source: UniProtKB
    11. nucleus Source: UniProtKB
    12. protein complex Source: UniProtKB
    13. PTW/PP1 phosphatase complex Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Kinetochore, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi125 – 1251H → A: Loss of activity. 1 Publication
    Mutagenesisi273 – 2731C → A, S or L: Abolishes interaction with microcystin toxin. 1 Publication

    Organism-specific databases

    PharmGKBiPA33611.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 323322Serine/threonine-protein phosphatase PP1-gamma catalytic subunitPRO_0000058787Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei307 – 3071Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylated by NEK2.2 Publications

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiP36873.
    PaxDbiP36873.
    PRIDEiP36873.

    PTM databases

    PhosphoSiteiP36873.

    Expressioni

    Gene expression databases

    ArrayExpressiP36873.
    BgeeiP36873.
    CleanExiHS_PPP1CC.
    GenevestigatoriP36873.

    Organism-specific databases

    HPAiCAB022645.
    HPA013661.

    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. Interacts with cyanobacterial toxin microcystin; disulfide-linked. Interacts with PPP1R3B and PPP1R7. Isoform gamma-2 interacts with SPZ1 By similarity. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with CDCA2. 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 PPP1R42; the interaction is direct By similarity. 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 isoform 1 and isoform 4 NEK2. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner.By similarity14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    A1DRY32EBI-3964623,EBI-4311408
    BRCA1P383982EBI-356283,EBI-349905
    ClockO087852EBI-356283,EBI-79859From a different organism.
    PPP1R2P412364EBI-356283,EBI-1056517
    PPP1R32Q7Z5V64EBI-3964623,EBI-4311771
    RANBP9Q96S593EBI-3964623,EBI-636085
    TCTEX1D4Q5JR983EBI-3964623,EBI-4311709
    TP53P046372EBI-356289,EBI-366083
    TP53BP2Q136256EBI-356283,EBI-77642
    URI1O947636EBI-356283,EBI-357067

    Protein-protein interaction databases

    BioGridi111495. 191 interactions.
    DIPiDIP-749N.
    IntActiP36873. 145 interactions.
    MINTiMINT-190765.
    STRINGi9606.ENSP00000335084.

    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
    Turni132 – 1354
    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 – 23810
    Beta strandi242 – 2465
    Beta strandi254 – 2585
    Turni259 – 2624
    Beta strandi263 – 2675
    Helixi272 – 2743
    Beta strandi280 – 2856
    Beta strandi291 – 2966

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IT6X-ray2.00A/B1-323[»]
    1JK7X-ray1.90A1-323[»]
    1U32X-ray2.00A6-298[»]
    2BCDX-ray2.10A1-323[»]
    2BDXX-ray2.30A1-323[»]
    ProteinModelPortaliP36873.
    SMRiP36873. Positions 6-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36873.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172697.
    HOVERGENiHBG000216.
    KOiK06269.
    OMAiPRSMITK.
    OrthoDBiEOG7TJ3K3.
    PhylomeDBiP36873.
    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: P36873-1) [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

    MADLDKLNID 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:June 1, 1994 - v1
    Checksum:i0EEEF0E842188536
    GO
    Isoform Gamma-2 (identifier: P36873-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:337
    Mass (Da):38,518
    Checksum:i9731E5A6C8EEBF46
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti152 – 1521F → S.
    Corresponds to variant rs11558237 [ dbSNP | Ensembl ].
    VAR_051734

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei315 – 3239GMITKQAKK → VASGLNPSIQKASNYRNNTV LYE in isoform Gamma-2. 1 PublicationVSP_005094

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74008 mRNA. Translation: CAA52169.1.
    BC014073 mRNA. Translation: AAH14073.1.
    L07395 mRNA. Translation: AAA19823.1.
    CCDSiCCDS58279.1. [P36873-2]
    CCDS9150.1. [P36873-1]
    PIRiS35699.
    S35700.
    RefSeqiNP_001231903.1. NM_001244974.1. [P36873-2]
    NP_002701.1. NM_002710.3. [P36873-1]
    UniGeneiHs.79081.

    Genome annotation databases

    EnsembliENST00000335007; ENSP00000335084; ENSG00000186298. [P36873-1]
    ENST00000340766; ENSP00000341779; ENSG00000186298. [P36873-2]
    GeneIDi5501.
    KEGGihsa:5501.
    UCSCiuc001tru.3. human. [P36873-1]
    uc021rdx.1. human. [P36873-2]

    Polymorphism databases

    DMDMi548573.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    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
    X74008 mRNA. Translation: CAA52169.1 .
    BC014073 mRNA. Translation: AAH14073.1 .
    L07395 mRNA. Translation: AAA19823.1 .
    CCDSi CCDS58279.1. [P36873-2 ]
    CCDS9150.1. [P36873-1 ]
    PIRi S35699.
    S35700.
    RefSeqi NP_001231903.1. NM_001244974.1. [P36873-2 ]
    NP_002701.1. NM_002710.3. [P36873-1 ]
    UniGenei Hs.79081.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IT6 X-ray 2.00 A/B 1-323 [» ]
    1JK7 X-ray 1.90 A 1-323 [» ]
    1U32 X-ray 2.00 A 6-298 [» ]
    2BCD X-ray 2.10 A 1-323 [» ]
    2BDX X-ray 2.30 A 1-323 [» ]
    ProteinModelPortali P36873.
    SMRi P36873. Positions 6-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111495. 191 interactions.
    DIPi DIP-749N.
    IntActi P36873. 145 interactions.
    MINTi MINT-190765.
    STRINGi 9606.ENSP00000335084.

    Chemistry

    BindingDBi P36873.
    ChEMBLi CHEMBL4438.

    PTM databases

    PhosphoSitei P36873.

    Polymorphism databases

    DMDMi 548573.

    Proteomic databases

    MaxQBi P36873.
    PaxDbi P36873.
    PRIDEi P36873.

    Protocols and materials databases

    DNASUi 5501.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335007 ; ENSP00000335084 ; ENSG00000186298 . [P36873-1 ]
    ENST00000340766 ; ENSP00000341779 ; ENSG00000186298 . [P36873-2 ]
    GeneIDi 5501.
    KEGGi hsa:5501.
    UCSCi uc001tru.3. human. [P36873-1 ]
    uc021rdx.1. human. [P36873-2 ]

    Organism-specific databases

    CTDi 5501.
    GeneCardsi GC12M111157.
    HGNCi HGNC:9283. PPP1CC.
    HPAi CAB022645.
    HPA013661.
    MIMi 176914. gene.
    neXtProti NX_P36873.
    PharmGKBi PA33611.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172697.
    HOVERGENi HBG000216.
    KOi K06269.
    OMAi PRSMITK.
    OrthoDBi EOG7TJ3K3.
    PhylomeDBi P36873.
    TreeFami TF354243.

    Enzyme and pathway databases

    Reactomei REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
    REACT_682. Mitotic Prometaphase.
    SignaLinki P36873.

    Miscellaneous databases

    ChiTaRSi PPP1CC. human.
    EvolutionaryTracei P36873.
    GeneWikii PPP1CC.
    GenomeRNAii 5501.
    NextBioi 21286.
    PROi P36873.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36873.
    Bgeei P36873.
    CleanExi HS_PPP1CC.
    Genevestigatori P36873.

    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. "Sequence of human protein serine/threonine phosphatase 1 gamma and localization of the gene (PPP1CC) encoding it to chromosome bands 12q24.1-q24.2."
      Barker H.M., Craig S.P., Spurr N.K., Cohen P.T.W.
      Biochim. Biophys. Acta 1178:228-233(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GAMMA-1 AND GAMMA-2).
    2. "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).
      Tissue: Placenta.
    3. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-15; 44-60; 99-122; 151-168 AND 247-260, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    4. Bienvenut W.V., Bilsland A.E., Keith W.N.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-15; 27-36; 44-60; 99-111; 133-141; 151-187 AND 239-260, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    5. "Molecular cloning and chromosomal localization of a human skeletal muscle PP-1 gamma 1 cDNA."
      Norman S.A., Mott D.M.
      Mamm. Genome 5:41-45(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-323 (ISOFORM GAMMA-1).
      Tissue: Skeletal muscle.
    6. "The cyanobacterial toxin microcystin binds covalently to cysteine-273 on protein phosphatase 1."
      MacKintosh R.W., Dalby K.N., Campbell D.G., Cohen P.T.W., Cohen P., MacKintosh C.
      FEBS Lett. 371:236-240(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MICROCYSTIN, MUTAGENESIS OF CYS-273.
    7. "PPP1R6, a novel member of the family of glycogen-targeting subunits of protein phosphatase 1."
      Armstrong C.G., Browne G.J., Cohen P., Cohen P.T.W.
      FEBS Lett. 418:210-214(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R3D.
    8. "Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells."
      Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.
      J. Cell Sci. 114:4219-4228(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP1R8, MUTAGENESIS OF HIS-125.
    9. "Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1."
      Connor J.H., Weiser D.C., Li S., Hallenbeck J.M., Shenolikar S.
      Mol. Cell. Biol. 21:6841-6850(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R15A.
    10. "Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1."
      Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W., Bollen M.
      J. Biol. Chem. 277:47331-47337(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R7.
    11. "Time-lapse imaging reveals dynamic relocalization of PP1gamma throughout the mammalian cell cycle."
      Trinkle-Mulcahy L., Andrews P.D., Wickramasinghe S., Sleeman J., Prescott A., Lam Y.W., Lyon C., Swedlow J.R., Lamond A.I.
      Mol. Biol. Cell 14:107-117(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Alternatively spliced protein variants as potential therapeutic targets for male infertility and contraception."
      Fardilha M., Wu W., Sa R., Fidalgo S., Sousa C., Mota C., da Cruz e Silva O.A., da Cruz e Silva E.F.
      Ann. N. Y. Acad. Sci. 1030:468-478(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEK2, PHOSPHORYLATION.
    13. "A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress."
      Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D., Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.
      Science 307:935-939(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    14. "Repo-Man recruits PP1 gamma to chromatin and is essential for cell viability."
      Trinkle-Mulcahy L., Andersen J., Lam Y.W., Moorhead G., Mann M., Lamond A.I.
      J. Cell Biol. 172:679-692(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDCA2.
    15. "Protein phosphatase-1alpha regulates centrosome splitting through Nek2."
      Mi J., Guo C., Brautigan D.L., Larner J.M.
      Cancer Res. 67:1082-1089(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEK2.
    16. "S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling."
      Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M., Aebersold R., Hess D., Krek W.
      Mol. Cell 28:28-40(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF RPS6KB1, ENZYME REGULATION, INTERACTION WITH URI1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    17. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NOM1.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
      Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
      Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
    20. "Identification and characterization of a novel human PP1 phosphatase complex."
      Lee J.H., You J., Dobrota E., Skalnik D.G.
      J. Biol. Chem. 285:24466-24476(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, INTERACTION WITH PPP1R8.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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.
    23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate."
      Egloff M.-P., Cohen P.T.W., Reinemer P., Barford D.
      J. Mol. Biol. 254:942-959(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    25. "Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1."
      Maynes J.T., Bateman K.S., Cherney M.M., Das A.K., Luu H.A., Holmes C.F., James M.N.
      J. Biol. Chem. 276:44078-44082(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE, COFACTOR.
    26. "Crystal structure and mutagenesis of a protein phosphatase-1:calcineurin hybrid elucidate the role of the beta12-beta13 loop in inhibitor binding."
      Maynes J.T., Perreault K.R., Cherney M.M., Luu H.A., James M.N., Holmes C.F.
      J. Biol. Chem. 279:43198-43206(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-298 IN COMPLEX WITH MANGANESE, CATALYTIC ACTIVITY, COFACTOR.

    Entry informationi

    Entry nameiPP1G_HUMAN
    AccessioniPrimary (citable) accession number: P36873
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 174 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Microcystin toxin is bound to Cys-273 through a thioether bond.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3