Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Details

Name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Synonyms
  • 3.1.3.16
  • PP-1G
  • Protein phosphatase 1C catalytic subunit
Gene Name
PPP1CC
Organism
Humans
Amino acid sequence
>lcl|BSEQ0002872|Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
MADLDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAE
KKKPNATRPVTPPRGMITKQAKK
Number of residues
323
Molecular Weight
36983.4
Theoretical pI
6.5
GO Classification
Functions
metal ion binding / phosphatase activity / phosphoprotein phosphatase activity / poly(A) RNA binding / protein kinase binding / protein N-terminus binding / protein serine/threonine phosphatase activity
Processes
cell division / circadian regulation of gene expression / entrainment of circadian clock by photoperiod / glycogen metabolic process / mitotic cell cycle / negative regulation of transforming growth factor beta receptor signaling pathway / neuron differentiation / protein dephosphorylation / regulation of circadian rhythm / small GTPase mediated signal transduction / small molecule metabolic process / transforming growth factor beta receptor signaling pathway / triglyceride catabolic process
Components
cleavage furrow / condensed chromosome kinetochore / cytoplasm / cytosol / dendritic spine / focal adhesion / midbody / mitochondrion / MLL5-L complex / nuclear speck / nucleolus / nucleus / protein complex / PTW/PP1 phosphatase complex
General Function
Protein serine/threonine phosphatase activity
Specific Function
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 Ca(2+)/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. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0021660|Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PPP1CC)
ATGGCGGATTTAGATAAACTCAACATCGACAGCATTATCCAACGGCTGCTGGAAGTGAGA
GGGTCCAAGCCTGGTAAGAATGTCCAGCTTCAGGAGAATGAAATCAGAGGACTGTGCTTA
AAGTCTCGTGAAATCTTTCTCAGTCAGCCTATCCTACTAGAACTTGAAGCACCACTCAAA
ATATGTGGTGACATCCATGGACAATACTATGATTTGCTGCGACTTTTTGAGTACGGTGGT
TTCCCACCAGAAAGCAACTACCTGTTTCTTGGGGACTATGTGGACAGGGGAAAGCAGTCA
TTGGAGACGATCTGCCTCTTACTGGCCTACAAAATAAAATATCCTGAGAATTTTTTTCTT
CTCAGAGGGAACCATGAATGTGCCAGCATCAACAGAATTTATGGATTTTATGATGAATGT
AAAAGAAGATACAACATTAAACTATGGAAAACTTTCACAGACTGTTTTAACTGTTTACCG
ATAGCAGCCATCGTGGATGAGAAGATATTCTGCTGTCATGGAGGTTTATCACCAGATCTT
CAATCTATGGAGCAGATTCGGCGAATTATGCGACCAACTGATGTACCAGATCAAGGTCTT
CTTTGTGATCTTTTGTGGTCTGACCCCGATAAAGATGTCTTAGGCTGGGGTGAAAATGAC
AGAGGAGTGTCCTTCACATTTGGTGCAGAAGTGGTTGCAAAATTTCTCCATAAGCATGAT
TTGGATCTTATATGTAGAGCCCATCAGGTGGTTGAAGATGGATATGAATTTTTTGCAAAG
AGGCAGTTGGTCACTCTGTTTTCTGCGCCCAATTATTGCGGAGAGTTTGACAATGCAGGT
GCCATGATGAGTGTGGATGAAACACTAATGTGTTCTTTTCAGATTTTAAAGCCTGCAGAG
AAAAAGAAGCCAAATGCCACGAGACCTGTAACGCCTCCAAGGGTTGCATCAGGCCTGAAC
CCGTCCATTCAGAAAGCTTCAAATTATAGAAACAATACTGTTCTATACGAGTGA
Chromosome Location
12
Locus
12q24.1-q24.2
External Identifiers
ResourceLink
UniProtKB IDP36873
UniProtKB Entry NamePP1G_HUMAN
GenBank Protein ID402778
GenBank Gene IDX74008
GenAtlas IDPPP1CC
HGNC IDHGNC:9283
General References
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  3. Norman SA, Mott DM: Molecular cloning and chromosomal localization of a human skeletal muscle PP-1 gamma 1 cDNA. Mamm Genome. 1994 Jan;5(1):41-5. [Article]
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  5. Armstrong CG, Browne GJ, Cohen P, Cohen PT: PPP1R6, a novel member of the family of glycogen-targetting subunits of protein phosphatase 1. FEBS Lett. 1997 Nov 24;418(1-2):210-4. [Article]
  6. Trinkle-Mulcahy L, Sleeman JE, Lamond AI: Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells. J Cell Sci. 2001 Dec;114(Pt 23):4219-28. [Article]
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  9. Trinkle-Mulcahy L, Andrews PD, Wickramasinghe S, Sleeman J, Prescott A, Lam YW, Lyon C, Swedlow JR, Lamond AI: Time-lapse imaging reveals dynamic relocalization of PP1gamma throughout the mammalian cell cycle. Mol Biol Cell. 2003 Jan;14(1):107-17. [Article]
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  13. Mi J, Guo C, Brautigan DL, Larner JM: Protein phosphatase-1alpha regulates centrosome splitting through Nek2. Cancer Res. 2007 Feb 1;67(3):1082-9. [Article]
  14. Djouder N, Metzler SC, Schmidt A, Wirbelauer C, Gstaiger M, Aebersold R, Hess D, Krek W: S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling. Mol Cell. 2007 Oct 12;28(1):28-40. [Article]
  15. Gunawardena SR, Ruis BL, Meyer JA, Kapoor M, Conklin KF: NOM1 targets protein phosphatase I to the nucleolus. J Biol Chem. 2008 Jan 4;283(1):398-404. Epub 2007 Oct 26. [Article]
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  18. Lee JH, You J, Dobrota E, Skalnik DG: Identification and characterization of a novel human PP1 phosphatase complex. J Biol Chem. 2010 Aug 6;285(32):24466-76. doi: 10.1074/jbc.M110.109801. Epub 2010 Jun 1. [Article]
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  20. Schmutz I, Wendt S, Schnell A, Kramer A, Mansuy IM, Albrecht U: Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock. PLoS One. 2011;6(6):e21325. doi: 10.1371/journal.pone.0021325. Epub 2011 Jun 21. [Article]
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  22. Nie H, Zheng Y, Li R, Guo TB, He D, Fang L, Liu X, Xiao L, Chen X, Wan B, Chin YE, Zhang JZ: Phosphorylation of FOXP3 controls regulatory T cell function and is inhibited by TNF-alpha in rheumatoid arthritis. Nat Med. 2013 Mar;19(3):322-8. doi: 10.1038/nm.3085. Epub 2013 Feb 10. [Article]
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  25. Egloff MP, Cohen PT, Reinemer P, Barford D: Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J Mol Biol. 1995 Dec 15;254(5):942-59. [Article]
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  27. Maynes JT, Perreault KR, Cherney MM, Luu HA, James MN, Holmes CF: Crystal structure and mutagenesis of a protein phosphatase-1:calcineurin hybrid elucidate the role of the beta12-beta13 loop in inhibitor binding. J Biol Chem. 2004 Oct 8;279(41):43198-206. Epub 2004 Jul 26. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB021699,10-Deepithio-9,10-DidehydroacanthifolicinexperimentalunknownDetails
DB02860Calyculin AexperimentalunknownDetails
DB04738MotuporinexperimentalunknownDetails