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Identification
HMDB Protein ID HMDBP01893
Secondary Accession Numbers
  • 7293
Name Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Synonyms
  1. PP-1G
  2. Protein phosphatase 1C catalytic subunit
Gene Name PPP1CC
Protein Type Unknown
Biological Properties
General Function Involved in hydrolase 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.
Pathways
  • Alcoholism
  • Amphetamine addiction
  • Dopaminergic synapse
  • Focal adhesion
  • Herpes simplex infection
  • Hippo signaling pathway
  • Insulin signaling pathway
  • Long-term potentiation
  • mRNA surveillance pathway
  • Oocyte meiosis
  • Proteoglycans in cancer
  • Regulation of actin cytoskeleton
  • Vascular smooth muscle contraction
Reactions
A phosphoprotein + Water → a protein + Phosphate details
GO Classification
Biological Process
small molecule metabolic process
cell division
glycogen metabolic process
mitotic prometaphase
triglyceride catabolic process
negative regulation of transforming growth factor beta receptor signaling pathway
transforming growth factor beta receptor signaling pathway
regulation of nucleocytoplasmic transport
protein dephosphorylation
Cellular Component
cytosol
mitochondrion
nucleolus
nuclear speck
cleavage furrow
condensed chromosome kinetochore
mitochondrial outer membrane
PTW/PP1 phosphatase complex
midbody
MLL5-L complex
Function
catalytic activity
hydrolase activity
Molecular Function
protein serine/threonine phosphatase activity
metal ion binding
Cellular Location
  1. Nucleus
  2. Nucleus
  3. Nucleus
  4. Cytoplasm
  5. nucleolus
  6. Nucleus speckle
  7. Chromosome
  8. centromere
  9. nucleoplasm
  10. kinetochore
  11. Cleavage furrow
  12. Midbody
Gene Properties
Chromosome Location 12
Locus 12q24.1-q24.2
SNPs PPP1CC
Gene Sequence
>972 bp
ATGGCGGATTTAGATAAACTCAACATCGACAGCATTATCCAACGGCTGCTGGAAGTGAGA
GGGTCCAAGCCTGGTAAGAATGTCCAGCTTCAGGAGAATGAAATCAGAGGACTGTGCTTA
AAGTCTCGTGAAATCTTTCTCAGTCAGCCTATCCTACTAGAACTTGAAGCACCACTCAAA
ATATGTGGTGACATCCATGGACAATACTATGATTTGCTGCGACTTTTTGAGTACGGTGGT
TTCCCACCAGAAAGCAACTACCTGTTTCTTGGGGACTATGTGGACAGGGGAAAGCAGTCA
TTGGAGACGATCTGCCTCTTACTGGCCTACAAAATAAAATATCCTGAGAATTTTTTTCTT
CTCAGAGGGAACCATGAATGTGCCAGCATCAACAGAATTTATGGATTTTATGATGAATGT
AAAAGAAGATACAACATTAAACTATGGAAAACTTTCACAGACTGTTTTAACTGTTTACCG
ATAGCAGCCATCGTGGATGAGAAGATATTCTGCTGTCATGGAGGTTTATCACCAGATCTT
CAATCTATGGAGCAGATTCGGCGAATTATGCGACCAACTGATGTACCAGATCAAGGTCTT
CTTTGTGATCTTTTGTGGTCTGACCCCGATAAAGATGTCTTAGGCTGGGGTGAAAATGAC
AGAGGAGTGTCCTTCACATTTGGTGCAGAAGTGGTTGCAAAATTTCTCCATAAGCATGAT
TTGGATCTTATATGTAGAGCCCATCAGGTGGTTGAAGATGGATATGAATTTTTTGCAAAG
AGGCAGTTGGTCACTCTGTTTTCTGCGCCCAATTATTGCGGAGAGTTTGACAATGCAGGT
GCCATGATGAGTGTGGATGAAACACTAATGTGTTCTTTTCAGATTTTAAAGCCTGCAGAG
AAAAAGAAGCCAAATGCCACGAGACCTGTAACGCCTCCAAGGGGTATGATCACAAAGCAA
GCAAAGAAATAG
Protein Properties
Number of Residues 323
Molecular Weight 38517.92
Theoretical pI 6.121
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
MADLDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAE
KKKPNATRPVTPPRGMITKQAKK
GenBank ID Protein 402778
UniProtKB/Swiss-Prot ID P36873
UniProtKB/Swiss-Prot Entry Name PP1G_HUMAN
PDB IDs
GenBank Gene ID X74008
GeneCard ID PPP1CC
GenAtlas ID PPP1CC
HGNC ID HGNC:9283
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  5. Fujiki R, Chikanishi T, Hashiba W, Ito H, Takada I, Roeder RG, Kitagawa H, Kato S: GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis. Nature. 2009 May 21;459(7245):455-9. doi: 10.1038/nature07954. Epub 2009 Apr 19. [PubMed:19377461 ]
  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. [PubMed:11739654 ]
  7. Connor JH, Weiser DC, Li S, Hallenbeck JM, Shenolikar S: Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1. Mol Cell Biol. 2001 Oct;21(20):6841-50. [PubMed:11564868 ]
  8. Ceulemans H, Vulsteke V, De Maeyer M, Tatchell K, Stalmans W, Bollen M: Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1. J Biol Chem. 2002 Dec 6;277(49):47331-7. Epub 2002 Sep 10. [PubMed:12226088 ]
  9. Boyce M, Bryant KF, Jousse C, Long K, Harding HP, Scheuner D, Kaufman RJ, Ma D, Coen DM, Ron D, Yuan J: A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress. Science. 2005 Feb 11;307(5711):935-9. [PubMed:15705855 ]
  10. 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. [PubMed:9414128 ]
  11. Barker HM, Craig SP, Spurr NK, Cohen PT: Sequence of human protein serine/threonine phosphatase 1 gamma and localization of the gene (PPP1CC) encoding it to chromosome bands 12q24.1-q24.2. Biochim Biophys Acta. 1993 Aug 18;1178(2):228-33. [PubMed:8394140 ]
  12. 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. [PubMed:8111128 ]
  13. MacKintosh RW, Dalby KN, Campbell DG, Cohen PT, Cohen P, MacKintosh C: The cyanobacterial toxin microcystin binds covalently to cysteine-273 on protein phosphatase 1. FEBS Lett. 1995 Sep 11;371(3):236-40. [PubMed:7556599 ]
  14. 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. [PubMed:12529430 ]
  15. Trinkle-Mulcahy L, Andersen J, Lam YW, Moorhead G, Mann M, Lamond AI: Repo-Man recruits PP1 gamma to chromatin and is essential for cell viability. J Cell Biol. 2006 Feb 27;172(5):679-92. Epub 2006 Feb 21. [PubMed:16492807 ]
  16. 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. [PubMed:17965019 ]
  17. 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. [PubMed:7500362 ]