PPP1CC

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit is an enzyme that in humans is encoded by the PPP1CC gene.[5]

PPP1CC
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1IT6, 1JK7, 1U32, 2BCD, 2BDX, 4UT2, 4UT3
Identifiers
Aliases	PPP1CC, PP-1G, PP1C, PPP1G, protein phosphatase 1 catalytic subunit gamma
External IDs	OMIM: 176914 MGI: 3647492 HomoloGene: 100608 GeneCards: PPP1CC
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q24.11 Start 110,719,680 bp[1] End 110,742,939 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 7|7 F2 Start 122,158,278 bp[2] End 122,175,273 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • phosphoprotein phosphatase activity • protein domain specific binding • protein N-terminus binding • phosphatase activity • GO:0032403 macromolecular complex binding • protein serine/threonine phosphatase activity • metal ion binding • protein phosphatase 1 binding • protein C-terminus binding • GO:0001948 protein binding • protein phosphatase binding • hydrolase activity • protein kinase binding • lamin binding • RNA binding Cellular component • cytoplasm • condensed chromosome kinetochore • cytosol • nuclear speck • focal adhesion • dendritic spine • chromosome • nucleoplasm • mitochondrial outer membrane • midbody • PTW/PP1 phosphatase complex • nucleolus • mitochondrion • cleavage furrow • chromosome, centromeric region • cell nucleus • kinetochore • nuclear chromosome, telomeric region • protein phosphatase type 1 complex • macromolecular complex • presynapse • postsynapse • glutamatergic synapse Biological process • regulation of nucleocytoplasmic transport • rhythmic process • protein dephosphorylation • circadian regulation of gene expression • cell division • regulation of circadian rhythm • neuron differentiation • glycogen metabolic process • cell cycle • entrainment of circadian clock by photoperiod • sister chromatid cohesion • carbohydrate metabolic process • positive regulation of glial cell proliferation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5501	434233
Ensembl	ENSG00000186298	ENSMUSG00000004455
UniProt	P36873	P63087
RefSeq (mRNA)	NM_001244974 NM_002710	XM_006508415
RefSeq (protein)	NP_001231903 NP_002701	NP_038664
Location (UCSC)	Chr 12: 110.72 – 110.74 Mb	Chr 5: 122.16 – 122.18 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

PPP1CC has been shown to interact with PPP1R15A,[6][7] SMARCB1,[6] TLX1[8] and PPP1R9B.[9][10]

References

1. GRCh38: Ensembl release 89: ENSG00000186298 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000004455 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: PPP1CC Protein phosphatase 1, catalytic subunit, gamma isoform".
6. Wu, Daniel Y; Tkachuck Douglas C; Roberson Rachel S; Schubach William H (Aug 2002). "The human SNF5/INI1 protein facilitates the function of the growth arrest and DNA damage-inducible protein (GADD34) and modulates GADD34-bound protein phosphatase-1 activity". J. Biol. Chem. United States. 277 (31): 27706–15. doi:10.1074/jbc.M200955200. ISSN 0021-9258. PMID 12016208.
7. Connor, J H; Weiser D C; Li S; Hallenbeck J M; Shenolikar S (Oct 2001). "Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1". Mol. Cell. Biol. United States. 21 (20): 6841–50. doi:10.1128/MCB.21.20.6841-6850.2001. ISSN 0270-7306. PMC 99861. PMID 11564868.
8. Kawabe, T; Muslin A J; Korsmeyer S J (Jan 1997). "HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint". Nature. ENGLAND. 385 (6615): 454–8. Bibcode:1997Natur.385..454K. doi:10.1038/385454a0. ISSN 0028-0836. PMID 9009195.
9. Hsieh-Wilson, L C; Allen P B; Watanabe T; Nairn A C; Greengard P (Apr 1999). "Characterization of the neuronal targeting protein spinophilin and its interactions with protein phosphatase-1". Biochemistry. UNITED STATES. 38 (14): 4365–73. doi:10.1021/bi982900m. ISSN 0006-2960. PMID 10194355.
10. Smith, F D; Oxford G S; Milgram S L (Jul 1999). "Association of the D2 dopamine receptor third cytoplasmic loop with spinophilin, a protein phosphatase-1-interacting protein". J. Biol. Chem. UNITED STATES. 274 (28): 19894–900. doi:10.1074/jbc.274.28.19894. ISSN 0021-9258. PMID 10391935.

Further reading

• Van Eynde A, Wera S, Beullens M, et al. (1996). "Molecular cloning of NIPP-1, a nuclear inhibitor of protein phosphatase-1, reveals homology with polypeptides involved in RNA processing". J. Biol. Chem. 270 (47): 28068–74. doi:10.1074/jbc.270.47.28068. PMID 7499293.
• Egloff MP, Cohen PT, Reinemer P, Barford D (1996). "Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate". J. Mol. Biol. 254 (5): 942–59. doi:10.1006/jmbi.1995.0667. PMID 7500362.
• MacKintosh RW, Dalby KN, Campbell DG, et al. (1995). "The cyanobacterial toxin microcystin binds covalently to cysteine-273 on protein phosphatase 1". FEBS Lett. 371 (3): 236–40. doi:10.1016/0014-5793(95)00888-G. PMID 7556599.
• Norman SA, Mott DM (1994). "Molecular cloning and chromosomal localization of a human skeletal muscle PP-1 gamma 1 cDNA". Mamm. Genome. 5 (1): 41–5. doi:10.1007/BF00360567. PMID 8111128.
• Barker HM, Craig SP, Spurr NK, Cohen PT (1993). "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. 1178 (2): 228–33. doi:10.1016/0167-4889(93)90014-G. PMID 8394140.
• Helps NR, Barker HM, Elledge SJ, Cohen PT (1996). "Protein phosphatase 1 interacts with p53BP2, a protein which binds to the tumour suppressor p53". FEBS Lett. 377 (3): 295–300. doi:10.1016/0014-5793(95)01347-4. PMID 8549741.
• Saadat M, Nomoto K, Mizuno Y, et al. (1996). "Assignment of the gene encoding type 1 gamma protein phosphatase catalytic subunit (PPP1CC) on human, rat, and mouse chromosomes". Jpn. J. Hum. Genet. 41 (1): 159–65. doi:10.1007/BF01892623. PMID 8914631.
• Armstrong CG, Browne GJ, Cohen P, Cohen PT (1998). "PPP1R6, a novel member of the family of glycogen-targeting subunits of protein phosphatase 1". FEBS Lett. 418 (1–2): 210–4. doi:10.1016/S0014-5793(97)01385-9. PMID 9414128.
• Andreassen PR, Lacroix FB, Villa-Moruzzi E, Margolis RL (1998). "Differential subcellular localization of protein phosphatase-1 alpha, gamma1, and delta isoforms during both interphase and mitosis in mammalian cells". J. Cell Biol. 141 (5): 1207–15. doi:10.1083/jcb.141.5.1207. PMC 2137188. PMID 9606212.
• Ajuh PM, Browne GJ, Hawkes NA, et al. (2000). "Association of a protein phosphatase 1 activity with the human factor C1 (HCF) complex". Nucleic Acids Res. 28 (3): 678–86. doi:10.1093/nar/28.3.678. PMC 102561. PMID 10637318.
• Yang J, Hurley TD, DePaoli-Roach AA (2000). "Interaction of inhibitor-2 with the catalytic subunit of type 1 protein phosphatase. Identification of a sequence analogous to the consensus type 1 protein phosphatase-binding motif". J. Biol. Chem. 275 (30): 22635–44. doi:10.1074/jbc.M003082200. PMID 10807923.
• Katayama H, Zhou H, Li Q, et al. (2002). "Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle". J. Biol. Chem. 276 (49): 46219–24. doi:10.1074/jbc.M107540200. PMID 11551964.
• Patel KG, Liu C, Cameron PL, Cameron RS (2001). "Myr 8, a novel unconventional myosin expressed during brain development associates with the protein phosphatase catalytic subunits 1alpha and 1gamma1". J. Neurosci. 21 (20): 7954–68. doi:10.1523/JNEUROSCI.21-20-07954.2001. PMC 6763852. PMID 11588169.
• Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
• Jones JA, Hannun YA (2002). "Tight binding inhibition of protein phosphatase-1 by phosphatidic acid. Specificity of inhibition by the phospholipid". J. Biol. Chem. 277 (18): 15530–8. doi:10.1074/jbc.M111555200. PMID 11856740.
• Wu DY, Tkachuck DC, Roberson RS, Schubach WH (2002). "The human SNF5/INI1 protein facilitates the function of the growth arrest and DNA damage-inducible protein (GADD34) and modulates GADD34-bound protein phosphatase-1 activity". J. Biol. Chem. 277 (31): 27706–15. doi:10.1074/jbc.M200955200. PMID 12016208.
• Bharucha DC, Zhou M, Nekhai S, et al. (2002). "A protein phosphatase from human T cells augments tat transactivation of the human immunodeficiency virus type 1 long-terminal repeat". Virology. 296 (1): 6–16. doi:10.1006/viro.2002.1438. PMID 12036313.
• Tan SL, Tareen SU, Melville MW, et al. (2002). "The direct binding of the catalytic subunit of protein phosphatase 1 to the PKR protein kinase is necessary but not sufficient for inactivation and disruption of enzyme dimer formation". J. Biol. Chem. 277 (39): 36109–17. doi:10.1074/jbc.M205109200. PMID 12138106.
• Eto M, Elliott E, Prickett TD, Brautigan DL (2003). "Inhibitor-2 regulates protein phosphatase-1 complexed with NimA-related kinase to induce centrosome separation". J. Biol. Chem. 277 (46): 44013–20. doi:10.1074/jbc.M208035200. PMID 12221103.
• Ceulemans H, Vulsteke V, De Maeyer M, et al. (2003). "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. 277 (49): 47331–7. doi:10.1074/jbc.M206838200. PMID 12226088.