PPP1CC

Protein-coding gene in the species Homo sapiens
PPP1CC
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1IT6, 1JK7, 1U32, 2BCD, 2BDX, 4UT2, 4UT3

Identifiers
AliasesPPP1CC, PP-1G, PP1C, PPP1G, protein phosphatase 1 catalytic subunit gamma
External IDsOMIM: 176914; MGI: 3647492; HomoloGene: 100608; GeneCards: PPP1CC; OMA:PPP1CC - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for PPP1CC
Genomic location for PPP1CC
Band12q24.11Start110,719,680 bp[1]
End110,742,939 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for PPP1CC
Genomic location for PPP1CC
Band7|7 F2Start122,158,278 bp[2]
End122,175,273 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • jejunal mucosa

  • right ventricle

  • parotid gland

  • Skeletal muscle tissue of biceps brachii

  • secondary oocyte

  • superficial temporal artery

  • duodenum

  • male germ cell

  • skin of hip

  • sperm
Top expressed in
  • neural layer of retina

  • spermatocyte

  • spermatid

  • genital tubercle

  • epiblast

  • tail of embryo

  • olfactory bulb

  • ventricular zone

  • ganglionic eminence

  • thymus
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • phosphoprotein phosphatase activity
  • protein domain specific binding
  • protein N-terminus binding
  • phosphatase activity
  • protein-containing complex binding
  • protein serine/threonine phosphatase activity
  • metal ion binding
  • protein phosphatase 1 binding
  • protein C-terminus binding
  • protein binding
  • protein phosphatase binding
  • hydrolase activity
  • protein kinase binding
  • lamin binding
  • RNA binding
Cellular component
  • cytoplasm
  • cytosol
  • nuclear speck
  • focal adhesion
  • dendritic spine
  • chromosome
  • nucleoplasm
  • mitochondrial outer membrane
  • midbody
  • PTW/PP1 phosphatase complex
  • nucleolus
  • mitochondrion
  • cleavage furrow
  • chromosome, centromeric region
  • nucleus
  • kinetochore
  • protein phosphatase type 1 complex
  • protein-containing 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
SpeciesHumanMouse
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 MbChr 5: 122.16 – 122.18 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

Interactions

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

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000186298 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b Wu DY, 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. 277 (31). United States: 27706–15. doi:10.1074/jbc.M200955200. ISSN 0021-9258. PMID 12016208.
  7. ^ Connor JH, 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. 21 (20). United States: 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. 385 (6615). ENGLAND: 454–8. Bibcode:1997Natur.385..454K. doi:10.1038/385454a0. ISSN 0028-0836. PMID 9009195. S2CID 608633.
  9. ^ Hsieh-Wilson LC, 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. 38 (14). UNITED STATES: 4365–73. doi:10.1021/bi982900m. ISSN 0006-2960. PMID 10194355.
  10. ^ Smith FD, 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. 274 (28). UNITED STATES: 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. S2CID 42021604.
  • 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. S2CID 21566111.
  • 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. S2CID 3010008.
  • 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. S2CID 21169749.
  • 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. Bibcode:2002CBio...12....1A. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
  • 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.
  • v
  • t
  • e
  • 1fjm: PROTEIN SERINE/THREONINE PHOSPHATASE-1 (ALPHA ISOFORM, TYPE I) COMPLEXED WITH MICROCYSTIN-LR TOXIN
    1fjm: PROTEIN SERINE/THREONINE PHOSPHATASE-1 (ALPHA ISOFORM, TYPE I) COMPLEXED WITH MICROCYSTIN-LR TOXIN
  • 1it6: CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CALYCULIN A AND THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASE 1
    1it6: CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CALYCULIN A AND THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASE 1
  • 1jk7: CRYSTAL STRUCTURE OF THE TUMOR-PROMOTER OKADAIC ACID BOUND TO PROTEIN PHOSPHATASE-1
    1jk7: CRYSTAL STRUCTURE OF THE TUMOR-PROMOTER OKADAIC ACID BOUND TO PROTEIN PHOSPHATASE-1
  • 1u32: Crystal structure of a Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid
    1u32: Crystal structure of a Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid
  • 2bcd: X-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin bound
    2bcd: X-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin bound
  • 2bdx: X-ray Crystal Structure of dihydromicrocystin-LA bound to Protein Phosphatase-1
    2bdx: X-ray Crystal Structure of dihydromicrocystin-LA bound to Protein Phosphatase-1
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