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PPP2CA

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Enzyme
PPP2CA
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2IAE, 2IE3, 2IE4, 2NPP, 2NYL, 2NYM, 3C5W, 3DW8, 3FGA, 3K7V, 3K7W, 3P71, 4I5L, 4I5N, 4IYP, 4LAC

Identifiers
AliasesPPP2CA, PP2Ac, PP2CA, PP2Calpha, RP-C, protein phosphatase 2 catalytic subunit alpha, NEDLBA
External IDsOMIM: 176915; MGI: 1321159; HomoloGene: 37660; GeneCards: PPP2CA; OMA:PPP2CA - orthologs
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)
Chromosome 5 (human)Genomic location for PPP2CAGenomic location for PPP2CA
Band5q31.1Start134,194,332 bp
End134,226,073 bp
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)
Chromosome 11 (mouse)Genomic location for PPP2CAGenomic location for PPP2CA
Band11|11 B1.3Start51,989,508 bp
End52,018,605 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • lateral nuclear group of thalamus

  • ventricular zone

  • ganglionic eminence

  • stromal cell of endometrium

  • Skeletal muscle tissue of rectus abdominis

  • postcentral gyrus

  • prefrontal cortex

  • pars compacta

  • Pons

  • right ventricle
Top expressed in
  • medial ganglionic eminence

  • molar

  • nucleus accumbens

  • substantia nigra

  • endocardial cushion

  • barrel cortex

  • atrioventricular valve

  • dorsal striatum

  • abdominal wall

  • human fetus
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5515

19052

Ensembl

ENSG00000113575

ENSMUSG00000020349

UniProt

P67775

P63330

RefSeq (mRNA)

NM_002715
NM_001355019

NM_019411

RefSeq (protein)

NP_002706
NP_001341948

NP_062284

Location (UCSC)Chr 5: 134.19 – 134.23 MbChr 11: 51.99 – 52.02 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform is an enzyme that (in humans) is encoded by the PPP2CA gene.

Function

This gene encodes the phosphatase 2A catalytic subunit. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. This gene encodes an alpha isoform of the catalytic subunit.

Interactions

PPP2CA has been shown to interact with:

See also

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000113575Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000020349Ensembl, 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. Jones TA, Barker HM, da Cruz e Silva EF, Mayer-Jaekel RE, Hemmings BA, Spurr NK, Sheer D, Cohen PT (April 1993). "Localization of the genes encoding the catalytic subunits of protein phosphatase 2A to human chromosome bands 5q23-->q31 and 8p12-->p11.2, respectively". Cytogenetics and Cell Genetics. 63 (1): 35–41. doi:10.1159/000133497. PMID 8383590.
  6. "Entrez Gene: PPP2CA protein phosphatase 2 (formerly 2A), catalytic subunit, alpha isoform".
  7. Deng X, Ito T, Carr B, Mumby M, May WS (Dec 1998). "Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A". The Journal of Biological Chemistry. 273 (51): 34157–63. doi:10.1074/jbc.273.51.34157. PMID 9852076.
  8. Marmorstein LY, McLaughlin PJ, Stanton JB, Yan L, Crabb JW, Marmorstein AD (Aug 2002). "Bestrophin interacts physically and functionally with protein phosphatase 2A". The Journal of Biological Chemistry. 277 (34): 30591–7. doi:10.1074/jbc.M204269200. PMID 12058047.
  9. Bennin DA, Don AS, Brake T, McKenzie JL, Rosenbaum H, Ortiz L, DePaoli-Roach AA, Horne MC (Jul 2002). "Cyclin G2 associates with protein phosphatase 2A catalytic and regulatory B' subunits in active complexes and induces nuclear aberrations and a G1/S phase cell cycle arrest". The Journal of Biological Chemistry. 277 (30): 27449–67. doi:10.1074/jbc.M111693200. PMID 11956189.
  10. ^ Goudreault M, D'Ambrosio LM, Kean MJ, Mullin MJ, Larsen BG, Sanchez A, Chaudhry S, Chen GI, Sicheri F, Nesvizhskii AI, Aebersold R, Raught B, Gingras AC (Jan 2009). "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein". Molecular & Cellular Proteomics. 8 (1): 157–71. doi:10.1074/mcp.M800266-MCP200. PMC 2621004. PMID 18782753.
  11. ^ Cheng A, Kaldis P, Solomon MJ (Nov 2000). "Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C alpha and beta 2 isoforms". The Journal of Biological Chemistry. 275 (44): 34744–9. doi:10.1074/jbc.M006210200. PMID 10934208.
  12. Gingras AC, Caballero M, Zarske M, Sanchez A, Hazbun TR, Fields S, Sonenberg N, Hafen E, Raught B, Aebersold R (Nov 2005). "A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity". Molecular & Cellular Proteomics. 4 (11): 1725–40. doi:10.1074/mcp.M500231-MCP200. PMID 16085932.
  13. Chen J, Peterson RT, Schreiber SL (Jun 1998). "Alpha 4 associates with protein phosphatases 2A, 4, and 6". Biochemical and Biophysical Research Communications. 247 (3): 827–32. doi:10.1006/bbrc.1998.8792. PMID 9647778.
  14. Chung H, Nairn AC, Murata K, Brautigan DL (Aug 1999). "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the alpha 4 subunit which promotes dephosphorylation of elongation factor-2". Biochemistry. 38 (32): 10371–6. doi:10.1021/bi990902g. PMID 10441131.
  15. ^ Zhou J, Pham HT, Ruediger R, Walter G (Jan 2003). "Characterization of the Aalpha and Abeta subunit isoforms of protein phosphatase 2A: differences in expression, subunit interaction, and evolution". The Biochemical Journal. 369 (Pt 2): 387–98. doi:10.1042/BJ20021244. PMC 1223084. PMID 12370081.
  16. Kamibayashi C, Lickteig RL, Estes R, Walter G, Mumby MC (Oct 1992). "Expression of the A subunit of protein phosphatase 2A and characterization of its interactions with the catalytic and regulatory subunits". The Journal of Biological Chemistry. 267 (30): 21864–72. doi:10.1016/S0021-9258(19)36692-X. PMID 1328247.
  17. Yan Z, Fedorov SA, Mumby MC, Williams RS (Feb 2000). "PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with Cdc6 and modulates DNA replication in human cells". Molecular and Cellular Biology. 20 (3): 1021–9. doi:10.1128/mcb.20.3.1021-1029.2000. PMC 85219. PMID 10629059.
  18. ^ McCright B, Rivers AM, Audlin S, Virshup DM (Sep 1996). "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm". The Journal of Biological Chemistry. 271 (36): 22081–9. doi:10.1074/jbc.271.36.22081. PMID 8703017.
  19. Ito A, Kataoka TR, Watanabe M, Nishiyama K, Mazaki Y, Sabe H, Kitamura Y, Nojima H (Feb 2000). "A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation". The EMBO Journal. 19 (4): 562–71. doi:10.1093/emboj/19.4.562. PMC 305594. PMID 10675325.
  20. Kawabe T, Muslin AJ, Korsmeyer SJ (Jan 1997). "HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint". Nature. 385 (6615): 454–8. Bibcode:1997Natur.385..454K. doi:10.1038/385454a0. PMID 9009195. S2CID 608633.

Further reading

PDB gallery
  • 2iae: Crystal structure of a protein phosphatase 2A (PP2A) holoenzyme. 2iae: Crystal structure of a protein phosphatase 2A (PP2A) holoenzyme.
  • 2ie3: Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor-inducing Toxins 2ie3: Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor-inducing Toxins
  • 2ie4: Structure of the Protein Phosphatase 2A Core Enzyme Bound to okadaic acid 2ie4: Structure of the Protein Phosphatase 2A Core Enzyme Bound to okadaic acid
  • 2npp: Structure of the Protein Phosphatase 2A Holoenzyme 2npp: Structure of the Protein Phosphatase 2A Holoenzyme
  • 2nyl: Crystal structure of Protein Phosphatase 2A (PP2A) holoenzyme with the catalytic subunit carboxyl terminus truncated 2nyl: Crystal structure of Protein Phosphatase 2A (PP2A) holoenzyme with the catalytic subunit carboxyl terminus truncated
  • 2nym: Crystal Structure of Protein Phosphatase 2A (PP2A) with C-terminus truncated catalytic subunit 2nym: Crystal Structure of Protein Phosphatase 2A (PP2A) with C-terminus truncated catalytic subunit
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