PPP2R2A

Protein phosphatase 2, regulatory subunit B, alpha
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsPPP2R2A ; B55A; B55ALPHA; PR52A; PR55A
External IDsOMIM: 604941 MGI: 1919228 HomoloGene: 2035 ChEMBL: 4284 GeneCards: PPP2R2A Gene
EC number3.1.3.16
Orthologs
SpeciesHumanMouse
Entrez552071978
EnsemblENSG00000221914ENSMUSG00000022052
UniProtP63151Q6P1F6
RefSeq (mRNA)NM_001177591NM_001205188
RefSeq (protein)NP_001171062NP_001192117
Location (UCSC)Chr 8:
26.15 – 26.23 Mb
Chr 14:
67.01 – 67.07 Mb
PubMed search

Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform is an enzyme that in humans is encoded by the PPP2R2A gene.[1]

The product of this gene belongs to the phosphatase 2 regulatory subunit B family. Protein phosphatase 2 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. The B regulatory subunit might modulate substrate selectivity and catalytic activity. This gene encodes an alpha isoform of the regulatory subunit B55 subfamily.[2]

==Interactions==

PPP2R2A has been shown to interact with PPP2R1B,[3][4] PPP2R1A,[4][5] TGF beta receptor 1,[6] P70-S6 Kinase 1[7][8] p107[9] and PPP2CA.[3][5]

References

  1. Mayer RE, Hendrix P, Cron P, Matthies R, Stone SR, Goris J, Merlevede W, Hofsteenge J, Hemmings BA (May 1991). "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoform". Biochemistry 30 (15): 3589–97. doi:10.1021/bi00229a001. PMID 1849734.
  2. "Entrez Gene: PPP2R2A protein phosphatase 2 (formerly 2A), regulatory subunit B, alpha isoform".
  3. 3.0 3.1 Kamibayashi, C; Lickteig R L; Estes R; Walter G; Mumby M C (October 1992). "Expression of the A subunit of protein phosphatase 2A and characterization of its interactions with the catalytic and regulatory subunits". J. Biol. Chem. (UNITED STATES) 267 (30): 21864–72. ISSN 0021-9258. PMID 1328247.
  4. 4.0 4.1 Zhou, Jin; Pham Huong T; Ruediger Ralf; Walter Gernot (January 2003). "Characterization of the Aalpha and Abeta subunit isoforms of protein phosphatase 2A: differences in expression, subunit interaction, and evolution". Biochem. J. (England) 369 (Pt 2): 387–98. doi:10.1042/BJ20021244. ISSN 0264-6021. PMC 1223084. PMID 12370081.
  5. 5.0 5.1 Goudreault, Marilyn; D'Ambrosio Lisa M, Kean Michelle J, Mullin Michael J, Larsen Brett G, Sanchez Amy, Chaudhry Sidharth, Chen Ginny I, Sicheri Frank, Nesvizhskii Alexey I, Aebersold Ruedi, Raught Brian, Gingras Anne-Claude (January 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". Mol. Cell Proteomics (United States) 8 (1): 157–71. doi:10.1074/mcp.M800266-MCP200. PMC 2621004. PMID 18782753.
  6. Griswold-Prenner, I; Kamibayashi C; Maruoka E M; Mumby M C; Derynck R (November 1998). "Physical and functional interactions between type I transforming growth factor beta receptors and Balpha, a WD-40 repeat subunit of phosphatase 2A". Mol. Cell. Biol. (UNITED STATES) 18 (11): 6595–604. ISSN 0270-7306. PMC 109244. PMID 9774674.
  7. Peterson, R T; Desai B N; Hardwick J S; Schreiber S L (April 1999). "Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycinassociated protein". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (8): 4438–42. doi:10.1073/pnas.96.8.4438. ISSN 0027-8424. PMC 16350. PMID 10200280.
  8. Bishop, Jessica D; Nien Wei Lun; Dauphinee Shauna M; Too Catherine K L (August 2006). "Prolactin activates mammalian target-of-rapamycin through phosphatidylinositol 3-kinase and stimulates phosphorylation of p70S6K and 4E-binding protein-1 in lymphoma cells". J. Endocrinol. (England) 190 (2): 307–12. doi:10.1677/joe.1.06368. ISSN 0022-0795. PMID 16899564.
  9. Jayadeva, G; Kurimchak A; Garriga J; Sotillo E; Davis AJ; Haines DS; Mumby M; Graña X (Sep 24, 2010). "B55alpha PP2A holoenzymes modulate the phosphorylation status of the retinoblastoma-related protein p107 and its activation.". J Biol Chem 285 (39): 29863–73. doi:10.1074/jbc.M110.162354. PMC 2943288. PMID 20663872.

Further reading