PPP2R2A

Protein phosphatase 2, regulatory subunit B, alpha
Identifiers
Symbols PPP2R2A; B55A; B55ALPHA; DKFZp686N05117; FLJ26613; FLJ41727; MGC52248; PR52A; PR55A
External IDs OMIM604941 MGI1919228 HomoloGene2035 GeneCards: PPP2R2A Gene
EC number 3.1.3.16
Orthologs
Species Human Mouse
Entrez 5520 71978
Ensembl ENSG00000221914 ENSMUSG00000022052
UniProt P63151 Q3TPC5
RefSeq (mRNA) NM_001177591.1 XM_001003559
RefSeq (protein) NP_001171062.1 XP_001003559
Location (UCSC) Chr 8:
26.15 – 26.23 Mb
Chr 14:
67.63 – 67.69 Mb
PubMed search [1] [2]

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] 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". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5520. 
  3. ^ a b 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. ^ a b 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1223084. 
  5. ^ a b 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2621004. 
  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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=109244. 
  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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16350. 
  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. 

Further reading