PPP2R2A

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PPP2R2A
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases PPP2R2A, B55A, B55ALPHA, PR52A, PR55A, protein phosphatase 2 regulatory subunit Balpha
External IDs MGI: 1919228 HomoloGene: 2035 GeneCards: PPP2R2A
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001177591
NM_002717

NM_001205188
NM_028032

RefSeq (protein)

NP_001171062
NP_002708

NP_001192117.1
NP_082308.1
NP_001192117
NP_082308

Location (UCSC) Chr 8: 26.29 – 26.37 Mb Chr 14: 67.01 – 67.07 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform is an enzyme that in humans is encoded by the PPP2R2A gene.[3]

Function[edit]

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.[4]

Interactions[edit]

PPP2R2A has been shown to interact with:

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Mayer RE, Hendrix P, Cron P, Matthies R, Stone SR, Goris J, Merlevede W, Hofsteenge J, Hemmings BA (Apr 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. 
  4. ^ "Entrez Gene: PPP2R2A protein phosphatase 2 (formerly 2A), regulatory subunit B, alpha isoform". 
  5. ^ Peterson RT, Desai BN, Hardwick JS, Schreiber SL (Apr 1999). "Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycinassociated protein". Proceedings of the National Academy of Sciences of the United States of America. 96 (8): 4438–42. doi:10.1073/pnas.96.8.4438. PMC 16350Freely accessible. PMID 10200280. 
  6. ^ Bishop JD, Nien WL, Dauphinee SM, Too CK (Aug 2006). "Prolactin activates mammalian target-of-rapamycin through phosphatidylinositol 3-kinase and stimulates phosphorylation of p70S6K and 4E-binding protein-1 in lymphoma cells". The Journal of Endocrinology. 190 (2): 307–12. doi:10.1677/joe.1.06368. PMID 16899564. 
  7. ^ a b 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. PMID 1328247. 
  8. ^ a b 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 2621004Freely accessible. PMID 18782753. 
  9. ^ a b 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 1223084Freely accessible. PMID 12370081. 
  10. ^ Griswold-Prenner I, Kamibayashi C, Maruoka EM, Mumby MC, Derynck R (Nov 1998). "Physical and functional interactions between type I transforming growth factor beta receptors and Balpha, a WD-40 repeat subunit of phosphatase 2A". Molecular and Cellular Biology. 18 (11): 6595–604. doi:10.1128/mcb.18.11.6595. PMC 109244Freely accessible. PMID 9774674. 
  11. ^ Jayadeva G, Kurimchak A, Garriga J, Sotillo E, Davis AJ, Haines DS, Mumby M, Graña X (Sep 2010). "B55alpha PP2A holoenzymes modulate the phosphorylation status of the retinoblastoma-related protein p107 and its activation". The Journal of Biological Chemistry. 285 (39): 29863–73. doi:10.1074/jbc.M110.162354. PMC 2943288Freely accessible. PMID 20663872. 

Further reading[edit]