PPP2R2A

Last updated
PPP2R2A
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases PPP2R2A , B55A, B55ALPHA, PR52A, PR55A, protein phosphatase 2 regulatory subunit Balpha, PR55alpha
External IDs OMIM: 604941 MGI: 1919228 HomoloGene: 2035 GeneCards: PPP2R2A
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001177591
NM_002717

NM_001205188
NM_028032
NM_001360033
NM_001360034

RefSeq (protein)

NP_001171062
NP_002708

NP_001192117
NP_082308
NP_001346962
NP_001346963

Location (UCSC) Chr 8: 26.29 – 26.37 Mb Chr 14: 67.25 – 67.31 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform is an enzyme regulator that in humans is encoded by the PPP2R2A gene. [5]

Contents

Function

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. [6]

Interactions

PPP2R2A has been shown to interact with:

Related Research Articles

<span class="mw-page-title-main">PPP2CA</span> Enzyme

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

<span class="mw-page-title-main">YWHAG</span> Protein-coding gene in the species Homo sapiens

14-3-3 protein gamma is a protein that in humans is encoded by the YWHAG gene.

<span class="mw-page-title-main">PPP2R1A</span> Enzyme

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform is an enzyme that in humans is encoded by the PPP2R1A gene. In the plant Arabidopsis thaliana a similar enzyme is encoded by the RCN1 gene (At1g25490).

<span class="mw-page-title-main">PPP2R2B</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform is an enzyme that in humans is encoded by the PPP2R2B gene.

<span class="mw-page-title-main">PPP2CB</span> Enzyme found in humans

Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform is an enzyme that in humans is encoded by the PPP2CB gene.

<span class="mw-page-title-main">PPP2R5A</span> Enzyme found in humans

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform is an enzyme that in humans is encoded by the PPP2R5A gene.

<span class="mw-page-title-main">PPP2R5C</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform is an enzyme that in humans is encoded by the PPP2R5C gene.

<span class="mw-page-title-main">PPP2R4</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein phosphatase 2A regulatory subunit B is an enzyme that in humans is encoded by the PPP2R4 gene.

<span class="mw-page-title-main">PPP2R1B</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform is an enzyme that in humans is encoded by the PPP2R1B gene.

<span class="mw-page-title-main">PPP2R3A</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha is an enzyme that in humans is encoded by the PPP2R3A gene. Protein phosphatase 2 is one of the four major Ser/Thr phosphatases and is implicated in the negative control of cell growth and division. Protein phosphatase 2 holoenzymes are heterotrimeric proteins composed of a structural subunit A, a catalytic subunit C, and a regulatory subunit B. The regulatory subunit is encoded by a diverse set of genes that have been grouped into the B/PR55, B'/PR61, and B''/PR72 families. These different regulatory subunits confer distinct enzymatic specificities and intracellular localizations to the holozenzyme. The product of this gene belongs to the B'' family. The B'' family has been further divided into subfamilies. The product of this gene belongs to the alpha subfamily of regulatory subunit B''. Alternative splicing results in multiple transcript variants encoding different isoforms.

<span class="mw-page-title-main">PPP2R5D</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform is an enzyme that in humans is encoded by the PPP2R5D gene. Mutations in PPP2R5D cause Jordan's Syndrome.

<span class="mw-page-title-main">PPP2R2C</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform is an enzyme that in humans is encoded by the PPP2R2C gene.

<span class="mw-page-title-main">PPP2R5B</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform is an enzyme that in humans is encoded by the PPP2R5B gene.

<span class="mw-page-title-main">PPP2R5E</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform is an enzyme that in humans is encoded by the PPP2R5E gene.

<span class="mw-page-title-main">STK24</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein kinase 24 is an enzyme that in humans is encoded by the STK24 gene located in the chromosome 13, band q32.2. It is also known as Mammalian STE20-like protein kinase 3 (MST-3). The protein is 443 amino acids long and its mass is 49 kDa.

<span class="mw-page-title-main">PPP2R3B</span> Protein-coding gene in humans

Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta is an enzyme that in humans is encoded by the PPP2R3B gene.

<span class="mw-page-title-main">Protein phosphatase 2</span> Class of enzyme complexes

Protein phosphatase 2 (PP2), also known as PP2A, is an enzyme that in humans is encoded by the PPP2CA gene. The PP2A heterotrimeric protein phosphatase is ubiquitously expressed, accounting for a large fraction of phosphatase activity in eukaryotic cells. Its serine/threonine phosphatase activity has a broad substrate specificity and diverse cellular functions. Among the targets of PP2A are proteins of oncogenic signaling cascades, such as Raf, MEK, and AKT, where PP2A may act as a tumor suppressor.

<span class="mw-page-title-main">Protein phosphatase 1</span>

Protein phosphatase 1 (PP1) belongs to a certain class of phosphatases known as protein serine/threonine phosphatases. This type of phosphatase includes metal-dependent protein phosphatases (PPMs) and aspartate-based phosphatases. PP1 has been found to be important in the control of glycogen metabolism, muscle contraction, cell progression, neuronal activities, splicing of RNA, mitosis, cell division, apoptosis, protein synthesis, and regulation of membrane receptors and channels.

<span class="mw-page-title-main">B56 domain</span>

Protein phosphatase 2A (PP2A) is a major intracellular protein phosphatase that regulates multiple aspects of cell growth and metabolism. Phosphorylation enables the activation or The ability of this widely distributed heterotrimeric enzyme to act on a diverse array of substrates is largely controlled by the nature of its regulatory B subunit. There are multiple families of B subunits, this family is called the B56 family.

Ceramide-activated protein phosphatases (CAPPs) are a group of enzymes that are activated by the lipid second messenger ceramide. Known CAPPs include members of the protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) families. CAPPs are a subset of intracellular serine/threonine phosphatases. Each CAPP consists of a catalytic subunit which confers phosphatase activity and a regulatory subunit which confers substrate specificity. CAPP involvement has been implicated in glycogen metabolism, apoptotic pathways related to cancer and other cellular pathways related to Alzheimer’s disease.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000221914 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022052 - 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. 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.
  6. "Entrez Gene: PPP2R2A protein phosphatase 2 (formerly 2A), regulatory subunit B, alpha isoform".
  7. 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. Bibcode:1999PNAS...96.4438P. doi: 10.1073/pnas.96.8.4438 . PMC   16350 . PMID   10200280.
  8. 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.
  9. 1 2 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.
  10. 1 2 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. 1 2 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.
  12. 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   109244 . PMID   9774674.
  13. 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   2943288 . PMID   20663872.

Further reading