PPP2R4

PTPA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2G62, 2HV6, 2HV7, 2IXM, 4LAC, 4NY3
Identifiers
Aliases	PTPA, PP2A, PR53, PPP2R4, protein phosphatase 2 regulatory subunit 4, protein phosphatase 2 phosphatase activator
External IDs	OMIM: 600756; MGI: 1346006; HomoloGene: 6149; GeneCards: PTPA; OMA:PTPA - orthologs
Gene location (Human) Chr. Chromosome 9 (human) Band 9q34.11 Start 129,110,950 bp End 129,148,946 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2 B|2 21.71 cM Start 30,416,039 bp End 30,447,806 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Brodmann area 10 frontal pole apex of heart middle frontal gyrus right frontal lobe anterior cingulate cortex right testis left testis paraflocculus of cerebellum amygdala Top expressed in aortic valve ascending aorta internal carotid artery external carotid artery dentate gyrus of hippocampal formation granule cell Paneth cell perirhinal cortex Rostral migratory stream molar lactiferous gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding protein tyrosine phosphatase activator activity protein homodimerization activity isomerase activity peptidyl-prolyl cis-trans isomerase activity ATPase activity protein binding protein heterodimerization activity protein phosphatase 2A binding phosphatase activator activity signaling receptor binding ATP binding protein phosphatase regulator activity Cellular component cytoplasm calcium channel complex protein phosphatase type 2A complex nucleoplasm extracellular exosome nucleus Biological process negative regulation of protein dephosphorylation positive regulation of protein dephosphorylation regulation of phosphoprotein phosphatase activity positive regulation of phosphoprotein phosphatase activity positive regulation of apoptotic process negative regulation of phosphoprotein phosphatase activity protein peptidyl-prolyl isomerization mitotic spindle organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5524 110854 Ensembl ENSG00000119383 ENSMUSG00000039515 UniProt Q15257 P58389 RefSeq (mRNA) NM_001193397 NM_001271832 NM_021131 NM_178000 NM_178001 NM_178002 NM_178003 NM_138748 RefSeq (protein) NP_001180326 NP_001258761 NP_066954 NP_821067 NP_821068 NP_821070 NP_620087 NP_001349662 NP_001349663 Location (UCSC) Chr 9: 129.11 – 129.15 Mb Chr 2: 30.42 – 30.45 Mb PubMed search
Wikidata
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Serine/threonine-protein phosphatase 2A regulatory subunit B is an enzyme that in humans is encoded by the PPP2R4 gene.

Protein phosphatase 2A is one of the four major Ser/Thr phosphatases and is implicated in the negative control of cell growth and division. Protein phosphatase 2A 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. This gene encodes a specific phosphotyrosyl phosphatase activator of the dimeric form of protein phosphatase 2A. Alternative splicing results in multiple transcript variants encoding different isoforms.

Interactions

PPP2R4 has been shown to interact with PPP2R3A, CCNG1 and Janus kinase 2.

Further reading

• Andersen JL, Planelles V (2005). "The role of Vpr in HIV-1 pathogenesis". Curr. HIV Res. 3 (1): 43–51. doi:10.2174/1570162052772988. PMID 15638722.
• Le Rouzic E, Benichou S (2006). "The Vpr protein from HIV-1: distinct roles along the viral life cycle". Retrovirology. 2: 11. doi:10.1186/1742-4690-2-11. PMC 554975. PMID 15725353.
• Zhao RY, Elder RT (2005). "Viral infections and cell cycle G2/M regulation". Cell Res. 15 (3): 143–9. doi:10.1038/sj.cr.7290279. PMID 15780175.
• Zhao RY, Bukrinsky M, Elder RT (2005). "HIV-1 viral protein R (Vpr) & host cellular responses". Indian J. Med. Res. 121 (4): 270–86. PMID 15817944.
• Soprano KJ, Purev E, Vuocolo S, Soprano DR (2006). "Rb2/p130 and protein phosphatase 2A: key mediators of ovarian carcinoma cell growth suppression by all-trans retinoic acid". Oncogene. 25 (38): 5315–25. doi:10.1038/sj.onc.1209679. PMID 16936753.
• Jakes S, Mellgren RL, Schlender KK (1986). "Isolation and characterization of an inhibitor-sensitive and a polycation-stimulated protein phosphatase from rat liver nuclei". Biochim. Biophys. Acta. 888 (1): 135–42. doi:10.1016/0167-4889(86)90079-0. PMID 3017441.
• Turowski P, Fernandez A, Favre B, et al. (1995). "Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression". J. Cell Biol. 129 (2): 397–410. doi:10.1083/jcb.129.2.397. PMC 2199911. PMID 7721943.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Cayla X, Van Hoof C, Bosch M, et al. (1994). "Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A". J. Biol. Chem. 269 (22): 15668–75. doi:10.1016/S0021-9258(17)40733-2. PMID 8195217.
• Okamoto K, Kamibayashi C, Serrano M, et al. (1996). "p53-dependent association between cyclin G and the B' subunit of protein phosphatase 2A". Mol. Cell. Biol. 16 (11): 6593–602. doi:10.1128/mcb.16.11.6593. PMC 231661. PMID 8887688.
• Tung HY, De Rocquigny H, Zhao LJ, et al. (1997). "Direct activation of protein phosphatase-2A0 by HIV-1 encoded protein complex NCp7:vpr". FEBS Lett. 401 (2–3): 197–201. doi:10.1016/S0014-5793(96)01470-6. PMID 9013886. S2CID 23293768.
• Hériché JK, Lebrin F, Rabilloud T, et al. (1997). "Regulation of protein phosphatase 2A by direct interaction with casein kinase 2alpha". Science. 276 (5314): 952–5. doi:10.1126/science.276.5314.952. PMID 9139659.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Ruediger R, Brewis N, Ohst K, Walter G (1998). "Increasing the ratio of PP2A core enzyme to holoenzyme inhibits Tat-stimulated HIV-1 transcription and virus production". Virology. 238 (2): 432–43. doi:10.1006/viro.1997.8873. PMID 9400615.
• Ogris E, Du X, Nelson KC, et al. (1999). "A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A". J. Biol. Chem. 274 (20): 14382–91. doi:10.1074/jbc.274.20.14382. PMC 3503312. PMID 10318862.
• Janssens V, Van Hoof C, De Baere I, et al. (2000). "Functional analysis of the promoter region of the human phosphotyrosine phosphatase activator gene: Yin Yang 1 is essential for core promoter activity". Biochem. J. 344 (3): 755–63. doi:10.1042/0264-6021:3440755. PMC 1220697. PMID 10585862.
• Janssens V, van Hoof C, Martens E, et al. (2000). "Identification and characterization of alternative splice products encoded by the human phosphotyrosyl phosphatase activator gene". Eur. J. Biochem. 267 (14): 4406–13. doi:10.1046/j.1432-1327.2000.01486.x. PMID 10880964.
• Elder RT, Yu M, Chen M, et al. (2001). "HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25". Virology. 287 (2): 359–70. doi:10.1006/viro.2001.1007. PMID 11531413.