PPP2R2C

PPP2R2C
Identifiers
Aliases	PPP2R2C, B55-GAMMA, IMYPNO, IMYPNO1, PR52, PR55G, protein phosphatase 2 regulatory subunit Bgamma, B55gamma
External IDs	OMIM: 605997; MGI: 2442660; HomoloGene: 36386; GeneCards: PPP2R2C; OMA:PPP2R2C - orthologs
Gene location (Human) Chr. Chromosome 4 (human) Band 4p16.1 Start 6,320,578 bp End 6,563,600 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 B3 Start 37,025,857 bp End 37,112,422 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in middle temporal gyrus Brodmann area 46 superior frontal gyrus parietal lobe postcentral gyrus occipital lobe Brodmann area 23 entorhinal cortex primary visual cortex prefrontal cortex Top expressed in visual cortex superior frontal gyrus primary visual cortex dentate gyrus of hippocampal formation granule cell primary motor cortex piriform cortex prefrontal cortex cingulate gyrus olfactory tubercle cerebellar cortex More reference expression data BioGPS n/a
Gene ontology Molecular function protein binding protein serine/threonine phosphatase activity protein phosphatase regulator activity Cellular component protein phosphatase type 2A complex cytosol Biological process mitotic cell cycle peptidyl-serine dephosphorylation developmental process regulation of phosphoprotein phosphatase activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5522 269643 Ensembl ENSG00000074211 ENSMUSG00000029120 UniProt Q9Y2T4 Q8BG02 RefSeq (mRNA) NM_001206994 NM_001206995 NM_001206996 NM_020416 NM_181876 NM_001363388 NM_172994 NM_001360003 RefSeq (protein) NP_001193923 NP_001193924 NP_001193925 NP_065149 NP_870991 NP_001350317 NP_766582 NP_001346932 Location (UCSC) Chr 4: 6.32 – 6.56 Mb Chr 5: 37.03 – 37.11 Mb PubMed search
Wikidata
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Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform is an enzyme that in humans is encoded by the PPP2R2C gene.

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 a gamma isoform of the regulatory subunit B55 subfamily. Alternatively spliced transcript variants encoding different isoforms have been identified.

Further reading

• Zolnierowicz S (Oct 2000). "Type 2A protein phosphatase, the complex regulator of numerous signaling pathways". Biochemical Pharmacology. 60 (8): 1225–35. doi:10.1016/S0006-2952(00)00424-X. PMID 11007961.
• Andersen JL, Planelles V (Jan 2005). "The role of Vpr in HIV-1 pathogenesis". Current HIV Research. 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 (Mar 2005). "Viral infections and cell cycle G2/M regulation". Cell Research. 15 (3): 143–9. doi:10.1038/sj.cr.7290279. PMID 15780175.
• Zhao RY, Bukrinsky M, Elder RT (Apr 2005). "HIV-1 viral protein R (Vpr) & host cellular responses". The Indian Journal of Medical Research. 121 (4): 270–86. PMID 15817944.
• Tung HY, De Rocquigny H, Zhao LJ, Cayla X, Roques BP, Ozon R (Jan 1997). "Direct activation of protein phosphatase-2A0 by HIV-1 encoded protein complex NCp7:vpr". FEBS Letters. 401 (2–3): 197–201. doi:10.1016/S0014-5793(96)01470-6. PMID 9013886. S2CID 23293768.
• Ruediger R, Brewis N, Ohst K, Walter G (Nov 1997). "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.
• Strack S, Zaucha JA, Ebner FF, Colbran RJ, Wadzinski BE (Mar 1998). "Brain protein phosphatase 2A: developmental regulation and distinct cellular and subcellular localization by B subunits". The Journal of Comparative Neurology. 392 (4): 515–27. doi:10.1002/(SICI)1096-9861(19980323)392:4<515::AID-CNE8>3.0.CO;2-3. PMID 9514514. S2CID 20496320.
• Sanger Centre, The; Washington University Genome Sequencing Cente, The (Nov 1998). "Toward a complete human genome sequence". Genome Research. 8 (11): 1097–108. doi:10.1101/gr.8.11.1097. PMID 9847074.
• Elder RT, Yu M, Chen M, Zhu X, Yanagida M, Zhao Y (Sep 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.
• Kutsenko AS, Gizatullin RZ, Al-Amin AN, Wang F, Kvasha SM, Podowski RM, Matushkin YG, Gyanchandani A, Muravenko OV, Levitsky VG, Kolchanov NA, Protopopov AI, Kashuba VI, Kisselev LL, Wasserman W, Wahlestedt C, Zabarovsky ER (Jul 2002). "NotI flanking sequences: a tool for gene discovery and verification of the human genome". Nucleic Acids Research. 30 (14): 3163–70. doi:10.1093/nar/gkf428. PMC 135748. PMID 12136098.
• Shern JF, Sharer JD, Pallas DC, Bartolini F, Cowan NJ, Reed MS, Pohl J, Kahn RA (Oct 2003). "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A". The Journal of Biological Chemistry. 278 (42): 40829–36. doi:10.1074/jbc.M308678200. PMID 12912990.
• Chen W, Possemato R, Campbell KT, Plattner CA, Pallas DC, Hahn WC (Feb 2004). "Identification of specific PP2A complexes involved in human cell transformation". Cancer Cell. 5 (2): 127–36. doi:10.1016/S1535-6108(04)00026-1. PMID 14998489.