Biology:PPP2R3B
Generic protein structure example |
Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta is an enzyme that in humans is encoded by the PPP2R3B gene.[1][2]
Function
Protein phosphatase 2 (formerly named type 2A) 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 beta subfamily of regulatory subunit B''. Alternative splicing results in multiple transcript variants encoding different isoforms.[2]
Interactions
PPP2R3B has been shown to interact with PPP2R1B,[3] PPP2R1A,[3][4] CDC6[5] and PPP2CA.[4][5]
References
- ↑ "Elevated DNA sequence diversity in the genomic region of the phosphatase PPP2R3L gene in the human pseudoautosomal region". Cytogenetics and Cell Genetics 91 (1–4): 224–30. February 2001. doi:10.1159/000056849. PMID 11173861.
- ↑ 2.0 2.1 "Entrez Gene: PPP2R3B protein phosphatase 2 (formerly 2A), regulatory subunit B, beta". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=28227.
- ↑ 3.0 3.1 "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. Jan 2003. doi:10.1042/BJ20021244. PMID 12370081.
- ↑ 4.0 4.1 "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. Jan 2009. doi:10.1074/mcp.M800266-MCP200. PMID 18782753.
- ↑ 5.0 5.1 "PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with Cdc6 and modulates DNA replication in human cells". Molecular and Cellular Biology 20 (3): 1021–9. Feb 2000. doi:10.1128/MCB.20.3.1021-1029.2000. PMID 10629059.
Further reading
- "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research 6 (9): 791–806. Sep 1996. doi:10.1101/gr.6.9.791. PMID 8889548.
- "Binding specificity of protein phosphatase 2A core enzyme for regulatory B subunits and T antigens". Journal of Virology 73 (1): 839–42. Jan 1999. doi:10.1128/JVI.73.1.839-842.1999. PMID 9847399.
- "Antigens recognized by autologous antibody in patients with renal-cell carcinoma". International Journal of Cancer 83 (4): 456–64. Nov 1999. doi:10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5. PMID 10508479.
- "PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with Cdc6 and modulates DNA replication in human cells". Molecular and Cellular Biology 20 (3): 1021–9. Feb 2000. doi:10.1128/MCB.20.3.1021-1029.2000. PMID 10629059.
- "Protein phosphatase 2A interacts with the Src kinase substrate p130(CAS)". Oncogene 20 (42): 6057–65. Sep 2001. doi:10.1038/sj.onc.1204735. PMID 11593413.
- "Identification and characterization of B"-subunits of protein phosphatase 2 A in Xenopus laevis oocytes and adult tissues". European Journal of Biochemistry 270 (2): 376–87. Jan 2003. doi:10.1046/j.1432-1033.2003.03398.x. PMID 12605688.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "Up-regulation of GPR48 induced by down-regulation of p27Kip1 enhances carcinoma cell invasiveness and metastasis". Cancer Research 66 (24): 11623–31. Dec 2006. doi:10.1158/0008-5472.CAN-06-2629. PMID 17178856.