Probable DNA dC->dU-editing enzyme APOBEC-3B is a protein that in humans is encoded by the APOBEC3Bgene.[1][2][3]
This gene is a member of the cytidine deaminasegene family. It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22. Members of the cluster encode proteins that are structurally and functionally related to the C to U RNA-editing cytidine deaminase APOBEC1. It is thought that the proteins may be RNA editing enzymes and have roles in growth or cell cycle control. This gene along with APOBEC3A have been in recent years found associated with mutagenesis of several cancers. The APOBEC3A and APOBEC3B proteins can cause specific mutations in cancer genomes called APOBEC mutagenesis and several factors including genetic and environmental influence this mutation pattern among patients specifically in bladder and breast cancer. [3]
References
↑Jarmuz A, Chester A, Bayliss J, Gisbourne J, Dunham I, Scott J, Navaratnam N (Feb 2002). "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22". Genomics. 79 (3): 285–96. doi:10.1006/geno.2002.6718. PMID11863358.
↑Madsen P, Anant S, Rasmussen HH, Gromov P, Vorum H, Dumanski JP, Tommerup N, Collins JE, Wright CL, Dunham I, MacGinnitie AJ, Davidson NO, Celis JE (Sep 1999). "Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1". J Invest Dermatol. 113 (2): 162–9. doi:10.1046/j.1523-1747.1999.00682.x. PMID10469298.
Wedekind JE, Dance GS, Sowden MP, Smith HC (2003). "Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business". Trends Genet. 19 (4): 207–16. doi:10.1016/S0168-9525(03)00054-4. PMID12683974.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. doi:10.1038/990031. PMID10591208.
Yu Q, Chen D, König R, et al. (2005). "APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication". J. Biol. Chem. 279 (51): 53379–86. doi:10.1074/jbc.M408802200. PMID15466872.
Rose KM, Marin M, Kozak SL, Kabat D (2005). "Regulated production and anti-HIV type 1 activities of cytidine deaminases APOBEC3B, 3F, and 3G". AIDS Res. Hum. Retroviruses. 21 (7): 611–9. doi:10.1089/aid.2005.21.611. PMID16060832.
Stenglein MD, Harris RS (2006). "APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism". J. Biol. Chem. 281 (25): 16837–41. doi:10.1074/jbc.M602367200. PMID16648136.
Hakata Y, Landau NR (2007). "Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains". J. Biol. Chem. 281 (48): 36624–31. doi:10.1074/jbc.M604980200. PMID17020885.
An APOBEC cytidine deaminase mutagenesis pattern is widespread in human cancers
Steven A Roberts, Michael S Lawrence, Leszek J Klimczak, Sara A Grimm, David Fargo, Petar Stojanov, Adam Kiezun, Gregory V Kryukov, Scott L Carter, Gordon Saksena, Shawn Harris, Ruchir R Shah, Michael A Resnick, Gad Getz & Dmitry A Gordenin
Candace D Middlebrooks, A Rouf Banday, Konichi Matsuda, et al. Association of germline variants in the APOBEC3 region with cancer risk and enrichment with APOBEC-signature mutations in tumors Exit Disclaimer. Nature Genetics 2016.