APOBEC3B

From Wikipedia, the free encyclopedia


Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3B
Identifiers
Symbol(s) APOBEC3B; APOBEC1L; ARCD3; ARP4; DJ742C19.2; FLJ21201; PHRBNL; bK150C2.2
External IDs OMIM: 607110 HomoloGene88714
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 9582 n/a
Ensembl ENSG00000179750 n/a
Uniprot Q9UH17 n/a
Refseq NM_004900 (mRNA)
NP_004891 (protein)
n/a (mRNA)
n/a (protein)
Location Chr 22: 37.71 - 37.72 Mb n/a
Pubmed search [1] n/a

Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3B, also known as APOBEC3B, is a human gene.[1]

This gene is a member of the cytidine deaminase gene 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.[1]

[edit] References

[edit] Further reading

  • 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. PMID 12683974. 
  • Madsen P, Anant S, Rasmussen HH, et al. (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. PMID 10469298. 
  • 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. PMID 10591208. 
  • Jarmuz A, Chester A, Bayliss J, et al. (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. PMID 11863358. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Mariani R, Chen D, Schröfelbauer B, et al. (2003). "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.". Cell 114 (1): 21–31. PMID 12859895. 
  • Sawyer SL, Emerman M, Malik HS (2006). "Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G.". PLoS Biol. 2 (9): E275. doi:10.1371/journal.pbio.0020275. PMID 15269786. 
  • 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. PMID 15466872. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334. 
  • 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. PMID 16060832. 
  • Bogerd HP, Wiegand HL, Doehle BP, et al. (2006). "APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells.". Nucleic Acids Res. 34 (1): 89–95. doi:10.1093/nar/gkj416. PMID 16407327. 
  • 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. PMID 16648136. 
  • 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. PMID 17020885. 
  • Kidd JM, Newman TL, Tuzun E, et al. (2007). "Population stratification of a common APOBEC gene deletion polymorphism.". PLoS Genet. 3 (4): e63. doi:10.1371/journal.pgen.0030063. PMID 17447845.