ADARB2

Adenosine deaminase, RNA-specific, B2 (non-functional)
Identifiers
SymbolsADARB2 ; ADAR3; RED2
External IDsOMIM: 602065 MGI: 2151118 HomoloGene: 10276 GeneCards: ADARB2 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez10594191
EnsemblENSG00000185736ENSMUSG00000052551
UniProtQ9NS39Q9JI20
RefSeq (mRNA)NM_018702NM_001289530
RefSeq (protein)NP_061172NP_001276459
Location (UCSC)Chr 10:
1.23 – 1.78 Mb		Chr 13:
8.2 – 8.77 Mb
PubMed search

Double-stranded RNA-specific editase B2 is an enzyme that in humans is encoded by the ADARB2 gene.[1][2][3]

Function

RNA-editing deaminase-2 (RED2, or ADARB2) is a member of the double-stranded RNA (dsRNA) adenosine deaminase family of RNA-editing enzymes. Adenosine deamination of pre-mRNA results in a change in the amino acid sequence of the gene product, which differs from that predicted by the genomic DNA sequence. Other members of this family include DRADA (ADAR) and RED1 (ADARB1).[3][1]

Unlike ADAR1 and ADAR2, ADAR3 has demonstrated no editing ability in vitro. It has been shown to suppress 5-HT2C RNA editing in vitro through a yet unknown mechanism, and may thus work as a negative regulator.[4]

References

  1. ↑ 1.0 1.1 Mittaz L, Antonarakis SE, Higuchi M, Scott HS (Sep 1997). "Localization of a novel human RNA-editing deaminase (hRED2 or ADARB2) to chromosome 10p15". Human Genetics 100 (3-4): 398–400. doi:10.1007/s004390050523. PMID 9272162.
  2. ↑ Chen CX, Cho DS, Wang Q, Lai F, Carter KC, Nishikura K (May 2000). "A third member of the RNA-specific adenosine deaminase gene family, ADAR3, contains both single- and double-stranded RNA binding domains". RNA 6 (5): 755–67. doi:10.1017/S1355838200000170. PMC 1369955. PMID 10836796.
  3. ↑ 3.0 3.1 "Entrez Gene: ADARB2 adenosine deaminase, RNA-specific, B2 (RED2 homolog rat)".
  4. ↑ Hong HQ, Lin JS, Chen L (Feb 2015). "Regulatory factors governing Adenosine-to-Inosine (A-to-I) RNA editing". Bioscience Reports. doi:10.1042/BSR20140190. PMID 25662729.

Further reading

  • Valenzuela A, Blanco J, Callebaut C, Jacotot E, Lluis C, Hovanessian AG et al. (1997). "HIV-1 envelope gp120 and viral particles block adenosine deaminase binding to human CD26". Advances in Experimental Medicine and Biology 421: 185–92. doi:10.1007/978-1-4757-9613-1_24. PMID 9330696.
  • Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R et al. (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI et al. (Jan 2005). "Nucleolar proteome dynamics". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
  • Herrera C, Morimoto C, Blanco J, Mallol J, Arenzana F, Lluis C et al. (Jun 2001). "Comodulation of CXCR4 and CD26 in human lymphocytes". The Journal of Biological Chemistry 276 (22): 19532–9. doi:10.1074/jbc.M004586200. PMID 11278278.
  • Blanco J, Valenzuela A, Herrera C, Lluís C, Hovanessian AG, Franco R (Jul 2000). "The HIV-1 gp120 inhibits the binding of adenosine deaminase to CD26 by a mechanism modulated by CD4 and CXCR4 expression". FEBS Letters 477 (1-2): 123–8. doi:10.1016/S0014-5793(00)01751-8. PMID 10899322.
  • Valenzuela A, Blanco J, Callebaut C, Jacotot E, Lluis C, Hovanessian AG et al. (Apr 1997). "Adenosine deaminase binding to human CD26 is inhibited by HIV-1 envelope glycoprotein gp120 and viral particles". Journal of Immunology 158 (8): 3721–9. PMID 9103436.
  • Hillier LD, Lennon G, Becker M, Bonaldo MF, Chiapelli B, Chissoe S et al. (Sep 1996). "Generation and analysis of 280,000 human expressed sequence tags". Genome Research 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID 8889549.