OAS2

2'-5'-oligoadenylate synthetase 2, 69/71kDa
Identifiers
Symbols	OAS2 ; MGC78578
External IDs	OMIM: 603350 MGI: 2180852 HomoloGene: 49478 GeneCards: OAS2 Gene
EC number	2.7.7.84
Gene ontology Molecular function • 2'-5'-oligoadenylate synthetase activity • double-stranded RNA binding • protein binding • ATP binding • zinc ion binding • metal ion binding Cellular component • nucleus • cytoplasm • mitochondrion • endoplasmic reticulum • cytosol • membrane • intracellular membrane-bounded organelle • perinuclear region of cytoplasm Biological process • nucleobase-containing compound metabolic process • purine nucleotide biosynthetic process • RNA catabolic process • protein glycosylation • response to virus • protein myristoylation • cytokine-mediated signaling pathway • defense response to virus • interferon-gamma-mediated signaling pathway • type I interferon signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4939	246728
Ensembl	ENSG00000111335	ENSMUSG00000032690
UniProt	P29728	E9Q9A9
RefSeq (mRNA)	NM_001032731	NM_145227
RefSeq (protein)	NP_001027903	NP_660262
Location (UCSC)	Chr 12: 112.98 – 113.01 Mb	Chr 5: 120.73 – 120.75 Mb
PubMed search

2'-5'-oligoadenylate synthetase 2 is an enzyme that in humans is encoded by the OAS2 gene.^[1][2]

This gene encodes a member of the 2-5A synthetase family, essential proteins involved in the innate immune response to viral infection. The encoded protein is induced by interferons and uses adenosine triphosphate in 2'-specific nucleotidyl transfer reactions to synthesize 2',5'-oligoadenylates (2-5As). These molecules activate latent RNase L, which results in viral RNA degradation and the inhibition of viral replication. The three known members of this gene family are located in a cluster on chromosome 12. Alternatively spliced transcript variants encoding different isoforms have been described.^[2]

References

1. Hovnanian A, Rebouillat D, Mattei MG, Levy ER, Marie I, Monaco AP, Hovanessian AG (Dec 1998). "The human 2',5'-oligoadenylate synthetase locus is composed of three distinct genes clustered on chromosome 12q24.2 encoding the 100-, 69-, and 40-kDa forms". Genomics 52 (3): 267–277. doi:10.1006/geno.1998.5443. PMID 9790745.
2. "Entrez Gene: OAS2 2'-5'-oligoadenylate synthetase 2, 69/71kDa".

Further reading

• Justesen J, Hartmann R, Kjeldgaard NO (2000). "Gene structure and function of the 2'-5'-oligoadenylate synthetase family". Cell. Mol. Life Sci. 57 (11): 1593–1612. doi:10.1007/PL00000644. PMID 11092454.
• Marié I, Hovanessian AG (1992). "The 69-kDa 2-5A synthetase is composed of two homologous and adjacent functional domains". J. Biol. Chem. 267 (14): 9933–9. PMID 1577824.
• Silverman RH, Sengupta DN (1991). "Translational regulation by HIV leader RNA, TAT, and interferon-inducible enzymes". J. Exp. Pathol. 5 (2): 69–77. PMID 1708818.
• Marié I, Svab J, Robert N, et al. (1990). "Differential expression and distinct structure of 69- and 100-kDa forms of 2-5A synthetase in human cells treated with interferon". J. Biol. Chem. 265 (30): 18601–7. PMID 2211721.
• Hovanessian AG, Laurent AG, Chebath J, et al. (1987). "Identification of 69-kd and 100-kd forms of 2-5A synthetase in interferon-treated human cells by specific monoclonal antibodies". EMBO J. 6 (5): 1273–80. PMC 553929. PMID 2440675.
• Marié I, Galabru J, Svab J, Hovanessian AG (1989). "Preparation and characterization of polyclonal antibodies specific for the 69 and 100 k-dalton forms of human 2-5A synthetase". Biochem. Biophys. Res. Commun. 160 (2): 580–587. doi:10.1016/0006-291X(89)92472-8. PMID 2470369.
• Hovanessian AG, Svab J, Marié I, et al. (1988). "Characterization of 69- and 100-kDa forms of 2-5A-synthetase from interferon-treated human cells". J. Biol. Chem. 263 (10): 4945–9. PMID 3350819.
• Solinas A, Cossu P, Poddighe P, et al. (1994). "Changes of serum 2',5'-oligoadenylate synthetase activity during interferon treatment of chronic hepatitis C". Liver 13 (5): 253–8. PMID 8259037.
• Besse S, Rebouillat D, Marie I, et al. (1998). "Ultrastructural localization of interferon-inducible double-stranded RNA-activated enzymes in human cells". Exp. Cell Res. 239 (2): 379–392. doi:10.1006/excr.1997.3908. PMID 9521856.
• Sarkar SN, Ghosh A, Wang HW, et al. (1999). "The nature of the catalytic domain of 2'-5'-oligoadenylate synthetases". J. Biol. Chem. 274 (36): 25535–25542. doi:10.1074/jbc.274.36.25535. PMID 10464285.
• 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): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Scherer SE, Muzny DM, Buhay CJ, et al. (2006). "The finished DNA sequence of human chromosome 12". Nature 440 (7082): 346–351. doi:10.1038/nature04569. PMID 16541075.