OAS2

Protein-coding gene in the species Homo sapiens
OAS2
Identifiers
AliasesOAS2, 2'-5'-oligoadenylate synthetase 2
External IDsOMIM: 603350; MGI: 2180852; HomoloGene: 49478; GeneCards: OAS2; OMA:OAS2 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for OAS2
Genomic location for OAS2
Band12q24.13Start112,978,395 bp[1]
End113,011,723 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for OAS2
Genomic location for OAS2
Band5 F|5 60.64 cMStart120,868,398 bp[2]
End120,887,918 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • monocyte

  • granulocyte

  • lymph node

  • decidua

  • appendix

  • gallbladder

  • spleen

  • right lung

  • blood

  • olfactory zone of nasal mucosa
Top expressed in
  • mucous cell of stomach

  • submandibular gland

  • epithelium of stomach

  • blood

  • myocardium of ventricle

  • subcutaneous adipose tissue

  • cervix

  • cornea

  • right ventricle

  • cardiac muscles
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • nucleotide binding
  • nucleotidyltransferase activity
  • zinc ion binding
  • metal ion binding
  • 2'-5'-oligoadenylate synthetase activity
  • protein binding
  • RNA binding
  • double-stranded RNA binding
  • ATP binding
Cellular component
  • cytoplasm
  • membrane
  • endoplasmic reticulum
  • mitochondrion
  • perinuclear region of cytoplasm
  • nucleus
  • nucleoplasm
  • cytosol
  • intracellular membrane-bounded organelle
Biological process
  • purine nucleotide biosynthetic process
  • interferon-gamma-mediated signaling pathway
  • immune system process
  • protein myristoylation
  • response to virus
  • RNA catabolic process
  • protein glycosylation
  • defense response to virus
  • type I interferon signaling pathway
  • immune response
  • innate immune response
  • nucleobase-containing compound metabolic process
  • response to bacterium
  • regulation of ribonuclease activity
  • regulation of lactation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

4939

246728

Ensembl

ENSG00000111335

ENSMUSG00000032690

UniProt

P29728

E9Q9A9

RefSeq (mRNA)

NM_001032731
NM_002535
NM_016817

NM_145227
NM_001347448

RefSeq (protein)

NP_001027903
NP_002526
NP_058197

NP_001334377
NP_660262

Location (UCSC)Chr 12: 112.98 – 113.01 MbChr 5: 120.87 – 120.89 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

2'-5'-oligoadenylate synthetase 2 is an enzyme that in humans is encoded by the OAS2 gene.[5][6]

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.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000111335 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032690 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ a b "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. S2CID 19154357.
  • 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. doi:10.1016/S0021-9258(19)50182-X. 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. doi:10.1016/S0021-9258(17)44794-6. 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. doi:10.1002/j.1460-2075.1987.tb02364.x. 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. doi:10.1016/S0021-9258(18)68878-7. 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. doi:10.1111/j.1600-0676.1993.tb00640.x. 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2006Natur.440..346S. doi:10.1038/nature04569. PMID 16541075.


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