{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P29728","secondaryAccessions":["A8K9T1","Q6PJ33","Q86XX8"],"uniProtkbId":"OAS2_HUMAN","entryAudit":{"firstPublicDate":"1993-04-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-01-23","entryVersion":206,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"2'-5'-oligoadenylate synthase 2"},"shortNames":[{"value":"(2-5')oligo(A) synthase 2"},{"value":"2-5A synthase 2"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10464285"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11986302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9880569"}],"value":"2.7.7.84"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1577824"}],"value":"p69 OAS / p71 OAS"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1577824"}],"value":"p69OAS / p71OAS"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:8087"}],"value":"OAS2"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"E9Q9A9"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10464285"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11682059"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19923450"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40412389"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9880569"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21142819"}],"value":"Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:10464285, PubMed:9880569). Activated by detection of double stranded RNA (dsRNA): catalyzes the formation of 2'-5'-oligoadenylates (2-5A) from polymerization of ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation (PubMed:10464285, PubMed:11682059, PubMed:9880569, PubMed:40412389). Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:10464285, PubMed:9880569). Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL (PubMed:21142819). In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (PubMed:21142819). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:34407"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:67143"}],"ecNumber":"2.7.7.84","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10464285"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11682059"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11986302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9880569"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11682059"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11682059"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40412389"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9880569"}],"value":"Produced as a latent enzyme which is activated by double stranded RNA (dsRNA) generated during the course of viral infection (PubMed:9880569). The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated (PubMed:9880569). ssRNA or dsDNA do not act as activators (PubMed:9880569). Strongly inhibited by copper and iron (PubMed:11682059). Down-regulated by Zn(2+); Zn(2+) stabilizes the homodimeric form that is less responsive than monomers to activation by dsRNA (PubMed:11682059, PubMed:40412389). Partially inhibited by cobalt and nickel ions (PubMed:11682059)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":2.1,"unit":"mM","substrate":"ATP","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10464285"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11986302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9880569"}]}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10464285"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40412389"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9880569"}],"value":"Homodimer; homodimerization is mediated by coordination of Zn(2+) and down-regulates enzyme activity in response to dsRNA (PubMed:10464285, PubMed:40412389, PubMed:9880569). 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