{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P29597","secondaryAccessions":["Q6QB10","Q96CH0"],"uniProtkbId":"TYK2_HUMAN","entryAudit":{"firstPublicDate":"1993-04-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2004-12-07","entryVersion":246,"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":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Non-receptor tyrosine-protein kinase TYK2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10542297"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7526154"}],"value":"2.7.10.2"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:12440"}],"value":"TYK2"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10542297"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10995743"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25762719"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29162862"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7526154"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7638186"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7657660"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7813427"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8232552"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9188471"}],"value":"Non-membrane spanning protein tyrosine kinase involved in numerous cytokines and interferons signaling, which regulates cell growth, development, cell migration, innate and adaptive immunity (PubMed:10542297, PubMed:10995743, PubMed:7657660, PubMed:7813427, PubMed:8232552). Plays both structural and catalytic roles in numerous interleukins and interferons (IFN-alpha/beta) signaling (PubMed:10542297). Associates with heterodimeric cytokine receptor complexes and activates STAT family members including STAT1, STAT3, STAT4 or STAT6 (PubMed:10542297, PubMed:7638186). The heterodimeric cytokine receptor complexes are composed of (1) a TYK2-associated receptor chain (IFNAR1, IL12RB1, IL10RB or IL13RA1), and (2) a second receptor chain associated either with JAK1 or JAK2 (PubMed:10542297, PubMed:25762719, PubMed:7526154, PubMed:7813427). In response to cytokine-binding to receptors, phosphorylates and activates receptors (IFNAR1, IL12RB1, IL10RB or IL13RA1), creating docking sites for STAT members (PubMed:7526154, PubMed:7657660). In turn, recruited STATs are phosphorylated by TYK2 (or JAK1/JAK2 on the second receptor chain), form homo- and heterodimers, translocate to the nucleus, and regulate cytokine/growth factor responsive genes (PubMed:10542297, PubMed:25762719, PubMed:7657660). Negatively regulates STAT3 activity by promototing phosphorylation at a specific tyrosine that differs from the site used for signaling (PubMed:29162862). Involved in the oncostatin-M-mediated signaling pathway through both type I OSM receptor complex (heterodimers composed of LIFR and IL6ST) and type II OSM receptor complex (heterodimers composed of OSMR and IL6ST) (PubMed:9188471)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10596"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:20101"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:61978"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.10.2","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10542297"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7526154"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24843152"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25762719"}],"value":"The protein kinase 1 domain (also termed pseudokinase domain) mediates autoinhibition of the TYK2 kinase domain"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10995743"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15277531"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15899890"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20478313"}],"value":"Interacts (via FERM domain) with JAKMIP1 (PubMed:15277531, PubMed:20478313). Interacts with PIK3R1; this interaction is important for cell migration (PubMed:10995743). Interacts with MPL/TPOR (PubMed:15899890)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16987978"}],"value":"(Microbial infection) Interacts with Epstein-Barr virus protein LMP1; this interaction inhibits TYK2-mediated interferon signaling"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10523853"}],"value":"(Microbial infection) Interacts with papillomavirus-18 protein E6; this interaction impairs JAK-STAT activation by interferon-alpha"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32213613"}],"value":"(Microbial infection) Interacts with Epstein-Barr virus (EBV) tegument protein BGLF2; this interaction participates in the inhibition of type I IFN signaling by the 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