{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P23458","secondaryAccessions":["Q59GQ2","Q9UD26"],"uniProtkbId":"JAK1_HUMAN","entryAudit":{"firstPublicDate":"1991-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2008-11-25","entryVersion":248,"sequenceVersion":2},"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":"Tyrosine-protein kinase JAK1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1848670"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7615558"}],"value":"2.7.10.2"}]},"alternativeNames":[{"fullName":{"value":"Janus kinase 1"},"shortNames":[{"value":"JAK-1"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:6190"}],"value":"JAK1"},"synonyms":[{"value":"JAK1A"},{"value":"JAK1B"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11294841"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11909529"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12133952"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15194700"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16239216"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27384491"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28111307"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32750333"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7615558"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7657660"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8232552"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9188471"}],"value":"Non-membrane spanning protein tyrosine kinase that phosphorylates signal-transducing subunits of cytokine receptor complexes like IL2RB, IL10RA, IFNAR2, IL6ST, LIFR, OSMR and IL31RA (PubMed:11909529, PubMed:12133952, PubMed:15194700, PubMed:16239216, PubMed:28111307, PubMed:32750333, PubMed:7615558, PubMed:8232552, PubMed:9188471). Functionally, is involved in the IFN-alpha/beta/gamma signal pathway (PubMed:16239216, PubMed:28111307, PubMed:32750333, PubMed:7615558, PubMed:8232552). Mechanistically, in response to interferon-binding to IFNAR1-IFNAR2 heterodimer, phosphorylates and activates its binding partner IFNAR2, creating docking sites for STAT proteins (PubMed:7759950). Directly phosphorylates STAT proteins but also activates STAT signaling through the transactivation of other JAK kinases associated with signaling receptors (PubMed:16239216, PubMed:32750333, PubMed:8232552). Involved in the MT-RNR2/humanin-mediated signaling pathway leading to STAT3 phosphorylation (PubMed:27384491). Binding of CNTF or the CLCF1/CLF heterodimer to CNTFR leads to IL6ST/gp130-LIFR dimerization followed by activation of JAK1 and JAK2 which in turns phosphorylate IL6ST/gp130 and LIFR (PubMed:11294841). The tyrosine phosphorylated signaling receptors serve in turn as docking proteins for STAT3 (PubMed:11294841). 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). 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). Involved in the Interleukin-31-mediated signaling pathway through the IL31 receptor complex (heterodimers composed of OSMR and IL31RA) (PubMed:15194700)"}],"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:0000255","source":"PROSITE-ProRule","id":"PRU10028"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1848670"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7615558"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7615558"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7615558"}],"value":"Mn(2+) was used in the in vitro kinase assay but Mg(2+) is likely to be the in vivo cofactor."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P52332"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12133952"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12200137"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15194700"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15277531"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7615558"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7759950"}],"value":"Interacts with IFNGR1 (PubMed:7615558). Interacts with JAKMIP1 (PubMed:15277531). Interacts with SHB (PubMed:12200137). Interacts (via N-terminus) with IL2RB and IL10RA (via its cytoplasmic domain) (PubMed:12133952). Interacts with FER (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P23458","intActId":"EBI-1383438"},"interactantTwo":{"uniProtKBAccession":"P04626","geneName":"ERBB2","intActId":"EBI-641062"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P23458","intActId":"EBI-1383438"},"interactantTwo":{"uniProtKBAccession":"P48551","geneName":"IFNAR2","intActId":"EBI-958408"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P23458","intActId":"EBI-1383438"},"interactantTwo":{"uniProtKBAccession":"P40189-1","geneName":"IL6ST","intActId":"EBI-15742214"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P23458","intActId":"EBI-1383438"},"interactantTwo":{"uniProtKBAccession":"O60674","geneName":"JAK2","intActId":"EBI-518647"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P23458","intActId":"EBI-1383438"},"interactantTwo":{"uniProtKBAccession":"Q99650","geneName":"OSMR","intActId":"EBI-2804080"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P23458","intActId":"EBI-1383438"},"interactantTwo":{"uniProtKBAccession":"Q13485","geneName":"SMAD4","intActId":"EBI-347263"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P23458","intActId":"EBI-1383438"},"interactantTwo":{"uniProtKBAccession":"P42224","geneName":"STAT1","intActId":"EBI-1057697"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P23458","intActId":"EBI-1383438"},"interactantTwo":{"uniProtKBAccession":"P40763","geneName":"STAT3","intActId":"EBI-518675"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"value":"Wholly intracellular, possibly membrane associated"}]},"subcellularLocations":[{"location":{"value":"Endomembrane system","id":"SL-0147"},"topology":{"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7896447"}],"value":"Expressed at higher levels in primary colon tumors than in normal colon tissue. The expression level in metastatic colon tumors is comparable to the expression level in normal colon tissue"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16239216"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32750333"}],"value":"The protein kinase 1 domain is also called the pseudokinase domain and has a regulatory role through the transactivation of other JAK kinases associated with signaling receptors"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32750333"}],"value":"The protein kinase 2 domain is the catalytically active domain"}],"commentType":"DOMAIN"},{"texts":[{"value":"The FERM domain mediates interaction with JAKMIP1"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11909529"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7615558"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8232552"}],"value":"Autophosphorylated (PubMed:7615558). Phosphorylated by TYK2 on tyrosine residues in response to type-I interferon signaling, leading to its activation (PubMed:8232552). Phosphorylated on tyrosine residues in response to interferon gamma signaling (PubMed:7615558). Dephosphorylation of Tyr-1034 and Tyr-1035 by PTPN2 negatively regulates cytokine-mediated signaling (PubMed:11909529)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26027934"}],"value":"Ubiquitinated by RNF125; leading to its degradation by the proteasome"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Autoinflammation, immune dysregulation, and eosinophilia","diseaseAccession":"DI-05905","acronym":"AIIDE","description":"An autosomal dominant disorder characterized by immune dysregulation, severe atopic dermatitis, and chronic gastrointestinal inflammation. 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