{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O15111","secondaryAccessions":["O14666","Q13132","Q5W0I4","Q92467"],"uniProtkbId":"IKKA_HUMAN","entryAudit":{"firstPublicDate":"2001-06-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-01-11","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":{"value":"Inhibitor of nuclear factor kappa-B kinase subunit alpha"},"shortNames":[{"value":"I-kappa-B kinase alpha"},{"value":"IKK-A"},{"value":"IKK-alpha"},{"value":"IkBKA"},{"value":"IkappaB kinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9244310"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9252186"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9346484"}],"value":"2.7.11.10"}]},"alternativeNames":[{"fullName":{"value":"Conserved helix-loop-helix ubiquitous kinase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9346484"}],"value":"I-kappa-B kinase 1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9346484"}],"value":"IKK-1"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9346484"}],"value":"IKK1"}]},{"fullName":{"value":"Nuclear factor NF-kappa-B inhibitor kinase alpha"},"shortNames":[{"value":"NFKBIKA"}]},{"fullName":{"value":"Transcription factor 16"},"shortNames":[{"value":"TCF-16"}]}]},"genes":[{"geneName":{"value":"CHUK"},"synonyms":[{"value":"IKKA"},{"value":"TCF16"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60680"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12789342"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15084260"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17434128"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20434986"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20501937"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21765415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30217973"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35952808"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9244310"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9252186"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9346484"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18626576"}],"value":"Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on serine residues (PubMed:18626576, PubMed:35952808, PubMed:9244310, PubMed:9252186, PubMed:9346484). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). Negatively regulates the pathway by phosphorylating the scaffold protein TAXBP1 and thus promoting the assembly of the A20/TNFAIP3 ubiquitin-editing complex (composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and RNF11) (PubMed:21765415). Therefore, CHUK plays a key role in the negative feedback of NF-kappa-B canonical signaling to limit inflammatory gene activation. As part of the non-canonical pathway of NF-kappa-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes (PubMed:20501937). In turn, these complexes regulate genes encoding molecules involved in B-cell survival and lymphoid organogenesis. Also participates in the negative feedback of the non-canonical NF-kappa-B signaling pathway by phosphorylating and destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates CREBBP and consequently increases both its transcriptional and histone acetyltransferase activities (PubMed:17434128). Modulates chromatin accessibility at NF-kappa-B-responsive promoters by phosphorylating histones H3 at 'Ser-10' that are subsequently acetylated at 'Lys-14' by CREBBP (PubMed:12789342). Additionally, phosphorylates the CREBBP-interacting protein NCOA3. Also phosphorylates FOXO3 and may regulate this pro-apoptotic transcription factor (PubMed:15084260). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates AMBRA1 following mitophagy induction, promoting AMBRA1 interaction with ATG8 family proteins and its mitophagic activity (PubMed:30217973)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[I-kappa-B protein] + ATP = O-phospho-L-seryl-[I-kappa-B protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19073"},{"database":"Rhea","id":"RHEA-COMP:13698"},{"database":"Rhea","id":"RHEA-COMP:13699"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.10","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9244310"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9252186"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9346484"}]}},{"texts":[{"value":"Activated when phosphorylated and inactivated when dephosphorylated"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60680"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10195894"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11971985"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12612076"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15084260"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15173580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15456791"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16177806"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17540171"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19150425"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20434986"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23091055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23776175"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26334375"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27426725"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30341167"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32935379"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9751059"}],"value":"Component of the I-kappa-B-kinase (IKK) core complex consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/IKBKG subunits (PubMed:32935379). The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex (PubMed:10195894, PubMed:12612076). The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65 (By similarity). Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP (PubMed:11971985). Part of a 70-90 kDa complex at least consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14 (PubMed:9751059). Directly interacts with TRPC4AP (By similarity). May interact with TRAF2 (PubMed:19150425). Interacts with NALP2 (PubMed:15456791). May interact with MAVS/IPS1 (PubMed:16177806). Interacts with ARRB1 and ARRB2 (PubMed:15173580). Interacts with NLRC5; prevents CHUK phosphorylation and kinase activity (PubMed:20434986). Interacts with PIAS1; this interaction induces PIAS1 phosphorylation (PubMed:17540171). Interacts with ZNF268 isoform 2; the interaction is further increased in a TNF-dependent manner (PubMed:23091055). Interacts with FOXO3 (PubMed:15084260). Interacts with IFIT5; the interaction synergizes the recruitment of IKK to MAP3K7 and enhances IKK phosphorylation (PubMed:26334375). Interacts with LRRC14 (PubMed:27426725). Interacts with SASH1 (PubMed:23776175). Directly interacts with DDX3X after the physiological activation of the TLR7 and TLR8 pathways; this interaction enhances CHUK autophosphorylation (PubMed:30341167)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20855622"}],"value":"(Microbial infection) Interacts with InlC of Listeria monocytogenes"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q16543","geneName":"CDC37","intActId":"EBI-295634"},"numberOfExperiments":9,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"P46527","geneName":"CDKN1B","intActId":"EBI-519280"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q13451","geneName":"FKBP5","intActId":"EBI-306914"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"P07900","geneName":"HSP90AA1","intActId":"EBI-296047"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"P08238","geneName":"HSP90AB1","intActId":"EBI-352572"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"O14920","geneName":"IKBKB","intActId":"EBI-81266"},"numberOfExperiments":20,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q9Y6K9","geneName":"IKBKG","intActId":"EBI-81279"},"numberOfExperiments":32,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q92985","geneName":"IRF7","intActId":"EBI-968267"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q99558","geneName":"MAP3K14","intActId":"EBI-358011"},"numberOfExperiments":13,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q5TCX8","geneName":"MAP3K21","intActId":"EBI-1057380"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"P01106","geneName":"MYC","intActId":"EBI-447544"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"P19838","geneName":"NFKB1","intActId":"EBI-300010"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"P25963","geneName":"NFKBIA","intActId":"EBI-307386"},"numberOfExperiments":16,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q15653","geneName":"NFKBIB","intActId":"EBI-352889"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q04206","geneName":"RELA","intActId":"EBI-73886"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q15796","geneName":"SMAD2","intActId":"EBI-1040141"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q86VP1","geneName":"TAX1BP1","intActId":"EBI-529518"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"P03129","geneName":"E7","intActId":"EBI-866453"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q07857","geneName":"E7","intActId":"EBI-9690349"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q6TY28","geneName":"E7","intActId":"EBI-9690312"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q6TY35","geneName":"E7","intActId":"EBI-9690239"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q80901","geneName":"E7","intActId":"EBI-9690278"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q8B5B5","geneName":"E7","intActId":"EBI-9690330"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"P71451","geneName":"inlC","intActId":"EBI-21019720"},"numberOfExperiments":3,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"P24772","geneName":"OPG200","intActId":"EBI-4291651"},"numberOfExperiments":3,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"O15111","intActId":"EBI-81249"},"interactantTwo":{"uniProtKBAccession":"Q77M19","geneName":"P/V","intActId":"EBI-6149376"},"numberOfExperiments":2,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"value":"Shuttles between the cytoplasm and the nucleus"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12789342"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30341167"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12789342"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"value":"Widely expressed"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18626576"}],"value":"The kinase domain is located in the N-terminal region. The leucine zipper is important to allow homo- and heterodimerization. At the C-terminal region is located the region responsible for the interaction with NEMO/IKBKG"}],"commentType":"DOMAIN"},{"texts":[{"value":"Phosphorylated by MAP3K14/NIK, AKT and to a lesser extent by MEKK1, and dephosphorylated by PP2A. Autophosphorylated"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35952808"}],"value":"Ubiquitinated by TRIM56 via 'Lys-63'-linked ubiquitination, promoting activation of CHUK/IKKA"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17116858"}],"value":"(Microbial infection) Acetylation of Thr-179 by Yersinia YopJ prevents phosphorylation and activation, thus blocking the I-kappa-B signaling pathway"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Cocoon syndrome","diseaseAccession":"DI-02978","acronym":"COCOS","description":"A lethal syndrome characterized by multiple fetal malformations including defective face and seemingly absent limbs, which are bound to the trunk and encased under the skin.","diseaseCrossReference":{"database":"MIM","id":"613630"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20961246"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Bartsocas-Papas syndrome 2","diseaseAccession":"DI-06116","acronym":"BPS2","description":"An autosomal recessive, severe form of popliteal pterygium syndrome. Popliteal pterygia syndromes have considerable variability in severity and in the associated phenotypic features but they are all characterized by cutaneous webbing across one or more major joints, cleft lip and/or palate, syndactyly, and genital malformations.","diseaseCrossReference":{"database":"MIM","id":"619339"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25691407"}]},"note":{"texts":[{"value":"The disease may be caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00159"}],"value":"Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":745,"modifier":"EXACT"}},"description":"Inhibitor of nuclear factor kappa-B kinase subunit alpha","featureId":"PRO_0000086011"},{"type":"Domain","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"Protein kinase","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00159"}]},{"type":"Region","location":{"start":{"value":455,"modifier":"EXACT"},"end":{"value":476,"modifier":"EXACT"}},"description":"Leucine-zipper"},{"type":"Region","location":{"start":{"value":738,"modifier":"EXACT"},"end":{"value":743,"modifier":"EXACT"}},"description":"NEMO-binding"},{"type":"Active site","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00159"},{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10027"}]},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00159"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00159"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Modified residue","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Phosphothreonine; by PKB/AKT1 and SGK1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10485710"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19088076"}]},{"type":"Modified residue","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"Phosphoserine; by MAP3K14","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9520446"}]},{"type":"Modified residue","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"(Microbial infection) O-acetylthreonine; by Yersinia YopJ","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17116858"}]},{"type":"Modified residue","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"Phosphoserine; by SGK1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19088076"}]},{"type":"Natural variant","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"in dbSNP:rs34427437","featureCrossReferences":[{"database":"dbSNP","id":"rs34427437"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17344846"}],"featureId":"VAR_040565","alternativeSequence":{"originalSequence":"S","alternativeSequences":["C"]}},{"type":"Natural variant","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"in dbSNP:rs2230803","featureCrossReferences":[{"database":"dbSNP","id":"rs2230803"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17344846"}],"featureId":"VAR_040566","alternativeSequence":{"originalSequence":"V","alternativeSequences":["A"]}},{"type":"Natural variant","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"in dbSNP:rs2230804","featureCrossReferences":[{"database":"dbSNP","id":"rs2230804"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15164054"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17344846"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8777433"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9244310"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9252186"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9813230"}],"featureId":"VAR_021359","alternativeSequence":{"originalSequence":"V","alternativeSequences":["I"]}},{"type":"Mutagenesis","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Loss of phosphorylation and decrease of kinase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10485710"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"Loss of kinase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9244310"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9346484"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"Loss of autophosphorylation.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9244310"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9346484"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["M"]}},{"type":"Mutagenesis","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"Loss of phosphorylation and of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9346484"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9520446"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"Full activation.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9346484"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9520446"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["E"]}},{"type":"Mutagenesis","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"No change in phosphorylation.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9520446"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"No change in phosphorylation.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9520446"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Sequence conflict","location":{"start":{"value":543,"modifier":"EXACT"},"end":{"value":543,"modifier":"EXACT"}},"description":"in Ref. 2; AAC51671","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["G"]}},{"type":"Sequence conflict","location":{"start":{"value":604,"modifier":"EXACT"},"end":{"value":604,"modifier":"EXACT"}},"description":"in Ref. 7; AAC50713","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["R"]}},{"type":"Sequence conflict","location":{"start":{"value":679,"modifier":"EXACT"},"end":{"value":680,"modifier":"EXACT"}},"description":"in Ref. 7; AAC50713","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"TS","alternativeSequences":["AY"]}},{"type":"Sequence conflict","location":{"start":{"value":684,"modifier":"EXACT"},"end":{"value":684,"modifier":"EXACT"}},"description":"in Ref. 3; no nucleotide entry and 7; AAC50713","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"P","alternativeSequences":["A"]}},{"type":"Sequence conflict","location":{"start":{"value":686,"modifier":"EXACT"},"end":{"value":687,"modifier":"EXACT"}},"description":"in Ref. 7; AAC50713","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"TS","alternativeSequences":["DL"]}},{"type":"Helix","location":{"start":{"value":735,"modifier":"EXACT"},"end":{"value":737,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3BRT"}]},{"type":"Helix","location":{"start":{"value":741,"modifier":"EXACT"},"end":{"value":743,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3BRT"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0007","category":"PTM","name":"Acetylation"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-1267","category":"Technical term","name":"Proteomics identification"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0723","category":"Molecular function","name":"Serine/threonine-protein kinase"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0832","category":"PTM","name":"Ubl conjugation"}],"references":[{"referenceNumber":1,"citation":{"id":"9244310","citationType":"journal article","authors":["Regnier C.H.","Song H.Y.","Gao X.","Goeddel D.V.","Cao Z.","Rothe M."],"citationCrossReferences":[{"database":"PubMed","id":"9244310"},{"database":"DOI","id":"10.1016/s0092-8674(00)80344-x"}],"title":"Identification and characterization of an IkappaB kinase.","publicationDate":"1997","journal":"Cell","firstPage":"373","lastPage":"383","volume":"90"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA]","FUNCTION","CATALYTIC ACTIVITY","MUTAGENESIS OF LYS-44","VARIANT ILE-268"],"referenceComments":[{"value":"T-cell","type":"TISSUE"}]},{"referenceNumber":2,"citation":{"id":"9252186","citationType":"journal article","authors":["DiDonato J.A.","Hayakawa M.","Rothwarf D.M.","Zandi E.","Karin M."],"citationCrossReferences":[{"database":"PubMed","id":"9252186"},{"database":"DOI","id":"10.1038/41493"}],"title":"A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB.","publicationDate":"1997","journal":"Nature","firstPage":"548","lastPage":"554","volume":"388"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA]","PARTIAL PROTEIN SEQUENCE","FUNCTION","CATALYTIC ACTIVITY","VARIANT ILE-268"]},{"referenceNumber":3,"citation":{"id":"9346484","citationType":"journal article","authors":["Mercurio F.","Zhu H.","Murray B.W.","Shevchenko A.","Bennett B.L.","Li J.W.","Young D.B.","Barbosa M.","Mann M.","Manning A.","Rao A."],"citationCrossReferences":[{"database":"PubMed","id":"9346484"},{"database":"DOI","id":"10.1126/science.278.5339.860"}],"title":"IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation.","publicationDate":"1997","journal":"Science","firstPage":"860","lastPage":"866","volume":"278"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA]","PARTIAL PROTEIN SEQUENCE","FUNCTION","CATALYTIC ACTIVITY","MUTAGENESIS OF LYS-44 AND SER-176"],"referenceComments":[{"value":"Cervix carcinoma","type":"TISSUE"}]},{"referenceNumber":4,"citation":{"id":"9813230","citationType":"journal article","authors":["Hu M.C.-T.","Wang Y.-P."],"citationCrossReferences":[{"database":"PubMed","id":"9813230"},{"database":"DOI","id":"10.1016/s0378-1119(98)00462-4"}],"title":"IkappaB kinase-alpha and -beta genes are coexpressed in adult and embryonic tissues but localized to different human chromosomes.","publicationDate":"1998","journal":"Gene","firstPage":"31","lastPage":"40","volume":"222"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA]","VARIANT ILE-268"],"referenceComments":[{"value":"Heart","type":"TISSUE"}]},{"referenceNumber":5,"citation":{"id":"CI-2Q517G2GQHI2S","citationType":"submission","authoringGroup":["SeattleSNPs variation discovery resource"],"publicationDate":"JUN-2004","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":6,"citation":{"id":"15164054","citationType":"journal article","authors":["Deloukas P.","Earthrowl M.E.","Grafham D.V.","Rubenfield M.","French L.","Steward C.A.","Sims S.K.","Jones M.C.","Searle S.","Scott C.","Howe K.","Hunt S.E.","Andrews T.D.","Gilbert J.G.R.","Swarbreck D.","Ashurst J.L.","Taylor A.","Battles J.","Bird C.P.","Ainscough R.","Almeida J.P.","Ashwell R.I.S.","Ambrose K.D.","Babbage A.K.","Bagguley C.L.","Bailey J.","Banerjee R.","Bates K.","Beasley H.","Bray-Allen S.","Brown A.J.","Brown J.Y.","Burford D.C.","Burrill W.","Burton J.","Cahill P.","Camire D.","Carter N.P.","Chapman J.C.","Clark S.Y.","Clarke G.","Clee C.M.","Clegg S.","Corby N.","Coulson A.","Dhami P.","Dutta I.","Dunn M.","Faulkner L.","Frankish A.","Frankland J.A.","Garner P.","Garnett J.","Gribble S.","Griffiths C.","Grocock R.","Gustafson E.","Hammond S.","Harley J.L.","Hart E.","Heath P.D.","Ho T.P.","Hopkins B.","Horne J.","Howden P.J.","Huckle E.","Hynds C.","Johnson C.","Johnson D.","Kana A.","Kay M.","Kimberley A.M.","Kershaw J.K.","Kokkinaki M.","Laird G.K.","Lawlor S.","Lee H.M.","Leongamornlert D.A.","Laird G.","Lloyd C.","Lloyd D.M.","Loveland J.","Lovell J.","McLaren S.","McLay K.E.","McMurray A.","Mashreghi-Mohammadi M.","Matthews L.","Milne S.","Nickerson T.","Nguyen M.","Overton-Larty E.","Palmer S.A.","Pearce A.V.","Peck A.I.","Pelan S.","Phillimore B.","Porter K.","Rice C.M.","Rogosin A.","Ross M.T.","Sarafidou T.","Sehra H.K.","Shownkeen R.","Skuce C.D.","Smith M.","Standring L.","Sycamore N.","Tester J.","Thorpe A.","Torcasso W.","Tracey A.","Tromans A.","Tsolas J.","Wall M.","Walsh J.","Wang H.","Weinstock K.","West A.P.","Willey D.L.","Whitehead S.L.","Wilming L.","Wray P.W.","Young L.","Chen Y.","Lovering R.C.","Moschonas N.K.","Siebert R.","Fechtel K.","Bentley D.","Durbin R.M.","Hubbard T.","Doucette-Stamm L.","Beck S.","Smith D.R.","Rogers J."],"citationCrossReferences":[{"database":"PubMed","id":"15164054"},{"database":"DOI","id":"10.1038/nature02462"}],"title":"The DNA sequence and comparative analysis of human chromosome 10.","publicationDate":"2004","journal":"Nature","firstPage":"375","lastPage":"381","volume":"429"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]","VARIANT ILE-268"]},{"referenceNumber":7,"citation":{"id":"8777433","citationType":"journal article","authors":["Connelly M.A.","Marcu K.B."],"citationCrossReferences":[{"database":"PubMed","id":"8777433"}],"title":"CHUK, a new member of the helix-loop-helix and leucine zipper families of interacting proteins, contains a serine-threonine kinase catalytic domain.","publicationDate":"1995","journal":"Cell. Mol. Biol. Res.","firstPage":"537","lastPage":"549","volume":"41"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA] OF 32-745","VARIANT ILE-268"],"referenceComments":[{"value":"Cervix carcinoma","type":"TISSUE"}]},{"referenceNumber":8,"citation":{"id":"17116858","citationType":"journal article","authors":["Mittal R.","Peak-Chew S.Y.","McMahon H.T."],"citationCrossReferences":[{"database":"PubMed","id":"17116858"},{"database":"DOI","id":"10.1073/pnas.0608995103"}],"title":"Acetylation of MEK2 and I kappa B kinase (IKK) activation loop residues by YopJ inhibits signaling.","publicationDate":"2006","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"18574","lastPage":"18579","volume":"103"},"referencePositions":["PROTEIN SEQUENCE OF 169-181","INACTIVATION BY YERSINIA YOPJ (MICROBIAL INFECTION)","ACETYLATION AT THR-179 (MICROBIAL INFECTION)","IDENTIFICATION BY MASS SPECTROMETRY"]},{"referenceNumber":9,"citation":{"id":"9751059","citationType":"journal article","authors":["Cohen L.","Henzel W.J.","Baeuerle P.A."],"citationCrossReferences":[{"database":"PubMed","id":"9751059"},{"database":"DOI","id":"10.1038/26254"}],"title":"IKAP is a scaffold protein of the IkappaB kinase complex.","publicationDate":"1998","journal":"Nature","firstPage":"292","lastPage":"296","volume":"395"},"referencePositions":["IDENTIFICATION IN A COMPLEX WITH IKBKB; NFKBIA; RELA; ELP1 AND MAP3K14"]},{"referenceNumber":10,"citation":{"id":"9520446","citationType":"journal article","authors":["Ling L.","Cao Z.","Goeddel D.V."],"citationCrossReferences":[{"database":"PubMed","id":"9520446"},{"database":"DOI","id":"10.1073/pnas.95.7.3792"}],"title":"NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176.","publicationDate":"1998","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"3792","lastPage":"3797","volume":"95"},"referencePositions":["PHOSPHORYLATION AT SER-176","MUTAGENESIS OF SER-176; THR-179 AND SER-180"]},{"referenceNumber":11,"citation":{"id":"10485710","citationType":"journal article","authors":["Ozes O.N.","Mayo L.D.","Gustin J.A.","Pfeffer S.R.","Pfeffer L.M.","Donner D.B."],"citationCrossReferences":[{"database":"PubMed","id":"10485710"},{"database":"DOI","id":"10.1038/43466"}],"title":"NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase.","publicationDate":"1999","journal":"Nature","firstPage":"82","lastPage":"85","volume":"401"},"referencePositions":["PHOSPHORYLATION AT THR-23","MUTAGENESIS OF THR-23"]},{"referenceNumber":12,"citation":{"id":"10195894","citationType":"journal article","authors":["Delhase M.","Hayakawa M.","Chen Y.","Karin M."],"citationCrossReferences":[{"database":"PubMed","id":"10195894"},{"database":"DOI","id":"10.1126/science.284.5412.309"}],"title":"Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation.","publicationDate":"1999","journal":"Science","firstPage":"309","lastPage":"313","volume":"284"},"referencePositions":["INTERACTION WITH IKBKB"]},{"referenceNumber":13,"citation":{"id":"9819420","citationType":"journal article","authors":["Nemoto S.","DiDonato J.A.","Lin A."],"citationCrossReferences":[{"database":"PubMed","id":"9819420"},{"database":"DOI","id":"10.1128/mcb.18.12.7336"}],"title":"Coordinate regulation of IkappaB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-kappaB-inducing kinase.","publicationDate":"1998","journal":"Mol. Cell. Biol.","firstPage":"7336","lastPage":"7343","volume":"18"},"referencePositions":["IKK PHOSPHORYLATION"]},{"referenceNumber":14,"citation":{"id":"10712233","citationType":"journal article","authors":["Jobin C.","Sartor R.B."],"citationCrossReferences":[{"database":"PubMed","id":"10712233"},{"database":"DOI","id":"10.1152/ajpcell.2000.278.3.c451"}],"title":"The I kappa B/NF-kappa B system: a key determinant of mucosal inflammation and protection.","publicationDate":"2000","journal":"Am. J. Physiol.","firstPage":"C451","lastPage":"C462","volume":"278"},"referencePositions":["REVIEW"]},{"referenceNumber":15,"citation":{"id":"11971985","citationType":"journal article","authors":["Wu R.-C.","Qin J.","Hashimoto Y.","Wong J.","Xu J.","Tsai S.Y.","Tsai M.-J.","O'Malley B.W."],"citationCrossReferences":[{"database":"PubMed","id":"11971985"},{"database":"DOI","id":"10.1128/mcb.22.10.3549-3561.2002"}],"title":"Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase.","publicationDate":"2002","journal":"Mol. Cell. Biol.","firstPage":"3549","lastPage":"3561","volume":"22"},"referencePositions":["SUBUNIT OF A COMPLEX CONTAINING CREBBP; NCOA2; NCOA3; IKBKB AND IKBKG"]},{"referenceNumber":16,"citation":{"id":"12612076","citationType":"journal article","authors":["Tegethoff S.","Behlke J.","Scheidereit C."],"citationCrossReferences":[{"database":"PubMed","id":"12612076"},{"database":"DOI","id":"10.1128/mcb.23.6.2029-2041.2003"}],"title":"Tetrameric oligomerization of IkappaB kinase gamma (IKKgamma) is obligatory for IKK complex activity and NF-kappaB activation.","publicationDate":"2003","journal":"Mol. Cell. Biol.","firstPage":"2029","lastPage":"2041","volume":"23"},"referencePositions":["COMPOSITION OF THE IKK COMPLEX"]},{"referenceNumber":17,"citation":{"id":"12789342","citationType":"journal article","authors":["Yamamoto Y.","Verma U.N.","Prajapati S.","Kwak Y.T.","Gaynor R.B."],"citationCrossReferences":[{"database":"PubMed","id":"12789342"},{"database":"DOI","id":"10.1038/nature01576"}],"title":"Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression.","publicationDate":"2003","journal":"Nature","firstPage":"655","lastPage":"659","volume":"423"},"referencePositions":["SUBCELLULAR LOCATION","FUNCTION IN PHOSPHORYLATION OF HISTONE H3"]},{"referenceNumber":18,"citation":{"id":"15084260","citationType":"journal article","authors":["Hu M.C.","Lee D.F.","Xia W.","Golfman L.S.","Ou-Yang F.","Yang J.Y.","Zou Y.","Bao S.","Hanada N.","Saso H.","Kobayashi R.","Hung M.C."],"citationCrossReferences":[{"database":"PubMed","id":"15084260"},{"database":"DOI","id":"10.1016/s0092-8674(04)00302-2"}],"title":"IkappaB kinase promotes tumorigenesis through inhibition of forkhead FOXO3a.","publicationDate":"2004","journal":"Cell","firstPage":"225","lastPage":"237","volume":"117"},"referencePositions":["FUNCTION","INTERACTION WITH FOXO3"]},{"referenceNumber":19,"citation":{"id":"15456791","citationType":"journal article","authors":["Bruey J.-M.","Bruey-Sedano N.","Newman R.","Chandler S.","Stehlik C.","Reed J.C."],"citationCrossReferences":[{"database":"PubMed","id":"15456791"},{"database":"DOI","id":"10.1074/jbc.m406741200"}],"title":"PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates NF-kappaB and caspase-1 activation in macrophages.","publicationDate":"2004","journal":"J. Biol. Chem.","firstPage":"51897","lastPage":"51907","volume":"279"},"referencePositions":["INTERACTION WITH NALP2"]},{"referenceNumber":20,"citation":{"id":"15173580","citationType":"journal article","authors":["Witherow D.S.","Garrison T.R.","Miller W.E.","Lefkowitz R.J."],"citationCrossReferences":[{"database":"PubMed","id":"15173580"},{"database":"DOI","id":"10.1073/pnas.0402851101"}],"title":"beta-Arrestin inhibits NF-kappaB activity by means of its interaction with the NF-kappaB inhibitor IkappaBalpha.","publicationDate":"2004","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"8603","lastPage":"8607","volume":"101"},"referencePositions":["INTERACTION WITH ARRB1 AND ARRB2"]},{"referenceNumber":21,"citation":{"id":"16177806","citationType":"journal article","authors":["Meylan E.","Curran J.","Hofmann K.","Moradpour D.","Binder M.","Bartenschlager R.","Tschopp J."],"citationCrossReferences":[{"database":"PubMed","id":"16177806"},{"database":"DOI","id":"10.1038/nature04193"}],"title":"Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus.","publicationDate":"2005","journal":"Nature","firstPage":"1167","lastPage":"1172","volume":"437"},"referencePositions":["INTERACTION WITH MAVS"]},{"referenceNumber":22,"citation":{"id":"17540171","citationType":"journal article","authors":["Liu B.","Yang Y.","Chernishof V.","Loo R.R.","Jang H.","Tahk S.","Yang R.","Mink S.","Shultz D.","Bellone C.J.","Loo J.A.","Shuai K."],"citationCrossReferences":[{"database":"PubMed","id":"17540171"},{"database":"DOI","id":"10.1016/j.cell.2007.03.056"}],"title":"Proinflammatory stimuli induce IKKalpha-mediated phosphorylation of PIAS1 to restrict inflammation and immunity.","publicationDate":"2007","journal":"Cell","firstPage":"903","lastPage":"914","volume":"129"},"referencePositions":["INTERACTION WITH PIAS1"]},{"referenceNumber":23,"citation":{"id":"17434128","citationType":"journal article","authors":["Huang W.C.","Ju T.K.","Hung M.C.","Chen C.C."],"citationCrossReferences":[{"database":"PubMed","id":"17434128"},{"database":"DOI","id":"10.1016/j.molcel.2007.02.019"}],"title":"Phosphorylation of CBP by IKKalpha promotes cell growth by switching the binding preference of CBP from p53 to NF-kappaB.","publicationDate":"2007","journal":"Mol. Cell","firstPage":"75","lastPage":"87","volume":"26"},"referencePositions":["FUNCTION IN PHOSPHORYLATION OF CREBBP"]},{"referenceNumber":24,"citation":{"id":"18626576","citationType":"journal article","authors":["Solt L.A.","May M.J."],"citationCrossReferences":[{"database":"PubMed","id":"18626576"},{"database":"DOI","id":"10.1007/s12026-008-8025-1"}],"title":"The IkappaB kinase complex: master regulator of NF-kappaB signaling.","publicationDate":"2008","journal":"Immunol. Res.","firstPage":"3","lastPage":"18","volume":"42"},"referencePositions":["REVIEW","DOMAIN"]},{"referenceNumber":25,"citation":{"id":"19088076","citationType":"journal article","authors":["Tai D.J.","Su C.C.","Ma Y.L.","Lee E.H."],"citationCrossReferences":[{"database":"PubMed","id":"19088076"},{"database":"DOI","id":"10.1074/jbc.m805055200"}],"title":"SGK1 phosphorylation of IkappaB Kinase alpha and p300 Up-regulates NF-kappaB activity and increases N-Methyl-D-aspartate receptor NR2A and NR2B expression.","publicationDate":"2009","journal":"J. Biol. Chem.","firstPage":"4073","lastPage":"4089","volume":"284"},"referencePositions":["PHOSPHORYLATION AT THR-23 AND SER-180 BY SGK1"]},{"referenceNumber":26,"citation":{"id":"19150425","citationType":"journal article","authors":["Li S.","Wang L.","Dorf M.E."],"citationCrossReferences":[{"database":"PubMed","id":"19150425"},{"database":"DOI","id":"10.1016/j.molcel.2008.11.023"}],"title":"PKC phosphorylation of TRAF2 mediates IKKalpha/beta recruitment and K63-linked polyubiquitination.","publicationDate":"2009","journal":"Mol. Cell","firstPage":"30","lastPage":"42","volume":"33"},"referencePositions":["INTERACTION WITH TRAF2"]},{"referenceNumber":27,"citation":{"id":"20434986","citationType":"journal article","authors":["Cui J.","Zhu L.","Xia X.","Wang H.Y.","Legras X.","Hong J.","Ji J.","Shen P.","Zheng S.","Chen Z.J.","Wang R.F."],"citationCrossReferences":[{"database":"PubMed","id":"20434986"},{"database":"DOI","id":"10.1016/j.cell.2010.03.040"}],"title":"NLRC5 negatively regulates the NF-kappaB and type I interferon signaling pathways.","publicationDate":"2010","journal":"Cell","firstPage":"483","lastPage":"496","volume":"141"},"referencePositions":["FUNCTION","INTERACTION WITH NLRC5"]},{"referenceNumber":28,"citation":{"id":"20855622","citationType":"journal article","authors":["Gouin E.","Adib-Conquy M.","Balestrino D.","Nahori M.A.","Villiers V.","Colland F.","Dramsi S.","Dussurget O.","Cossart P."],"citationCrossReferences":[{"database":"PubMed","id":"20855622"},{"database":"DOI","id":"10.1073/pnas.1007765107"}],"title":"The Listeria monocytogenes InlC protein interferes with innate immune responses by targeting the I{kappa}B kinase subunit IKK{alpha}.","publicationDate":"2010","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"17333","lastPage":"17338","volume":"107"},"referencePositions":["INTERACTION WITH L.MONOCYTOGENES INLC (MICROBIAL INFECTION)"]},{"referenceNumber":29,"citation":{"id":"20961246","citationType":"journal article","authors":["Lahtela J.","Nousiainen H.O.","Stefanovic V.","Tallila J.","Viskari H.","Karikoski R.","Gentile M.","Saloranta C.","Varilo T.","Salonen R.","Kestila M."],"citationCrossReferences":[{"database":"PubMed","id":"20961246"},{"database":"DOI","id":"10.1056/nejmoa0911698"}],"title":"Mutant CHUK and severe fetal encasement malformation.","publicationDate":"2010","journal":"N. Engl. J. Med.","firstPage":"1631","lastPage":"1637","volume":"363"},"referencePositions":["INVOLVEMENT IN COCOS"]},{"referenceNumber":30,"citation":{"id":"20501937","citationType":"journal article","authors":["Razani B.","Zarnegar B.","Ytterberg A.J.","Shiba T.","Dempsey P.W.","Ware C.F.","Loo J.A.","Cheng G."],"citationCrossReferences":[{"database":"PubMed","id":"20501937"},{"database":"DOI","id":"10.1126/scisignal.2000778"}],"title":"Negative feedback in noncanonical NF-kappaB signaling modulates NIK stability through IKKalpha-mediated phosphorylation.","publicationDate":"2010","journal":"Sci. Signal.","firstPage":"RA41","lastPage":"RA41","volume":"3"},"referencePositions":["FUNCTION IN MAP3K14 PHOSPHORYLATION"]},{"referenceNumber":31,"citation":{"id":"21269460","citationType":"journal article","authors":["Burkard T.R.","Planyavsky M.","Kaupe I.","Breitwieser F.P.","Buerckstuemmer T.","Bennett K.L.","Superti-Furga G.","Colinge J."],"citationCrossReferences":[{"database":"PubMed","id":"21269460"},{"database":"DOI","id":"10.1186/1752-0509-5-17"}],"title":"Initial characterization of the human central proteome.","publicationDate":"2011","journal":"BMC Syst. Biol.","firstPage":"17","lastPage":"17","volume":"5"},"referencePositions":["IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]"]},{"referenceNumber":32,"citation":{"id":"21765415","citationType":"journal article","authors":["Shembade N.","Pujari R.","Harhaj N.S.","Abbott D.W.","Harhaj E.W."],"citationCrossReferences":[{"database":"PubMed","id":"21765415"},{"database":"DOI","id":"10.1038/ni.2066"}],"title":"The kinase IKKalpha inhibits activation of the transcription factor NF-kappaB by phosphorylating the regulatory molecule TAX1BP1.","publicationDate":"2011","journal":"Nat. Immunol.","firstPage":"834","lastPage":"843","volume":"12"},"referencePositions":["FUNCTION IN PHOSPHORYLATION OF TAX1BP1"]},{"referenceNumber":33,"citation":{"id":"23091055","citationType":"journal article","authors":["Wang W.","Guo M.","Hu L.","Cai J.","Zeng Y.","Luo J.","Shu Z.","Li W.","Huang Z."],"citationCrossReferences":[{"database":"PubMed","id":"23091055"},{"database":"DOI","id":"10.1074/jbc.m112.399923"}],"title":"The zinc finger protein ZNF268 is overexpressed in human cervical cancer and contributes to tumorigenesis via enhancing NF-kappaB signaling.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"42856","lastPage":"42866","volume":"287"},"referencePositions":["INTERACTION WITH ZNF268","SUBUNIT"]},{"referenceNumber":34,"citation":{"id":"23776175","citationType":"journal article","authors":["Dauphinee S.M.","Clayton A.","Hussainkhel A.","Yang C.","Park Y.J.","Fuller M.E.","Blonder J.","Veenstra T.D.","Karsan A."],"citationCrossReferences":[{"database":"PubMed","id":"23776175"},{"database":"DOI","id":"10.4049/jimmunol.1200583"}],"title":"SASH1 is a scaffold molecule in endothelial TLR4 signaling.","publicationDate":"2013","journal":"J. Immunol.","firstPage":"892","lastPage":"901","volume":"191"},"referencePositions":["INTERACTION WITH SASH1"]},{"referenceNumber":35,"citation":{"id":"26334375","citationType":"journal article","authors":["Zheng C.","Zheng Z.","Zhang Z.","Meng J.","Liu Y.","Ke X.","Hu Q.","Wang H."],"citationCrossReferences":[{"database":"PubMed","id":"26334375"},{"database":"DOI","id":"10.1016/j.cellsig.2015.08.018"}],"title":"IFIT5 positively regulates NF-kappaB signaling through synergizing the recruitment of IkappaB kinase (IKK) to TGF-beta-activated kinase 1 (TAK1).","publicationDate":"2015","journal":"Cell. Signal.","firstPage":"2343","lastPage":"2354","volume":"27"},"referencePositions":["INTERACTION WITH IFIT5"]},{"referenceNumber":36,"citation":{"id":"27426725","citationType":"journal article","authors":["Wu C.","Yang Y.","Ou J.","Zhu L.","Zhao W.","Cui J."],"citationCrossReferences":[{"database":"PubMed","id":"27426725"},{"database":"DOI","id":"10.1016/j.yexcr.2016.07.011"}],"title":"LRRC14 attenuates Toll-like receptor-mediated NF-kappa-B signaling through disruption of IKK complex.","publicationDate":"2016","journal":"Exp. Cell Res.","firstPage":"65","lastPage":"73","volume":"347"},"referencePositions":["INTERACTION WITH LRRC14"]},{"referenceNumber":37,"citation":{"id":"30341167","citationType":"journal article","authors":["Fullam A.","Gu L.","Hoehn Y.","Schroeder M."],"citationCrossReferences":[{"database":"PubMed","id":"30341167"},{"database":"DOI","id":"10.1042/bcj20180163"}],"title":"DDX3 directly facilitates IKKalpha activation and regulates downstream signalling pathways.","publicationDate":"2018","journal":"Biochem. J.","firstPage":"3595","lastPage":"3607","volume":"475"},"referencePositions":["INTERACTION WITH DDX3X","SUBCELLULAR LOCATION"]},{"referenceNumber":38,"citation":{"id":"30217973","citationType":"journal article","authors":["Di Rita A.","Peschiaroli A.","D'Acunzo P.","Strobbe D.","Hu Z.","Gruber J.","Nygaard M.","Lambrughi M.","Melino G.","Papaleo E.","Dengjel J.","El Alaoui S.","Campanella M.","Doetsch V.","Rogov V.V.","Strappazzon F.","Cecconi F."],"citationCrossReferences":[{"database":"PubMed","id":"30217973"},{"database":"DOI","id":"10.1038/s41467-018-05722-3"}],"title":"HUWE1 E3 ligase promotes PINK1/PARKIN-independent mitophagy by regulating AMBRA1 activation via IKKalpha.","publicationDate":"2018","journal":"Nat. Commun.","firstPage":"3755","lastPage":"3755","volume":"9"},"referencePositions":["FUNCTION"]},{"referenceNumber":39,"citation":{"id":"32935379","citationType":"journal article","authors":["Chathuranga K.","Kim T.H.","Lee H.","Park J.S.","Kim J.H.","Chathuranga W.A.G.","Ekanayaka P.","Choi Y.J.","Lee C.H.","Kim C.J.","Jung J.U.","Lee J.S."],"citationCrossReferences":[{"database":"PubMed","id":"32935379"},{"database":"DOI","id":"10.15252/embj.2020105139"}],"title":"Negative regulation of NEMO signaling by the ubiquitin E3 ligase MARCH2.","publicationDate":"2020","journal":"EMBO J.","firstPage":"e105139","lastPage":"e105139","volume":"39"},"referencePositions":["IDENTIFICATION IN THE IKK COMPLEX"]},{"referenceNumber":40,"citation":{"id":"35952808","citationType":"journal article","authors":["Liu Y.","Chen Y.","Ding C.","Zhu X.","Song X.","Ren Y.","Wang Q.","Zhang Y.","Sun X."],"citationCrossReferences":[{"database":"PubMed","id":"35952808"},{"database":"DOI","id":"10.1016/j.ijbiomac.2022.08.019"}],"title":"TRIM56 positively regulates TNFalpha-induced NF-kappaB signaling by enhancing the ubiquitination of TAK1.","publicationDate":"2022","journal":"Int. J. Biol. Macromol.","firstPage":"571","lastPage":"578","volume":"219"},"referencePositions":["FUNCTION","UBIQUITINATION BY TRIM56"]},{"referenceNumber":41,"citation":{"id":"25691407","citationType":"journal article","authors":["Leslie E.J.","O'Sullivan J.","Cunningham M.L.","Singh A.","Goudy S.L.","Ababneh F.","Alsubaie L.","Ch'ng G.S.","van der Laar I.M.","Hoogeboom A.J.","Dunnwald M.","Kapoor S.","Jiramongkolchai P.","Standley J.","Manak J.R.","Murray J.C.","Dixon M.J."],"citationCrossReferences":[{"database":"PubMed","id":"25691407"},{"database":"DOI","id":"10.1002/ajmg.a.36896"}],"title":"Expanding the genetic and phenotypic spectrum of popliteal pterygium disorders.","publicationDate":"2015","journal":"Am. J. Med. Genet. A","firstPage":"545","lastPage":"552","volume":"167A"},"referencePositions":["INVOLVEMENT IN BPS2"]},{"referenceNumber":42,"citation":{"id":"17344846","citationType":"journal article","authors":["Greenman C.","Stephens P.","Smith R.","Dalgliesh G.L.","Hunter C.","Bignell G.","Davies H.","Teague J.","Butler A.","Stevens C.","Edkins S.","O'Meara S.","Vastrik I.","Schmidt E.E.","Avis T.","Barthorpe S.","Bhamra G.","Buck G.","Choudhury B.","Clements J.","Cole J.","Dicks E.","Forbes S.","Gray K.","Halliday K.","Harrison R.","Hills K.","Hinton J.","Jenkinson A.","Jones D.","Menzies A.","Mironenko T.","Perry J.","Raine K.","Richardson D.","Shepherd R.","Small A.","Tofts C.","Varian J.","Webb T.","West S.","Widaa S.","Yates A.","Cahill D.P.","Louis D.N.","Goldstraw P.","Nicholson A.G.","Brasseur F.","Looijenga L.","Weber B.L.","Chiew Y.-E.","DeFazio A.","Greaves M.F.","Green A.R.","Campbell P.","Birney E.","Easton D.F.","Chenevix-Trench G.","Tan M.-H.","Khoo S.K.","Teh B.T.","Yuen S.T.","Leung S.Y.","Wooster R.","Futreal P.A.","Stratton M.R."],"citationCrossReferences":[{"database":"PubMed","id":"17344846"},{"database":"DOI","id":"10.1038/nature05610"}],"title":"Patterns of somatic mutation in human cancer genomes.","publicationDate":"2007","journal":"Nature","firstPage":"153","lastPage":"158","volume":"446"},"referencePositions":["VARIANTS [LARGE SCALE ANALYSIS] CYS-126; ALA-155 AND ILE-268"]},{"referenceNumber":43,"citation":{"id":"18462684","citationType":"journal article","authors":["Rushe M.","Silvian L.","Bixler S.","Chen L.L.","Cheung A.","Bowes S.","Cuervo H.","Berkowitz S.","Zheng T.","Guckian K.","Pellegrini M.","Lugovskoy A."],"citationCrossReferences":[{"database":"PubMed","id":"18462684"},{"database":"DOI","id":"10.1016/j.str.2008.02.012"}],"title":"Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site.","publicationDate":"2008","journal":"Structure","firstPage":"798","lastPage":"808","volume":"16"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 732-745"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF012890","properties":[{"key":"ProteinId","value":"AAC51662.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"AF009225","properties":[{"key":"ProteinId","value":"AAC51671.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"AF080157","properties":[{"key":"ProteinId","value":"AAD08996.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"AY652653","properties":[{"key":"ProteinId","value":"AAT49098.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AL138921","properties":[{"key":"ProteinId","value":"-"},{"key":"Status","value":"NOT_ANNOTATED_CDS"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"U22512","properties":[{"key":"ProteinId","value":"AAC50713.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"CCDS","id":"CCDS7488.1","properties":[{"key":"Description","value":"-"}]},{"database":"RefSeq","id":"NP_001269.3","properties":[{"key":"NucleotideSequenceId","value":"NM_001278.5"}]},{"database":"PDB","id":"3BRT","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.25 A"},{"key":"Chains","value":"A/C=732-745"}]},{"database":"PDB","id":"5EBZ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"4.50 A"},{"key":"Chains","value":"A/B/C/D/E/F/G/H/I/J/K/L=10-660"}]},{"database":"PDB","id":"5TQW","properties":[{"key":"Method","value":"EM"},{"key":"Resolution","value":"5.60 A"},{"key":"Chains","value":"A/B=10-660"}]},{"database":"PDB","id":"5TQX","properties":[{"key":"Method","value":"EM"},{"key":"Resolution","value":"5.40 A"},{"key":"Chains","value":"A/B=10-660"}]},{"database":"PDB","id":"5TQY","properties":[{"key":"Method","value":"EM"},{"key":"Resolution","value":"5.20 A"},{"key":"Chains","value":"A/B=10-660"}]},{"database":"PDBsum","id":"3BRT","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5EBZ","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5TQW","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5TQX","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5TQY","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"EMDB","id":"EMD-8436","properties":[{"key":"Description","value":"-"}]},{"database":"EMDB","id":"EMD-8437","properties":[{"key":"Description","value":"-"}]},{"database":"EMDB","id":"EMD-8438","properties":[{"key":"Description","value":"-"}]},{"database":"EMDB","id":"EMD-8439","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"107569","properties":[{"key":"Interactions","value":"239"}]},{"database":"ComplexPortal","id":"CPX-3269","properties":[{"key":"EntryName","value":"IkappaB kinase complex"}]},{"database":"CORUM","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"DIP","id":"DIP-27526N","properties":[{"key":"Description","value":"-"}]},{"database":"ELM","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"O15111","properties":[{"key":"Number of interactors","value":"2633"}]},{"database":"IntAct","id":"O15111","properties":[{"key":"Interactions","value":"118"}]},{"database":"MINT","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"NDEx","id":"IQUERY-CP-CHUK","properties":[{"key":"Evidences","value":"93 NDEx IQuery Curated Pathways"}]},{"database":"STRING","id":"9606.ENSP00000359424","properties":[{"key":"Description","value":"-"}]},{"database":"BindingDB","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"ChEMBL","id":"CHEMBL3476","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB06151","properties":[{"key":"GenericName","value":"Acetylcysteine"}]},{"database":"DrugBank","id":"DB00233","properties":[{"key":"GenericName","value":"Aminosalicylic acid"}]},{"database":"DrugBank","id":"DB00244","properties":[{"key":"GenericName","value":"Mesalazine"}]},{"database":"DrugBank","id":"DB00795","properties":[{"key":"GenericName","value":"Sulfasalazine"}]},{"database":"DrugCentral","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"GuidetoPHARMACOLOGY","id":"1989","properties":[{"key":"Description","value":"-"}]},{"database":"GlyGen","id":"O15111","properties":[{"key":"glycosylation","value":"3 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (2 sites)"}]},{"database":"iPTMnet","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"PhosphoSitePlus","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"BioMuta","id":"CHUK","properties":[{"key":"Description","value":"-"}]},{"database":"CPTAC","id":"CPTAC-1220","properties":[{"key":"Description","value":"-"}]},{"database":"CPTAC","id":"CPTAC-1221","properties":[{"key":"Description","value":"-"}]},{"database":"CPTAC","id":"CPTAC-2837","properties":[{"key":"Description","value":"-"}]},{"database":"CPTAC","id":"CPTAC-3087","properties":[{"key":"Description","value":"-"}]},{"database":"jPOST","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"MassIVE","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"9606-ENSP00000359424","properties":[{"key":"Description","value":"-"}]},{"database":"PeptideAtlas","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"ProteomicsDB","id":"48449","properties":[{"key":"Description","value":"-"}]},{"database":"Pumba","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"Antibodypedia","id":"801","properties":[{"key":"antibodies","value":"1480 antibodies from 54 providers"}]},{"database":"DNASU","id":"1147","properties":[{"key":"Description","value":"-"}]},{"database":"Ensembl","id":"ENST00000370397.8","properties":[{"key":"ProteinId","value":"ENSP00000359424.6"},{"key":"GeneId","value":"ENSG00000213341.12"}]},{"database":"GeneID","id":"1147","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"hsa:1147","properties":[{"key":"Description","value":"-"}]},{"database":"MANE-Select","id":"ENST00000370397.8","properties":[{"key":"ProteinId","value":"ENSP00000359424.6"},{"key":"RefSeqNucleotideId","value":"NM_001278.5"},{"key":"RefSeqProteinId","value":"NP_001269.3"}]},{"database":"UCSC","id":"uc001kqp.4","properties":[{"key":"OrganismName","value":"human"}]},{"database":"AGR","id":"HGNC:1974","properties":[{"key":"Description","value":"-"}]},{"database":"ClinPGx","id":"PA26510","properties":[{"key":"Description","value":"-"}]},{"database":"CTD","id":"1147","properties":[{"key":"Description","value":"-"}]},{"database":"DisGeNET","id":"1147","properties":[{"key":"Description","value":"-"}]},{"database":"GeneCards","id":"CHUK","properties":[{"key":"Description","value":"-"}]},{"database":"HGNC","id":"HGNC:1974","properties":[{"key":"GeneName","value":"CHUK"}]},{"database":"HPA","id":"ENSG00000213341","properties":[{"key":"ExpressionPatterns","value":"Low tissue specificity"}]},{"database":"MalaCards","id":"CHUK","properties":[{"key":"Description","value":"-"}]},{"database":"MIM","id":"600664","properties":[{"key":"Type","value":"gene"}]},{"database":"MIM","id":"613630","properties":[{"key":"Type","value":"phenotype"}]},{"database":"MIM","id":"619339","properties":[{"key":"Type","value":"phenotype"}]},{"database":"OpenTargets","id":"ENSG00000213341","properties":[{"key":"Description","value":"-"}]},{"database":"Orphanet","id":"697403","properties":[{"key":"Disease","value":"Combined immunodeficiency-hypogammaglobulinemia-skeletal anomalies syndrome due to IKBKA deficiency"}]},{"database":"Orphanet","id":"465824","properties":[{"key":"Disease","value":"Fetal encasement syndrome"}]},{"database":"VEuPathDB","id":"HostDB:ENSG00000213341","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"KOG4250","properties":[{"key":"ToxonomicScope","value":"Eukaryota"}]},{"database":"GeneTree","id":"ENSGT00950000182937","properties":[{"key":"Description","value":"-"}]},{"database":"HOGENOM","id":"CLU_000288_101_2_1","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"FILMDHI","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"267381at2759","properties":[{"key":"Description","value":"-"}]},{"database":"PAN-GO","id":"O15111","properties":[{"key":"Number of GO annotations","value":"6 GO annotations based on evolutionary models"}]},{"database":"PhylomeDB","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.7.11.10","properties":[{"key":"OrganismId","value":"2681"}]},{"database":"PathwayCommons","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"Reactome","id":"R-HSA-1169091","properties":[{"key":"PathwayName","value":"Activation of NF-kappaB in B cells"}]},{"database":"Reactome","id":"R-HSA-1236974","properties":[{"key":"PathwayName","value":"ER-Phagosome pathway"}]},{"database":"Reactome","id":"R-HSA-168638","properties":[{"key":"PathwayName","value":"NOD1/2 Signaling Pathway"}]},{"database":"Reactome","id":"R-HSA-168927","properties":[{"key":"PathwayName","value":"TICAM1, RIP1-mediated IKK complex recruitment"}]},{"database":"Reactome","id":"R-HSA-1810476","properties":[{"key":"PathwayName","value":"RIP-mediated NFkB activation via ZBP1"}]},{"database":"Reactome","id":"R-HSA-198323","properties":[{"key":"PathwayName","value":"AKT phosphorylates targets in the cytosol"}]},{"database":"Reactome","id":"R-HSA-202424","properties":[{"key":"PathwayName","value":"Downstream TCR signaling"}]},{"database":"Reactome","id":"R-HSA-2871837","properties":[{"key":"PathwayName","value":"FCERI mediated NF-kB activation"}]},{"database":"Reactome","id":"R-HSA-445989","properties":[{"key":"PathwayName","value":"TAK1-dependent IKK and NF-kappa-B activation"}]},{"database":"Reactome","id":"R-HSA-5357905","properties":[{"key":"PathwayName","value":"Regulation of TNFR1 signaling"}]},{"database":"Reactome","id":"R-HSA-5357956","properties":[{"key":"PathwayName","value":"TNFR1-induced NF-kappa-B signaling pathway"}]},{"database":"Reactome","id":"R-HSA-5602636","properties":[{"key":"PathwayName","value":"IKBKB deficiency causes SCID"}]},{"database":"Reactome","id":"R-HSA-5603027","properties":[{"key":"PathwayName","value":"IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR)"}]},{"database":"Reactome","id":"R-HSA-5603029","properties":[{"key":"PathwayName","value":"IkBA variant leads to EDA-ID"}]},{"database":"Reactome","id":"R-HSA-5607761","properties":[{"key":"PathwayName","value":"Dectin-1 mediated noncanonical NF-kB signaling"}]},{"database":"Reactome","id":"R-HSA-5607764","properties":[{"key":"PathwayName","value":"CLEC7A (Dectin-1) signaling"}]},{"database":"Reactome","id":"R-HSA-5674400","properties":[{"key":"PathwayName","value":"Constitutive Signaling by AKT1 E17K in Cancer"}]},{"database":"Reactome","id":"R-HSA-5676590","properties":[{"key":"PathwayName","value":"NIK-->noncanonical NF-kB signaling"}]},{"database":"Reactome","id":"R-HSA-5684264","properties":[{"key":"PathwayName","value":"MAP3K8 (TPL2)-dependent MAPK1/3 activation"}]},{"database":"Reactome","id":"R-HSA-9020702","properties":[{"key":"PathwayName","value":"Interleukin-1 signaling"}]},{"database":"Reactome","id":"R-HSA-933542","properties":[{"key":"PathwayName","value":"TRAF6 mediated NF-kB activation"}]},{"database":"Reactome","id":"R-HSA-933543","properties":[{"key":"PathwayName","value":"NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10"}]},{"database":"Reactome","id":"R-HSA-937039","properties":[{"key":"PathwayName","value":"IRAK1 recruits IKK complex"}]},{"database":"Reactome","id":"R-HSA-937041","properties":[{"key":"PathwayName","value":"IKK complex recruitment mediated by RIP1"}]},{"database":"Reactome","id":"R-HSA-9705671","properties":[{"key":"PathwayName","value":"SARS-CoV-2 activates/modulates innate and adaptive immune responses"}]},{"database":"Reactome","id":"R-HSA-975144","properties":[{"key":"PathwayName","value":"IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation"}]},{"database":"Reactome","id":"R-HSA-9758274","properties":[{"key":"PathwayName","value":"Regulation of NF-kappa B signaling"}]},{"database":"Reactome","id":"R-HSA-9833482","properties":[{"key":"PathwayName","value":"PKR-mediated signaling"}]},{"database":"Reactome","id":"R-HSA-9860276","properties":[{"key":"PathwayName","value":"SLC15A4:TASL-dependent IRF5 activation"}]},{"database":"Reactome","id":"R-HSA-9860927","properties":[{"key":"PathwayName","value":"Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZO1 and integrins in endothelial cells"}]},{"database":"Reactome","id":"R-HSA-9909505","properties":[{"key":"PathwayName","value":"Modulation of host responses by IFN-stimulated genes"}]},{"database":"SABIO-RK","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"SignaLink","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"SIGNOR","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"Agora","id":"ENSG00000213341","properties":[{"key":"NominatedTarget","value":"-"}]},{"database":"BioGRID-ORCS","id":"1147","properties":[{"key":"hits","value":"43 hits in 1198 CRISPR screens"}]},{"database":"CD-CODE","id":"8C2F96ED","properties":[{"key":"EntryName","value":"Centrosome"}]},{"database":"ChiTaRS","id":"CHUK","properties":[{"key":"OrganismName","value":"human"}]},{"database":"EvolutionaryTrace","id":"O15111","properties":[{"key":"Description","value":"-"}]},{"database":"GeneWiki","id":"CHUK","properties":[{"key":"Description","value":"-"}]},{"database":"GenomeRNAi","id":"1147","properties":[{"key":"Description","value":"-"}]},{"database":"Pharos","id":"O15111","properties":[{"key":"DevelopmentLevel","value":"Tchem"}]},{"database":"PRO","id":"PR:O15111","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000005640","properties":[{"key":"Component","value":"Chromosome 10"}]},{"database":"RNAct","id":"O15111","properties":[{"key":"moleculeType","value":"protein"}]},{"database":"Bgee","id":"ENSG00000213341","properties":[{"key":"ExpressionPatterns","value":"Expressed in secondary oocyte and 197 other cell types or tissues"}]},{"database":"GO","id":"GO:0035631","properties":[{"key":"GoTerm","value":"C:CD40 receptor complex"},{"key":"GoEvidenceType","value":"ISS:BHF-UCL"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"30341167"}]},{"database":"GO","id":"GO:0009898","properties":[{"key":"GoTerm","value":"C:cytoplasmic side of plasma membrane"},{"key":"GoEvidenceType","value":"ISS:BHF-UCL"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IDA:HPA"}]},{"database":"GO","id":"GO:0008385","properties":[{"key":"GoTerm","value":"C:IkappaB kinase complex"},{"key":"GoEvidenceType","value":"IPI:ComplexPortal"}],"evidences":[{"evidenceCode":"ECO:0000353","source":"PubMed","id":"20434986"}]},{"database":"GO","id":"GO:0005654","properties":[{"key":"GoTerm","value":"C:nucleoplasm"},{"key":"GoEvidenceType","value":"IDA:HPA"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12789342"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008384","properties":[{"key":"GoTerm","value":"F:IkappaB kinase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"9244310"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"9252186"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"9346484"}]},{"database":"GO","id":"GO:0046982","properties":[{"key":"GoTerm","value":"F:protein heterodimerization activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"23091055"}]},{"database":"GO","id":"GO:0042803","properties":[{"key":"GoTerm","value":"F:protein homodimerization activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"23091055"}]},{"database":"GO","id":"GO:0004672","properties":[{"key":"GoTerm","value":"F:protein kinase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"20434986"}]},{"database":"GO","id":"GO:0004674","properties":[{"key":"GoTerm","value":"F:protein serine/threonine kinase activity"},{"key":"GoEvidenceType","value":"IDA:ARUK-UCL"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"12656673"}]},{"database":"GO","id":"GO:0044877","properties":[{"key":"GoTerm","value":"F:protein-containing complex binding"},{"key":"GoEvidenceType","value":"IEA:Ensembl"}]},{"database":"GO","id":"GO:0097110","properties":[{"key":"GoTerm","value":"F:scaffold protein binding"},{"key":"GoEvidenceType","value":"IDA:MGI"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"23776175"}]},{"database":"GO","id":"GO:1990459","properties":[{"key":"GoTerm","value":"F:transferrin receptor binding"},{"key":"GoEvidenceType","value":"IPI:ARUK-UCL"}],"evidences":[{"evidenceCode":"ECO:0000353","source":"PubMed","id":"23016877"}]},{"database":"GO","id":"GO:0009653","properties":[{"key":"GoTerm","value":"P:anatomical structure morphogenesis"},{"key":"GoEvidenceType","value":"TAS:ProtInc"}],"evidences":[{"evidenceCode":"ECO:0000304","source":"PubMed","id":"10747982"}]},{"database":"GO","id":"GO:0007249","properties":[{"key":"GoTerm","value":"P:canonical NF-kappaB signal transduction"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"9244310"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"9252186"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"9346484"}]},{"database":"GO","id":"GO:0071356","properties":[{"key":"GoTerm","value":"P:cellular response to tumor necrosis factor"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"23091055"}]},{"database":"GO","id":"GO:0098586","properties":[{"key":"GoTerm","value":"P:cellular response to virus"},{"key":"GoEvidenceType","value":"IMP:CAFA"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"24784232"}]},{"database":"GO","id":"GO:0006955","properties":[{"key":"GoTerm","value":"P:immune response"},{"key":"GoEvidenceType","value":"TAS:ProtInc"}],"evidences":[{"evidenceCode":"ECO:0000304","source":"PubMed","id":"9346484"}]},{"database":"GO","id":"GO:0006954","properties":[{"key":"GoTerm","value":"P:inflammatory response"},{"key":"GoEvidenceType","value":"TAS:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000304","source":"PubMed","id":"18626576"}]},{"database":"GO","id":"GO:0045087","properties":[{"key":"GoTerm","value":"P:innate immune response"},{"key":"GoEvidenceType","value":"TAS:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000304","source":"PubMed","id":"18626576"}]},{"database":"GO","id":"GO:0038061","properties":[{"key":"GoTerm","value":"P:non-canonical NF-kappaB signal transduction"},{"key":"GoEvidenceType","value":"IDA:UniProt"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"26189595"}]},{"database":"GO","id":"GO:0043123","properties":[{"key":"GoTerm","value":"P:positive regulation of canonical NF-kappaB signal transduction"},{"key":"GoEvidenceType","value":"IDA:ARUK-UCL"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"12656673"}]},{"database":"GO","id":"GO:0032727","properties":[{"key":"GoTerm","value":"P:positive regulation of interferon-alpha production"},{"key":"GoEvidenceType","value":"IMP:CAFA"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"24784232"}]},{"database":"GO","id":"GO:0045944","properties":[{"key":"GoTerm","value":"P:positive regulation of transcription by RNA polymerase II"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"23091055"}]},{"database":"GO","id":"GO:0010034","properties":[{"key":"GoTerm","value":"P:response to acetate"},{"key":"GoEvidenceType","value":"IEA:Ensembl"}]},{"database":"GO","id":"GO:0043200","properties":[{"key":"GoTerm","value":"P:response to amino acid"},{"key":"GoEvidenceType","value":"IEA:Ensembl"}]},{"database":"GO","id":"GO:0061847","properties":[{"key":"GoTerm","value":"P:response to cholecystokinin"},{"key":"GoEvidenceType","value":"IEA:Ensembl"}]},{"database":"GO","id":"GO:0033194","properties":[{"key":"GoTerm","value":"P:response to hydroperoxide"},{"key":"GoEvidenceType","value":"IEA:Ensembl"}]},{"database":"GO","id":"GO:0009636","properties":[{"key":"GoTerm","value":"P:response to toxic substance"},{"key":"GoEvidenceType","value":"IEA:Ensembl"}]},{"database":"GO","id":"GO:0009615","properties":[{"key":"GoTerm","value":"P:response to virus"},{"key":"GoEvidenceType","value":"TAS:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000304","source":"PubMed","id":"18626576"}]},{"database":"GO","id":"GO:0009410","properties":[{"key":"GoTerm","value":"P:response to xenobiotic stimulus"},{"key":"GoEvidenceType","value":"IEA:Ensembl"}]},{"database":"GO","id":"GO:0003009","properties":[{"key":"GoTerm","value":"P:skeletal muscle contraction"},{"key":"GoEvidenceType","value":"IEA:Ensembl"}]},{"database":"GO","id":"GO:0051146","properties":[{"key":"GoTerm","value":"P:striated muscle cell differentiation"},{"key":"GoEvidenceType","value":"IEA:Ensembl"}]},{"database":"GO","id":"GO:0034142","properties":[{"key":"GoTerm","value":"P:toll-like receptor 4 signaling pathway"},{"key":"GoEvidenceType","value":"IDA:UniProt"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"26189595"}]},{"database":"GO","id":"GO:0033209","properties":[{"key":"GoTerm","value":"P:tumor necrosis factor-mediated signaling pathway"},{"key":"GoEvidenceType","value":"IMP:ARUK-UCL"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"12656673"}]},{"database":"CDD","id":"cd14039","properties":[{"key":"EntryName","value":"STKc_IKK_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd17046","properties":[{"key":"EntryName","value":"Ubl_IKKA_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.1270.250:FF:000001","properties":[{"key":"EntryName","value":"Inhibitor of nuclear factor kappa-B kinase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.20.90:FF:000061","properties":[{"key":"EntryName","value":"Inhibitor of nuclear factor kappa-B kinase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.510.10:FF:000147","properties":[{"key":"EntryName","value":"Inhibitor of nuclear factor kappa-B kinase subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1270.250","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.250.2110","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.20.90","properties":[{"key":"EntryName","value":"Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.510.10","properties":[{"key":"EntryName","value":"Transferase(Phosphotransferase) domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"IDEAL","id":"IID00526","properties":[{"key":"Description","value":"-"}]},{"database":"InterPro","id":"IPR041185","properties":[{"key":"EntryName","value":"IKBKB_SDD"}]},{"database":"InterPro","id":"IPR046375","properties":[{"key":"EntryName","value":"IKBKB_SDD_sf"}]},{"database":"InterPro","id":"IPR051180","properties":[{"key":"EntryName","value":"IKK"}]},{"database":"InterPro","id":"IPR022007","properties":[{"key":"EntryName","value":"IKKbetaNEMObind"}]},{"database":"InterPro","id":"IPR011009","properties":[{"key":"EntryName","value":"Kinase-like_dom_sf"}]},{"database":"InterPro","id":"IPR000719","properties":[{"key":"EntryName","value":"Prot_kinase_dom"}]},{"database":"InterPro","id":"IPR017441","properties":[{"key":"EntryName","value":"Protein_kinase_ATP_BS"}]},{"database":"InterPro","id":"IPR008271","properties":[{"key":"EntryName","value":"Ser/Thr_kinase_AS"}]},{"database":"InterPro","id":"IPR064033","properties":[{"key":"EntryName","value":"UBL_IKK"}]},{"database":"PANTHER","id":"PTHR22969","properties":[{"key":"EntryName","value":"IKB KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22969:SF13","properties":[{"key":"EntryName","value":"INHIBITOR OF NUCLEAR FACTOR KAPPA-B KINASE SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18397","properties":[{"key":"EntryName","value":"IKBKB_SDD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12179","properties":[{"key":"EntryName","value":"IKKbetaNEMObind"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00069","properties":[{"key":"EntryName","value":"Pkinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF29299","properties":[{"key":"EntryName","value":"UBL_IKK"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01239","properties":[{"key":"EntryName","value":"IKKbetaNEMObind"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00220","properties":[{"key":"EntryName","value":"S_TKc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56112","properties":[{"key":"EntryName","value":"Protein kinase-like (PK-like)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00107","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50011","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_DOM"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00108","properties":[{"key":"EntryName","value":"PROTEIN_KINASE_ST"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MERPPGLRPGAGGPWEMRERLGTGGFGNVCLYQHRELDLKIAIKSCRLELSTKNRERWCHEIQIMKKLNHANVVKACDVPEELNILIHDVPLLAMEYCSGGDLRKLLNKPENCCGLKESQILSLLSDIGSGIRYLHENKIIHRDLKPENIVLQDVGGKIIHKIIDLGYAKDVDQGSLCTSFVGTLQYLAPELFENKPYTATVDYWSFGTMVFECIAGYRPFLHHLQPFTWHEKIKKKDPKCIFACEEMSGEVRFSSHLPQPNSLCSLVVEPMENWLQLMLNWDPQQRGGPVDLTLKQPRCFVLMDHILNLKIVHILNMTSAKIISFLLPPDESLHSLQSRIERETGINTGSQELLSETGISLDPRKPASQCVLDGVRGCDSYMVYLFDKSKTVYEGPFASRSLSDCVNYIVQDSKIQLPIIQLRKVWAEAVHYVSGLKEDYSRLFQGQRAAMLSLLRYNANLTKMKNTLISASQQLKAKLEFFHKSIQLDLERYSEQMTYGISSEKMLKAWKEMEEKAIHYAEVGVIGYLEDQIMSLHAEIMELQKSPYGRRQGDLMESLEQRAIDLYKQLKHRPSDHSYSDSTEMVKIIVHTVQSQDRVLKELFGHLSKLLGCKQKIIDLLPKVEVALSNIKEADNTVMFMQGKRQKEIWHLLKIACTQSSARSLVGSSLEGAVTPQTSAWLPPTSAEHDHSLSCVVTPQDGETSAQMIEENLNCLGHLSTIIHEANEEQGNSMMNLDWSWLTE","length":745,"molWeight":84640,"crc64":"4EA55C6FFC66FA16","md5":"446AB468A56CBCDDBFA576A3FE4F3A6A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"SUBUNIT":2,"INTERACTION":26,"SUBCELLULAR LOCATION":1,"TISSUE SPECIFICITY":1,"DOMAIN":1,"PTM":3,"DISEASE":2,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Region":2,"Active site":1,"Binding site":2,"Modified residue":4,"Natural variant":3,"Mutagenesis":7,"Sequence conflict":5,"Helix":2},"uniParcId":"UPI000013D6C7"}}