{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q13546","secondaryAccessions":["A0AV89","B2RAG1","B4E3F9","Q13180","Q59H33"],"uniProtkbId":"RIPK1_HUMAN","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2005-02-01","entryVersion":245,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Receptor-interacting serine/threonine-protein kinase 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473668"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30988283"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8612133"}],"value":"2.7.11.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8612133"}],"value":"Cell death protein RIP"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16603398"}],"value":"Receptor-interacting protein 1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16603398"}],"value":"RIP-1"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:10019"}],"value":"RIPK1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8612133"}],"value":"RIP"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16603398"}],"value":"RIP1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60855"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11101870"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15310755"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17389591"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17703191"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19524512"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19524513"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24144979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29440439"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30988283"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32657447"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35831301"}],"value":"Serine-threonine kinase which is a key regulator of TNF-mediated apoptosis, necroptosis and inflammatory pathways (PubMed:17703191, PubMed:24144979, PubMed:31827280, PubMed:31827281, PubMed:32657447, PubMed:35831301). Exhibits kinase activity-dependent functions that regulate cell death and kinase-independent scaffold functions regulating inflammatory signaling and cell survival (PubMed:11101870, PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Has kinase-independent scaffold functions: upon binding of TNF to TNFR1, RIPK1 is recruited to the TNF-R1 signaling complex (TNF-RSC also known as complex I) where it acts as a scaffold protein promoting cell survival, in part, by activating the canonical NF-kappa-B pathway (By similarity). Kinase activity is essential to regulate necroptosis and apoptosis, two parallel forms of cell death: upon activation of its protein kinase activity, regulates assembly of two death-inducing complexes, namely complex IIa (RIPK1-FADD-CASP8), which drives apoptosis, and the complex IIb (RIPK1-RIPK3-MLKL), which drives necroptosis (By similarity). RIPK1 is required to limit CASP8-dependent TNFR1-induced apoptosis (By similarity). In normal conditions, RIPK1 acts as an inhibitor of RIPK3-dependent necroptosis, a process mediated by RIPK3 component of complex IIb, which catalyzes phosphorylation of MLKL upon induction by ZBP1 (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Inhibits RIPK3-mediated necroptosis via FADD-mediated recruitment of CASP8, which cleaves RIPK1 and limits TNF-induced necroptosis (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Required to inhibit apoptosis and necroptosis during embryonic development: acts by preventing the interaction of TRADD with FADD thereby limiting aberrant activation of CASP8 (By similarity). In addition to apoptosis and necroptosis, also involved in inflammatory response by promoting transcriptional production of pro-inflammatory cytokines, such as interleukin-6 (IL6) (PubMed:31827280, PubMed:31827281). Phosphorylates RIPK3: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (PubMed:19524513). Phosphorylates DAB2IP at 'Ser-728' in a TNF-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade (PubMed:15310755, PubMed:17389591). Required for ZBP1-induced NF-kappa-B activation in response to DNA damage (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"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":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473668"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30988283"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8612133"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473668"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30988283"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8612133"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60855"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473668"}],"value":"Serine-threonine kinase activity is inhibited by linear polyubiquitination ('Met-1'-linked) by the LUBAC complex (By similarity). Inhibited by necrostatins, including necrostatin-1, necrostatin-3 and necrostatin-4 (PubMed:23473668)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60855"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10356400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10358032"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10409763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11116146"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11734559"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11854271"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14754897"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16127453"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17389591"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17449468"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17703191"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18450452"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19524512"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21887730"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21931591"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22265414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24130170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24204270"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25736436"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29440439"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29681455"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29883609"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35831301"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8612133"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9044836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9927690"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.36"}],"value":"Homodimer (PubMed:29440439, PubMed:29681455). Interacts (via RIP homotypic interaction motif) with RIPK3 (via RIP homotypic interaction motif); this interaction induces RIPK1 phosphorylation and formation of a RIPK1-RIPK3 necroptosis-inducing complex (PubMed:10358032, PubMed:11734559, PubMed:19524512, PubMed:29681455, PubMed:29883609). Upon TNF-induced necrosis, the RIPK1-RIPK3 dimer further interacts with PGAM5 and MLKL; the formation of this complex leads to PGAM5 phosphorylation and increase in PGAM5 phosphatase activity (PubMed:22265414). Interacts (via the death domain) with TNFRSF6 (via the death domain) and TRADD (via the death domain) (PubMed:8612133). Is recruited by TRADD to TNFRSF1A in a TNF-dependent process (PubMed:24130170). Binds RNF216, EGFR, IKBKG, TRAF1, TRAF2 and TRAF3 (PubMed:11116146, PubMed:11854271, PubMed:8612133, PubMed:9927690). Interacts with BNLF1 (PubMed:10409763). Interacts with SQSTM1 upon TNF stimulation (PubMed:10356400). May interact with MAVS/IPS1 (PubMed:16127453). Interacts with ZFAND5 (PubMed:14754897). Interacts with RBCK1 (PubMed:17449468). Interacts with ZBP1 (By similarity). Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4 (PubMed:21931591). Interacts (via kinase domain) with DAB2IP (via Ras-GAP domain); the interaction occurs in a TNF-dependent manner (PubMed:15310755, PubMed:17389591). Interacts with ARHGEF2 (PubMed:21887730). Interacts (via protein kinase domain) with RFFL; involved in RIPK1 ubiquitination (PubMed:18450452). Interacts with RNF34; involved in RIPK1 ubiquitination (Ref.36). Interacts with TICAM1 and this interaction is enhanced in the presence of WDFY1 (PubMed:25736436). Interacts with PELI1 (PubMed:29883609). Interacts (via death domain) with CRADD (via death domain); the interaction is direct (PubMed:9044836). Component of complex IIa composed of at least RIPK1, FADD and CASP8 (By similarity). Component of the AIM2 PANoptosome complex, a multiprotein complex that drives inflammatory cell death (PANoptosis) (By similarity). Interacts with MAP3K7, CFLAR, CASP8, FADD and NEMO (By similarity). Interacts with TAX1BP1; this interaction negatively regulates RIPK1 ubiquitination (PubMed:17703191). Interacts with GRB2 (PubMed:35831301). Interacts with DDX24; this interaction disrupts RLR signaling activation of IFN-dependent transcription factor IRF7 (PubMed:24204270)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28659487"}],"value":"(Microbial infection) Interacts with mumps virus protein SH; this interaction inhibits downstream NF-kappa-B pathway activation"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18442983"}],"value":"(Microbial infection) Interacts with Murid herpesvirus 1 protein RIR1"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25674983"}],"value":"(Microbial infection) Interacts (via RIP homotypic interaction motif) with herpes simplex virus 1/HHV-1 protein RIR1/ICP6 (via RIP homotypic interaction motif); this interaction prevents necroptosis activation"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25674983"}],"value":"(Microbial infection) Interacts (via RIP homotypic interaction motif) with herpes simplex virus 2/HHV-2 protein RIR1/ICP10 (via RIP homotypic interaction motif); this interaction prevents necroptosis activation"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"P04083","geneName":"ANXA1","intActId":"EBI-354007"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q13490","geneName":"BIRC2","intActId":"EBI-514538"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q13489","geneName":"BIRC3","intActId":"EBI-517709"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q92851","geneName":"CASP10","intActId":"EBI-495095"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q14790","geneName":"CASP8","intActId":"EBI-78060"},"numberOfExperiments":28,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q8IVM0","geneName":"CCDC50","intActId":"EBI-723996"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"P48729","geneName":"CSNK1A1","intActId":"EBI-1383726"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q13158","geneName":"FADD","intActId":"EBI-494804"},"numberOfExperiments":12,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q9Y6K9","geneName":"IKBKG","intActId":"EBI-81279"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q96AB6","geneName":"NTAN1","intActId":"EBI-12401218"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q9ULZ3","geneName":"PYCARD","intActId":"EBI-751215"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q13546","geneName":"RIPK1","intActId":"EBI-358507"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q9Y572","geneName":"RIPK3","intActId":"EBI-298250"},"numberOfExperiments":27,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"P19438","geneName":"TNFRSF1A","intActId":"EBI-299451"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q13077","geneName":"TRAF1","intActId":"EBI-359224"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q12933","geneName":"TRAF2","intActId":"EBI-355744"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q13114","geneName":"TRAF3","intActId":"EBI-357631"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"Q13107","geneName":"USP4","intActId":"EBI-723290"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"B7UI21","geneName":"nleB1","intActId":"EBI-16070376"},"numberOfExperiments":4,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"P0DTD1","geneName":"rep","chainId":"PRO_0000449629","intActId":"EBI-25475885"},"numberOfExperiments":6,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"Q13546","intActId":"EBI-358507"},"interactantTwo":{"uniProtKBAccession":"U5TQE9","geneName":"UL39","intActId":"EBI-11894787"},"numberOfExperiments":3,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60855"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9ZUF4"}],"value":"Cell membrane","id":"SL-0039"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q13546-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q13546-2"],"sequenceIds":["VSP_037690"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29681455"}],"value":"The RIP homotypic interaction motif (RHIM) mediates interaction with the RHIM motif of RIPK1. Both motifs form a hetero-amyloid serpentine fold, stabilized by hydrophobic packing and featuring an unusual Cys-Ser ladder of alternating Ser (from RIPK1) and Cys (from RIPK3)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10356400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29440439"}],"value":"The death domain mediates dimerization and activation of its kinase activity during necroptosis and apoptosis (PubMed:29440439). It engages other DD-containing proteins as well as a central (intermediate) region important for NF-kB activation and RHIM-dependent signaling (PubMed:10356400)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32657447"}],"value":"(Microbial infection) Proteolytically cleaved by S.flexneri OspD3 within the RIP homotypic interaction motif (RHIM), leading to its degradation and inhibition of necroptosis"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60855"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10521396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827281"}],"value":"Proteolytically cleaved by CASP8 at Asp-324 (PubMed:10521396, PubMed:31827280, PubMed:31827281). Cleavage is crucial for limiting TNF-induced apoptosis, necroptosis and inflammatory response (PubMed:31827280, PubMed:31827281). Cleavage abolishes NF-kappa-B activation and enhances the interaction of TRADD with FADD (PubMed:10521396). Proteolytically cleaved by CASP6 during intrinsic apoptosis (PubMed:22858542)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60855"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18408713"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19524513"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30988283"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827280"}],"value":"RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (PubMed:18408713, PubMed:19524513, PubMed:31827280). Phosphorylation of Ser-161 by RIPK3 is necessary for the formation of the necroptosis-inducing complex (PubMed:18408713). Phosphorylation at Ser-25 represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (PubMed:30988283). Phosphorylated at Ser-320 by MAP3K7 which requires prior ubiquitination with 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2 (By similarity). This phosphorylation positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24144979"}],"value":"Deubiquitinated by USP7; this modification is required for TNF-induced apoptosis"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60855"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15258597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16603398"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18450452"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21455173"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21931591"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29883609"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.36"}],"value":"Ubiquitinated with 'Lys-11'-, 'Lys-48'-, 'Lys-63'- and linear-linked type ubiquitin (PubMed:15258597, PubMed:16603398, PubMed:17703191, PubMed:18450452, PubMed:21455173, PubMed:21931591, PubMed:29883609, Ref.36). Polyubiquitination with 'Lys-63'-linked chains by TRAF2 induces association with the IKK complex (PubMed:15258597). Deubiquitination of 'Lys-63'-linked chains and polyubiquitination with 'Lys-48'-linked chains by TNFAIP3 leads to RIPK1 proteasomal degradation and consequently down-regulates TNF-induced NF-kappa-B signaling (PubMed:15258597). 'Lys-48'-linked polyubiquitination by RFFL or RNF34 also promotes proteasomal degradation and negatively regulates TNF-induced NF-kappa-B signaling (PubMed:18450452, Ref.36). Linear polyubiquitinated; the head-to-tail linear polyubiquitination ('Met-1'-linked) is mediated by the LUBAC complex and decreases protein kinase activity (PubMed:21455173). Deubiquitination of linear polyubiquitin by CYLD promotes the kinase activity (By similarity). Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B (PubMed:21931591). Ubiquitinated with 'Lys-63'-linked chains by PELI1 (PubMed:29883609). Ubiquitination at Lys-377 with 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2 is essential for its phosphorylation at Ser-320 mediated by MAP3K7 (By similarity). This ubiquitination is required for NF-kB activation, suppresses RIPK1 kinase activity and plays a critical role in preventing cell death during embryonic development (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23955153"}],"value":"(Microbial infection) Glycosylated at Arg-603 by enteropathogenic E.coli protein NleB1: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Immunodeficiency 57 with autoinflammation","diseaseAccession":"DI-05328","acronym":"IMD57","description":"An autosomal recessive primary immunodeficiency characterized by lymphopenia and recurrent viral, bacterial, and fungal infections. Patients exhibit early-onset inflammatory bowel disease involving the upper and lower gastrointestinal tract, and develop progressive polyarthritis.","diseaseCrossReference":{"database":"MIM","id":"618108"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30026316"}]},"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30026316"}],"value":"The disease is caused by variants affecting the gene represented in this entry. 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