{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q14790","secondaryAccessions":["O14676","Q14791","Q14792","Q14793","Q14794","Q14795","Q14796","Q15780","Q15806","Q53TT5","Q8TDI1","Q8TDI2","Q8TDI3","Q8TDI4","Q8TDI5","Q96T22","Q9C0K4","Q9UQ81"],"uniProtkbId":"CASP8_HUMAN","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-11-01","entryVersion":268,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12010809"}],"value":"Caspase-8"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12010809"}],"value":"CASP-8"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23516580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32929201"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34012073"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8962078"}],"value":"3.4.22.61"}]},"alternativeNames":[{"fullName":{"value":"Apoptotic cysteine protease"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8962078"}],"value":"Apoptotic protease Mch-5"}},{"fullName":{"value":"CAP4"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8681377"}],"value":"FADD-homologous ICE/ced-3-like protease"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8681377"}],"value":"FADD-like ICE"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8681377"}],"value":"FLICE"}]},{"fullName":{"value":"ICE-like apoptotic protease 5"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8681376"}],"value":"MORT1-associated ced-3 homolog"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8681376"}],"value":"MACH"}]}],"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8962078"}],"value":"Caspase-8 subunit p18"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8962078"}],"value":"Caspase-8 subunit p10"}}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9931493"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:1509"}],"value":"CASP8"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8962078"}],"value":"MCH5"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O89110"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16916640"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18216014"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23516580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27109099"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32929201"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34012073"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35338844"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35446120"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8681376"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8681377"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8755496"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8962078"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9006941"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9184224"}],"value":"Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224). Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for FAS/CD95-mediated and TNFRSF1A-induced cell death (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224). Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (PubMed:16916640, PubMed:8962078, PubMed:9006941). Binding to the adapter molecule FADD recruits it to either receptor FAS/TNFRSF6 or TNFRSF1A (PubMed:8681376, PubMed:8681377). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed:9184224). The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (PubMed:9184224). Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (PubMed:9184224). Also cleaves and activates BID, thereby promoting cytochrome C release from mitochrondria (By similarity). In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-324', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response (PubMed:31827280, PubMed:31827281). Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-C and -D (GSDMC and GSDMD, respectively): gasdermin cleavage promotes release of the N-terminal moiety that binds to membranes and forms pores, triggering pyroptosis (PubMed:32929201, PubMed:34012073). Initiates pyroptosis following inactivation of MAP3K7/TAK1 (By similarity). Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production (By similarity). May participate in the Granzyme B (GZMB) cell death pathways (PubMed:8755496). Cleaves PARP1 and PARP2 (PubMed:8681376). Independent of its protease activity, promotes cell migration following phosphorylation at Tyr-380 (PubMed:18216014, PubMed:27109099)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8681376"}],"value":"Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex"}],"commentType":"FUNCTION","molecule":"Isoform 5"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8681376"}],"value":"Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex"}],"commentType":"FUNCTION","molecule":"Isoform 6"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12010809"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8681376"}],"value":"Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex (Probable). Acts as an inhibitor of the caspase cascade (PubMed:12010809)"}],"commentType":"FUNCTION","molecule":"Isoform 7"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8681376"}],"value":"Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex"}],"commentType":"FUNCTION","molecule":"Isoform 8"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala).","ecNumber":"3.4.22.61","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16916640"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23516580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32929201"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34012073"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8962078"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O89110"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23516580"}],"value":"CASP8 activity is restricted by RIPK1 (By similarity). Inhibited by the effector protein NleF that is produced by pathogenic E.coli; this inhibits apoptosis (PubMed:23516580)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O89110"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9JHX4"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10442631"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10508784"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15069192"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15509781"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16378960"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18846110"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27109099"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28602583"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8681376"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8681377"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9184224"}],"value":"Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 18 kDa (p18) and a 10 kDa (p10) subunit (PubMed:10508784). Component of the death-induced signaling complex (DISC) composed of cell surface receptor FAS/CD95 or TNFRSF1A, adapter protein FADD and the CASP8 protease; recruitment of CASP8 to the complex is required for processing of CASP8 into the p18 and p10 subunits (PubMed:8681376, PubMed:8681377, PubMed:9184224). Component of the AIM2 PANoptosome complex, a multiprotein complex that drives inflammatory cell death (PANoptosis) (By similarity). Interacts with CFLAR and PEA15 (PubMed:10442631). Interacts with TNFAIP8L2 (By similarity). Interacts with CASP8AP2 (PubMed:16378960). Interacts with RFFL and RNF34; negatively regulate CASP8 through proteasomal degradation (PubMed:15069192). Interacts with NOL3; decreases CASP8 activity in a mitochondria localization- and phosphorylation-dependent manner and this interaction is dissociated by calcium (PubMed:15509781). Interacts with UBR2ca (PubMed:28602583). Interacts with RIPK1 (By similarity). Interacts with stimulated TNFRSF10B; this interaction is followed by CASP8 proteolytic cleavage and activation (PubMed:18846110). Interacts (phosphorylated on Tyr-380) with PIK3R1 (PubMed:27109099)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11917123"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9334338"}],"value":"Interacts at the endoplasmic reticulum with a complex containing BCAP31, BAP29, BCL2 and/or BCL2L1"}],"commentType":"SUBUNIT","molecule":"Isoform 9"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11427719"}],"value":"(Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein vICA/UL36; this interaction inhibits CASP8 activation"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23516580"}],"value":"(Microbial infection) Interacts with NleF from pathogenic E.coli"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16378960"}],"value":"(Microbial infection) Interacts with molluscum contagiosum virus protein MC160"}],"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":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"P05067","geneName":"APP","intActId":"EBI-77613"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"P10275","geneName":"AR","intActId":"EBI-608057"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"P51572","geneName":"BCAP31","intActId":"EBI-77683"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"Q92851","geneName":"CASP10","intActId":"EBI-495095"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"Q14790","geneName":"CASP8","intActId":"EBI-78060"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"Q9UKL3","geneName":"CASP8AP2","intActId":"EBI-2339650"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"O15519","geneName":"CFLAR","intActId":"EBI-514941"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"O15519-1","geneName":"CFLAR","intActId":"EBI-4567563"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"Q13618","geneName":"CUL3","intActId":"EBI-456129"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"Q13158","geneName":"FADD","intActId":"EBI-494804"},"numberOfExperiments":46,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"P25445","geneName":"FAS","intActId":"EBI-494743"},"numberOfExperiments":15,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"P25445-1","geneName":"FAS","intActId":"EBI-15749113"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"P48023","geneName":"FASLG","intActId":"EBI-495538"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"Q06787-7","geneName":"FMR1","intActId":"EBI-25856644"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"Q13418","geneName":"ILK","intActId":"EBI-747644"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"Q9UDY8","geneName":"MALT1","intActId":"EBI-1047372"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"O60936","geneName":"NOL3","intActId":"EBI-740992"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"P53350","geneName":"PLK1","intActId":"EBI-476768"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"P29350","geneName":"PTPN6","intActId":"EBI-78260"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"P04049","geneName":"RAF1","intActId":"EBI-365996"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"Q13546","geneName":"RIPK1","intActId":"EBI-358507"},"numberOfExperiments":28,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"Q969K3","geneName":"RNF34","intActId":"EBI-2340642"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"P21580","geneName":"TNFAIP3","intActId":"EBI-527670"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"O00220","geneName":"TNFRSF10A","intActId":"EBI-518861"},"numberOfExperiments":11,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"P13051-2","geneName":"UNG","intActId":"EBI-25834258"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790","intActId":"EBI-78060"},"interactantTwo":{"uniProtKBAccession":"Q96AX1","geneName":"VPS33A","intActId":"EBI-2527283"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790-1","intActId":"EBI-288309"},"interactantTwo":{"uniProtKBAccession":"Q13158","geneName":"FADD","intActId":"EBI-494804"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790-2","intActId":"EBI-15777741"},"interactantTwo":{"uniProtKBAccession":"O15519-1","geneName":"CFLAR","intActId":"EBI-4567563"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14790-5","intActId":"EBI-288326"},"interactantTwo":{"uniProtKBAccession":"Q13158","geneName":"FADD","intActId":"EBI-494804"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000004629","intActId":"EBI-4478080"},"interactantTwo":{"uniProtKBAccession":"Q14790","geneName":"CASP8","chainId":"PRO_0000004631","intActId":"EBI-12736099"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18216014"}],"value":"Recruitment to lamellipodia of migrating cells is enhanced by phosphorylation at Tyr-380"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9JHX4"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9JHX4"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18216014"}],"value":"Cell projection, lamellipodium","id":"SL-0291"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"synonyms":[{"value":"Alpha-1"}],"isoformIds":["Q14790-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"synonyms":[{"value":"Alpha-2"},{"value":"MCH5-beta"}],"isoformIds":["Q14790-2"],"sequenceIds":["VSP_000810"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"synonyms":[{"value":"Alpha-3"}],"isoformIds":["Q14790-3"],"sequenceIds":["VSP_000813"],"isoformSequenceStatus":"Described"},{"name":{"value":"4"},"synonyms":[{"value":"Alpha-4"}],"isoformIds":["Q14790-4"],"sequenceIds":["VSP_000809","VSP_000810"],"isoformSequenceStatus":"Described"},{"name":{"value":"5"},"synonyms":[{"value":"Beta-1"}],"isoformIds":["Q14790-5"],"sequenceIds":["VSP_000814","VSP_000815"],"isoformSequenceStatus":"Described"},{"name":{"value":"6"},"synonyms":[{"value":"Beta-2"}],"isoformIds":["Q14790-6"],"sequenceIds":["VSP_000811","VSP_000812"],"isoformSequenceStatus":"Described"},{"name":{"value":"7"},"synonyms":[{"value":"Beta-3"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12010809"}],"value":"8L"}],"isoformIds":["Q14790-7"],"sequenceIds":["VSP_000816","VSP_000817"],"isoformSequenceStatus":"Described"},{"name":{"value":"8"},"synonyms":[{"value":"Beta-4"}],"isoformIds":["Q14790-8"],"sequenceIds":["VSP_000810","VSP_000816","VSP_000817"],"isoformSequenceStatus":"Described"},{"name":{"value":"9"},"synonyms":[{"value":"8L"}],"isoformIds":["Q14790-9"],"sequenceIds":["VSP_000808"],"isoformSequenceStatus":"Described"}]},{"texts":[{"value":"Isoform 1, isoform 5 and isoform 7 are expressed in a wide variety of tissues. Highest expression in peripheral blood leukocytes, spleen, thymus and liver. Barely detectable in brain, testis and skeletal muscle"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18216014"}],"value":"The catalytic domain is sufficient for recruitment to lamellipodia but catalytic activity is not necessary"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11917123"}],"value":"Contains a N-terminal extension that is required for interaction with the BCAP31 complex"}],"commentType":"DOMAIN","molecule":"Isoform 9"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8962078"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9184224"}],"value":"Generation of the p10 and p18 subunits requires association with the death-inducing signaling complex (DISC), whereas additional processing is likely due to the autocatalytic activity of the activated protease. GZMB and CASP10 can be involved in these processing events"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16619028"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18216014"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20937773"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27109099"}],"value":"Phosphorylation on Ser-387 during mitosis by CDK1 inhibits activation by proteolysis and prevents apoptosis (PubMed:20937773). Phosphorylation on Tyr-380 by SRC is mediated by interaction with the SRC SH2 domain and does not affect dimerization or recruitment to the death-inducing signaling complex (DISC) but negatively regulates DISC-mediated processing and activation of CASP8, down-regulating its proapoptotic function (PubMed:16619028, PubMed:27109099). Phosphorylation on Tyr-380 also enhances localization to lamellipodia in migrating cells (PubMed:18216014)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35338844"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35446120"}],"value":"(Microbial infection) ADP-riboxanation by C.violaceum CopC blocks CASP8 processing, preventing CASP8 activation and ability to mediate extrinsic apoptosis"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8962078"}],"value":"(Microbial infection) Proteolytically cleaved by the cowpox virus CRMA death inhibitory protein"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17450141"}],"value":"Genetic variations in CASP8 are associated with reduced risk of lung cancer [MIM:211980] in a population of Han Chinese subjects. 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