Casp8
entrez
64044
canonical
uniprot
Q9JHX4
canonical
ensembl
ENSRNOG00000012331
resolver
ensembl
ENSRNOG00055023227
resolver
ensembl
ENSRNOG00060017095
resolver
ensembl
ENSRNOG00065029007
resolver
ensp
ENSRNOP00000016613
resolver
ensp
ENSRNOP00000103046
resolver
ensp
ENSRNOP00055032394
resolver
ensp
ENSRNOP00060023524
resolver
ensp
ENSRNOP00065041174
resolver
enst
ENSRNOT00000140357
resolver
enst
ENSRNOT00055039920
resolver
enst
ENSRNOT00060029215
resolver
enst
ENSRNOT00065050115
resolver
genesymbol
Casp8
resolver
uniprot_entry
CASP8_RAT
resolver
activity_regulation
ACTIVITY REGULATION: CASP8 activity is restricted by RIPK1. {ECO:0000250|UniProtKB:O89110}.
uniprot
proteins
amino_acid_sequence
MDFHSCLYDIAERLGNEELAALKFLCLDHIPQKKQESINDVLVLFQRLQEEGMLEEDNLSFLKELLFHISRRDLLSRVLKSSPEEMVRELQVLGKAQVSAYRVMLFKLSEDMDKEDLKSFKFLLITEIPKCKLQDNSSLLDIFVEMEKRTILAENNLVTLKSICFRVNRSLLGRIDDYERSSTERRMSTEGGEELPVSVLDEVTIKMQDMWDSPGEQESESLNSDNVYQMKSKPRGYCLIFNNNNFSKAREDIPKLSNMRDRKGTNYDEEALSKTFKELHFEIVSFSDCTASQIHEVLVSYQSKDHKGKDCFICCILSHGDKGIVYGTDGKEASIYELTSYFTGSKCPSLAGKPKIFFIQACQGNNFQKAVPVPDETGLEQEHVLEEDSSSYKNYIPDEADFLLGMATVKNCVSYRDPTRGTWYIQSLCQSLRERCPRGEDILSILTGVNYDVSNKDNPRNMGKQMPQPIFTLRKKLFFPPN
uniprot
proteins
ec_number
3.4.22.61
uniprot
proteins
function
FUNCTION: 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 (By similarity). 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:10197541). Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (By similarity). Binding to the adapter molecule FADD recruits it to either receptor FAS/CD95 or TNFRSF1A (PubMed:10197541). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (By similarity). The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (By similarity). Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (By similarity). 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-325', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response (By similarity). 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 (By similarity). 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 (By similarity). Cleaves PARP1 and PARP2 (By similarity). {ECO:0000250|UniProtKB:O89110, ECO:0000250|UniProtKB:Q14790, ECO:0000269|PubMed:10197541}.
uniprot
proteins
mass_dalton
55339
uniprot
proteins
post_translational_modification
PTM: Generation of the 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 (By similarity). {ECO:0000250|UniProtKB:Q14790}.; PTM: Phosphorylation on Ser-389 during mitosis by CDK1 inhibits activation by proteolysis and prevents apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes (By similarity). {ECO:0000250|UniProtKB:Q14790}.
uniprot
proteins
protein_family
Peptidase C14A family
uniprot
proteins
pubmed
10197541
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15383280
uniprot
proteins
pubmed
22673903
uniprot
proteins
sequence_length
482
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10197541}. Nucleus {ECO:0000269|PubMed:10197541}.
uniprot
proteins