about
P688
Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-betaC/EBPbeta phosphorylation by RSK creates a functional XEXD caspase inhibitory box critical for cell survivalCaveolin-1 mediates Fas-BID signaling in hyperoxia-induced apoptosisNo death without life: vital functions of apoptotic effectorsA novel function of caspase-8 in the regulation of androgen-receptor-driven gene expressionPellino3 targets RIP1 and regulates the pro-apoptotic effects of TNF-αFADD and caspase-8 control the outcome of autophagic signaling in proliferating T cellsInhibition of both the extrinsic and intrinsic death pathways through nonhomotypic death-fold interactionsVhlh gene deletion induces Hif-1-mediated cell death in thymocytesEx vivo whole-embryo culture of caspase-8-deficient embryos normalize their aberrant phenotypes in the developing neural tube and heartTNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II membersActive caspase-8 translocates into the nucleus of apoptotic cells to inactivate poly(ADP-ribose) polymerase-2Caspase-8 serves both apoptotic and nonapoptotic rolesApoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD.TIPE2, a negative regulator of innate and adaptive immunity that maintains immune homeostasisActivation of pro-death Bcl-2 family proteins and mitochondria apoptosis pathway in tumor necrosis factor-alpha-induced liver injuryMolecular cloning and characterization of mouse caspase-8Relief of extrinsic pathway inhibition by the Bid-dependent mitochondrial release of Smac in Fas-mediated hepatocyte apoptosisTranscriptional activation of known and novel apoptotic pathways by Nur77 orphan steroid receptorCaspase 8 inhibits programmed necrosis by processing CYLDCatalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosisThe phosphoprotein protein PEA-15 inhibits Fas- but increases TNF-R1-mediated caspase-8 activity and apoptosisThe E3 ubiquitin ligase itch couples JNK activation to TNFalpha-induced cell death by inducing c-FLIP(L) turnoverSurvival function of the FADD-CASPASE-8-cFLIP(L) complexPalmitoylation is required for efficient Fas cell death signalingMechanisms of necroptosis in T cellsNEMO Prevents Steatohepatitis and Hepatocellular Carcinoma by Inhibiting RIPK1 Kinase Activity-Mediated Hepatocyte ApoptosisRIPK1 blocks early postnatal lethality mediated by caspase-8 and RIPK3Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis.Phosphorylation and linear ubiquitin direct A20 inhibition of inflammation.Death-domain dimerization-mediated activation of RIPK1 controls necroptosis and RIPK1-dependent apoptosis.RIPK1 regulates RIPK3-MLKL-driven systemic inflammation and emergency hematopoiesis.Cleavage of RIPK1 by caspase-8 is crucial for limiting apoptosis and necroptosisK63-linked ubiquitination regulates RIPK1 kinase activity to prevent cell death during embryogenesis and inflammationMutations that prevent caspase cleavage of RIPK1 cause autoinflammatory disease
P921
Q22011091-2A9897A1-D0C0-4CBC-8D66-BD36B28C81CAQ24291845-A80FF954-CB85-4694-A4F3-26C75FB53FB2Q24295138-60AAE403-519B-4F25-A517-BB32F2F10C6CQ24319057-F832DDAF-7DA2-4BF2-996B-040F5065EFFBQ24336995-5256F98F-5231-4C0D-8814-CE0FC4BF5D73Q24338172-D7D315B6-9069-4558-B730-20F7A4F2E0C5Q24646372-BBB65BB8-FF37-448C-817D-9B1282FAEF48Q28283531-AEA89C22-81E9-4530-A416-8F0671E5BBDBQ28504459-26E2AD91-3656-4B02-BE99-1685820F7BACQ28504797-020E5560-B17B-4FFB-AEE5-02B00DFEB8ABQ28505598-32F03BC9-1718-4A4D-9664-96BCE4EC52E3Q28506471-EE6C80CE-A880-4E71-8529-AD01B962D2C8Q28507001-189BB9D1-F981-4EBF-9FD6-B5A0E0DF2DA5Q28507273-54F70063-14A5-43E2-8F9C-FC858F1EE8B0Q28509230-EEA0F6C0-8479-490F-A7A7-361F6F36B4F6Q28509883-929C05D3-2EFB-4B8C-A47D-5197CB32ADF4Q28510480-7D68C4A1-8A0F-43E2-87E1-0491284B4409Q28512377-3069D70A-767F-472C-B8C5-A8D61BCCF55DQ28512848-78928A6A-BC7F-4766-8DDA-4F1007D593C2Q28584927-3808DC3D-0298-4030-8367-1244D3C8EADCQ28584976-85909FF0-9DC2-4A32-9FA6-3F5DD53D8FD4Q28587650-3C74DE80-37EF-49B1-8A5C-25712DC6F51FQ28588830-03943AA6-FC57-4822-AC35-B73BE735009FQ28589465-CA6275FB-3DC8-4BEB-9E64-A36F76289DDDQ28591409-4561EDB4-E463-4DBD-89CA-B1FD2AB9CA02Q28592588-BD0ECC98-D0AB-4404-8D86-68229A937682Q28593092-AE497F5A-CEB6-4433-8580-093040D58B78Q33798944-6FA04FEB-539C-459A-B499-8DA32E8E6ED0Q34659851-8E50EC9A-BFF4-42A0-89C4-9C9A8FE84864Q41791638-FEBBFBE6-FB02-4839-9A4A-BF8FC8C8B4A7Q50026384-4CC801D5-4FD9-433F-8518-C01EC90B9501Q50663781-A1A59E24-D401-4329-B5A4-F922520181BBQ90069563-119E76D9-FA1B-4117-884D-40D1E87B6465Q90100569-B7DEE037-8915-49AE-9CC5-415BB611C084Q91892511-3B36A194-1D63-4AA1-841A-95EA6A7F99F8
P921
description
mammalian protein found in Mus musculus
@en
protein
@id
protein
@sv
proteinë
@sq
proteïne in Caspase 8
@nl
protèin
@ace
protéine
@fr
بروتين في فأر المنازل
@ar
name
Caspase 8
@en
Caspase 8
@nl
type
label
Caspase 8
@en
Caspase 8
@nl
altLabel
Casp8
@en
Fas-linked ICE-like protease
@en
caspase-8
@en
uniprot:O89110
@en
prefLabel
Caspase 8
@en
Caspase 8
@nl
P361
P527
P637
P680
P681
P682
P705
P352
P279
P31
P352
P527
P637
NP_001073595
NP_001264855
XP_006495697
P680
P681
P682
P702
P703
P705
ENSMUSP00000027189
ENSMUSP00000127375
ENSMUSP00000140335
ENSMUSP00000140546