about
P688
Caveolin-1 mediates Fas-BID signaling in hyperoxia-induced apoptosisCaspase-8 and caspase-10 activate NF-kappaB through RIP, NIK and IKKalpha kinasesNo death without life: vital functions of apoptotic effectorsPhosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammationFADD 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 interactionsTNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II membersApoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD.Fas/tumor necrosis factor receptor death signaling is required for axotomy-induced death of motoneurons in vivoComplementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunityTIPE2, a negative regulator of innate and adaptive immunity that maintains immune homeostasisThe mouse cell surface protein TOSO regulates Fas/Fas ligand-induced apoptosis through its binding to Fas-associated death domainCatalytic 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) complexcIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species productionPalmitoylation is required for efficient Fas cell death signalingNEMO Prevents Steatohepatitis and Hepatocellular Carcinoma by Inhibiting RIPK1 Kinase Activity-Mediated Hepatocyte ApoptosisActivity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis.Regulation of RIPK1 activation by TAK1-mediated phosphorylation dictates apoptosis and necroptosis.Phosphorylation and linear ubiquitin direct A20 inhibition of inflammation.Death-domain dimerization-mediated activation of RIPK1 controls necroptosis and RIPK1-dependent apoptosis.K63-linked ubiquitination regulates RIPK1 kinase activity to prevent cell death during embryogenesis and inflammationRIPK1 prevents TRADD-driven, but TNFR1 independent, apoptosis during development
P921
Q24295138-BDE74E35-94DC-4255-A529-A24DF5F90AA2Q24311623-F2051328-AD40-40C8-B06F-FD16908DD50CQ24319057-277400CE-634F-4EEA-B465-A74A2E9E4E28Q24338129-495DDA32-1E27-4FE8-9425-9475F19E2BE0Q24646372-66E5C861-10EF-4950-BED0-1AB691DAB8D1Q28283531-398770F5-22D0-441C-85DF-B13959F186B9Q28505598-9C71832F-3D17-4A31-B9CC-908813B7DC29Q28507273-F66E8663-0E78-4C1D-B367-4325A657C803Q28508506-5F70ADEB-F70F-40AC-A938-869384545C65Q28509135-3D6F7B14-792C-49BE-9C10-C634F34624B1Q28509230-C10F24EF-4FE1-4F7F-AB28-DB0560301074Q28512719-DE0A7ACF-E4D6-4197-8E49-BE14E49B62FDQ28584976-C825375A-5244-4A9D-86DC-AFAC2A876A84Q28587650-D5FFF55B-764B-4413-AC6F-B2418661D4BAQ28588830-A8B557E1-3E1D-4E18-A25A-B07EAB831661Q28589465-5666805E-D1A6-4012-8C22-5604BED5FB8EQ28591258-2F0ABE8C-988B-41DF-AD3F-8F7DC3A83006Q28591409-E8B24A37-DE90-489F-8CDA-A513F6BF66FEQ28593092-CB23272D-489E-44EC-919B-F69F12C98DACQ34659851-8C401AA8-F94A-4AFC-86FA-A76586D79CFBQ41527499-77FF8BFC-57DB-4A9F-8A23-D0C6298E15ABQ41791638-CEB0A82D-AD55-46EF-BF48-7E1F519B6008Q50026384-82490FE5-E980-4286-A967-7DBA7C4E5369Q90100569-F9B37B9F-02F3-426E-9A70-0D713D068458Q91304398-62D2587A-C416-4239-B20C-79A37BC9FD0A
P921
description
mammalian protein found in Mus musculus
@en
protein
@id
protein
@sv
proteinë
@sq
proteïne in Fas (TNFRSF6)-associated via death domain
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protèin
@ace
protéine
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بروتين في فأر المنازل
@ar
name
Fas (TNFRSF6)-associated via death domain
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Fas
@nl
type
label
Fas (TNFRSF6)-associated via death domain
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Fas
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altLabel
FAS-associated death domain protein
@en
FAS-associating death domain-containing protein
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Fadd
@en
Fas-associating protein with death domain
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mediator of receptor induced toxicity
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protein FADD
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prefLabel
Fas (TNFRSF6)-associated via death domain
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Fas
@nl