about
sameAs
activated TLR3:TRIF:RIP1:FADD:pro-caspase-8activated TLR3:TRIF:RIP1:FADDactivated TLR4:TRIF:RIP1:FADD:pro-caspase-8activated TLR4:TRIF:RIP1:FADDviral dsRNA:IFIH1; viral dsRNA:K63polyUb-DDX58:MAVS:RIPK1:FADDFADD:Casp-8/10 prodomainFASL:FAS Receptor Trimer:FADDTNFSF10:TNFRSF10A;B:FADDTRADD:TRAF2:RIP1(325-671):FADDTRADD:TRAF2:RIP1:FADDTLR3-induced ripoptosome assemblyTLR4-induced ripoptosome assemblyMAVS interacts with RIPK1 and FADDFasL:Fas binds FADDTRADD:TRAF2:RIP1 complex binds FADDTRAIL:TRAIL receptor trimers bind FADD
P527
P688
Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector moleculeCaspase-10 is an initiator caspase in death receptor signalingVesicles released by activated T cells induce both Fas-mediated RIP-dependent apoptotic and Fas-independent nonapoptotic cell deathsTWEAK induces apoptosis through a death-signaling complex comprising receptor-interacting protein 1 (RIP1), Fas-associated death domain (FADD), and caspase-8The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutationsA novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domainFADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosisCaspase-8 prevents sustained activation of NF-kappaB in monocytes undergoing macrophagic differentiationWhole-exome-sequencing-based discovery of human FADD deficiencycIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoformsRibosomal protein S3 interacts with TRADD to induce apoptosis through caspase dependent JNK activationCasper is a FADD- and caspase-related inducer of apoptosisA pathway sensor for genome-wide screens of intracellular proteolytic cleavageDJ-1 inhibits TRAIL-induced apoptosis by blocking pro-caspase-8 recruitment to FADDCompetitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1PMLRARα binds to Fas and suppresses Fas-mediated apoptosis through recruiting c-FLIP in vivoIPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon inductionBovine herpesvirus 4 BORFE2 protein inhibits Fas- and tumor necrosis factor receptor 1-induced apoptosis and contains death effector domains shared with other gamma-2 herpesvirusesInvolvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell deathCARD-8 protein, a new CARD family member that regulates caspase-1 activation and apoptosis.A protein-protein interaction map of the TNF-induced NF-κB signal transduction pathway
P921
Q50260896-9F94CD52-CE03-40E2-93C1-2481DE1B3548Q50260899-150B20C4-BABB-4062-8620-5A4387288A70Q50261079-B71BB732-B1EF-4ECB-95A7-877966BE16E9Q50261081-43A08636-F8AA-440C-AC50-9585491563CEQ50261561-E714EE2E-0206-4F3F-91A2-566481598D46Q50261578-A615656D-8758-4290-8A09-4EA7F11CB7C2Q50270681-C7CE5781-38D6-401F-A34E-23F1C16B2C4AQ50270692-8C26C33A-4192-481F-AA6D-EBEB63427470Q50270700-FF3AF04D-585D-4A95-9CDD-D1FDF9C862F8Q50270705-90F369A8-0627-4443-9E3C-AD1BE03C24B2Q50291744-B267FFB7-2B9D-4F84-9CCE-D5DA1ABA034AQ50291835-D0412936-FCE1-4095-8A39-ABDBFC1C25D6Q50292025-B25CA53B-85CB-40D3-A527-0B1935CA3E4FQ50299336-6A49359A-CF0D-4F5B-81AA-864E3C2538EEQ50299352-1A4CDE01-B932-4881-9DAB-557DC90A4F88Q50299374-772ECDF9-826C-44F9-8DB8-ADBB84C0F40D
P527
Q24290576-45EC4887-2A02-4A0E-AFF9-768228017501Q24291922-F045E452-1D43-4A01-B813-4F0747AF38F3Q24296483-C1E582D5-8F95-4C58-9C08-EE1E35001C3FQ24300508-024619C2-4477-49A7-A530-C866307713EAQ24302236-76B2294B-46DE-4F3E-A8C8-397B9887BF13Q24306835-93C5C403-E0D9-4F76-8F29-00661AFC73ADQ24307362-EC6F1A0C-5162-4EDD-9295-45FA1A22CB7CQ24307493-D41254F4-B24D-4389-BDD5-96470C87DF17Q24309135-45D62C48-15C1-4650-8C19-AFC4C409EDC3Q24311676-98BBBB59-322B-4BFD-B356-A997C5204980Q24314607-278FECE8-CB53-4E42-9C4B-8BCC95C9CDABQ24315042-AAC9259D-658F-4EC8-9D79-CF57B3A39FE4Q24316457-D4DA97A6-F492-4D34-AF76-E3EC48886179Q24316876-5084F108-B133-4F46-80AA-BF3D79E039C4Q24317322-8B157521-3A1A-434B-A378-83F5B029019AQ24317781-8313CF6C-BD98-4265-A983-9DEE4BFC4E10Q24318426-D988A8DD-D726-4EB5-A160-7B50C4885FF4Q24320374-913F954F-9ABB-46D1-A051-47466EB67C24Q24336389-9EF7C803-FDEA-483B-AB2A-F8DCB2C1E314Q30668600-5633885D-B583-4B51-84D6-4698C945D974Q60044295-519B24F0-C947-47BF-8D33-0BE8766DE3ED
P921
description
Protein in Homo sapiens
@de
mammalian protein found in Homo sapiens
@en
protein
@id
protein
@sv
proteinë
@sq
proteïne in Fas associated via death domain
@nl
protèin
@ace
protéine
@fr
بروتين في الإنسان العاقل
@ar
name
FADD
@fr
FADD
@hu
Fas associated via death domain
@en
Fas associated via death domain
@nl
type
label
FADD
@fr
FADD
@hu
Fas associated via death domain
@en
Fas associated via death domain
@nl
altLabel
FADD
@en
FAS-associated death domain protein
@en
Fas (TNFRSF6)-associated via death domain
@en
Fas-associating death domain-containing protein
@en
Fas-associating protein with death domain
@en
Mediator of receptor induced toxicity
@en
Protein FADD
@en
growth-inhibiting gene 3 protein
@en
mediator of receptor-induced toxicity
@en
prefLabel
FADD
@fr
FADD
@hu
Fas associated via death domain
@en
Fas associated via death domain
@nl
P638
P680
P681
P682
P352
P486
P637
P31
P352
P486
P637
P638
P680
P681
P682
P702
P703
P705
ENSP00000301838