HUMAN:FADD

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	FADD (synonyms: MORT1)
Protein Name(s)	FAS-associated death domain protein FAS-associating death domain-containing protein Growth-inhibiting gene 3 protein Mediator of receptor induced toxicity Protein FADD
External Links
UniProt	Q13158
EMBL	U24231 X84709 AY423721 AK291005 BT006927 CR456738 DQ449938 CH471076 BC000334
CCDS	CCDS8196.1
PIR	A56912
RefSeq	NP_003815.1
UniGene	Hs.86131
PDB	1A1W 1A1Z 1E3Y 1E41 2GF5 3EZQ 3OQ9
PDBsum	1A1W 1A1Z 1E3Y 1E41 2GF5 3EZQ 3OQ9
ProteinModelPortal	Q13158
SMR	Q13158
BioGrid	114302
DIP	DIP-286N
IntAct	Q13158
MINT	MINT-91814
STRING	9606.ENSP00000301838
PhosphoSite	Q13158
DMDM	2498355
MaxQB	Q13158
PaxDb	Q13158
PeptideAtlas	Q13158
PRIDE	Q13158
DNASU	8772
Ensembl	ENST00000301838
GeneID	8772
KEGG	hsa:8772
UCSC	uc001opm.2
CTD	8772
GeneCards	GC11P070049
HGNC	HGNC:3573
HPA	CAB010209 HPA001464
MIM	602457 613759
neXtProt	NX_Q13158
Orphanet	306550 99806
PharmGKB	PA27972
eggNOG	NOG43830
GeneTree	ENSGT00390000002105
HOGENOM	HOG000112490
HOVERGEN	HBG000853
InParanoid	Q13158
KO	K02373
OMA	CQMNLVA
OrthoDB	EOG76X61Z
PhylomeDB	Q13158
TreeFam	TF102046
Reactome	REACT_1503 REACT_150361 REACT_164011 REACT_25039 REACT_402 REACT_832 REACT_900
SignaLink	Q13158
EvolutionaryTrace	Q13158
GeneWiki	FADD
GenomeRNAi	8772
NextBio	32890
PRO	PR:Q13158
Proteomes	UP000005640
Bgee	Q13158
CleanEx	HS_FADD
ExpressionAtlas	Q13158
Genevestigator	Q13158
GO	GO:0031265 GO:0044297 GO:0005829 GO:0031264 GO:0045121 GO:0043005 GO:0097342 GO:0035877 GO:0005123 GO:0042802 GO:0002020 GO:0032813 GO:0097202 GO:0006919 GO:0006915 GO:0097190 GO:0071260 GO:0051607 GO:0097191 GO:0097192 GO:0008625 GO:0045087 GO:0048535 GO:0097049 GO:0002756 GO:0097527 GO:0070236 GO:0060546 GO:0042104 GO:0002821 GO:0043065 GO:2000454 GO:2001238 GO:1902043 GO:0043123 GO:0032729 GO:0032757 GO:0045651 GO:0045862 GO:0001916 GO:0045944 GO:0032760 GO:0060340 GO:0051291 GO:2001239 GO:0048536 GO:0033077 GO:0043029 GO:0048538 GO:0034138 GO:0034142 GO:0002224 GO:0036462 GO:0035666 GO:0016032
Gene3D	1.10.533.10
InterPro	IPR011029 IPR000488 IPR001875 IPR016729
Pfam	PF00531 PF01335
PIRSF	PIRSF018586
SMART	SM00005 SM00031
SUPFAM	SSF47986
PROSITE	PS50017 PS50168

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0016265	death	PMID:7538907^[1]	ECO:0000316		UniProtKB:P25445 UniProtKB:Q13158	P		Figures 4 and 5	complete CACAO 3545
	GO:0031264		PMID:7538907^[1]	ECO:0000247		PMID:7538907^[1]			Analysis of data using Northern blotting, sequence alignment and expression vectors	complete CACAO 9344
	GO:0031264	death-inducing signaling complex	PMID:7536190^[2]	ECO:0000315			C		Northern and Sequence Analyses	complete CACAO 9345
	GO:0045559		PMID:14702039^[3]	ECO:0000314					Sequence analysis	complete CACAO 9346
	GO:0031265		PMID:10825539^[4]	ECO:0000247		PMID:10825539^[4]			Analysis of Sequence ALignment, Figure 2	complete CACAO 9348
	GO:0031264		PMID:9582077^[5]	ECO:0000247		PMID:958207^[6]			Analysis from FIgure 1 Northern blotting, and Figure 3 Sequence Alignment	complete CACAO 9349
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:11821383^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0089720	caspase binding	PMID:9343261^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14790	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:22510408^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:22510408^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0036462	TRAIL-activated apoptotic signaling pathway	PMID:21785459^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21785459^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:21785459^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14790	F		Seeded From UniProt	complete
involved_in	GO:0097527	necroptotic signaling pathway	PMID:11101870^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097202	activation of cysteine-type endopeptidase activity	PMID:18387192^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097190	apoptotic signaling pathway	PMID:11101870^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:16127453^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045862	positive regulation of proteolysis	PMID:18387192^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032760	positive regulation of tumor necrosis factor production	PMID:16127453^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032757	positive regulation of interleukin-8 production	PMID:16127453^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031264	death-inducing signaling complex	PMID:11101870^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:2001238	positive regulation of extrinsic apoptotic signaling pathway	PMID:21525013^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(GO:0031264)	Seeded From UniProt	complete
involved_in	GO:2000454	positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q61160	P		Seeded From UniProt	complete
part_of	GO:0097342	ripoptosome	PMID:21737330^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0097191	extrinsic apoptotic signaling pathway	PMID:16611992^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097191	extrinsic apoptotic signaling pathway	PMID:21785459^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071260	cellular response to mechanical stimulus	PMID:19593445^[17]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070236	negative regulation of activation-induced cell death of T cells	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q61160	P		Seeded From UniProt	complete
involved_in	GO:0060340	positive regulation of type I interferon-mediated signaling pathway	PMID:21109225^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051607	defense response to virus	PMID:21109225^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048538	thymus development	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q61160	P		Seeded From UniProt	complete
involved_in	GO:0048536	spleen development	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q61160	P		Seeded From UniProt	complete
involved_in	GO:0048535	lymph node development	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q61160	P		Seeded From UniProt	complete
involved_in	GO:0045651	positive regulation of macrophage differentiation	PMID:17047155^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043123	positive regulation of I-kappaB kinase/NF-kappaB signaling	PMID:12761501^[20]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:20935634^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043029	T cell homeostasis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q61160	P		Seeded From UniProt	complete
involved_in	GO:0042104	positive regulation of activated T cell proliferation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q61160	P		Seeded From UniProt	complete
enables	GO:0035877	death effector domain binding	PMID:11717445^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14790	F		Seeded From UniProt	complete
enables	GO:0035877	death effector domain binding	PMID:11717445^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q92851	F		Seeded From UniProt	complete
involved_in	GO:0033077	T cell differentiation in thymus	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q61160	P		Seeded From UniProt	complete
enables	GO:0032813	tumor necrosis factor receptor superfamily binding	PMID:21109225^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P25445	F		Seeded From UniProt	complete
involved_in	GO:0032729	positive regulation of interferon-gamma production	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q61160	P		Seeded From UniProt	complete
part_of	GO:0031265	CD95 death-inducing signaling complex	PMID:20935634^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031264	death-inducing signaling complex	PMID:21803845^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:22891283^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0002821	positive regulation of adaptive immune response	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q61160	P		Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:9208847^[25]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14790	F		Seeded From UniProt	complete
involved_in	GO:0001916	positive regulation of T cell mediated cytotoxicity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q61160	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:8681376^[26]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13158	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:7536190^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13158	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:30561431^[27]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13158	F		Seeded From UniProt	complete
involved_in	GO:2001238	positive regulation of extrinsic apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:2000454	positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0097192	extrinsic apoptotic signaling pathway in absence of ligand	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0097191	extrinsic apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0097049	motor neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0070236	negative regulation of activation-induced cell death of T cells	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0060546	negative regulation of necroptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0048538	thymus development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0048536	spleen development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0048535	lymph node development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0043029	T cell homeostasis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0042104	positive regulation of activated T cell proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0033077	T cell differentiation in thymus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0032729	positive regulation of interferon-gamma production	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0002821	positive regulation of adaptive immune response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0001916	positive regulation of T cell mediated cytotoxicity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61160 ensembl:ENSMUSP00000033394	P		Seeded From UniProt	complete
involved_in	GO:0060544	regulation of necroptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	P		Seeded From UniProt	complete
involved_in	GO:0048148	behavioral response to cocaine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	P		Seeded From UniProt	complete
part_of	GO:0045121	membrane raft	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	C		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	F		Seeded From UniProt	complete
part_of	GO:0044297	cell body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	C		Seeded From UniProt	complete
involved_in	GO:0043278	response to morphine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	P		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	C		Seeded From UniProt	complete
involved_in	GO:0042220	response to cocaine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	P		Seeded From UniProt	complete
enables	GO:0033612	receptor serine/threonine kinase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	C		Seeded From UniProt	complete
part_of	GO:0031265	CD95 death-inducing signaling complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	C		Seeded From UniProt	complete
part_of	GO:0031264	death-inducing signaling complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	C		Seeded From UniProt	complete
enables	GO:0005164	tumor necrosis factor receptor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	F		Seeded From UniProt	complete
enables	GO:0005123	death receptor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	F		Seeded From UniProt	complete
enables	GO:0002020	protease binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	F		Seeded From UniProt	complete
involved_in	GO:0001822	kidney development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8R2E7 ensembl:ENSRNOP00000066289	P		Seeded From UniProt	complete
involved_in	GO:0007165	signal transduction	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000488	P		Seeded From UniProt	complete
involved_in	GO:0042981	regulation of apoptotic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001875	P		Seeded From UniProt	complete
involved_in	GO:0008625	extrinsic apoptotic signaling pathway via death domain receptors	PMID:7538907^[1]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005123	death receptor binding	PMID:7538907^[1]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0097191	extrinsic apoptotic signaling pathway	PMID:18309324^[28]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031264	death-inducing signaling complex	PMID:18309324^[28]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1902042	negative regulation of extrinsic apoptotic signaling pathway via death domain receptors	Reactome:R-HSA-5675456 Reactome:R-HSA-3465429	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902041	regulation of extrinsic apoptotic signaling pathway via death domain receptors	Reactome:R-HSA-3371378	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097190	apoptotic signaling pathway	Reactome:R-HSA-9013895 Reactome:R-HSA-75157 Reactome:R-HSA-2562564	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071550	death-inducing signaling complex assembly	Reactome:R-HSA-5357786	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035666	TRIF-dependent toll-like receptor signaling pathway	Reactome:R-HSA-937061	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034138	toll-like receptor 3 signaling pathway	Reactome:R-HSA-168164	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007166	cell surface receptor signaling pathway	Reactome:R-HSA-73887	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	Reactome:R-HSA-69416	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-933539 Reactome:R-HSA-933532 Reactome:R-HSA-933526 Reactome:R-HSA-933523 Reactome:R-HSA-9013895 Reactome:R-HSA-9013889 Reactome:R-HSA-83650 Reactome:R-HSA-83586 Reactome:R-HSA-75240 Reactome:R-HSA-75187 Reactome:R-HSA-75146 Reactome:R-HSA-73945 Reactome:R-HSA-5675456 Reactome:R-HSA-3465459 Reactome:R-HSA-3465448 Reactome:R-HSA-3465429 Reactome:R-HSA-3371360 Reactome:R-HSA-3371359 Reactome:R-HSA-2562564 Reactome:R-HSA-2562541 Reactome:R-HSA-168934 Reactome:R-HSA-141316 Reactome:R-HSA-141310 Reactome:R-HSA-141159 Reactome:R-HSA-141156 Reactome:R-HSA-140978 Reactome:R-HSA-139952	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0053	P		Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0399	P		Seeded From UniProt	complete
involved_in	GO:0002376	immune system process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0391	P		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Chinnaiyan, AM et al. (1995) FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 81 505-12 PubMed GONUTS page
↑ ^2.0 ^2.1 Boldin, MP et al. (1995) A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J. Biol. Chem. 270 7795-8 PubMed GONUTS page
↑ Ota, T et al. (2004) Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat. Genet. 36 40-5 PubMed GONUTS page
↑ ^4.0 ^4.1 Telliez, JB et al. (2000) LRDD, a novel leucine rich repeat and death domain containing protein. Biochim. Biophys. Acta 1478 280-8 PubMed GONUTS page
↑ Eberstadt, M et al. (1998) NMR structure and mutagenesis of the FADD (Mort1) death-effector domain. Nature 392 941-5 PubMed GONUTS page
↑ McPhail, AT et al. (1976) X-ray crystal structure and conformation of a spin-labeled acetylcholine, DL-4-[N,N-dimethyl-n-(ethan-2'-olacetate)amino]-2,2,6,6-tetramethylpiperidine-1-oxyliodide. Mol. Pharmacol. 12 590-7 PubMed GONUTS page
↑ Razmara, M et al. (2002) CARD-8 protein, a new CARD family member that regulates caspase-1 activation and apoptosis. J. Biol. Chem. 277 13952-8 PubMed GONUTS page
↑ Wang, GH et al. (1997) Bovine herpesvirus 4 BORFE2 protein inhibits Fas- and tumor necrosis factor receptor 1-induced apoptosis and contains death effector domains shared with other gamma-2 herpesviruses. J. Virol. 71 8928-32 PubMed GONUTS page
↑ ^9.0 ^9.1 Jang, CY et al. (2012) Ribosomal protein S3 interacts with TRADD to induce apoptosis through caspase dependent JNK activation. Biochem. Biophys. Res. Commun. 421 474-8 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Fu, K et al. (2012) DJ-1 inhibits TRAIL-induced apoptosis by blocking pro-caspase-8 recruitment to FADD. Oncogene 31 1311-22 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Holler, N et al. (2000) Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat. Immunol. 1 489-95 PubMed GONUTS page
↑ ^12.0 ^12.1 Ketteler, R et al. (2008) A pathway sensor for genome-wide screens of intracellular proteolytic cleavage. Genome Biol. 9 R64 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Kawai, T et al. (2005) IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction. Nat. Immunol. 6 981-8 PubMed GONUTS page
↑ Ikner, A & Ashkenazi, A (2011) TWEAK induces apoptosis through a death-signaling complex comprising receptor-interacting protein 1 (RIP1), Fas-associated death domain (FADD), and caspase-8. J. Biol. Chem. 286 21546-54 PubMed GONUTS page
↑ Feoktistova, M et al. (2011) cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms. Mol. Cell 43 449-63 PubMed GONUTS page
↑ Zheng, L et al. (2006) Competitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1. Mol. Cell. Biol. 26 3505-13 PubMed GONUTS page
↑ Smith, AJ et al. (2009) Expression of the Bcl-2 protein BAD promotes prostate cancer growth. PLoS ONE 4 e6224 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 Bolze, A et al. (2010) Whole-exome-sequencing-based discovery of human FADD deficiency. Am. J. Hum. Genet. 87 873-81 PubMed GONUTS page
↑ Rébé, C et al. (2007) Caspase-8 prevents sustained activation of NF-kappaB in monocytes undergoing macrophagic differentiation. Blood 109 1442-50 PubMed GONUTS page
↑ Matsuda, A et al. (2003) Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene 22 3307-18 PubMed GONUTS page
↑ ^21.0 ^21.1 Wang, L et al. (2010) The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nat. Struct. Mol. Biol. 17 1324-9 PubMed GONUTS page
↑ ^22.0 ^22.1 Wang, J et al. (2001) Caspase-10 is an initiator caspase in death receptor signaling. Proc. Natl. Acad. Sci. U.S.A. 98 13884-8 PubMed GONUTS page
↑ Tao, RH et al. (2011) PMLRARα binds to Fas and suppresses Fas-mediated apoptosis through recruiting c-FLIP in vivo. Blood 118 3107-18 PubMed GONUTS page
↑ Koncz, G et al. (2012) Vesicles released by activated T cells induce both Fas-mediated RIP-dependent apoptotic and Fas-independent nonapoptotic cell deaths. J. Immunol. 189 2815-23 PubMed GONUTS page
↑ Shu, HB et al. (1997) Casper is a FADD- and caspase-related inducer of apoptosis. Immunity 6 751-63 PubMed GONUTS page
↑ Boldin, MP et al. (1996) Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 85 803-15 PubMed GONUTS page
↑ Van Quickelberghe, E et al. (2018) A protein-protein interaction map of the TNF-induced NF-κB signal transduction pathway. Sci Data 5 180289 PubMed GONUTS page
↑ ^28.0 ^28.1 Galluzzi, L et al. (2008) No death without life: vital functions of apoptotic effectors. Cell Death Differ. 15 1113-23 PubMed GONUTS page

[PMID:7538907-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Chinnaiyan, AM et al. (1995) FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 81 505-12 PubMed GONUTS page

[PMID:7536190-2] 2.0 ^2.1 Boldin, MP et al. (1995) A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J. Biol. Chem. 270 7795-8 PubMed GONUTS page

[PMID:14702039-3] Ota, T et al. (2004) Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat. Genet. 36 40-5 PubMed GONUTS page

[PMID:10825539-4] 4.0 ^4.1 Telliez, JB et al. (2000) LRDD, a novel leucine rich repeat and death domain containing protein. Biochim. Biophys. Acta 1478 280-8 PubMed GONUTS page

[PMID:9582077-5] Eberstadt, M et al. (1998) NMR structure and mutagenesis of the FADD (Mort1) death-effector domain. Nature 392 941-5 PubMed GONUTS page

[PMID:958207-6] McPhail, AT et al. (1976) X-ray crystal structure and conformation of a spin-labeled acetylcholine, DL-4-[N,N-dimethyl-n-(ethan-2'-olacetate)amino]-2,2,6,6-tetramethylpiperidine-1-oxyliodide. Mol. Pharmacol. 12 590-7 PubMed GONUTS page

[PMID:11821383-7] Razmara, M et al. (2002) CARD-8 protein, a new CARD family member that regulates caspase-1 activation and apoptosis. J. Biol. Chem. 277 13952-8 PubMed GONUTS page

[PMID:9343261-8] Wang, GH et al. (1997) Bovine herpesvirus 4 BORFE2 protein inhibits Fas- and tumor necrosis factor receptor 1-induced apoptosis and contains death effector domains shared with other gamma-2 herpesviruses. J. Virol. 71 8928-32 PubMed GONUTS page

[PMID:22510408-9] 9.0 ^9.1 Jang, CY et al. (2012) Ribosomal protein S3 interacts with TRADD to induce apoptosis through caspase dependent JNK activation. Biochem. Biophys. Res. Commun. 421 474-8 PubMed GONUTS page

[PMID:21785459-10] 10.0 ^10.1 ^10.2 ^10.3 Fu, K et al. (2012) DJ-1 inhibits TRAIL-induced apoptosis by blocking pro-caspase-8 recruitment to FADD. Oncogene 31 1311-22 PubMed GONUTS page

[PMID:11101870-11] 11.0 ^11.1 ^11.2 Holler, N et al. (2000) Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat. Immunol. 1 489-95 PubMed GONUTS page

[PMID:18387192-12] 12.0 ^12.1 Ketteler, R et al. (2008) A pathway sensor for genome-wide screens of intracellular proteolytic cleavage. Genome Biol. 9 R64 PubMed GONUTS page

[PMID:16127453-13] 13.0 ^13.1 ^13.2 Kawai, T et al. (2005) IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction. Nat. Immunol. 6 981-8 PubMed GONUTS page

[PMID:21525013-14] Ikner, A & Ashkenazi, A (2011) TWEAK induces apoptosis through a death-signaling complex comprising receptor-interacting protein 1 (RIP1), Fas-associated death domain (FADD), and caspase-8. J. Biol. Chem. 286 21546-54 PubMed GONUTS page

[PMID:21737330-15] Feoktistova, M et al. (2011) cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms. Mol. Cell 43 449-63 PubMed GONUTS page

[PMID:16611992-16] Zheng, L et al. (2006) Competitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1. Mol. Cell. Biol. 26 3505-13 PubMed GONUTS page

[PMID:19593445-17] Smith, AJ et al. (2009) Expression of the Bcl-2 protein BAD promotes prostate cancer growth. PLoS ONE 4 e6224 PubMed GONUTS page

[PMID:21109225-18] 18.0 ^18.1 ^18.2 Bolze, A et al. (2010) Whole-exome-sequencing-based discovery of human FADD deficiency. Am. J. Hum. Genet. 87 873-81 PubMed GONUTS page

[PMID:17047155-19] Rébé, C et al. (2007) Caspase-8 prevents sustained activation of NF-kappaB in monocytes undergoing macrophagic differentiation. Blood 109 1442-50 PubMed GONUTS page

[PMID:12761501-20] Matsuda, A et al. (2003) Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene 22 3307-18 PubMed GONUTS page

[PMID:20935634-21] 21.0 ^21.1 Wang, L et al. (2010) The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nat. Struct. Mol. Biol. 17 1324-9 PubMed GONUTS page

[PMID:11717445-22] 22.0 ^22.1 Wang, J et al. (2001) Caspase-10 is an initiator caspase in death receptor signaling. Proc. Natl. Acad. Sci. U.S.A. 98 13884-8 PubMed GONUTS page

[PMID:21803845-23] Tao, RH et al. (2011) PMLRARα binds to Fas and suppresses Fas-mediated apoptosis through recruiting c-FLIP in vivo. Blood 118 3107-18 PubMed GONUTS page

[PMID:22891283-24] Koncz, G et al. (2012) Vesicles released by activated T cells induce both Fas-mediated RIP-dependent apoptotic and Fas-independent nonapoptotic cell deaths. J. Immunol. 189 2815-23 PubMed GONUTS page

[PMID:9208847-25] Shu, HB et al. (1997) Casper is a FADD- and caspase-related inducer of apoptosis. Immunity 6 751-63 PubMed GONUTS page

[PMID:8681376-26] Boldin, MP et al. (1996) Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 85 803-15 PubMed GONUTS page

[PMID:30561431-27] Van Quickelberghe, E et al. (2018) A protein-protein interaction map of the TNF-induced NF-κB signal transduction pathway. Sci Data 5 180289 PubMed GONUTS page

[PMID:18309324-28] 28.0 ^28.1 Galluzzi, L et al. (2008) No death without life: vital functions of apoptotic effectors. Cell Death Differ. 15 1113-23 PubMed GONUTS page

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HUMAN:FADD

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