FADD
entrez
8772
canonical
uniprot
Q13158
canonical
ensembl
ENSG00000168040
resolver
ensp
ENSP00000301838
resolver
enst
ENST00000301838
resolver
genesymbol
FADD
resolver
genesymbol_syn
MORT1
resolver
hgnc
HGNC:3573
resolver
uniprot
Q14866
resolver
uniprot
Q6IBR4
resolver
uniprot_entry
FADD_HUMAN
resolver
uniprot_sec
Q14866
resolver
uniprot_sec
Q6IBR4
resolver
amino_acid_sequence
MDPFLVLLHSVSSSLSSSELTELKFLCLGRVGKRKLERVQSGLDLFSMLLEQNDLEPGHTELLRELLASLRRHDLLRRVDDFEAGAAAGAAPGEEDLCAAFNVICDNVGKDWRRLARQLKVSDTKIDSIEDRYPRNLTERVRESLRIWKNTEKENATVAHLVGALRSCQMNLVADLVQEVQQARDLQNRSGAMSPMSWNSDASTSEAS
uniprot
proteins
disease_involvement
DISEASE: Infections, recurrent, associated with encephalopathy, hepatic dysfunction and cardiovascular malformations (IEHDCM) [MIM:613759]: A condition with biological features of autoimmune lymphoproliferative syndrome such as high-circulating CD4(-)CD8(-)TCR-alpha-beta(+) T-cell counts, and elevated IL10 and FASL levels. Affected individuals suffer from recurrent, stereotypical episodes of fever, encephalopathy, and mild liver dysfunction sometimes accompanied by generalized seizures. The episodes can be triggered by varicella zoster virus (VZV), measles mumps rubella (MMR) attenuated vaccine, parainfluenza virus, and Epstein-Barr virus (EBV). {ECO:0000269|PubMed:21109225}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Apoptotic adapter molecule that recruits caspases CASP8 or CASP10 to the activated FAS/CD95 or TNFRSF1A/TNFR-1 receptors (PubMed:16762833, PubMed:19118384, PubMed:20935634, PubMed:23955153, PubMed:24025841, PubMed:7538907, PubMed:9184224). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed:16762833, PubMed:19118384, PubMed:20935634, PubMed:7538907, PubMed:9184224). Active CASP8 initiates the subsequent cascade of caspases mediating apoptosis (PubMed:16762833). Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling (PubMed:21109225, PubMed:24204270). {ECO:0000269|PubMed:16762833, ECO:0000269|PubMed:19118384, ECO:0000269|PubMed:20935634, ECO:0000269|PubMed:21109225, ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841, ECO:0000269|PubMed:24204270, ECO:0000269|PubMed:7538907, ECO:0000269|PubMed:9184224}.
uniprot
proteins
mass_dalton
23279
uniprot
proteins
mutagenesis
MUTAGEN 12; /note="S->R: Loss of interaction with CASP8."; /evidence="ECO:0000269|PubMed:16762833"; MUTAGEN 25; /note="F->R: Loss of interaction with FAS. Loss of self-association. Abolishes induction of apoptosis."; /evidence="ECO:0000269|PubMed:16762833"; MUTAGEN 33; /note="K->E: Loss of self-association."; /evidence="ECO:0000269|PubMed:16762833"; MUTAGEN 38; /note="R->A: Loss of interaction with CASP8."; /evidence="ECO:0000269|PubMed:16762833"; MUTAGEN 44; /note="D->R: Loss of interaction with CASP8. Abolishes induction of apoptosis. Decreased interaction with FAS."; /evidence="ECO:0000269|PubMed:16762833"; MUTAGEN 51; /note="E->R: Loss of interaction with CASP8."; /evidence="ECO:0000269|PubMed:16762833"; MUTAGEN 117; /note="R->A: Abolished GlcNAcylation by E.coli NleB1."; /evidence="ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:30979585"; MUTAGEN 117; /note="R->E: Loss of interaction with FAS."; /evidence="ECO:0000269|PubMed:20935634"; MUTAGEN 121; /note="V->N: Loss of interaction with FAS."; /evidence="ECO:0000269|PubMed:7538907"; MUTAGEN 123; /note="D->R: Strongly decreased interaction with FAS."; /evidence="ECO:0000269|PubMed:20935634"; MUTAGEN 135; /note="R->E: Strongly decreased interaction with FAS."; /evidence="ECO:0000269|PubMed:20935634"; MUTAGEN 142; /note="R->E: Decreased interaction with FAS."; /evidence="ECO:0000269|PubMed:20935634"; MUTAGEN 172; /note="L->A,E: Loss of interaction with FAS."; /evidence="ECO:0000269|PubMed:19118384, ECO:0000269|PubMed:20935634"; MUTAGEN 172; /note="L->K: Strongly decreased interaction with FAS."; /evidence="ECO:0000269|PubMed:19118384, ECO:0000269|PubMed:20935634"; MUTAGEN 175; /note="D->K: Strongly decreased interaction with FAS."; /evidence="ECO:0000269|PubMed:20935634"; MUTAGEN 176; /note="L->E: Decreased interaction with FAS."; /evidence="ECO:0000269|PubMed:19118384
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Glycosylated at Arg-117 by enteropathogenic E.coli protein NleB1, C.rodentium protein NleB and S.typhimurium protein Ssek1: arginine GlcNAcylation prevents recruitment of caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. {ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841, ECO:0000269|PubMed:28069818, ECO:0000269|PubMed:28860194}.
uniprot
proteins
pubmed
10442631
uniprot
proteins
pubmed
10825539
uniprot
proteins
pubmed
10964568
uniprot
proteins
pubmed
11034606
uniprot
proteins
pubmed
11259186
uniprot
proteins
pubmed
12702765
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16127453
uniprot
proteins
pubmed
16762833
uniprot
proteins
pubmed
18632871
uniprot
proteins
pubmed
18846110
uniprot
proteins
pubmed
19118384
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20935634
uniprot
proteins
pubmed
21109225
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23955153
uniprot
proteins
pubmed
24025841
uniprot
proteins
pubmed
24204270
uniprot
proteins
pubmed
28069818
uniprot
proteins
pubmed
28860194
uniprot
proteins
pubmed
30979585
uniprot
proteins
pubmed
7536190
uniprot
proteins
pubmed
7538907
uniprot
proteins
pubmed
9184224
uniprot
proteins
pubmed
9582077
uniprot
proteins
sequence_length
208
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24204270}.
uniprot
proteins