TRADD
entrez
8717
canonical
uniprot
Q15628
canonical
ensembl
ENSG00000102871
resolver
ensp
ENSP00000341268
resolver
ensp
ENSP00000527894
resolver
genesymbol
TRADD
resolver
hgnc
HGNC:12030
resolver
uniprot
B2RDS3
resolver
uniprot
B3KQZ9
resolver
uniprot
Q52NZ1
resolver
uniprot_entry
TRADD_HUMAN
resolver
uniprot_sec
B2RDS3
resolver
uniprot_sec
B3KQZ9
resolver
uniprot_sec
Q52NZ1
resolver
amino_acid_sequence
MAAGQNGHEEWVGSAYLFVESSLDKVVLSDAYAHPQQKVAVYRALQAALAESGGSPDVLQMLKIHRSDPQLIVQLRFCGRQPCGRFLRAYREGALRAALQRSLAAALAQHSVPLQLELRAGAERLDALLADEERCLSCILAQQPDRLRDEELAELEDALRNLKCGSGARGGDGEVASAPLQPPVPSLSEVKPPPPPPPAQTFLFQGQPVVNRPLSLKDQQTFARSVGLKWRKVGRSLQRGCRALRDPALDSLAYEYEREGLYEQAFQLLRRFVQAEGRRATLQRLVEALEENELTSLAEDLLGLTDPNGGLA
uniprot
proteins
function
FUNCTION: Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD (PubMed:23955153, PubMed:7758105, PubMed:8612133). Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B (PubMed:7758105, PubMed:8612133). The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A (By similarity). {ECO:0000250|UniProtKB:Q3U0V2, ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:7758105, ECO:0000269|PubMed:8612133}.
uniprot
proteins
mass_dalton
34247
uniprot
proteins
mutagenesis
MUTAGEN 235; /note="R->A,K: Abolished GlcNAcylation by E.coli NleB1. Abolished ability to self-oligomerize. Strongly reduced GlcNAcylation by S.typhimurium Ssek1; when associated with A-245."; /evidence="ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:32766249"; MUTAGEN 245; /note="R->A: Strongly reduced GlcNAcylation by S.typhimurium Ssek1; when associated with A-235."; /evidence="ECO:0000269|PubMed:32766249
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Glycosylated at Arg-235 by enteropathogenic E.coli protein NleB1, C.rodentium protein NleB and S.typhimurium proteins Ssek1 and Ssek3: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNFRSF1A/TNFR1 complex, thereby disrupting TNF signaling. {ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:28069818, ECO:0000269|PubMed:29449376, ECO:0000269|PubMed:30902834, ECO:0000269|PubMed:32766249}.
uniprot
proteins
pubmed
10356400
uniprot
proteins
pubmed
10892748
uniprot
proteins
pubmed
10911999
uniprot
proteins
pubmed
11032752
uniprot
proteins
pubmed
11684708
uniprot
proteins
pubmed
14585990
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15310755
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
20628368
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21307340
uniprot
proteins
pubmed
23429285
uniprot
proteins
pubmed
23955153
uniprot
proteins
pubmed
24130170
uniprot
proteins
pubmed
28069818
uniprot
proteins
pubmed
29449376
uniprot
proteins
pubmed
30902834
uniprot
proteins
pubmed
30979585
uniprot
proteins
pubmed
32766249
uniprot
proteins
pubmed
7758105
uniprot
proteins
pubmed
8612133
uniprot
proteins
sequence_length
312
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3U0V2}. Cytoplasm {ECO:0000269|PubMed:11684708}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11684708}. Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000250|UniProtKB:Q3U0V2}.
uniprot
proteins