TRADD
Domain
Requires the intact death domain to associate with TNFRSF1A/TNFR1.
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).
Post-translational modifications
(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.
Tissue Specificity
Found in all examined tissues.
Cellular localization
- Nucleus
- Cytoplasm
- Cytoplasm
- Cytoskeleton
- Shuttles between the cytoplasm and the nucleus.
Alternative names
Tumor necrosis factor receptor type 1-associated DEATH domain protein, TNFR1-associated DEATH domain protein, TNFRSF1A-associated via death domain, TRADD