Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD (PubMed:7758105, PubMed:8612133, PubMed:23955153). 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). Stimulation of TNF-alpha receptor TNFRSF1A leads to the formation of two distinct signaling complexes (PubMed:7758105, PubMed:8612133, PubMed:14585990, PubMed:21307340). Plasma membrane-bound complex I is composed of TNFRSF1A, TRADD, RIPK1, TRAF2 and BIRC2/c-IAP1 or BIRC3 which interacts with CHUCK/IKK-alpha, IKBKB/IKK-beta and IKBKG/IKK-gamma promoting cell survival (PubMed:7758105, PubMed:8612133, PubMed:14585990, PubMed:21307340). Subsequently, TRADD, RIPK1 and TRAF2 dissociate from TNFRSF1A and form cytoplasmic complex II with FADD and caspase CASP8 promoting cell apoptosis (PubMed:21307340). Within complex I, interacts with TNFRSF1A/TNFR1, TRAF2 and kinase RIPK1 (PubMed:7758105, PubMed:10892748, PubMed:8612133). Within complex I, interacts with TRPC4AP; the interaction promotes NF-kappa B activation (PubMed:14585990). UXT1 associates with complex I; the interaction prevents the formation of complex II (PubMed:21307340). Within complex I Interacts with scaffold protein DAB2IP (PubMed:15310755). Interacts with autophagy receptor SQSTM1 (PubMed:10356400). Interacts with E3 ligase TRIP12 (By similarity). Interacts with kinase HIPK2 (PubMed:11032752). Interacts with keratin KRT14 (PubMed:11684708). Interacts with keratin KRT18 (PubMed:11684708). Interacts with keratins KRT16 and KRT17 (By similarity). Interacts with FADD (By similarity). Interacts with TOMM70 (PubMed:20628368). Shuttles between the cytoplasm and the nucleus. Found in all examined tissues. Requires the intact death domain to associate with TNFRSF1A/TNFR1. (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. Extended N-terminus.