Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD (By similarity). Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B (By similarity). 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 (PubMed:22561347). Stimulation of TNF-alpha receptor TNFRSF1A leads to the formation of two distinct signaling complexes (PubMed:14585990). 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:14585990). Subsequently, TRADD, RIPK1 and TRAF2 dissociate from TNFRSF1A and form cytoplasmic complex II with FADD and caspase CASP8 promoting cell apoptosis (By similarity). Within complex I, interacts with TNFRSF1A/TNFR1, TRAF2 and kinase RIPK1 (By similarity). 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 (By similarity). Within complex I Interacts with scaffold protein DAB2IP (By similarity). Interacts with autophagy receptor SQSTM1 (By similarity). Interacts with E3 ligase TRIP12 (PubMed:22561347). Interacts with kinase HIPK2 (By similarity). Interacts with keratin KRT14 (PubMed:16702408). Interacts with keratin KRT18 (By similarity). Interacts with KRT16 and KRT17 (PubMed:16702408). Interacts with FADD (PubMed:30185824). Interacts with TOMM70 (By similarity). Shuttles between the cytoplasm and the nucleus. Requires the intact death domain to associate with TNFRSF1A/TNFR1. (Microbial infection) Glycosylated at Arg-243 by S.typhimurium protein Ssek1: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNFRSF1A/TNFR1 complex, thereby disrupting TNF signaling. Mice develop tumors. In a C57BL/6 genetic background, mice exhibit a shorter lifespan than wild-type, but exhibit low incidences of observable tumor formation. In the FVB/N background, which is more tumor-prone, mice show a significant increas in the spontaneous development of a broad range of tumor types.