Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF- kappa-B. Homotrimer. Can interact with TRADD and RIPK1. Regulated by p53/TP53. Widely expressed in adult and fetal tissues; very highly expressed in tumor cell lines such as HeLaS3, K-562, HL-60, SW480, A-549 and G-361; highly expressed in heart, peripheral blood lymphocytes, liver, pancreas, spleen, thymus, prostate, ovary, uterus, placenta, testis, esophagus, stomach and throughout the intestinal tract; not detectable in brain. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Membrane protein, integral
Cellular Component: cell surface; plasma membrane; integral to membrane; intracellular
Molecular Function: protein binding; TRAIL binding; receptor activity
Biological Process: caspase activation; regulation of apoptosis; cell surface receptor linked signal transduction; positive regulation of I-kappaB kinase/NF-kappaB cascade; induction of apoptosis via death domain receptors; apoptosis; activation of NF-kappaB-inducing kinase; programmed cell death; negative regulation of caspase activity
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.