an adaptor molecule that mediates apoptosis. Recruited through its C-terminal death domain by Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TRAIL-receptor, participating in the death signaling initiated by these receptors. Interaction with the receptors unmasks the N-terminal effector domain of this protein, which recruits caspase-8, and thereby activates the cysteine protease cascade. Knockout studies in mice also suggest the importance of this protein in early T cell development. Note: This description may include information from UniProtKB.
Molecular Function: death receptor binding; identical protein binding; protease binding; protein binding; protein complex binding; tumor necrosis factor receptor binding; tumor necrosis factor receptor superfamily binding
Biological Process: apoptosis; caspase activation; cell surface receptor linked signal transduction; defense response to virus; induction of apoptosis via death domain receptors; innate immune response; lymph node development; positive regulation of activated T cell proliferation; positive regulation of adaptive immune response; positive regulation of apoptosis; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of interferon-gamma production; positive regulation of interleukin-8 production; positive regulation of macrophage differentiation; positive regulation of proteolysis; positive regulation of T cell mediated cytotoxicity; positive regulation of transcription from RNA polymerase II promoter; positive regulation of tumor necrosis factor production; protein heterooligomerization; spleen development; T cell differentiation in the thymus; T cell homeostasis; thymus development; viral reproduction
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.