a pro-apoptotic member of the Bcl-2 superfamily. Targets intracellular membranes and contains a BH3 death domain. Heterodimerizes with either the pro-apoptotic protein BAX or the anti-apoptotic protein BCL2, antagonizing its protective effect. The activity of BID is regulated by Caspase 8-mediated cleavage, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, causing translocation to mitochondria where it triggers cytochrome c release. Multiple alternatively spliced variants have been found. Note: This description may include information from UniProtKB.
Molecular Function: protein binding; ubiquitin protein ligase binding; death receptor binding
Biological Process: caspase activation; release of cytochrome c from mitochondria; positive regulation of protein homooligomerization; positive regulation of apoptosis; apoptosis; DNA damage response, signal transduction; programmed cell death; response to estradiol stimulus; regulation of cell proliferation; positive regulation of protein oligomerization; neuron apoptosis; apoptotic mitochondrial changes; induction of apoptosis via death domain receptors; brain development; protein targeting to mitochondrion; protein homooligomerization
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.