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; protein heterodimerization activity; ubiquitin protein ligase binding
Biological Process: apoptotic mitochondrial changes; caspase activation; DNA damage response, signal transduction; organelle ATP synthesis coupled electron transport; positive regulation of apoptosis; positive regulation of protein homooligomerization; positive regulation of protein oligomerization; protein homooligomerization; protein targeting to mitochondrion; regulation of apoptosis; regulation of cell proliferation; regulation of protein oligomerization; release of cytochrome c from mitochondria