a proapoptotic member of the Bcl-2 family. Displaces Bax from binding to Bcl-2 and Bcl-xL, resulting in cell death. Survival factors such as IL-3 can inhibit the apoptotic activity of Bad inducing the phosphorylation of Bad by Akt and p90RSK. 14-3-3 proteins bind phosphorylated Bad, inhibiting its binding to Bcl-2 and Bcl-xL. Phosphorylation by mitochondria-anchored PKA in the BH3 domain can block the dimerization of Bad and Bcl-xL. Note: This description may include information from UniProtKB.
Molecular Function: protein kinase B binding; protein binding; protein heterodimerization activity; phospholipid binding; caspase activator activity; protein phosphatase binding; protein kinase binding; lipid binding; protein phosphatase 2B binding
Biological Process: caspase activation; release of cytochrome c from mitochondria; apoptosis; positive regulation of proteolysis; positive regulation of apoptosis; cytokine and chemokine mediated signaling pathway; suppression by virus of host apoptosis; positive regulation of insulin secretion; ADP metabolic process; positive regulation of caspase activity; cellular process regulating host cell cycle in response to virus; glucose homeostasis; regulation of caspase activity; positive regulation of apoptosis by virus; ATP metabolic process; regulation of apoptosis; cell proliferation; glucose catabolic process; positive regulation of T cell differentiation; induction of apoptosis via death domain receptors; DNA damage response, signal transduction resulting in induction of apoptosis; pore complex biogenesis; positive regulation of B cell differentiation; regulation of mitochondrial membrane permeability; positive regulation of epithelial cell proliferation; positive regulation of glucokinase 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.