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: caspase activator activity; lipid binding; phospholipid binding; protein binding; protein heterodimerization activity; protein kinase B binding; protein kinase binding; protein phosphatase 2B binding; protein phosphatase binding
Biological Process: ADP metabolic process; apoptosis; ATP metabolic process; caspase activation; cell proliferation; cellular process regulating host cell cycle in response to virus; cytokine and chemokine mediated signaling pathway; DNA damage response, signal transduction resulting in induction of apoptosis; glucose catabolic process; glucose homeostasis; induction of apoptosis via death domain receptors; negative regulation of cytolysis; pore complex biogenesis; positive regulation of apoptosis; positive regulation of apoptosis by virus; positive regulation of B cell differentiation; positive regulation of caspase activity; positive regulation of epithelial cell proliferation; positive regulation of glucokinase activity; positive regulation of insulin secretion; positive regulation of proteolysis; positive regulation of T cell differentiation; regulation of apoptosis; regulation of caspase activity; regulation of mitochondrial membrane permeability; release of cytochrome c from mitochondria; suppression by virus of host apoptosis