1G5J57212015ENSG00000002330ENSMUSG00000024959Q92934Q61337NM_032989NM_004322NM_007522NM_001285453NP_004313NP_116784NP_001272382NP_031548The BCL2 associated agonist of cell death[5] (BAD) protein is a pro-apoptotic member of the Bcl-2 gene family which is involved in initiating apoptosis.

It does not contain a C-terminal transmembrane domain for outer mitochondrial membrane and nuclear envelope targeting, unlike most other members of the Bcl-2 family.

Bax/Bak are believed to initiate apoptosis by forming a pore in the mitochondrial outer membrane that allows cytochrome c to escape into the cytoplasm and activate the pro-apoptotic caspase cascade.

The anti-apoptotic Bcl-2 and Bcl-xL proteins inhibit cytochrome c release through the mitochondrial pore and also inhibit activation of the cytoplasmic caspase cascade by cytochrome c.[8] Dephosphorylated BAD forms a heterodimer with Bcl-2 and Bcl-xL, inactivating them and thus allowing Bax/Bak-triggered apoptosis.

When BAD is phosphorylated by Akt/protein kinase B (triggered by PIP3), it forms the BAD-(14-3-3) protein heterodimer.