BAG3, BIS, BAG family molecular chaperone regulator 3, BAG-3, Bcl-2-associated athanogene 3, Bcl-2-binding protein Bis, Docking protein CAIR-1
BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. [provided by RefSeq, Jul 2008],function:Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity.,similarity:Contains 1 BAG domain.,similarity:Contains 2 WW domains.,subunit:Binds to the ATPase domain of HSP70/HSC chaperones. Binds to Bcl-2 and PLC-gamma.,
