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BAG3 a co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSC70. Has anti-apoptotic activity. Plays a role in the HSF1 nucleocytoplasmic transport. May be involved in neuronal differentiation and migration. Note: This description may include information from UniProtKB.
Protein type: Apoptosis; Chaperone
Chromosomal Location of Human Ortholog: 10q26.11
Cellular Component: cytoplasm; cytosol; neuron projection; nucleus; plasma membrane; Z disc
Molecular Function: adenyl-nucleotide exchange factor activity; cadherin binding; chaperone binding; protein binding; protein complex binding
Biological Process: brain development; induction of apoptosis via death domain receptors; negative regulation of apoptosis; positive regulation of protein export from nucleus; positive regulation of transcription factor import into nucleus; protein folding; protein stabilization; regulation of catalytic activity; spinal cord development
Disease: Cardiomyopathy, Dilated, 1hh; Myopathy, Myofibrillar, 6
Reference #:  O95817 (UniProtKB)
Alt. Names/Synonyms: BAG family molecular chaperone regulator 3; BAG-3; BAG-family molecular chaperone regulator-3; BAG3; Bcl-2-associated athanogene 3; Bcl-2-binding protein Bis; BCL2-associated athanogene 3; BCL2-binding athanogene 3; BIS; CAIR-1; Docking protein CAIR-1; MGC104307
Gene Symbols: BAG3
Molecular weight: 61,595 Da
Basal Isoelectric point: 6.46  Predict pI for various phosphorylation states
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Protein Structure Not Found.
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