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- Table of Contents
Facts about BAG family molecular chaperone regulator 3.
Co-chaperone for HSP70 and HSC70 chaperone proteins.
Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP in the HSP70 and HSC70 proteins thereby triggering client/substrate protein release.Nucleotide release is mediated through its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated through its binding to the substrate-binding domain (SBD) of HSPA8/HSC70 (PubMed:9873016, PubMed:27474739). Has anti-apoptotic activity (PubMed:10597216).
Human | |
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Gene Name: | BAG3 |
Uniprot: | O95817 |
Entrez: | 9531 |
Belongs to: |
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No superfamily |
BAG family molecular chaperone regulator 3; BAG-3; BAG-family molecular chaperone regulator-3; Bcl-2-associated athanogene 3; BCL2-associated athanogene 3; BCL2-binding athanogene 3; Bcl-2-binding protein Bis; BIS; CAIR-1; Docking protein CAIR-1; MGC104307
Mass (kDA):
61.595 kDA
Human | |
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Location: | 10q26.11 |
Sequence: | 10; NC_000010.11 (119651380..119677819) |
Nucleus. Cytoplasm. Colocalizes with HSF1 to the nucleus upon heat stress (PubMed:26159920).
PMID: 9873016 by Takayama S., et al. An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators.
PMID: 10597216 by Lee J.H., et al. Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell death.