BAG2

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 predicted BAG2 protein contains 211 amino acids. 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]

BCL2-associated athanogene 2

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 (PubMed:24318877, PubMed:9873016).

Negative regulation of protein binding Source: ARUK-UCL
Negative regulation of protein ubiquitination Source: ARUK-UCL
Negative regulation of ubiquitin protein ligase activity Source: ARUK-UCL
Positive regulation of proteasomal protein catabolic process Source: ARUK-UCL
Positive regulation of protein processing Source: ARUK-UCL
Protein folding Source: ProtInc
Protein metabolic process Source: MGI
Protein stabilization Source: ARUK-UCL
Regulation of cellular response to heat Source: Reactome

Dendritic microtubule; Cytosol, Axon; Chaperone complex; Dendrite