UniProt Summary: Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone- substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity). {ECO:0000250, ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:18620420}.
Pfam DomainsGO Terms
Pfam Domains
TPR 2
TPR 1
DnaJ
GO Terms
chaperone cofactor-dependent protein refolding
de novo posttranslational protein folding
de novo protein folding
chaperone-mediated protein folding
heat shock protein binding
regulation of cellular response to heat
protein folding
cytoskeleton
regulation of cellular response to stress
regulation of response to stress
membrane
CRISPR Data
Compound HitMost Correlated Genes in ChemogenomicsTissues where Essential in the Avana Dataset (DepMap 20Q1)