Heat shock protein 90kDa beta member 1 (HSP90B1), known also as endoplasmin, gp96, grp94 and ERp99, is a chaperone protein that in humans is encoded by the HSP90B1 gene. HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is an endoplasmic reticulum HSP90 protein. Other HSP90 proteins are found in cytosol (see HSP90AA1; MIM 140571) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications.
Molecular chaperone that functions in the processing and transport of secreted proteins. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity.