FunctionIn cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.
Tissue specificityHSPA1B is testis-specific.
Sequence similaritiesBelongs to the heat shock protein 70 family.
Cellular localizationCytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs.