Heat shock 70 kDa protein 6 (HSPA6)

Molecular chaperone implicated in a huge array of cellular processes, such as protection of the proteome from pressure, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the right folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation.

This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is governed by its nucleotide bound state.