HSPA6
Description
The HSPA6 (heat shock protein family A (Hsp70) member 6) is a protein-coding gene located on chromosome 1.
Heat shock 70 kDa protein 6 is a protein encoded by the HSPA6 gene in humans.
HSPA6 is a molecular chaperone involved in a wide range of cellular processes, including: protecting the proteome from stress, folding and transporting newly synthesized polypeptides, activating the breakdown of misfolded proteins, and assembling and disassembling protein complexes. It plays a crucial role in protein quality control, ensuring proteins fold correctly, refolding misfolded proteins, and directing misfolded proteins for degradation. This is accomplished through cycles of ATP binding, ATP hydrolysis, and ADP release, mediated by co-chaperones. Its affinity for polypeptides is regulated by its nucleotide-bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolyzing ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It repeatedly cycles through ATP hydrolysis and nucleotide exchange, allowing for cycles of substrate binding and release.
HSPA6 is also known as HSP70B'.
