HSPA2


Description

The HSPA2 (heat shock protein family A (Hsp70) member 2) is a protein-coding gene located on chromosome 14.

Heat shock-related 70 kDa protein 2 is a protein that in humans is encoded by the HSPA2 gene.

HSPA2 acts as a molecular chaperone, participating in various cellular functions. It shields the proteome from stress, assists in folding and transporting newly synthesized polypeptides, activates the degradation of misfolded proteins, and aids in forming and disassembling protein complexes. Playing a key role in protein quality control, it ensures correct protein folding, refolds misfolded proteins, and directs proteins for degradation. This process is achieved through cycles of ATP binding, hydrolysis, and ADP release, regulated by co-chaperones. The affinity for polypeptides varies depending on its nucleotide binding state. In the ATP-bound state, it has low affinity for substrates, but upon ATP hydrolysis to ADP, it undergoes a conformational change, increasing its affinity. This dynamic process of ATP hydrolysis and nucleotide exchange enables cycles of substrate binding and release (PubMed:26865365). It is involved in spermatogenesis, possibly contributing to maintaining spindle integrity during meiosis in male germ cells in association with SHCBP1L (By similarity). {ECO:0000250|UniProtKB:P17156, ECO:0000303|PubMed:26865365}

HSPA2 is also known as HSP70-2, HSP70-3.

Associated Diseases



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