HSPA2 In 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. Interacts with ZNF541. Component of the CatSper complex. Belongs to the heat shock protein 70 family. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Heat shock protein
Chromosomal Location of Human Ortholog: 14q23.3
Cellular Component:  CatSper complex; cell surface; cytosol; male germ cell nucleus; meiotic spindle; synaptonemal complex
Molecular Function:  chaperone binding; disordered domain specific binding; enzyme binding; glycolipid binding; protein binding; tau protein binding; unfolded protein binding
Biological Process:  male meiosis I; male meiotic nuclear division; negative regulation of inclusion body assembly; positive regulation of calcium-transporting ATPase activity; positive regulation of G2/M transition of mitotic cell cycle; positive regulation of protein phosphorylation; protein refolding; response to cold; response to heat; spermatid development; spermatogenesis; synaptonemal complex disassembly
Reference #:  P54652 (UniProtKB)
Alt. Names/Synonyms: Heat shock 70 kDa protein 2; heat shock 70kD protein 2; heat shock 70kDa protein 2; Heat shock-related 70 kDa protein 2; HSP70-2; HSP70-3; HSP72; HSPA2
Gene Symbols: HSPA2
Molecular weight: 70,021 Da
Basal Isoelectric point: 5.56  Predict pI for various phosphorylation states
Select Structure to View Below

HSPA2

Protein Structure Not Found.


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