Hsp70 genes, members of a multigene family, encode heat-inducible 70 kDa heat-shock proteins that function as molecular chaperones. They have been identified in most organelles of eukaryotic cells as well as in bacteria. The N-terminus of Hsp70 binds ATP with high affinity and the C-terminus binds proteins and polypeptides. Hsp70s bind nascent ploypeptides as well as partially folded intermediates of proteins, thus preventing their aggregation and/or misfolding. Binding of ATP triggers a conformational change that results in the release of bound protein. Hsp70s function in protein synthesis, protein folding and oligomerization, and protein transport.
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Protein Aliases: constitutive heat shock protein 70; epididymis luminal protein 33; epididymis secretory sperm binding protein Li 72p; Heat shock 70 kDa protein 8; heat shock 70kd protein 10; heat shock 70kD protein 8; heat shock 70kDa protein 8; Heat shock cognate 71 kDa protein; heat shock cognate hsc73; heat shock cognate protein 54; Heat shock cognate protein 70; heat shock protein 8; heat shock protein A8; heat shock protein cognate 70; LAP-1; Lipopolysaccharide-associated protein 1; LPS-associated protein 1; N-myristoyltransferase inhibitor protein 71
Gene Aliases: 2410008N15Rik; HEL-33; HEL-S-72p; HSC54; HSC70; HSC71; Hsc73; HSP71; HSP73; HSPA10; HSPA8; LAP-1; LAP1; NIP71