Heat shock protein 70, conserved site
IPR018181
Definition
Heat shock proteins, Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region PMID:9476895. Hsp70 proteins have an average molecular weight of 70kDa [[cite:PMID:2686623], [cite:PMID:2944601], [cite:PMID:3282176]]. In most species,there are many proteins that belong to the hsp70 family. Some of these are only expressed under stress conditions (strictly inducible), while some are present in cells under normal growth conditions and are not heat-inducible (constitutive or cognate) [[cite:PMID:2143562], [cite:PMID:2841196]]. Hsp70 proteins can be found in different cellular compartments(nuclear, cytosolic, mitochondrial, endoplasmic reticulum, for example). This entry represents three conserved sites of the heat shock 70 protein family.
15 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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