Heat shock protein 70 family
IPR013126
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 the Hsp70 family, and includes chaperone protein DnaK and luminal-binding proteins. It also includes heat shock protein 110 (Hsp110) from Caenorhabditis elegans which helps prevent the aggregation of denatured proteins in neurons PMID:19165329. Also included is endoplasmic reticulum (ER) chaperone BiP (HSPA5) which is important for protein folding and quality control in the ER PMID:26655470. The Heat Shock Protein 70 (HSP70) family is a group of highly conserved molecular chaperones involved in a variety of cellular processes. Members of this family play crucial roles in the folding of newly synthesized proteins, preventing the aggregation of denatured proteins under stress, assisting in protein translocation into organelles, and participating in the degradation of damaged proteins. They are also implicated in the assembly of multimeric protein complexes within the endoplasmic reticulum. Some HSP70 proteins act as nucleotide-exchange factors, promoting the release of ADP from other chaperones to trigger substrate release. They are essential for cellular protection against stress conditions such as heat shock and hypoxia, where they may help in cytoprotection and protein folding.
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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