Heat shock protein Hsp90, N-terminal
IPR020575
Definition
Prokaryotes and eukaryotes respond to heat shock and other forms of environmental stress by inducing synthesis of heat-shock proteins (hsp) PMID:2853609. The 90kDa heat shock protein, Hsp90, is one of the most abundant proteins in eukaryotic cells, comprising 1-2% of cellular proteins under non-stress conditions PMID:15069952. Its contribution to various cellular processes including signal transduction, protein folding, protein degradation and morphological evolution has been extensively studied [[cite:PMID:8419347], [cite:PMID:7914036]]. The full functional activity of Hsp90 is gained in concert with other co-chaperones, playing an important role in the folding of newly synthesised proteins and stabilisation and refolding of denatured proteins after stress. Apart from its co-chaperones, Hsp90 binds to an array of client proteins, where the co-chaperone requirement varies and depends on the actual client [[cite:PMID:19697319], [cite:PMID:24462206], [cite:PMID:26616658], [cite:PMID:26884463], [cite:PMID:26929380], [cite:PMID:22008467]]. This entry represents the histidine kinase-like ATPase (HATPase) domain Hsp90 from eukaryotes and its bacterial homologues, known as HtpG (High temperature protein G).
9 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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