| Description | Prokaryotes and eukaryotes respond to heat shock and other forms of environmental stress by inducing synthesis of heat-shock proteins (hsp) [ ]. 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 []. Its contribution to various cellular processes including signal transduction, protein folding, protein degradation and morphological evolution has been extensively studied [, ]. 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.The sequences of hsp90s show a distinctive domain structure, with a highly-conserved N-terminal domain separated from a conserved, acidic C-terminal domain by a highly-acidic, flexible linker region.The signature pattern for the hsp90 family of proteins is located in a highly conserved region found in the N-terminal part of these proteins. | Name | Heat shock protein Hsp90, conserved site |
| Short Name | Heat_shock_protein_90_CS | Type | Conserved_site |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
