Heat shock protein Hsp90, N-terminal (IPR020575)

Short name: Hsp90_N

Overlapping homologous superfamilies

Domain relationships


Prokaryotes and eukaryotes respond to heat shock and other forms of environmental stress by inducing synthesis of heat-shock proteins (hsp) [PMID: 2853609]. The 90 kDa 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 [PMID: 8419347, 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.

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.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.