InterPro : IPR020575

Name  Heat shock protein Hsp90, N-terminal Short Name  Hsp90_N
Type  Domain Description  Prokaryotes and eukaryotes respond to heat shock and other forms of environmental stress by inducing synthesis of heat-shock proteins (hsp) []. 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 []. 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. Thesequences of hsp90s show a distinctive domain structure, with a highly-conserved N-terminal domain separated from a conserved, acidic C-terminaldomain by a highly-acidic, flexible linker region.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

1 Contains

Id Name Short Name Type
IPR019805 Heat shock protein Hsp90, conserved site Heat_shock_protein_90_CS Conserved_site

1 Found In

Id Name Short Name Type
IPR001404 Heat shock protein Hsp90 family Hsp90_fam Family

1 Parent Features

Id Name Short Name Type
IPR003594 Histidine kinase-like ATPase, C-terminal domain HATPase_C Domain

4 Publications

First Author Title Year Journal Volume Pages
Lindquist S The heat-shock proteins. 1988 Annu Rev Genet 22 631-77
Nadeau K Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases. 1993 J Biol Chem 268 1479-87
Jakob U Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones. 1994 Trends Biochem Sci 19 205-11
Sreedhar AS Hsp90 isoforms: functions, expression and clinical importance. 2004 FEBS Lett 562 11-5



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)