InterPro : IPR001404

Name  Heat shock protein Hsp90 family Short Name  Hsp90_fam
Type  Family Description  Molecular chaperones, or heat shock proteins (Hsps) are ubiquitous proteins that act to maintain proper protein folding within the cell []. They assist in the folding of nascent polypeptide chains, and are also involved in the re-folding of denatured proteins following proteotoxic stress. As their name implies, the heat shock proteins were first identified as proteins that were up-regulated under conditions of elevated temperature. However, subsequent studies have shown that increased Hsp expression is induced by a variety of cellular stresses, including oxidative stress and inflammation. Five major Hsp families have been determined, and are categorized according to their molecular size (Hsp100, Hsp90, Hsp70, Hsp60, and the small Hsps). Hsps are involved in a variety of cellular processes that are ATP-dependent. These include: prevention of protein aggregation, protein degradation, protein trafficking, and maintenance of signalling proteins in a conformation that permits activation.Hsp90 chaperones are unique in their ability to regulate a specific subset of cellular signalling proteins that have been implicated in disease processes, including intracellular protein kinases, steroid hormone receptors, and growth factor receptors [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

4 Contains

Id Name Short Name Type
IPR020568 Ribosomal protein S5 domain 2-type fold Ribosomal_S5_D2-typ_fold Domain
IPR003594 Histidine kinase-like ATPase, C-terminal domain HATPase_C Domain
IPR020575 Heat shock protein Hsp90, N-terminal Hsp90_N Domain
IPR019805 Heat shock protein Hsp90, conserved site Heat_shock_protein_90_CS Conserved_site

0 Found In

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Lund PA Microbial molecular chaperones. 2001 Adv Microb Physiol 44 93-140
Pratt WB The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. 1998 Proc Soc Exp Biol Med 217 420-34



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)