InterPro : IPR018181

Name  Heat shock protein 70, conserved site Short Name  Heat_shock_70_CS
Type  Conserved_site Description  Heat shock proteins, Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region [].Hsp70 proteins have an average molecular weight of 70 kDa [, , ]. In most species,there are many proteins that belong to the hsp70 family. Some of these are only expressed under stress conditions (strictly inducible), while some are present in cells under normal growth conditions and are not heat-inducible (constitutive or cognate) [, ]. Hsp70 proteins can be found in different cellular compartments(nuclear, cytosolic, mitochondrial, endoplasmic reticulum, for example).This entry represents three conserved sites of the heat shock 70 protein family.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

3 Found In

Id Name Short Name Type
IPR013126 Heat shock protein 70 family Hsp_70_fam Family
IPR012725 Chaperone DnaK Chaperone_DnaK Family
IPR010236 ISC system FeS cluster assembly, HscA chaperone ISC_FeS_clus_asmbl_HscA Family

0 Parent Features

6 Publications

First Author Title Year Journal Volume Pages
Craig EA Essential roles of 70kDa heat inducible proteins. 1989 Bioessays 11 48-52
Pelham HR Speculations on the functions of the major heat shock and glucose-regulated proteins. 1986 Cell 46 959-61
Bukau B The Hsp70 and Hsp60 chaperone machines. 1998 Cell 92 351-66
Snutch TP The Caenorhabditis elegans hsp70 gene family: a molecular genetic characterization. 1988 Gene 64 241-55
Pelham H Heat-shock proteins. Coming in from the cold. 1988 Nature 332 776-7
Flaherty KM Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. 1990 Nature 346 623-8

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)