PROSITE documentation PDOC00269
Heat shock hsp70 proteins family signatures


Prokaryotic and eukaryotic organisms respond to heat shock or other environmental stress by the induction of the synthesis of proteins collectively known as heat-shock proteins (hsp) [1]. Amongst them is a family of proteins with an average molecular weight of 70 Kd, known as the hsp70 proteins [2,3,4]. In most species, there are many proteins that belong to the hsp70 family. Some of them are expressed under unstressed conditions. Hsp70 proteins can be found in different cellular compartments (nuclear, cytosolic, mitochondrial, endoplasmic reticulum, etc.). Some of the hsp70 family proteins are listed below:

  • In Escherichia coli and other bacteria, the main hsp70 protein is known as the dnaK protein. A second protein, hscA, has been recently discovered. dnaK is also found in the chloroplast genome of red algae.
  • In yeast, at least ten hsp70 proteins are known to exist: SSA1 to SSA4, SSB1, SSB2, SSC1, SSD1 (KAR2), SSE1 (MSI3) and SSE2.
  • In Drosophila, there are at least eight different hsp70 proteins: HSP70, HSP68, and HSC-1 to HSC-6.
  • In mammals, there are at least eight different proteins: HSPA1 to HSPA6, HSC70, and GRP78 (also known as the immunoglobulin heavy chain binding protein (BiP)).
  • In the sugar beet yellow virus (SBYV), a hsp70 homolog has been shown [5] to exist.
  • In archaebacteria, hsp70 proteins are also present [6].

All proteins belonging to the hsp70 family bind ATP. A variety of functions has been postulated for hsp70 proteins. It now appears [7] that some hsp70 proteins play an important role in the transport of proteins across membranes. They also seem to be involved in protein folding and in the assembly/ disassembly of protein complexes [8].

We have derived three signature patterns for the hsp70 family of proteins; the first centered on a conserved pentapeptide found in the N-terminal section of these proteins; the two others on conserved regions located in the central part of the sequence.

Expert(s) to contact by email:

Genevaux P.

Last update:

December 2004 / Pattern and text revised.


Technical section

PROSITE methods (with tools and information) covered by this documentation:

HSP70_1, PS00297; Heat shock hsp70 proteins family signature 1  (PATTERN)

HSP70_2, PS00329; Heat shock hsp70 proteins family signature 2  (PATTERN)

HSP70_3, PS01036; Heat shock hsp70 proteins family signature 3  (PATTERN)


1AuthorsLindquist S. Craig E.A.
TitleThe heat-shock proteins.
SourceAnnu. Rev. Genet. 22:631-677(1988).
PubMed ID2853609

2AuthorsPelham H.R.B.
TitleSpeculations on the functions of the major heat shock and glucose-regulated proteins.
SourceCell 46:959-961(1986).
PubMed ID2944601

3AuthorsPelham H.
TitleHeat-shock proteins. Coming in from the cold.
SourceNature 332:776-777(1988).
PubMed ID3282176

4AuthorsCraig E.A.
TitleEssential roles of 70kDa heat inducible proteins.
SourceBioEssays 11:48-52(1989).
PubMed ID2686623

5AuthorsAgranovsky A.A. Boyko V.P. Karasev A.V. Koonin E.V. Dolja V.V.
TitlePutative 65 kDa protein of beet yellows closterovirus is a homologue of HSP70 heat shock proteins.
SourceJ. Mol. Biol. 217:603-610(1991).
PubMed ID2005613

6AuthorsGupta R.S. Singh B.
TitleCloning of the HSP70 gene from Halobacterium marismortui: relatedness of archaebacterial HSP70 to its eubacterial homologs and a model for the evolution of the HSP70 gene.
SourceJ. Bacteriol. 174:4594-4605(1992).
PubMed ID1624448

7AuthorsDeshaies R.J. Koch B.D. Schekman R.
TitleThe role of stress proteins in membrane biogenesis.
SourceTrends Biochem. Sci. 13:384-388(1988).
PubMed ID3072700

8AuthorsCraig E.A. Gross C.A.
TitleIs hsp70 the cellular thermometer?
SourceTrends Biochem. Sci. 16:135-140(1991).
PubMed ID1877088

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)