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InterPro: IPR001023 Heat shock protein Hsp70

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10297 proteins

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Accession List
Matches in BioMart

Accession

IPR001023 Hsp70

Type

Family

Signatures Help

Database	ID	Name	Proteins
PRINTS	PR00301	HEATSHOCK70	7434
PANTHER	PTHR19375	Hsp70	10179
Signatures in BioMart

InterPro Relationships Help

Children

IPR004753 Cell shape determining protein MreB/Mrl
IPR013126 Heat shock protein 70

Contains

IPR018181 Heat shock protein 70, conserved site

GO Term annotation Help

Function

GO:0005524 ATP binding

InterPro annotation

Entry Details in BioMart

Abstract

A family of heat shock proteins, the hsp70 proteins have an average molecular weight of 70 kDa [1, 2, 3]. 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) [4, 5]. Hsp70 proteins can be found in different cellular compartments (nuclear, cytosolic, mitochondrial, endoplasmic reticulum, etc.).

Little is known of the function of hsp70 proteins. Some evidence suggests that the constitutive members have a role in the disassembly of clathrin cages [4], and may also participate in the post-translational transmembrane targetting of proteins to cellular organelles. No specific activities or associations have been found for the inducible members [4], although it has been suggested that they may accept incoming precursor proteins, keep them unfolded, then pass them on to the hsp60/hsp10 (cpn60/cpn10) complex for folding and assembly.

Structural links Help

PDB - click here

SCOP: a.8.4.1 , b.130.1.1 , c.55.1.1

CATH: 2.60.34.10 , 3.30.30.30 , 3.30.420.40 , 3.90.640.10

Database links Help

Blocks: IPB001023

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001023

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O97125 Heat shock protein 68

P08107 Heat shock 70 kDa protein 1

P09446 Heat shock 70 kDa protein A

P11484 Heat shock protein SSB1

P63017 Heat shock cognate 71 kDa protein

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR018181	Heat shock protein 70, conserved site
IPR001023	Heat shock protein Hsp70
IPR013126	Heat shock protein 70
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Craig EA. Essential roles of 70kDa heat inducible proteins. Bioessays 11 48-52 1989 [PubMed: 2686623] http://dx.doi.org/10.1002/bies.950110203
2.	Pelham HR. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 46 959-61 1986 [PubMed: 2944601] http://dx.doi.org/10.1016/0092-8674(86)90693-8
3.	Pelham H. Heat-shock proteins. Coming in from the cold. Nature 332 776-7 1988 [PubMed: 3282176] http://dx.doi.org/10.1038/332776a0
4.	Flaherty KM, DeLuca-Flaherty C, McKay DB. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346 623-8 1990 [PubMed: 2143562] http://dx.doi.org/10.1038/346623a0
5.	Snutch TP, Heschl MF, Baillie DL. The Caenorhabditis elegans hsp70 gene family: a molecular genetic characterization. Gene 64 241-55 1988 [PubMed: 2841196] http://dx.doi.org/10.1016/0378-1119(88)90339-3

Additional Reading Open in usermanual
	Schlossman DM, Schmid SL, Braell WA, Rothman JE. An enzyme that removes clathrin coats: purification of an uncoating ATPase. J. Cell Biol. 99 1984 723-33 [PubMed: 6146630] http://dx.doi.org/10.1083/jcb.99.2.723
	Jiang J, Prasad K, Lafer EM, Sousa R. Structural basis of interdomain communication in the Hsc70 chaperone. Mol. Cell 20 2005 513-24 [PubMed: 16307916] http://dx.doi.org/10.1016/j.molcel.2005.09.028
	Schuermann JP, Jiang J, Cuellar J, Llorca O, Wang L, Gimenez LE, Jin S, Taylor AB, Demeler B, Morano KA, Hart PJ, Valpuesta JM, Lafer EM, Sousa R. Structure of the Hsp110:Hsc70 nucleotide exchange machine. Mol. Cell 31 2008 232-43 [PubMed: 18550409] http://dx.doi.org/10.1016/j.molcel.2008.05.006
	Chang YW, Sun YJ, Wang C, Hsiao CD. Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation. J. Biol. Chem. 283 2008 15502-11 [PubMed: 18400763] http://dx.doi.org/10.1074/jbc.M708992200
	Cupp-Vickery JR, Peterson JC, Ta DT, Vickery LE. Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC. J. Mol. Biol. 342 2004 1265-78 [PubMed: 15351650] http://dx.doi.org/10.1016/j.jmb.2004.07.025
	Branden CI. Protein chemistry. Founding fathers and families. Nature 346 1990 607-8 [PubMed: 2143560] http://dx.doi.org/10.1038/346607a0
	Jiang J, Maes EG, Taylor AB, Wang L, Hinck AP, Lafer EM, Sousa R. Structural basis of J cochaperone binding and regulation of Hsp70. Mol. Cell 28 2007 422-33 [PubMed: 17996706] http://dx.doi.org/10.1016/j.molcel.2007.08.022
	Morimoto RI, Hunt C, Huang SY, Berg KL, Banerji SS. Organization, nucleotide sequence, and transcription of the chicken HSP70 gene. J. Biol. Chem. 261 1986 12692-9 [PubMed: 3017985] http://intl.jbc.org/cgi/reprint/261/27/12692.pdf
	Flaherty KM, McKay DB, Kabsch W, Holmes KC. Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc. Natl. Acad. Sci. U.S.A. 88 1991 5041-5 [PubMed: 1828889] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=1828889&action=stream&blobtype=pdf

InterPro 24.0