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{
"metadata": {
"accession": "IPR018181",
"entry_id": null,
"type": "conserved_site",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"prosite": {
"PS00297": "Heat shock hsp70 proteins family signature 1",
"PS00329": "Heat shock hsp70 proteins family signature 2",
"PS01036": "Heat shock hsp70 proteins family signature 3"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR018181",
"name": "Heat shock protein 70, conserved site",
"type": "Conserved_site",
"children": []
},
"name": {
"name": "Heat shock protein 70, conserved site",
"short": "Heat_shock_70_CS"
},
"description": [
{
"text": "<p>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 [[cite:PUB00000958]].</p>\n\n<p>Hsp70 proteins have an average molecular weight of 70kDa [[cite:PUB00000712], [cite:PUB00000809], [cite:PUB00004019]]. 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) [[cite:PUB00004070], [cite:PUB00001766]]. Hsp70 proteins can be found in different cellular compartments(nuclear, cytosolic, mitochondrial, endoplasmic reticulum, for example).</p>\n\n<p>This entry represents three conserved sites of the heat shock 70 protein family.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00000958": {
"PMID": 9476895,
"ISBN": null,
"volume": "92",
"issue": "3",
"year": 1998,
"title": "The Hsp70 and Hsp60 chaperone machines.",
"URL": null,
"raw_pages": "351-66",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Bukau B",
"Horwich AL."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0092-8674(00)80928-9"
},
"PUB00000712": {
"PMID": 2686623,
"ISBN": null,
"volume": "11",
"issue": "2-3",
"year": 1989,
"title": "Essential roles of 70kDa heat inducible proteins.",
"URL": null,
"raw_pages": "48-52",
"medline_journal": "Bioessays",
"ISO_journal": "Bioessays",
"authors": [
"Craig EA."
],
"DOI_URL": "http://dx.doi.org/10.1002/bies.950110203"
},
"PUB00000809": {
"PMID": 2944601,
"ISBN": null,
"volume": "46",
"issue": "7",
"year": 1986,
"title": "Speculations on the functions of the major heat shock and glucose-regulated proteins.",
"URL": null,
"raw_pages": "959-61",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Pelham HR."
],
"DOI_URL": "http://dx.doi.org/10.1016/0092-8674(86)90693-8"
},
"PUB00004019": {
"PMID": 3282176,
"ISBN": null,
"volume": "332",
"issue": "6167",
"year": 1988,
"title": "Heat-shock proteins. Coming in from the cold.",
"URL": null,
"raw_pages": "776-7",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Pelham H."
],
"DOI_URL": "http://dx.doi.org/10.1038/332776a0"
},
"PUB00004070": {
"PMID": 2143562,
"ISBN": null,
"volume": "346",
"issue": "6285",
"year": 1990,
"title": "Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein.",
"URL": null,
"raw_pages": "623-8",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Flaherty KM",
"DeLuca-Flaherty C",
"McKay DB."
],
"DOI_URL": "http://dx.doi.org/10.1038/346623a0"
},
"PUB00001766": {
"PMID": 2841196,
"ISBN": null,
"volume": "64",
"issue": "2",
"year": 1988,
"title": "The Caenorhabditis elegans hsp70 gene family: a molecular genetic characterization.",
"URL": null,
"raw_pages": "241-55",
"medline_journal": "Gene",
"ISO_journal": "Gene",
"authors": [
"Snutch TP",
"Heschl MF",
"Baillie DL."
],
"DOI_URL": "http://dx.doi.org/10.1016/0378-1119(88)90339-3"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 268680,
"pathways": 163,
"proteins": 117355,
"proteomes": 21230,
"sets": 0,
"structural_models": {
"alphafold": 98383,
"bfvd": 23
},
"structures": 257,
"taxa": 49173
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
