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{
"metadata": {
"accession": "cd11733",
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"source_database": "cdd",
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"name": {
"name": "nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and similar proteins",
"short": "ASKHA_NBD_HSP70_HSPA9"
},
"description": [
{
"text": "<p>This subgroup includes human mitochondrial HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74). It acts as a chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. It interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. HSPA9 regulates erythropoiesis via stabilization of ISC assembly. It may play a role in the control of cell proliferation and cellular aging. Members in this subgroup belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent \"client\" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). [[cite:PUB00156868], [cite:PUB00156943], [cite:PUB00156944], [cite:PUB00156945], [cite:PUB00156946], [cite:PUB00156947], [cite:PUB00156948], [cite:PUB00156949], [cite:PUB00156950], [cite:PUB00156951], [cite:PUB00156952], [cite:PUB00156953]]</p>",
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"volume": "5",
"issue": null,
"year": 2015,
"title": "Mutations in the heat-shock protein A9 (HSPA9) gene cause the EVEN-PLUS syndrome of congenital malformations and skeletal dysplasia.",
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"raw_pages": "17154",
"medline_journal": "Sci Rep",
"ISO_journal": "Sci Rep",
"authors": [
"Royer-Bertrand B",
"Castillo-Taucher S",
"Moreno-Salinas R",
"Cho TJ",
"Chae JH",
"Choi M",
"Kim OH",
"Dikoglu E",
"Campos-Xavier B",
"Girardi E",
"Superti-Furga G",
"Bonafe L",
"Rivolta C",
"Unger S",
"Superti-Furga A."
],
"DOI_URL": "https://doi.org/10.1038/srep17154"
},
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"volume": "123",
"issue": "16",
"year": 2019,
"title": "Biophysical Consequences of EVEN-PLUS Syndrome Mutations for the Function of Mortalin.",
"URL": null,
"raw_pages": "3383-3396",
"medline_journal": "J Phys Chem B",
"ISO_journal": "J Phys Chem B",
"authors": [
"Moseng MA",
"Nix JC",
"Page RC."
],
"DOI_URL": "https://doi.org/10.1021/acs.jpcb.9b00071"
},
"PUB00156947": {
"PMID": 23940031,
"ISBN": null,
"volume": "288",
"issue": "40",
"year": 2013,
"title": "Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU).",
"URL": null,
"raw_pages": "28755-70",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Cai K",
"Frederick RO",
"Kim JH",
"Reinen NM",
"Tonelli M",
"Markley JL."
],
"DOI_URL": "https://doi.org/10.1074/jbc.M113.482042"
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"volume": "19",
"issue": "19",
"year": 2010,
"title": "Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesis.",
"URL": null,
"raw_pages": "3816-34",
"medline_journal": "Hum Mol Genet",
"ISO_journal": "Hum Mol Genet",
"authors": [
"Uhrigshardt H",
"Singh A",
"Kovtunovych G",
"Ghosh M",
"Rouault TA."
],
"DOI_URL": "https://doi.org/10.1093/hmg/ddq301"
},
"PUB00156952": {
"PMID": 7829505,
"ISBN": null,
"volume": "270",
"issue": "4",
"year": 1995,
"title": "Cloning and subcellular localization of human mitochondrial hsp70.",
"URL": null,
"raw_pages": "1705-10",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Bhattacharyya T",
"Karnezis AN",
"Murphy SP",
"Hoang T",
"Freeman BC",
"Phillips B",
"Morimoto RI."
],
"DOI_URL": "https://doi.org/10.1074/jbc.270.4.1705"
},
"PUB00156944": {
"PMID": 26702583,
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"volume": "26",
"issue": null,
"year": 2016,
"title": "Mitochondrial Hspa9/Mortalin regulates erythroid differentiation via iron-sulfur cluster assembly.",
"URL": null,
"raw_pages": "94-103",
"medline_journal": "Mitochondrion",
"ISO_journal": "Mitochondrion",
"authors": [
"Shan Y",
"Cortopassi G."
],
"DOI_URL": "https://doi.org/10.1016/j.mito.2015.12.005"
},
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"volume": "117",
"issue": "5",
"year": 2011,
"title": "Knockdown of Hspa9, a del(5q31.2) gene, results in a decrease in hematopoietic progenitors in mice.",
"URL": null,
"raw_pages": "1530-9",
"medline_journal": "Blood",
"ISO_journal": "Blood",
"authors": [
"Chen TH",
"Kambal A",
"Krysiak K",
"Walshauser MA",
"Raju G",
"Tibbitts JF",
"Walter MJ."
],
"DOI_URL": "https://doi.org/10.1182/blood-2010-06-293167"
},
"PUB00156946": {
"PMID": 26491070,
"ISBN": null,
"volume": "126",
"issue": "25",
"year": 2015,
"title": "Congenital sideroblastic anemia due to mutations in the mitochondrial HSP70 homologue HSPA9.",
"URL": null,
"raw_pages": "2734-8",
"medline_journal": "Blood",
"ISO_journal": "Blood",
"authors": [
"Schmitz-Abe K",
"Ciesielski SJ",
"Schmidt PJ",
"Campagna DR",
"Rahimov F",
"Schilke BA",
"Cuijpers M",
"Rieneck K",
"Lausen B",
"Linenberger ML",
"Sendamarai AK",
"Guo C",
"Hofmann I",
"Newburger PE",
"Matthews D",
"Shimamura A",
"Snijders PJ",
"Towne MC",
"Niemeyer CM",
"Watson HG",
"Dziegiel MH",
"Heeney MM",
"May A",
"Bottomley SS",
"Swinkels DW",
"Markianos K",
"Craig EA",
"Fleming MD."
],
"DOI_URL": "https://doi.org/10.1182/blood-2015-09-659854"
},
"PUB00156949": {
"PMID": 23462535,
"ISBN": null,
"volume": "56",
"issue": null,
"year": 2013,
"title": "Structural and stability studies of the human mtHsp70-escort protein 1: an essential mortalin co-chaperone.",
"URL": null,
"raw_pages": "140-8",
"medline_journal": "Int J Biol Macromol",
"ISO_journal": "Int J Biol Macromol",
"authors": [
"Dores-Silva PR",
"Minari K",
"Ramos CH",
"Barbosa LR",
"Borges JC."
],
"DOI_URL": "https://doi.org/10.1016/j.ijbiomac.2013.02.009"
},
"PUB00156868": {
"PMID": 24687350,
"ISBN": null,
"volume": "23",
"issue": "6",
"year": 2014,
"title": "Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone.",
"URL": null,
"raw_pages": "833-42",
"medline_journal": "Protein Sci",
"ISO_journal": "Protein Sci",
"authors": [
"Amick J",
"Schlanger SE",
"Wachnowsky C",
"Moseng MA",
"Emerson CC",
"Dare M",
"Luo WI",
"Ithychanda SS",
"Nix JC",
"Cowan JA",
"Page RC",
"Misra S."
],
"DOI_URL": "https://doi.org/10.1002/pro.2466"
},
"PUB00156953": {
"PMID": 7684501,
"ISBN": null,
"volume": "13",
"issue": "6",
"year": 1993,
"title": "Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family.",
"URL": null,
"raw_pages": "3598-610",
"medline_journal": "Mol Cell Biol",
"ISO_journal": "Mol Cell Biol",
"authors": [
"Domanico SZ",
"DeNagel DC",
"Dahlseid JN",
"Green JM",
"Pierce SK."
],
"DOI_URL": "https://doi.org/10.1128/mcb.13.6.3598-3610.1993"
},
"PUB00156948": {
"PMID": 23541579,
"ISBN": null,
"volume": "434",
"issue": "1",
"year": 2013,
"title": "Extracellular heat shock protein A9 is a novel interaction partner of podoplanin in oral squamous cell carcinoma cells.",
"URL": null,
"raw_pages": "124-30",
"medline_journal": "Biochem Biophys Res Commun",
"ISO_journal": "Biochem Biophys Res Commun",
"authors": [
"Tsuneki M",
"Maruyama S",
"Yamazaki M",
"Xu B",
"Essa A",
"Abe T",
"Babkair H",
"Cheng J",
"Yamamoto T",
"Saku T."
],
"DOI_URL": "https://doi.org/10.1016/j.bbrc.2013.03.057"
}
},
"set_info": {
"accession": "cl17037",
"name": "NBD_sugar-kinase_HSP70_actin"
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"counters": {
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"is_llm": false,
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"representative_structure": {
"accession": "6p2u",
"name": "Structure of Mortalin-NBD with N6-propargyladenosine-5'-diphosphate"
}
}
}
