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Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (MOT) (Peptide-binding protein 74) (PBP74)

 GRP75_HUMAN             Reviewed;         679 AA.
P38646; B2RCM1; P30036; P31932; Q1HB43; Q53H23; Q6GU03; Q9BWB7;
Q9UC56;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
27-MAY-2002, sequence version 2.
20-JUN-2018, entry version 200.
RecName: Full=Stress-70 protein, mitochondrial;
AltName: Full=75 kDa glucose-regulated protein;
Short=GRP-75;
AltName: Full=Heat shock 70 kDa protein 9;
AltName: Full=Mortalin;
Short=MOT;
AltName: Full=Peptide-binding protein 74;
Short=PBP74;
Flags: Precursor;
Name=HSPA9; Synonyms=GRP75, HSPA9B, mt-HSP70;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=B-cell;
PubMed=7684501; DOI=10.1128/MCB.13.6.3598;
Domanico S.Z., Denagel D.C., Dahlseid J.N., Green J.M., Pierce S.K.;
"Cloning of the gene encoding peptide-binding protein 74 shows that it
is a new member of the heat shock protein 70 family.";
Mol. Cell. Biol. 13:3598-3610(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7829505; DOI=10.1074/jbc.270.4.1705;
Bhattacharyya T., Karnezis A.N., Murphy S.P., Hoang T., Freeman B.C.,
Phillips B., Morimoto R.I.;
"Cloning and subcellular localization of human mitochondrial hsp70.";
J. Biol. Chem. 270:1705-1710(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-184.
NIEHS SNPs program;
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-74.
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 47-68.
TISSUE=Colon carcinoma;
PubMed=9150948; DOI=10.1002/elps.1150180344;
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[9]
PROTEIN SEQUENCE OF 47-66.
TISSUE=Mammary gland;
PubMed=7498169; DOI=10.1002/elps.11501601202;
Giometti C.S., Tollaksen S.L., Chubb C., Williams C., Huberman E.;
"Analysis of proteins from human breast epithelial cells using two-
dimensional gel electrophoresis.";
Electrophoresis 16:1215-1224(1995).
[10]
PROTEIN SEQUENCE OF 47-56.
TISSUE=Liver;
PubMed=1286669; DOI=10.1002/elps.11501301201;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by
microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[11]
SEQUENCE REVISION.
TISSUE=Liver;
PubMed=8313870; DOI=10.1002/elps.11501401181;
Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C.,
Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.;
"Human liver protein map: update 1993.";
Electrophoresis 14:1216-1222(1993).
[12]
PROTEIN SEQUENCE OF 86-99; 108-121; 160-173; 188-202; 207-234;
349-360; 378-391; 395-405; 469-485; 499-513 AND 542-555, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[13]
INTERACTION WITH FXN.
PubMed=17331979; DOI=10.1093/hmg/ddm038;
Shan Y., Napoli E., Cortopassi G.;
"Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex
and multiple mitochondrial chaperones.";
Hum. Mol. Genet. 16:929-941(2007).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-138; LYS-143;
LYS-234; LYS-288; LYS-300; LYS-567 AND LYS-646, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
INTERACTION WITH HSCB.
PubMed=20668094; DOI=10.1093/hmg/ddq301;
Uhrigshardt H., Singh A., Kovtunovych G., Ghosh M., Rouault T.A.;
"Characterization of the human HSC20, an unusual DnaJ type III
protein, involved in iron-sulfur cluster biogenesis.";
Hum. Mol. Genet. 19:3816-3834(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
FUNCTION.
PubMed=21123823; DOI=10.1182/blood-2010-06-293167;
Chen T.H., Kambal A., Krysiak K., Walshauser M.A., Raju G.,
Tibbitts J.F., Walter M.J.;
"Knockdown of Hspa9, a del(5q31.2) gene, results in a decrease in
hematopoietic progenitors in mice.";
Blood 117:1530-1539(2011).
[18]
MALONYLATION AT LYS-206.
PubMed=21908771; DOI=10.1074/mcp.M111.012658;
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
Dai J., Verdin E., Ye Y., Zhao Y.;
"The first identification of lysine malonylation substrates and its
regulatory enzyme.";
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
[19]
IDENTIFICATION IN THE MINOS/MITOS COMPLEX.
PubMed=22114354; DOI=10.1091/mbc.E11-09-0774;
Alkhaja A.K., Jans D.C., Nikolov M., Vukotic M., Lytovchenko O.,
Ludewig F., Schliebs W., Riedel D., Urlaub H., Jakobs S., Deckers M.;
"MINOS1 is a conserved component of mitofilin complexes and required
for mitochondrial function and cristae organization.";
Mol. Biol. Cell 23:247-257(2012).
[20]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=22002106; DOI=10.1074/mcp.M111.013680;
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
"Systematic analysis of protein pools, isoforms, and modifications
affecting turnover and subcellular localization.";
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
[21]
INTERACTION WITH TESPA.
PubMed=23501103; DOI=10.1016/j.bbrc.2013.02.099;
Matsuzaki H., Fujimoto T., Tanaka M., Shirasawa S.;
"Tespa1 is a novel component of mitochondria-associated endoplasmic
reticulum membranes and affects mitochondrial calcium flux.";
Biochem. Biophys. Res. Commun. 433:322-326(2013).
[22]
INTERACTION WITH PDPN.
PubMed=23541579; DOI=10.1016/j.bbrc.2013.03.057;
Tsuneki M., Maruyama S., Yamazaki M., Xu B., Essa A., Abe T.,
Babkair H., Cheng J., Yamamoto T., Saku T.;
"Extracellular heat shock protein A9 is a novel interaction partner of
podoplanin in oral squamous cell carcinoma cells.";
Biochem. Biophys. Res. Commun. 434:124-130(2013).
[23]
INTERACTION WITH DNLZ.
PubMed=23462535; DOI=10.1016/j.ijbiomac.2013.02.009;
Dores-Silva P.R., Minari K., Ramos C.H., Barbosa L.R., Borges J.C.;
"Structural and stability studies of the human mtHsp70-escort protein
1: An essential mortalin co-chaperone.";
Int. J. Biol. Macromol. 56:140-148(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-87 AND SER-408, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-513, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[27]
INVOLVEMENT IN SIDBA4, VARIANTS SIDBA4 PRO-212; SER-388; LYS-415 AND
458-ILE-ASN-459 DEL, AND VARIANTS LEU-200; LYS-539; TRP-573 AND
LYS-577.
PubMed=26491070; DOI=10.1182/blood-2015-09-659854;
Schmitz-Abe K., Ciesielski S.J., Schmidt P.J., Campagna D.R.,
Rahimov F., Schilke B.A., Cuijpers M., Rieneck K., Lausen B.,
Linenberger M.L., Sendamarai A.K., Guo C., Hofmann I., Newburger P.E.,
Matthews D., Shimamura A., Snijders P.J., Towne M.C., Niemeyer C.M.,
Watson H.G., Dziegiel M.H., Heeney M.M., May A., Bottomley S.S.,
Swinkels D.W., Markianos K., Craig E.A., Fleming M.D.;
"Congenital sideroblastic anemia due to mutations in the mitochondrial
HSP70 homologue HSPA9.";
Blood 126:2734-2738(2015).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[29]
INVOLVEMENT IN EVPLS, AND VARIANTS EVPLS TRP-126 AND CYS-128.
PubMed=26598328; DOI=10.1038/srep17154;
Royer-Bertrand B., Castillo-Taucher S., Moreno-Salinas R., Cho T.J.,
Chae J.H., Choi M., Kim O.H., Dikoglu E., Campos-Xavier B.,
Girardi E., Superti-Furga G., Bonafe L., Rivolta C., Unger S.,
Superti-Furga A.;
"Mutations in the heat-shock protein A9 (HSPA9) gene cause the EVEN-
PLUS syndrome of congenital malformations and skeletal dysplasia.";
Sci. Rep. 5:17154-17154(2015).
[30]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FXN; NFU1; NFS1 AND
ISCU, AND MUTAGENESIS OF GLY-489.
PubMed=26702583; DOI=10.1016/j.mito.2015.12.005;
Shan Y., Cortopassi G.;
"Mitochondrial Hspa9/Mortalin regulates erythroid differentiation via
iron-sulfur cluster assembly.";
Mitochondrion 26:94-103(2016).
-!- FUNCTION: Chaperone protein which plays an important role in
mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with
and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and
ISCU (PubMed:26702583). Regulates erythropoiesis via stabilization
of ISC assembly (PubMed:21123823, PubMed:26702583). May play a
role in the control of cell proliferation and cellular aging (By
similarity). {ECO:0000250|UniProtKB:P38647,
ECO:0000269|PubMed:21123823, ECO:0000269|PubMed:26702583}.
-!- SUBUNIT: Interacts strongly with the intermediate form of FXN and
weakly with its mature form (PubMed:17331979, PubMed:26702583).
Interacts with HSCB (PubMed:20668094). Associates with the
mitochondrial contact site and cristae organizing system (MICOS)
complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19,
CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and
QIL1/MIC13. This complex was also known under the names MINOS or
MitOS complex. The MICOS complex associates with mitochondrial
outer membrane proteins SAMM50, MTX1, MTX2 and DNAJC11,
mitochondrial inner membrane protein TMEM11 and with HSPA9
(PubMed:22114354). Interacts with DNLZ, the interaction is
required to prevent self-aggregation (PubMed:23462535). Interacts
with TESPA1 (PubMed:23501103). Interacts with PDPN
(PubMed:23541579). Interacts with NFU1, NFS1 and ISCU
(PubMed:26702583). {ECO:0000269|PubMed:17331979,
ECO:0000269|PubMed:20668094, ECO:0000269|PubMed:22114354,
ECO:0000269|PubMed:23462535, ECO:0000269|PubMed:23501103,
ECO:0000269|PubMed:23541579, ECO:0000269|PubMed:26702583}.
-!- INTERACTION:
P00533:EGFR; NbExp=4; IntAct=EBI-354932, EBI-297353;
Q8IWL3:HSCB; NbExp=14; IntAct=EBI-354932, EBI-1805738;
Q8WX92:NELFB; NbExp=2; IntAct=EBI-354932, EBI-347721;
P04637:TP53; NbExp=6; IntAct=EBI-354932, EBI-366083;
O15350:TP73; NbExp=11; IntAct=EBI-354932, EBI-389606;
A4D2J0:YKT6; NbExp=3; IntAct=EBI-354932, EBI-10173443;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22002106,
ECO:0000269|PubMed:26702583}. Nucleus, nucleolus
{ECO:0000269|PubMed:22002106}.
-!- DISEASE: Anemia, sideroblastic, 4 (SIDBA4) [MIM:182170]: A form of
sideroblastic anemia, a bone marrow disorder defined by the
presence of pathologic iron deposits in erythroblast mitochondria.
Sideroblastic anemia is characterized by anemia of varying
severity, hypochromic peripheral erythrocytes, systemic iron
overload secondary to chronic ineffective erythropoiesis, and the
presence of bone marrow ringed sideroblasts. Sideroblasts are
characterized by iron-loaded mitochondria clustered around the
nucleus. SIDBA4 has been reported to be inherited as an autosomal
recessive disease, with a pseudodominant pattern of inheritance in
some families. {ECO:0000269|PubMed:26491070}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Even-plus syndrome (EVPLS) [MIM:616854]: An autosomal
recessive syndrome characterized by epiphyseal and vertebral
dysplasia, prenatal-onset short stature, a distinct craniofacial
phenotype with microtia, a flat facial profile with flat nose and
triangular nares, cardiac malformations, and additional findings
such as anal atresia, hypodontia, aplasia cutis, and others.
{ECO:0000269|PubMed:26598328}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/hspa9b/";
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EMBL; L11066; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; L15189; AAA67526.1; -; mRNA.
EMBL; AK315177; BAG37618.1; -; mRNA.
EMBL; AK222758; BAD96478.1; -; mRNA.
EMBL; DQ531046; ABF50973.1; -; Genomic_DNA.
EMBL; CH471062; EAW62129.1; -; Genomic_DNA.
EMBL; BC000478; AAH00478.1; -; mRNA.
EMBL; BC024034; AAH24034.1; -; mRNA.
CCDS; CCDS4208.1; -.
PIR; B48127; B48127.
RefSeq; NP_004125.3; NM_004134.6.
UniGene; Hs.184233; -.
PDB; 3N8E; X-ray; 2.80 A; A/B=439-597.
PDB; 4KBO; X-ray; 2.80 A; A=52-431.
PDBsum; 3N8E; -.
PDBsum; 4KBO; -.
ProteinModelPortal; P38646; -.
SMR; P38646; -.
BioGrid; 109545; 231.
CORUM; P38646; -.
DIP; DIP-32936N; -.
IntAct; P38646; 66.
MINT; P38646; -.
STRING; 9606.ENSP00000297185; -.
iPTMnet; P38646; -.
PhosphoSitePlus; P38646; -.
SwissPalm; P38646; -.
BioMuta; HSPA9; -.
DMDM; 21264428; -.
DOSAC-COBS-2DPAGE; P38646; -.
OGP; P38646; -.
REPRODUCTION-2DPAGE; IPI00007765; -.
SWISS-2DPAGE; P38646; -.
UCD-2DPAGE; P38646; -.
EPD; P38646; -.
MaxQB; P38646; -.
PaxDb; P38646; -.
PeptideAtlas; P38646; -.
PRIDE; P38646; -.
ProteomicsDB; 55304; -.
TopDownProteomics; P38646; -.
DNASU; 3313; -.
Ensembl; ENST00000297185; ENSP00000297185; ENSG00000113013.
GeneID; 3313; -.
KEGG; hsa:3313; -.
UCSC; uc003ldf.4; human.
CTD; 3313; -.
DisGeNET; 3313; -.
EuPathDB; HostDB:ENSG00000113013.12; -.
GeneCards; HSPA9; -.
HGNC; HGNC:5244; HSPA9.
HPA; CAB005219; -.
HPA; HPA000898; -.
MalaCards; HSPA9; -.
MIM; 182170; phenotype.
MIM; 600548; gene.
MIM; 616854; phenotype.
neXtProt; NX_P38646; -.
OpenTargets; ENSG00000113013; -.
PharmGKB; PA162391712; -.
eggNOG; KOG0102; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00920000149123; -.
HOVERGEN; HBG051845; -.
InParanoid; P38646; -.
KO; K04043; -.
OMA; ISIKRHM; -.
OrthoDB; EOG091G0386; -.
PhylomeDB; P38646; -.
TreeFam; TF105046; -.
Reactome; R-HSA-1268020; Mitochondrial protein import.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-8949613; Cristae formation.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
SIGNOR; P38646; -.
ChiTaRS; HSPA9; human.
EvolutionaryTrace; P38646; -.
GeneWiki; HSPA9; -.
GenomeRNAi; 3313; -.
PRO; PR:P38646; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113013; -.
ExpressionAtlas; P38646; baseline and differential.
Genevisible; P38646; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0051082; F:unfolded protein binding; TAS:UniProtKB.
GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IMP:UniProtKB.
GO; GO:1902037; P:negative regulation of hematopoietic stem cell differentiation; IEA:Ensembl.
GO; GO:0006611; P:protein export from nucleus; IEA:Ensembl.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0045646; P:regulation of erythrocyte differentiation; IMP:UniProtKB.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
HAMAP; MF_00332; DnaK; 1.
InterPro; IPR012725; Chaperone_DnaK.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
PANTHER; PTHR19375; PTHR19375; 1.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
TIGRFAMs; TIGR02350; prok_dnaK; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Chaperone; Complete proteome;
Direct protein sequencing; Disease mutation; Dwarfism; Methylation;
Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transit peptide.
TRANSIT 1 46 Mitochondrion.
{ECO:0000269|PubMed:1286669,
ECO:0000269|PubMed:7498169,
ECO:0000269|PubMed:9150948}.
CHAIN 47 679 Stress-70 protein, mitochondrial.
/FTId=PRO_0000013563.
REGION 1 432 Interaction with NFS1.
{ECO:0000269|PubMed:26702583}.
REGION 432 679 Interaction with FXN and ISCU.
{ECO:0000269|PubMed:26702583}.
MOD_RES 76 76 N6-acetyllysine.
{ECO:0000250|UniProtKB:P38647}.
MOD_RES 87 87 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 135 135 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 135 135 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P38647}.
MOD_RES 138 138 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 138 138 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P38647}.
MOD_RES 143 143 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 206 206 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P38647}.
MOD_RES 206 206 N6-malonyllysine; alternate.
{ECO:0000269|PubMed:21908771}.
MOD_RES 206 206 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P38647}.
MOD_RES 234 234 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 288 288 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 300 300 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 300 300 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P38647}.
MOD_RES 368 368 N6-succinyllysine.
{ECO:0000250|UniProtKB:P38647}.
MOD_RES 394 394 N6-succinyllysine.
{ECO:0000250|UniProtKB:P38647}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 513 513 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 567 567 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 567 567 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P38647}.
MOD_RES 600 600 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P38647}.
MOD_RES 600 600 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P38647}.
MOD_RES 610 610 N6-succinyllysine.
{ECO:0000250|UniProtKB:P38647}.
MOD_RES 612 612 N6-acetyllysine.
{ECO:0000250|UniProtKB:P38647}.
MOD_RES 646 646 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 646 646 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P38647}.
VARIANT 74 74 Q -> R (in dbSNP:rs17856004).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_046482.
VARIANT 126 126 R -> W (in EVPLS; dbSNP:rs751478142).
{ECO:0000269|PubMed:26598328}.
/FTId=VAR_076662.
VARIANT 127 127 R -> G (in dbSNP:rs35091799).
/FTId=VAR_049622.
VARIANT 128 128 Y -> C (in EVPLS; dbSNP:rs765368797).
{ECO:0000269|PubMed:26598328}.
/FTId=VAR_076663.
VARIANT 184 184 H -> Y. {ECO:0000269|Ref.5}.
/FTId=VAR_046483.
VARIANT 200 200 S -> L (in dbSNP:rs199715716).
{ECO:0000269|PubMed:26491070}.
/FTId=VAR_076664.
VARIANT 212 212 S -> P (in SIDBA4; unknown pathological
significance; dbSNP:rs768283289).
{ECO:0000269|PubMed:26491070}.
/FTId=VAR_076665.
VARIANT 225 225 A -> G (in dbSNP:rs34558740).
/FTId=VAR_049623.
VARIANT 388 388 G -> S (in SIDBA4; unknown pathological
significance).
{ECO:0000269|PubMed:26491070}.
/FTId=VAR_076666.
VARIANT 415 415 E -> K (in SIDBA4; unknown pathological
significance).
{ECO:0000269|PubMed:26491070}.
/FTId=VAR_076667.
VARIANT 458 459 Missing (in SIDBA4).
{ECO:0000269|PubMed:26491070}.
/FTId=VAR_076668.
VARIANT 539 539 T -> K. {ECO:0000269|PubMed:26491070}.
/FTId=VAR_076669.
VARIANT 573 573 R -> W (in dbSNP:rs147723579).
{ECO:0000269|PubMed:26491070}.
/FTId=VAR_076670.
VARIANT 577 577 E -> K (in dbSNP:rs905439101).
{ECO:0000269|PubMed:26491070}.
/FTId=VAR_076671.
MUTAGEN 489 489 G->E: Significant loss of interaction
with FXN and ISCU. Significant increase
in interaction with NFS1.
{ECO:0000269|PubMed:26702583}.
CONFLICT 48 48 S -> P (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 66 66 C -> S (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 176 176 E -> V (in Ref. 3; BAG37618).
{ECO:0000305}.
CONFLICT 184 184 H -> R (in Ref. 7; AAH00478/AAH24034).
{ECO:0000305}.
CONFLICT 249 249 T -> A (in Ref. 4; BAD96478).
{ECO:0000305}.
CONFLICT 385 385 L -> P (in Ref. 4; BAD96478).
{ECO:0000305}.
CONFLICT 540 540 G -> R (in Ref. 2; AAA67526).
{ECO:0000305}.
STRAND 56 59 {ECO:0000244|PDB:4KBO}.
STRAND 62 71 {ECO:0000244|PDB:4KBO}.
STRAND 74 77 {ECO:0000244|PDB:4KBO}.
STRAND 91 93 {ECO:0000244|PDB:4KBO}.
STRAND 99 102 {ECO:0000244|PDB:4KBO}.
HELIX 103 106 {ECO:0000244|PDB:4KBO}.
TURN 107 111 {ECO:0000244|PDB:4KBO}.
HELIX 113 115 {ECO:0000244|PDB:4KBO}.
HELIX 120 122 {ECO:0000244|PDB:4KBO}.
TURN 123 125 {ECO:0000244|PDB:4KBO}.
HELIX 131 139 {ECO:0000244|PDB:4KBO}.
STRAND 141 146 {ECO:0000244|PDB:4KBO}.
STRAND 148 156 {ECO:0000244|PDB:4KBO}.
STRAND 159 161 {ECO:0000244|PDB:4KBO}.
HELIX 163 182 {ECO:0000244|PDB:4KBO}.
STRAND 188 193 {ECO:0000244|PDB:4KBO}.
HELIX 199 211 {ECO:0000244|PDB:4KBO}.
STRAND 215 221 {ECO:0000244|PDB:4KBO}.
HELIX 222 229 {ECO:0000244|PDB:4KBO}.
HELIX 232 234 {ECO:0000244|PDB:4KBO}.
STRAND 236 245 {ECO:0000244|PDB:4KBO}.
STRAND 250 258 {ECO:0000244|PDB:4KBO}.
STRAND 261 270 {ECO:0000244|PDB:4KBO}.
HELIX 275 294 {ECO:0000244|PDB:4KBO}.
HELIX 302 318 {ECO:0000244|PDB:4KBO}.
TURN 319 321 {ECO:0000244|PDB:4KBO}.
STRAND 323 333 {ECO:0000244|PDB:4KBO}.
STRAND 340 347 {ECO:0000244|PDB:4KBO}.
HELIX 348 354 {ECO:0000244|PDB:4KBO}.
HELIX 356 360 {ECO:0000244|PDB:4KBO}.
HELIX 363 372 {ECO:0000244|PDB:4KBO}.
TURN 377 379 {ECO:0000244|PDB:4KBO}.
STRAND 382 387 {ECO:0000244|PDB:4KBO}.
HELIX 388 391 {ECO:0000244|PDB:4KBO}.
HELIX 393 403 {ECO:0000244|PDB:4KBO}.
TURN 413 415 {ECO:0000244|PDB:4KBO}.
HELIX 416 428 {ECO:0000244|PDB:4KBO}.
STRAND 445 448 {ECO:0000244|PDB:3N8E}.
STRAND 452 458 {ECO:0000244|PDB:3N8E}.
STRAND 463 472 {ECO:0000244|PDB:3N8E}.
STRAND 482 490 {ECO:0000244|PDB:3N8E}.
HELIX 494 496 {ECO:0000244|PDB:3N8E}.
STRAND 497 505 {ECO:0000244|PDB:3N8E}.
STRAND 518 524 {ECO:0000244|PDB:3N8E}.
STRAND 530 536 {ECO:0000244|PDB:3N8E}.
TURN 537 539 {ECO:0000244|PDB:3N8E}.
STRAND 542 548 {ECO:0000244|PDB:3N8E}.
HELIX 555 567 {ECO:0000244|PDB:3N8E}.
HELIX 569 590 {ECO:0000244|PDB:3N8E}.
SEQUENCE 679 AA; 73680 MW; 90969A8D06757753 CRC64;
MISASRAAAA RLVGAAASRG PTAARHQDSW NGLSHEAFRL VSRRDYASEA IKGAVVGIDL
GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL VGMPAKRQAV TNPNNTFYAT
KRLIGRRYDD PEVQKDIKNV PFKIVRASNG DAWVEAHGKL YSPSQIGAFV LMKMKETAEN
YLGHTAKNAV ITVPAYFNDS QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKVI
AVYDLGGGTF DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK
DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDSSGPK HLNMKLTRAQ FEGIVTDLIR
RTIAPCQKAM QDAEVSKSDI GEVILVGGMT RMPKVQQTVQ DLFGRAPSKA VNPDEAVAIG
AAIQGGVLAG DVTDVLLLDV TPLSLGIETL GGVFTKLINR NTTIPTKKSQ VFSTAADGQT
QVEIKVCQGE REMAGDNKLL GQFTLIGIPP APRGVPQIEV TFDIDANGIV HVSAKDKGTG
REQQIVIQSS GGLSKDDIEN MVKNAEKYAE EDRRKKERVE AVNMAEGIIH DTETKMEEFK
DQLPADECNK LKEEISKMRE LLARKDSETG ENIRQAASSL QQASLKLFEM AYKKMASERE
GSGSSGTGEQ KEDQKEEKQ


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