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Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (Peptide-binding protein 74) (PBP74) (p66 MOT)

 GRP75_MOUSE             Reviewed;         679 AA.
P38647; Q3TW93; Q3UVN1; Q3V015; Q7TSZ0; Q9CQ05;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 3.
02-JUN-2021, entry version 196.
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;
AltName: Full=Peptide-binding protein 74;
Short=PBP74;
AltName: Full=p66 MOT;
Flags: Precursor;
Name=Hspa9; Synonyms=Grp75, Hsp74, Hspa9a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=CD-1-ICR; TISSUE=Embryonic fibroblast;
PubMed=8454632;
Wadhwa R., Kaul S.C., Ikawa Y., Sugimoto Y.;
"Identification of a novel member of mouse hsp70 family. Its association
with cellular mortal phenotype.";
J. Biol. Chem. 268:6615-6621(1993).
[2]
SEQUENCE REVISION TO 123.
Wadhwa R.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE.
STRAIN=CD-1-ICR; TISSUE=Embryonic fibroblast;
PubMed=7693662;
Wadhwa R., Kaul S.C., Sugimoto Y., Mitsui Y.;
"Induction of cellular senescence by transfection of cytosolic mortalin
cDNA in NIH 3T3 cells.";
J. Biol. Chem. 268:22239-22242(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=8262211; DOI=10.1016/0014-5793(93)81602-v;
Michikawa Y., Baba T., Arai Y., Sakakura T., Kusakabe M.;
"Structure and organization of the gene encoding a mouse mitochondrial
stress-70 protein.";
FEBS Lett. 336:27-33(1993).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/HeN; TISSUE=Kidney;
PubMed=7692847; DOI=10.1006/bbrc.1993.2238;
Michikawa Y., Baba T., Arai Y., Sakakura T., Tanaka M., Kusakabe M.;
"Antigenic protein specific for C3H strain mouse is a mitochondrial stress-
70 protein.";
Biochem. Biophys. Res. Commun. 196:223-232(1993).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and DBA/2J; TISSUE=Embryo, Kidney, and Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[11]
PROTEIN SEQUENCE OF 47-70.
TISSUE=Fibroblast;
PubMed=7523108; DOI=10.1002/elps.11501501101;
Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
"Separation and sequencing of familiar and novel murine proteins using
preparative two-dimensional gel electrophoresis.";
Electrophoresis 15:735-745(1994).
[12]
PROTEIN SEQUENCE OF 188-202; 266-284; 349-360; 395-405 AND 499-513, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[13]
SUBCELLULAR LOCATION.
PubMed=7865888; DOI=10.1091/mbc.5.11.1265;
Dahlseid J.N., Lill R., Green J.M., Xu X., Qiu Y., Pierce S.K.;
"PBP74, a new member of the mammalian 70-kDa heat shock protein family, is
a mitochondrial protein.";
Mol. Biol. Cell 5:1265-1275(1994).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[15]
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).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-300; LYS-360 AND
LYS-567, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-138; LYS-206;
LYS-300; LYS-360; LYS-368; LYS-394; LYS-567; LYS-600; LYS-610 AND LYS-646,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast, and Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76; LYS-135; LYS-138; LYS-206;
LYS-234; LYS-288; LYS-300; LYS-360; LYS-567; LYS-600; LYS-612 AND LYS-646,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in mitochondria
identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
[18]
FUNCTION.
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 (PubMed:26702583).
Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1,
NFS1 and ISCU (By similarity). Regulates erythropoiesis via
stabilization of ISC assembly (PubMed:21123823). May play a role in the
control of cell proliferation and cellular aging (PubMed:8454632).
{ECO:0000250|UniProtKB:P38646, ECO:0000269|PubMed:21123823,
ECO:0000269|PubMed:26702583, ECO:0000269|PubMed:8454632}.
-!- SUBUNIT: Interacts strongly with the intermediate form of FXN and
weakly with its mature form. Interacts with HSCB. Associates with the
mitochondrial contact site and cristae organizing system (MICOS)
complex, composed of at least MICOS10/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. Interacts with DNLZ, the interaction is required
to prevent self-aggregation. Interacts with TESPA1. Interacts with
PDPN. Interacts with NFU1, NFS1 and ISCU.
{ECO:0000250|UniProtKB:P38646}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7865888}.
Nucleus, nucleolus {ECO:0000250|UniProtKB:P38646}.
-!- TISSUE SPECIFICITY: Found in all the cell types examined.
-!- INDUCTION: Not induced by heat shock, instead protein level is
decreased.
-!- POLYMORPHISM: Two forms of the protein have been found, MOT-1, found in
mortal cells and MOT-2, found in immortal cells. The sequence of MOT-2
is shown here.
-!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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EMBL; D11089; BAA01862.2; -; mRNA.
EMBL; L06896; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; D17666; BAA04548.1; -; Genomic_DNA.
EMBL; D17556; BAA04493.1; -; mRNA.
EMBL; AK004946; BAB23690.1; -; mRNA.
EMBL; AK002634; BAB22248.1; -; mRNA.
EMBL; AK133501; BAE21690.1; -; mRNA.
EMBL; AK137109; BAE23238.1; -; mRNA.
EMBL; AK145965; BAE26790.1; -; mRNA.
EMBL; AK159791; BAE35373.1; -; mRNA.
EMBL; AK165958; BAE38486.1; -; mRNA.
EMBL; AK167856; BAE39874.1; -; mRNA.
EMBL; AC114820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC131675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466557; EDK97122.1; -; Genomic_DNA.
EMBL; BC052727; AAH52727.1; -; mRNA.
EMBL; BC057343; AAH57343.1; -; mRNA.
CCDS; CCDS29138.1; -.
PIR; S39839; A48127.
RefSeq; NP_034611.2; NM_010481.2.
SMR; P38647; -.
BioGRID; 200457; 70.
IntAct; P38647; 31.
MINT; P38647; -.
STRING; 10090.ENSMUSP00000025217; -.
iPTMnet; P38647; -.
PhosphoSitePlus; P38647; -.
SwissPalm; P38647; -.
COMPLUYEAST-2DPAGE; P38647; -.
REPRODUCTION-2DPAGE; IPI00133903; -.
REPRODUCTION-2DPAGE; P38647; -.
SWISS-2DPAGE; P38647; -.
EPD; P38647; -.
jPOST; P38647; -.
PaxDb; P38647; -.
PeptideAtlas; P38647; -.
PRIDE; P38647; -.
ProteomicsDB; 271100; -.
ABCD; P38647; 1 sequenced antibody.
Antibodypedia; 646; 748 antibodies.
DNASU; 15526; -.
Ensembl; ENSMUST00000025217; ENSMUSP00000025217; ENSMUSG00000024359.
GeneID; 15526; -.
KEGG; mmu:15526; -.
UCSC; uc008elv.2; mouse.
CTD; 3313; -.
MGI; MGI:96245; Hspa9.
eggNOG; KOG0102; Eukaryota.
GeneTree; ENSGT00920000149123; -.
HOGENOM; CLU_005965_2_1_1; -.
InParanoid; P38647; -.
OMA; ISIKRHM; -.
OrthoDB; 288077at2759; -.
TreeFam; TF105046; -.
Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
BioGRID-ORCS; 15526; 21 hits in 43 CRISPR screens.
ChiTaRS; Hspa9; mouse.
PRO; PR:P38647; -.
Proteomes; UP000000589; Chromosome 18.
RNAct; P38647; protein.
Bgee; ENSMUSG00000024359; Expressed in metanephric ureteric bud and 306 other tissues.
Genevisible; P38647; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005759; C:mitochondrial matrix; IDA:MGI.
GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IBA:GO_Central.
GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
GO; GO:0051087; F:chaperone binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0017134; F:fibroblast growth factor binding; ISO:MGI.
GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:UniProtKB.
GO; GO:1902037; P:negative regulation of hematopoietic stem cell differentiation; IMP:UniProtKB.
GO; GO:1903707; P:negative regulation of hemopoiesis; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
GO; GO:0006611; P:protein export from nucleus; IDA:MGI.
GO; GO:0042026; P:protein refolding; IBA:GO_Central.
GO; GO:0045646; P:regulation of erythrocyte differentiation; ISS:UniProtKB.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
HAMAP; MF_00332; DnaK; 1.
InterPro; IPR043129; ATPase_NBD.
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.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF53067; SSF53067; 2.
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;
Acetylation; ATP-binding; Chaperone; Direct protein sequencing;
Methylation; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Transit peptide.
TRANSIT 1..46
/note="Mitochondrion"
/evidence="ECO:0000269|PubMed:7523108"
CHAIN 47..679
/note="Stress-70 protein, mitochondrial"
/id="PRO_0000013564"
REGION 1..432
/note="Interaction with NFS1"
/evidence="ECO:0000250|UniProtKB:P38646"
REGION 432..679
/note="Interaction with FXN and ISCU"
/evidence="ECO:0000250|UniProtKB:P38646"
REGION 656..679
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 665..679
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 76
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:23576753"
MOD_RES 87
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P38646"
MOD_RES 135
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:23576753,
ECO:0007744|PubMed:23806337"
MOD_RES 135
/note="N6-succinyllysine; alternate"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 138
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:23576753"
MOD_RES 138
/note="N6-succinyllysine; alternate"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 143
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P38646"
MOD_RES 206
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:23576753"
MOD_RES 206
/note="N6-malonyllysine; alternate"
/evidence="ECO:0000250"
MOD_RES 206
/note="N6-succinyllysine; alternate"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 234
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:23576753"
MOD_RES 288
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:23576753"
MOD_RES 300
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:23576753,
ECO:0007744|PubMed:23806337"
MOD_RES 300
/note="N6-succinyllysine; alternate"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 360
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:23576753,
ECO:0007744|PubMed:23806337"
MOD_RES 360
/note="N6-succinyllysine; alternate"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 368
/note="N6-succinyllysine"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 394
/note="N6-succinyllysine"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 408
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P38646"
MOD_RES 513
/note="Omega-N-methylarginine"
/evidence="ECO:0000250|UniProtKB:P38646"
MOD_RES 567
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:23576753,
ECO:0007744|PubMed:23806337"
MOD_RES 567
/note="N6-succinyllysine; alternate"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 600
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:23576753"
MOD_RES 600
/note="N6-succinyllysine; alternate"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 610
/note="N6-succinyllysine"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 612
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:23576753"
MOD_RES 646
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:23576753"
MOD_RES 646
/note="N6-succinyllysine; alternate"
/evidence="ECO:0007744|PubMed:23806337"
VARIANT 618
/note="M -> V (in MOT-1)"
VARIANT 624
/note="G -> R (in MOT-1)"
CONFLICT 5
/note="S -> T (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 78
/note="L -> Q (in Ref. 7; BAE21690)"
/evidence="ECO:0000305"
CONFLICT 106
/note="K -> R (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 150
/note="G -> S (in Ref. 7; BAE35373)"
/evidence="ECO:0000305"
CONFLICT 522
/note="F -> S (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
SEQUENCE 679 AA; 73461 MW; DF1C997775627928 CRC64;
MISASRAAAA RLVGTAASRS PAAARPQDGW NGLSHEAFRF VSRRDYASEA IKGAVVGIDL
GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL VGMPAKRQAV TNPNNTFYAT
KRLIGRRYDD PEVQKDTKNV PFKIVRASNG DAWVEAHGKL YSPSQIGAFV LMKMKETAEN
YLGHTAKNAV ITVPAYFNDS QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKVI
AVYDLGGGTF DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK
DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDASGPK HLNMKLTRAQ FEGIVTDLIK
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 LKEEISKMRA LLAGKDSETG ENIRQAASSL QQASLKLFEM AYKKMASERE
GSGSSGTGEQ KEDQKEEKQ


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[Hspa9 Grp75 Hsp74 Hspa9a] Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (Peptide-binding protein 74) (PBP74) (p66 MOT)
[HSPA9 GRP75 HSPA9B mt-HSP70] Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (MOT) (Peptide-binding protein 74) (PBP74)
[Hspa9 Grp75 Hspa9a] Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (Peptide-binding protein 74) (PBP74) (mtHSP70)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (Steroidogenesis-activator polypeptide)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (Fragment)
[HSPA5 GRP78 I79_019946] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPA9] Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Hsp90b1 Grp94 Tra-1 Tra1] Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Endoplasmic reticulum resident protein 99) (ERp99) (Heat shock protein 90 kDa beta member 1) (Polymorphic tumor rejection antigen 1) (Tumor rejection antigen gp96)
[HSPB1 HSP27 HSP28] Heat shock protein beta-1 (HspB1) (28 kDa heat shock protein) (Estrogen-regulated 24 kDa protein) (Heat shock 27 kDa protein) (HSP 27) (Stress-responsive protein 27) (SRP27)
[HSPA9 RCJMB04_2m8] Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9)
[HSPA1A HSP72 HSPA1 HSX70] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1)
[HSPA8 HSC70 HSP73 HSPA10] Heat shock cognate 71 kDa protein (EC 3.6.4.10) (Heat shock 70 kDa protein 8) (Lipopolysaccharide-associated protein 1) (LAP-1) (LPS-associated protein 1)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSP90B1 GRP94 TRA1] Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1) (Tumor rejection antigen 1) (gp96 homolog)
[SSC1 ENS1] Import motor subunit, mitochondrial (EC 3.6.4.10) (Endonuclease SceI 75 kDa subunit) (Endo.SceI 75 kDa subunit) (Heat shock protein SSC1, mitochondrial) (mtHSP70)
[HSPA1B HSP72] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2)
[HSP70-4 HSC70-4 HSP70 MED37_2 MED37C At3g12580 T16H11.7 T2E22.11] Heat shock 70 kDa protein 4 (Heat shock cognate 70 kDa protein 4) (Heat shock cognate protein 70-4) (AtHsc70-4) (Heat shock protein 70-4) (AtHsp70-4)
[HSP60 MIF4 YLR259C L8479.10] Heat shock protein 60, mitochondrial (CPN60) (P66) (Stimulator factor I 66 kDa component)
[HYOU1 GRP170 ORP150] Hypoxia up-regulated protein 1 (150 kDa oxygen-regulated protein) (ORP-150) (170 kDa glucose-regulated protein) (GRP-170)
[HSPA8 HSC70] Heat shock cognate 71 kDa protein (EC 3.6.4.10) (Heat shock 70 kDa protein 8)
[HSP90B1 GRP94 TRA1] Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1)
[Hspa8 Hsc70 Hsc73] Heat shock cognate 71 kDa protein (EC 3.6.4.10) (Heat shock 70 kDa protein 8)
[Hspa8 Hsc70 Hsc73] Heat shock cognate 71 kDa protein (EC 3.6.4.10) (Heat shock 70 kDa protein 8)
[Hspa1b Hsp70-2 Hspa2] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1)

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