GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

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.
02-JUN-2021, entry version 225.
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]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
"Proteomic characterization of the human centrosome by protein correlation
profiling.";
Nature 426:570-574(2003).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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 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 (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:
P38646; P00533: EGFR; NbExp=5; IntAct=EBI-354932, EBI-297353;
P38646; Q9HAV7: GRPEL1; NbExp=2; IntAct=EBI-354932, EBI-1043499;
P38646; Q8IWL3: HSCB; NbExp=15; IntAct=EBI-354932, EBI-1805738;
P38646; Q8WX92: NELFB; NbExp=2; IntAct=EBI-354932, EBI-347721;
P38646; P04637: TP53; NbExp=6; IntAct=EBI-354932, EBI-366083;
P38646; O15350: TP73; NbExp=11; IntAct=EBI-354932, EBI-389606;
P38646; P13693: TPT1; NbExp=4; IntAct=EBI-354932, EBI-1783169;
P38646; 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 variants 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 variants 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/";
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
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.
PDB; 3N8E; X-ray; 2.80 A; A/B=439-597.
PDB; 4KBO; X-ray; 2.80 A; A=52-431.
PDB; 6NHK; X-ray; 2.78 A; A/B=54-429.
PDB; 6P2U; X-ray; 2.00 A; A=52-431.
PDB; 6PMT; X-ray; 2.30 A; A=52-431.
PDBsum; 3N8E; -.
PDBsum; 4KBO; -.
PDBsum; 6NHK; -.
PDBsum; 6P2U; -.
PDBsum; 6PMT; -.
SMR; P38646; -.
BioGRID; 109545; 402.
ComplexPortal; CPX-6129; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17A variant.
ComplexPortal; CPX-6130; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17B variant.
CORUM; P38646; -.
DIP; DIP-32936N; -.
IntAct; P38646; 180.
MINT; P38646; -.
STRING; 9606.ENSP00000297185; -.
ChEMBL; CHEMBL4295757; -.
iPTMnet; P38646; -.
MetOSite; 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; -.
jPOST; P38646; -.
MassIVE; P38646; -.
MaxQB; P38646; -.
PaxDb; P38646; -.
PeptideAtlas; P38646; -.
PRIDE; P38646; -.
ProteomicsDB; 55304; -.
TopDownProteomics; P38646; -.
ABCD; P38646; 8 sequenced antibodies.
Antibodypedia; 646; 748 antibodies.
DNASU; 3313; -.
Ensembl; ENST00000297185; ENSP00000297185; ENSG00000113013.
GeneID; 3313; -.
KEGG; hsa:3313; -.
UCSC; uc003ldf.4; human.
CTD; 3313; -.
DisGeNET; 3313; -.
GeneCards; HSPA9; -.
HGNC; HGNC:5244; HSPA9.
HPA; ENSG00000113013; Low tissue specificity.
MalaCards; HSPA9; -.
MIM; 182170; phenotype.
MIM; 600548; gene.
MIM; 616854; phenotype.
neXtProt; NX_P38646; -.
OpenTargets; ENSG00000113013; -.
Orphanet; 260305; Autosomal recessive sideroblastic anemia.
Orphanet; 496751; EVEN-plus syndrome.
PharmGKB; PA162391712; -.
VEuPathDB; HostDB:ENSG00000113013.12; -.
eggNOG; KOG0102; Eukaryota.
GeneTree; ENSGT00920000149123; -.
HOGENOM; CLU_005965_2_1_1; -.
InParanoid; P38646; -.
OMA; ISIKRHM; -.
OrthoDB; 288077at2759; -.
PhylomeDB; P38646; -.
TreeFam; TF105046; -.
BRENDA; 3.6.4.10; 2681.
PathwayCommons; P38646; -.
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; -.
BioGRID-ORCS; 3313; 739 hits in 974 CRISPR screens.
ChiTaRS; HSPA9; human.
EvolutionaryTrace; P38646; -.
GeneWiki; HSPA9; -.
GenomeRNAi; 3313; -.
Pharos; P38646; Tbio.
PRO; PR:P38646; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; P38646; protein.
Bgee; ENSG00000113013; Expressed in adrenal tissue and 245 other tissues.
ExpressionAtlas; P38646; baseline and differential.
Genevisible; P38646; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0140275; C:MIB complex; 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:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0001401; C:SAM complex; HDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IBA:GO_Central.
GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
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; 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; IMP:UniProtKB.
GO; GO:0007007; P:inner mitochondrial membrane organization; IC: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:1903707; P:negative regulation of hemopoiesis; IEA:Ensembl.
GO; GO:0006611; P:protein export from nucleus; IEA:Ensembl.
GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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; 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;
3D-structure; Acetylation; ATP-binding; Chaperone;
Direct protein sequencing; Disease variant; Dwarfism; Methylation;
Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Transit peptide.
TRANSIT 1..46
/note="Mitochondrion"
/evidence="ECO:0000269|PubMed:1286669,
ECO:0000269|PubMed:7498169, ECO:0000269|PubMed:9150948"
CHAIN 47..679
/note="Stress-70 protein, mitochondrial"
/id="PRO_0000013563"
REGION 1..432
/note="Interaction with NFS1"
/evidence="ECO:0000269|PubMed:26702583"
REGION 432..679
/note="Interaction with FXN and ISCU"
/evidence="ECO:0000269|PubMed:26702583"
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:0000250|UniProtKB:P38647"
MOD_RES 87
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 135
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 135
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P38647"
MOD_RES 138
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 138
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P38647"
MOD_RES 143
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 206
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P38647"
MOD_RES 206
/note="N6-malonyllysine; alternate"
/evidence="ECO:0000269|PubMed:21908771"
MOD_RES 206
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P38647"
MOD_RES 234
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 288
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 300
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 300
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P38647"
MOD_RES 368
/note="N6-succinyllysine"
/evidence="ECO:0000250|UniProtKB:P38647"
MOD_RES 394
/note="N6-succinyllysine"
/evidence="ECO:0000250|UniProtKB:P38647"
MOD_RES 408
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 513
/note="Omega-N-methylarginine"
/evidence="ECO:0007744|PubMed:24129315"
MOD_RES 567
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 567
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P38647"
MOD_RES 600
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P38647"
MOD_RES 600
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P38647"
MOD_RES 610
/note="N6-succinyllysine"
/evidence="ECO:0000250|UniProtKB:P38647"
MOD_RES 612
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P38647"
MOD_RES 646
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 646
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P38647"
VARIANT 74
/note="Q -> R (in dbSNP:rs17856004)"
/evidence="ECO:0000269|PubMed:15489334"
/id="VAR_046482"
VARIANT 126
/note="R -> W (in EVPLS; dbSNP:rs751478142)"
/evidence="ECO:0000269|PubMed:26598328"
/id="VAR_076662"
VARIANT 127
/note="R -> G (in dbSNP:rs35091799)"
/id="VAR_049622"
VARIANT 128
/note="Y -> C (in EVPLS; dbSNP:rs765368797)"
/evidence="ECO:0000269|PubMed:26598328"
/id="VAR_076663"
VARIANT 184
/note="H -> Y"
/evidence="ECO:0000269|Ref.5"
/id="VAR_046483"
VARIANT 200
/note="S -> L (in dbSNP:rs199715716)"
/evidence="ECO:0000269|PubMed:26491070"
/id="VAR_076664"
VARIANT 212
/note="S -> P (in SIDBA4; unknown pathological
significance; dbSNP:rs768283289)"
/evidence="ECO:0000269|PubMed:26491070"
/id="VAR_076665"
VARIANT 225
/note="A -> G (in dbSNP:rs34558740)"
/id="VAR_049623"
VARIANT 388
/note="G -> S (in SIDBA4; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:26491070"
/id="VAR_076666"
VARIANT 415
/note="E -> K (in SIDBA4; unknown pathological
significance)"
/evidence="ECO:0000269|PubMed:26491070"
/id="VAR_076667"
VARIANT 458..459
/note="Missing (in SIDBA4)"
/evidence="ECO:0000269|PubMed:26491070"
/id="VAR_076668"
VARIANT 539
/note="T -> K"
/evidence="ECO:0000269|PubMed:26491070"
/id="VAR_076669"
VARIANT 573
/note="R -> W (in dbSNP:rs147723579)"
/evidence="ECO:0000269|PubMed:26491070"
/id="VAR_076670"
VARIANT 577
/note="E -> K (in dbSNP:rs905439101)"
/evidence="ECO:0000269|PubMed:26491070"
/id="VAR_076671"
MUTAGEN 489
/note="G->E: Significant loss of interaction with FXN and
ISCU. Significant increase in interaction with NFS1."
/evidence="ECO:0000269|PubMed:26702583"
CONFLICT 48
/note="S -> P (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 66
/note="C -> S (in Ref. 9; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 176
/note="E -> V (in Ref. 3; BAG37618)"
/evidence="ECO:0000305"
CONFLICT 184
/note="H -> R (in Ref. 7; AAH00478/AAH24034)"
/evidence="ECO:0000305"
CONFLICT 249
/note="T -> A (in Ref. 4; BAD96478)"
/evidence="ECO:0000305"
CONFLICT 385
/note="L -> P (in Ref. 4; BAD96478)"
/evidence="ECO:0000305"
CONFLICT 540
/note="G -> R (in Ref. 2; AAA67526)"
/evidence="ECO:0000305"
STRAND 55..59
/evidence="ECO:0007829|PDB:6P2U"
STRAND 62..71
/evidence="ECO:0007829|PDB:6P2U"
STRAND 74..77
/evidence="ECO:0007829|PDB:6P2U"
STRAND 85..88
/evidence="ECO:0007829|PDB:6P2U"
STRAND 90..93
/evidence="ECO:0007829|PDB:6P2U"
STRAND 95..97
/evidence="ECO:0007829|PDB:6NHK"
STRAND 99..102
/evidence="ECO:0007829|PDB:6P2U"
HELIX 103..106
/evidence="ECO:0007829|PDB:6P2U"
TURN 107..111
/evidence="ECO:0007829|PDB:6P2U"
HELIX 113..115
/evidence="ECO:0007829|PDB:6P2U"
STRAND 116..118
/evidence="ECO:0007829|PDB:6P2U"
HELIX 120..122
/evidence="ECO:0007829|PDB:6P2U"
TURN 123..125
/evidence="ECO:0007829|PDB:6P2U"
HELIX 131..139
/evidence="ECO:0007829|PDB:6P2U"
STRAND 142..146
/evidence="ECO:0007829|PDB:6P2U"
STRAND 150..156
/evidence="ECO:0007829|PDB:6P2U"
STRAND 159..161
/evidence="ECO:0007829|PDB:6P2U"
HELIX 163..182
/evidence="ECO:0007829|PDB:6P2U"
STRAND 188..193
/evidence="ECO:0007829|PDB:6P2U"
HELIX 199..211
/evidence="ECO:0007829|PDB:6P2U"
STRAND 215..221
/evidence="ECO:0007829|PDB:6P2U"
HELIX 222..229
/evidence="ECO:0007829|PDB:6P2U"
HELIX 232..234
/evidence="ECO:0007829|PDB:6P2U"
STRAND 236..245
/evidence="ECO:0007829|PDB:6P2U"
STRAND 250..258
/evidence="ECO:0007829|PDB:6P2U"
STRAND 261..270
/evidence="ECO:0007829|PDB:6P2U"
HELIX 275..293
/evidence="ECO:0007829|PDB:6P2U"
HELIX 298..300
/evidence="ECO:0007829|PDB:6PMT"
HELIX 302..318
/evidence="ECO:0007829|PDB:6P2U"
TURN 319..321
/evidence="ECO:0007829|PDB:6P2U"
STRAND 323..334
/evidence="ECO:0007829|PDB:6P2U"
STRAND 339..347
/evidence="ECO:0007829|PDB:6P2U"
HELIX 348..354
/evidence="ECO:0007829|PDB:6P2U"
HELIX 356..360
/evidence="ECO:0007829|PDB:6P2U"
HELIX 363..372
/evidence="ECO:0007829|PDB:6P2U"
TURN 377..379
/evidence="ECO:0007829|PDB:6P2U"
STRAND 382..387
/evidence="ECO:0007829|PDB:6P2U"
HELIX 388..391
/evidence="ECO:0007829|PDB:6P2U"
HELIX 393..403
/evidence="ECO:0007829|PDB:6P2U"
TURN 413..415
/evidence="ECO:0007829|PDB:6P2U"
HELIX 416..428
/evidence="ECO:0007829|PDB:6P2U"
STRAND 445..448
/evidence="ECO:0007829|PDB:3N8E"
STRAND 452..458
/evidence="ECO:0007829|PDB:3N8E"
STRAND 463..472
/evidence="ECO:0007829|PDB:3N8E"
STRAND 482..490
/evidence="ECO:0007829|PDB:3N8E"
HELIX 494..496
/evidence="ECO:0007829|PDB:3N8E"
STRAND 497..505
/evidence="ECO:0007829|PDB:3N8E"
STRAND 518..524
/evidence="ECO:0007829|PDB:3N8E"
STRAND 530..536
/evidence="ECO:0007829|PDB:3N8E"
TURN 537..539
/evidence="ECO:0007829|PDB:3N8E"
STRAND 542..548
/evidence="ECO:0007829|PDB:3N8E"
HELIX 555..567
/evidence="ECO:0007829|PDB:3N8E"
HELIX 569..590
/evidence="ECO:0007829|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


Related products :

Catalog number Product name Quantity
20-272-190886 Grp75 - Mouse monoclonal [30A5] to Grp75; 75 kDa glucose-regulated protein; GRP 75; Heat shock 70 kDa protein 9; Peptide-binding protein 74; PBP74; Mortalin; MOT Monoclonal 0.025 ml
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 1 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.01 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
18-003-43409 Heat shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
18-003-42935 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
E0693h ELISA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 96T
U0693h CLIA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 2 96T
10-782-55038 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.2 mg
10-782-55038 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
E0693h ELISA kit 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive pro 96T
18-785-210206 HSP27 (Phospho-Ser78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210205 HSP27 (Phospho-Ser15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210206 HSP27 (Phospho-Ser78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210205 HSP27 (Phospho-Ser15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210207 HSP27 (Phospho-Ser82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210207 HSP27 (Phospho-Ser82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
10-002-38024 Hsp27 human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 1 mg
18-785-210210 HSP27 (Ab-82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210210 HSP27 (Ab-82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210209 HSP27 (Ab-78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
10-002-38024 Hsp27 human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.1 mg
18-785-210209 HSP27 (Ab-78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210208 HSP27 (Ab-15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210208 HSP27 (Ab-15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
Pathways :
WP1502: Mitochondrial biogenesis
WP2199: Seed Development
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP2292: Chemokine signaling pathway
WP731: Sterol regulatory element binding protein related
WP525: Mitochondrial Unfolded-Protein Response
WP1689: Porphyrin and chlorophyll metabolism
WP73: G Protein Signaling Pathways
WP1625: Base excision repair
WP1693: Purine metabolism
WP2324: AGE/RAGE pathway
WP1654: gamma-Hexachlorocyclohexane degradation
WP1661: Glyoxylate and dicarboxylate metabolism
WP2032: TSH signaling pathway
WP1165: G Protein Signaling Pathways
WP1672: Mismatch repair
WP211: BMP signaling pathway
WP931: G Protein Signaling Pathways
WP1676: Non-homologous end-joining
WP2203: TSLP Signaling Pathway
WP1566: Citrate cycle (TCA cycle)
WP1624: Bacterial secretion system
WP2272: Pathogenic Escherichia coli infection
WP1692: Protein export

Related Genes :
[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)
[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)
[Hspa1a Hsp70-1 Hspa1] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2)

Bibliography :