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78 kDa glucose-regulated protein (GRP-78) (Endoplasmic reticulum lumenal Ca(2 )-binding protein grp78) (Heat shock 70 kDa protein 5) (Immunoglobulin heavy chain-binding protein) (BiP)

 GRP78_HUMAN             Reviewed;         654 AA.
P11021; B0QZ61; Q2EF78; Q9NPF1; Q9UK02;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
11-JUL-2001, sequence version 2.
27-SEP-2017, entry version 206.
RecName: Full=78 kDa glucose-regulated protein {ECO:0000303|PubMed:2840249};
Short=GRP-78 {ECO:0000303|PubMed:2840249};
AltName: Full=Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78 {ECO:0000303|Ref.4};
AltName: Full=Heat shock 70 kDa protein 5;
AltName: Full=Immunoglobulin heavy chain-binding protein {ECO:0000250|UniProtKB:P20029};
Short=BiP {ECO:0000250|UniProtKB:P20029};
Flags: Precursor;
Name=HSPA5 {ECO:0000312|HGNC:HGNC:5238};
Synonyms=GRP78 {ECO:0000303|PubMed:2840249};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2840249; DOI=10.1089/dna.1988.7.275;
Ting J., Lee A.S.;
"Human gene encoding the 78,000-dalton glucose-regulated protein and
its pseudogene: structure, conservation, and regulation.";
DNA 7:275-286(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Cervix carcinoma;
Chao C.C.K.;
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
Hansen J.J., Nielsen M.N., Jorgensen M.M., Gregersen N., Bolund L.;
"Grp78 is involved in the quality control of the LDL-receptor.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Bermudez-Fajardo A., Llewellyn D.H., Campbell A.K., Errington R.R.;
"Sequence differences between human grp78/BiP isolated from HeLa cells
and previously reported human sequences.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-543.
NIEHS SNPs program;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
PubMed=1480470; DOI=10.1093/nar/20.24.6481;
Chao C.C.K., Lin-Chao S.;
"A direct-repeat sequence of the human BiP gene is required for
A23187-mediated inducibility and an inducible nuclear factor
binding.";
Nucleic Acids Res. 20:6481-6485(1992).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 20-650, AND DISEASE.
TISSUE=Articular cartilage;
PubMed=11160188; DOI=10.4049/jimmunol.166.3.1492;
Corrigall V.M., Bodman-Smith M.D., Fife M.S., Canas B., Myers L.K.,
Wooley P., Soh C., Staines N.A., Pappin D.J.C., Berlo S.E.,
van Eden W., van Der Zee R., Lanchbury J.S., Panayi G.S.;
"The human endoplasmic reticulum molecular chaperone BiP is an
autoantigen for rheumatoid arthritis and prevents the induction of
experimental arthritis.";
J. Immunol. 166:1492-1498(2001).
[11]
PROTEIN SEQUENCE OF 22-38.
TISSUE=Mammary carcinoma;
PubMed=9150946; DOI=10.1002/elps.1150180342;
Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E.,
Simpson R.J., Dorow D.S.;
"Two-dimensional electrophoretic analysis of human breast carcinoma
proteins: mapping of proteins that bind to the SH3 domain of mixed
lineage kinase MLK2.";
Electrophoresis 18:588-598(1997).
[12]
PROTEIN SEQUENCE OF 19-39, AND FUNCTION.
PubMed=2294010; DOI=10.1210/endo-126-1-672;
Dana R.C., Welch W.J., Deftos L.J.;
"Heat shock proteins bind calcitonin.";
Endocrinology 126:672-674(1990).
[13]
PROTEIN SEQUENCE OF 19-40.
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).
[14]
PROTEIN SEQUENCE OF 61-74; 82-96; 102-113; 124-152; 164-181; 186-214;
307-336; 353-367; 448-464; 475-492; 563-573; 602-617 AND 622-654, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-518, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(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]
INTERACTION WITH CCDC88B, SUBCELLULAR LOCATION, AND INDUCTION BY ER
STRESS.
PubMed=21289099; DOI=10.1091/mbc.E10-08-0724;
Matsushita E., Asai N., Enomoto A., Kawamoto Y., Kato T., Mii S.,
Maeda K., Shibata R., Hattori S., Hagikura M., Takahashi K.,
Sokabe M., Murakumo Y., Murohara T., Takahashi M.;
"Protective role of Gipie, a Girdin family protein, in endoplasmic
reticulum stress responses in endothelial cells.";
Mol. Biol. Cell 22:736-747(2011).
[18]
PROTEIN SEQUENCE OF 582-596, INTERACTION WITH METTL23, METHYLATION AT
LYS-585, MUTAGENESIS OF LYS-585, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
"A newly uncovered group of distantly related lysine
methyltransferases preferentially interact with molecular chaperones
to regulate their activity.";
PLoS Genet. 9:E1003210-E1003210(2013).
[19]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[20]
INTERACTION WITH TRIM21.
PubMed=12699405; DOI=10.1046/j.1365-2249.2003.02153.x;
Purcell A.W., Todd A., Kinoshita G., Lynch T.A., Keech C.L.,
Gething M.J., Gordon T.P.;
"Association of stress proteins with autoantigens: a possible
mechanism for triggering autoimmunity?";
Clin. Exp. Immunol. 132:193-200(2003).
[21]
INTERACTION WITH DNAJC10.
PubMed=12411443; DOI=10.1074/jbc.M206995200;
Cunnea P.M., Miranda-Vizuete A., Bertoli G., Simmen T.,
Damdimopoulos A.E., Hermann S., Leinonen S., Huikko M.P.,
Gustafsson J.-A., Sitia R., Spyrou G.;
"ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ
and thioredoxin domains, is expressed in secretory cells or following
ER stress.";
J. Biol. Chem. 278:1059-1066(2003).
[22]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=12643545; DOI=10.1021/pr025562r;
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
Hearing V.J., Hunt D.F., Appella E.;
"Proteomic analysis of early melanosomes: identification of novel
melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[23]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[24]
INTERACTION WITH ERLEC1; OS9; SEL1L AND SYVN1.
PubMed=18502753; DOI=10.1074/jbc.M709336200;
Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K.;
"Human XTP3-B forms an endoplasmic reticulum quality control scaffold
with the HRD1-SEL1L ubiquitin ligase complex and BiP.";
J. Biol. Chem. 283:20914-20924(2008).
[25]
INTERACTION WITH ERLEC1; OS9; SEL1L AND SYVN1.
PubMed=18264092; DOI=10.1038/ncb1689;
Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.;
"OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L
ubiquitin ligase complex for ERAD.";
Nat. Cell Biol. 10:272-282(2008).
[26]
INTERACTION WITH PCSK4, AND SUBCELLULAR LOCATION.
PubMed=21080038; DOI=10.1007/s11010-010-0635-y;
Gyamera-Acheampong C., Sirois F., Denis N.J., Mishra P., Figeys D.,
Basak A., Mbikay M.;
"The precursor to the germ cell-specific PCSK4 proteinase is
inefficiently activated in transfected somatic cells: evidence of
interaction with the BiP chaperone.";
Mol. Cell. Biochem. 348:43-52(2011).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[28]
METHYLATION AT LYS-585, AND MUTAGENESIS OF LYS-585.
PubMed=23921388; DOI=10.1074/jbc.M113.483248;
Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S.,
Melki R., Falnes P.O.;
"Identification and characterization of a novel human
methyltransferase modulating Hsp70 function through lysine
methylation.";
J. Biol. Chem. 288:27752-27763(2013).
[29]
FUNCTION, INTERACTION WITH CEMIP, AND SUBCELLULAR LOCATION.
PubMed=23990668; DOI=10.1093/jnci/djt224;
Evensen N.A., Kuscu C., Nguyen H.L., Zarrabi K., Dufour A., Kadam P.,
Hu Y.J., Pulkoski-Gross A., Bahou W.F., Zucker S., Cao J.;
"Unraveling the role of KIAA1199, a novel endoplasmic reticulum
protein, in cancer cell migration.";
J. Natl. Cancer Inst. 105:1402-1416(2013).
[30]
FUNCTION, AND INTERACTION WITH DNAJC10.
PubMed=23769672; DOI=10.1016/j.molcel.2013.05.014;
Oka O.B., Pringle M.A., Schopp I.M., Braakman I., Bulleid N.J.;
"ERdj5 is the ER reductase that catalyzes the removal of non-native
disulfides and correct folding of the LDL receptor.";
Mol. Cell 50:793-804(2013).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-518, AND 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).
[32]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-585 AND LYS-591, 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).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-352, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[34]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-352 AND LYS-353, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-352, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[36]
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).
[37]
INTERACTION WITH CIPC.
PubMed=26657846; DOI=10.1016/j.bbrc.2015.11.117;
Matsunaga R., Nishino T., Yokoyama A., Nakashima A., Kikkawa U.,
Konishi H.;
"Versatile function of the circadian protein CIPC as a regulator of
Erk activation.";
Biochem. Biophys. Res. Commun. 469:377-383(2016).
[38]
INTERACTION WITH INPP5K.
PubMed=26940976; DOI=10.1111/gtc.12353;
Ijuin T., Hatano N., Takenawa T.;
"Glucose-regulated protein 78 (GRP78) binds directly to PIP3
phosphatase SKIP and determines its localization.";
Genes Cells 21:457-465(2016).
[39]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-352, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[40]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 26-410.
PubMed=20072699; DOI=10.1371/journal.pone.0008625;
Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T.,
Moche M., Schuler H.;
"Crystal structures of the ATPase domains of four human Hsp70
isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and
HSPA5/BiP/GRP78.";
PLoS ONE 5:E8625-E8625(2010).
[41]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 26-407 IN COMPLEXES WITH ATP
ANALOG.
PubMed=21526763; DOI=10.1021/jm101625x;
Macias A.T., Williamson D.S., Allen N., Borgognoni J., Clay A.,
Daniels Z., Dokurno P., Drysdale M.J., Francis G.L., Graham C.J.,
Howes R., Matassova N., Murray J.B., Parsons R., Shaw T.,
Surgenor A.E., Terry L., Wang Y., Wood M., Massey A.J.;
"Adenosine-derived inhibitors of 78 kDa glucose regulated protein
(Grp78) ATPase: insights into isoform selectivity.";
J. Med. Chem. 54:4034-4041(2011).
-!- FUNCTION: Plays a role in facilitating the assembly of multimeric
protein complexes inside the endoplasmic reticulum. Involved in
the correct folding of proteins and degradation of misfolded
proteins via its interaction with DNAJC10, probably to facilitate
the release of DNAJC10 from its substrate (By similarity).
{ECO:0000250|UniProtKB:P20029, ECO:0000269|PubMed:2294010,
ECO:0000269|PubMed:23769672, ECO:0000269|PubMed:23990668}.
-!- SUBUNIT: Interacts with DNAJC1 (via J domain) (By similarity).
Component of an EIF2 complex at least composed of CELF1/CUGBP1,
CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By similarity).
Part of a large chaperone multiprotein complex comprising DNAJB11,
HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1
and very small amounts of ERP29, but not, or at very low levels,
CALR nor CANX (By similarity). Interacts with TMEM132A and TRIM21
(PubMed:12699405). May form a complex with ERLEC1, OS9, SEL1L and
SYVN1 (PubMed:18264092,PubMed:18502753). Interacts with DNAJC10
(PubMed:12411443, PubMed:23769672). Interacts with MX1 (By
similarity). Interacts with METTL23 (PubMed:23349634). Interacts
with CEMIP; the interaction induces calcium leakage from the
endoplasmic reticulum and cell migration (PubMed:23990668).
Interacts with PCSK4 form; the interaction takes place in the
endoplasmic reticulum (PubMed:21080038). Interacts with CIPC
(PubMed:26657846). Interacts with CCDC88B (via C-terminus); the
interaction opposes ERN1-mediated JNK activation, protecting
against apoptosis (PubMed:21289099). Interacts with INPP5K;
necessary for INPP5K localization at the endoplasmic reticulum
(PubMed:26940976). {ECO:0000250|UniProtKB:P20029,
ECO:0000269|PubMed:12411443, ECO:0000269|PubMed:12699405,
ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18502753,
ECO:0000269|PubMed:21080038, ECO:0000269|PubMed:21289099,
ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:23769672,
ECO:0000269|PubMed:23990668, ECO:0000269|PubMed:26657846,
ECO:0000269|PubMed:26940976}.
-!- INTERACTION:
Q6T424:-; NbExp=3; IntAct=EBI-354921, EBI-7888150;
P31749:AKT1; NbExp=2; IntAct=EBI-354921, EBI-296087;
P18850:ATF6; NbExp=2; IntAct=EBI-354921, EBI-852157;
Q6E0U4:DMKN; NbExp=3; IntAct=EBI-354921, EBI-7943171;
Q9UBS4:DNAJB11; NbExp=3; IntAct=EBI-354921, EBI-713113;
Q91YW3:Dnajc3 (xeno); NbExp=2; IntAct=EBI-354921, EBI-8381770;
Q9NZJ5:EIF2AK3; NbExp=4; IntAct=EBI-354921, EBI-766076;
O75460:ERN1; NbExp=3; IntAct=EBI-354921, EBI-371750;
Q15691:MAPRE1; NbExp=3; IntAct=EBI-354921, EBI-1004115;
Q96IZ0:PAWR; NbExp=8; IntAct=EBI-354921, EBI-595869;
Q62627:Pawr (xeno); NbExp=4; IntAct=EBI-354921, EBI-1187240;
P04049:RAF1; NbExp=4; IntAct=EBI-354921, EBI-365996;
P61619:SEC61A1; NbExp=3; IntAct=EBI-354921, EBI-358919;
P08670:VIM; NbExp=3; IntAct=EBI-354921, EBI-353844;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000269|PubMed:21080038, ECO:0000269|PubMed:21289099,
ECO:0000269|PubMed:23990668}. Melanosome
{ECO:0000269|PubMed:12643545}. Cytoplasm
{ECO:0000250|UniProtKB:P20029}. Note=Identified by mass
spectrometry in melanosome fractions from stage I to stage IV.
{ECO:0000269|PubMed:12643545}.
-!- INDUCTION: By endoplasmic reticulum stress.
{ECO:0000269|PubMed:21289099}.
-!- DISEASE: Note=Autoantigen in rheumatoid arthritis.
{ECO:0000269|PubMed:11160188}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/hspa5/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HSPA5ID40876ch9q33.html";
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EMBL; M19645; AAA52614.1; -; Genomic_DNA.
EMBL; X87949; CAA61201.1; -; mRNA.
EMBL; AJ271729; CAB71335.1; -; mRNA.
EMBL; AF216292; AAF42836.1; -; mRNA.
EMBL; DQ385847; ABD04090.1; -; Genomic_DNA.
EMBL; AL354710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW87620.1; -; Genomic_DNA.
EMBL; BC020235; AAH20235.1; -; mRNA.
EMBL; X59969; CAA42595.1; -; Genomic_DNA.
EMBL; AF188611; AAF13605.1; ALT_SEQ; mRNA.
CCDS; CCDS6863.1; -.
PIR; A29821; A29821.
RefSeq; NP_005338.1; NM_005347.4.
UniGene; Hs.743241; -.
PDB; 3IUC; X-ray; 2.40 A; A/C=26-410.
PDB; 3LDL; X-ray; 2.30 A; A/B=26-407.
PDB; 3LDN; X-ray; 2.20 A; A/B=26-407.
PDB; 3LDO; X-ray; 1.95 A; A/B=26-407.
PDB; 3LDP; X-ray; 2.20 A; A/B=26-407.
PDB; 5E84; X-ray; 2.99 A; A/B/C/D/E/F=25-633.
PDB; 5E85; X-ray; 2.57 A; A=418-637.
PDB; 5E86; X-ray; 2.68 A; A=418-637.
PDB; 5EVZ; X-ray; 1.85 A; A/B=26-407.
PDB; 5EX5; X-ray; 1.90 A; A/B=26-407.
PDB; 5EXW; X-ray; 1.90 A; A/B=26-407.
PDB; 5EY4; X-ray; 1.86 A; A/B=26-407.
PDB; 5F0X; X-ray; 1.60 A; A/B=26-407.
PDB; 5F1X; X-ray; 1.90 A; A/B=26-407.
PDB; 5F2R; X-ray; 2.15 A; A/B=26-407.
PDBsum; 3IUC; -.
PDBsum; 3LDL; -.
PDBsum; 3LDN; -.
PDBsum; 3LDO; -.
PDBsum; 3LDP; -.
PDBsum; 5E84; -.
PDBsum; 5E85; -.
PDBsum; 5E86; -.
PDBsum; 5EVZ; -.
PDBsum; 5EX5; -.
PDBsum; 5EXW; -.
PDBsum; 5EY4; -.
PDBsum; 5F0X; -.
PDBsum; 5F1X; -.
PDBsum; 5F2R; -.
ProteinModelPortal; P11021; -.
SMR; P11021; -.
BioGrid; 109541; 558.
CORUM; P11021; -.
DIP; DIP-33189N; -.
ELM; P11021; -.
IntAct; P11021; 207.
MINT; MINT-1135308; -.
STRING; 9606.ENSP00000324173; -.
BindingDB; P11021; -.
ChEMBL; CHEMBL1781865; -.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB00025; Antihemophilic Factor (Recombinant).
iPTMnet; P11021; -.
PhosphoSitePlus; P11021; -.
SwissPalm; P11021; -.
BioMuta; HSPA5; -.
DMDM; 14916999; -.
DOSAC-COBS-2DPAGE; P11021; -.
OGP; P11021; -.
REPRODUCTION-2DPAGE; P11021; -.
SWISS-2DPAGE; P11021; -.
UCD-2DPAGE; P11021; -.
EPD; P11021; -.
PaxDb; P11021; -.
PeptideAtlas; P11021; -.
PRIDE; P11021; -.
TopDownProteomics; P11021; -.
DNASU; 3309; -.
Ensembl; ENST00000324460; ENSP00000324173; ENSG00000044574.
GeneID; 3309; -.
KEGG; hsa:3309; -.
CTD; 3309; -.
DisGeNET; 3309; -.
EuPathDB; HostDB:ENSG00000044574.7; -.
GeneCards; HSPA5; -.
HGNC; HGNC:5238; HSPA5.
HPA; CAB005221; -.
HPA; HPA038845; -.
HPA; HPA038846; -.
MIM; 138120; gene.
neXtProt; NX_P11021; -.
OpenTargets; ENSG00000044574; -.
PharmGKB; PA29504; -.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00890000139357; -.
HOGENOM; HOG000228135; -.
HOVERGEN; HBG051845; -.
InParanoid; P11021; -.
KO; K09490; -.
OMA; CVGVMQK; -.
OrthoDB; EOG091G0352; -.
PhylomeDB; P11021; -.
TreeFam; TF105044; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-381033; ATF6 (ATF6-alpha) activates chaperones.
Reactome; R-HSA-381042; PERK regulates gene expression.
Reactome; R-HSA-381070; IRE1alpha activates chaperones.
Reactome; R-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
ChiTaRS; HSPA5; human.
EvolutionaryTrace; P11021; -.
GeneWiki; Binding_immunoglobulin_protein; -.
GenomeRNAi; 3309; -.
PRO; PR:P11021; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000044574; -.
CleanEx; HS_HSPA5; -.
ExpressionAtlas; P11021; baseline and differential.
Genevisible; P11021; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:BHF-UCL.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:AgBase.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
GO; GO:0051087; F:chaperone binding; TAS:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0051787; F:misfolded protein binding; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; TAS:UniProtKB.
GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; IEA:Ensembl.
GO; GO:0036500; P:ATF6-mediated unfolded protein response; TAS:Reactome.
GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl.
GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:0071287; P:cellular response to manganese ion; IEA:Ensembl.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl.
GO; GO:0021589; P:cerebellum structural organization; IEA:Ensembl.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; TAS:BHF-UCL.
GO; GO:0006983; P:ER overload response; IEA:Ensembl.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0035437; P:maintenance of protein localization in endoplasmic reticulum; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0090074; P:negative regulation of protein homodimerization activity; TAS:ParkinsonsUK-UCL.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0036499; P:PERK-mediated unfolded protein response; TAS:Reactome.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; TAS:ParkinsonsUK-UCL.
GO; GO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL.
GO; GO:1903891; P:regulation of ATF6-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:1903894; P:regulation of IRE1-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:1903897; P:regulation of PERK-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:0060904; P:regulation of protein folding in endoplasmic reticulum; TAS:BHF-UCL.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:1904313; P:response to methamphetamine hydrochloride; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IEA:Ensembl.
GO; GO:0097501; P:stress response to metal ion; IEA:Ensembl.
GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB.
GO; GO:1901998; P:toxin transport; IEA:Ensembl.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; TAS:BHF-UCL.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C.
InterPro; IPR029047; HSP70_peptide-bd.
InterPro; IPR013126; Hsp_70_fam.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00014; ER_TARGET; 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; Complete proteome; Cytoplasm;
Direct protein sequencing; Endoplasmic reticulum; Isopeptide bond;
Methylation; Nitration; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Signal; Ubl conjugation.
SIGNAL 1 18 {ECO:0000269|PubMed:2294010,
ECO:0000269|PubMed:9150948}.
CHAIN 19 654 78 kDa glucose-regulated protein.
/FTId=PRO_0000013566.
NP_BIND 36 39 ATP.
NP_BIND 227 229 ATP.
NP_BIND 293 300 ATP.
NP_BIND 364 367 ATP.
MOTIF 651 654 Prevents secretion from ER.
BINDING 96 96 ATP.
MOD_RES 86 86 Phosphoserine.
{ECO:0000250|UniProtKB:P06761}.
MOD_RES 125 125 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 160 160 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 213 213 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 326 326 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 353 353 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 447 447 N6-succinyllysine.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 518 518 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 585 585 N6,N6,N6-trimethyllysine; by METTL21A; in
vitro. {ECO:0000244|PubMed:24129315,
ECO:0000269|PubMed:23349634,
ECO:0000269|PubMed:23921388}.
MOD_RES 585 585 N6,N6-dimethyllysine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 585 585 N6-methyllysine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 591 591 N6-methyllysine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 643 643 Phosphothreonine.
{ECO:0000250|UniProtKB:P20029}.
MOD_RES 648 648 Phosphothreonine.
{ECO:0000250|UniProtKB:P20029}.
CROSSLNK 352 352 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 353 353 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
VARIANT 543 543 N -> H (in dbSNP:rs35356639).
{ECO:0000269|Ref.5}.
/FTId=VAR_025815.
MUTAGEN 585 585 K->R: Complete loss of in vitro
methylation by METTL21A.
{ECO:0000269|PubMed:23349634,
ECO:0000269|PubMed:23921388}.
CONFLICT 297 297 Missing (in Ref. 1; AAA52614 and 2;
CAA61201). {ECO:0000305}.
CONFLICT 418 418 D -> H (in Ref. 1; AAA52614 and 2;
CAA61201). {ECO:0000305}.
CONFLICT 439 439 R -> S (in Ref. 1; AAA52614 and 2;
CAA61201). {ECO:0000305}.
CONFLICT 447 447 K -> N (in Ref. 1; AAA52614 and 2;
CAA61201). {ECO:0000305}.
STRAND 31 34 {ECO:0000244|PDB:5F0X}.
STRAND 37 45 {ECO:0000244|PDB:5F0X}.
STRAND 47 52 {ECO:0000244|PDB:5F0X}.
STRAND 60 63 {ECO:0000244|PDB:5F0X}.
STRAND 66 68 {ECO:0000244|PDB:5F0X}.
STRAND 74 76 {ECO:0000244|PDB:5F0X}.
HELIX 78 82 {ECO:0000244|PDB:5F0X}.
HELIX 84 86 {ECO:0000244|PDB:3LDN}.
HELIX 88 90 {ECO:0000244|PDB:5F0X}.
STRAND 91 93 {ECO:0000244|PDB:3IUC}.
HELIX 95 97 {ECO:0000244|PDB:5F0X}.
TURN 98 100 {ECO:0000244|PDB:5F0X}.
HELIX 106 114 {ECO:0000244|PDB:5F0X}.
STRAND 116 122 {ECO:0000244|PDB:5F0X}.
STRAND 125 131 {ECO:0000244|PDB:5F0X}.
STRAND 137 140 {ECO:0000244|PDB:5F0X}.
HELIX 142 161 {ECO:0000244|PDB:5F0X}.
STRAND 167 172 {ECO:0000244|PDB:5F0X}.
HELIX 178 190 {ECO:0000244|PDB:5F0X}.
STRAND 194 200 {ECO:0000244|PDB:5F0X}.
HELIX 201 208 {ECO:0000244|PDB:5F0X}.
TURN 209 212 {ECO:0000244|PDB:5F0X}.
STRAND 215 225 {ECO:0000244|PDB:5F0X}.
STRAND 230 238 {ECO:0000244|PDB:5F0X}.
STRAND 241 250 {ECO:0000244|PDB:5F0X}.
HELIX 255 274 {ECO:0000244|PDB:5F0X}.
HELIX 278 280 {ECO:0000244|PDB:5F0X}.
HELIX 282 298 {ECO:0000244|PDB:5F0X}.
TURN 299 301 {ECO:0000244|PDB:5F0X}.
STRAND 302 313 {ECO:0000244|PDB:5F0X}.
STRAND 316 323 {ECO:0000244|PDB:5F0X}.
HELIX 324 337 {ECO:0000244|PDB:5F0X}.
HELIX 339 348 {ECO:0000244|PDB:5F0X}.
HELIX 353 355 {ECO:0000244|PDB:5F0X}.
STRAND 358 363 {ECO:0000244|PDB:5F0X}.
HELIX 364 367 {ECO:0000244|PDB:5F0X}.
HELIX 369 378 {ECO:0000244|PDB:5F0X}.
TURN 379 381 {ECO:0000244|PDB:5F0X}.
TURN 390 392 {ECO:0000244|PDB:5F0X}.
HELIX 393 405 {ECO:0000244|PDB:5F0X}.
STRAND 415 419 {ECO:0000244|PDB:5E84}.
STRAND 424 428 {ECO:0000244|PDB:5E85}.
TURN 429 431 {ECO:0000244|PDB:5E85}.
STRAND 432 437 {ECO:0000244|PDB:5E85}.
STRAND 442 455 {ECO:0000244|PDB:5E85}.
STRAND 460 467 {ECO:0000244|PDB:5E85}.
HELIX 473 475 {ECO:0000244|PDB:5E85}.
STRAND 476 485 {ECO:0000244|PDB:5E85}.
STRAND 491 493 {ECO:0000244|PDB:5E84}.
STRAND 497 503 {ECO:0000244|PDB:5E85}.
STRAND 509 515 {ECO:0000244|PDB:5E85}.
TURN 516 518 {ECO:0000244|PDB:5E85}.
STRAND 521 526 {ECO:0000244|PDB:5E85}.
TURN 528 531 {ECO:0000244|PDB:5E85}.
HELIX 535 547 {ECO:0000244|PDB:5E85}.
HELIX 549 577 {ECO:0000244|PDB:5E85}.
TURN 579 581 {ECO:0000244|PDB:5E85}.
HELIX 582 585 {ECO:0000244|PDB:5E85}.
HELIX 590 606 {ECO:0000244|PDB:5E85}.
HELIX 613 634 {ECO:0000244|PDB:5E85}.
SEQUENCE 654 AA; 72333 MW; 59B7D8D85BC32A00 CRC64;
MKLSLVAAML LLLSAARAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV EIIANDQGNR
ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG RTWNDPSVQQ DIKFLPFKVV
EKKTKPYIQV DIGGGQTKTF APEEISAMVL TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ
RQATKDAGTI AGLNVMRIIN EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG
VFEVVATNGD THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS
SQHQARIEIE SFYEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD LKKSDIDEIV
LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV QAGVLSGDQD TGDLVLLDVC
PLTLGIETVG GVMTKLIPRN TVVPTKKSQI FSTASDNQPT VTIKVYEGER PLTKDNHLLG
TFDLTGIPPA PRGVPQIEVT FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER
MVNDAEKFAE EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSSED KETMEKAVEE
KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSAGP PPTGEEDTAE KDEL


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E1497h ELISA kit 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER pro 96T
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
EIAAB30362 CaBP2,Cabp2,Calcium-binding protein 2,Endoplasmic reticulum resident protein 70,Endoplasmic reticulum resident protein 72,ER protein 70,ER protein 72,ERp70,Erp70,ERp72,ERp-72,Pdia4,Protein disulfide-i
SPC-180D GRP78 (Bip) BIP, Grp78, HspA5, MIF2, immunoglobulin heavy chain binding protein Host Species Rabbit Species Reactivity Human, Mouse, Rat, Canine. Other species not yet tested. 100ug
SPC-180C GRP78 (Bip) BIP, Grp78, HspA5, MIF2, immunoglobulin heavy chain binding protein Host Species Rabbit Species Reactivity Human, Mouse, Rat, Canine. Other species not yet tested. 25ug
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
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
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


 

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