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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)

 BIP_HUMAN               Reviewed;         654 AA.
P11021; B0QZ61; Q2EF78; Q9NPF1; Q9UK02;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
11-JUL-2001, sequence version 2.
23-MAY-2018, entry version 213.
RecName: Full=Endoplasmic reticulum chaperone BiP {ECO:0000305};
EC=3.6.4.10 {ECO:0000269|PubMed:26655470};
AltName: Full=78 kDa glucose-regulated protein {ECO:0000303|PubMed:2840249};
Short=GRP-78 {ECO:0000303|PubMed:2840249};
AltName: Full=Binding-immunoglobulin protein {ECO:0000303|Ref.4};
Short=BiP {ECO:0000303|Ref.4};
AltName: Full=Heat shock protein 70 family protein 5 {ECO:0000305};
Short=HSP70 family protein 5 {ECO:0000305};
AltName: Full=Heat shock protein family A member 5 {ECO:0000312|HGNC:HGNC:5238};
AltName: Full=Immunoglobulin heavy chain-binding protein {ECO:0000303|Ref.4};
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]
FUNCTION.
PubMed=1550958;
Ng D.T., Watowich S.S., Lamb R.A.;
"Analysis in vivo of GRP78-BiP/substrate interactions and their role
in induction of the GRP78-BiP gene.";
Mol. Biol. Cell 3:143-155(1992).
[16]
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).
[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]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
FUNCTION.
PubMed=19538957; DOI=10.1016/j.yexcr.2009.06.009;
Oikawa D., Kimata Y., Kohno K., Iwawaki T.;
"Activation of mammalian IRE1alpha upon ER stress depends on
dissociation of BiP rather than on direct interaction with unfolded
proteins.";
Exp. Cell Res. 315:2496-2504(2009).
[28]
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).
[29]
INTERACTION WITH MANF.
PubMed=22637475; DOI=10.1074/jbc.M112.356345;
Glembotski C.C., Thuerauf D.J., Huang C., Vekich J.A., Gottlieb R.A.,
Doroudgar S.;
"Mesencephalic astrocyte-derived neurotrophic factor protects the
heart from ischemic damage and is selectively secreted upon
sarco/endoplasmic reticulum calcium depletion.";
J. Biol. Chem. 287:25893-25904(2012).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
AMPYLATION.
PubMed=25601083; DOI=10.1074/jbc.M114.618348;
Sanyal A., Chen A.J., Nakayasu E.S., Lazar C.S., Zbornik E.A.,
Worby C.A., Koller A., Mattoo S.;
"A novel link between Fic (filamentation induced by cAMP)-mediated
adenylylation/AMPylation and the unfolded protein response.";
J. Biol. Chem. 290:8482-8499(2015).
[39]
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).
[40]
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).
[41]
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).
[42]
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).
[43]
REVIEW.
PubMed=28286085; DOI=10.1016/j.gene.2017.03.005;
Wang J., Lee J., Liem D., Ping P.;
"HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic
reticulum.";
Gene 618:14-23(2017).
[44]
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).
[45]
FUNCTION, INTERACTION WITH LOXL2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=28332555; DOI=10.1038/srep44988;
Cuevas E.P., Eraso P., Mazon M.J., Santos V., Moreno-Bueno G.,
Cano A., Portillo F.;
"LOXL2 drives epithelial-mesenchymal transition via activation of
IRE1-XBP1 signalling pathway.";
Sci. Rep. 7:44988-44988(2017).
[46]
SUBCELLULAR LOCATION.
PubMed=29497057; DOI=10.1038/s41467-018-03355-0;
Bai M., Vozdek R., Hnizda A., Jiang C., Wang B., Kuchar L., Li T.,
Zhang Y., Wood C., Feng L., Dang Y., Ma D.K.;
"Conserved roles of C. elegans and human MANFs in sulfatide binding
and cytoprotection.";
Nat. Commun. 9:897-897(2018).
[47]
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).
[48]
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).
[49] {ECO:0000244|PDB:5E84, ECO:0000244|PDB:5E85, ECO:0000244|PDB:5E86}
X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 418-637 IN COMPLEX WITH ATP,
CATALYTIC ACTIVITY, ENZYME REGULATION, AND MUTAGENESIS OF THR-229.
PubMed=26655470; DOI=10.1016/j.str.2015.10.012;
Yang J., Nune M., Zong Y., Zhou L., Liu Q.;
"Close and allosteric opening of the polypeptide-binding site in a
human Hsp70 chaperone BiP.";
Structure 23:2191-2203(2015).
-!- FUNCTION: Endoplasmic reticulum chaperone that plays a key role in
protein folding and quality control in the endoplasmic reticulum
lumen (PubMed:2294010, PubMed:23769672, PubMed:23990668,
PubMed:28332555). Involved in the correct folding of proteins and
degradation of misfolded proteins via its interaction with
DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5
from its substrate (By similarity). Acts as a key repressor of the
ERN1/IRE1-mediated unfolded protein response (UPR)
(PubMed:1550958, PubMed:19538957). In the unstressed endoplasmic
reticulum, recruited by DNAJB9/ERdj4 to the luminal region of
ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1,
thereby inactivating ERN1/IRE1 (By similarity). Accumulation of
misfolded protein in the endoplasmic reticulum causes release of
HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent
activation of ERN1/IRE1 (By similarity).
{ECO:0000250|UniProtKB:G3I8R9, ECO:0000250|UniProtKB:P20029,
ECO:0000269|PubMed:1550958, ECO:0000269|PubMed:19538957,
ECO:0000269|PubMed:2294010, ECO:0000269|PubMed:23769672,
ECO:0000269|PubMed:23990668, ECO:0000269|PubMed:28332555}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:26655470}.
-!- ENZYME REGULATION: The chaperone activity is regulated by ATP-
induced allosteric coupling of the nucleotide-binding (NBD) and
substrate-binding (SBD) domains. In the ADP-bound and nucleotide-
free (apo) states, the two domains have little interaction
(PubMed:26655470). In contrast, in the ATP-bound state the two
domains are tightly coupled, which results in drastically
accelerated kinetics in both binding and release of polypeptide
substrates (PubMed:26655470). J domain-containing co-chaperones
(DNAJB9/ERdj4 or DNAJC10/ERdj5) stimulate the ATPase activity and
are required for efficient substrate recognition by HSPA5/BiP (By
similarity). Homooligomerization inactivates participating
HSPA5/BiP protomers and probably act as reservoirs to store
HSPA5/BiP molecules when they are not needed by the cell (By
similarity). {ECO:0000250|UniProtKB:G3I8R9,
ECO:0000269|PubMed:26655470, ECO:0000303|PubMed:28286085}.
-!- SUBUNIT: Monomer and homooligomer; homooligomerization via the
interdomain linker inactivates the chaperone activity and acts as
a storage of HSPA5/BiP molecules (By similarity). 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 DNAJB9/ERdj4;
leading to recruit HSPA5/BiP to ERN1/IRE1 (By similarity).
Interacts with ERN1/IRE1; interaction takes place following
interaction with DNAJB9/ERdj4 and leads to inactivate ERN1/IRE1
(By similarity). 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).
Interacts with MANF; the interaction is direct (PubMed:22637475).
Interacts with LOXL2; leading to activate the ERN1/IRE1-XBP1
pathway of the unfolded protein response (PubMed:28332555).
{ECO:0000250|UniProtKB:G3I8R9, 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:22637475, ECO:0000269|PubMed:23349634,
ECO:0000269|PubMed:23769672, ECO:0000269|PubMed:23990668,
ECO:0000269|PubMed:26657846, ECO:0000269|PubMed:26940976,
ECO:0000269|PubMed:28332555}.
-!- 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;
O75460-1:ERN1; NbExp=4; IntAct=EBI-354921, EBI-15600828;
Q96IZ0:PAWR; NbExp=8; IntAct=EBI-354921, EBI-595869;
Q62627:Pawr (xeno); NbExp=4; IntAct=EBI-354921, EBI-1187240;
P04049:RAF1; NbExp=5; IntAct=EBI-354921, EBI-365996;
P61619:SEC61A1; NbExp=3; IntAct=EBI-354921, EBI-358919;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000269|PubMed:21080038, ECO:0000269|PubMed:21289099,
ECO:0000269|PubMed:23990668, ECO:0000269|PubMed:29497057}.
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}.
-!- DOMAIN: The interdomain linker regulates the chaperone activity by
mediating the formation of homooligomers. Homooligomers are formed
by engagement of the interdomain linker of one HSPA5/BiP molecule
as a typical substrate of an adjacent HSPA5/BiP molecule.
HSPA5/BiP oligomerization inactivates participating HSPA5/BiP
protomers. HSPA5/BiP oligomers probably act as reservoirs to store
HSPA5/BiP molecules when they are not needed by the cell. When the
levels of unfolded proteins rise, cells can rapidly break up these
oligomers to make active monomers. {ECO:0000250|UniProtKB:G3I8R9}.
-!- PTM: AMPylated by FICD (PubMed:25601083). In unstressed cells,
AMPylation at Thr-518 by FICD inactivates the chaperome activity:
AMPylated form is locked in a relatively inert state and only
weakly stimulated by J domain-containing proteins (By similarity).
In response to endoplasmic reticulum stress, de-AMPylation by the
same protein, FICD, restores the chaperone activity (By
similarity). {ECO:0000250|UniProtKB:G3I8R9,
ECO:0000269|PubMed:25601083}.
-!- DISEASE: Note=Autoantigen in rheumatoid arthritis.
{ECO:0000269|PubMed:11160188}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
-!- CAUTION: AMPylation was initially reported to take place at Ser-
365 and Thr-366 in vitro, and promote activation of HSPA5/BiP
(PubMed:25601083). However, it was later shown that AMPylation
takes place at Thr-518 and leads to inactivation of HSPA5/BiP.
{ECO:0000250|UniProtKB:G3I8R9, ECO:0000269|PubMed:25601083}.
-!- 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.
PDB; 6ASY; X-ray; 1.85 A; A/B=25-633.
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; -.
PDBsum; 6ASY; -.
ProteinModelPortal; P11021; -.
SMR; P11021; -.
BioGrid; 109541; 571.
CORUM; P11021; -.
DIP; DIP-33189N; -.
ELM; P11021; -.
IntAct; P11021; 194.
MINT; P11021; -.
STRING; 9606.ENSP00000324173; -.
BindingDB; P11021; -.
ChEMBL; CHEMBL1781865; -.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB00025; Antihemophilic Factor (Recombinant).
TCDB; 1.A.33.1.6; the cation channel-forming heat shock protein-70 (hsp70) family.
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; ENSGT00910000144045; -.
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.
SIGNOR; P11021; -.
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; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA: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; HDA: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; IMP:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0032991; C:protein-containing 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; HDA: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:0071480; P:cellular response to gamma radiation; 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:1903895; P:negative regulation of IRE1-mediated unfolded protein response; ISS:UniProtKB.
GO; GO:0090074; P:negative regulation of protein homodimerization activity; ISS:UniProtKB.
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:0097501; P:stress response to metal ion; IEA:Ensembl.
GO; GO:0021762; P:substantia nigra development; HEP: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_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
PANTHER; PTHR19375; PTHR19375; 1.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
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; Hydrolase;
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 Endoplasmic reticulum chaperone BiP.
/FTId=PRO_0000013566.
NP_BIND 36 39 ATP. {ECO:0000269|PubMed:21526763}.
NP_BIND 227 229 ATP. {ECO:0000269|PubMed:21526763}.
NP_BIND 293 300 ATP. {ECO:0000269|PubMed:21526763}.
NP_BIND 364 367 ATP. {ECO:0000269|PubMed:21526763}.
REGION 125 280 Nucleotide-binding (NBD).
{ECO:0000303|PubMed:28286085}.
REGION 409 419 Interdomain linker.
{ECO:0000250|UniProtKB:G3I8R9}.
REGION 420 500 Substrate-binding (SBD).
{ECO:0000303|PubMed:28286085}.
MOTIF 651 654 Prevents secretion from ER.
{ECO:0000255}.
BINDING 96 96 ATP. {ECO:0000269|PubMed:21526763}.
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 271 271 N6-acetyllysine.
{ECO:0000250|UniProtKB:P0DMV8}.
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 492 492 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 518 518 O-AMP-threonine.
{ECO:0000250|UniProtKB:G3I8R9}.
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 229 229 T->A: Impaired ATPase activity.
{ECO:0000269|PubMed:26655470}.
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:6ASY}.
HELIX 88 90 {ECO:0000244|PDB:5F0X}.
STRAND 91 93 {ECO:0000244|PDB:6ASY}.
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:6ASY}.
STRAND 424 428 {ECO:0000244|PDB:6ASY}.
TURN 429 431 {ECO:0000244|PDB:5E85}.
STRAND 433 437 {ECO:0000244|PDB:6ASY}.
STRAND 442 451 {ECO:0000244|PDB:6ASY}.
STRAND 461 468 {ECO:0000244|PDB:6ASY}.
HELIX 473 475 {ECO:0000244|PDB:6ASY}.
STRAND 476 484 {ECO:0000244|PDB:6ASY}.
STRAND 491 493 {ECO:0000244|PDB:6ASY}.
STRAND 497 503 {ECO:0000244|PDB:6ASY}.
STRAND 509 515 {ECO:0000244|PDB:6ASY}.
TURN 516 518 {ECO:0000244|PDB:6ASY}.
STRAND 521 526 {ECO:0000244|PDB:5E85}.
TURN 528 531 {ECO:0000244|PDB:5E85}.
HELIX 535 576 {ECO:0000244|PDB:6ASY}.
TURN 579 581 {ECO:0000244|PDB:6ASY}.
HELIX 582 585 {ECO:0000244|PDB:6ASY}.
HELIX 588 607 {ECO:0000244|PDB:6ASY}.
HELIX 613 631 {ECO:0000244|PDB:6ASY}.
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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