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78 kDa glucose-regulated protein (GRP-78) (Heat shock 70 kDa protein 5) (Immunoglobulin heavy chain-binding protein) (BiP)

 GRP78_MOUSE             Reviewed;         655 AA.
P20029; O35642; Q3UFF2; Q61630;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 3.
25-OCT-2017, entry version 185.
RecName: Full=78 kDa glucose-regulated protein {ECO:0000250|UniProtKB:P11021};
Short=GRP-78 {ECO:0000250|UniProtKB:P11021};
AltName: Full=Heat shock 70 kDa protein 5;
AltName: Full=Immunoglobulin heavy chain-binding protein {ECO:0000303|PubMed:2895472};
Short=BiP {ECO:0000303|PubMed:2895472};
Flags: Precursor;
Name=Hspa5 {ECO:0000312|MGI:MGI:95835}; Synonyms=Grp78;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2895472; DOI=10.1073/pnas.85.7.2250;
Haas I.G., Meo T.;
"cDNA cloning of the immunoglobulin heavy chain binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 85:2250-2254(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-46.
PubMed=2559088;
Kozutsumi Y., Normington K., Press E., Slaughter C., Sambrook J.,
Gething M.J.;
"Identification of immunoglobulin heavy chain binding protein as
glucose-regulated protein 78 on the basis of amino acid sequence,
immunological cross-reactivity, and functional activity.";
J. Cell Sci. Suppl. 11:115-137(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=8645260; DOI=10.1006/bbrc.1996.0313;
Kajiwara K., Nagawawa H., Shimizu-Nishikawa K., Ookura T., Kimura M.,
Sugaya E.;
"Molecular characterization of seizure-related genes isolated by
differential screening.";
Biochem. Biophys. Res. Commun. 219:795-799(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
STRAIN=C3B10RF1; TISSUE=Liver;
PubMed=7607546; DOI=10.1016/0378-1119(95)00083-I;
Tillman J.B., Mote P.L., Walford R.L., Spindler S.R.;
"Structure and regulation of the mouse GRP78 (BiP) promoter by glucose
and calcium ionophore.";
Gene 158:225-229(1995).
[7]
PROTEIN SEQUENCE OF 20-36.
TISSUE=Fibroblast;
PubMed=7523108; DOI=10.1002/elps.11501501101;
Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
"Separation and sequencing of familiar and novel murine proteins using
preparative two-dimensional gel electrophoresis.";
Electrophoresis 15:735-745(1994).
[8]
PROTEIN SEQUENCE OF 51-75; 140-153; 156-164; 166-182; 187-215;
308-337; 354-368; 449-493; 525-541 AND 623-634, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Klug S., Friebe K., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 488-655.
PubMed=2583523; DOI=10.1016/0378-1119(89)90054-1;
Parfett C.L.J., Hofbauer R., Brudzynski K., Edwards D.R.,
Denhardt D.T.;
"Differential screening of a cDNA library with cDNA probes amplified
in a heterologous host: isolation of murine GRP78 (BiP) and other
serum-regulated low-abundance mRNAs.";
Gene 82:291-303(1989).
[10]
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).
[11]
INTERACTION WITH DNAJC1.
PubMed=12065409; DOI=10.1093/emboj/cdf315;
Dudek J., Volkmer J., Bies C., Guth S., Mueller A., Lerner M.,
Feick P., Schaefer K.-H., Morgenstern E., Hennessy F., Blatch G.L.,
Janoscheck K., Heim N., Scholtes P., Frien M., Nastainczyk W.,
Zimmermann R.;
"A novel type of co-chaperone mediates transmembrane recruitment of
DnaK-like chaperones to ribosomes.";
EMBO J. 21:2958-2967(2002).
[12]
FUNCTION, AND 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).
[13]
NITRATION [LARGE SCALE ANALYSIS] AT TYR-161, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16800626; DOI=10.1021/bi060474w;
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
Squier T.C., Bigelow D.J.;
"Endogenously nitrated proteins in mouse brain: links to
neurodegenerative disease.";
Biochemistry 45:8009-8022(2006).
[14]
IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CELF1; CALR;
CALR3 AND HSP90B1.
PubMed=16931514; DOI=10.1074/jbc.M605701200;
Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H.,
Hershey J.W., Timchenko N.A.;
"Age-specific CUGBP1-eIF2 complex increases translation of
CCAAT/enhancer-binding protein beta in old liver.";
J. Biol. Chem. 281:32806-32819(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-644; THR-649 AND
SER-650, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[18]
SUBCELLULAR LOCATION, AND INTERACTION WITH MX1.
PubMed=21992152; DOI=10.1089/jir.2010.0132;
Numajiri Haruki A., Naito T., Nishie T., Saito S., Nagata K.;
"Interferon-inducible antiviral protein MxA enhances cell death
triggered by endoplasmic reticulum stress.";
J. Interferon Cytokine Res. 31:847-856(2011).
[19]
METHYLATION AT LYS-586.
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).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126; LYS-214; LYS-327 AND
LYS-354, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-448, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Plays a role in facilitating the assembly of multimeric
protein complexes inside the endoplasmic reticulum
(PubMed:12475965). 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 (PubMed:12411443). {ECO:0000250|UniProtKB:Q96P69,
ECO:0000269|PubMed:12411443, ECO:0000269|PubMed:12475965}.
-!- SUBUNIT: Interacts with DNAJC1 (via J domain) (PubMed:12065409).
Component of an EIF2 complex at least composed of CELF1/CUGBP1,
CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (PubMed:16931514).
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 (PubMed:12475965). Interacts with TMEM132A and
TRIM21 (By similarity). May form a complex with ERLEC1, OS9, SEL1L
and SYVN1 (By similarity). Interacts with DNAJC10
(PubMed:12411443). Interacts with MX1 (PubMed:21992152). Interacts
with METTL23 (By similarity). Interacts with CEMIP; the
interaction induces calcium leakage from the endoplasmic reticulum
and cell migration (By similarity). Interacts with PCSK4 form; the
interaction takes place in the endoplasmic reticulum (By
similarity). Interacts with CIPC (By similarity). Interacts with
CCDC88B (via C-terminus); the interaction opposes ERN1-mediated
JNK activation, protecting against apoptosis (By similarity).
Interacts with INPP5K; necessary for INPP5K localization at the
endoplasmic reticulum (By similarity).
{ECO:0000250|UniProtKB:P11021, ECO:0000250|UniProtKB:Q96P69,
ECO:0000269|PubMed:12065409, ECO:0000269|PubMed:12411443,
ECO:0000269|PubMed:12475965, ECO:0000269|PubMed:16931514,
ECO:0000269|PubMed:21992152}.
-!- INTERACTION:
O35451:Atf6b; NbExp=2; IntAct=EBI-772325, EBI-8361741;
Q99KV1:Dnajb11; NbExp=4; IntAct=EBI-772325, EBI-8328260;
O75460:ERN1 (xeno); NbExp=2; IntAct=EBI-772325, EBI-371750;
P00441:SOD1 (xeno); NbExp=7; IntAct=EBI-772325, EBI-990792;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000255|PROSITE-ProRule:PRU10138,
ECO:0000269|PubMed:21992152}. Melanosome
{ECO:0000250|UniProtKB:P11021}. Cytoplasm
{ECO:0000269|PubMed:21992152}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
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EMBL; AJ002387; CAA05361.1; -; mRNA.
EMBL; M19351; AAA37315.1; -; mRNA.
EMBL; D78645; BAA11462.1; -; mRNA.
EMBL; AK076079; BAC36166.1; -; mRNA.
EMBL; AK146647; BAE27328.1; -; mRNA.
EMBL; AK148539; BAE28609.1; -; mRNA.
EMBL; AK151647; BAE30576.1; -; mRNA.
EMBL; AK152020; BAE30882.1; -; mRNA.
EMBL; AK166739; BAE38982.1; -; mRNA.
EMBL; AK169034; BAE40825.1; -; mRNA.
EMBL; BC050927; AAH50927.1; -; mRNA.
EMBL; U16277; AAA76734.1; -; Genomic_DNA.
EMBL; M30779; AAA37742.1; -; mRNA.
CCDS; CCDS15950.1; -.
PIR; A37048; A37048.
RefSeq; NP_001156906.1; NM_001163434.1.
RefSeq; NP_071705.3; NM_022310.3.
UniGene; Mm.330160; -.
UniGene; Mm.470180; -.
UniGene; Mm.474909; -.
ProteinModelPortal; P20029; -.
SMR; P20029; -.
BioGrid; 200078; 39.
CORUM; P20029; -.
DIP; DIP-32341N; -.
IntAct; P20029; 33.
MINT; MINT-1177274; -.
STRING; 10090.ENSMUSP00000028222; -.
iPTMnet; P20029; -.
PhosphoSitePlus; P20029; -.
SwissPalm; P20029; -.
COMPLUYEAST-2DPAGE; P20029; -.
REPRODUCTION-2DPAGE; IPI00319992; -.
REPRODUCTION-2DPAGE; P20029; -.
SWISS-2DPAGE; P20029; -.
UCD-2DPAGE; P20029; -.
EPD; P20029; -.
MaxQB; P20029; -.
PaxDb; P20029; -.
PeptideAtlas; P20029; -.
PRIDE; P20029; -.
TopDownProteomics; P20029; -.
Ensembl; ENSMUST00000028222; ENSMUSP00000028222; ENSMUSG00000026864.
Ensembl; ENSMUST00000100171; ENSMUSP00000097747; ENSMUSG00000026864.
GeneID; 14828; -.
KEGG; mmu:14828; -.
UCSC; uc008jis.2; mouse.
CTD; 3309; -.
MGI; MGI:95835; Hspa5.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00900000140908; -.
HOGENOM; HOG000228135; -.
HOVERGEN; HBG051845; -.
InParanoid; P20029; -.
KO; K09490; -.
OMA; CVGVMQK; -.
OrthoDB; EOG091G0352; -.
PhylomeDB; P20029; -.
TreeFam; TF105044; -.
Reactome; R-MMU-114608; Platelet degranulation.
ChiTaRS; Hspa5; mouse.
PRO; PR:P20029; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026864; -.
CleanEx; MM_HSPA5; -.
ExpressionAtlas; P20029; baseline and differential.
Genevisible; P20029; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IDA:ParkinsonsUK-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:BHF-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0030496; C:midbody; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISO:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0051787; F:misfolded protein binding; IDA:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0043022; F:ribosome binding; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; IMP:BHF-UCL.
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; ISO:MGI.
GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
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; IMP:BHF-UCL.
GO; GO:0021589; P:cerebellum structural organization; IMP:BHF-UCL.
GO; GO:0006983; P:ER overload response; IDA:MGI.
GO; GO:0035437; P:maintenance of protein localization in endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IGI:MGI.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0040019; P:positive regulation of embryonic development; TAS:BHF-UCL.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:BHF-UCL.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:BHF-UCL.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:MGI.
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; IEA:Ensembl.
GO; GO:1901998; P:toxin transport; IMP:MGI.
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;
Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Endoplasmic reticulum; Isopeptide bond;
Methylation; Nitration; Nucleotide-binding; Phosphoprotein;
Reference proteome; Signal; Ubl conjugation.
SIGNAL 1 19 {ECO:0000269|PubMed:2559088,
ECO:0000269|PubMed:7523108}.
CHAIN 20 655 78 kDa glucose-regulated protein.
/FTId=PRO_0000013568.
NP_BIND 37 40 ATP. {ECO:0000250}.
NP_BIND 228 230 ATP. {ECO:0000250}.
NP_BIND 294 301 ATP. {ECO:0000250}.
NP_BIND 365 368 ATP. {ECO:0000250}.
MOTIF 652 655 Prevents secretion from ER.
BINDING 97 97 ATP. {ECO:0000250}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:P06761}.
MOD_RES 126 126 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 161 161 Nitrated tyrosine.
{ECO:0000244|PubMed:16800626}.
MOD_RES 214 214 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 272 272 N6-acetyllysine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 327 327 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 354 354 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 448 448 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 493 493 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 519 519 Phosphothreonine.
{ECO:0000250|UniProtKB:P11021}.
MOD_RES 586 586 N6,N6,N6-trimethyllysine; by METTL21A; in
vitro. {ECO:0000269|PubMed:23921388}.
MOD_RES 586 586 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P11021}.
MOD_RES 586 586 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P11021}.
MOD_RES 592 592 N6-methyllysine.
{ECO:0000250|UniProtKB:P11021}.
MOD_RES 644 644 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 649 649 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 650 650 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
CROSSLNK 353 353 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11021}.
CROSSLNK 354 354 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P11021}.
CONFLICT 43 43 V -> F (in Ref. 3; BAA11462).
{ECO:0000305}.
CONFLICT 245 245 V -> W (in Ref. 3; BAA11462).
{ECO:0000305}.
CONFLICT 329 329 E -> G (in Ref. 3; BAA11462).
{ECO:0000305}.
CONFLICT 361 361 V -> A (in Ref. 3; BAA11462).
{ECO:0000305}.
CONFLICT 474 474 T -> R (in Ref. 1; CAA05361).
{ECO:0000305}.
CONFLICT 591 591 D -> G (in Ref. 9; AAA37742).
{ECO:0000305}.
CONFLICT 596 596 E -> K (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 655 AA; 72422 MW; AFB795D15E20FAC2 CRC64;
MMKFTVVAAA LLLLGAVRAE EEDKKEDVGT VVGIDLGTTY SCVGVFKNGR VEIIANDQGN
RITPSYVAFT PEGERLIGDA AKNQLTSNPE NTVFDAKRLI GRTWNDPSVQ QDIKFLPFKV
VEKKTKPYIQ VDIGGGQTKT FAPEEISAMV LTKMKETAEA YLGKKVTHAV VTVPAYFNDA
QRQATKDAGT IAGLNVMRII NEPTAAAIAY GLDKREGEKN ILVFDLGGGT FDVSLLTIDN
GVFEVVATNG DTHLGGEDFD QRVMEHFIKL YKKKTGKDVR KDNRAVQKLR REVEKAKRAL
SSQHQARIEI ESFFEGEDFS ETLTRAKFEE LNMDLFRSTM KPVQKVLEDS DLKKSDIDEI
VLVGGSTRIP KIQQLVKEFF NGKEPSRGIN PDEAVAYGAA VQAGVLSGDQ DTGDLVLLDV
CPLTLGIETV GGVMTKLIPR NTVVPTKKSQ IFSTASDNQP TVTIKVYEGE RPLTKDNHLL
GTFDLTGIPP APRGVPQIEV TFEIDVNGIL RVTAEDKGTG NKNKITITND QNRLTPEEIE
RMVNDAEKFA EEDKKLKERI DTRNELESYA YSLKNQIGDK EKLGGKLSSE DKETMEKAVE
EKIEWLESHQ DADIEDFKAK KKELEEIVQP IISKLYGSGG PPPTGEEDTS EKDEL


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