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UniProtKB/Swiss-Prot entry P11021


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GRP78_HUMAN
Primary accession number P11021
Secondary accession numbers Q2EF78 Q9NPF1 Q9UK02
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 11, 2001 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 112)
Name and origin of the protein
Protein name 78 kDa glucose-regulated protein [Precursor]
Synonyms GRP 78
Heat shock 70 kDa protein 5
Immunoglobulin heavy chain-binding protein
BiP
Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78
Gene name
Name: HSPA5
Synonyms: GRP78
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2840249 [NCBI, ExPASy, EBI, Israel, Japan]
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 MRNA].
TISSUE=Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
DOI=10.1093/nar/20.24.6481; PubMed=1480470 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 20-650, AND DISEASE.
TISSUE=Articular cartilage;
PubMed=11160188 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
PROTEIN SEQUENCE OF 22-38.
TISSUE=Mammary carcinoma;
DOI=10.1002/elps.1150180342; PubMed=9150946 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
PROTEIN SEQUENCE OF 19-39, AND FUNCTION.
PubMed=2294010 [NCBI, ExPASy, EBI, Israel, Japan]
Dana R.C., Welch W.J., Deftos L.J.;
"Heat shock proteins bind calcitonin.";
Endocrinology 126:672-674(1990).
[11]
PROTEIN SEQUENCE OF 19-40.
TISSUE=Colon carcinoma;
DOI=10.1002/elps.1150180344; PubMed=9150948 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
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 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.
[13]
COMPONENT OF A CHAPERONE COMPLEX.
DOI=10.1091/mbc.E02-05-0311; PubMed=12475965 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr025562r; PubMed=12643545 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-466, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[17]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M19645; AAA52614.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X87949; CAA61201.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ271729; CAB71335.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF216292; AAF42836.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ385847; ABD04090.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020235; AAH20235.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X59969; CAA42595.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF188611; AAF13605.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00003362; -.
PIR A29821; A29821.
RefSeq NP_005338.1; -.
UniGene Hs.605502
3D structure databases
HSSP P19120; 3HSC. [HSSP ENTRY / PDB]
SMR P11021; 28-576.
ModBase P11021.
Protein-protein interaction databases
IntAct P11021; 48.
PTM databases
PhosphoSite P11021; -.
Enzyme and pathway databases
Reactome REACT_604; Hemostasis.
2D gel databases
SWISS-2DPAGE P11021; -.
DOSAC-COBS-2DPAGE P11021; -.
OGP P11021; -.
PHCI-2DPAGE P11021; -.
PMMA-2DPAGE P11021; -.
REPRODUCTION-2DPAGE P11021; -.
Siena-2DPAGE P11021; -.
Organism-specific databases
GeneCards GC09M127036; -.
H-InvDB HIX0008382; -.
HGNC HGNC:5238; HSPA5.
GenAtlas HSPA5.
HPA CAB005221; -.
MIM 138120; gene. [NCBI / EBI]
180300; phenotype. [NCBI / EBI]
PharmGKB PA29504; -.
Gene expression databases
ArrayExpress P11021; -.
Bgee P11021; -.
CleanEx HS_HSPA5; -.
GermOnline ENSG00000044574; Homo sapiens.
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0005788; Cellular component: endoplasmic reticulum lumen (traceable author statement from UniProtKB).
GO:0005793; Cellular component: ER-Golgi intermediate compartment (inferred from direct assay from UniProtKB).
GO:0030176; Cellular component: integral to endoplasmic reticulum membrane (inferred from direct assay from UniProtKB).
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0048471; Cellular component: perinuclear region of cytoplasm (inferred from direct assay from UniProtKB).
GO:0005524; Molecular function: ATP binding (non-traceable author statement from UniProtKB).
GO:0005509; Molecular function: calcium ion binding (traceable author statement from UniProtKB).
GO:0043027; Molecular function: caspase inhibitor activity (inferred from direct assay from UniProtKB).
GO:0030674; Molecular function: protein binding, bridging (non-traceable author statement from UniProtKB).
GO:0051082; Molecular function: unfolded protein binding (traceable author statement from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (inferred from mutant phenotype from UniProtKB).
GO:0042149; Biological process: cellular response to glucose starvation (inferred from direct assay from UniProtKB).
GO:0043154; Biological process: negative regulation of caspase activity (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000886; ER_targeting_sequence.
IPR018181; Heat_shock_70_CS.
IPR001023; Hsp70.
IPR013126; Hsp_70.
Graphical view of domain structure.
PANTHER PTHR19375; Hsp70; 1.
Pfam PF00012; HSP70; 1.
Pfam graphical view of domain structure.
PRINTS PR00301; HEATSHOCK70.
ProDom PD000089; Hsp70; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00014; ER_TARGET; 1.
PS00297; HSP70_1; 1.
PS00329; HSP70_2; 1.
PS01036; HSP70_3; 1.
Proteomic databases
PRIDE P11021; -.
Genome annotation databases
Ensembl ENSG00000044574; Homo sapiens. [Contig view]
GeneID 3309; -.
KEGG hsa:3309; -.
Phylogenomic databases
HOVERGEN P11021; -.
OMA P11021; FEGERPM.
Other
DrugBank DB00025; Antihemophilic Factor.
NextBio 13123; -.
SOURCE HSPA5; Homo sapiens.
ProtoNet P11021.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Direct protein sequencing; Endoplasmic reticulum; Nucleotide-binding; Phosphoprotein; Polymorphism; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18      
CHAIN   19   654  636     78 kDa glucose-regulated protein. PRO_0000013566
MOTIF   651   654  4     Prevents secretion from ER. 
MOD_RES   166   166        Phosphothreonine (By similarity). 
MOD_RES   466   466        Phosphotyrosine. 
MOD_RES   571   571        Phosphoserine (By similarity). 
VARIANT   543   543  1     N -> H. VAR_025815 [3D]
CONFLICT   297   297        Missing (in Ref. 1 and 2). 
CONFLICT   418   418        D -> H (in Ref. 1 and 2). 
CONFLICT   439   439        R -> S (in Ref. 1 and 2). 
CONFLICT   447   447        K -> N (in Ref. 1 and 2). 
Sequence information
Length: 654 AA [This is the length of the unprocessed precursor] Molecular weight: 72333 Da [This is the MW of the unprocessed precursor] CRC64: 59B7D8D85BC32A00 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKLSLVAAML LLLSAARAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV EIIANDQGNR 

        70         80         90        100        110        120 
ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG RTWNDPSVQQ DIKFLPFKVV 

       130        140        150        160        170        180 
EKKTKPYIQV DIGGGQTKTF APEEISAMVL TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ 

       190        200        210        220        230        240 
RQATKDAGTI AGLNVMRIIN EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG 

       250        260        270        280        290        300 
VFEVVATNGD THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS 

       310        320        330        340        350        360 
SQHQARIEIE SFYEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD LKKSDIDEIV 

       370        380        390        400        410        420 
LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV QAGVLSGDQD TGDLVLLDVC 

       430        440        450        460        470        480 
PLTLGIETVG GVMTKLIPRN TVVPTKKSQI FSTASDNQPT VTIKVYEGER PLTKDNHLLG 

       490        500        510        520        530        540 
TFDLTGIPPA PRGVPQIEVT FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER 

       550        560        570        580        590        600 
MVNDAEKFAE EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSSED KETMEKAVEE 

       610        620        630        640        650 
KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSAGP PPTGEEDTAE KDEL 

P11021 in FASTA format

View entry in raw text format (no links)
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