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P11021 (GRP78_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
78 kDa glucose-regulated protein

Short name=GRP-78
Alternative name(s):
Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78
Heat shock 70 kDa protein 5
Immunoglobulin heavy chain-binding protein
Short name=BiP
Gene names
Name:HSPA5
Synonyms:GRP78
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length654 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably 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. Ref.12 Ref.26 Ref.27

Subunit structure

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. 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. Interacts with TMEM132A and TRIM21. May form a complex with ERLEC1, OS9, SEL1L and SYVN1. Interacts with DNAJC10 and MX1. Interacts with METTL23. Interacts with CEMIP; the interaction induces calcium leakage from the endoplamic reticulum and cell migration. Ref.15 Ref.17 Ref.18 Ref.21 Ref.22 Ref.26 Ref.27

Subcellular location

Endoplasmic reticulum lumen. Melanosome. Cytoplasm By similarity. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.19 Ref.20 Ref.26

Involvement in disease

Autoantigen in rheumatoid arthritis. Ref.10

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Cellular componentCytoplasm
Endoplasmic reticulum
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Methylation
Nitration
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity. Source: GOC

ER overload response

Inferred from electronic annotation. Source: Ensembl

ER-associated ubiquitin-dependent protein catabolic process

Traceable author statement PubMed 19816510. Source: BHF-UCL

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to antibiotic

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose starvation

Inferred from direct assay PubMed 10085239. Source: UniProtKB

cellular response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

cerebellar Purkinje cell layer development

Inferred from electronic annotation. Source: Ensembl

cerebellum structural organization

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum unfolded protein response

Traceable author statement PubMed 19816510. Source: BHF-UCL

maintenance of protein localization in endoplasmic reticulum

Inferred from mutant phenotype Ref.26. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 10760948PubMed 12665508. Source: UniProtKB

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of cell migration

Inferred from mutant phenotype Ref.26. Source: UniProtKB

positive regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

regulation of protein folding in endoplasmic reticulum

Traceable author statement PubMed 19816510. Source: BHF-UCL

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from mutant phenotype PubMed 11943137. Source: UniProtKB

endoplasmic reticulum chaperone complex

Inferred from direct assay PubMed 18400946. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

endoplasmic reticulum-Golgi intermediate compartment

Inferred from direct assay PubMed 15308636. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337. Source: UniProt

integral component of endoplasmic reticulum membrane

Inferred from direct assay PubMed 11181571. Source: BHF-UCL

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from direct assay PubMed 15166316. Source: UniProtKB

nucleus

Inferred from mutant phenotype PubMed 11943137. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

calcium ion binding

Traceable author statement PubMed 16130169. Source: UniProtKB

chaperone binding

Traceable author statement PubMed 19816510. Source: BHF-UCL

misfolded protein binding

Inferred from direct assay PubMed 18400946. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction Ref.18. Source: UniProtKB

ribosome binding

Inferred from electronic annotation. Source: Ensembl

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 8666824. Source: UniProtKB

unfolded protein binding

Traceable author statement PubMed 16130169. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.12 Ref.13
Chain19 – 65463678 kDa glucose-regulated protein
PRO_0000013566

Regions

Nucleotide binding36 – 394ATP
Nucleotide binding227 – 2293ATP
Nucleotide binding293 – 3008ATP
Nucleotide binding364 – 3674ATP
Motif651 – 6544Prevents secretion from ER

Sites

Binding site961ATP

Amino acid modifications

Modified residue1251N6-acetyllysine By similarity
Modified residue1601Nitrated tyrosine By similarity
Modified residue2131N6-acetyllysine By similarity
Modified residue3261N6-acetyllysine By similarity
Modified residue3531N6-acetyllysine By similarity
Modified residue4471N6-succinyllysine By similarity
Modified residue5181Phosphothreonine Ref.23
Modified residue5851N6,N6,N6-trimethyllysine; by METTL21A; in vitro Ref.15 Ref.25

Natural variations

Natural variant5431N → H. Ref.5
Corresponds to variant rs35356639 [ dbSNP | Ensembl ].
VAR_025815

Experimental info

Mutagenesis5851K → R: Complete loss of in vitro methylation by METTL21A. Ref.15 Ref.25
Sequence conflict2971Missing in AAA52614. Ref.1
Sequence conflict2971Missing in CAA61201. Ref.2
Sequence conflict4181D → H in AAA52614. Ref.1
Sequence conflict4181D → H in CAA61201. Ref.2
Sequence conflict4391R → S in AAA52614. Ref.1
Sequence conflict4391R → S in CAA61201. Ref.2
Sequence conflict4471K → N in AAA52614. Ref.1
Sequence conflict4471K → N in CAA61201. Ref.2

Secondary structure

........................................................................ 654
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11021 [UniParc].

Last modified July 11, 2001. Version 2.
Checksum: 59B7D8D85BC32A00

FASTA65472,333
        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 

« Hide

References

« Hide 'large scale' references
[1]"Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation."
Ting J., Lee A.S.
DNA 7:275-286(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Chao C.C.K.
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cervix carcinoma.
[3]"Grp78 is involved in the quality control of the LDL-receptor."
Hansen J.J., Nielsen M.N., Jorgensen M.M., Gregersen N., Bolund L.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[4]"Sequence differences between human grp78/BiP isolated from HeLa cells and previously reported human sequences."
Bermudez-Fajardo A., Llewellyn D.H., Campbell A.K., Errington R.R.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]NIEHS SNPs program
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-543.
[6]"DNA sequence and analysis of human chromosome 9."
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. expand/collapse author list , 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.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle.
[9]"A direct-repeat sequence of the human BiP gene is required for A23187-mediated inducibility and an inducible nuclear factor binding."
Chao C.C.K., Lin-Chao S.
Nucleic Acids Res. 20:6481-6485(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
[10]"The human endoplasmic reticulum molecular chaperone BiP is an autoantigen for rheumatoid arthritis and prevents the induction of experimental arthritis."
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.
J. Immunol. 166:1492-1498(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-650, DISEASE.
Tissue: Articular cartilage.
[11]"Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2."
Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S.
Electrophoresis 18:588-598(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-38.
Tissue: Mammary carcinoma.
[12]"Heat shock proteins bind calcitonin."
Dana R.C., Welch W.J., Deftos L.J.
Endocrinology 126:672-674(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-39, FUNCTION.
[13]"A two-dimensional gel database of human colon carcinoma proteins."
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-40.
Tissue: Colon carcinoma.
[14]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[15]"A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 582-596, INTERACTION WITH METTL23, METHYLATION AT LYS-585, MUTAGENESIS OF LYS-585, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF A CHAPERONE COMPLEX.
[17]"Association of stress proteins with autoantigens: a possible mechanism for triggering autoimmunity?"
Purcell A.W., Todd A., Kinoshita G., Lynch T.A., Keech C.L., Gething M.J., Gordon T.P.
Clin. Exp. Immunol. 132:193-200(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM21.
[18]"ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress."
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.
J. Biol. Chem. 278:1059-1066(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAJC10.
[19]"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
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.
J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[20]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
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.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[21]"Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP."
Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K.
J. Biol. Chem. 283:20914-20924(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERLEC1; OS9; SEL1L AND SYVN1.
[22]"OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD."
Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.
Nat. Cell Biol. 10:272-282(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERLEC1; OS9; SEL1L AND SYVN1.
[23]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-585, MUTAGENESIS OF LYS-585.
[26]"Unraveling the role of KIAA1199, a novel endoplasmic reticulum protein, in cancer cell migration."
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.
J. Natl. Cancer Inst. 105:1402-1416(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CEMIP, SUBCELLULAR LOCATION.
[27]"ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor."
Oka O.B., Pringle M.A., Schopp I.M., Braakman I., Bulleid N.J.
Mol. Cell 50:793-804(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DNAJC10.
[28]"Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78."
Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T., Moche M., Schuler H.
PLoS ONE 5:E8625-E8625(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 26-410.
[29]"Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity."
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.
J. Med. Chem. 54:4034-4041(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 26-407 IN COMPLEXES WITH ATP ANALOG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19645 Genomic DNA. Translation: AAA52614.1.
X87949 mRNA. Translation: CAA61201.1.
AJ271729 mRNA. Translation: CAB71335.1.
AF216292 mRNA. Translation: AAF42836.1.
DQ385847 Genomic DNA. Translation: ABD04090.1.
AL354710 Genomic DNA. Translation: CAQ08732.1.
CH471090 Genomic DNA. Translation: EAW87620.1.
BC020235 mRNA. Translation: AAH20235.1.
X59969 Genomic DNA. Translation: CAA42595.1.
AF188611 mRNA. Translation: AAF13605.1. Sequence problems.
PIRA29821.
RefSeqNP_005338.1. NM_005347.4.
UniGeneHs.743241.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IUCX-ray2.40A/C26-410[»]
3LDLX-ray2.30A/B26-407[»]
3LDNX-ray2.20A/B26-407[»]
3LDOX-ray1.95A/B26-407[»]
3LDPX-ray2.20A/B26-407[»]
ProteinModelPortalP11021.
SMRP11021. Positions 26-637.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109541. 245 interactions.
DIPDIP-33189N.
IntActP11021. 100 interactions.
MINTMINT-1135308.
STRING9606.ENSP00000324173.

Chemistry

BindingDBP11021.
ChEMBLCHEMBL1781865.
DrugBankDB00025. Antihemophilic Factor.

PTM databases

PhosphoSiteP11021.

Polymorphism databases

DMDM14916999.

2D gel databases

DOSAC-COBS-2DPAGEP11021.
OGPP11021.
REPRODUCTION-2DPAGEP11021.
SWISS-2DPAGEP11021.
UCD-2DPAGEP11021.

Proteomic databases

PaxDbP11021.
PRIDEP11021.

Protocols and materials databases

DNASU3309.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324460; ENSP00000324173; ENSG00000044574.
GeneID3309.
KEGGhsa:3309.
UCSCuc004bpn.3. human.

Organism-specific databases

CTD3309.
GeneCardsGC09M127997.
HGNCHGNC:5238. HSPA5.
HPACAB005221.
HPA038845.
HPA038846.
MIM138120. gene.
neXtProtNX_P11021.
PharmGKBPA29504.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0443.
HOGENOMHOG000228135.
HOVERGENHBG051845.
InParanoidP11021.
KOK09490.
OMADKRAVQK.
OrthoDBEOG780RKX.
PhylomeDBP11021.
TreeFamTF105044.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

BgeeP11021.
CleanExHS_HSPA5.
GenevestigatorP11021.

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSPA5. human.
EvolutionaryTraceP11021.
GeneWikiBinding_immunoglobulin_protein.
GenomeRNAi3309.
NextBio13123.
PROP11021.
SOURCESearch...

Entry information

Entry nameGRP78_HUMAN
AccessionPrimary (citable) accession number: P11021
Secondary accession number(s): B0QZ61 expand/collapse secondary AC list , Q2EF78, Q9NPF1, Q9UK02
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 11, 2001
Last modified: April 16, 2014
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM