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Reviewed, UniProtKB/Swiss-Prot P11021 (GRP78_HUMAN)

Last modified February 9, 2010. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    78 kDa glucose-regulated protein
      Short name=GRP-78
Alternative name(s):
    Heat shock 70 kDa protein 5
    Immunoglobulin heavy chain-binding protein
      Short name=BiP
    Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78
Gene names
Name: HSPA5
Synonyms: GRP78
OrganismHomo sapiens (Human) [Complete 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 ER. Ref.12

Subunit structure

Interacts with DNAJC1 (via J domain) By similarity. Component of an EIF2 complex at least composed of CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Part a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with TMEM132A. May form a complex with ERLEC1, OS9, SEL1L and SYVN1. Ref.20 Ref.21

Subcellular location

Endoplasmic reticulum lumen. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.16 Ref.17

Involvement in disease

Autoantigen in rheumatoid arthritis [MIM:180300]. Ref.10

Sequence similarities

Belongs to the heat shock protein 70 family.

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

Motif651 – 6544Prevents secretion from ER

Amino acid modifications

Modified residue1661Phosphothreonine By similarity
Modified residue2681N6-acetyllysine Ref.22
Modified residue4661Phosphotyrosine Ref.18
Modified residue5711Phosphoserine By similarity

Natural variations

Natural variant5431N → H: dbSNP rs35356639. Ref.5
VAR_025815

Experimental info

Sequence conflict2971Missing Ref.1
Sequence conflict2971Missing Ref.2
Sequence conflict4181D → H Ref.1
Sequence conflict4181D → H Ref.2
Sequence conflict4391R → S Ref.1
Sequence conflict4391R → S Ref.2
Sequence conflict4471K → N Ref.1
Sequence conflict4471K → N Ref.2

Sequences

Sequence LengthMass (Da)Tools
P11021-1 [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: 2840249] [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: 15164053] [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: 15489334] [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: 1480470] [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: 11160188] [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: 9150946] [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: 2294010] [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: 9150948] [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, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[15]"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: 12475965] [Abstract]
Cited for: COMPONENT OF A CHAPERONE COMPLEX.
[16]"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: 12643545] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]"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: 17081065] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[18]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-466, MASS SPECTROMETRY.
[19]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]"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: 18502753] [Abstract]
Cited for: INTERACTION WITH ERLEC1; OS9; SEL1L AND SYVN1.
[21]"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: 18264092] [Abstract]
Cited for: INTERACTION WITH ERLEC1; OS9; SEL1L AND SYVN1.
[22]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-268, MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

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.
IPIIPI00003362.
PIRA29821.
RefSeqNP_005338.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IUCX-ray2.40A/C26-410[»]
SMRP11021. Positions 28-570, 417-641.
ModBaseSearch...

Protein-protein interaction databases

IntActP11021. 56 interactions.
STRINGP11021.

PTM databases

PhosphoSiteP11021.

2-D gel databases

SWISS-2DPAGEP11021.
DOSAC-COBS-2DPAGEP11021.
OGPP11021.
PHCI-2DPAGEP11021.
PMMA-2DPAGEP11021.
REPRODUCTION-2DPAGEP11021.
Siena-2DPAGEP11021.

Proteomic databases

PRIDEP11021.

Genome annotation databases

EnsemblENST00000324460; ENSP00000324173; ENSG00000044574; Homo sapiens. [Genome view]
GeneID3309.
KEGGhsa:3309.
UCSCuc004bpn.1. human.

Organism-specific databases

CTD3309.
GeneCardsGC09M127036.
H-InvDBHIX0008382.
HGNCHGNC:5238. HSPA5.
HPACAB005221.
CAB019420.
MIM138120. gene.
180300. phenotype.
PharmGKBPA29504.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG14855.
HOVERGENP11021.
InParanoidP11021.
OMAKNSKPHI.
OrthoDBEOG9X6FTN.
PhylomeDBP11021.

Enzyme and pathway databases

ReactomeREACT_15380. Diabetes pathways.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP11021.
BgeeP11021.
CleanExHS_HSPA5.
GenevestigatorP11021.
GermOnlineENSG00000044574. Homo sapiens.

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR001023. Hsp70.
IPR013126. Hsp_70.
[Graphical view]
PANTHERPTHR19375. Hsp70. 1 hit.
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 Resources

DrugBankDB00025. Antihemophilic Factor.
NextBio13123.
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: February 9, 2010
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 9

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents