78 kDa glucose-regulated protein precursor

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Reviewed, UniProtKB/Swiss-Prot P11021 (GRP78_HUMAN)

Last modified July 7, 2009. Version 113. History...

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

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Names and origin

Protein names

Recommended name:
    78 kDa glucose-regulated protein
Alternative name(s):
    GRP 78
    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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	654 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Ref.10
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.
Subcellular location	Endoplasmic reticulum lumen. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.14 Ref.15
Involvement in disease	Autoantigen in rheumatoid arthritis [MIM:180300]. Ref.8
Sequence similarities	Belongs to the heat shock protein 70 family.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	anti-apoptosis Inferred from mutant phenotype. Source: UniProtKB cellular response to glucose starvation Inferred from direct assay. Source: UniProtKB negative regulation of caspase activity Inferred from direct assay. Source: UniProtKB
Cellular component	ER-Golgi intermediate compartment Inferred from direct assay. Source: UniProtKB cell surface Inferred from direct assay. Source: UniProtKB endoplasmic reticulum lumen Traceable author statement. Source: UniProtKB integral to endoplasmic reticulum membrane Inferred from direct assay. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Non-traceable author statement. Source: UniProtKB calcium ion binding Traceable author statement. Source: UniProtKB caspase inhibitor activity Inferred from direct assay. Source: UniProtKB protein binding, bridging Non-traceable author statement. Source: UniProtKB unfolded protein binding Traceable author statement. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
EIF2AK3	Q9NZJ5	1	EBI-354921,EBI-766076
NDRG1	Q92597	1	EBI-354921,EBI-716486
PTEN	P60484	1	EBI-354921,EBI-696162
RAF1	P04049	3	EBI-354921,EBI-365996

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

Ref.10 Ref.11

Chain

19 – 654

636

78 kDa glucose-regulated protein

PRO_0000013566

Regions

Motif

651 – 654

Prevents secretion from ER

Amino acid modifications

Modified residue

166

Phosphothreonine By similarity

Modified residue

466

Phosphotyrosine Ref.16

Modified residue

571

Phosphoserine By similarity

Natural variations

Natural variant

543

N → H Ref.5

VAR_025815

Experimental info

Sequence conflict

297

Missing Ref.1

Sequence conflict

297

Missing Ref.2

Sequence conflict

418

D → H Ref.1

Sequence conflict

418

D → H Ref.2

Sequence conflict

439

R → S Ref.1

Sequence conflict

439

R → S Ref.2

Sequence conflict

447

K → N Ref.1

Sequence conflict

447

K → N Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P11021-1 [UniParc].

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

654

72,333

        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

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References

	« Hide 'large scale' referencesShow '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]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases
	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. BC020235 mRNA. Translation: AAH20235.1. X59969 Genomic DNA. Translation: CAA42595.1. AF188611 mRNA. Translation: AAF13605.1. Sequence problems.
IPI	IPI00003362.
PIR	A29821.
RefSeq	NP_005338.1.
UniGene	Hs.605502
3D structure databases
HSSP	HSSP built from PDB template 3HSC based on UniProtKB P19120.
SMR	P11021. Positions 28-576.
ModBase	Search...
Protein-protein interaction databases
IntAct	P11021. 48 interactions.
PTM databases
PhosphoSite	P11021.
2-D gel databases
SWISS-2DPAGE	P11021.
DOSAC-COBS-2DPAGE	P11021.
OGP	P11021.
PHCI-2DPAGE	P11021.
PMMA-2DPAGE	P11021.
REPRODUCTION-2DPAGE	P11021.
Siena-2DPAGE	P11021.
Proteomic databases
PRIDE	P11021.
Genome annotation databases
Ensembl	ENSG00000044574. Homo sapiens. [Contig view]
GeneID	3309.
KEGG	hsa:3309.
UCSC	uc004bpn.1. human.
Organism-specific databases
GeneCards	GC09M127036.
H-InvDB	HIX0008382.
HGNC	HGNC:5238. HSPA5.
HPA	CAB005221.
MIM	138120. gene. 180300. phenotype.
PharmGKB	PA29504.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P11021.
OMA	P11021. FEGERPM.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P11021.
Bgee	P11021.
CleanEx	HS_HSPA5.
GermOnline	ENSG00000044574. Homo sapiens.
Family and domain databases
InterPro	IPR000886. ER_targeting_sequence. IPR018181. Heat_shock_70_CS. IPR001023. Hsp70. IPR013126. Hsp_70. [Graphical view]
PANTHER	PTHR19375. Hsp70. 1 hit.
Pfam	PF00012. HSP70. 1 hit. [Graphical view]
PRINTS	PR00301. HEATSHOCK70.
ProDom	PD000089. Hsp70. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00014. ER_TARGET. 1 hit. PS00297. HSP70_1. 1 hit. PS00329. HSP70_2. 1 hit. PS01036. HSP70_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00025. Antihemophilic Factor.
NextBio	13123.
SOURCE	Search...

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Entry information

Entry name

GRP78_HUMAN

Accession

Primary (citable) accession number: P11021
Secondary accession number(s): Q2EF78, Q9NPF1, Q9UK02

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 11, 2001
Last modified:	July 7, 2009
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents