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P11021

- GRP78_HUMAN

UniProt

P11021 - GRP78_HUMAN

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Protein

78 kDa glucose-regulated protein

Gene

HSPA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei96 – 961ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 394ATP
Nucleotide bindingi227 – 2293ATP
Nucleotide bindingi293 – 3008ATP
Nucleotide bindingi364 – 3674ATP

GO - Molecular functioni

  1. ATPase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. calcium ion binding Source: UniProtKB
  4. chaperone binding Source: BHF-UCL
  5. enzyme binding Source: BHF-UCL
  6. glycoprotein binding Source: UniProt
  7. misfolded protein binding Source: UniProtKB
  8. protein domain specific binding Source: UniProtKB
  9. ribosome binding Source: Ensembl
  10. ubiquitin protein ligase binding Source: UniProtKB
  11. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. ATP catabolic process Source: GOC
  3. blood coagulation Source: Reactome
  4. cellular protein metabolic process Source: Reactome
  5. cellular response to antibiotic Source: Ensembl
  6. cellular response to glucose starvation Source: UniProtKB
  7. cellular response to interleukin-4 Source: Ensembl
  8. cerebellar Purkinje cell layer development Source: Ensembl
  9. cerebellum structural organization Source: Ensembl
  10. endoplasmic reticulum unfolded protein response Source: BHF-UCL
  11. ER-associated ubiquitin-dependent protein catabolic process Source: BHF-UCL
  12. ER overload response Source: Ensembl
  13. maintenance of protein localization in endoplasmic reticulum Source: UniProtKB
  14. negative regulation of apoptotic process Source: UniProtKB
  15. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  16. platelet activation Source: Reactome
  17. platelet degranulation Source: Reactome
  18. positive regulation of cell migration Source: UniProtKB
  19. positive regulation of protein ubiquitination Source: Ensembl
  20. regulation of protein folding in endoplasmic reticulum Source: BHF-UCL
  21. substantia nigra development Source: UniProt
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_18277. PERK regulates gene expression.
REACT_18348. ATF6-alpha activates chaperones.
REACT_18368. IRE1alpha activates chaperones.
REACT_18423. ATF6-alpha activates chaperone genes.
REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:HSPA5
Synonyms:GRP78
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:5238. HSPA5.

Subcellular locationi

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

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. endoplasmic reticulum Source: UniProtKB
  3. endoplasmic reticulum chaperone complex Source: UniProtKB
  4. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  5. endoplasmic reticulum lumen Source: Reactome
  6. endoplasmic reticulum membrane Source: Reactome
  7. extracellular vesicular exosome Source: UniProt
  8. focal adhesion Source: UniProtKB
  9. integral component of endoplasmic reticulum membrane Source: BHF-UCL
  10. membrane Source: UniProtKB
  11. midbody Source: UniProtKB
  12. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Autoantigen in rheumatoid arthritis.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi585 – 5851K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications

Organism-specific databases

PharmGKBiPA29504.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18182 PublicationsAdd
BLAST
Chaini19 – 65463678 kDa glucose-regulated proteinPRO_0000013566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251N6-acetyllysineBy similarity
Modified residuei160 – 1601Nitrated tyrosineBy similarity
Modified residuei213 – 2131N6-acetyllysineBy similarity
Modified residuei326 – 3261N6-acetyllysineBy similarity
Modified residuei353 – 3531N6-acetyllysineBy similarity
Modified residuei447 – 4471N6-succinyllysineBy similarity
Modified residuei518 – 5181Phosphothreonine1 Publication
Modified residuei585 – 5851N6,N6,N6-trimethyllysine; by METTL21A; in vitro2 Publications

Keywords - PTMi

Acetylation, Methylation, Nitration, Phosphoprotein

Proteomic databases

MaxQBiP11021.
PaxDbiP11021.
PRIDEiP11021.

2D gel databases

DOSAC-COBS-2DPAGEP11021.
OGPiP11021.
REPRODUCTION-2DPAGEP11021.
SWISS-2DPAGEP11021.
UCD-2DPAGEP11021.

PTM databases

PhosphoSiteiP11021.

Expressioni

Gene expression databases

BgeeiP11021.
CleanExiHS_HSPA5.
ExpressionAtlasiP11021. baseline and differential.
GenevestigatoriP11021.

Organism-specific databases

HPAiCAB005221.
HPA038845.
HPA038846.

Interactioni

Subunit structurei

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.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q6T4243EBI-354921,EBI-7888150
AKT1P317492EBI-354921,EBI-296087
DMKNQ6E0U43EBI-354921,EBI-7943171
DNAJB11Q9UBS42EBI-354921,EBI-713113
Dnajc3Q91YW32EBI-354921,EBI-8381770From a different organism.
PAWRQ96IZ08EBI-354921,EBI-595869
PawrQ626274EBI-354921,EBI-1187240From a different organism.
RAF1P040494EBI-354921,EBI-365996
SEC61A1P616193EBI-354921,EBI-358919

Protein-protein interaction databases

BioGridi109541. 271 interactions.
DIPiDIP-33189N.
IntActiP11021. 103 interactions.
MINTiMINT-1135308.
STRINGi9606.ENSP00000324173.

Structurei

Secondary structure

1
654
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 344Combined sources
Beta strandi37 – 4610Combined sources
Beta strandi49 – 524Combined sources
Beta strandi60 – 634Combined sources
Beta strandi66 – 683Combined sources
Beta strandi74 – 763Combined sources
Helixi78 – 825Combined sources
Helixi84 – 863Combined sources
Helixi88 – 903Combined sources
Beta strandi91 – 933Combined sources
Helixi95 – 973Combined sources
Turni98 – 1003Combined sources
Helixi106 – 1149Combined sources
Beta strandi116 – 1227Combined sources
Beta strandi125 – 1317Combined sources
Beta strandi137 – 1404Combined sources
Helixi142 – 16120Combined sources
Beta strandi167 – 1726Combined sources
Helixi178 – 19013Combined sources
Beta strandi194 – 2007Combined sources
Helixi201 – 2088Combined sources
Helixi211 – 2133Combined sources
Beta strandi215 – 22511Combined sources
Beta strandi230 – 2389Combined sources
Beta strandi241 – 25010Combined sources
Helixi255 – 27319Combined sources
Helixi278 – 2803Combined sources
Helixi282 – 29817Combined sources
Turni299 – 3013Combined sources
Beta strandi302 – 31312Combined sources
Beta strandi316 – 3238Combined sources
Helixi324 – 33613Combined sources
Helixi339 – 34810Combined sources
Helixi353 – 3553Combined sources
Beta strandi358 – 3636Combined sources
Helixi364 – 3674Combined sources
Helixi369 – 37810Combined sources
Turni379 – 3813Combined sources
Turni390 – 3923Combined sources
Helixi393 – 40614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP11021.
SMRiP11021. Positions 26-635.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11021.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi651 – 6544Prevents secretion from ER

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0443.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP11021.
KOiK09490.
OMAiDKRAVQK.
OrthoDBiEOG780RKX.
PhylomeDBiP11021.
TreeFamiTF105044.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11021-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLSLVAAML LLLSAARAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV
60 70 80 90 100
EIIANDQGNR ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG
110 120 130 140 150
RTWNDPSVQQ DIKFLPFKVV EKKTKPYIQV DIGGGQTKTF APEEISAMVL
160 170 180 190 200
TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ RQATKDAGTI AGLNVMRIIN
210 220 230 240 250
EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG VFEVVATNGD
260 270 280 290 300
THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS
310 320 330 340 350
SQHQARIEIE SFYEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD
360 370 380 390 400
LKKSDIDEIV LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV
410 420 430 440 450
QAGVLSGDQD TGDLVLLDVC PLTLGIETVG GVMTKLIPRN TVVPTKKSQI
460 470 480 490 500
FSTASDNQPT VTIKVYEGER PLTKDNHLLG TFDLTGIPPA PRGVPQIEVT
510 520 530 540 550
FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER MVNDAEKFAE
560 570 580 590 600
EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSSED KETMEKAVEE
610 620 630 640 650
KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSAGP PPTGEEDTAE

KDEL
Length:654
Mass (Da):72,333
Last modified:July 11, 2001 - v2
Checksum:i59B7D8D85BC32A00
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti297 – 2971Missing in AAA52614. (PubMed:2840249)Curated
Sequence conflicti297 – 2971Missing in CAA61201. 1 PublicationCurated
Sequence conflicti418 – 4181D → H in AAA52614. (PubMed:2840249)Curated
Sequence conflicti418 – 4181D → H in CAA61201. 1 PublicationCurated
Sequence conflicti439 – 4391R → S in AAA52614. (PubMed:2840249)Curated
Sequence conflicti439 – 4391R → S in CAA61201. 1 PublicationCurated
Sequence conflicti447 – 4471K → N in AAA52614. (PubMed:2840249)Curated
Sequence conflicti447 – 4471K → N in CAA61201. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti543 – 5431N → H.1 Publication
Corresponds to variant rs35356639 [ dbSNP | Ensembl ].
VAR_025815

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6863.1.
PIRiA29821.
RefSeqiNP_005338.1. NM_005347.4.
UniGeneiHs.743241.

Genome annotation databases

EnsembliENST00000324460; ENSP00000324173; ENSG00000044574.
GeneIDi3309.
KEGGihsa:3309.
UCSCiuc004bpn.3. human.

Polymorphism databases

DMDMi14916999.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS6863.1.
PIRi A29821.
RefSeqi NP_005338.1. NM_005347.4.
UniGenei Hs.743241.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IUC X-ray 2.40 A/C 26-410 [» ]
3LDL X-ray 2.30 A/B 26-407 [» ]
3LDN X-ray 2.20 A/B 26-407 [» ]
3LDO X-ray 1.95 A/B 26-407 [» ]
3LDP X-ray 2.20 A/B 26-407 [» ]
ProteinModelPortali P11021.
SMRi P11021. Positions 26-635.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109541. 271 interactions.
DIPi DIP-33189N.
IntActi P11021. 103 interactions.
MINTi MINT-1135308.
STRINGi 9606.ENSP00000324173.

Chemistry

ChEMBLi CHEMBL1781865.
DrugBanki DB00945. Acetylsalicylic acid.
DB00025. Antihemophilic Factor.

PTM databases

PhosphoSitei P11021.

Polymorphism databases

DMDMi 14916999.

2D gel databases

DOSAC-COBS-2DPAGE P11021.
OGPi P11021.
REPRODUCTION-2DPAGE P11021.
SWISS-2DPAGE P11021.
UCD-2DPAGE P11021.

Proteomic databases

MaxQBi P11021.
PaxDbi P11021.
PRIDEi P11021.

Protocols and materials databases

DNASUi 3309.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000324460 ; ENSP00000324173 ; ENSG00000044574 .
GeneIDi 3309.
KEGGi hsa:3309.
UCSCi uc004bpn.3. human.

Organism-specific databases

CTDi 3309.
GeneCardsi GC09M127997.
HGNCi HGNC:5238. HSPA5.
HPAi CAB005221.
HPA038845.
HPA038846.
MIMi 138120. gene.
neXtProti NX_P11021.
PharmGKBi PA29504.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0443.
HOGENOMi HOG000228135.
HOVERGENi HBG051845.
InParanoidi P11021.
KOi K09490.
OMAi DKRAVQK.
OrthoDBi EOG780RKX.
PhylomeDBi P11021.
TreeFami TF105044.

Enzyme and pathway databases

Reactomei REACT_18277. PERK regulates gene expression.
REACT_18348. ATF6-alpha activates chaperones.
REACT_18368. IRE1alpha activates chaperones.
REACT_18423. ATF6-alpha activates chaperone genes.
REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSi HSPA5. human.
EvolutionaryTracei P11021.
GeneWikii Binding_immunoglobulin_protein.
GenomeRNAii 3309.
NextBioi 13123.
PROi P11021.
SOURCEi Search...

Gene expression databases

Bgeei P11021.
CleanExi HS_HSPA5.
ExpressionAtlasi P11021. baseline and differential.
Genevestigatori P11021.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  20. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 26-407 IN COMPLEXES WITH ATP ANALOG.

Entry informationi

Entry nameiGRP78_HUMAN
AccessioniPrimary (citable) accession number: P11021
Secondary accession number(s): B0QZ61
, Q2EF78, Q9NPF1, Q9UK02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 11, 2001
Last modified: November 26, 2014
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3