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P11021

- GRP78_HUMAN

UniProt

P11021 - GRP78_HUMAN

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
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 2 (11 Jul 2001)
      Previous versions | rss
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    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 binding Source: UniProtKB
    9. protein domain specific binding Source: UniProtKB
    10. ribosome binding Source: Ensembl
    11. ubiquitin protein ligase binding Source: UniProtKB
    12. 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

    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. integral component of endoplasmic reticulum membrane Source: BHF-UCL
    9. melanosome Source: UniProtKB-SubCell
    10. membrane Source: UniProtKB
    11. midbody Source: UniProtKB
    12. nucleus Source: UniProtKB

    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.
    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. 221 interactions.
    DIPiDIP-33189N.
    IntActiP11021. 101 interactions.
    MINTiMINT-1135308.
    STRINGi9606.ENSP00000324173.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 26-637.
    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

    MKLSLVAAML LLLSAARAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV    50
    EIIANDQGNR ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG 100
    RTWNDPSVQQ DIKFLPFKVV EKKTKPYIQV DIGGGQTKTF APEEISAMVL 150
    TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ RQATKDAGTI AGLNVMRIIN 200
    EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG VFEVVATNGD 250
    THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS 300
    SQHQARIEIE SFYEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD 350
    LKKSDIDEIV LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV 400
    QAGVLSGDQD TGDLVLLDVC PLTLGIETVG GVMTKLIPRN TVVPTKKSQI 450
    FSTASDNQPT VTIKVYEGER PLTKDNHLLG TFDLTGIPPA PRGVPQIEVT 500
    FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER MVNDAEKFAE 550
    EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSSED KETMEKAVEE 600
    KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSAGP PPTGEEDTAE 650
    KDEL 654
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 26-637.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109541. 221 interactions.
    DIPi DIP-33189N.
    IntActi P11021. 101 interactions.
    MINTi MINT-1135308.
    STRINGi 9606.ENSP00000324173.

    Chemistry

    BindingDBi P11021.
    ChEMBLi CHEMBL1781865.
    DrugBanki 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.
    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

    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: October 1, 2014
    This is version 172 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