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P06761

- GRP78_RAT

UniProt

P06761 - GRP78_RAT

Protein

78 kDa glucose-regulated protein

Gene

Hspa5

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      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 By similarity.By similarity

    Sites

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

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. misfolded protein binding Source: MGI
    3. protein binding Source: IntAct
    4. ribosome binding Source: Ensembl
    5. unfolded protein binding Source: RGD

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Ensembl
    2. cellular response to antibiotic Source: RGD
    3. cellular response to glucose starvation Source: Ensembl
    4. cellular response to interleukin-4 Source: Ensembl
    5. cerebellar Purkinje cell layer development Source: Ensembl
    6. cerebellum structural organization Source: Ensembl
    7. ER overload response Source: Ensembl
    8. maintenance of protein localization in endoplasmic reticulum Source: UniProtKB
    9. negative regulation of apoptotic process Source: Ensembl
    10. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
    11. positive regulation of cell migration Source: UniProtKB
    12. positive regulation of protein ubiquitination Source: Ensembl
    13. proteolysis involved in cellular protein catabolic process Source: Ensembl
    14. response to endoplasmic reticulum stress Source: MGI

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_100458. ATF6-alpha activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended 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
    Steroidogenesis-activator polypeptide
    Gene namesi
    Name:Hspa5
    Synonyms:Grp78
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi2843. Hspa5.

    Subcellular locationi

    Endoplasmic reticulum lumen. Melanosome By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. COP9 signalosome Source: Ensembl
    3. endoplasmic reticulum Source: MGI
    4. endoplasmic reticulum chaperone complex Source: Ensembl
    5. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
    6. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    7. integral component of endoplasmic reticulum membrane Source: Ensembl
    8. melanosome Source: UniProtKB-SubCell
    9. membrane Source: MGI
    10. midbody Source: Ensembl
    11. mitochondrion Source: RGD
    12. smooth endoplasmic reticulum Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818By similarityAdd
    BLAST
    Chaini19 – 65463678 kDa glucose-regulated proteinPRO_0000013569Add
    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 – 5181PhosphothreonineBy similarity
    Modified residuei585 – 5851N6,N6,N6-trimethyllysine; by METTL21A; in vitroBy similarity
    Modified residuei649 – 6491PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Methylation, Nitration, Phosphoprotein

    Proteomic databases

    PaxDbiP06761.
    PRIDEiP06761.

    PTM databases

    PhosphoSiteiP06761.

    Expressioni

    Gene expression databases

    GenevestigatoriP06761.

    Interactioni

    Subunit structurei

    May form a complex with ERLEC1, OS9, SEL1L and SYVN1 By similarity. Interacts with DNAJC1 (via J domain). Interacts with TRIM21 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. Interacts with MX1. Interacts with METTL23 and DNAJC10. Interacts with CEMIP; the interaction induces calcium leakage from the endoplamic reticulum and cell migration By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Sigmar1Q9R0C93EBI-916036,EBI-1557826
    TgP068826EBI-916036,EBI-1549657

    Protein-protein interaction databases

    BioGridi247646. 8 interactions.
    IntActiP06761. 16 interactions.
    MINTiMINT-4575479.
    STRINGi10116.ENSRNOP00000025064.

    Structurei

    3D structure databases

    ProteinModelPortaliP06761.
    SMRiP06761. Positions 28-570.
    ModBaseiSearch...
    MobiDBiSearch...

    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.
    GeneTreeiENSGT00750000117237.
    HOGENOMiHOG000228135.
    HOVERGENiHBG051845.
    InParanoidiP06761.
    KOiK09490.
    OMAiDKRAVQK.
    OrthoDBiEOG780RKX.
    PhylomeDBiP06761.
    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.

    P06761-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFTVVAAAL LLLCAVRAEE 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 SFFEGEDFSE 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 KLGGKLSPED KETMEKAVEE 600
    KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSGGP PPTGEEDTSE 650
    KDEL 654
    Length:654
    Mass (Da):72,347
    Last modified:April 1, 1988 - v1
    Checksum:i9D686C6484150108
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 291T → M in AAA41277. (PubMed:3468506)Curated
    Sequence conflicti649 – 6491S → D AA sequence (PubMed:3563495)Curated
    Sequence conflicti651 – 6511K → KK AA sequence (PubMed:3563495)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14050 mRNA. Translation: AAA40817.1.
    BC062017 mRNA. Translation: AAH62017.1.
    M14866 Genomic DNA. Translation: AAA41277.1.
    PIRiA23948. HHRTGB.
    RefSeqiNP_037215.1. NM_013083.2.
    UniGeneiRn.11088.

    Genome annotation databases

    EnsembliENSRNOT00000025067; ENSRNOP00000025064; ENSRNOG00000018294.
    GeneIDi25617.
    KEGGirno:25617.
    UCSCiRGD:2843. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14050 mRNA. Translation: AAA40817.1 .
    BC062017 mRNA. Translation: AAH62017.1 .
    M14866 Genomic DNA. Translation: AAA41277.1 .
    PIRi A23948. HHRTGB.
    RefSeqi NP_037215.1. NM_013083.2.
    UniGenei Rn.11088.

    3D structure databases

    ProteinModelPortali P06761.
    SMRi P06761. Positions 28-570.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247646. 8 interactions.
    IntActi P06761. 16 interactions.
    MINTi MINT-4575479.
    STRINGi 10116.ENSRNOP00000025064.

    PTM databases

    PhosphoSitei P06761.

    Proteomic databases

    PaxDbi P06761.
    PRIDEi P06761.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000025067 ; ENSRNOP00000025064 ; ENSRNOG00000018294 .
    GeneIDi 25617.
    KEGGi rno:25617.
    UCSCi RGD:2843. rat.

    Organism-specific databases

    CTDi 3309.
    RGDi 2843. Hspa5.

    Phylogenomic databases

    eggNOGi COG0443.
    GeneTreei ENSGT00750000117237.
    HOGENOMi HOG000228135.
    HOVERGENi HBG051845.
    InParanoidi P06761.
    KOi K09490.
    OMAi DKRAVQK.
    OrthoDBi EOG780RKX.
    PhylomeDBi P06761.
    TreeFami TF105044.

    Enzyme and pathway databases

    Reactomei REACT_100458. ATF6-alpha activates chaperone genes.

    Miscellaneous databases

    NextBioi 607375.
    PROi P06761.

    Gene expression databases

    Genevestigatori P06761.

    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. "An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein."
      Munro S., Pelham H.R.B.
      Cell 46:291-300(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Prostate.
    3. "Rat gene encoding the 78-kDa glucose-regulated protein GRP78: its regulatory sequences and the effect of protein glycosylation on its expression."
      Chang S.C., Wooden S.K., Nakaki T., Kim Y.K., Lin A.Y., Kung L., Attenello J.W., Lee A.S.
      Proc. Natl. Acad. Sci. U.S.A. 84:680-684(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
    4. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 50-60; 165-181; 307-324; 475-492 AND 533-540, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain, Hippocampus and Spinal cord.
    5. "Steroidogenesis-activator polypeptide isolated from a rat Leydig cell tumor."
      Pedersen R.C., Brownie A.C.
      Science 236:188-190(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 626-654.
    6. "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.
    7. "Cloning and characterization of a novel GRP78-binding protein in the rat brain."
      Oh-hashi K., Naruse Y., Amaya F., Shimosato G., Tanaka M.
      J. Biol. Chem. 278:10531-10537(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMEM132A.
      Strain: Sprague-Dawley.

    Entry informationi

    Entry nameiGRP78_RAT
    AccessioniPrimary (citable) accession number: P06761
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3