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P08113

- ENPL_MOUSE

UniProt

P08113 - ENPL_MOUSE

Protein

Endoplasmin

Gene

Hsp90b1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei107 – 1071ATPBy similarity
    Binding sitei149 – 1491ATPBy similarity
    Binding sitei162 – 1621ATPBy similarity
    Binding sitei168 – 1681ATPBy similarity
    Binding sitei199 – 1991ATP; via amide nitrogenBy similarity
    Binding sitei448 – 4481ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. low-density lipoprotein particle receptor binding Source: MGI
    3. protein binding Source: UniProtKB
    4. protein phosphatase binding Source: MGI
    5. RNA binding Source: Ensembl
    6. virion binding Source: Ensembl

    GO - Biological processi

    1. actin rod assembly Source: MGI
    2. cellular response to ATP Source: MGI
    3. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
    4. negative regulation of apoptotic process Source: Ensembl
    5. protein folding Source: InterPro
    6. regulation of phosphoprotein phosphatase activity Source: MGI
    7. response to hypoxia Source: Ensembl

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    ATP-binding, Calcium, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196581. Scavenging by Class A Receptors.
    REACT_198976. Trafficking and processing of endosomal TLR.
    REACT_32838. ATF6-alpha activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoplasmin
    Alternative name(s):
    94 kDa glucose-regulated protein
    Short name:
    GRP-94
    Endoplasmic reticulum resident protein 99
    Short name:
    ERp99
    Heat shock protein 90 kDa beta member 1
    Polymorphic tumor rejection antigen 1
    Tumor rejection antigen gp96
    Gene namesi
    Name:Hsp90b1
    Synonyms:Grp94, Tra-1, Tra1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:98817. Hsp90b1.

    Subcellular locationi

    Endoplasmic reticulum lumen 1 Publication. Melanosome By similarity

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. endoplasmic reticulum Source: MGI
    3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    4. endoplasmic reticulum membrane Source: Ensembl
    5. extracellular region Source: Reactome
    6. melanosome Source: UniProtKB-SubCell
    7. midbody Source: Ensembl
    8. perinuclear region of cytoplasm Source: Ensembl
    9. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi103 – 1031E → A: Loss of CNPY3-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 802781EndoplasminPRO_0000013599Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi138 – 138Interchain
    Glycosylationi217 – 2171N-linked (GlcNAc...)1 Publication
    Modified residuei306 – 3061PhosphoserineBy similarity
    Modified residuei404 – 4041N6-succinyllysine1 Publication
    Glycosylationi445 – 4451N-linked (GlcNAc...)Sequence Analysis
    Modified residuei479 – 4791N6-acetyllysine1 Publication
    Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence Analysis
    Modified residuei633 – 6331N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP08113.
    PaxDbiP08113.
    PRIDEiP08113.

    2D gel databases

    REPRODUCTION-2DPAGEP08113.
    SWISS-2DPAGEP08113.

    PTM databases

    PhosphoSiteiP08113.

    Miscellaneous databases

    PMAP-CutDBP08113.

    Expressioni

    Gene expression databases

    ArrayExpressiP08113.
    BgeeiP08113.
    CleanExiMM_HSP90B1.
    GenevestigatoriP08113.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. 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 OS9 By similarity. Interacts with AIMP1; regulates its retention in the endoplasmic reticulum. Interacts with CNPY3; this interaction is disrupted in the presence of ATP. Interacts with TLR4, TLR9 and TLR11, but not with TLR3. Interacts with MZB1 in a calcium-dependent manner. Interacts with METTL23 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi204301. 8 interactions.
    DIPiDIP-32352N.
    IntActiP08113. 11 interactions.
    MINTiMINT-1863762.

    Structurei

    3D structure databases

    ProteinModelPortaliP08113.
    SMRiP08113. Positions 72-755.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi799 – 8024Prevents secretion from ER

    Sequence similaritiesi

    Belongs to the heat shock protein 90 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0326.
    HOGENOMiHOG000031988.
    HOVERGENiHBG007374.
    InParanoidiP08113.
    KOiK09487.
    OMAiQSSHHPS.
    OrthoDBiEOG780RM0.
    PhylomeDBiP08113.
    TreeFamiTF105969.

    Family and domain databases

    Gene3Di3.30.565.10. 2 hits.
    HAMAPiMF_00505. HSP90.
    InterProiIPR003594. HATPase_ATP-bd.
    IPR019805. Heat_shock_protein_90_CS.
    IPR001404. Hsp90_fam.
    IPR020575. Hsp90_N.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view]
    PANTHERiPTHR11528. PTHR11528. 1 hit.
    PfamiPF00183. HSP90. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002583. Hsp90. 1 hit.
    PRINTSiPR00775. HEATSHOCK90.
    SMARTiSM00387. HATPase_c. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 2 hits.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00298. HSP90. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P08113-1 [UniParc]FASTAAdd to Basket

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    MRVLWVLGLC CVLLTFGFVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ    50
    REEEAIQLDG LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF 100
    LRELISNASD ALDKIRLISL TDENALAGNE ELTVKIKCDK EKNLLHVTDT 150
    GVGMTREELV KNLGTIAKSG TSEFLNKMTE AQEDGQSTSE LIGQFGVGFY 200
    SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT LGRGTTITLV 250
    LKEEASDYLE LDTIKNLVRK YSQFINFPIY VWSSKTETVE EPLEEDEAAK 300
    EEKEESDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV 350
    EEDEYKAFYK SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE 400
    YGSKKSDYIK LYVRRVFITD DFHDMMPKYL NFVKGVVDSD DLPLNVSRET 450
    LQQHKLLKVI RKKLVRKTLD MIKKIADEKY NDTFWKEFGT NIKLGVIEDH 500
    SNRTRLAKLL RFQSSHHSTD ITSLDQYVER MKEKQDKIYF MAGSSRKEAE 550
    SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE 600
    SEKTKESREA TEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS 650
    QYGWSGNMER IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR 700
    IKEDEDDKTV MDLAVVLFET ATLRSGYLLP DTKAYGDRIE RMLRLSLNID 750
    PEAQVEEEPE EEPEDTSEDA EDSEQDEGEE MDAGTEEEEE ETEKESTEKD 800
    EL 802
    Length:802
    Mass (Da):92,476
    Last modified:April 1, 1990 - v2
    Checksum:iBDF33B9BD86BFC5F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03297 mRNA. Translation: AAA37573.1.
    M29652 mRNA. Translation: AAA37743.1.
    M16370 mRNA. Translation: AAA40023.1.
    CCDSiCCDS36019.1.
    PIRiA29317.
    RefSeqiNP_035761.1. NM_011631.1.
    UniGeneiMm.87773.

    Genome annotation databases

    EnsembliENSMUST00000020238; ENSMUSP00000020238; ENSMUSG00000020048.
    GeneIDi22027.
    KEGGimmu:22027.
    UCSCiuc007gqi.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03297 mRNA. Translation: AAA37573.1 .
    M29652 mRNA. Translation: AAA37743.1 .
    M16370 mRNA. Translation: AAA40023.1 .
    CCDSi CCDS36019.1.
    PIRi A29317.
    RefSeqi NP_035761.1. NM_011631.1.
    UniGenei Mm.87773.

    3D structure databases

    ProteinModelPortali P08113.
    SMRi P08113. Positions 72-755.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204301. 8 interactions.
    DIPi DIP-32352N.
    IntActi P08113. 11 interactions.
    MINTi MINT-1863762.

    PTM databases

    PhosphoSitei P08113.

    2D gel databases

    REPRODUCTION-2DPAGE P08113.
    SWISS-2DPAGE P08113.

    Proteomic databases

    MaxQBi P08113.
    PaxDbi P08113.
    PRIDEi P08113.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020238 ; ENSMUSP00000020238 ; ENSMUSG00000020048 .
    GeneIDi 22027.
    KEGGi mmu:22027.
    UCSCi uc007gqi.1. mouse.

    Organism-specific databases

    CTDi 7184.
    MGIi MGI:98817. Hsp90b1.

    Phylogenomic databases

    eggNOGi COG0326.
    HOGENOMi HOG000031988.
    HOVERGENi HBG007374.
    InParanoidi P08113.
    KOi K09487.
    OMAi QSSHHPS.
    OrthoDBi EOG780RM0.
    PhylomeDBi P08113.
    TreeFami TF105969.

    Enzyme and pathway databases

    Reactomei REACT_196581. Scavenging by Class A Receptors.
    REACT_198976. Trafficking and processing of endosomal TLR.
    REACT_32838. ATF6-alpha activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi HSP90B1. mouse.
    NextBioi 301772.
    PMAP-CutDB P08113.
    PROi P08113.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08113.
    Bgeei P08113.
    CleanExi MM_HSP90B1.
    Genevestigatori P08113.

    Family and domain databases

    Gene3Di 3.30.565.10. 2 hits.
    HAMAPi MF_00505. HSP90.
    InterProi IPR003594. HATPase_ATP-bd.
    IPR019805. Heat_shock_protein_90_CS.
    IPR001404. Hsp90_fam.
    IPR020575. Hsp90_N.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view ]
    PANTHERi PTHR11528. PTHR11528. 1 hit.
    Pfami PF00183. HSP90. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002583. Hsp90. 1 hit.
    PRINTSi PR00775. HEATSHOCK90.
    SMARTi SM00387. HATPase_c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 2 hits.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00298. HSP90. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94)."
      Mazzarella R.A., Green M.
      J. Biol. Chem. 262:8875-8883(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 76-84; 88-95; 117-135; 143-156; 244-265; 270-285; 385-404; 416-428; 435-448; 512-530; 609-623 AND 640-660, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    3. "Isolation and identification of partial cDNA clones for endoplasmin, the major glycoprotein of mammalian endoplasmic reticulum."
      Smith M.J., Koch G.L.E.
      J. Mol. Biol. 194:345-347(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 378-507.
    4. "5'-structural analysis of genes encoding polymorphic antigens of chemically induced tumors."
      Srivastava P.K., Chen Y.-T., Old L.J.
      Proc. Natl. Acad. Sci. U.S.A. 84:3807-3811(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-88.
    5. "HSP100, a 100-kDa heat shock protein, is a Ca2+-calmodulin-regulated actin-binding protein."
      Koyasu S., Nishida E., Miyata Y., Sakai H., Yahara I.
      J. Biol. Chem. 264:15083-15087(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 271-284; 328-339 AND 633-659.
    6. "Analysis of the structure and synthesis of GRP94, an abundant stress protein of the endoplasmic reticulum."
      Qu D., Mazzarella R.A., Green M.
      DNA Cell Biol. 13:117-124(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERCHAIN DISULFIDE BOND.
    7. "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.
    8. "Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-binding protein beta in old liver."
      Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H., Hershey J.W., Timchenko N.A.
      J. Biol. Chem. 281:32806-32819(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CELF1; CALR3; HSPA5 AND CALR.
    9. "Mzb1 protein regulates calcium homeostasis, antibody secretion, and integrin activation in innate-like B cells."
      Flach H., Rosenbaum M., Duchniewicz M., Kim S., Zhang S.L., Cahalan M.D., Mittler G., Grosschedl R.
      Immunity 33:723-735(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MZB1.
    10. "Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone."
      Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z.
      Nat. Commun. 1:79-79(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CNPY3; TLR4; TLR9 AND TLR11, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-103.
    11. Erratum
      Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z.
      Nat. Commun. 3:653-653(2012)
    12. "Aminoacyl-tRNA synthetase-interacting multifunctional protein 1/p43 controls endoplasmic reticulum retention of heat shock protein gp96: its pathological implications in lupus-like autoimmune diseases."
      Han J.M., Park S.G., Liu B., Park B.-J., Kim J.Y., Jin C.H., Song Y.W., Li Z., Kim S.
      Am. J. Pathol. 170:2042-2054(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AIMP1.
    13. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-217.
    14. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-479, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-404 AND LYS-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiENPL_MOUSE
    AccessioniPrimary (citable) accession number: P08113
    Secondary accession number(s): P11427
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3