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Protein

Endoplasmin

Gene

HSP90B1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Kineticsi

  1. KM=10 µM for ATP1 Publication

    Sites

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

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    ATP-binding, Calcium, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_296399. Trafficking and processing of endosomal TLR.
    REACT_345639. Scavenging by Class A Receptors.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoplasmin
    Alternative name(s):
    94 kDa glucose-regulated protein
    Short name:
    GRP-94
    Heat shock protein 90 kDa beta member 1
    Gene namesi
    Name:HSP90B1
    Synonyms:GRP94, TRA1
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254 Componenti: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Sarcoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi103 – 1031E → A: Loss of ATPase activity. 1 Publication
    Mutagenesisi448 – 4481R → A: Reduces ATPase activity by 85%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 804783EndoplasminPRO_0000013597Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
    Modified residuei64 – 641PhosphoserineBy similarity
    Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi138 – 138InterchainBy similarity
    Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis
    Modified residuei288 – 2881Phosphothreonine; by CK2Sequence Analysis
    Modified residuei306 – 3061Phosphoserine; by CK2Sequence Analysis
    Modified residuei404 – 4041N6-succinyllysineBy similarity
    Glycosylationi445 – 4451N-linked (GlcNAc...)Sequence Analysis
    Modified residuei447 – 4471PhosphoserineBy similarity
    Modified residuei479 – 4791N6-acetyllysineBy similarity
    Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence Analysis
    Modified residuei633 – 6331N6-succinyllysineBy similarity
    Modified residuei766 – 7661Phosphothreonine; by CK2Sequence Analysis
    Modified residuei770 – 7701Phosphothreonine; by CK2Sequence Analysis
    Modified residuei774 – 7741Phosphothreonine; by CK2Sequence Analysis
    Modified residuei786 – 7861Phosphothreonine; by CK2Sequence Analysis

    Post-translational modificationi

    Phosphorylated by CK2.1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP41148.
    PRIDEiP41148.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By similarity). 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 AIMP1; regulates its retention in the endoplasmic reticulum. Interacts with OS9 (By similarity). Interacts with CNPY3; this interaction is disrupted in the presence of ATP. Interacts with several TLRs, including TLR4 and TLR9, but not with TLR3 (By similarity). Interacts with MZB1 in a calcium-dependent manner (By similarity). Interacts with METTL23 (By similarity).By similarity

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000011044.

    Structurei

    Secondary structure

    1
    804
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni72 – 743Combined sources
    Helixi80 – 9213Combined sources
    Turni93 – 953Combined sources
    Helixi99 – 12123Combined sources
    Turni123 – 1286Combined sources
    Beta strandi134 – 1396Combined sources
    Turni140 – 1434Combined sources
    Beta strandi144 – 1496Combined sources
    Helixi156 – 1649Combined sources
    Helixi169 – 18416Combined sources
    Helixi189 – 1946Combined sources
    Helixi198 – 2047Combined sources
    Beta strandi206 – 2149Combined sources
    Beta strandi216 – 2183Combined sources
    Beta strandi221 – 2288Combined sources
    Beta strandi230 – 2345Combined sources
    Beta strandi241 – 25111Combined sources
    Helixi253 – 2597Combined sources
    Helixi261 – 27212Combined sources
    Beta strandi279 – 2846Combined sources
    Beta strandi331 – 3355Combined sources
    Turni342 – 3443Combined sources
    Turni347 – 3493Combined sources
    Helixi352 – 36110Combined sources
    Beta strandi370 – 3778Combined sources
    Beta strandi379 – 3813Combined sources
    Beta strandi383 – 3897Combined sources
    Beta strandi409 – 4135Combined sources
    Beta strandi416 – 4205Combined sources
    Helixi428 – 4303Combined sources
    Beta strandi434 – 4429Combined sources
    Beta strandi444 – 4463Combined sources
    Helixi448 – 4525Combined sources
    Helixi455 – 47420Combined sources
    Helixi477 – 4826Combined sources
    Helixi484 – 49815Combined sources
    Helixi500 – 5023Combined sources
    Helixi503 – 5075Combined sources
    Beta strandi512 – 5143Combined sources
    Beta strandi517 – 5193Combined sources
    Helixi524 – 5307Combined sources
    Beta strandi537 – 5426Combined sources
    Helixi546 – 5505Combined sources
    Helixi553 – 5553Combined sources
    Helixi556 – 5605Combined sources
    Beta strandi566 – 5683Combined sources
    Helixi572 – 5787Combined sources
    Beta strandi586 – 5905Combined sources
    Helixi602 – 61413Combined sources
    Helixi616 – 6249Combined sources
    Turni625 – 6306Combined sources
    Beta strandi631 – 6366Combined sources
    Beta strandi644 – 6496Combined sources
    Helixi656 – 66813Combined sources
    Beta strandi677 – 6804Combined sources
    Beta strandi683 – 6875Combined sources
    Helixi692 – 70312Combined sources
    Helixi708 – 72518Combined sources
    Helixi732 – 74413Combined sources
    Turni751 – 7577Combined sources
    Helixi758 – 7603Combined sources
    Helixi762 – 7643Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QY5X-ray1.75A69-337[»]
    1QY8X-ray1.85A69-337[»]
    1QYEX-ray2.10A69-337[»]
    1TBWX-ray2.15A/B69-286[»]
    A/B328-337[»]
    1TC0X-ray2.20A/B69-286[»]
    A/B328-337[»]
    1TC6X-ray1.87A/B69-286[»]
    A/B328-337[»]
    1U0YX-ray2.30A69-337[»]
    1U0ZX-ray1.90A/B69-286[»]
    A/B328-337[»]
    1U2OX-ray2.10A/B69-286[»]
    A/B328-337[»]
    1YSZX-ray2.65A69-286[»]
    A328-337[»]
    1YT0X-ray2.40A69-286[»]
    A328-337[»]
    1YT1X-ray2.20A/B69-286[»]
    A/B328-337[»]
    1YT2X-ray3.25A69-337[»]
    2ESAX-ray1.90A69-286[»]
    A328-337[»]
    2EXLX-ray2.35A/B69-286[»]
    A/B328-337[»]
    2FYPX-ray1.95A/B69-286[»]
    A/B328-337[»]
    2GFDX-ray2.30A/B69-286[»]
    A/B328-337[»]
    2GQPX-ray1.50A/B69-286[»]
    A/B328-337[»]
    2H8MX-ray1.80A/B69-286[»]
    A/B328-337[»]
    2HCHX-ray2.30A/B69-286[»]
    A/B328-337[»]
    2HG1X-ray2.30A/B69-286[»]
    2O1TX-ray3.20A/B/C/D/E/F/G/H/I/J336-765[»]
    2O1UX-ray2.40A/B73-286[»]
    A/B328-754[»]
    2O1VX-ray2.45A/B73-286[»]
    A/B328-754[»]
    2O1WX-ray3.40A/B/C/D/E73-286[»]
    A/B/C/D/E328-594[»]
    3O2FX-ray2.00A/B69-286[»]
    A/B328-337[»]
    ProteinModelPortaliP41148.
    SMRiP41148. Positions 69-755.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP41148.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi801 – 8044Prevents secretion from ERSequence Analysis

    Sequence similaritiesi

    Belongs to the heat shock protein 90 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0326.
    HOGENOMiHOG000031988.
    HOVERGENiHBG007374.
    InParanoidiP41148.
    KOiK09487.

    Family and domain databases

    Gene3Di3.30.565.10. 2 hits.
    HAMAPiMF_00505. HSP90.
    InterProiIPR003594. HATPase_C.
    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.

    P41148-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ
    60 70 80 90 100
    REEEAIQLDG LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF
    110 120 130 140 150
    LRELISNASD ALDKIRLISL TDENALAGNE ELTVKIKCDK EKNLLHVTDT
    160 170 180 190 200
    GVGMTREELV KNLGTIAKSG TSEFLNKMTE AQEDGQSTSE LIGQFGVGFY
    210 220 230 240 250
    SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT LGRGTTITLV
    260 270 280 290 300
    LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK
    310 320 330 340 350
    EEKEDSDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV
    360 370 380 390 400
    EDDEYKAFYK SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE
    410 420 430 440 450
    YGSKKSDYIK LYVRRVFITD DFHDMMPKYL NFVKGVVDSD DLPLNVSRET
    460 470 480 490 500
    LQQHKLLKVI RKKLVRKTLD MIKKIADEKY NDTFWKEFGT NIKLGVIEDH
    510 520 530 540 550
    SNRTRLAKLL RFQSSHHPSD ITSLDQYVER MKEKQDKIYF MAGSSRKEAE
    560 570 580 590 600
    SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
    610 620 630 640 650
    SEKTKESREA IEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS
    660 670 680 690 700
    QYGWSGNMER IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIKDMLRR
    710 720 730 740 750
    VKEDEDDKTV SDLAVVLFET ATLRSGYLLP DTKAYGDRIE RMLRLSLNID
    760 770 780 790 800
    PDAKVEEEPE EEPEETTEDT TEDTEQDDEE EMDAGTDDEE QETVKKSTAE

    KDEL
    Length:804
    Mass (Da):92,514
    Last modified:February 1, 1995 - v1
    Checksum:i36AA126EDCFFC2D5
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U01153 mRNA. Translation: AAA17708.1.
    PIRiA53211.
    RefSeqiNP_001003327.1. NM_001003327.1.
    UniGeneiCfa.3896.

    Genome annotation databases

    GeneIDi404019.
    KEGGicfa:404019.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U01153 mRNA. Translation: AAA17708.1.
    PIRiA53211.
    RefSeqiNP_001003327.1. NM_001003327.1.
    UniGeneiCfa.3896.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QY5X-ray1.75A69-337[»]
    1QY8X-ray1.85A69-337[»]
    1QYEX-ray2.10A69-337[»]
    1TBWX-ray2.15A/B69-286[»]
    A/B328-337[»]
    1TC0X-ray2.20A/B69-286[»]
    A/B328-337[»]
    1TC6X-ray1.87A/B69-286[»]
    A/B328-337[»]
    1U0YX-ray2.30A69-337[»]
    1U0ZX-ray1.90A/B69-286[»]
    A/B328-337[»]
    1U2OX-ray2.10A/B69-286[»]
    A/B328-337[»]
    1YSZX-ray2.65A69-286[»]
    A328-337[»]
    1YT0X-ray2.40A69-286[»]
    A328-337[»]
    1YT1X-ray2.20A/B69-286[»]
    A/B328-337[»]
    1YT2X-ray3.25A69-337[»]
    2ESAX-ray1.90A69-286[»]
    A328-337[»]
    2EXLX-ray2.35A/B69-286[»]
    A/B328-337[»]
    2FYPX-ray1.95A/B69-286[»]
    A/B328-337[»]
    2GFDX-ray2.30A/B69-286[»]
    A/B328-337[»]
    2GQPX-ray1.50A/B69-286[»]
    A/B328-337[»]
    2H8MX-ray1.80A/B69-286[»]
    A/B328-337[»]
    2HCHX-ray2.30A/B69-286[»]
    A/B328-337[»]
    2HG1X-ray2.30A/B69-286[»]
    2O1TX-ray3.20A/B/C/D/E/F/G/H/I/J336-765[»]
    2O1UX-ray2.40A/B73-286[»]
    A/B328-754[»]
    2O1VX-ray2.45A/B73-286[»]
    A/B328-754[»]
    2O1WX-ray3.40A/B/C/D/E73-286[»]
    A/B/C/D/E328-594[»]
    3O2FX-ray2.00A/B69-286[»]
    A/B328-337[»]
    ProteinModelPortaliP41148.
    SMRiP41148. Positions 69-755.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000011044.

    Chemistry

    BindingDBiP41148.
    ChEMBLiCHEMBL4748.

    Proteomic databases

    PaxDbiP41148.
    PRIDEiP41148.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi404019.
    KEGGicfa:404019.

    Organism-specific databases

    CTDi7184.

    Phylogenomic databases

    eggNOGiCOG0326.
    HOGENOMiHOG000031988.
    HOVERGENiHBG007374.
    InParanoidiP41148.
    KOiK09487.

    Enzyme and pathway databases

    ReactomeiREACT_296399. Trafficking and processing of endosomal TLR.
    REACT_345639. Scavenging by Class A Receptors.

    Miscellaneous databases

    EvolutionaryTraceiP41148.
    NextBioi20817506.
    PROiP41148.

    Family and domain databases

    Gene3Di3.30.565.10. 2 hits.
    HAMAPiMF_00505. HSP90.
    InterProiIPR003594. HATPase_C.
    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]
    ProtoNetiSearch...

    Publicationsi

    1. "GRP94 resides within cardiac sarcoplasmic reticulum vesicles and is phosphorylated by casein kinase II."
      Cala S.E., Jones L.R.
      J. Biol. Chem. 269:5926-5931(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION.
      Tissue: Heart.
    2. "Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation."
      Soldano K.L., Jivan A., Nicchitta C.V., Gewirth D.T.
      J. Biol. Chem. 278:48330-48338(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 69-337 IN COMPLEX WITH ADENOSINE ANALOG.
    3. "Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone."
      Immormino R.M., Dollins D.E., Shaffer P.L., Soldano K.L., Walker M.A., Gewirth D.T.
      J. Biol. Chem. 279:46162-46171(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 69-337 IN COMPLEXES WITH ATP; ADP AND AMP, SUBUNIT.
    4. "Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change."
      Dollins D.E., Immormino R.M., Gewirth D.T.
      J. Biol. Chem. 280:30438-30447(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 69-337 OF APOPROTEIN AND IN COMPLEXES WITH ADP AND NECA.
    5. "Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones."
      Dollins D.E., Warren J.J., Immormino R.M., Gewirth D.T.
      Mol. Cell 28:41-56(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 73-754 IN COMPLEXES WITH AMPPNP AND ADP, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-103 AND ARG-448, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiENPL_CANFA
    AccessioniPrimary (citable) accession number: P41148
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: May 27, 2015
    This is version 136 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

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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.