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Protein

Endoplasmin

Gene

HSP90B1

Organism
Canis lupus familiaris (Dog) (Canis 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)DescriptionActionsGraphical viewLength
    Binding sitei107ATP1
    Binding sitei149ATP1
    Binding sitei162ATP1
    Binding sitei168ATPBy similarity1
    Binding sitei199ATP; via amide nitrogen1
    Binding sitei448ATPBy similarity1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    ATP-binding, Calcium, Nucleotide-binding

    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 lupus familiaris (Dog) (Canis familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    Proteomesi
    • UP000002254 Componenti: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Sarcoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi103E → A: Loss of ATPase activity. 1 Publication1
    Mutagenesisi448R → A: Reduces ATPase activity by 85%. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL4748.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 21Sequence analysisAdd BLAST21
    ChainiPRO_000001359722 – 804EndoplasminAdd BLAST783

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi62N-linked (GlcNAc...)Sequence analysis1
    Modified residuei64PhosphoserineBy similarity1
    Glycosylationi107N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi138InterchainBy similarity
    Modified residuei172PhosphoserineBy similarity1
    Glycosylationi217N-linked (GlcNAc...)Sequence analysis1
    Modified residuei288Phosphothreonine; by CK2Sequence analysis1
    Modified residuei306Phosphoserine; by CK2Sequence analysisBy similarity1
    Modified residuei403PhosphoserineBy similarity1
    Modified residuei404N6-succinyllysineBy similarity1
    Glycosylationi445N-linked (GlcNAc...)Sequence analysis1
    Modified residuei447PhosphoserineBy similarity1
    Modified residuei479N6-acetyllysineBy similarity1
    Glycosylationi481N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi502N-linked (GlcNAc...)Sequence analysis1
    Modified residuei633N6-succinyllysineBy similarity1
    Modified residuei766Phosphothreonine; by CK2Sequence analysis1
    Modified residuei770Phosphothreonine; by CK2Sequence analysis1
    Modified residuei774Phosphothreonine; by CK2Sequence analysis1
    Modified residuei786Phosphothreonine; by CK2Sequence analysisBy similarity1

    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.

    Chemistry databases

    BindingDBiP41148.

    Structurei

    Secondary structure

    1804
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni72 – 74Combined sources3
    Helixi80 – 92Combined sources13
    Turni93 – 95Combined sources3
    Helixi99 – 121Combined sources23
    Turni123 – 128Combined sources6
    Beta strandi134 – 139Combined sources6
    Turni140 – 143Combined sources4
    Beta strandi144 – 149Combined sources6
    Helixi156 – 164Combined sources9
    Helixi169 – 184Combined sources16
    Helixi189 – 194Combined sources6
    Helixi198 – 204Combined sources7
    Beta strandi206 – 214Combined sources9
    Beta strandi216 – 218Combined sources3
    Beta strandi221 – 228Combined sources8
    Beta strandi230 – 234Combined sources5
    Beta strandi241 – 251Combined sources11
    Helixi253 – 259Combined sources7
    Helixi261 – 272Combined sources12
    Beta strandi279 – 284Combined sources6
    Beta strandi331 – 335Combined sources5
    Turni342 – 344Combined sources3
    Turni347 – 349Combined sources3
    Helixi352 – 361Combined sources10
    Beta strandi370 – 377Combined sources8
    Beta strandi379 – 381Combined sources3
    Beta strandi383 – 389Combined sources7
    Beta strandi409 – 413Combined sources5
    Beta strandi416 – 420Combined sources5
    Helixi428 – 430Combined sources3
    Beta strandi434 – 442Combined sources9
    Beta strandi444 – 446Combined sources3
    Helixi448 – 452Combined sources5
    Helixi455 – 474Combined sources20
    Helixi477 – 482Combined sources6
    Helixi484 – 498Combined sources15
    Helixi500 – 502Combined sources3
    Helixi503 – 507Combined sources5
    Beta strandi512 – 514Combined sources3
    Beta strandi517 – 519Combined sources3
    Helixi524 – 530Combined sources7
    Beta strandi537 – 542Combined sources6
    Helixi546 – 550Combined sources5
    Helixi553 – 555Combined sources3
    Helixi556 – 560Combined sources5
    Beta strandi566 – 568Combined sources3
    Helixi572 – 578Combined sources7
    Beta strandi586 – 590Combined sources5
    Helixi602 – 614Combined sources13
    Helixi616 – 624Combined sources9
    Turni625 – 630Combined sources6
    Beta strandi631 – 636Combined sources6
    Beta strandi644 – 649Combined sources6
    Helixi656 – 668Combined sources13
    Beta strandi677 – 680Combined sources4
    Beta strandi683 – 687Combined sources5
    Helixi692 – 703Combined sources12
    Helixi708 – 725Combined sources18
    Helixi732 – 744Combined sources13
    Turni751 – 757Combined sources7
    Helixi758 – 760Combined sources3
    Helixi762 – 764Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5IN9X-ray2.60A/B69-286[»]
    A/B328-337[»]
    ProteinModelPortaliP41148.
    SMRiP41148.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP41148.

    Family & Domainsi

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi801 – 804Prevents secretion from ERSequence analysis4

    Sequence similaritiesi

    Belongs to the heat shock protein 90 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG0020. Eukaryota.
    COG0326. LUCA.
    HOGENOMiHOG000031988.
    HOVERGENiHBG007374.
    InParanoidiP41148.
    KOiK09487.

    Family and domain databases

    Gene3Di3.30.565.10. 2 hits.
    HAMAPiMF_00505. HSP90. 1 hit.
    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.
    PfamiPF02518. HATPase_c. 1 hit.
    PF00183. 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_001003327.2.
    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_001003327.2.
    UniGeneiCfa.3896.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5IN9X-ray2.60A/B69-286[»]
    A/B328-337[»]
    ProteinModelPortaliP41148.
    SMRiP41148.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000011044.

    Chemistry databases

    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

    eggNOGiKOG0020. Eukaryota.
    COG0326. LUCA.
    HOGENOMiHOG000031988.
    HOVERGENiHBG007374.
    InParanoidiP41148.
    KOiK09487.

    Miscellaneous databases

    EvolutionaryTraceiP41148.
    PROiP41148.

    Family and domain databases

    Gene3Di3.30.565.10. 2 hits.
    HAMAPiMF_00505. HSP90. 1 hit.
    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.
    PfamiPF02518. HATPase_c. 1 hit.
    PF00183. 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...

    Entry informationi

    Entry nameiENPL_CANLF
    AccessioniPrimary (citable) accession number: P41148
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: November 2, 2016
    This is version 145 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

    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 one 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.