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Entry version 161 (05 Jun 2019)
Sequence version 1 (01 Feb 1995)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD) (By similarity). Has ATPase activity (PubMed:17936703).By similarity1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=10 µM for ATP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei107ATPCombined sources3 Publications1
    Binding sitei149ATPCombined sources3 Publications1
    Binding sitei162ATPCombined sources3 Publications1
    Binding sitei199ATP; via amide nitrogenCombined sources3 Publications1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei448Important for ATP hydrolysis1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • unfolded protein binding Source: GO_Central

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionChaperone
    LigandATP-binding, Calcium, Nucleotide-binding

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:HSP90B1
    Synonyms:GRP941 Publication, TRA1
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9615 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002254 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Endoplasmic reticulum, Sarcoplasmic reticulum

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi103E → A: Loss of ATPase activity. 1 Publication1
    Mutagenesisi448R → A: Reduces ATPase activity by 85%. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4748

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21Sequence analysisAdd BLAST21
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001359722 – 804EndoplasminAdd BLAST783

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi62N-linked (GlcNAc...) asparagineSequence analysis1
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei64PhosphoserineBy similarity1
    Glycosylationi107N-linked (GlcNAc...) asparagineSequence analysis1
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi138InterchainBy similarity
    Modified residuei172PhosphoserineBy similarity1
    Glycosylationi217N-linked (GlcNAc...) asparagineSequence analysis1
    Modified residuei288Phosphothreonine; by CK2Sequence analysis1
    Modified residuei306Phosphoserine; by CK2Sequence analysisBy similarity1
    Modified residuei403PhosphoserineBy similarity1
    Modified residuei404N6-succinyllysineBy similarity1
    Glycosylationi445N-linked (GlcNAc...) asparagineSequence analysis1
    Modified residuei447PhosphoserineBy similarity1
    Modified residuei479N6-acetyllysineBy similarity1
    Glycosylationi481N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi502N-linked (GlcNAc...) asparagineSequence 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

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Phosphorylated by CK2.1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P41148

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P41148

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Detected in heart muscle (at protein level).1 Publication

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

    GO - Molecular functioni

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    9612.ENSCAFP00000011044

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P41148

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1804
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P41148

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P41148

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi801 – 804Prevents secretion from ERSequence analysis4

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the heat shock protein 90 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0020 Eukaryota
    COG0326 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000031988

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P41148

    KEGG Orthology (KO)

    More...
    KOi
    K09487

    Database of Orthologous Groups

    More...
    OrthoDBi
    172471at2759

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00075 HATPase_c, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.20.120.790, 1 hit
    3.30.565.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00505 HSP90, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR003594 HATPase_C
    IPR036890 HATPase_C_sf
    IPR019805 Heat_shock_protein_90_CS
    IPR037196 HSP90_C
    IPR001404 Hsp90_fam
    IPR020575 Hsp90_N
    IPR020568 Ribosomal_S5_D2-typ_fold

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11528 PTHR11528, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02518 HATPase_c, 1 hit
    PF00183 HSP90, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF002583 Hsp90, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00775 HEATSHOCK90

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00387 HATPase_c, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF110942 SSF110942, 1 hit
    SSF54211 SSF54211, 1 hit
    SSF55874 SSF55874, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00014 ER_TARGET, 1 hit
    PS00298 HSP90, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i36AA126EDCFFC2D5
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    U01153 mRNA Translation: AAA17708.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A53211

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001003327.1, NM_001003327.2

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    404019

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    cfa:404019

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    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[»]
    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[»]
    5TTZX-ray2.71A/B69-286[»]
    5ULSX-ray2.62A/B48-286[»]
    A/B328-754[»]
    5WMTX-ray2.75A/B/C/D69-286[»]
    6AOLX-ray2.76A69-286[»]
    6AOMX-ray2.87A/B69-286[»]
    6ASPX-ray2.70A/B69-286[»]
    6ASQX-ray2.35A/B69-286[»]
    6BAWX-ray2.70A/B/C/D69-286[»]
    6C91X-ray2.90B/C69-286[»]
    6CYIX-ray1.76A69-337[»]
    6D1XX-ray2.30A69-337[»]
    6D28X-ray1.75A69-337[»]
    SMRiP41148
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9612.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

    Comparative Toxicogenomics Database

    More...
    CTDi
    7184

    Phylogenomic databases

    eggNOGiKOG0020 Eukaryota
    COG0326 LUCA
    HOGENOMiHOG000031988
    InParanoidiP41148
    KOiK09487
    OrthoDBi172471at2759

    Miscellaneous databases

    EvolutionaryTraceiP41148

    Protein Ontology

    More...
    PROi
    PR:P41148

    Family and domain databases

    CDDicd00075 HATPase_c, 1 hit
    Gene3Di1.20.120.790, 1 hit
    3.30.565.10, 1 hit
    HAMAPiMF_00505 HSP90, 1 hit
    InterProiView protein in InterPro
    IPR003594 HATPase_C
    IPR036890 HATPase_C_sf
    IPR019805 Heat_shock_protein_90_CS
    IPR037196 HSP90_C
    IPR001404 Hsp90_fam
    IPR020575 Hsp90_N
    IPR020568 Ribosomal_S5_D2-typ_fold
    PANTHERiPTHR11528 PTHR11528, 1 hit
    PfamiView protein in Pfam
    PF02518 HATPase_c, 1 hit
    PF00183 HSP90, 1 hit
    PIRSFiPIRSF002583 Hsp90, 1 hit
    PRINTSiPR00775 HEATSHOCK90
    SMARTiView protein in SMART
    SM00387 HATPase_c, 1 hit
    SUPFAMiSSF110942 SSF110942, 1 hit
    SSF54211 SSF54211, 1 hit
    SSF55874 SSF55874, 1 hit
    PROSITEiView protein in PROSITE
    PS00014 ER_TARGET, 1 hit
    PS00298 HSP90, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiENPL_CANLF
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P41148
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: June 5, 2019
    This is version 161 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
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