Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P07900 (HS90A_HUMAN)

Entry version 248 (03 Jul 2019)
Sequence version 5 (23 Jan 2007)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Heat shock protein HSP 90-alpha

Gene

HSP90AA1

Organism
Homo sapiens (Human)
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 promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues(PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385).3 Publications7 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

In the resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer which is defined as the open conformation (PubMed:18400751). Upon ATP-binding, the N-terminal domain undergoes significant conformational changes and comes in contact to form an active closed conformation (PubMed:18400751). After HSP90 finishes its chaperoning tasks of assisting the proper folding, stabilization and activation of client proteins under the active state, ATP molecule is hydrolyzed to ADP which then dissociates from HSP90 and directs the protein back to the resting state (PubMed:18400751). Co-chaperone TSC1 promotes ATP binding and inhibits HSP90AA1 ATPase activity (PubMed:29127155). Binding to phosphorylated AHSA1 promotes HSP90AA1 ATPase activity (PubMed:29127155). Inhibited by Ganetespib (STA-9090) and SNX-2112 (PubMed:29127155).2 Publications

<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=300 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 sitei51ATP1
    Binding sitei93ATP1
    Binding sitei112ATPBy similarity1
    Binding sitei138ATP; via amide nitrogen1
    Binding sitei400ATPBy similarity1

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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
    Biological processStress response
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-HSA-1227986 Signaling by ERBB2
    R-HSA-1236382 Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
    R-HSA-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
    R-HSA-192905 vRNP Assembly
    R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
    R-HSA-203615 eNOS activation
    R-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition
    R-HSA-3000484 Scavenging by Class F Receptors
    R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
    R-HSA-3371511 HSF1 activation
    R-HSA-3371568 Attenuation phase
    R-HSA-3371571 HSF1-dependent transactivation
    R-HSA-380259 Loss of Nlp from mitotic centrosomes
    R-HSA-380270 Recruitment of mitotic centrosome proteins and complexes
    R-HSA-380284 Loss of proteins required for interphase microtubule organization from the centrosome
    R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
    R-HSA-399954 Sema3A PAK dependent Axon repulsion
    R-HSA-4420097 VEGFA-VEGFR2 Pathway
    R-HSA-5218920 VEGFR2 mediated vascular permeability
    R-HSA-5336415 Uptake and function of diphtheria toxin
    R-HSA-5601884 PIWI-interacting RNA (piRNA) biogenesis
    R-HSA-5620912 Anchoring of the basal body to the plasma membrane
    R-HSA-5637810 Constitutive Signaling by EGFRvIII
    R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
    R-HSA-6798695 Neutrophil degranulation
    R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
    R-HSA-8854518 AURKA Activation by TPX2
    R-HSA-8863795 Downregulation of ERBB2 signaling
    R-HSA-8939211 ESR-mediated signaling
    R-HSA-9009391 Non-genomic estrogen signaling
    R-HSA-9018519 Estrogen-dependent gene expression

    SIGNOR Signaling Network Open Resource

    More...    SIGNORi    		P07900

    Protein family/group databases

    MoonDB Database of extreme multifunctional and moonlighting proteins

    More...    MoonDBi    		P07900 Predicted

    <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:
    Heat shock protein HSP 90-alpha
    Alternative name(s):
    Heat shock 86 kDa
    Short name:
    HSP 86
    Short name:
    HSP86
    Lipopolysaccharide-associated protein 2
    Short name:
    LAP-2
    Short name:
    LPS-associated protein 2
    Renal carcinoma antigen NY-REN-38
    <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:HSP90AA1
    Synonyms:HSP90A, HSPC1, HSPCA
    <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>OrganismiHomo sapiens (Human)
    <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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <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
    • UP000005640 <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: Chromosome 14

    Organism-specific databases

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:5253 HSP90AA1

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		140571 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_P07900

    <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

    Cell membrane, Cytoplasm, Membrane, Nucleus

    <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>Mutagenesisi47E → A: Strong ATP-binding. Strong interaction with HSF1, HIF1A, ERBB2, MET, KEAP1 and RHOBTB2. No effect on interaction with TSC1. 2 Publications1
    Mutagenesisi93D → A: Impaired ATP-binding. Strong interaction with HIF1A, MET, KEAP1 and RHOBTB2. Loss of interaction with HSF1 and ERBB2. Los of interaction with TSC1. 2 Publications1
    Mutagenesisi97G → D: Abolishes ATPase activity. 1 Publication1
    Mutagenesisi313Y → E: Loss of interaction with TSC1 and increases interacrion with AHSA1. 1 Publication1
    Mutagenesisi313Y → F: No deffect on the interaction with TSC1. 1 Publication1
    Mutagenesisi598C → A, N or D: Reduces ATPase activity and client protein activation. 2 Publications1
    Mutagenesisi598C → S: Loss of S-nitrosylation. 2 Publications1
    Mutagenesisi728 – 732Missing : Loss of interaction with TSC1. 1 Publication5

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		3320

    Open Targets

    More...    OpenTargetsi    		ENSG00000080824

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA29519

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL3880

    Drug and drug target database

    More...    DrugBanki    		DB07317 (3E)-3-[(phenylamino)methylidene]dihydrofuran-2(3H)-one
    DB03080 17-Dmag
    DB08786 4-(2-methoxyethoxy)-6-methylpyrimidin-2-amine
    DB03809 9-Butyl-8-(3-Methoxybenzyl)-9h-Purin-6-Amine
    DB03899 9-Butyl-8-(4-Methoxybenzyl)-9h-Purin-6-Amine
    DB05134 CNF1010
    DB02424 Geldanamycin
    DB07325 N-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)METHYL]-3-{[(E)-(2-OXODIHYDROFURAN-3(2H)-YLIDENE)METHYL]AMINO}BENZENESULFONAMIDE
    DB00716 Nedocromil
    DB00615 Rifabutin
    DB06070 SNX-5422

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...    GuidetoPHARMACOLOGYi    		2905

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		HSP90AA1

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		92090606

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <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_00000629112 – 732Heat shock protein HSP 90-alphaAdd BLAST731

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 residuei5Phosphothreonine; by PRKDC1 Publication1
    Modified residuei7Phosphothreonine; by PRKDC1 Publication1
    Modified residuei58N6-acetyllysineBy similarity1
    Modified residuei84N6-acetyllysineBy similarity1
    Modified residuei231PhosphoserineCombined sources1 Publication1
    Modified residuei252PhosphoserineCombined sources1
    Modified residuei263PhosphoserineCombined sources1 Publication1
    Modified residuei313PhosphotyrosineBy similarity1
    Modified residuei443N6-acetyllysineCombined sources1
    Modified residuei453PhosphoserineBy similarity1
    Modified residuei458N6-acetyllysineCombined sources1
    Modified residuei476PhosphoserineCombined sources1
    Modified residuei489N6-acetyllysineCombined sources1
    Modified residuei492PhosphotyrosineBy similarity1
    Modified residuei585N6-acetyllysineCombined sources1
    Modified residuei598S-nitrosocysteine1 Publication1
    Modified residuei641PhosphoserineCombined sources1

    <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

    ISGylated.1 Publication
    S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.1 Publication
    Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1. Ubiquitination promotes translocation into the cytoplasm away from the membrane and secretory pathways.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P07900

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P07900

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		P07900

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

    More...    PaxDbi    		P07900

    PeptideAtlas

    More...    PeptideAtlasi    		P07900

    PRoteomics IDEntifications database

    More...    PRIDEi    		P07900

    ProteomicsDB human proteome resource

    More...    ProteomicsDBi    		52031
    52032 [P07900-2]

    Consortium for Top Down Proteomics

    More...    TopDownProteomicsi    		P07900-1 [P07900-1]

    2D gel databases

    USC-OGP 2-DE database

    More...    OGPi    		P07900

    REPRODUCTION-2DPAGE

    More...    REPRODUCTION-2DPAGEi    		IPI00784295

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...    CarbonylDBi    		P07900

    GlyConnect protein glycosylation platform

    More...    GlyConnecti    		1301

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P07900

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...    PhosphoSitePlusi    		P07900

    SwissPalm database of S-palmitoylation events

    More...    SwissPalmi    		P07900

    Miscellaneous databases

    CutDB - Proteolytic event database

    More...    PMAP-CutDBi    		P07900

    <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

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000080824 Expressed in 252 organ(s), highest expression level in middle temporal gyrus

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		P07900 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		P07900 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		CAB002058

    <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 (PubMed:7588731, PubMed:8289821, PubMed:18400751, PubMed:29127155). Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C or STIP1 (PubMed:15383005, PubMed:9195923).

    Forms a complex containing HSP90AA1, TSC1 and TSC2; TSC1 is required to recruit TCS2 to the complex (PubMed:29127155). The closed form interacts (via the middle domain and TPR repeat-binding motif) with co-chaperone TSC1 (via C-terminus) (PubMed:29127155).

    Interacts with TOM34 (PubMed:9660753).

    Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex (PubMed:11274138, PubMed:9817749).

    Interacts with CHORDC1 and DNAJC7 (PubMed:12853476, PubMed:19875381).

    Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems (PubMed:16307917, PubMed:27353360).

    Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity (PubMed:15383005, PubMed:15577939, PubMed:16531226, PubMed:27353360). Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8 (PubMed:11276205).

    Interacts with KSR1 (PubMed:10409742).

    Interacts with co-chaperone CDC37 (via C-terminus); the interaction inhibits HSP90AA1 ATPase activity (PubMed:23569206, PubMed:27353360). May interact with NWD1 (PubMed:24681825).

    Interacts with FNIP1 and FNIP2; the interaction inhibits HSP90AA1 ATPase activity (PubMed:17028174, PubMed:27353360).

    Interacts with co-chaperone AHSA1 (phosphorylated on 'Tyr-223'); the interaction activates HSP90AA1 ATPase activity and results in the dissociation of TSC1 from HSP90AA1 (PubMed:12604615, PubMed:27353360, PubMed:29127155).

    Interacts with FLCN in the presence of FNIP1 (PubMed:27353360).

    Interacts with HSP70, STIP1 and PTGES3 (PubMed:27353360).

    Interacts with SMYD3; this interaction enhances SMYD3 histone-lysine N-methyltransferase (PubMed:15235609, PubMed:25738358).

    Interacts with SGTA (via TPR repeats) (PubMed:15708368).

    Interacts with TTC1 (via TPR repeats) (PubMed:15708368).

    Interacts with HSF1 in an ATP-dependent manner (PubMed:11583998. PubMed:26517842).

    Interacts with MET; the interaction suppresses MET kinase activity (PubMed:26517842).

    Interacts with ERBB2 in an ATP-dependent manner; the interaction suppresses ERBB2 kinase activity (PubMed:26517842).

    Interacts with HIF1A, KEAP1 and RHOBTB2 (PubMed:26517842).

    Interacts with HSF1; this interaction is decreased in a IER5-dependent manner, promoting HSF1 accumulation in the nucleus, homotrimerization and DNA-binding activities (PubMed:26754925).

    Interacts with STUB1 and SMAD3 (PubMed:24613385).

    Interacts with HSP90AB1; interaction is constitutive (PubMed:20353823).

    Interacts with HECTD1 (via N-terminus) (By similarity).

    Interacts with NR3C1 (via domain NR LBD) and NR1D1 (via domain NR LBD) (By similarity).

    Interacts with NLPR12 (PubMed:30559449, PubMed:17947705).

    By similarity31 Publications

    (Microbial infection)

    Interacts with herpes simplex virus 1 protein US11; this interaction inhibits TBK1-induced interferon production.

    1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		109552, 872 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...    ComplexPortali    		CPX-3288 HSP90A-CDC37 chaperone complex

    CORUM comprehensive resource of mammalian protein complexes

    More...    CORUMi    		P07900

    Database of interacting proteins

    More...    DIPi    		DIP-27595N

    Protein interaction database and analysis system

    More...    IntActi    		P07900, 250 interactors

    Molecular INTeraction database

    More...    MINTi    		P07900

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000335153

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P07900

    <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

    1732
    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    		P07900

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P07900

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni9 – 236Interaction with NR3C1By similarityAdd BLAST228
    Regioni271 – 616Interaction with NR3C1By similarityAdd BLAST346
    Regioni284 – 732Interaction with FLCN and FNIP11 PublicationAdd BLAST449
    Regioni284 – 620Interaction with FNIP2 and TSC12 PublicationsAdd BLAST337
    Regioni628 – 731Interaction with NR1D1By similarityAdd BLAST104
    Regioni682 – 732Required for homodimerization1 PublicationAdd BLAST51
    Regioni728 – 732Essential for interaction with SMYD3, TSC1 and STIP1/HOP2 Publications5
    Regioni729 – 732Essential for interaction with SGTA and TTC11 Publication4

    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>Motifi723 – 732TPR repeat-binding1 Publication10

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.1 Publication

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG0019 Eukaryota
    KOG0020 Eukaryota
    COG0326 LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00950000182747

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P07900

    KEGG Orthology (KO)

    More...    KOi    		K04079

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		MRRMKEM

    Database of Orthologous Groups

    More...    OrthoDBi    		188544at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P07900

    TreeFam database of animal gene trees

    More...    TreeFami    		TF300686

    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
    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>Sequences (2+)i

    <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.

    This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P07900-1) [UniParc]FASTAAdd to basket
    Also known as: HSP90AA1-1, HSP90-alpha 2

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS 
            60         70         80         90        100
    NSSDALDKIR YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK 
           110        120        130        140        150
    ADLINNLGTI AKSGTKAFME ALQAGADISM IGQFGVGFYS AYLVAEKVTV 
           160        170        180        190        200
    ITKHNDDEQY AWESSAGGSF TVRTDTGEPM GRGTKVILHL KEDQTEYLEE 
           210        220        230        240        250
    RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED KEEEKEKEEK 
           260        270        280        290        300
    ESEDKPEIED VGSDEEEEKK DGDKKKKKKI KEKYIDQEEL NKTKPIWTRN 
           310        320        330        340        350
    PDDITNEEYG EFYKSLTNDW EDHLAVKHFS VEGQLEFRAL LFVPRRAPFD 
           360        370        380        390        400
    LFENRKKKNN IKLYVRRVFI MDNCEELIPE YLNFIRGVVD SEDLPLNISR 
           410        420        430        440        450
    EMLQQSKILK VIRKNLVKKC LELFTELAED KENYKKFYEQ FSKNIKLGIH 
           460        470        480        490        500
    EDSQNRKKLS ELLRYYTSAS GDEMVSLKDY CTRMKENQKH IYYITGETKD 
           510        520        530        540        550
    QVANSAFVER LRKHGLEVIY MIEPIDEYCV QQLKEFEGKT LVSVTKEGLE 
           560        570        580        590        600
    LPEDEEEKKK QEEKKTKFEN LCKIMKDILE KKVEKVVVSN RLVTSPCCIV 
           610        620        630        640        650
    TSTYGWTANM ERIMKAQALR DNSTMGYMAA KKHLEINPDH SIIETLRQKA 
           660        670        680        690        700
    EADKNDKSVK DLVILLYETA LLSSGFSLED PQTHANRIYR MIKLGLGIDE 
           710        720        730 
    DDPTADDTSA AVTEEMPPLE GDDDTSRMEE VD
    Length:732
    Mass (Da):84,660
    Last modified:January 23, 2007 - v5
    <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:i969F65FCC0BC86FD
    GO
    Isoform 2 (identifier: P07900-2) [UniParc]FASTAAdd to basket
    Also known as: HSP90AA1-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MPPCSGGDGS...QPFILLRLLM

    Show »
    Length:854
    Mass (Da):98,161
    Checksum:i404BD8CAD5E68DB0
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    G3V2J8G3V2J8_HUMAN
    Heat shock protein HSP 90-alpha
    HSP90AA1
    		174Annotation score:

    Annotation score:1 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>
    H0YJF5H0YJF5_HUMAN
    Heat shock protein HSP 90-alpha
    HSP90AA1
    		52Annotation score:

    Annotation score:1 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>
    G3V592G3V592_HUMAN
    Heat shock protein HSP 90-alpha
    HSP90AA1
    		80Annotation score:

    Annotation score:1 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>
    A0A0U1RR69A0A0U1RR69_HUMAN
    Heat shock protein HSP 90-alpha
    HSP90AA1
    		100Annotation score:

    Annotation score:1 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 Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti63S → T in CAA33259 (PubMed:2780322).Curated1
    Sequence conflicti74K → R in CAI64495 (PubMed:16269234).Curated1
    Sequence conflicti74K → R in BAG51711 (PubMed:14702039).Curated1
    Sequence conflicti86D → G in CAI64495 (PubMed:16269234).Curated1
    Sequence conflicti86D → G in BAG51711 (PubMed:14702039).Curated1
    Sequence conflicti162W → D AA sequence (PubMed:10409742).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Isoform 2 (identifier: P07900-2)
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti71M → L. Corresponds to variant dbSNP:rs8005905Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0266041M → MPPCSGGDGSTPPGPSLRDR DCPAQSAEYPRDRLDPRPGS PSEASSPPFLRSRAPVNWYQ EKAQVFLWHLMVSGSTTLLC LWKQPFHVSAFPVTASLAFR QSQGAGQHLYKDLQPFILLR LLM in isoform 2. 2 Publications1

    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
    		X15183 mRNA Translation: CAA33259.1
    M27024 Genomic DNA Translation: AAA63194.1
    AJ890082 mRNA Translation: CAI64495.1
    AJ890083 mRNA Translation: CAI64496.1
    DQ314871 Genomic DNA Translation: ABC40730.1
    AK056446 mRNA Translation: BAG51711.1
    AK291115 mRNA Translation: BAF83804.1
    AK291607 mRNA Translation: BAF84296.1
    AL133223 Genomic DNA No translation available.
    CH471061 Genomic DNA Translation: EAW81765.1
    X07270 mRNA Translation: CAA30255.1
    M30626 Genomic DNA Translation: AAA36023.1
    BC000987 mRNA Translation: AAH00987.1
    BC121062 mRNA Translation: AAI21063.1
    D87666 mRNA Translation: BAA13430.1
    D87666 mRNA Translation: BAA13431.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS32160.1 [P07900-2]
    CCDS9967.1 [P07900-1]

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A32319 HHHU86

    NCBI Reference Sequences

    More...    RefSeqi    		NP_001017963.2, NM_001017963.2 [P07900-2]
    NP_005339.3, NM_005348.3 [P07900-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000216281; ENSP00000216281; ENSG00000080824 [P07900-1]
    ENST00000334701; ENSP00000335153; ENSG00000080824 [P07900-2]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		3320

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:3320

    UCSC genome browser

    More...    UCSCi    		uc001yku.5 human [P07900-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    <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
    		X15183 mRNA Translation: CAA33259.1
    M27024 Genomic DNA Translation: AAA63194.1
    AJ890082 mRNA Translation: CAI64495.1
    AJ890083 mRNA Translation: CAI64496.1
    DQ314871 Genomic DNA Translation: ABC40730.1
    AK056446 mRNA Translation: BAG51711.1
    AK291115 mRNA Translation: BAF83804.1
    AK291607 mRNA Translation: BAF84296.1
    AL133223 Genomic DNA No translation available.
    CH471061 Genomic DNA Translation: EAW81765.1
    X07270 mRNA Translation: CAA30255.1
    M30626 Genomic DNA Translation: AAA36023.1
    BC000987 mRNA Translation: AAH00987.1
    BC121062 mRNA Translation: AAI21063.1
    D87666 mRNA Translation: BAA13430.1
    D87666 mRNA Translation: BAA13431.1
    CCDSiCCDS32160.1 [P07900-2]
    CCDS9967.1 [P07900-1]
    PIRiA32319 HHHU86
    RefSeqiNP_001017963.2, NM_001017963.2 [P07900-2]
    NP_005339.3, NM_005348.3 [P07900-1]

    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
    1BYQX-ray1.50A9-236[»]
    1OSFX-ray1.75A9-223[»]
    1UY6X-ray1.90A2-236[»]
    1UY7X-ray1.90A2-236[»]
    1UY8X-ray1.98A2-236[»]
    1UY9X-ray2.00A2-236[»]
    1UYCX-ray2.00A2-236[»]
    1UYDX-ray2.20A2-236[»]
    1UYEX-ray2.00A2-236[»]
    1UYFX-ray2.00A2-236[»]
    1UYGX-ray2.00A2-236[»]
    1UYHX-ray2.20A2-236[»]
    1UYIX-ray2.20A2-236[»]
    1UYKX-ray2.20A2-236[»]
    1UYLX-ray1.40A2-236[»]
    1YC1X-ray1.70A9-236[»]
    1YC3X-ray2.12A9-236[»]
    1YC4X-ray1.81A9-236[»]
    1YERX-ray1.65A9-236[»]
    1YESX-ray2.20A9-236[»]
    1YETX-ray1.90A9-236[»]
    2BSMX-ray2.05A2-236[»]
    2BT0X-ray1.90A/B2-236[»]
    2BUGNMR-B728-732[»]
    2BYHX-ray1.90A11-236[»]
    2BYIX-ray1.60A11-236[»]
    2BZ5X-ray1.90A/B2-236[»]
    2C2LX-ray3.30E/F/G/H724-732[»]
    2CCSX-ray1.79A1-236[»]
    2CCTX-ray2.30A1-236[»]
    2CCUX-ray2.70A1-236[»]
    2FWYX-ray2.10A1-236[»]
    2FWZX-ray2.10A1-236[»]
    2H55X-ray2.00A1-236[»]
    2JJCX-ray1.95A9-223[»]
    2K5BNMR-A14-223[»]
    2QF6X-ray3.10A/B/C/D17-223[»]
    2QFOX-ray1.68A/B17-223[»]
    2QG0X-ray1.85A/B17-223[»]
    2QG2X-ray1.80A17-223[»]
    2UWDX-ray1.90A2-236[»]
    2VCIX-ray2.00A1-236[»]
    2VCJX-ray2.50A1-236[»]
    2WI1X-ray2.30A1-236[»]
    2WI2X-ray2.09A/B1-236[»]
    2WI3X-ray1.90A1-236[»]
    2WI4X-ray2.40A1-236[»]
    2WI5X-ray2.10A1-236[»]
    2WI6X-ray2.18A1-236[»]
    2WI7X-ray2.50A1-236[»]
    2XABX-ray1.90A/B9-236[»]
    2XDKX-ray1.97A9-236[»]
    2XDLX-ray1.98A9-236[»]
    2XDSX-ray1.97A9-236[»]
    2XDUX-ray1.74A14-224[»]
    2XDXX-ray2.42A9-236[»]
    2XHRX-ray2.20A9-236[»]
    2XHTX-ray2.27A9-236[»]
    2XHXX-ray2.80A9-236[»]
    2XJGX-ray2.25A9-236[»]
    2XJJX-ray1.90A/B9-236[»]
    2XJXX-ray1.66A9-236[»]
    2XK2X-ray1.95A9-236[»]
    2YE2X-ray1.90A9-236[»]
    2YE3X-ray1.95A9-236[»]
    2YE4X-ray2.30A9-236[»]
    2YE5X-ray1.73A9-236[»]
    2YE6X-ray2.56A9-236[»]
    2YE7X-ray2.20A9-236[»]
    2YE8X-ray2.30A9-236[»]
    2YE9X-ray2.20A9-236[»]
    2YEAX-ray1.73A9-236[»]
    2YEBX-ray2.40A9-236[»]
    2YECX-ray2.10A9-236[»]
    2YEDX-ray2.10A9-236[»]
    2YEEX-ray2.30A9-236[»]
    2YEFX-ray1.55A9-236[»]
    2YEGX-ray2.50A/B9-236[»]
    2YEHX-ray2.10A9-236[»]
    2YEIX-ray2.20A9-236[»]
    2YEJX-ray2.20A9-236[»]
    2YI0X-ray1.60A1-229[»]
    2YI5X-ray2.50A1-229[»]
    2YI6X-ray1.80A1-229[»]
    2YI7X-ray1.40A1-229[»]
    2YJWX-ray1.61A18-223[»]
    2YJXX-ray1.83A18-223[»]
    2YK2X-ray1.74A18-223[»]
    2YK9X-ray1.32A18-223[»]
    2YKBX-ray1.93A18-223[»]
    2YKCX-ray1.67A18-223[»]
    2YKEX-ray1.43A18-223[»]
    2YKIX-ray1.67A18-223[»]
    2YKJX-ray1.46A18-223[»]
    3B24X-ray1.70A/B9-236[»]
    3B25X-ray1.75A9-236[»]
    3B26X-ray2.10A/B9-236[»]
    3B27X-ray1.50A9-236[»]
    3B28X-ray1.35A/B9-236[»]
    3BM9X-ray1.60A14-236[»]
    3BMYX-ray1.60A14-236[»]
    3D0BX-ray1.74A1-232[»]
    3EKOX-ray1.55A/B9-225[»]
    3EKRX-ray2.00A/B9-225[»]
    3FT5X-ray1.90A9-236[»]
    3FT8X-ray2.00A9-236[»]
    3HEKX-ray1.95A/B9-225[»]
    3HHUX-ray1.59A/B1-224[»]
    3HYYX-ray1.90A9-236[»]
    3HYZX-ray2.30A/B9-236[»]
    3HZ1X-ray2.30A9-236[»]
    3HZ5X-ray1.90A9-236[»]
    3INWX-ray1.95A10-236[»]
    3INXX-ray1.75A10-236[»]
    3K97X-ray1.95A9-236[»]
    3K98X-ray2.40A/B9-225[»]
    3K99X-ray2.10A/B/C/D9-225[»]
    3MNRX-ray1.90P1-232[»]
    3O0IX-ray1.47A1-236[»]
    3OW6X-ray1.80A17-223[»]
    3OWBX-ray2.05A17-223[»]
    3OWDX-ray1.63A17-223[»]
    3Q6MX-ray3.00A/B/C293-732[»]
    3Q6NX-ray3.05A/B/C/D/E/F293-732[»]
    3QDDX-ray1.79A1-236[»]
    3QTFX-ray1.57A14-236[»]
    3R4MX-ray1.70A9-236[»]
    3R4NX-ray2.00A/B9-225[»]
    3R4OX-ray2.65A/B9-225[»]
    3R4PX-ray1.70A/B9-225[»]
    3R91X-ray1.58A14-236[»]
    3R92X-ray1.58A14-236[»]
    3RKZX-ray1.57A14-236[»]
    3RLPX-ray1.70A/B9-225[»]
    3RLQX-ray1.90A/B9-225[»]
    3RLRX-ray1.70A/B9-225[»]
    3T0HX-ray1.20A9-236[»]
    3T0ZX-ray2.19A9-236[»]
    3T10X-ray1.24A9-236[»]
    3T1KX-ray1.50A/B9-236[»]
    3T2SX-ray1.50A/B9-236[»]
    3TUHX-ray1.80A/B16-224[»]
    3VHAX-ray1.39A9-236[»]
    3VHCX-ray1.41A9-236[»]
    3VHDX-ray1.52A/B9-236[»]
    3WHAX-ray1.30A/B9-236[»]
    3WQ9X-ray1.80A1-236[»]
    4AIFX-ray2.01D/E726-732[»]
    4AWOX-ray1.70A/B9-236[»]
    4AWPX-ray1.82A/B9-236[»]
    4AWQX-ray1.60A/B9-236[»]
    4B7PX-ray1.70A9-236[»]
    4BQGX-ray1.90A9-236[»]
    4BQJX-ray2.00A9-236[»]
    4CGQX-ray2.00Q726-732[»]
    4CGUX-ray2.11C726-732[»]
    4CGVX-ray2.54E/F726-732[»]
    4CGWX-ray3.00C/D726-732[»]
    4CWFX-ray2.00A9-236[»]
    4CWNX-ray1.80A9-236[»]
    4CWOX-ray2.31A9-236[»]
    4CWPX-ray1.95A9-236[»]
    4CWQX-ray2.00A9-236[»]
    4CWRX-ray2.00A9-236[»]
    4CWSX-ray2.30A9-236[»]
    4CWTX-ray1.90A9-236[»]
    4EEHX-ray1.60A9-236[»]
    4EFTX-ray2.12A9-236[»]
    4EFUX-ray2.00A9-236[»]
    4EGHX-ray1.60A9-236[»]
    4EGIX-ray1.79A9-236[»]
    4EGKX-ray1.69A9-236[»]
    4FCPX-ray2.00A/B1-236[»]
    4FCQX-ray2.15A1-236[»]
    4FCRX-ray1.70A1-236[»]
    4HY6X-ray1.65A9-236[»]
    4JQLX-ray1.72A9-236[»]
    4L8ZX-ray1.70A9-236[»]
    4L90X-ray2.00A9-236[»]
    4L91X-ray1.75A9-236[»]
    4L93X-ray1.84A/B9-236[»]
    4L94X-ray1.65A9-236[»]
    4LWEX-ray1.50A17-224[»]
    4LWFX-ray1.75A17-224[»]
    4LWGX-ray1.60A17-224[»]
    4LWHX-ray1.70A16-224[»]
    4LWIX-ray1.70A17-224[»]
    4NH7X-ray2.00A/B9-236[»]
    4NH8X-ray1.65A9-236[»]
    4O04X-ray1.82A9-236[»]
    4O05X-ray1.79A9-236[»]
    4O07X-ray1.86A9-236[»]
    4O09X-ray1.96A9-236[»]
    4O0BX-ray1.93A9-236[»]
    4R3MX-ray1.80A16-224[»]
    4U93X-ray1.55A1-236[»]
    4W7TX-ray1.80A1-236[»]
    4XIPX-ray1.70A9-236[»]
    4XIQX-ray1.84A9-236[»]
    4XIRX-ray1.70A9-236[»]
    4XITX-ray1.86A9-236[»]
    4YKQX-ray1.91A2-236[»]
    4YKRX-ray1.61A2-236[»]
    4YKTX-ray1.85A2-236[»]
    4YKUX-ray1.70A2-236[»]
    4YKWX-ray1.85A/B2-236[»]
    4YKXX-ray1.80A2-236[»]
    4YKYX-ray1.78A2-236[»]
    4YKZX-ray1.85A2-236[»]
    5CF0X-ray1.80A9-236[»]
    5FNCX-ray2.20A1-236[»]
    5FNDX-ray2.00A1-236[»]
    5FNFX-ray2.10A1-236[»]
    5GGZX-ray2.02A/B/C/D16-225[»]
    5J20X-ray1.76A17-223[»]
    5J27X-ray1.70A16-224[»]
    5J2VX-ray1.59A17-223[»]
    5J2XX-ray1.22A17-224[»]
    5J64X-ray1.38A9-236[»]
    5J6LX-ray1.75A9-236[»]
    5J6MX-ray1.64A9-234[»]
    5J6NX-ray1.90A9-234[»]
    5J80X-ray1.17A9-233[»]
    5J82X-ray2.17A9-233[»]
    5J86X-ray1.87A9-233[»]
    5J8MX-ray1.90A/B9-233[»]
    5J8UX-ray1.75A/B9-233[»]
    5J9XX-ray1.80A9-233[»]
    5LNYX-ray1.88A9-236[»]
    5LNZX-ray1.54A9-236[»]
    5LO0X-ray2.30A9-236[»]
    5LO1X-ray2.70A9-236[»]
    5LO5X-ray1.44A9-236[»]
    5LO6X-ray2.40A9-236[»]
    5LQ9X-ray1.90A17-223[»]
    5LR1X-ray1.44A18-223[»]
    5LR7X-ray1.86A18-223[»]
    5LRLX-ray1.33A18-223[»]
    5LRZX-ray2.00A18-223[»]
    5LS1X-ray1.85A17-223[»]
    5M4EX-ray1.90A9-236[»]
    5M4HX-ray2.00A9-236[»]
    5NYHX-ray1.65A9-236[»]
    5NYIX-ray1.44A9-235[»]
    5OCIX-ray1.62A9-236[»]
    5OD7X-ray2.00A9-236[»]
    5ODXX-ray1.82A9-236[»]
    5T21X-ray2.10A18-223[»]
    5VYYX-ray1.79A1-236[»]
    5XQDX-ray1.60A9-236[»]
    5XQEX-ray1.70A9-236[»]
    5XR5X-ray1.60A9-236[»]
    5XR9X-ray1.50A9-236[»]
    5XRBX-ray1.65A9-236[»]
    5XRDX-ray1.30A9-236[»]
    5XREX-ray1.50A9-236[»]
    5ZR3X-ray2.50A/C/E/G1-236[»]
    6B99X-ray1.60A1-236[»]
    6B9AX-ray1.65A/B1-236[»]
    6CEOX-ray1.90A1-236[»]
    6CYGX-ray1.50A/B1-236[»]
    6CYHX-ray1.49A/B1-236[»]
    6EI5X-ray2.20A15-223[»]
    6EL5X-ray1.67A1-236[»]
    6ELNX-ray1.60A17-223[»]
    6ELOX-ray1.80A1-236[»]
    6ELPX-ray1.85A1-236[»]
    6EY8X-ray2.16A1-236[»]
    6EY9X-ray2.00A1-236[»]
    6EYAX-ray2.10A1-236[»]
    6EYBX-ray1.90A1-236[»]
    6F1NX-ray2.09A1-236[»]
    6FCJX-ray2.49A9-236[»]
    6FDPNMR-B724-732[»]
    6GP4X-ray1.70A1-236[»]
    6GP8X-ray1.75A1-236[»]
    6GPFX-ray1.55A1-236[»]
    6GPHX-ray1.56A1-236[»]
    6GPOX-ray1.48A1-236[»]
    6GPPX-ray1.51A1-236[»]
    6GPRX-ray2.35A1-236[»]
    6GPTX-ray2.00A1-236[»]
    6GPWX-ray1.60A1-236[»]
    6GPYX-ray2.25A1-236[»]
    6GQ6X-ray2.25A1-236[»]
    6GQRX-ray2.05A1-236[»]
    6GQSX-ray1.43A1-236[»]
    6GQUX-ray1.72A1-236[»]
    6GR1X-ray2.05A1-236[»]
    6GR3X-ray1.88A1-236[»]
    6GR4X-ray1.50A1-236[»]
    6GR5X-ray1.34A1-236[»]
    SMRiP07900
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi109552, 872 interactors
    ComplexPortaliCPX-3288 HSP90A-CDC37 chaperone complex
    CORUMiP07900
    DIPiDIP-27595N
    IntActiP07900, 250 interactors
    MINTiP07900
    STRINGi9606.ENSP00000335153

    Chemistry databases

    BindingDBiP07900
    ChEMBLiCHEMBL3880
    DrugBankiDB07317 (3E)-3-[(phenylamino)methylidene]dihydrofuran-2(3H)-one
    DB03080 17-Dmag
    DB08786 4-(2-methoxyethoxy)-6-methylpyrimidin-2-amine
    DB03809 9-Butyl-8-(3-Methoxybenzyl)-9h-Purin-6-Amine
    DB03899 9-Butyl-8-(4-Methoxybenzyl)-9h-Purin-6-Amine
    DB05134 CNF1010
    DB02424 Geldanamycin
    DB07325 N-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)METHYL]-3-{[(E)-(2-OXODIHYDROFURAN-3(2H)-YLIDENE)METHYL]AMINO}BENZENESULFONAMIDE
    DB00716 Nedocromil
    DB00615 Rifabutin
    DB06070 SNX-5422
    GuidetoPHARMACOLOGYi2905

    Protein family/group databases

    MoonDBiP07900 Predicted

    PTM databases

    CarbonylDBiP07900
    GlyConnecti1301
    iPTMnetiP07900
    PhosphoSitePlusiP07900
    SwissPalmiP07900

    Polymorphism and mutation databases

    BioMutaiHSP90AA1
    DMDMi92090606

    2D gel databases

    OGPiP07900
    REPRODUCTION-2DPAGEiIPI00784295

    Proteomic databases

    EPDiP07900
    jPOSTiP07900
    MaxQBiP07900
    PaxDbiP07900
    PeptideAtlasiP07900
    PRIDEiP07900
    ProteomicsDBi52031
    52032 [P07900-2]
    TopDownProteomicsiP07900-1 [P07900-1]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000216281; ENSP00000216281; ENSG00000080824 [P07900-1]
    ENST00000334701; ENSP00000335153; ENSG00000080824 [P07900-2]
    GeneIDi3320
    KEGGihsa:3320
    UCSCiuc001yku.5 human [P07900-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		3320
    DisGeNETi3320

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		HSP90AA1
    HGNCiHGNC:5253 HSP90AA1
    HPAiCAB002058
    MIMi140571 gene
    neXtProtiNX_P07900
    OpenTargetsiENSG00000080824
    PharmGKBiPA29519

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG0019 Eukaryota
    KOG0020 Eukaryota
    COG0326 LUCA
    GeneTreeiENSGT00950000182747
    InParanoidiP07900
    KOiK04079
    OMAiMRRMKEM
    OrthoDBi188544at2759
    PhylomeDBiP07900
    TreeFamiTF300686

    Enzyme and pathway databases

    ReactomeiR-HSA-1227986 Signaling by ERBB2
    R-HSA-1236382 Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
    R-HSA-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
    R-HSA-192905 vRNP Assembly
    R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
    R-HSA-203615 eNOS activation
    R-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition
    R-HSA-3000484 Scavenging by Class F Receptors
    R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
    R-HSA-3371511 HSF1 activation
    R-HSA-3371568 Attenuation phase
    R-HSA-3371571 HSF1-dependent transactivation
    R-HSA-380259 Loss of Nlp from mitotic centrosomes
    R-HSA-380270 Recruitment of mitotic centrosome proteins and complexes
    R-HSA-380284 Loss of proteins required for interphase microtubule organization from the centrosome
    R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
    R-HSA-399954 Sema3A PAK dependent Axon repulsion
    R-HSA-4420097 VEGFA-VEGFR2 Pathway
    R-HSA-5218920 VEGFR2 mediated vascular permeability
    R-HSA-5336415 Uptake and function of diphtheria toxin
    R-HSA-5601884 PIWI-interacting RNA (piRNA) biogenesis
    R-HSA-5620912 Anchoring of the basal body to the plasma membrane
    R-HSA-5637810 Constitutive Signaling by EGFRvIII
    R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
    R-HSA-6798695 Neutrophil degranulation
    R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
    R-HSA-8854518 AURKA Activation by TPX2
    R-HSA-8863795 Downregulation of ERBB2 signaling
    R-HSA-8939211 ESR-mediated signaling
    R-HSA-9009391 Non-genomic estrogen signaling
    R-HSA-9018519 Estrogen-dependent gene expression
    SIGNORiP07900

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...    ChiTaRSi    		HSP90AA1 human
    EvolutionaryTraceiP07900

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...    GenomeRNAii    		3320
    PMAP-CutDBiP07900

    Protein Ontology

    More...    PROi    		PR:P07900

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000080824 Expressed in 252 organ(s), highest expression level in middle temporal gyrus
    ExpressionAtlasiP07900 baseline and differential
    GenevisibleiP07900 HS

    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
    PS00298 HSP90, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		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 nameiHS90A_HUMAN
    <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: P07900
    Secondary accession number(s): A8K500
    , B3KPJ9, Q2PP14, Q5CAQ6, Q5CAQ7, Q9BVQ5
    <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: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: July 3, 2019
    This is version 248 of the entry and version 5 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
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <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
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again