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UniProtKB - P07900 (HS90A_HUMAN)

Entry version 265 (25 May 2022)
Sequence version 5 (23 Jan 2007)
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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, PubMed:12526792).

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).

Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792).

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).

Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812).

3 Publications10 Publications

(Microbial infection) Seems to interfere with N.meningitidis NadA-mediated invasion of human cells. Decreasing HSP90 levels increases adhesion and entry of E.coli expressing NadA into human Chang cells; increasing its levels leads to decreased adhesion and invasion.

1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 geldanamycin, Ganetespib (STA-9090) and SNX-2112 (PubMed:29127155, PubMed:12526792).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%5Fsection">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, Hydrolase
Biological processHost-virus interaction, Stress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.6.4.10, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P07900

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-168928, DDX58/IFIH1-mediated induction of interferon-alpha/beta
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) in the presence of ligand
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-5675482, Regulation of necroptotic cell death
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, Extra-nuclear estrogen signaling
R-HSA-9013418, RHOBTB2 GTPase cycle
R-HSA-9018519, Estrogen-dependent gene expression
R-HSA-9613829, Chaperone Mediated Autophagy
R-HSA-9634285, Constitutive Signaling by Overexpressed ERBB2
R-HSA-9646399, Aggrephagy
R-HSA-9652282, Drug-mediated inhibition of ERBB2 signaling
R-HSA-9664565, Signaling by ERBB2 KD Mutants
R-HSA-9665233, Resistance of ERBB2 KD mutants to trastuzumab
R-HSA-9665244, Resistance of ERBB2 KD mutants to sapitinib
R-HSA-9665245, Resistance of ERBB2 KD mutants to tesevatinib
R-HSA-9665246, Resistance of ERBB2 KD mutants to neratinib
R-HSA-9665247, Resistance of ERBB2 KD mutants to osimertinib
R-HSA-9665249, Resistance of ERBB2 KD mutants to afatinib
R-HSA-9665250, Resistance of ERBB2 KD mutants to AEE788
R-HSA-9665251, Resistance of ERBB2 KD mutants to lapatinib
R-HSA-9665348, Signaling by ERBB2 ECD mutants
R-HSA-9665686, Signaling by ERBB2 TMD/JMD mutants
R-HSA-9665737, Drug resistance in ERBB2 TMD/JMD mutants
R-HSA-9679191, Potential therapeutics for SARS

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P07900

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%5Fand%5Ftaxonomy%5Fsection">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-alphaCurated (EC:3.6.4.101 Publication)
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%5Fand%5Ftaxonomy%5Fsection">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:HSP90AA1Imported
Synonyms:HSP90A, HSPC1, HSPCA
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000080824

<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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, 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%5Fand%5Fbiotech%5Fsection">'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 – 732MEEVD → AAAA: Loss of interaction with TOMM70. No effect on interaction with IRF3. 1 Publication5
Mutagenesisi728 – 732Missing : Loss of interaction with TSC1. 1 Publication5
Mutagenesisi729 – 732Missing : Loss of interaction with TOMM70. 1 Publication4
Mutagenesisi731 – 732VD → AA: Loss of interaction with TOMM70. No effect on interaction with IRF3. 2 Publications2

Organism-specific databases

DisGeNET

More...DisGeNETi		3320

Open Targets

More...OpenTargetsi		ENSG00000080824

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA29519

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P07900, Tchem

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
DB08197, (5E,7S)-2-amino-7-(4-fluoro-2-pyridin-3-ylphenyl)-4-methyl-7,8-dihydroquinazolin-5(6H)-one oxime
DB08443, 2-(1H-pyrrol-1-ylcarbonyl)benzene-1,3,5-triol
DB08557, 2-[(2-methoxyethyl)amino]-4-(4-oxo-1,2,3,4-tetrahydro-9H-carbazol-9-yl)benzamide
DB08789, 2-AMINO-4-(2,4-DICHLOROPHENYL)-N-ETHYLTHIENO[2,3-D]PYRIMIDINE-6-CARBOXAMIDE
DB06969, 2-amino-4-[2,4-dichloro-5-(2-pyrrolidin-1-ylethoxy)phenyl]-N-ethylthieno[2,3-d]pyrimidine-6-carboxamide
DB08788, 3,6-DIAMINO-5-CYANO-4-(4-ETHOXYPHENYL)THIENO[2,3-B]PYRIDINE-2-CARBOXAMIDE
DB07324, 3-({2-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)ETHYNYL]BENZYL}AMINO)-1,3-OXAZOL-2(3H)-ONE
DB02840, 4-(1,3-Benzodioxol-5-Yl)-5-(5-Ethyl-2,4-Dihydroxyphenyl)-2h-Pyrazole-3-Carboxylic Acid
DB03749, 4-(1h-Imidazol-4-Yl)-3-(5-Ethyl-2,4-Dihydroxy-Phenyl)-1h-Pyrazole
DB08787, 4-(2,4-dichlorophenyl)-5-phenyldiazenyl-pyrimidin-2-amine
DB08786, 4-(2-methoxyethoxy)-6-methylpyrimidin-2-amine
DB07502, 4-bromo-6-(6-hydroxy-1,2-benzisoxazol-3-yl)benzene-1,3-diol
DB07100, 4-CHLORO-6-(4-PIPERAZIN-1-YL-1H-PYRAZOL-5-YL)BENZENE-1,3-DIOL
DB06957, 4-CHLORO-6-(4-{4-[4-(METHYLSULFONYL)BENZYL]PIPERAZIN-1-YL}-1H-PYRAZOL-5-YL)BENZENE-1,3-DIOL
DB07601, 4-chloro-6-{5-[(2-morpholin-4-ylethyl)amino]-1,2-benzisoxazol-3-yl}benzene-1,3-diol
DB08194, 4-methyl-7,8-dihydro-5H-thiopyrano[4,3-d]pyrimidin-2-amine
DB08442, 4-{[(2R)-2-(2-methylphenyl)pyrrolidin-1-yl]carbonyl}benzene-1,3-diol
DB07495, 5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-N-ETHYL-4-(4-METHOXYPHENYL)-1H-PYRAZOLE-3-CARBOXAMIDE
DB06964, 5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-N-ETHYL-4-(4-METHOXYPHENYL)ISOXAZOLE-3-CARBOXAMIDE
DB06961, 5-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-[4-(morpholin-4-ylmethyl)phenyl]isoxazole-3-carboxamide
DB06958, 5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-N-ETHYL-4-PIPERAZIN-1-YL-1H-PYRAZOLE-3-CARBOXAMIDE
DB07319, 6-(3-BROMO-2-NAPHTHYL)-1,3,5-TRIAZINE-2,4-DIAMINE
DB03137, 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9-Pent-9h-Purin-6-Ylamine
DB03093, 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine
DB02550, 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-2-Fluoro-9-Pent-4-Ylnyl-9h-Purin-6-Ylamine
DB04505, 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-9-Pent-4-Ylnyl-9h-Purin-6-Ylamine
DB07877, 8-(6-BROMO-BENZO[1,3]DIOXOL-5-YLSULFANYL)-9-(3-ISOPROPYLAMINO-PROPYL)-ADENINE
DB04254, 8-Benzo[1,3]Dioxol-,5-Ylmethyl-9-Butyl-2-Fluoro-9h-Purin-6-Ylamine
DB08436, 8-BENZO[1,3]DIOXOL-,5-YLMETHYL-9-BUTYL-9H
DB04054, 9-Butyl-8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine
DB02359, 9-Butyl-8-(2,5-Dimethoxy-Benzyl)-9h-Purin-6-Ylamine
DB03504, 9-Butyl-8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-9h-Purin-6-Ylamine
DB02754, 9-Butyl-8-(3,4,5-Trimethoxybenzyl)-9h-Purin-6-Amine
DB03809, 9-Butyl-8-(3-Methoxybenzyl)-9h-Purin-6-Amine
DB03899, 9-Butyl-8-(4-Methoxybenzyl)-9h-Purin-6-Amine
DB12442, Alvespimycin
DB07594, CCT-018159
DB09130, Copper
DB02424, Geldanamycin
DB06956, N-(4-ACETYLPHENYL)-5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-1H-PYRAZOLE-4-CARBOXAMIDE
DB07325, N-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)METHYL]-3-{[(E)-(2-OXODIHYDROFURAN-3(2H)-YLIDENE)METHYL]AMINO}BENZENESULFONAMIDE
DB04588, N-[4-(AMINOSULFONYL)BENZYL]-5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-1H-PYRAZOLE-4-CARBOXAMIDE
DB00716, Nedocromil
DB09221, Polaprezinc
DB04216, Quercetin
DB00615, Rifabutin
DB06070, SNX-5422
DB05134, Tanespimycin

DrugCentral

More...DrugCentrali		P07900

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2905

Genetic variation 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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		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: a multi-organism proteome resource

More...ProteomicsDBi		52031 [P07900-1]
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, 1 N-Linked glycan (1 site)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P07900, 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P07900

MetOSite database of methionine sulfoxide sites

More...MetOSitei		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

<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 middle temporal gyrus and 265 other tissues

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		ENSG00000080824, Tissue enhanced (brain)

<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%5Fsection">'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%5Fsection">'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).

Interacts with PDCL3 (By similarity).

Interacts with TOMM70; the interaction is required for preprotein mitochondrial import (PubMed:12526792).

Interacts with TOMM70, IRF3 and TBK1; the interactions are direct and mediate the association of TOMM70 with IRF3 and TBK1 (PubMed:20628368).

Forms a complex with ASL, ASS1 and NOS2; the complex regulates cell-autonomous L-arginine synthesis and citrulline recycling while channeling extracellular L-arginine to nitric oxide synthesis pathway.

By similarity33 Publications

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

1 Publication

(Microbial infection) Interacts with N.meningitidis serogroup B adhesin A (nadA). Interaction is stabilized by ADP and 17-AAG (17-N-allylamino-17-demethoxygeldanamycin) and inhibited by ATP. Decreasing HSP90 levels increases adhesion and entry of bacterial into human Chang cells; increasing its levels leads to decreased adhseion and invasion.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P07900
With#Exp.IntAct
ADAMTSL4 - isoform 3 [Q6UY14-3]3EBI-296047,EBI-10173507
AHSA1 [O95433]4EBI-296047,EBI-448610
APP [P05067]5EBI-296047,EBI-77613
BTBD1 [Q9H0C5]4EBI-296047,EBI-935503
CAMK2A [Q9UQM7]5EBI-296047,EBI-1383687
CCDC117 [Q8IWD4]5EBI-296047,EBI-3387963
CCDC32 [Q9BV29]3EBI-296047,EBI-2874058
CDC37 [Q16543]14EBI-296047,EBI-295634
CDC37L1 [Q7L3B6]2EBI-296047,EBI-2841876
CDK9 [P50750]3EBI-296047,EBI-1383449
CERS2 [Q96G23]2EBI-296047,EBI-1057080
CHORDC1 [Q9UHD1]8EBI-296047,EBI-2550959
CHUK [O15111]3EBI-296047,EBI-81249
CORO6 - isoform 4 [Q6QEF8-4]3EBI-296047,EBI-10699285
CRMP1 [Q14194]3EBI-296047,EBI-473101
CTNNB1 [P35222]3EBI-296047,EBI-491549
CYTH1 [Q15438]3EBI-296047,EBI-997830
DYRK4 [Q9NR20]2EBI-296047,EBI-3914009
EGFR [P00533]7EBI-296047,EBI-297353
ERBB2 [P04626]5EBI-296047,EBI-641062
FKBP4 [Q02790]8EBI-296047,EBI-1047444
FKBP5 [Q13451]8EBI-296047,EBI-306914
FKBP8 [Q14318]7EBI-296047,EBI-724839
FYN [P06241]6EBI-296047,EBI-515315
HSFY2 - isoform 3 [Q96LI6-3]3EBI-296047,EBI-25830912
itself6EBI-296047,EBI-296047
HSP90AB1 [Q6PK50]2EBI-296047,EBI-9356629
IKBKG [Q9Y6K9]3EBI-296047,EBI-81279
IP6K2 [Q9UHH9]2EBI-296047,EBI-747509
JUN [P05412]4EBI-296047,EBI-852823
KAT5 - isoform 1 [Q92993-2]3EBI-296047,EBI-20795332
KSR2 [Q6VAB6]6EBI-296047,EBI-6424389
LCK [P06239]3EBI-296047,EBI-1348
MAP3K14 [Q99558]5EBI-296047,EBI-358011
MAP3K7 - isoform 1A [O43318-2]5EBI-296047,EBI-358700
MOS [P00540]2EBI-296047,EBI-1757866
NR3C1 [P04150]8EBI-296047,EBI-493507
NUDCD2 [Q8WVJ2]4EBI-296047,EBI-1052153
PAFAH1B1 [P43034]5EBI-296047,EBI-720620
PPP5C [P53041]12EBI-296047,EBI-716663
PRKACA [P17612]4EBI-296047,EBI-476586
PRUNE2 [A0A0C4DFM3]3EBI-296047,EBI-25830870
PSKH2 [Q96QS6]2EBI-296047,EBI-6424813
PTGES3 [Q15185]6EBI-296047,EBI-1049387
RAF1 [P04049]4EBI-296047,EBI-365996
REST [Q13127]4EBI-296047,EBI-926706
RPAP3 [Q9H6T3]6EBI-296047,EBI-356928
RPS3A [P61247]3EBI-296047,EBI-352378
SRC [P12931]3EBI-296047,EBI-621482
STK11 [Q15831]3EBI-296047,EBI-306838
STUB1 [Q9UNE7]9EBI-296047,EBI-357085
TOMM70 [O94826]4EBI-296047,EBI-2800236
TSSK6 [Q9BXA6]2EBI-296047,EBI-851883
TXN [P10599]3EBI-296047,EBI-594644
WDCP - isoform 2 [Q9H6R7-2]3EBI-296047,EBI-25833271
PPID [P26882] from Bos taurus.4EBI-296047,EBI-6477155
S100a1 [P35467] from Rattus norvegicus.4EBI-296047,EBI-6477109

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		109552, 1052 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, 387 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

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P07900, protein

<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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P07900

Biological Magnetic Resonance Data Bank

More...BMRBi		P07900

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

More...SMRi		P07900

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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
Regioni225 – 278DisorderedSequence analysisAdd BLAST54
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
Regioni700 – 732DisorderedSequence analysisAdd BLAST33
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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi243 – 257Basic and acidic residuesSequence analysisAdd BLAST15

<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

Ensembl GeneTree

More...GeneTreei		ENSGT01020000230401

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_006684_1_3_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P07900

Identification of Orthologs from Complete Genome Data

More...OMAi		AHDQPME

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

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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 <p><strong>What is the canonical sequence?</strong><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 variantiVAR_08283571M → LCuratedCorresponds 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		ENST00000216281.13; ENSP00000216281.8; ENSG00000080824.19
ENST00000334701.11; ENSP00000335153.7; ENSG00000080824.19 [P07900-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3320

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3320

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000216281.13; ENSP00000216281.8; NM_005348.4; NP_005339.3

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[»]
6HHRX-ray2.00A17-224[»]
6KSQX-ray2.20A293-554[»]
6LR9X-ray2.20A9-236[»]
6LSZX-ray1.99A9-236[»]
6LT8X-ray1.59A9-236[»]
6LTIX-ray1.59A9-236[»]
6LTKX-ray2.14A9-236[»]
6N8XX-ray1.49A1-236[»]
6OLXX-ray1.44A1-236[»]
6TN4X-ray1.27AAA9-236[»]
6TN5X-ray1.17AAA9-236[»]
6U98X-ray1.50A2-236[»]
6U99X-ray1.60A2-236[»]
6U9AX-ray1.65A2-236[»]
6U9BX-ray1.75A2-236[»]
7DMCX-ray2.34A16-224[»]
7KRJelectron microscopy2.56A/B1-732[»]
7KW7electron microscopy3.57A/B1-732[»]
7L7Ielectron microscopy3.30A/B1-732[»]
7L7Jelectron microscopy3.10A/B1-732[»]
7LSZX-ray1.70A1-293[»]
7LT0X-ray1.70A1-293[»]
AlphaFoldDBiP07900
BMRBiP07900
SMRiP07900
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi109552, 1052 interactors
ComplexPortaliCPX-3288, HSP90A-CDC37 chaperone complex
CORUMiP07900
DIPiDIP-27595N
IntActiP07900, 387 interactors
MINTiP07900
STRINGi9606.ENSP00000335153

Chemistry databases

BindingDBiP07900
ChEMBLiCHEMBL3880
DrugBankiDB07317, (3E)-3-[(phenylamino)methylidene]dihydrofuran-2(3H)-one
DB08197, (5E,7S)-2-amino-7-(4-fluoro-2-pyridin-3-ylphenyl)-4-methyl-7,8-dihydroquinazolin-5(6H)-one oxime
DB08443, 2-(1H-pyrrol-1-ylcarbonyl)benzene-1,3,5-triol
DB08557, 2-[(2-methoxyethyl)amino]-4-(4-oxo-1,2,3,4-tetrahydro-9H-carbazol-9-yl)benzamide
DB08789, 2-AMINO-4-(2,4-DICHLOROPHENYL)-N-ETHYLTHIENO[2,3-D]PYRIMIDINE-6-CARBOXAMIDE
DB06969, 2-amino-4-[2,4-dichloro-5-(2-pyrrolidin-1-ylethoxy)phenyl]-N-ethylthieno[2,3-d]pyrimidine-6-carboxamide
DB08788, 3,6-DIAMINO-5-CYANO-4-(4-ETHOXYPHENYL)THIENO[2,3-B]PYRIDINE-2-CARBOXAMIDE
DB07324, 3-({2-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)ETHYNYL]BENZYL}AMINO)-1,3-OXAZOL-2(3H)-ONE
DB02840, 4-(1,3-Benzodioxol-5-Yl)-5-(5-Ethyl-2,4-Dihydroxyphenyl)-2h-Pyrazole-3-Carboxylic Acid
DB03749, 4-(1h-Imidazol-4-Yl)-3-(5-Ethyl-2,4-Dihydroxy-Phenyl)-1h-Pyrazole
DB08787, 4-(2,4-dichlorophenyl)-5-phenyldiazenyl-pyrimidin-2-amine
DB08786, 4-(2-methoxyethoxy)-6-methylpyrimidin-2-amine
DB07502, 4-bromo-6-(6-hydroxy-1,2-benzisoxazol-3-yl)benzene-1,3-diol
DB07100, 4-CHLORO-6-(4-PIPERAZIN-1-YL-1H-PYRAZOL-5-YL)BENZENE-1,3-DIOL
DB06957, 4-CHLORO-6-(4-{4-[4-(METHYLSULFONYL)BENZYL]PIPERAZIN-1-YL}-1H-PYRAZOL-5-YL)BENZENE-1,3-DIOL
DB07601, 4-chloro-6-{5-[(2-morpholin-4-ylethyl)amino]-1,2-benzisoxazol-3-yl}benzene-1,3-diol
DB08194, 4-methyl-7,8-dihydro-5H-thiopyrano[4,3-d]pyrimidin-2-amine
DB08442, 4-{[(2R)-2-(2-methylphenyl)pyrrolidin-1-yl]carbonyl}benzene-1,3-diol
DB07495, 5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-N-ETHYL-4-(4-METHOXYPHENYL)-1H-PYRAZOLE-3-CARBOXAMIDE
DB06964, 5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-N-ETHYL-4-(4-METHOXYPHENYL)ISOXAZOLE-3-CARBOXAMIDE
DB06961, 5-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-[4-(morpholin-4-ylmethyl)phenyl]isoxazole-3-carboxamide
DB06958, 5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-N-ETHYL-4-PIPERAZIN-1-YL-1H-PYRAZOLE-3-CARBOXAMIDE
DB07319, 6-(3-BROMO-2-NAPHTHYL)-1,3,5-TRIAZINE-2,4-DIAMINE
DB03137, 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9-Pent-9h-Purin-6-Ylamine
DB03093, 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine
DB02550, 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-2-Fluoro-9-Pent-4-Ylnyl-9h-Purin-6-Ylamine
DB04505, 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-9-Pent-4-Ylnyl-9h-Purin-6-Ylamine
DB07877, 8-(6-BROMO-BENZO[1,3]DIOXOL-5-YLSULFANYL)-9-(3-ISOPROPYLAMINO-PROPYL)-ADENINE
DB04254, 8-Benzo[1,3]Dioxol-,5-Ylmethyl-9-Butyl-2-Fluoro-9h-Purin-6-Ylamine
DB08436, 8-BENZO[1,3]DIOXOL-,5-YLMETHYL-9-BUTYL-9H
DB04054, 9-Butyl-8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine
DB02359, 9-Butyl-8-(2,5-Dimethoxy-Benzyl)-9h-Purin-6-Ylamine
DB03504, 9-Butyl-8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-9h-Purin-6-Ylamine
DB02754, 9-Butyl-8-(3,4,5-Trimethoxybenzyl)-9h-Purin-6-Amine
DB03809, 9-Butyl-8-(3-Methoxybenzyl)-9h-Purin-6-Amine
DB03899, 9-Butyl-8-(4-Methoxybenzyl)-9h-Purin-6-Amine
DB12442, Alvespimycin
DB07594, CCT-018159
DB09130, Copper
DB02424, Geldanamycin
DB06956, N-(4-ACETYLPHENYL)-5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-1H-PYRAZOLE-4-CARBOXAMIDE
DB07325, N-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)METHYL]-3-{[(E)-(2-OXODIHYDROFURAN-3(2H)-YLIDENE)METHYL]AMINO}BENZENESULFONAMIDE
DB04588, N-[4-(AMINOSULFONYL)BENZYL]-5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-1H-PYRAZOLE-4-CARBOXAMIDE
DB00716, Nedocromil
DB09221, Polaprezinc
DB04216, Quercetin
DB00615, Rifabutin
DB06070, SNX-5422
DB05134, Tanespimycin
DrugCentraliP07900
GuidetoPHARMACOLOGYi2905

Protein family/group databases

MoonDBiP07900, Predicted

PTM databases

CarbonylDBiP07900
GlyConnecti1301, 1 N-Linked glycan (1 site)
GlyGeniP07900, 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site)
iPTMnetiP07900
MetOSiteiP07900
PhosphoSitePlusiP07900
SwissPalmiP07900

Genetic variation databases

BioMutaiHSP90AA1
DMDMi92090606

2D gel databases

OGPiP07900
REPRODUCTION-2DPAGEiIPI00784295

Proteomic databases

EPDiP07900
jPOSTiP07900
MassIVEiP07900
MaxQBiP07900
PaxDbiP07900
PeptideAtlasiP07900
PRIDEiP07900
ProteomicsDBi52031 [P07900-1]
52032 [P07900-2]
TopDownProteomicsiP07900-1 [P07900-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3676, 1853 antibodies from 44 providers

The DNASU plasmid repository

More...DNASUi		3320

Genome annotation databases

EnsembliENST00000216281.13; ENSP00000216281.8; ENSG00000080824.19
ENST00000334701.11; ENSP00000335153.7; ENSG00000080824.19 [P07900-2]
GeneIDi3320
KEGGihsa:3320
MANE-SelectiENST00000216281.13; ENSP00000216281.8; NM_005348.4; NP_005339.3
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
HPAiENSG00000080824, Tissue enhanced (brain)
MIMi140571, gene
neXtProtiNX_P07900
OpenTargetsiENSG00000080824
PharmGKBiPA29519
VEuPathDBiHostDB:ENSG00000080824

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0019, Eukaryota
GeneTreeiENSGT01020000230401
HOGENOMiCLU_006684_1_3_1
InParanoidiP07900
OMAiAHDQPME
OrthoDBi188544at2759
PhylomeDBiP07900
TreeFamiTF300686

Enzyme and pathway databases

BRENDAi3.6.4.10, 2681
PathwayCommonsiP07900
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-168928, DDX58/IFIH1-mediated induction of interferon-alpha/beta
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) in the presence of ligand
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-5675482, Regulation of necroptotic cell death
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, Extra-nuclear estrogen signaling
R-HSA-9013418, RHOBTB2 GTPase cycle
R-HSA-9018519, Estrogen-dependent gene expression
R-HSA-9613829, Chaperone Mediated Autophagy
R-HSA-9634285, Constitutive Signaling by Overexpressed ERBB2
R-HSA-9646399, Aggrephagy
R-HSA-9652282, Drug-mediated inhibition of ERBB2 signaling
R-HSA-9664565, Signaling by ERBB2 KD Mutants
R-HSA-9665233, Resistance of ERBB2 KD mutants to trastuzumab
R-HSA-9665244, Resistance of ERBB2 KD mutants to sapitinib
R-HSA-9665245, Resistance of ERBB2 KD mutants to tesevatinib
R-HSA-9665246, Resistance of ERBB2 KD mutants to neratinib
R-HSA-9665247, Resistance of ERBB2 KD mutants to osimertinib
R-HSA-9665249, Resistance of ERBB2 KD mutants to afatinib
R-HSA-9665250, Resistance of ERBB2 KD mutants to AEE788
R-HSA-9665251, Resistance of ERBB2 KD mutants to lapatinib
R-HSA-9665348, Signaling by ERBB2 ECD mutants
R-HSA-9665686, Signaling by ERBB2 TMD/JMD mutants
R-HSA-9665737, Drug resistance in ERBB2 TMD/JMD mutants
R-HSA-9679191, Potential therapeutics for SARS
SignaLinkiP07900
SIGNORiP07900

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		3320, 37 hits in 1091 CRISPR screens

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
PharosiP07900, Tchem

Protein Ontology

More...PROi		PR:P07900
RNActiP07900, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000080824, Expressed in middle temporal gyrus and 265 other tissues
ExpressionAtlasiP07900, baseline and differential
GenevisibleiP07900, HS

Family and domain databases

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

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%5Fand%5Fisoforms">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: May 25, 2022
This is version 265 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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