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Entry version 258 (29 Sep 2021)
Sequence version 4 (23 Jan 2007)
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Protein

Heat shock protein HSP 90-beta

Gene

HSP90AB1

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 linked to its ATPase 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:16478993, PubMed:19696785).

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. 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. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. 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. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397).

Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385).

Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673).

Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823).

Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059).

3 Publications6 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. Upon ATP-binding, the N-terminal domain undergoes significant conformational changes and comes in contact to form an active closed conformation. 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.1 Publication

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

  1. KM=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 sitei46ATPBy similarity1
Binding sitei88ATP1
Binding sitei107ATPBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei126 – 127Cleaved under oxidative stress1 Publication2
Binding sitei133ATP; via amide nitrogenBy similarity1
Binding sitei392ATPBy 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

GO - Biological processi

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

Molecular functionChaperone
Biological processStress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.6.4.10, 2681

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
P08238

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-168928, DDX58/IFIH1-mediated induction of interferon-alpha/beta
R-HSA-2029482, Regulation of actin dynamics for phagocytic cup formation
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-399954, Sema3A PAK dependent Axon repulsion
R-HSA-5336415, Uptake and function of diphtheria toxin
R-HSA-6798695, Neutrophil degranulation
R-HSA-844456, The NLRP3 inflammasome
R-HSA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8937144, Aryl hydrocarbon receptor signalling
R-HSA-8939211, ESR-mediated signaling
R-HSA-9013418, RHOBTB2 GTPase cycle
R-HSA-9018519, Estrogen-dependent gene expression
R-HSA-9613829, Chaperone Mediated Autophagy
R-HSA-9660826, Purinergic signaling in leishmaniasis infection
R-HSA-9679191, Potential therapeutics for SARS

SIGNOR Signaling Network Open Resource

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SIGNORi
P08238

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P08238, Predicted

Transport Classification Database

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TCDBi
8.A.163.1.1, the hsp90/cdc37 (hsp90/cdc37) family

<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-beta
Short name:
HSP 90
Alternative name(s):
Heat shock 84 kDa
Short name:
HSP 84
Short name:
HSP84
<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:HSP90AB1Imported
Synonyms:HSP90B, HSPC2, HSPCB
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 6

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:5258, HSP90AB1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
140572, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P08238

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000096384

<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, Nucleus, Secreted

<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>Mutagenesisi42E → A: Strong ATP-binding. Strong interaction with HSF1, HIF1A, ERBB2, MET, KEAP1 and RHOBTB2. 1 Publication1
Mutagenesisi88D → A: Impaired ATP-binding. Strong interaction with HIF1A, MET, KEAP1 and RHOBTB2. Loss of interaction with HSF1 and ERBB2. 1 Publication1
Mutagenesisi226S → A: Increases the binding affinity for AHR; when associated with A-255. Increases AHR transcription activity; when associated with A-255. 1 Publication1
Mutagenesisi226S → E: No effect on the interaction with AHR; when associated with E-255. 1 Publication1
Mutagenesisi255S → A: Increases the binding affinity for AHR; when associated with A-226. Increases AHR transcription activity; when associated with A-226. 1 Publication1
Mutagenesisi255S → E: No effect on the interaction with AHR; when associated with E-226. 1 Publication1
Mutagenesisi301Y → F: Decreases interaction with NOS3 and SRC. impairs resists LPS-induced tyrosine phosphorylation. Does not block LPS-induced pp60src phosphorylation. 1 Publication1
Mutagenesisi531K → A: Highly decreases the signal of SMYD2-dependent HSP90AB1 methylation; when associated with A-574. Diminishes dimerized form; when associated with A-574. Reduces interaction with STIP1 or CDC37; when associated with A-574. 1 Publication1
Mutagenesisi574K → A: Decreases the signal of SMYD2-dependent HSP90AB1 methylation. Highly decreases the signal of SMYD2-dependent HSP90AB1 methylation; when associated with A-531. Diminishes dimerized form; when associated with A-531. Reduces interaction with STIP1 or CDC37; when associated with A-531. 1 Publication1
Mutagenesisi590C → A, N or D: Reduced ATPase activity and client protein activation. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
3326

Open Targets

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OpenTargetsi
ENSG00000096384

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29524

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P08238, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4303

Drug and drug target database

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DrugBanki
DB08293, (5E)-12-CHLORO-13,15-DIHYDROXY-4,7,8,9-TETRAHYDRO-2-BENZOXACYCLOTRIDECINE-1,10(3H,11H)-DIONE
DB08153, (5E)-14-CHLORO-15,17-DIHYDROXY-4,7,8,9,10,11-HEXAHYDRO-2-BENZOXACYCLOPENTADECINE-1,12(3H,13H)-DIONE
DB08292, (5Z)-12-CHLORO-13,15-DIHYDROXY-4,7,8,9-TETRAHYDRO-2-BENZOXACYCLOTRIDECINE-1,10(3H,11H)-DIONE
DB08346, (5Z)-13-CHLORO-14,16-DIHYDROXY-3,4,7,8,9,10-HEXAHYDRO-1H-2-BENZOXACYCLOTETRADECINE-1,11(12H)-DIONE
DB08465, 2-(3-AMINO-2,5,6-TRIMETHOXYPHENYL)ETHYL 5-CHLORO-2,4-DIHYDROXYBENZOATE
DB08045, 4-{4-[4-(3-AMINOPROPOXY)PHENYL]-1H-PYRAZOL-5-YL}-6-CHLOROBENZENE-1,3-DIOL
DB07877, 8-(6-BROMO-BENZO[1,3]DIOXOL-5-YLSULFANYL)-9-(3-ISOPROPYLAMINO-PROPYL)-ADENINE
DB02754, 9-Butyl-8-(3,4,5-Trimethoxybenzyl)-9h-Purin-6-Amine
DB07594, CCT-018159
DB02424, Geldanamycin
DB08464, METHYL 3-CHLORO-2-{3-[(2,5-DIHYDROXY-4-METHOXYPHENYL)AMINO]-3-OXOPROPYL}-4,6-DIHYDROXYBENZOATE
DB09221, Polaprezinc
DB03758, Radicicol
DB06070, SNX-5422
DB05134, Tanespimycin

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2907

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
HSP90AB1

Domain mapping of disease mutations (DMDM)

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DMDMi
17865718

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000629172 – 724Heat shock protein HSP 90-betaAdd BLAST723

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 residuei219N6-succinyllysineBy similarity1
Modified residuei226PhosphoserineCombined sources1
Modified residuei255PhosphoserineCombined sources1 Publication1
Modified residuei261PhosphoserineBy similarity1
Modified residuei297PhosphothreonineCombined sources1
Modified residuei301Phosphotyrosine; by SRC1 Publication1
Modified residuei305PhosphotyrosineBy similarity1
Modified residuei307PhosphoserineCombined sources1
Modified residuei399N6-malonyllysine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi434O-linked (GlcNAc) serineBy similarity1
Modified residuei435N6-acetyllysineCombined sources1
Modified residuei445PhosphoserineCombined sources1
Glycosylationi452O-linked (GlcNAc) serineBy similarity1
Modified residuei479PhosphothreonineCombined sources1
Modified residuei481N6-acetyllysineCombined sources1
Modified residuei484PhosphotyrosineBy similarity1
Modified residuei531N6-methylated lysine; alternate1 Publication1
Modified residuei531N6-succinyllysine; alternateBy similarity1
Modified residuei574N6-methylated lysine1 Publication1
Modified residuei577N6-succinyllysineBy similarity1
Modified residuei590S-nitrosocysteine1 Publication1
Modified residuei624N6-acetyllysineBy similarity1
Modified residuei669PhosphoserineCombined sources1
Modified residuei718Phosphoserine; by PLK2 and PLK31 Publication1

<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

Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro).1 Publication
ISGylated.1 Publication
S-nitrosylated; negatively regulates the ATPase activity.1 Publication
Phosphorylation at Tyr-301 by SRC is induced by lipopolysaccharide (PubMed:23585225). Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction (PubMed:15581363).2 Publications
Methylated by SMYD2; facilitates dimerization and chaperone complex formation; promotes cancer cell proliferation.1 Publication
Cleaved following oxidative stress resulting in HSP90AB1 protein radicals formation; disrupts the chaperoning function and the degradation of its client proteins.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P08238

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P08238

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P08238

MaxQB - The MaxQuant DataBase

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MaxQBi
P08238

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

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PaxDbi
P08238

PeptideAtlas

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PeptideAtlasi
P08238

PRoteomics IDEntifications database

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PRIDEi
P08238

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
52096

Consortium for Top Down Proteomics

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TopDownProteomicsi
P08238

2D gel databases

USC-OGP 2-DE database

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OGPi
P08238

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P08238

GlyConnect protein glycosylation platform

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GlyConnecti
1302, 2 N-Linked glycans (2 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

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GlyGeni
P08238, 5 sites, 2 N-linked glycans (2 sites), 2 O-linked glycans (1 site)

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P08238

MetOSite database of methionine sulfoxide sites

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MetOSitei
P08238

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

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PhosphoSitePlusi
P08238

SwissPalm database of S-palmitoylation events

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SwissPalmi
P08238

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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By heat shock.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000096384, Expressed in hypothalamus and 252 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P08238, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P08238, HS

Organism-specific databases

Human Protein Atlas

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HPAi
ENSG00000096384, Low tissue specificity

<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

Monomer (PubMed:24880080). Homodimer (PubMed:7588731, PubMed:18400751).

Forms a complex with CDK6 and CDC37 (PubMed:9482106, PubMed:25486457).

Interacts with UNC45A; binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer (PubMed:16478993).

Interacts with CHORDC1 (By similarity).

Interacts with DNAJC7 (PubMed:18620420).

Interacts with FKBP4 (PubMed:15159550). May interact with NWD1 (PubMed:24681825).

Interacts with SGTA (PubMed:16580629).

Interacts with HSF1 in an ATP-dependent manner.

Interacts with MET; the interaction suppresses MET kinase activity.

Interacts with ERBB2 in an ATP-dependent manner; the interaction suppresses ERBB2 kinase activity.

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

Interacts with STUB1 and SMAD3 (PubMed:24613385).

Interacts with XPO1 and AHSA1 (PubMed:22022502, PubMed:25486457).

Interacts with BIRC2 (PubMed:25486457).

Interacts with KCNQ4; promotes cell surface expression of KCNQ4 (PubMed:23431407).

Interacts with BIRC2; prevents auto-ubiquitination and degradation of its client protein BIRC2 (PubMed:18239673).

Interacts with NOS3 (PubMed:23585225).

Interacts with AHR; interaction is inhibited by HSP90AB1 phosphorylation on Ser-226 and Ser-255 (PubMed:15581363).

Interacts with STIP1 and CDC37; upon SMYD2-dependent methylation (PubMed:24880080).

Interacts with JAK2 and PRKCE; promotes functional activation in a heat shock-dependent manner (PubMed:20353823).

Interacts with HSP90AA1; interaction is constitutive (PubMed:20353823). HSP90AB1-CDC37 chaperone complex interacts with inactive MAPK7 (via N-terminal half) in resting cells; the interaction is MAP2K5-independent and prevents from ubiquitination and proteasomal degradation (PubMed:23428871).

Interacts with CDC25A; prevents heat shock-mediated CDC25A degradation and contributes to cell cycle progression (PubMed:22843495).

Interacts with TP53 (via DNA binding domain); suppresses TP53 aggregation and prevents from irreversible thermal inactivation (PubMed:15358771).

Interacts with TGFB1 processed form (LAP); inhibits latent TGFB1 activation (PubMed:20599762).

Interacts with TRIM8; prevents nucleus translocation of phosphorylated STAT3 and HSP90AB1 (By similarity).

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

Interacts with PDCL3 (By similarity).

Interacts with TTC4 (via TPR repeats) (PubMed:18320024).

Interacts with IL1B; the interaction facilitates cargo translocation into the ERGIC (PubMed:32272059).

By similarity24 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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

P08238
With#Exp.IntAct
ACVR1B [P36896]2EBI-352572,EBI-1384128
AGO1 [Q9UL18]3EBI-352572,EBI-527363
AHSA1 [O95433]4EBI-352572,EBI-448610
AIP [O00170]8EBI-352572,EBI-704197
AKT1 [P31749]3EBI-352572,EBI-296087
AKT2 [P31751]2EBI-352572,EBI-296058
ALK [Q9UM73]2EBI-352572,EBI-357361
AMHR2 [Q16671]2EBI-352572,EBI-6423788
AMPD3 [Q01432]2EBI-352572,EBI-1223554
ARAF [P10398]8EBI-352572,EBI-365961
AURKB [Q96GD4]4EBI-352572,EBI-624291
AXL [P30530]3EBI-352572,EBI-2850927
BLK [P51451]2EBI-352572,EBI-2105445
BMX [P51813]3EBI-352572,EBI-696657
BRAF [P15056]4EBI-352572,EBI-365980
BTK [Q06187]2EBI-352572,EBI-624835
CAMK2A [Q9UQM7]3EBI-352572,EBI-1383687
CAMK2G [Q13555]2EBI-352572,EBI-1383465
CDC37 [Q16543]11EBI-352572,EBI-295634
CDC37L1 [Q7L3B6]5EBI-352572,EBI-2841876
CDK10 [Q15131]2EBI-352572,EBI-1646959
CDK14 [O94921]2EBI-352572,EBI-1043945
CDK15 [Q96Q40]2EBI-352572,EBI-1051975
CDK3 [Q00526]2EBI-352572,EBI-1245761
CDK4 [P11802]4EBI-352572,EBI-295644
CDK6 [Q00534]2EBI-352572,EBI-295663
CDK7 [P50613]2EBI-352572,EBI-1245958
CDK9 [P50750]2EBI-352572,EBI-1383449
CHEK1 [O14757]3EBI-352572,EBI-974488
CHORDC1 [Q9UHD1]6EBI-352572,EBI-2550959
CILK1 [Q9UPZ9]2EBI-352572,EBI-6381479
CSNK1E [P49674]2EBI-352572,EBI-749343
CUL1 [Q13616]2EBI-352572,EBI-359390
CUL2 [Q13617]2EBI-352572,EBI-456179
CUL3 [Q13618]3EBI-352572,EBI-456129
CUL4A [Q13619]2EBI-352572,EBI-456106
CUL4B [Q13620]2EBI-352572,EBI-456067
DDR2 [Q16832]2EBI-352572,EBI-1381484
EGFR [P00533]10EBI-352572,EBI-297353
EPHA2 [P29317]2EBI-352572,EBI-702104
ERBB2 [P04626]4EBI-352572,EBI-641062
ERBB3 [P21860]3EBI-352572,EBI-720706
ERBB4 [Q15303]2EBI-352572,EBI-80371
FAM162A [Q96A26]3EBI-352572,EBI-6123466
FBXL2 [Q9UKC9]2EBI-352572,EBI-724253
FBXO24 [O75426]2EBI-352572,EBI-6425658
FBXW2 [Q9UKT8]2EBI-352572,EBI-914727
FGFR1 [P11362]2EBI-352572,EBI-1028277
FGFR3 [P22607]2EBI-352572,EBI-348399
FGR [P09769]4EBI-352572,EBI-1383732
FKBP4 [Q02790]6EBI-352572,EBI-1047444
FKBP5 [Q13451]16EBI-352572,EBI-306914
FLT4 [P35916]2EBI-352572,EBI-1005467
FYN [P06241]4EBI-352572,EBI-515315
GSK3A [P49840]3EBI-352572,EBI-1044067
HASPIN [Q8TF76]2EBI-352572,EBI-1237328
HCK [P08631]3EBI-352572,EBI-346340
itself4EBI-352572,EBI-352572
IKBKE [Q14164]2EBI-352572,EBI-307369
IKBKG [Q9Y6K9]3EBI-352572,EBI-81279
ITK [Q08881]2EBI-352572,EBI-968552
KLHL38 [Q2WGJ6]3EBI-352572,EBI-6426443
LCK [P06239]4EBI-352572,EBI-1348
LIMK2 [P53671]2EBI-352572,EBI-1384350
LYN [P07948]2EBI-352572,EBI-79452
MAGEB6 [Q8N7X4]3EBI-352572,EBI-6447163
MAP2K5 [Q13163]3EBI-352572,EBI-307294
MAP3K14 [Q99558]4EBI-352572,EBI-358011
MAP3K8 [P41279]2EBI-352572,EBI-354900
MAP3K9 [P80192]2EBI-352572,EBI-3951604
MAP4K1 [Q92918]3EBI-352572,EBI-881
MAPK4 [P31152]2EBI-352572,EBI-3906061
MAPT - isoform Tau-F [P10636-8]11EBI-352572,EBI-366233
MATK [P42679]2EBI-352572,EBI-751664
MUSK [O15146]2EBI-352572,EBI-6423196
MYLK2 [Q9H1R3]3EBI-352572,EBI-356910
MYLK4 [Q86YV6]2EBI-352572,EBI-6424604
NEK9 [Q8TD19]2EBI-352572,EBI-1044009
NR1I2 [O75469]2EBI-352572,EBI-3905991
PDIK1L [Q8N165]2EBI-352572,EBI-6423298
POGK [Q9P215]2EBI-352572,EBI-2555775
PPP5C [P53041]7EBI-352572,EBI-716663
PRKAA1 [Q13131]2EBI-352572,EBI-1181405
PRKACB [P22694]2EBI-352572,EBI-2679622
PRKCE [Q02156]4EBI-352572,EBI-706254
PRKCG [P05129]2EBI-352572,EBI-949799
PRKCZ [Q05513]2EBI-352572,EBI-295351
PRKD1 [Q15139]2EBI-352572,EBI-1181072
PRKN [O60260]2EBI-352572,EBI-716346
PRKX [P51817]2EBI-352572,EBI-4302903
PSKH1 [P11801]2EBI-352572,EBI-3922781
PSKH2 [Q96QS6]2EBI-352572,EBI-6424813
PTGES3 [Q15185]4EBI-352572,EBI-1049387
PTK6 [Q13882]3EBI-352572,EBI-1383632
RAF1 [P04049]5EBI-352572,EBI-365996
RGS6 [P49758]2EBI-352572,EBI-6426927
ROR2 [Q01974]2EBI-352572,EBI-6422642
RPL11 [P62913]2EBI-352572,EBI-354380
RPS6KA1 [Q15418]4EBI-352572,EBI-963034
RPS6KA3 [P51812]3EBI-352572,EBI-1046616
STIP1 [P31948]4EBI-352572,EBI-1054052
STK11 [Q15831]4EBI-352572,EBI-306838
STK38 [Q15208]2EBI-352572,EBI-458376
STUB1 [Q9UNE7]5EBI-352572,EBI-357085
SUGT1 - isoform 2 [Q9Y2Z0-2]2EBI-352572,EBI-10768076
TBK1 [Q9UHD2]2EBI-352572,EBI-356402
TESK2 [Q96S53]2EBI-352572,EBI-1384110
TNK2 [Q07912]3EBI-352572,EBI-603457
TSSK6 [Q9BXA6]3EBI-352572,EBI-851883
TTC4 [O95801]5EBI-352572,EBI-1050890
TYK2 [P29597]2EBI-352572,EBI-1383454
UNC45B [Q8IWX7]2EBI-352572,EBI-9363363
YES1 [P07947]3EBI-352572,EBI-515331

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
109558, 537 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3285, HSP90B-CDC37 chaperone complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P08238

Database of interacting proteins

More...
DIPi
DIP-413N

Protein interaction database and analysis system

More...
IntActi
P08238, 567 interactors

Molecular INTeraction database

More...
MINTi
P08238

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000360609

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P08238

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P08238, 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

1724
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
P08238

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
P08238

<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>Regioni2 – 527Interaction with TP531 PublicationAdd BLAST526
Regioni2 – 214Interaction with BIRC21 PublicationAdd BLAST213
Regioni9 – 231Interaction with NR3C1By similarityAdd BLAST223
Regioni215 – 552Interaction with AHSA11 PublicationAdd BLAST338
Regioni222 – 270DisorderedSequence analysisAdd BLAST49
Regioni264 – 608Interaction with NR3C1By similarityAdd BLAST345
Regioni620 – 723Interaction with NR1D1By similarityAdd BLAST104
Regioni696 – 724DisorderedSequence analysisAdd BLAST29

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>Motifi720 – 724TPR repeat-binding5

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 biasi241 – 270Basic and acidic residuesSequence analysisAdd BLAST30

<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.By similarity

<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
P08238

Identification of Orthologs from Complete Genome Data

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OMAi
TRMKAEQ

Database of Orthologous Groups

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OrthoDBi
924636at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P08238

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

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...
IDEALi
IID00536

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

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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>Sequencei

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

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P08238-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA
60 70 80 90 100
LDKIRYESLT DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN
110 120 130 140 150
NLGTIAKSGT KAFMEALQAG ADISMIGQFG VGFYSAYLVA EKVVVITKHN
160 170 180 190 200
DDEQYAWESS AGGSFTVRAD HGEPIGRGTK VILHLKEDQT EYLEERRVKE
210 220 230 240 250
VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE DKDDEEKPKI
260 270 280 290 300
EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE
310 320 330 340 350
YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK
360 370 380 390 400
NNIKLYVRRV FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI
410 420 430 440 450
LKVIRKNIVK KCLELFSELA EDKENYKKFY EAFSKNLKLG IHEDSTNRRR
460 470 480 490 500
LSELLRYHTS QSGDEMTSLS EYVSRMKETQ KSIYYITGES KEQVANSAFV
510 520 530 540 550
ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG LELPEDEEEK
560 570 580 590 600
KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA
610 620 630 640 650
NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA
660 670 680 690 700
VKDLVVLLFE TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVAAEEP
710 720
NAAVPDEIPP LEGDEDASRM EEVD
Length:724
Mass (Da):83,264
Last modified:January 23, 2007 - v4
<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:iA93118C214D03810
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAD14062 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence CAB66478 differs from that shown. Reason: Frameshift.Curated

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 conflicti147T → R in AAA36025 (PubMed:3301534).Curated1
Sequence conflicti177R → M in AAA36025 (PubMed:3301534).Curated1
Sequence conflicti403V → A in CAB66478 (PubMed:11230166).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_049624349K → E. Corresponds to variant dbSNP:rs11538975Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M16660 mRNA Translation: AAA36025.1
J04988 Genomic DNA Translation: AAA36026.1
AY359878 mRNA Translation: AAQ63401.1
AL136543 mRNA Translation: CAB66478.1 Frameshift.
AK312255 mRNA Translation: BAG35187.1
DQ314872 Genomic DNA Translation: ABC40731.1
AL139392 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX04257.1
BC004928 mRNA Translation: AAH04928.1
BC009206 mRNA Translation: AAH09206.2
BC012807 mRNA Translation: AAH12807.1
BC014485 mRNA Translation: AAH14485.1
BC016753 mRNA Translation: AAH16753.1
BC068474 mRNA Translation: AAH68474.1
AH007358 Genomic DNA Translation: AAD14062.3 Different initiation.
AF275719 mRNA Translation: AAF82792.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS4909.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A29461, HHHU84
T46243

NCBI Reference Sequences

More...
RefSeqi
NP_001258898.1, NM_001271969.1
NP_001258899.1, NM_001271970.1
NP_001258900.1, NM_001271971.1
NP_031381.2, NM_007355.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000353801; ENSP00000325875; ENSG00000096384
ENST00000371554; ENSP00000360609; ENSG00000096384
ENST00000371646; ENSP00000360709; ENSG00000096384
ENST00000620073; ENSP00000481908; ENSG00000096384

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3326

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3326

UCSC genome browser

More...
UCSCi
uc003oxa.3, human

<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
M16660 mRNA Translation: AAA36025.1
J04988 Genomic DNA Translation: AAA36026.1
AY359878 mRNA Translation: AAQ63401.1
AL136543 mRNA Translation: CAB66478.1 Frameshift.
AK312255 mRNA Translation: BAG35187.1
DQ314872 Genomic DNA Translation: ABC40731.1
AL139392 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX04257.1
BC004928 mRNA Translation: AAH04928.1
BC009206 mRNA Translation: AAH09206.2
BC012807 mRNA Translation: AAH12807.1
BC014485 mRNA Translation: AAH14485.1
BC016753 mRNA Translation: AAH16753.1
BC068474 mRNA Translation: AAH68474.1
AH007358 Genomic DNA Translation: AAD14062.3 Different initiation.
AF275719 mRNA Translation: AAF82792.1
CCDSiCCDS4909.1
PIRiA29461, HHHU84
T46243
RefSeqiNP_001258898.1, NM_001271969.1
NP_001258899.1, NM_001271970.1
NP_001258900.1, NM_001271971.1
NP_031381.2, NM_007355.3

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
1QZ2X-ray3.00G/H720-724[»]
1UYMX-ray2.45A2-221[»]
2L6JNMR-B720-724[»]
3FWVX-ray2.20C/D719-723[»]
3NMQX-ray2.20A1-223[»]
3PRYX-ray2.28A/B/C284-543[»]
3UQ3X-ray2.60B/C720-724[»]
5FWKelectron microscopy3.90A/B1-724[»]
5FWLelectron microscopy9.00A/B1-724[»]
5FWMelectron microscopy8.00A/B1-724[»]
5FWPelectron microscopy7.20A/B1-724[»]
5UC4X-ray2.05A/B/C/D1-218[»]
5UCHX-ray2.65A/B/C/D1-218[»]
5UCIX-ray2.70A/B/C/D1-218[»]
5UCJX-ray1.69A/B/C/D1-218[»]
6N8WX-ray3.09A/B/C/D1-231[»]
6N8YX-ray1.55A1-221[»]
SMRiP08238
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi109558, 537 interactors
ComplexPortaliCPX-3285, HSP90B-CDC37 chaperone complex
CORUMiP08238
DIPiDIP-413N
IntActiP08238, 567 interactors
MINTiP08238
STRINGi9606.ENSP00000360609

Chemistry databases

BindingDBiP08238
ChEMBLiCHEMBL4303
DrugBankiDB08293, (5E)-12-CHLORO-13,15-DIHYDROXY-4,7,8,9-TETRAHYDRO-2-BENZOXACYCLOTRIDECINE-1,10(3H,11H)-DIONE
DB08153, (5E)-14-CHLORO-15,17-DIHYDROXY-4,7,8,9,10,11-HEXAHYDRO-2-BENZOXACYCLOPENTADECINE-1,12(3H,13H)-DIONE
DB08292, (5Z)-12-CHLORO-13,15-DIHYDROXY-4,7,8,9-TETRAHYDRO-2-BENZOXACYCLOTRIDECINE-1,10(3H,11H)-DIONE
DB08346, (5Z)-13-CHLORO-14,16-DIHYDROXY-3,4,7,8,9,10-HEXAHYDRO-1H-2-BENZOXACYCLOTETRADECINE-1,11(12H)-DIONE
DB08465, 2-(3-AMINO-2,5,6-TRIMETHOXYPHENYL)ETHYL 5-CHLORO-2,4-DIHYDROXYBENZOATE
DB08045, 4-{4-[4-(3-AMINOPROPOXY)PHENYL]-1H-PYRAZOL-5-YL}-6-CHLOROBENZENE-1,3-DIOL
DB07877, 8-(6-BROMO-BENZO[1,3]DIOXOL-5-YLSULFANYL)-9-(3-ISOPROPYLAMINO-PROPYL)-ADENINE
DB02754, 9-Butyl-8-(3,4,5-Trimethoxybenzyl)-9h-Purin-6-Amine
DB07594, CCT-018159
DB02424, Geldanamycin
DB08464, METHYL 3-CHLORO-2-{3-[(2,5-DIHYDROXY-4-METHOXYPHENYL)AMINO]-3-OXOPROPYL}-4,6-DIHYDROXYBENZOATE
DB09221, Polaprezinc
DB03758, Radicicol
DB06070, SNX-5422
DB05134, Tanespimycin
GuidetoPHARMACOLOGYi2907

Protein family/group databases

MoonDBiP08238, Predicted
TCDBi8.A.163.1.1, the hsp90/cdc37 (hsp90/cdc37) family

PTM databases

CarbonylDBiP08238
GlyConnecti1302, 2 N-Linked glycans (2 sites)
GlyGeniP08238, 5 sites, 2 N-linked glycans (2 sites), 2 O-linked glycans (1 site)
iPTMnetiP08238
MetOSiteiP08238
PhosphoSitePlusiP08238
SwissPalmiP08238

Genetic variation databases

BioMutaiHSP90AB1
DMDMi17865718

2D gel databases

OGPiP08238

Proteomic databases

EPDiP08238
jPOSTiP08238
MassIVEiP08238
MaxQBiP08238
PaxDbiP08238
PeptideAtlasiP08238
PRIDEiP08238
ProteomicsDBi52096
TopDownProteomicsiP08238

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
P08238, 1 sequenced antibody

Antibodypedia a portal for validated antibodies

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Antibodypediai
3929, 1727 antibodies

The DNASU plasmid repository

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DNASUi
3326

Genome annotation databases

EnsembliENST00000353801; ENSP00000325875; ENSG00000096384
ENST00000371554; ENSP00000360609; ENSG00000096384
ENST00000371646; ENSP00000360709; ENSG00000096384
ENST00000620073; ENSP00000481908; ENSG00000096384
GeneIDi3326
KEGGihsa:3326
UCSCiuc003oxa.3, human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3326
DisGeNETi3326

GeneCards: human genes, protein and diseases

More...
GeneCardsi
HSP90AB1
HGNCiHGNC:5258, HSP90AB1
HPAiENSG00000096384, Low tissue specificity
MIMi140572, gene
neXtProtiNX_P08238
OpenTargetsiENSG00000096384
PharmGKBiPA29524
VEuPathDBiHostDB:ENSG00000096384

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0019, Eukaryota
GeneTreeiENSGT01020000230401
HOGENOMiCLU_006684_1_3_1
InParanoidiP08238
OMAiTRMKAEQ
OrthoDBi924636at2759
PhylomeDBiP08238
TreeFamiTF300686

Enzyme and pathway databases

BRENDAi3.6.4.10, 2681
PathwayCommonsiP08238
ReactomeiR-HSA-168928, DDX58/IFIH1-mediated induction of interferon-alpha/beta
R-HSA-2029482, Regulation of actin dynamics for phagocytic cup formation
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-399954, Sema3A PAK dependent Axon repulsion
R-HSA-5336415, Uptake and function of diphtheria toxin
R-HSA-6798695, Neutrophil degranulation
R-HSA-844456, The NLRP3 inflammasome
R-HSA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8937144, Aryl hydrocarbon receptor signalling
R-HSA-8939211, ESR-mediated signaling
R-HSA-9013418, RHOBTB2 GTPase cycle
R-HSA-9018519, Estrogen-dependent gene expression
R-HSA-9613829, Chaperone Mediated Autophagy
R-HSA-9660826, Purinergic signaling in leishmaniasis infection
R-HSA-9679191, Potential therapeutics for SARS
SIGNORiP08238

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
3326, 110 hits in 1039 CRISPR screens

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

More...
ChiTaRSi
HSP90AB1, human
EvolutionaryTraceiP08238

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
HSP90AB1

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

More...
GenomeRNAii
3326
PharosiP08238, Tchem

Protein Ontology

More...
PROi
PR:P08238
RNActiP08238, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000096384, Expressed in hypothalamus and 252 other tissues
ExpressionAtlasiP08238, baseline and differential
GenevisibleiP08238, HS

Family and domain databases

Gene3Di1.20.120.790, 1 hit
3.30.565.10, 1 hit
HAMAPiMF_00505, HSP90, 1 hit
IDEALiIID00536
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 nameiHS90B_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: P08238
Secondary accession number(s): B2R5P0
, Q5T9W7, Q9NQW0, Q9NTK6
<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: September 29, 2021
This is version 258 of the entry and version 4 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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