UniProtKB - P07900 (HS90A_HUMAN)
Heat shock protein HSP 90-alpha
HSP90AA1
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 PublicationCatalytic activityi
- EC:3.6.4.101 Publication
Activity regulationi
Kineticsi
- KM=300 µM for ATP1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 51 | ATP | 1 | |
Binding sitei | 93 | ATP | 1 | |
Binding sitei | 112 | ATPBy similarity | 1 | |
Binding sitei | 138 | ATP; via amide nitrogen | 1 | |
Binding sitei | 400 | ATPBy similarity | 1 |
GO - Molecular functioni
- ATP binding Source: UniProtKB
- ATP hydrolysis activity Source: UniProtKB
- disordered domain specific binding Source: CAFA
- DNA polymerase binding Source: BHF-UCL
- GTPase binding Source: UniProtKB
- histone deacetylase binding Source: BHF-UCL
- identical protein binding Source: UniProtKB
- MHC class II protein complex binding Source: UniProtKB
- nitric-oxide synthase regulator activity Source: UniProtKB
- protein folding chaperone Source: Ensembl
- protein homodimerization activity Source: UniProtKB
- protein tyrosine kinase binding Source: UniProtKB
- RNA binding Source: UniProtKB
- scaffold protein binding Source: UniProtKB
- tau protein binding Source: ARUK-UCL
- TPR domain binding Source: UniProtKB
- ubiquitin protein ligase binding Source: ARUK-UCL
- unfolded protein binding Source: GO_Central
GO - Biological processi
- activation of innate immune response Source: UniProtKB
- axon extension Source: ARUK-UCL
- cellular response to heat Source: GO_Central
- cellular response to virus Source: UniProtKB
- central nervous system neuron axonogenesis Source: ARUK-UCL
- chaperone-mediated autophagy Source: ParkinsonsUK-UCL
- chaperone-mediated protein complex assembly Source: BHF-UCL
- establishment of cell polarity Source: ARUK-UCL
- mitochondrial transport Source: UniProtKB
- positive regulation of cellular protein catabolic process Source: ARUK-UCL
- positive regulation of defense response to virus by host Source: UniProtKB
- positive regulation of interferon-beta production Source: UniProtKB
- positive regulation of nitric oxide biosynthetic process Source: UniProtKB
- positive regulation of peptidyl-serine phosphorylation Source: ARUK-UCL
- positive regulation of protein kinase B signaling Source: ARUK-UCL
- positive regulation of protein phosphorylation Source: ARUK-UCL
- positive regulation of protein polymerization Source: ARUK-UCL
- positive regulation of tau-protein kinase activity Source: ARUK-UCL
- positive regulation of telomerase activity Source: BHF-UCL
- protein folding Source: GO_Central
- protein insertion into mitochondrial outer membrane Source: BHF-UCL
- protein refolding Source: UniProtKB
- protein stabilization Source: UniProtKB
- protein unfolding Source: ParkinsonsUK-UCL
- regulation of apoptotic process Source: UniProtKB
- regulation of protein-containing complex assembly Source: ParkinsonsUK-UCL
- regulation of protein localization Source: ARUK-UCL
- regulation of protein ubiquitination Source: BHF-UCL
- response to antibiotic Source: AgBase
- response to cold Source: AgBase
- response to heat Source: AgBase
- response to unfolded protein Source: UniProtKB
- telomerase holoenzyme complex assembly Source: BHF-UCL
- telomere maintenance via telomerase Source: BHF-UCL
Keywordsi
Molecular function | Chaperone, Hydrolase |
Biological process | Host-virus interaction, Stress response |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 3.6.4.10, 2681 |
PathwayCommonsi | P07900 |
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 |
SignaLinki | P07900 |
SIGNORi | P07900 |
Protein family/group databases
MoonDBi | P07900, Predicted |
Names & Taxonomyi
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 |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:5253, HSP90AA1 |
MIMi | 140571, gene |
neXtProti | NX_P07900 |
VEuPathDBi | HostDB:ENSG00000080824 |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Plasma membrane
- Cell membrane 1 Publication
Mitochondrion
- Mitochondrion 1 Publication
Nucleus
- Nucleus By similarity
Other locations
- Melanosome 1 Publication
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Cytosol
- cytosol Source: GO_Central
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
- extracellular region Source: Reactome
Lysosome
- lysosomal lumen Source: ParkinsonsUK-UCL
Mitochondrion
- mitochondrion Source: UniProtKB
Nucleus
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB
Plasma Membrane
- plasma membrane Source: GO_Central
Other locations
- axonal growth cone Source: ARUK-UCL
- cytoplasm Source: CAFA
- dendritic growth cone Source: ARUK-UCL
- endocytic vesicle lumen Source: Reactome
- ficolin-1-rich granule lumen Source: Reactome
- melanosome Source: UniProtKB-SubCell
- membrane Source: UniProtKB
- myelin sheath Source: GO_Central
- neuronal cell body Source: ARUK-UCL
- perinuclear region of cytoplasm Source: ARUK-UCL
- protein-containing complex Source: UniProtKB
- secretory granule lumen Source: Reactome
Keywords - Cellular componenti
Cell membrane, Cytoplasm, Membrane, Mitochondrion, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 47 | E → A: Strong ATP-binding. Strong interaction with HSF1, HIF1A, ERBB2, MET, KEAP1 and RHOBTB2. No effect on interaction with TSC1. 2 Publications | 1 | |
Mutagenesisi | 93 | D → 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 Publications | 1 | |
Mutagenesisi | 97 | G → D: Abolishes ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 313 | Y → E: Loss of interaction with TSC1 and increases interacrion with AHSA1. 1 Publication | 1 | |
Mutagenesisi | 313 | Y → F: No deffect on the interaction with TSC1. 1 Publication | 1 | |
Mutagenesisi | 598 | C → A, N or D: Reduces ATPase activity and client protein activation. 2 Publications | 1 | |
Mutagenesisi | 598 | C → S: Loss of S-nitrosylation. 2 Publications | 1 | |
Mutagenesisi | 728 – 732 | MEEVD → AAAA: Loss of interaction with TOMM70. No effect on interaction with IRF3. 1 Publication | 5 | |
Mutagenesisi | 728 – 732 | Missing : Loss of interaction with TSC1. 1 Publication | 5 | |
Mutagenesisi | 729 – 732 | Missing : Loss of interaction with TOMM70. 1 Publication | 4 | |
Mutagenesisi | 731 – 732 | VD → AA: Loss of interaction with TOMM70. No effect on interaction with IRF3. 2 Publications | 2 |
Organism-specific databases
DisGeNETi | 3320 |
OpenTargetsi | ENSG00000080824 |
PharmGKBi | PA29519 |
Miscellaneous databases
Pharosi | P07900, Tchem |
Chemistry databases
ChEMBLi | CHEMBL3880 |
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 |
DrugCentrali | P07900 |
GuidetoPHARMACOLOGYi | 2905 |
Genetic variation databases
BioMutai | HSP90AA1 |
DMDMi | 92090606 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000062911 | 2 – 732 | Heat shock protein HSP 90-alphaAdd BLAST | 731 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 5 | Phosphothreonine; by PRKDC1 Publication | 1 | |
Modified residuei | 7 | Phosphothreonine; by PRKDC1 Publication | 1 | |
Modified residuei | 58 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 84 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 231 | PhosphoserineCombined sources1 Publication | 1 | |
Modified residuei | 252 | PhosphoserineCombined sources | 1 | |
Modified residuei | 263 | PhosphoserineCombined sources1 Publication | 1 | |
Modified residuei | 313 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 443 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 453 | PhosphoserineBy similarity | 1 | |
Modified residuei | 458 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 476 | PhosphoserineCombined sources | 1 | |
Modified residuei | 489 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 492 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 585 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 598 | S-nitrosocysteine1 Publication | 1 | |
Modified residuei | 641 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugationProteomic databases
EPDi | P07900 |
jPOSTi | P07900 |
MassIVEi | P07900 |
MaxQBi | P07900 |
PaxDbi | P07900 |
PeptideAtlasi | P07900 |
PRIDEi | P07900 |
ProteomicsDBi | 52031 [P07900-1] 52032 [P07900-2] |
TopDownProteomicsi | P07900-1 [P07900-1] |
2D gel databases
OGPi | P07900 |
REPRODUCTION-2DPAGEi | IPI00784295 |
PTM databases
CarbonylDBi | P07900 |
GlyConnecti | 1301, 1 N-Linked glycan (1 site) |
GlyGeni | P07900, 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site) |
iPTMneti | P07900 |
MetOSitei | P07900 |
PhosphoSitePlusi | P07900 |
SwissPalmi | P07900 |
Expressioni
Gene expression databases
Bgeei | ENSG00000080824, Expressed in middle temporal gyrus and 265 other tissues |
ExpressionAtlasi | P07900, baseline and differential |
Genevisiblei | P07900, HS |
Organism-specific databases
HPAi | ENSG00000080824, Tissue enhanced (brain) |
Interactioni
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 PublicationBinary interactionsi
P07900
GO - Molecular functioni
- disordered domain specific binding Source: CAFA
- DNA polymerase binding Source: BHF-UCL
- GTPase binding Source: UniProtKB
- histone deacetylase binding Source: BHF-UCL
- identical protein binding Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- protein tyrosine kinase binding Source: UniProtKB
- scaffold protein binding Source: UniProtKB
- tau protein binding Source: ARUK-UCL
- TPR domain binding Source: UniProtKB
- ubiquitin protein ligase binding Source: ARUK-UCL
- unfolded protein binding Source: GO_Central
Protein-protein interaction databases
BioGRIDi | 109552, 1052 interactors |
ComplexPortali | CPX-3288, HSP90A-CDC37 chaperone complex |
CORUMi | P07900 |
DIPi | DIP-27595N |
IntActi | P07900, 387 interactors |
MINTi | P07900 |
STRINGi | 9606.ENSP00000335153 |
Chemistry databases
BindingDBi | P07900 |
Miscellaneous databases
RNActi | P07900, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P07900 |
BMRBi | P07900 |
SMRi | P07900 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P07900 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 9 – 236 | Interaction with NR3C1By similarityAdd BLAST | 228 | |
Regioni | 225 – 278 | DisorderedSequence analysisAdd BLAST | 54 | |
Regioni | 271 – 616 | Interaction with NR3C1By similarityAdd BLAST | 346 | |
Regioni | 284 – 732 | Interaction with FLCN and FNIP11 PublicationAdd BLAST | 449 | |
Regioni | 284 – 620 | Interaction with FNIP2 and TSC12 PublicationsAdd BLAST | 337 | |
Regioni | 628 – 731 | Interaction with NR1D1By similarityAdd BLAST | 104 | |
Regioni | 682 – 732 | Required for homodimerization1 PublicationAdd BLAST | 51 | |
Regioni | 700 – 732 | DisorderedSequence analysisAdd BLAST | 33 | |
Regioni | 728 – 732 | Essential for interaction with SMYD3, TSC1 and STIP1/HOP2 Publications | 5 | |
Regioni | 729 – 732 | Essential for interaction with SGTA and TTC11 Publication | 4 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 723 – 732 | TPR repeat-binding1 Publication | 10 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 243 – 257 | Basic and acidic residuesSequence analysisAdd BLAST | 15 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0019, Eukaryota |
GeneTreei | ENSGT01020000230401 |
HOGENOMi | CLU_006684_1_3_1 |
InParanoidi | P07900 |
OMAi | AHDQPME |
OrthoDBi | 188544at2759 |
PhylomeDBi | P07900 |
TreeFami | TF300686 |
Family and domain databases
Gene3Di | 1.20.120.790, 1 hit 3.30.565.10, 1 hit |
HAMAPi | MF_00505, HSP90, 1 hit |
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 |
PANTHERi | PTHR11528, PTHR11528, 1 hit |
Pfami | View protein in Pfam PF02518, HATPase_c, 1 hit PF00183, HSP90, 1 hit |
PIRSFi | PIRSF002583, Hsp90, 1 hit |
PRINTSi | PR00775, HEATSHOCK90 |
SMARTi | View protein in SMART SM00387, HATPase_c, 1 hit |
SUPFAMi | SSF110942, SSF110942, 1 hit SSF54211, SSF54211, 1 hit SSF55874, SSF55874, 1 hit |
PROSITEi | View protein in PROSITE PS00298, HSP90, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketG3V2J8 | G3V2J8_HUMAN | Heat shock protein HSP 90-alpha | HSP90AA1 | 174 | Annotation score: | ||
H0YJF5 | H0YJF5_HUMAN | Heat shock protein HSP 90-alpha | HSP90AA1 | 52 | Annotation score: | ||
G3V592 | G3V592_HUMAN | Heat shock protein HSP 90-alpha | HSP90AA1 | 80 | Annotation score: | ||
A0A0U1RR69 | A0A0U1RR69_HUMAN | Heat shock protein HSP 90-alpha | HSP90AA1 | 100 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 63 | S → T in CAA33259 (PubMed:2780322).Curated | 1 | |
Sequence conflicti | 74 | K → R in CAI64495 (PubMed:16269234).Curated | 1 | |
Sequence conflicti | 74 | K → R in BAG51711 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 86 | D → G in CAI64495 (PubMed:16269234).Curated | 1 | |
Sequence conflicti | 86 | D → G in BAG51711 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 162 | W → D AA sequence (PubMed:10409742).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
---|---|---|---|---|---|
Isoform 2 (identifier: P07900-2) | |||||
Natural variantiVAR_082835 | 71 | M → LCuratedCorresponds to variant dbSNP:rs8005905Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_026604 | 1 | M → MPPCSGGDGSTPPGPSLRDR DCPAQSAEYPRDRLDPRPGS PSEASSPPFLRSRAPVNWYQ EKAQVFLWHLMVSGSTTLLC LWKQPFHVSAFPVTASLAFR QSQGAGQHLYKDLQPFILLR LLM in isoform 2. 2 Publications | 1 |
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 |
CCDSi | CCDS32160.1 [P07900-2] CCDS9967.1 [P07900-1] |
PIRi | A32319, HHHU86 |
RefSeqi | NP_001017963.2, NM_001017963.2 [P07900-2] NP_005339.3, NM_005348.3 [P07900-1] |
Genome annotation databases
Ensembli | ENST00000216281.13; ENSP00000216281.8; ENSG00000080824.19 ENST00000334701.11; ENSP00000335153.7; ENSG00000080824.19 [P07900-2] |
GeneIDi | 3320 |
KEGGi | hsa:3320 |
MANE-Selecti | ENST00000216281.13; ENSP00000216281.8; NM_005348.4; NP_005339.3 |
UCSCi | uc001yku.5, human [P07900-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
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 |
CCDSi | CCDS32160.1 [P07900-2] CCDS9967.1 [P07900-1] |
PIRi | A32319, HHHU86 |
RefSeqi | NP_001017963.2, NM_001017963.2 [P07900-2] NP_005339.3, NM_005348.3 [P07900-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BYQ | X-ray | 1.50 | A | 9-236 | [»] | |
1OSF | X-ray | 1.75 | A | 9-223 | [»] | |
1UY6 | X-ray | 1.90 | A | 2-236 | [»] | |
1UY7 | X-ray | 1.90 | A | 2-236 | [»] | |
1UY8 | X-ray | 1.98 | A | 2-236 | [»] | |
1UY9 | X-ray | 2.00 | A | 2-236 | [»] | |
1UYC | X-ray | 2.00 | A | 2-236 | [»] | |
1UYD | X-ray | 2.20 | A | 2-236 | [»] | |
1UYE | X-ray | 2.00 | A | 2-236 | [»] | |
1UYF | X-ray | 2.00 | A | 2-236 | [»] | |
1UYG | X-ray | 2.00 | A | 2-236 | [»] | |
1UYH | X-ray | 2.20 | A | 2-236 | [»] | |
1UYI | X-ray | 2.20 | A | 2-236 | [»] | |
1UYK | X-ray | 2.20 | A | 2-236 | [»] | |
1UYL | X-ray | 1.40 | A | 2-236 | [»] | |
1YC1 | X-ray | 1.70 | A | 9-236 | [»] | |
1YC3 | X-ray | 2.12 | A | 9-236 | [»] | |
1YC4 | X-ray | 1.81 | A | 9-236 | [»] | |
1YER | X-ray | 1.65 | A | 9-236 | [»] | |
1YES | X-ray | 2.20 | A | 9-236 | [»] | |
1YET | X-ray | 1.90 | A | 9-236 | [»] | |
2BSM | X-ray | 2.05 | A | 2-236 | [»] | |
2BT0 | X-ray | 1.90 | A/B | 2-236 | [»] | |
2BUG | NMR | - | B | 728-732 | [»] | |
2BYH | X-ray | 1.90 | A | 11-236 | [»] | |
2BYI | X-ray | 1.60 | A | 11-236 | [»] | |
2BZ5 | X-ray | 1.90 | A/B | 2-236 | [»] | |
2C2L | X-ray | 3.30 | E/F/G/H | 724-732 | [»] | |
2CCS | X-ray | 1.79 | A | 1-236 | [»] | |
2CCT | X-ray | 2.30 | A | 1-236 | [»] | |
2CCU | X-ray | 2.70 | A | 1-236 | [»] | |
2FWY | X-ray | 2.10 | A | 1-236 | [»] | |
2FWZ | X-ray | 2.10 | A | 1-236 | [»] | |
2H55 | X-ray | 2.00 | A | 1-236 | [»] | |
2JJC | X-ray | 1.95 | A | 9-223 | [»] | |
2K5B | NMR | - | A | 14-223 | [»] | |
2QF6 | X-ray | 3.10 | A/B/C/D | 17-223 | [»] | |
2QFO | X-ray | 1.68 | A/B | 17-223 | [»] | |
2QG0 | X-ray | 1.85 | A/B | 17-223 | [»] | |
2QG2 | X-ray | 1.80 | A | 17-223 | [»] | |
2UWD | X-ray | 1.90 | A | 2-236 | [»] | |
2VCI | X-ray | 2.00 | A | 1-236 | [»] | |
2VCJ | X-ray | 2.50 | A | 1-236 | [»] | |
2WI1 | X-ray | 2.30 | A | 1-236 | [»] | |
2WI2 | X-ray | 2.09 | A/B | 1-236 | [»] | |
2WI3 | X-ray | 1.90 | A | 1-236 | [»] | |
2WI4 | X-ray | 2.40 | A | 1-236 | [»] | |
2WI5 | X-ray | 2.10 | A | 1-236 | [»] | |
2WI6 | X-ray | 2.18 | A | 1-236 | [»] | |
2WI7 | X-ray | 2.50 | A | 1-236 | [»] | |
2XAB | X-ray | 1.90 | A/B | 9-236 | [»] | |
2XDK | X-ray | 1.97 | A | 9-236 | [»] | |
2XDL | X-ray | 1.98 | A | 9-236 | [»] | |
2XDS | X-ray | 1.97 | A | 9-236 | [»] | |
2XDU | X-ray | 1.74 | A | 14-224 | [»] | |
2XDX | X-ray | 2.42 | A | 9-236 | [»] | |
2XHR | X-ray | 2.20 | A | 9-236 | [»] | |
2XHT | X-ray | 2.27 | A | 9-236 | [»] | |
2XHX | X-ray | 2.80 | A | 9-236 | [»] | |
2XJG | X-ray | 2.25 | A | 9-236 | [»] | |
2XJJ | X-ray | 1.90 | A/B | 9-236 | [»] | |
2XJX | X-ray | 1.66 | A | 9-236 | [»] | |
2XK2 | X-ray | 1.95 | A | 9-236 | [»] | |
2YE2 | X-ray | 1.90 | A | 9-236 | [»] | |
2YE3 | X-ray | 1.95 | A | 9-236 | [»] | |
2YE4 | X-ray | 2.30 | A | 9-236 | [»] | |
2YE5 | X-ray | 1.73 | A | 9-236 | [»] | |
2YE6 | X-ray | 2.56 | A | 9-236 | [»] | |
2YE7 | X-ray | 2.20 | A | 9-236 | [»] | |
2YE8 | X-ray | 2.30 | A | 9-236 | [»] | |
2YE9 | X-ray | 2.20 | A | 9-236 | [»] | |
2YEA | X-ray | 1.73 | A | 9-236 | [»] | |
2YEB | X-ray | 2.40 | A | 9-236 | [»] | |
2YEC | X-ray | 2.10 | A | 9-236 | [»] | |
2YED | X-ray | 2.10 | A | 9-236 | [»] | |
2YEE | X-ray | 2.30 | A | 9-236 | [»] | |
2YEF | X-ray | 1.55 | A | 9-236 | [»] | |
2YEG | X-ray | 2.50 | A/B | 9-236 | [»] | |
2YEH | X-ray | 2.10 | A | 9-236 | [»] | |
2YEI | X-ray | 2.20 | A | 9-236 | [»] | |
2YEJ | X-ray | 2.20 | A | 9-236 | [»] | |
2YI0 | X-ray | 1.60 | A | 1-229 | [»] | |
2YI5 | X-ray | 2.50 | A | 1-229 | [»] | |
2YI6 | X-ray | 1.80 | A | 1-229 | [»] | |
2YI7 | X-ray | 1.40 | A | 1-229 | [»] | |
2YJW | X-ray | 1.61 | A | 18-223 | [»] | |
2YJX | X-ray | 1.83 | A | 18-223 | [»] | |
2YK2 | X-ray | 1.74 | A | 18-223 | [»] | |
2YK9 | X-ray | 1.32 | A | 18-223 | [»] | |
2YKB | X-ray | 1.93 | A | 18-223 | [»] | |
2YKC | X-ray | 1.67 | A | 18-223 | [»] | |
2YKE | X-ray | 1.43 | A | 18-223 | [»] | |
2YKI | X-ray | 1.67 | A | 18-223 | [»] | |
2YKJ | X-ray | 1.46 | A | 18-223 | [»] | |
3B24 | X-ray | 1.70 | A/B | 9-236 | [»] | |
3B25 | X-ray | 1.75 | A | 9-236 | [»] | |
3B26 | X-ray | 2.10 | A/B | 9-236 | [»] | |
3B27 | X-ray | 1.50 | A | 9-236 | [»] | |
3B28 | X-ray | 1.35 | A/B | 9-236 | [»] | |
3BM9 | X-ray | 1.60 | A | 14-236 | [»] | |
3BMY | X-ray | 1.60 | A | 14-236 | [»] | |
3D0B | X-ray | 1.74 | A | 1-232 | [»] | |
3EKO | X-ray | 1.55 | A/B | 9-225 | [»] | |
3EKR | X-ray | 2.00 | A/B | 9-225 | [»] | |
3FT5 | X-ray | 1.90 | A | 9-236 | [»] | |
3FT8 | X-ray | 2.00 | A | 9-236 | [»] | |
3HEK | X-ray | 1.95 | A/B | 9-225 | [»] | |
3HHU | X-ray | 1.59 | A/B | 1-224 | [»] | |
3HYY | X-ray | 1.90 | A | 9-236 | [»] | |
3HYZ | X-ray | 2.30 | A/B | 9-236 | [»] | |
3HZ1 | X-ray | 2.30 | A | 9-236 | [»] | |
3HZ5 | X-ray | 1.90 | A | 9-236 | [»] | |
3INW | X-ray | 1.95 | A | 10-236 | [»] | |
3INX | X-ray | 1.75 | A | 10-236 | [»] | |
3K97 | X-ray | 1.95 | A | 9-236 | [»] | |
3K98 | X-ray | 2.40 | A/B | 9-225 | [»] | |
3K99 | X-ray | 2.10 | A/B/C/D | 9-225 | [»] | |
3MNR | X-ray | 1.90 | P | 1-232 | [»] | |
3O0I | X-ray | 1.47 | A | 1-236 | [»] | |
3OW6 | X-ray | 1.80 | A | 17-223 | [»] | |
3OWB | X-ray | 2.05 | A | 17-223 | [»] | |
3OWD | X-ray | 1.63 | A | 17-223 | [»] | |
3Q6M | X-ray | 3.00 | A/B/C | 293-732 | [»] | |
3Q6N | X-ray | 3.05 | A/B/C/D/E/F | 293-732 | [»] | |
3QDD | X-ray | 1.79 | A | 1-236 | [»] | |
3QTF | X-ray | 1.57 | A | 14-236 | [»] | |
3R4M | X-ray | 1.70 | A | 9-236 | [»] | |
3R4N | X-ray | 2.00 | A/B | 9-225 | [»] | |
3R4O | X-ray | 2.65 | A/B | 9-225 | [»] | |
3R4P | X-ray | 1.70 | A/B | 9-225 | [»] | |
3R91 | X-ray | 1.58 | A | 14-236 | [»] | |
3R92 | X-ray | 1.58 | A | 14-236 | [»] | |
3RKZ | X-ray | 1.57 | A | 14-236 | [»] | |
3RLP | X-ray | 1.70 | A/B | 9-225 | [»] | |
3RLQ | X-ray | 1.90 | A/B | 9-225 | [»] | |
3RLR | X-ray | 1.70 | A/B | 9-225 | [»] | |
3T0H | X-ray | 1.20 | A | 9-236 | [»] | |
3T0Z | X-ray | 2.19 | A | 9-236 | [»] | |
3T10 | X-ray | 1.24 | A | 9-236 | [»] | |
3T1K | X-ray | 1.50 | A/B | 9-236 | [»] | |
3T2S | X-ray | 1.50 | A/B | 9-236 | [»] | |
3TUH | X-ray | 1.80 | A/B | 16-224 | [»] | |
3VHA | X-ray | 1.39 | A | 9-236 | [»] | |
3VHC | X-ray | 1.41 | A | 9-236 | [»] | |
3VHD | X-ray | 1.52 | A/B | 9-236 | [»] | |
3WHA | X-ray | 1.30 | A/B | 9-236 | [»] | |
3WQ9 | X-ray | 1.80 | A | 1-236 | [»] | |
4AIF | X-ray | 2.01 | D/E | 726-732 | [»] | |
4AWO | X-ray | 1.70 | A/B | 9-236 | [»] | |
4AWP | X-ray | 1.82 | A/B | 9-236 | [»] | |
4AWQ | X-ray | 1.60 | A/B | 9-236 | [»] | |
4B7P | X-ray | 1.70 | A | 9-236 | [»] | |
4BQG | X-ray | 1.90 | A | 9-236 | [»] | |
4BQJ | X-ray | 2.00 | A | 9-236 | [»] | |
4CGQ | X-ray | 2.00 | Q | 726-732 | [»] | |
4CGU | X-ray | 2.11 | C | 726-732 | [»] | |
4CGV | X-ray | 2.54 | E/F | 726-732 | [»] | |
4CGW | X-ray | 3.00 | C/D | 726-732 | [»] | |
4CWF | X-ray | 2.00 | A | 9-236 | [»] | |
4CWN | X-ray | 1.80 | A | 9-236 | [»] | |
4CWO | X-ray | 2.31 | A | 9-236 | [»] | |
4CWP | X-ray | 1.95 | A | 9-236 | [»] | |
4CWQ | X-ray | 2.00 | A | 9-236 | [»] | |
4CWR | X-ray | 2.00 | A | 9-236 | [»] | |
4CWS | X-ray | 2.30 | A | 9-236 | [»] | |
4CWT | X-ray | 1.90 | A | 9-236 | [»] | |
4EEH | X-ray | 1.60 | A | 9-236 | [»] | |
4EFT | X-ray | 2.12 | A | 9-236 | [»] | |
4EFU | X-ray | 2.00 | A | 9-236 | [»] | |
4EGH | X-ray | 1.60 | A | 9-236 | [»] | |
4EGI | X-ray | 1.79 | A | 9-236 | [»] | |
4EGK | X-ray | 1.69 | A | 9-236 | [»] | |
4FCP | X-ray | 2.00 | A/B | 1-236 | [»] | |
4FCQ | X-ray | 2.15 | A | 1-236 | [»] | |
4FCR | X-ray | 1.70 | A | 1-236 | [»] | |
4HY6 | X-ray | 1.65 | A | 9-236 | [»] | |
4JQL | X-ray | 1.72 | A | 9-236 | [»] | |
4L8Z | X-ray | 1.70 | A | 9-236 | [»] | |
4L90 | X-ray | 2.00 | A | 9-236 | [»] | |
4L91 | X-ray | 1.75 | A | 9-236 | [»] | |
4L93 | X-ray | 1.84 | A/B | 9-236 | [»] | |
4L94 | X-ray | 1.65 | A | 9-236 | [»] | |
4LWE | X-ray | 1.50 | A | 17-224 | [»] | |
4LWF | X-ray | 1.75 | A | 17-224 | [»] | |
4LWG | X-ray | 1.60 | A | 17-224 | [»] | |
4LWH | X-ray | 1.70 | A | 16-224 | [»] | |
4LWI | X-ray | 1.70 | A | 17-224 | [»] | |
4NH7 | X-ray | 2.00 | A/B | 9-236 | [»] | |
4NH8 | X-ray | 1.65 | A | 9-236 | [»] | |
4O04 | X-ray | 1.82 | A | 9-236 | [»] | |
4O05 | X-ray | 1.79 | A | 9-236 | [»] | |
4O07 | X-ray | 1.86 | A | 9-236 | [»] | |
4O09 | X-ray | 1.96 | A | 9-236 | [»] | |
4O0B | X-ray | 1.93 | A | 9-236 | [»] | |
4R3M | X-ray | 1.80 | A | 16-224 | [»] | |
4U93 | X-ray | 1.55 | A | 1-236 | [»] | |
4W7T | X-ray | 1.80 | A | 1-236 | [»] | |
4XIP | X-ray | 1.70 | A | 9-236 | [»] | |
4XIQ | X-ray | 1.84 | A | 9-236 | [»] | |
4XIR | X-ray | 1.70 | A | 9-236 | [»] | |
4XIT | X-ray | 1.86 | A | 9-236 | [»] | |
4YKQ | X-ray | 1.91 | A | 2-236 | [»] | |
4YKR | X-ray | 1.61 | A | 2-236 | [»] | |
4YKT | X-ray | 1.85 | A | 2-236 | [»] | |
4YKU | X-ray | 1.70 | A | 2-236 | [»] | |
4YKW | X-ray | 1.85 | A/B | 2-236 | [»] | |
4YKX | X-ray | 1.80 | A | 2-236 | [»] | |
4YKY | X-ray | 1.78 | A | 2-236 | [»] | |
4YKZ | X-ray | 1.85 | A | 2-236 | [»] | |
5CF0 | X-ray | 1.80 | A | 9-236 | [»] | |
5FNC | X-ray | 2.20 | A | 1-236 | [»] | |
5FND | X-ray | 2.00 | A | 1-236 | [»] | |
5FNF | X-ray | 2.10 | A | 1-236 | [»] | |
5GGZ | X-ray | 2.02 | A/B/C/D | 16-225 | [»] | |
5J20 | X-ray | 1.76 | A | 17-223 | [»] | |
5J27 | X-ray | 1.70 | A | 16-224 | [»] | |
5J2V | X-ray | 1.59 | A | 17-223 | [»] | |
5J2X | X-ray | 1.22 | A | 17-224 | [»] | |
5J64 | X-ray | 1.38 | A | 9-236 | [»] | |
5J6L | X-ray | 1.75 | A | 9-236 | [»] | |
5J6M | X-ray | 1.64 | A | 9-234 | [»] | |
5J6N | X-ray | 1.90 | A | 9-234 | [»] | |
5J80 | X-ray | 1.17 | A | 9-233 | [»] | |
5J82 | X-ray | 2.17 | A | 9-233 | [»] | |
5J86 | X-ray | 1.87 | A | 9-233 | [»] | |
5J8M | X-ray | 1.90 | A/B | 9-233 | [»] | |
5J8U | X-ray | 1.75 | A/B | 9-233 | [»] | |
5J9X | X-ray | 1.80 | A | 9-233 | [»] | |
5LNY | X-ray | 1.88 | A | 9-236 | [»] | |
5LNZ | X-ray | 1.54 | A | 9-236 | [»] | |
5LO0 | X-ray | 2.30 | A | 9-236 | [»] | |
5LO1 | X-ray | 2.70 | A | 9-236 | [»] | |
5LO5 | X-ray | 1.44 | A | 9-236 | [»] | |
5LO6 | X-ray | 2.40 | A | 9-236 | [»] | |
5LQ9 | X-ray | 1.90 | A | 17-223 | [»] | |
5LR1 | X-ray | 1.44 | A | 18-223 | [»] | |
5LR7 | X-ray | 1.86 | A | 18-223 | [»] | |
5LRL | X-ray | 1.33 | A | 18-223 | [»] | |
5LRZ | X-ray | 2.00 | A | 18-223 | [»] | |
5LS1 | X-ray | 1.85 | A | 17-223 | [»] | |
5M4E | X-ray | 1.90 | A | 9-236 | [»] | |
5M4H | X-ray | 2.00 | A | 9-236 | [»] | |
5NYH | X-ray | 1.65 | A | 9-236 | [»] | |
5NYI | X-ray | 1.44 | A | 9-235 | [»] | |
5OCI | X-ray | 1.62 | A | 9-236 | [»] | |
5OD7 | X-ray | 2.00 | A | 9-236 | [»] | |
5ODX | X-ray | 1.82 | A | 9-236 | [»] | |
5T21 | X-ray | 2.10 | A | 18-223 | [»] | |
5VYY | X-ray | 1.79 | A | 1-236 | [»] | |
5XQD | X-ray | 1.60 | A | 9-236 | [»] | |
5XQE | X-ray | 1.70 | A | 9-236 | [»] | |
5XR5 | X-ray | 1.60 | A | 9-236 | [»] | |
5XR9 | X-ray | 1.50 | A | 9-236 | [»] | |
5XRB | X-ray | 1.65 | A | 9-236 | [»] | |
5XRD | X-ray | 1.30 | A | 9-236 | [»] | |
5XRE | X-ray | 1.50 | A | 9-236 | [»] | |
5ZR3 | X-ray | 2.50 | A/C/E/G | 1-236 | [»] | |
6B99 | X-ray | 1.60 | A | 1-236 | [»] | |
6B9A | X-ray | 1.65 | A/B | 1-236 | [»] | |
6CEO | X-ray | 1.90 | A | 1-236 | [»] | |
6CYG | X-ray | 1.50 | A/B | 1-236 | [»] | |
6CYH | X-ray | 1.49 | A/B | 1-236 | [»] | |
6EI5 | X-ray | 2.20 | A | 15-223 | [»] | |
6EL5 | X-ray | 1.67 | A | 1-236 | [»] | |
6ELN | X-ray | 1.60 | A | 17-223 | [»] | |
6ELO | X-ray | 1.80 | A | 1-236 | [»] | |
6ELP | X-ray | 1.85 | A | 1-236 | [»] | |
6EY8 | X-ray | 2.16 | A | 1-236 | [»] | |
6EY9 | X-ray | 2.00 | A | 1-236 | [»] | |
6EYA | X-ray | 2.10 | A | 1-236 | [»] | |
6EYB | X-ray | 1.90 | A | 1-236 | [»] | |
6F1N | X-ray | 2.09 | A | 1-236 | [»] | |
6FCJ | X-ray | 2.49 | A | 9-236 | [»] | |
6FDP | NMR | - | B | 724-732 | [»] | |
6GP4 | X-ray | 1.70 | A | 1-236 | [»] | |
6GP8 | X-ray | 1.75 | A | 1-236 | [»] | |
6GPF | X-ray | 1.55 | A | 1-236 | [»] | |
6GPH | X-ray | 1.56 | A | 1-236 | [»] | |
6GPO | X-ray | 1.48 | A | 1-236 | [»] | |
6GPP | X-ray | 1.51 | A | 1-236 | [»] | |
6GPR | X-ray | 2.35 | A | 1-236 | [»] | |
6GPT | X-ray | 2.00 | A | 1-236 | [»] | |
6GPW | X-ray | 1.60 | A | 1-236 | [»] | |
6GPY | X-ray | 2.25 | A | 1-236 | [»] | |
6GQ6 | X-ray | 2.25 | A | 1-236 | [»] | |
6GQR | X-ray | 2.05 | A | 1-236 | [»] | |
6GQS | X-ray | 1.43 | A | 1-236 | [»] | |
6GQU | X-ray | 1.72 | A | 1-236 | [»] | |
6GR1 | X-ray | 2.05 | A | 1-236 | [»] | |
6GR3 | X-ray | 1.88 | A | 1-236 | [»] | |
6GR4 | X-ray | 1.50 | A | 1-236 | [»] | |
6GR5 | X-ray | 1.34 | A | 1-236 | [»] | |
6HHR | X-ray | 2.00 | A | 17-224 | [»] | |
6KSQ | X-ray | 2.20 | A | 293-554 | [»] | |
6LR9 | X-ray | 2.20 | A | 9-236 | [»] | |
6LSZ | X-ray | 1.99 | A | 9-236 | [»] | |
6LT8 | X-ray | 1.59 | A | 9-236 | [»] | |
6LTI | X-ray | 1.59 | A | 9-236 | [»] | |
6LTK | X-ray | 2.14 | A | 9-236 | [»] | |
6N8X | X-ray | 1.49 | A | 1-236 | [»] | |
6OLX | X-ray | 1.44 | A | 1-236 | [»] | |
6TN4 | X-ray | 1.27 | AAA | 9-236 | [»] | |
6TN5 | X-ray | 1.17 | AAA | 9-236 | [»] | |
6U98 | X-ray | 1.50 | A | 2-236 | [»] | |
6U99 | X-ray | 1.60 | A | 2-236 | [»] | |
6U9A | X-ray | 1.65 | A | 2-236 | [»] | |
6U9B | X-ray | 1.75 | A | 2-236 | [»] | |
7DMC | X-ray | 2.34 | A | 16-224 | [»] | |
7KRJ | electron microscopy | 2.56 | A/B | 1-732 | [»] | |
7KW7 | electron microscopy | 3.57 | A/B | 1-732 | [»] | |
7L7I | electron microscopy | 3.30 | A/B | 1-732 | [»] | |
7L7J | electron microscopy | 3.10 | A/B | 1-732 | [»] | |
7LSZ | X-ray | 1.70 | A | 1-293 | [»] | |
7LT0 | X-ray | 1.70 | A | 1-293 | [»] | |
AlphaFoldDBi | P07900 | |||||
BMRBi | P07900 | |||||
SMRi | P07900 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 109552, 1052 interactors |
ComplexPortali | CPX-3288, HSP90A-CDC37 chaperone complex |
CORUMi | P07900 |
DIPi | DIP-27595N |
IntActi | P07900, 387 interactors |
MINTi | P07900 |
STRINGi | 9606.ENSP00000335153 |
Chemistry databases
BindingDBi | P07900 |
ChEMBLi | CHEMBL3880 |
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 |
DrugCentrali | P07900 |
GuidetoPHARMACOLOGYi | 2905 |
Protein family/group databases
MoonDBi | P07900, Predicted |
PTM databases
CarbonylDBi | P07900 |
GlyConnecti | 1301, 1 N-Linked glycan (1 site) |
GlyGeni | P07900, 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site) |
iPTMneti | P07900 |
MetOSitei | P07900 |
PhosphoSitePlusi | P07900 |
SwissPalmi | P07900 |
Genetic variation databases
BioMutai | HSP90AA1 |
DMDMi | 92090606 |
2D gel databases
OGPi | P07900 |
REPRODUCTION-2DPAGEi | IPI00784295 |
Proteomic databases
EPDi | P07900 |
jPOSTi | P07900 |
MassIVEi | P07900 |
MaxQBi | P07900 |
PaxDbi | P07900 |
PeptideAtlasi | P07900 |
PRIDEi | P07900 |
ProteomicsDBi | 52031 [P07900-1] 52032 [P07900-2] |
TopDownProteomicsi | P07900-1 [P07900-1] |
Protocols and materials databases
Antibodypediai | 3676, 1853 antibodies from 44 providers |
DNASUi | 3320 |
Genome annotation databases
Ensembli | ENST00000216281.13; ENSP00000216281.8; ENSG00000080824.19 ENST00000334701.11; ENSP00000335153.7; ENSG00000080824.19 [P07900-2] |
GeneIDi | 3320 |
KEGGi | hsa:3320 |
MANE-Selecti | ENST00000216281.13; ENSP00000216281.8; NM_005348.4; NP_005339.3 |
UCSCi | uc001yku.5, human [P07900-1] |
Organism-specific databases
CTDi | 3320 |
DisGeNETi | 3320 |
GeneCardsi | HSP90AA1 |
HGNCi | HGNC:5253, HSP90AA1 |
HPAi | ENSG00000080824, Tissue enhanced (brain) |
MIMi | 140571, gene |
neXtProti | NX_P07900 |
OpenTargetsi | ENSG00000080824 |
PharmGKBi | PA29519 |
VEuPathDBi | HostDB:ENSG00000080824 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0019, Eukaryota |
GeneTreei | ENSGT01020000230401 |
HOGENOMi | CLU_006684_1_3_1 |
InParanoidi | P07900 |
OMAi | AHDQPME |
OrthoDBi | 188544at2759 |
PhylomeDBi | P07900 |
TreeFami | TF300686 |
Enzyme and pathway databases
BRENDAi | 3.6.4.10, 2681 |
PathwayCommonsi | P07900 |
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 |
SignaLinki | P07900 |
SIGNORi | P07900 |
Miscellaneous databases
BioGRID-ORCSi | 3320, 37 hits in 1091 CRISPR screens |
ChiTaRSi | HSP90AA1, human |
EvolutionaryTracei | P07900 |
GenomeRNAii | 3320 |
Pharosi | P07900, Tchem |
PROi | PR:P07900 |
RNActi | P07900, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000080824, Expressed in middle temporal gyrus and 265 other tissues |
ExpressionAtlasi | P07900, baseline and differential |
Genevisiblei | P07900, HS |
Family and domain databases
Gene3Di | 1.20.120.790, 1 hit 3.30.565.10, 1 hit |
HAMAPi | MF_00505, HSP90, 1 hit |
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 |
PANTHERi | PTHR11528, PTHR11528, 1 hit |
Pfami | View protein in Pfam PF02518, HATPase_c, 1 hit PF00183, HSP90, 1 hit |
PIRSFi | PIRSF002583, Hsp90, 1 hit |
PRINTSi | PR00775, HEATSHOCK90 |
SMARTi | View protein in SMART SM00387, HATPase_c, 1 hit |
SUPFAMi | SSF110942, SSF110942, 1 hit SSF54211, SSF54211, 1 hit SSF55874, SSF55874, 1 hit |
PROSITEi | View protein in PROSITE PS00298, HSP90, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | HS90A_HUMAN | |
Accessioni | P07900Primary (citable) accession number: P07900 Secondary accession number(s): A8K500 Q9BVQ5 | |
Entry historyi | Integrated 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. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families