UniProtKB - P07900 (HS90A_HUMAN)
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- BLAST>sp|P07900|HS90A_HUMAN Heat shock protein HSP 90-alpha OS=Homo sapiens OX=9606 GN=HSP90AA1 PE=1 SV=5 MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIR YESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFME ALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPM GRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKED KEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRN PDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNN IKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKC LELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDY CTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKT LVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIV TSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVK DLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPPLE GDDDTSRMEEVD
- Align
Heat shock protein HSP 90-alpha
HSP90AA1
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>Select a section on the left to see content.
<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
<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
- Ref.59"Hsp90, the concertmaster: tuning transcription."
Khurana N., Bhattacharyya S.
Front. Oncol. 5:100-100(2015) [PubMed] [Europe PMC] [Abstract]Cited for: REVIEW. - Ref.63"Hsp90: Friends, clients and natural foes."
Verma S., Goyal S., Jamal S., Singh A., Grover A.
Biochimie 127:227-240(2016) [PubMed] [Europe PMC] [Abstract]Cited for: REVIEW. - Ref.64"Review: The HSP90 molecular chaperone-an enigmatic ATPase."
Pearl L.H.
Biopolymers 105:594-607(2016) [PubMed] [Europe PMC] [Abstract]Cited for: REVIEW.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.16"S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities."
Martinez-Ruiz A., Villanueva L., Gonzalez de Orduna C., Lopez-Ferrer D., Higueras M.A., Tarin C., Rodriguez-Crespo I., Vazquez J., Lamas S.
Proc. Natl. Acad. Sci. U.S.A. 102:8525-8530(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 592-612, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-598, S-NITROSYLATION AT CYS-598. - Ref.23"Stable association of hsp90 and p23, but Not hsp70, with active human telomerase."
Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.
J. Biol. Chem. 276:15571-15574(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TERT, FUNCTION AS A CO-CHAPERONE IN TELOMERASE HOLOENZYME ASSEMBLY. - Ref.25"A CD14-independent LPS receptor cluster."
Triantafilou K., Triantafilou M., Dedrick R.L.
Nat. Immunol. 2:338-345(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5 AND HSPA8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.31"Molecular basis for TPR domain-mediated regulation of protein phosphatase 5."
Yang J., Roe S.M., Cliff M.J., Williams M.A., Ladbury J.E., Cohen P.T., Barford D.
EMBO J. 24:1-10(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PPP5C. - Ref.65"The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding."
Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D., Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W., Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S., Marston Linehan W., Bratslavsky G., Mollapour M.
Nat. Commun. 7:12037-12037(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FLCN; AHSA1; HSP70; CDC37; FNIP1; FNIP2; STUB1; STIP1; PTGES3 AND PPP5C. - Ref.67"Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients."
Woodford M.R., Sager R.A., Marris E., Dunn D.M., Blanden A.R., Murphy R.L., Rensing N., Shapiro O., Panaretou B., Prodromou C., Loh S.N., Gutmann D.H., Bourboulia D., Bratslavsky G., Wong M., Mollapour M.
EMBO J. 36:3650-3665(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, IDENTIFICATION IN A COMPLEX WITH TSC1 AND TSC2, INTERACTION WITH TSC1 AND AHSA1, SUBUNIT, MUTAGENESIS OF GLU-47; ASP-93; TYR-313 AND 728-MET--ASP-732.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.35"Conserved conformational changes in the ATPase cycle of human Hsp90."
Richter K., Soroka J., Skalniak L., Leskovar A., Hessling M., Reinstein J., Buchner J.
J. Biol. Chem. 283:17757-17765(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.67"Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients."
Woodford M.R., Sager R.A., Marris E., Dunn D.M., Blanden A.R., Murphy R.L., Rensing N., Shapiro O., Panaretou B., Prodromou C., Loh S.N., Gutmann D.H., Bourboulia D., Bratslavsky G., Wong M., Mollapour M.
EMBO J. 36:3650-3665(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, IDENTIFICATION IN A COMPLEX WITH TSC1 AND TSC2, INTERACTION WITH TSC1 AND AHSA1, SUBUNIT, MUTAGENESIS OF GLU-47; ASP-93; TYR-313 AND 728-MET--ASP-732.
<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
- KM=300 µM for ATP1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.35"Conserved conformational changes in the ATPase cycle of human Hsp90."
Richter K., Soroka J., Skalniak L., Leskovar A., Hessling M., Reinstein J., Buchner J.
J. Biol. Chem. 283:17757-17765(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ 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 sitei | 51 | ATP | 1 | |
| <p>This subsection of the ‘Function’ 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 sitei | 93 | ATP | 1 | |
| <p>This subsection of the ‘Function’ 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 sitei | 112 | ATPBy similarity | 1 | |
| <p>This subsection of the ‘Function’ 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 sitei | 138 | ATP; via amide nitrogen | 1 | |
| <p>This subsection of the ‘Function’ 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 sitei | 400 | ATPBy similarity | 1 |
<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
- ATPase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ATPase activity, coupled Source: Reactome
- ATP binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- disordered domain specific binding Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- DNA polymerase binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- GTPase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- histone deacetylase binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- identical protein binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- MHC class II protein complex binding Source: UniProtKBInferred from high throughput direct assayi
- nitric-oxide synthase regulator activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nucleotide binding Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- protein homodimerization activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein tyrosine kinase activity Source: ReactomeInferred from experimenti
- protein tyrosine kinase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
- scaffold protein binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- tau protein binding Source: ARUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- TPR domain binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ubiquitin protein ligase binding Source: ARUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- unfolded protein binding Source: InterPro
<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 - Biological processi
- axon extension Source: ARUK-UCL
- central nervous system neuron axonogenesis Source: ARUK-UCL
- chaperone-mediated autophagy Source: ParkinsonsUK-UCL <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- chaperone-mediated protein complex assembly Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ciliary basal body-plasma membrane docking Source: Reactome
- cofactor metabolic process Source: Reactome
- cytokine-mediated signaling pathway Source: Reactome
- ERBB2 signaling pathway Source: Reactome
- establishment of cell polarity Source: ARUK-UCL
- Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
- G2/M transition of mitotic cell cycle Source: Reactome
- mitochondrial transport Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- neutrophil degranulation Source: Reactome
- positive regulation of cellular protein catabolic process Source: ARUK-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- 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 <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of protein polymerization Source: ARUK-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of tau-protein kinase activity Source: ARUK-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of telomerase activity Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein import into mitochondrial outer membrane Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein refolding Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- protein stabilization Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- protein unfolding Source: ParkinsonsUK-UCL <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- receptor-mediated endocytosis Source: Reactome
- regulation of cellular protein localization Source: ARUK-UCL
- regulation of cellular response to heat Source: Reactome
- regulation of G2/M transition of mitotic cell cycle Source: Reactome
- regulation of nitric-oxide synthase activity Source: Reactome
- regulation of protein complex assembly Source: ParkinsonsUK-UCL <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- regulation of protein ubiquitination Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- response to antibiotic Source: AgBase
- response to cold Source: AgBase
- response to heat Source: AgBase
- response to unfolded protein Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- signal transduction Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- telomerase holoenzyme complex assembly Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- telomere maintenance via telomerase Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- vascular endothelial growth factor receptor signaling pathway Source: Reactome
<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 function | Chaperone |
| Biological process | Stress response |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1227986 Signaling by ERBB2 R-HSA-1236382 Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants R-HSA-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation R-HSA-192905 vRNP Assembly R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation R-HSA-203615 eNOS activation R-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition R-HSA-3000484 Scavenging by Class F Receptors R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR) R-HSA-3371511 HSF1 activation R-HSA-3371568 Attenuation phase R-HSA-3371571 HSF1-dependent transactivation R-HSA-380259 Loss of Nlp from mitotic centrosomes R-HSA-380270 Recruitment of mitotic centrosome proteins and complexes R-HSA-380284 Loss of proteins required for interphase microtubule organization from the centrosome R-HSA-380320 Recruitment of NuMA to mitotic centrosomes R-HSA-399954 Sema3A PAK dependent Axon repulsion R-HSA-4420097 VEGFA-VEGFR2 Pathway R-HSA-5218920 VEGFR2 mediated vascular permeability R-HSA-5336415 Uptake and function of diphtheria toxin R-HSA-5601884 PIWI-interacting RNA (piRNA) biogenesis R-HSA-5620912 Anchoring of the basal body to the plasma membrane R-HSA-5637810 Constitutive Signaling by EGFRvIII R-HSA-6785807 Interleukin-4 and 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-9018519 Estrogen-dependent gene expression |
SIGNOR Signaling Network Open Resource More...SIGNORi | P07900 |
Protein family/group databases
MoonDB Database of extreme multifunctional and moonlighting proteins More...MoonDBi | P07900 Predicted |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Heat shock protein HSP 90-alphaAlternative name(s): Heat shock 86 kDa Short name: HSP 86 Short name: HSP86 Lipopolysaccharide-associated protein 2 Short name: LAP-2 Short name: LPS-associated protein 2 Renal carcinoma antigen NY-REN-38 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:HSP90AA1 Synonyms:HSP90A, HSPC1, HSPCA |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo 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 identifieri | 9606 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000080824.18 |
Human Gene Nomenclature Database More...HGNCi | HGNC:5253 HSP90AA1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 140571 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P07900 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Plasma membrane
- Cell membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"A CD14-independent LPS receptor cluster."
Triantafilou K., Triantafilou M., Dedrick R.L.
Nat. Immunol. 2:338-345(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5 AND HSPA8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- Cell membrane 1 Publication
Nucleus
- Nucleus By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- Nucleus By similarity
Other locations
- Cytoplasm By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- Melanosome 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.46"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.- Cytoplasm By similarity
Cytosol
- cytosol Source: Reactome
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- extracellular region Source: Reactome
Lysosome
- lysosomal lumen Source: ParkinsonsUK-UCL <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
Nucleus
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKBInferred from high throughput direct assayi
Plasma Membrane
- plasma membrane Source: Reactome
- ruffle membrane Source: Ensembl
Other locations
- axonal growth cone Source: ARUK-UCL
- cytoplasm Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- dendritic growth cone Source: ARUK-UCL
- endocytic vesicle lumen Source: Reactome
- ficolin-1-rich granule lumen Source: Reactome
- melanosome Source: UniProtKB-SubCell
- membrane Source: UniProtKBInferred from high throughput direct assayi
- myelin sheath Source: Ensembl
- neuronal cell body Source: ARUK-UCL
- perinuclear region of cytoplasm Source: ARUK-UCL
- protein-containing complex Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- secretory granule lumen Source: Reactome
<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>Keywords - Cellular componenti
Cell membrane, Cytoplasm, Membrane, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>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 <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>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 <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 97 | G → D: Abolishes ATPase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 313 | Y → E: Loss of interaction with TSC1 and increases interacrion with AHSA1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 313 | Y → F: No deffect on the interaction with TSC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 598 | C → A, N or D: Reduces ATPase activity and client protein activation. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 598 | C → S: Loss of S-nitrosylation. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 728 – 732 | Missing : Loss of interaction with TSC1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 5 |
Organism-specific databases
DisGeNET More...DisGeNETi | 3320 |
Open Targets More...OpenTargetsi | ENSG00000080824 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA29519 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3880 |
Drug and drug target database More...DrugBanki | DB07317 (3E)-3-[(phenylamino)methylidene]dihydrofuran-2(3H)-one DB03080 17-Dmag DB08786 4-(2-methoxyethoxy)-6-methylpyrimidin-2-amine DB03809 9-Butyl-8-(3-Methoxybenzyl)-9h-Purin-6-Amine DB03899 9-Butyl-8-(4-Methoxybenzyl)-9h-Purin-6-Amine DB05134 CNF1010 DB02424 Geldanamycin DB07325 N-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)METHYL]-3-{[(E)-(2-OXODIHYDROFURAN-3(2H)-YLIDENE)METHYL]AMINO}BENZENESULFONAMIDE DB00716 Nedocromil DB00615 Rifabutin DB06070 SNX-5422 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2905 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | HSP90AA1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 92090606 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 methioninei | Removed1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000062911 | 2 – 732 | Heat shock protein HSP 90-alphaAdd BLAST | 731 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 residuei | 5 | Phosphothreonine; by PRKDC1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 residuei | 7 | Phosphothreonine; by PRKDC1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 residuei | 58 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 84 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 231 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 residuei | 252 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 263 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 residuei | 313 | PhosphotyrosineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 443 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 453 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 458 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 476 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 489 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 492 | PhosphotyrosineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 585 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 598 | S-nitrosocysteine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 residuei | 641 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.45"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]Cited for: ISGYLATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.16"S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities."
Martinez-Ruiz A., Villanueva L., Gonzalez de Orduna C., Lopez-Ferrer D., Higueras M.A., Tarin C., Rodriguez-Crespo I., Vazquez J., Lamas S.
Proc. Natl. Acad. Sci. U.S.A. 102:8525-8530(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 592-612, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-598, S-NITROSYLATION AT CYS-598.
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
<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>Keywords - PTMi
Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P07900 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P07900 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P07900 |
PeptideAtlas More...PeptideAtlasi | P07900 |
PRoteomics IDEntifications database More...PRIDEi | P07900 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 52031 52032 [P07900-2] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P07900-1 [P07900-1] |
2D gel databases
USC-OGP 2-DE database More...OGPi | P07900 |
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00784295 |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | P07900 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P07900 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P07900 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P07900 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | P07900 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000080824 |
CleanEx database of gene expression profiles More...CleanExi | HS_HSP90AA1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P07900 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P07900 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB002058 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
29 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization."
Stewart S., Sundaram M., Zhang Y., Lee J., Han M., Guan K.L.
Mol. Cell. Biol. 19:5523-5534(1999) [PubMed] [Europe PMC] [Abstract] - Ref.18"The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo."
Minami Y., Kimura Y., Kawasaki H., Suzuki K., Yahara I.
Mol. Cell. Biol. 14:1459-1464(1994) [PubMed] [Europe PMC] [Abstract]Cited for: HOMODIMERIZATION. - Ref.19"Mechanism of dimer formation of the 90-kDa heat-shock protein."
Nemoto T., Ohara-Nemoto Y., Ota M., Takagi T., Yokoyama K.
Eur. J. Biochem. 233:1-8(1995) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT. - Ref.20"Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin."
Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., Chinkers M., Pratt W.B.
J. Biol. Chem. 272:16224-16230(1997) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH NR3C1 AND FKBP4; PPID; PPP5C OR STIP1. - Ref.21"Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90."
Young J.C., Obermann W.M., Hartl F.U.
J. Biol. Chem. 273:18007-18010(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TOM34. - Ref.23"Stable association of hsp90 and p23, but Not hsp70, with active human telomerase."
Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.
J. Biol. Chem. 276:15571-15574(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TERT, FUNCTION AS A CO-CHAPERONE IN TELOMERASE HOLOENZYME ASSEMBLY. - Ref.24"Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex."
Guo Y., Guettouche T., Fenna M., Boellmann F., Pratt W.B., Toft D.O., Smith D.F., Voellmy R.
J. Biol. Chem. 276:45791-45799(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HSF1. - Ref.25"A CD14-independent LPS receptor cluster."
Triantafilou K., Triantafilou M., Dedrick R.L.
Nat. Immunol. 2:338-345(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5 AND HSPA8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.26"Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system."
Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C., Obermann W.M.
EMBO J. 22:3613-3623(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DNAJC7. - Ref.27"Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone."
Lotz G.P., Lin H., Harst A., Obermann W.M.J.
J. Biol. Chem. 278:17228-17235(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH AHSA1. - Ref.28"SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells."
Hamamoto R., Furukawa Y., Morita M., Iimura Y., Silva F.P., Li M., Yagyu R., Nakamura Y.
Nat. Cell Biol. 6:731-740(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SMYD3. - Ref.29"Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions."
Liou S.T., Wang C.
Arch. Biochem. Biophys. 435:253-263(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SGTA AND TTC1. - Ref.30"Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole."
Zeke T., Morrice N., Vazquez-Martin C., Cohen P.T.
Biochem. J. 385:45-56(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PPP5C, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.31"Molecular basis for TPR domain-mediated regulation of protein phosphatase 5."
Yang J., Roe S.M., Cliff M.J., Williams M.A., Ladbury J.E., Cohen P.T., Barford D.
EMBO J. 24:1-10(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PPP5C. - Ref.34"Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90."
Cliff M.J., Harris R., Barford D., Ladbury J.E., Williams M.A.
Structure 14:415-426(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PPP5C. - Ref.35"Conserved conformational changes in the ATPase cycle of human Hsp90."
Richter K., Soroka J., Skalniak L., Leskovar A., Hessling M., Reinstein J., Buchner J.
J. Biol. Chem. 283:17757-17765(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.44"A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein."
Gano J.J., Simon J.A.
Mol. Cell. Proteomics 9:255-270(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CHORDC1. - Ref.47"Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling."
Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L., Iwamatsu A., Esposito D., Gillette W.K., Hopkins R.F. III, Hartley J.L., Furihata M., Oishi S., Zhen W., Burke T.R. Jr., Linehan W.M., Schmidt L.S., Zbar B.
Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FNIP1, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.50"Stat1 mediates an auto-regulation of hsp90beta gene in heat shock response."
Cheng M.B., Zhang Y., Zhong X., Sutter B., Cao C.Y., Chen X.S., Cheng X.K., Zhang Y., Xiao L., Shen Y.F.
Cell. Signal. 22:1206-1213(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HSP90AB1. - Ref.54"Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites."
Eckl J.M., Rutz D.A., Haslbeck V., Zierer B.K., Reinstein J., Richter K.
J. Biol. Chem. 288:16032-16042(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CDC37. - Ref.58"The NLR-related protein NWD1 is associated with prostate cancer and modulates androgen receptor signaling."
Correa R.G., Krajewska M., Ware C.F., Gerlic M., Reed J.C.
Oncotarget 5:1666-1682(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NWD1. - Ref.60"C-terminal domain of SMYD3 serves as a unique HSP90-regulated motif in oncogenesis."
Brown M.A., Foreman K., Harriss J., Das C., Zhu L., Edwards M., Shaaban S., Tucker H.
Oncotarget 6:4005-4019(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SMYD3. - Ref.61"Client proteins and small molecule inhibitors display distinct binding preferences for constitutive and stress-induced HSP90 isoforms and their conformationally restricted mutants."
Prince T.L., Kijima T., Tatokoro M., Lee S., Tsutsumi S., Yim K., Rivas C., Alarcon S., Schwartz H., Khamit-Kush K., Scroggins B.T., Beebe K., Trepel J.B., Neckers L.
PLoS ONE 10:E0141786-E0141786(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HSF1; HIF1A; ERBB2; MET; KEAP1 AND RHOBTB2, MUTAGENESIS OF GLU-47 AND ASP-93. - Ref.65"The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding."
Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D., Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W., Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S., Marston Linehan W., Bratslavsky G., Mollapour M.
Nat. Commun. 7:12037-12037(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FLCN; AHSA1; HSP70; CDC37; FNIP1; FNIP2; STUB1; STIP1; PTGES3 AND PPP5C. - Ref.66"IER5 generates a novel hypo-phosphorylated active form of HSF1 and contributes to tumorigenesis."
Asano Y., Kawase T., Okabe A., Tsutsumi S., Ichikawa H., Tatebe S., Kitabayashi I., Tashiro F., Namiki H., Kondo T., Semba K., Aburatani H., Taya Y., Nakagama H., Ohki R.
Sci. Rep. 6:19174-19174(2016) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HSF1. - Ref.67"Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients."
Woodford M.R., Sager R.A., Marris E., Dunn D.M., Blanden A.R., Murphy R.L., Rensing N., Shapiro O., Panaretou B., Prodromou C., Loh S.N., Gutmann D.H., Bourboulia D., Bratslavsky G., Wong M., Mollapour M.
EMBO J. 36:3650-3665(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, IDENTIFICATION IN A COMPLEX WITH TSC1 AND TSC2, INTERACTION WITH TSC1 AND AHSA1, SUBUNIT, MUTAGENESIS OF GLU-47; ASP-93; TYR-313 AND 728-MET--ASP-732. - Ref.69"In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis."
Obermann W.M., Sondermann H., Russo A.A., Pavletich N.P., Hartl F.U.
J. Cell Biol. 143:901-910(1998) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 11-223 IN COMPLEX WITH ADP, CATALYTIC ACTIVITY, INTERACTION WITH PTGES3. - Ref.70"Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 724-732 IN COMPLEX WITH STUB1, INTERACTION WITH STUB1 AND UBE2N, MOTIF TPR REPEAT-BINDING.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
<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
- disordered domain specific binding Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- DNA polymerase binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- GTPase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- histone deacetylase binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- identical protein binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein homodimerization activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein tyrosine kinase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- scaffold protein binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- tau protein binding Source: ARUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- TPR domain binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ubiquitin protein ligase binding Source: ARUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- unfolded protein binding Source: InterPro
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 109552, 827 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-3288 HSP90A-CDC37 chaperone complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P07900 |
Database of interacting proteins More...DIPi | DIP-27595N |
Protein interaction database and analysis system More...IntActi | P07900, 255 interactors |
Molecular INTeraction database More...MINTi | P07900 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000335153 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P07900 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 18 – 21 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 24 – 35 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 43 – 65 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 23 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 67 – 70 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 78 – 83 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 84 – 87 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 88 – 93 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 100 – 104 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 105 – 108 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 111 – 123 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 128 – 134 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 137 – 143 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 145 – 153 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 155 – 157 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 160 – 164 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 169 – 174 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 181 – 190 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 192 – 198 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 200 – 210 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 212 – 216 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 218 – 220 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 221 – 224 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 225 – 227 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 228 – 230 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 296 – 298 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 306 – 317 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 324 – 331 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 333 – 335 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 337 – 343 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 361 – 365 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 368 – 372 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 380 – 382 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 386 – 392 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 408 – 427 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 431 – 451 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 21 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 453 – 455 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 456 – 460 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 464 – 467 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 468 – 472 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 477 – 482 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 490 – 495 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 499 – 503 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 506 – 508 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 509 – 514 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 518 – 521 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 525 – 529 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 530 – 532 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 539 – 543 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 555 – 567 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 569 – 578 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 580 – 582 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 584 – 588 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 593 – 601 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 603 – 605 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 608 – 613 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 632 – 636 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 641 – 652 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 657 – 673 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 681 – 694 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 728 – 730 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P07900 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P07900 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P07900 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Regioni | 284 – 732 | Interaction with FLCN and FNIP11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 449 | |
| <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>Regioni | 284 – 620 | Interaction with FNIP2 and TSC12 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 337 | |
| <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>Regioni | 682 – 732 | Required for homodimerization1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 51 | |
| <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>Regioni | 728 – 732 | Essential for interaction with SMYD3, TSC1 and STIP1/HOP2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 5 | |
| <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>Regioni | 729 – 732 | Essential for interaction with SGTA and TTC11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 4 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Motifi | 723 – 732 | TPR repeat-binding1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 10 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.70"Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 724-732 IN COMPLEX WITH STUB1, INTERACTION WITH STUB1 AND UBE2N, MOTIF TPR REPEAT-BINDING.
<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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0019 Eukaryota KOG0020 Eukaryota COG0326 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000149016 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG007374 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P07900 |
KEGG Orthology (KO) More...KOi | K04079 |
Identification of Orthologs from Complete Genome Data More...OMAi | VKRHSEF |
Database of Orthologous Groups More...OrthoDBi | EOG091G0270 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P07900 |
TreeFam database of animal gene trees More...TreeFami | TF300686 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00075 HATPase_c, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.120.790, 1 hit 3.30.565.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00505 HSP90, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR003594 HATPase_C IPR036890 HATPase_C_sf IPR019805 Heat_shock_protein_90_CS IPR037196 HSP90_C IPR001404 Hsp90_fam IPR020575 Hsp90_N IPR020568 Ribosomal_S5_D2-typ_fold |
The PANTHER Classification System More...PANTHERi | PTHR11528 PTHR11528, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF02518 HATPase_c, 1 hit PF00183 HSP90, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF002583 Hsp90, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00775 HEATSHOCK90 |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00387 HATPase_c, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF110942 SSF110942, 1 hit SSF54211 SSF54211, 1 hit SSF55874 SSF55874, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00298 HSP90, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
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
The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MPPCSGGDGS...QPFILLRLLM
10 20 30 40 50
MPPCSGGDGS TPPGPSLRDR DCPAQSAEYP RDRLDPRPGS PSEASSPPFL
60 70 80 90 100
RSRAPVNWYQ EKAQVFLWHL MVSGSTTLLC LWKQPFHVSA FPVTASLAFR
110 120 130 140 150
QSQGAGQHLY KDLQPFILLR LLMPEETQTQ DQPMEEEEVE TFAFQAEIAQ
160 170 180 190 200
LMSLIINTFY SNKEIFLREL ISNSSDALDK IRYESLTDPS KLDSGKELHI
210 220 230 240 250
NLIPNKQDRT LTIVDTGIGM TKADLINNLG TIAKSGTKAF MEALQAGADI
260 270 280 290 300
SMIGQFGVGF YSAYLVAEKV TVITKHNDDE QYAWESSAGG SFTVRTDTGE
310 320 330 340 350
PMGRGTKVIL HLKEDQTEYL EERRIKEIVK KHSQFIGYPI TLFVEKERDK
360 370 380 390 400
EVSDDEAEEK EDKEEEKEKE EKESEDKPEI EDVGSDEEEE KKDGDKKKKK
410 420 430 440 450
KIKEKYIDQE ELNKTKPIWT RNPDDITNEE YGEFYKSLTN DWEDHLAVKH
460 470 480 490 500
FSVEGQLEFR ALLFVPRRAP FDLFENRKKK NNIKLYVRRV FIMDNCEELI
510 520 530 540 550
PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNLVK KCLELFTELA
560 570 580 590 600
EDKENYKKFY EQFSKNIKLG IHEDSQNRKK LSELLRYYTS ASGDEMVSLK
610 620 630 640 650
DYCTRMKENQ KHIYYITGET KDQVANSAFV ERLRKHGLEV IYMIEPIDEY
660 670 680 690 700
CVQQLKEFEG KTLVSVTKEG LELPEDEEEK KKQEEKKTKF ENLCKIMKDI
710 720 730 740 750
LEKKVEKVVV SNRLVTSPCC IVTSTYGWTA NMERIMKAQA LRDNSTMGYM
760 770 780 790 800
AAKKHLEINP DHSIIETLRQ KAEADKNDKS VKDLVILLYE TALLSSGFSL
810 820 830 840 850
EDPQTHANRI YRMIKLGLGI DEDDPTADDT SAAVTEEMPP LEGDDDTSRM
EEVD
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 conflicti | 63 | S → T in CAA33259 (PubMed:2780322).Curated | 1 | |
| <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 conflicti | 74 | K → R in CAI64495 (PubMed:16269234).Curated | 1 | |
| <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 conflicti | 74 | K → R in BAG51711 (PubMed:14702039).Curated | 1 | |
| <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 conflicti | 86 | D → G in CAI64495 (PubMed:16269234).Curated | 1 | |
| <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 conflicti | 86 | D → G in BAG51711 (PubMed:14702039).Curated | 1 | |
| <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 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) | |||||
| <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 varianti | 71 | M → L. Corresponds to variant dbSNP:rs8005905Ensembl. | 1 | ||
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X15183 mRNA Translation: CAA33259.1 M27024 Genomic DNA Translation: AAA63194.1 AJ890082 mRNA Translation: CAI64495.1 AJ890083 mRNA Translation: CAI64496.1 DQ314871 Genomic DNA Translation: ABC40730.1 AK056446 mRNA Translation: BAG51711.1 AK291115 mRNA Translation: BAF83804.1 AK291607 mRNA Translation: BAF84296.1 AL133223 Genomic DNA No translation available. CH471061 Genomic DNA Translation: EAW81765.1 X07270 mRNA Translation: CAA30255.1 M30626 Genomic DNA Translation: AAA36023.1 BC000987 mRNA Translation: AAH00987.1 BC121062 mRNA Translation: AAI21063.1 D87666 mRNA Translation: BAA13430.1 D87666 mRNA Translation: BAA13431.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS32160.1 [P07900-2] CCDS9967.1 [P07900-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A32319 HHHU86 |
NCBI Reference Sequences More...RefSeqi | NP_001017963.2, NM_001017963.2 [P07900-2] NP_005339.3, NM_005348.3 [P07900-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.525600 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000216281; ENSP00000216281; ENSG00000080824 [P07900-1] ENST00000334701; ENSP00000335153; ENSG00000080824 [P07900-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3320 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:3320 |
UCSC genome browser More...UCSCi | uc001yku.5 human [P07900-1] |
<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>Keywords - Coding sequence diversityi
Alternative splicing<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P07900 | Epididymis luminal secretory protein 52 | 732 | |||
| P07900-2 | 854 | ||||
| HSP90AA1 protein (Fragment) | 638 | ||||
| Full-length cDNA 5-PRIME end of clone CS0DN005YI08 of Adult brain of Homo sapiens (human) (Fragment) | 262 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P07900 | Epididymis luminal secretory protein 52 | 732 | |||
| Heat shock protein HSP 90-alpha | 855 | ||||
| UPI00084CFFB3 | 266 | ||||
| UPI0003440D05 | 266 | ||||
| UPI00045D9044 | 152 | ||||
| +45 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P07900 | Epididymis luminal secretory protein 52 | 732 | |||
| Heat shock protein HSP 90-alpha | 855 | ||||
| UPI00084CFFB3 | 266 | ||||
| UPI0003440D05 | 266 | ||||
| UPI00045D9044 | 152 | ||||
| +953 | |||||
<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: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X15183 mRNA Translation: CAA33259.1 M27024 Genomic DNA Translation: AAA63194.1 AJ890082 mRNA Translation: CAI64495.1 AJ890083 mRNA Translation: CAI64496.1 DQ314871 Genomic DNA Translation: ABC40730.1 AK056446 mRNA Translation: BAG51711.1 AK291115 mRNA Translation: BAF83804.1 AK291607 mRNA Translation: BAF84296.1 AL133223 Genomic DNA No translation available. CH471061 Genomic DNA Translation: EAW81765.1 X07270 mRNA Translation: CAA30255.1 M30626 Genomic DNA Translation: AAA36023.1 BC000987 mRNA Translation: AAH00987.1 BC121062 mRNA Translation: AAI21063.1 D87666 mRNA Translation: BAA13430.1 D87666 mRNA Translation: BAA13431.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS32160.1 [P07900-2] CCDS9967.1 [P07900-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A32319 HHHU86 |
NCBI Reference Sequences More...RefSeqi | NP_001017963.2, NM_001017963.2 [P07900-2] NP_005339.3, NM_005348.3 [P07900-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.525600 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks 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 | [»] | |
| 5ODX | X-ray | 1.82 | A | 9-236 | [»] | |
| 5T21 | X-ray | 2.10 | A | 18-223 | [»] | |
| 5VYY | X-ray | 1.79 | A | 1-236 | [»] | |
| 6CEO | X-ray | 1.90 | A | 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 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P07900 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P07900 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 109552, 827 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-3288 HSP90A-CDC37 chaperone complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P07900 |
Database of interacting proteins More...DIPi | DIP-27595N |
Protein interaction database and analysis system More...IntActi | P07900, 255 interactors |
Molecular INTeraction database More...MINTi | P07900 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000335153 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P07900 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3880 |
Drug and drug target database More...DrugBanki | DB07317 (3E)-3-[(phenylamino)methylidene]dihydrofuran-2(3H)-one DB03080 17-Dmag DB08786 4-(2-methoxyethoxy)-6-methylpyrimidin-2-amine DB03809 9-Butyl-8-(3-Methoxybenzyl)-9h-Purin-6-Amine DB03899 9-Butyl-8-(4-Methoxybenzyl)-9h-Purin-6-Amine DB05134 CNF1010 DB02424 Geldanamycin DB07325 N-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)METHYL]-3-{[(E)-(2-OXODIHYDROFURAN-3(2H)-YLIDENE)METHYL]AMINO}BENZENESULFONAMIDE DB00716 Nedocromil DB00615 Rifabutin DB06070 SNX-5422 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2905 |
Protein family/group databases
MoonDB Database of extreme multifunctional and moonlighting proteins More...MoonDBi | P07900 Predicted |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | P07900 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P07900 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P07900 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P07900 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | HSP90AA1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 92090606 |
2D gel databases
USC-OGP 2-DE database More...OGPi | P07900 |
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00784295 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P07900 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P07900 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P07900 |
PeptideAtlas More...PeptideAtlasi | P07900 |
PRoteomics IDEntifications database More...PRIDEi | P07900 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 52031 52032 [P07900-2] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P07900-1 [P07900-1] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000216281; ENSP00000216281; ENSG00000080824 [P07900-1] ENST00000334701; ENSP00000335153; ENSG00000080824 [P07900-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3320 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:3320 |
UCSC genome browser More...UCSCi | uc001yku.5 human [P07900-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 3320 |
DisGeNET More...DisGeNETi | 3320 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000080824.18 |
GeneCards: human genes, protein and diseases More...GeneCardsi | HSP90AA1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:5253 HSP90AA1 |
Human Protein Atlas More...HPAi | CAB002058 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 140571 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P07900 |
Open Targets More...OpenTargetsi | ENSG00000080824 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA29519 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0019 Eukaryota KOG0020 Eukaryota COG0326 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000149016 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG007374 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P07900 |
KEGG Orthology (KO) More...KOi | K04079 |
Identification of Orthologs from Complete Genome Data More...OMAi | VKRHSEF |
Database of Orthologous Groups More...OrthoDBi | EOG091G0270 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P07900 |
TreeFam database of animal gene trees More...TreeFami | TF300686 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1227986 Signaling by ERBB2 R-HSA-1236382 Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants R-HSA-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation R-HSA-192905 vRNP Assembly R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation R-HSA-203615 eNOS activation R-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition R-HSA-3000484 Scavenging by Class F Receptors R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR) R-HSA-3371511 HSF1 activation R-HSA-3371568 Attenuation phase R-HSA-3371571 HSF1-dependent transactivation R-HSA-380259 Loss of Nlp from mitotic centrosomes R-HSA-380270 Recruitment of mitotic centrosome proteins and complexes R-HSA-380284 Loss of proteins required for interphase microtubule organization from the centrosome R-HSA-380320 Recruitment of NuMA to mitotic centrosomes R-HSA-399954 Sema3A PAK dependent Axon repulsion R-HSA-4420097 VEGFA-VEGFR2 Pathway R-HSA-5218920 VEGFR2 mediated vascular permeability R-HSA-5336415 Uptake and function of diphtheria toxin R-HSA-5601884 PIWI-interacting RNA (piRNA) biogenesis R-HSA-5620912 Anchoring of the basal body to the plasma membrane R-HSA-5637810 Constitutive Signaling by EGFRvIII R-HSA-6785807 Interleukin-4 and 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-9018519 Estrogen-dependent gene expression |
SIGNOR Signaling Network Open Resource More...SIGNORi | P07900 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | HSP90AA1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P07900 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 3320 |
CutDB - Proteolytic event database More...PMAP-CutDBi | P07900 |
Protein Ontology More...PROi | PR:P07900 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000080824 |
CleanEx database of gene expression profiles More...CleanExi | HS_HSP90AA1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P07900 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P07900 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd00075 HATPase_c, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.120.790, 1 hit 3.30.565.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00505 HSP90, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR003594 HATPase_C IPR036890 HATPase_C_sf IPR019805 Heat_shock_protein_90_CS IPR037196 HSP90_C IPR001404 Hsp90_fam IPR020575 Hsp90_N IPR020568 Ribosomal_S5_D2-typ_fold |
The PANTHER Classification System More...PANTHERi | PTHR11528 PTHR11528, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF02518 HATPase_c, 1 hit PF00183 HSP90, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF002583 Hsp90, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00775 HEATSHOCK90 |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00387 HATPase_c, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF110942 SSF110942, 1 hit SSF54211 SSF54211, 1 hit SSF55874 SSF55874, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00298 HSP90, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | HS90A_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>Accessioni | P07900Primary (citable) accession number: P07900 Secondary accession number(s): A8K500 , B3KPJ9, Q2PP14, Q5CAQ6, Q5CAQ7, Q9BVQ5 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1988 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | July 18, 2018 | |
| This is version 238 of the entry and version 5 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry 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. | |
<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
<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>Keywords - Technical termi
3D-structure, Complete proteome, 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
