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Entry version 156 (22 Apr 2020)
Sequence version 3 (23 Jan 2007)
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Protein

Heat shock protein HSP 90-alpha

Gene

Hsp90aa1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei51ATPBy similarity1
Binding sitei93ATPBy similarity1
Binding sitei112ATPBy similarity1
Binding sitei138ATP; via amide nitrogenBy similarity1
Binding sitei401ATPBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

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

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1227986 Signaling by ERBB2
R-RNO-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-RNO-2029482 Regulation of actin dynamics for phagocytic cup formation
R-RNO-203615 eNOS activation
R-RNO-2565942 Regulation of PLK1 Activity at G2/M Transition
R-RNO-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-RNO-3371511 HSF1 activation
R-RNO-3371568 Attenuation phase
R-RNO-3371571 HSF1-dependent transactivation
R-RNO-380259 Loss of Nlp from mitotic centrosomes
R-RNO-380270 Recruitment of mitotic centrosome proteins and complexes
R-RNO-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-RNO-380320 Recruitment of NuMA to mitotic centrosomes
R-RNO-399954 Sema3A PAK dependent Axon repulsion
R-RNO-4420097 VEGFA-VEGFR2 Pathway
R-RNO-5218920 VEGFR2 mediated vascular permeability
R-RNO-5620912 Anchoring of the basal body to the plasma membrane
R-RNO-6798695 Neutrophil degranulation
R-RNO-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-RNO-8854518 AURKA Activation by TPX2
R-RNO-8863795 Downregulation of ERBB2 signaling
R-RNO-8939211 ESR-mediated signaling
R-RNO-9009391 Extra-nuclear estrogen signaling
R-RNO-9018519 Estrogen-dependent gene expression

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Heat shock protein HSP 90-alpha
Alternative name(s):
Heat shock 86 kDa
Short name:
HSP 86
Short name:
HSP86
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Hsp90aa1
Synonyms:Hsp86, Hspca
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Rat genome database

More...
RGDi
631409 Hsp90aa1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000629152 – 733Heat shock protein HSP 90-alphaAdd BLAST732

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei5Phosphothreonine; by PRKDCBy similarity1
Modified residuei7Phosphothreonine; by PRKDCBy similarity1
Modified residuei58N6-acetyllysineBy similarity1
Modified residuei84N6-acetyllysineBy similarity1
Modified residuei231PhosphoserineCombined sources1
Modified residuei252PhosphoserineCombined sources1
Modified residuei263PhosphoserineCombined sources1
Modified residuei314PhosphotyrosineBy similarity1
Modified residuei444N6-acetyllysineBy similarity1
Modified residuei454PhosphoserineCombined sources1
Modified residuei459N6-acetyllysineBy similarity1
Modified residuei477PhosphoserineBy similarity1
Modified residuei490N6-acetyllysineBy similarity1
Modified residuei493PhosphotyrosineBy similarity1
Modified residuei586N6-acetyllysineBy similarity1
Modified residuei599S-nitrosocysteineBy similarity1
Modified residuei642PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P82995

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

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PaxDbi
P82995

PRoteomics IDEntifications database

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PRIDEi
P82995

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P82995

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P82995

<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
ENSRNOG00000007219 Expressed in testis and 8 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P82995 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (By similarity). Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C or STIP1 (By similarity).

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

Interacts with TOM34 (By similarity).

Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex (By similarity).

Interacts with CHORDC1 and DNAJC7 (By similarity).

Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems (By similarity).

Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity (By similarity). Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8 (By similarity).

Interacts with KSR1 (By similarity).

Interacts with co-chaperone CDC37 (via C-terminus); the interaction inhibits HSP90AA1 ATPase activity (By similarity). May interact with NWD1 (By similarity).

Interacts with FNIP1 and FNIP2; the interaction inhibits HSP90AA1 ATPase activity (By similarity).

Interacts with co-chaperone AHSA1 (phosphorylated on 'Tyr-223'); the interaction activates HSP90AA1 ATPase activity and results in the dissociation of TSC1 from HSP90AA1 (By similarity).

Interacts with FLCN in the presence of FNIP1 (By similarity).

Interacts with HSP70, STIP1 and PTGES3 (By similarity).

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

Interacts with SMYD3; this interaction enhances SMYD3 histone-lysine N-methyltransferase (By similarity).

Interacts with TTC1 (via TPR repeats) (By similarity).

Interacts with HSF1 in an ATP-dependent manner (By similarity).

Interacts with MET; the interaction suppresses MET kinase activity (By similarity).

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

Interacts with HIF1A, KEAP1 and RHOBTB2 (By similarity).

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

Interacts with STUB1 and SMAD3 (By similarity).

Interacts with HSP90AB1; interaction is constitutive (By similarity).

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

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

Interacts with NLPR12.

Interacts with PDCL3 (PubMed:27496612).

By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
256205, 24 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P82995

Protein interaction database and analysis system

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IntActi
P82995, 5 interactors

Molecular INTeraction database

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MINTi
P82995

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000009556

<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

3D structure databases

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

More...
SMRi
P82995

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni9 – 236Interaction with NR3C1By similarityAdd BLAST228
Regioni272 – 617Interaction with NR3C1By similarityAdd BLAST346
Regioni285 – 733Interaction with FLCN and FNIP1By similarityAdd BLAST449
Regioni285 – 621Interaction with FNIP2 and TSC1By similarityAdd BLAST337
Regioni629 – 732Interaction with NR1D1By similarityAdd BLAST104
Regioni683 – 733Required for homodimerizationBy similarityAdd BLAST51
Regioni729 – 733Essential for interaction with SMYD3, TSC1 and STIP1/HOPBy similarity5
Regioni730 – 733Essential for interaction with SGTA and TTC1By similarity4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi724 – 733TPR repeat-bindingBy similarity10

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

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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0019 Eukaryota
KOG0020 Eukaryota
COG0326 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182747

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_006684_1_3_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P82995

KEGG Orthology (KO)

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KOi
K04079

Identification of Orthologs from Complete Genome Data

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OMAi
VKRHSEF

Database of Orthologous Groups

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OrthoDBi
924636at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P82995

TreeFam database of animal gene trees

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TreeFami
TF300686

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.120.790, 1 hit
3.30.565.10, 1 hit

HAMAP database of protein families

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HAMAPi
MF_00505 HSP90, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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PANTHERi
PTHR11528 PTHR11528, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02518 HATPase_c, 1 hit
PF00183 HSP90, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF002583 Hsp90, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00775 HEATSHOCK90

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00387 HATPase_c, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF110942 SSF110942, 1 hit
SSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00298 HSP90, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P82995-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS
60 70 80 90 100
NSSDALDKIR YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK
110 120 130 140 150
ADLINNLGTI AKSGTKAFME ALQAGADISM IGQFGVGFYS AYLVAEKVTV
160 170 180 190 200
ITKHNDDEQY AWESSAGGSF TVRTDTGEPM GRGTKVILHL KEDQTEYLEE
210 220 230 240 250
RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKEE KEEEKEKEEK
260 270 280 290 300
ESDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR
310 320 330 340 350
NPDDITNEEY GEFYKSLTND WEEHLAVKHF SVEGQLEFRA LLFVPRRAPF
360 370 380 390 400
DLFENRKKKN NIKLYVRRVF IMDNCEELIP EYLNFIRGVV DSEDLPLNIS
410 420 430 440 450
REMLQQSKIL KVIRKNLVKK CLELFTELAE DKENYKKFYE QFSKNIKLGI
460 470 480 490 500
HEDSQNRKKL SELLRYYTSA SGDEMVSLKD YCTRMKENQK HIYFITGETK
510 520 530 540 550
DQVANSAFVE RLRKHGLEVI YMIEPIDEYC VQQLKEFEGK TLVSVTKEGL
560 570 580 590 600
ELPEDEEEKK KQEEKKTKFE NLCKIMKDIL EKKVEKVVVS NRLVTSPCCI
610 620 630 640 650
VTSTYGWTAN MERIMKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK
660 670 680 690 700
AEADKNDKSV KDLVILLYET ALLSSGFSLE DPQTHANRIY RMIKLGLGID
710 720 730
EDDPTVDDTS AAVTEEMPPL EGDDDTSRME EVD
Length:733
Mass (Da):84,815
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDF2C8383A6581D07
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AJ297736 Genomic DNA Translation: CAC39453.1
AJ428213 mRNA Translation: CAD21648.1
BC072489 mRNA Translation: AAH72489.1
BC085120 mRNA Translation: AAH85120.1

NCBI Reference Sequences

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RefSeqi
NP_786937.1, NM_175761.2
XP_008763191.1, XM_008764969.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000009556; ENSRNOP00000009556; ENSRNOG00000007219
ENSRNOT00000086310; ENSRNOP00000075715; ENSRNOG00000059714

Database of genes from NCBI RefSeq genomes

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GeneIDi
103692716
299331

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:103692716
rno:299331

UCSC genome browser

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UCSCi
RGD:631409 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297736 Genomic DNA Translation: CAC39453.1
AJ428213 mRNA Translation: CAD21648.1
BC072489 mRNA Translation: AAH72489.1
BC085120 mRNA Translation: AAH85120.1
RefSeqiNP_786937.1, NM_175761.2
XP_008763191.1, XM_008764969.2

3D structure databases

SMRiP82995
ModBaseiSearch...

Protein-protein interaction databases

BioGridi256205, 24 interactors
CORUMiP82995
IntActiP82995, 5 interactors
MINTiP82995
STRINGi10116.ENSRNOP00000009556

PTM databases

CarbonylDBiP82995
iPTMnetiP82995

Proteomic databases

jPOSTiP82995
PaxDbiP82995
PRIDEiP82995

Genome annotation databases

EnsembliENSRNOT00000009556; ENSRNOP00000009556; ENSRNOG00000007219
ENSRNOT00000086310; ENSRNOP00000075715; ENSRNOG00000059714
GeneIDi103692716
299331
KEGGirno:103692716
rno:299331
UCSCiRGD:631409 rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
3320
RGDi631409 Hsp90aa1

Phylogenomic databases

eggNOGiKOG0019 Eukaryota
KOG0020 Eukaryota
COG0326 LUCA
GeneTreeiENSGT00950000182747
HOGENOMiCLU_006684_1_3_1
InParanoidiP82995
KOiK04079
OMAiVKRHSEF
OrthoDBi924636at2759
PhylomeDBiP82995
TreeFamiTF300686

Enzyme and pathway databases

ReactomeiR-RNO-1227986 Signaling by ERBB2
R-RNO-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-RNO-2029482 Regulation of actin dynamics for phagocytic cup formation
R-RNO-203615 eNOS activation
R-RNO-2565942 Regulation of PLK1 Activity at G2/M Transition
R-RNO-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-RNO-3371511 HSF1 activation
R-RNO-3371568 Attenuation phase
R-RNO-3371571 HSF1-dependent transactivation
R-RNO-380259 Loss of Nlp from mitotic centrosomes
R-RNO-380270 Recruitment of mitotic centrosome proteins and complexes
R-RNO-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-RNO-380320 Recruitment of NuMA to mitotic centrosomes
R-RNO-399954 Sema3A PAK dependent Axon repulsion
R-RNO-4420097 VEGFA-VEGFR2 Pathway
R-RNO-5218920 VEGFR2 mediated vascular permeability
R-RNO-5620912 Anchoring of the basal body to the plasma membrane
R-RNO-6798695 Neutrophil degranulation
R-RNO-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-RNO-8854518 AURKA Activation by TPX2
R-RNO-8863795 Downregulation of ERBB2 signaling
R-RNO-8939211 ESR-mediated signaling
R-RNO-9009391 Extra-nuclear estrogen signaling
R-RNO-9018519 Estrogen-dependent gene expression

Miscellaneous databases

Protein Ontology

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PROi
PR:P82995

Gene expression databases

BgeeiENSRNOG00000007219 Expressed in testis and 8 other tissues
GenevisibleiP82995 RN

Family and domain databases

Gene3Di1.20.120.790, 1 hit
3.30.565.10, 1 hit
HAMAPiMF_00505 HSP90, 1 hit
InterProiView protein in InterPro
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR019805 Heat_shock_protein_90_CS
IPR037196 HSP90_C
IPR001404 Hsp90_fam
IPR020575 Hsp90_N
IPR020568 Ribosomal_S5_D2-typ_fold
PANTHERiPTHR11528 PTHR11528, 1 hit
PfamiView protein in Pfam
PF02518 HATPase_c, 1 hit
PF00183 HSP90, 1 hit
PIRSFiPIRSF002583 Hsp90, 1 hit
PRINTSiPR00775 HEATSHOCK90
SMARTiView protein in SMART
SM00387 HATPase_c, 1 hit
SUPFAMiSSF110942 SSF110942, 1 hit
SSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit
PROSITEiView protein in PROSITE
PS00298 HSP90, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHS90A_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P82995
Secondary accession number(s): Q91XW0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2007
Last modified: April 22, 2020
This is version 156 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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