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Entry version 202 (07 Apr 2021)
Sequence version 4 (23 Jan 2007)
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Protein

Heat shock protein HSP 90-beta

Gene

Hsp90ab1

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 linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. 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. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery. Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription. Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10.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.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 sitei46ATPBy similarity1
Binding sitei88ATPBy similarity1
Binding sitei107ATPBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei126 – 127Cleaved under oxidative stressBy similarity2
Binding sitei133ATP; via amide nitrogenBy similarity1
Binding sitei392ATPBy similarity1

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

GO - Biological processi

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

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-2029482, Regulation of actin dynamics for phagocytic cup formation
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-399954, Sema3A PAK dependent Axon repulsion
R-RNO-6798695, Neutrophil degranulation
R-RNO-844456, The NLRP3 inflammasome
R-RNO-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-RNO-8937144, Aryl hydrocarbon receptor signalling
R-RNO-8939211, ESR-mediated signaling
R-RNO-9013418, RHOBTB2 GTPase cycle
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-beta
Alternative name(s):
Heat shock 84 kDa
Short name:
HSP 84
Short name:
HSP84
<p>This subsection of the <a href="http://www.uniprot.org/help/names%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:Hsp90ab1
Synonyms:Hsp84, Hspcb
<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 9

Organism-specific databases

Rat genome database

More...
RGDi
1303075, Hsp90ab1

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus, Secreted

<p>This section 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 methionineiRemoved2 Publications
<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_00000629202 – 724Heat shock protein HSP 90-betaAdd BLAST723

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei219N6-succinyllysineBy similarity1
Modified residuei226PhosphoserineCombined sources1
Modified residuei255PhosphoserineCombined sources1
Modified residuei261PhosphoserineCombined sources1
Modified residuei297PhosphothreonineBy similarity1
Modified residuei301PhosphotyrosineBy similarity1
Modified residuei305PhosphotyrosineBy similarity1
Modified residuei307PhosphoserineBy similarity1
Modified residuei399N6-malonyllysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi434O-linked (GlcNAc) serineBy similarity1
Modified residuei435N6-acetyllysineBy similarity1
Modified residuei445PhosphoserineCombined sources1
Glycosylationi452O-linked (GlcNAc) serineBy similarity1
Modified residuei479PhosphothreonineBy similarity1
Modified residuei481N6-acetyllysineBy similarity1
Modified residuei484PhosphotyrosineBy similarity1
Modified residuei531N6-methylated lysine; alternateBy similarity1
Modified residuei531N6-succinyllysine; alternateBy similarity1
Modified residuei574N6-methylated lysineBy similarity1
Modified residuei577N6-succinyllysineBy similarity1
Modified residuei590S-nitrosocysteineBy similarity1
Modified residuei624N6-acetyllysineBy similarity1
Modified residuei669PhosphoserineBy similarity1
Modified residuei718Phosphoserine; by PLK2 and PLK3By 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

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

Keywords - PTMi

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

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P34058

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

More...
PaxDbi
P34058

PRoteomics IDEntifications database

More...
PRIDEi
P34058

2D gel databases

The World-2DPAGE database

More...
World-2DPAGEi
0004:P34058

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P34058, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P34058

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

More...
PhosphoSitePlusi
P34058

<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
ENSRNOG00000019834, Expressed in Ammon's horn and 21 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P34058, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P34058, 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

Monomer. Homodimer (By similarity).

Forms a complex with CDK6 and CDC37.

Interacts with UNC45A; binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer (By similarity).

Interacts with CHORDC1 (By similarity).

Interacts with DNAJC7.

Interacts with FKBP4. May interact with NWD1.

Interacts with SGTA.

Interacts with HSF1 in an ATP-dependent manner.

Interacts with MET; the interaction suppresses MET kinase activity.

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

Interacts with HIF1A, KEAP1 and RHOBTB2.

Interacts with STUB1 and SMAD3.

Interacts with XPO1 and AHSA1.

Interacts with BIRC2.

Interacts with KCNQ4; promotes cell surface expression of KCNQ4.

Interacts with BIRC2; prevents auto-ubiquitination and degradation of its client protein BIRC2.

Interacts with NOS3.

Interacts with AHR; interaction is inhibited by HSP90AB1 phosphorylation on Ser-226 and Ser-255.

Interacts with STIP1 and CDC37; upon SMYD2-dependent methylation.

Interacts with JAK2 and PRKCE; promotes functional activation in a heat shock-dependent manner.

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

Interacts with CDC25A; prevents heat shock-mediated CDC25A degradation and contributes to cell cycle progression (By similarity).

Interacts with TP53 (via DNA binding domain); suppresses TP53 aggregation and prevents from irreversible thermal inactivation (PubMed:8663025).

Interacts with TGFB1 processed form (LAP); inhibits latent TGFB1 activation (By similarity).

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

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

Interacts with PDCL3 (PubMed:27496612).

Interacts with TTC4 (via TPR repeats) (By similarity).

Interacts with IL1B; the interaction facilitates cargo translocation into the ERGIC (By similarity).

By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
256892, 12 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P34058

Protein interaction database and analysis system

More...
IntActi
P34058, 8 interactors

Molecular INTeraction database

More...
MINTi
P34058

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000026920

<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
P34058

Database of comparative protein structure models

More...
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>Regioni2 – 527Interaction with TP53By similarityAdd BLAST526
Regioni2 – 214Interaction with BIRC2By similarityAdd BLAST213
Regioni9 – 231Interaction with NR3C1By similarityAdd BLAST223
Regioni215 – 552Interaction with AHSA1By similarityAdd BLAST338
Regioni264 – 608Interaction with NR3C1By similarityAdd BLAST345
Regioni620 – 723Interaction with NR1D1By similarityAdd BLAST104

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi720 – 724TPR repeat-binding5

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

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.By similarity

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

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0019, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT01020000230401

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_006684_1_3_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P34058

Identification of Orthologs from Complete Genome Data

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OMAi
IMDNCEQ

Database of Orthologous Groups

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OrthoDBi
924636at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P34058

TreeFam database of animal gene trees

More...
TreeFami
TF300686

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.120.790, 1 hit
3.30.565.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00505, HSP90, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003594, HATPase_C
IPR036890, HATPase_C_sf
IPR019805, Heat_shock_protein_90_CS
IPR037196, HSP90_C
IPR001404, Hsp90_fam
IPR020575, Hsp90_N
IPR020568, Ribosomal_S5_D2-typ_fold

The PANTHER Classification System

More...
PANTHERi
PTHR11528, PTHR11528, 1 hit

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF002583, Hsp90, 1 hit

Protein Motif fingerprint database; a protein domain database

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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

More...
SUPFAMi
SSF110942, SSF110942, 1 hit
SSF54211, SSF54211, 1 hit
SSF55874, SSF55874, 1 hit

PROSITE; a protein domain and family database

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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

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

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P34058-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA
60 70 80 90 100
LDKIRYESLT DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN
110 120 130 140 150
NLGTIAKSGT KAFMEALQAG ADISMIGQFG VGFYSAYLVA EKVVVITKHN
160 170 180 190 200
DDEQYAWESS AGGSFTVRAD HGEPIGRGTK VILHLKEDQT EYLEERRVKE
210 220 230 240 250
VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE DKEDEEKPKI
260 270 280 290 300
EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE
310 320 330 340 350
YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK
360 370 380 390 400
NNIKLYVRRV FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI
410 420 430 440 450
LKVIRKNIVK KCLELFSELA EDKENYKKFY EAFSKNLKLG IHEDSTNRRR
460 470 480 490 500
LSELLRYHTS QSGDEMTSLS EYVSRMKETQ KSIYYITGES KEQVANSAFV
510 520 530 540 550
ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG LELPEDEEEK
560 570 580 590 600
KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA
610 620 630 640 650
NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA
660 670 680 690 700
VKDLVVLLFE TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVTAEEP
710 720
SAAVPDEIPP LEGDEDASRM EEVD
Length:724
Mass (Da):83,281
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCE323E81CE173ECB
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2K793A0A0G2K793_RAT
Heat shock protein HSP 90-beta
Hsp90ab1
694Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti6 – 7HH → QK AA sequence (PubMed:3189818).Curated2
Sequence conflicti11E → P AA sequence (PubMed:3189818).Curated1
Sequence conflicti17F → T AA sequence (PubMed:3189818).Curated1
Sequence conflicti20E → F AA sequence (PubMed:3189818).Curated1
Sequence conflicti26S → F in AAH82009 (PubMed:15489334).Curated1
Sequence conflicti82R → A in AAB23369 (PubMed:1525042).Curated1
Sequence conflicti368E → D in AAB23369 (PubMed:1525042).Curated1
Sequence conflicti375N → D in ABE27999 (Ref. 3) Curated1
Sequence conflicti559K → R in AAB23369 (PubMed:1525042).Curated1
Sequence conflicti664 – 674LSSGFSLEDPQ → SSLASHFRRPK in AAB23369 (PubMed:1525042).CuratedAdd BLAST11

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
S45392 mRNA Translation: AAB23369.1
AY695392 mRNA Translation: AAT99568.1
AY695393 mRNA Translation: AAT99569.1
DQ022068 Genomic DNA Translation: ABE27999.1
BC082009 mRNA Translation: AAH82009.1

Protein sequence database of the Protein Information Resource

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PIRi
S71306

NCBI Reference Sequences

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RefSeqi
NP_001004082.3, NM_001004082.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000026920; ENSRNOP00000026920; ENSRNOG00000019834

Database of genes from NCBI RefSeq genomes

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GeneIDi
301252

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:301252

UCSC genome browser

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UCSCi
RGD:1303075, 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
S45392 mRNA Translation: AAB23369.1
AY695392 mRNA Translation: AAT99568.1
AY695393 mRNA Translation: AAT99569.1
DQ022068 Genomic DNA Translation: ABE27999.1
BC082009 mRNA Translation: AAH82009.1
PIRiS71306
RefSeqiNP_001004082.3, NM_001004082.3

3D structure databases

SMRiP34058
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi256892, 12 interactors
CORUMiP34058
IntActiP34058, 8 interactors
MINTiP34058
STRINGi10116.ENSRNOP00000026920

PTM databases

GlyGeniP34058, 2 sites
iPTMnetiP34058
PhosphoSitePlusiP34058

2D gel databases

World-2DPAGEi0004:P34058

Proteomic databases

jPOSTiP34058
PaxDbiP34058
PRIDEiP34058

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
P34058, 1 sequenced antibody

Genome annotation databases

EnsembliENSRNOT00000026920; ENSRNOP00000026920; ENSRNOG00000019834
GeneIDi301252
KEGGirno:301252
UCSCiRGD:1303075, rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
3326
RGDi1303075, Hsp90ab1

Phylogenomic databases

eggNOGiKOG0019, Eukaryota
GeneTreeiENSGT01020000230401
HOGENOMiCLU_006684_1_3_1
InParanoidiP34058
OMAiIMDNCEQ
OrthoDBi924636at2759
PhylomeDBiP34058
TreeFamiTF300686

Enzyme and pathway databases

ReactomeiR-RNO-2029482, Regulation of actin dynamics for phagocytic cup formation
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-399954, Sema3A PAK dependent Axon repulsion
R-RNO-6798695, Neutrophil degranulation
R-RNO-844456, The NLRP3 inflammasome
R-RNO-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-RNO-8937144, Aryl hydrocarbon receptor signalling
R-RNO-8939211, ESR-mediated signaling
R-RNO-9013418, RHOBTB2 GTPase cycle
R-RNO-9018519, Estrogen-dependent gene expression

Miscellaneous databases

Protein Ontology

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PROi
PR:P34058

Gene expression databases

BgeeiENSRNOG00000019834, Expressed in Ammon's horn and 21 other tissues
ExpressionAtlasiP34058, baseline and differential
GenevisibleiP34058, 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
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHS90B_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: P34058
Secondary accession number(s): Q1PSW2
, Q66H55, Q68GV5, Q9QWC6
<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: February 1, 1994
Last sequence update: January 23, 2007
Last modified: April 7, 2021
This is version 202 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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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