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Entry version 159 (05 Jun 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Heat shock protein 90

Gene

daf-21

Organism
Caenorhabditis elegans
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. 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. By stabilizing the receptor-type guanylate cyclase daf-11 or another signal transduction component that regulates cGMP levels, plays a role in dauer formation and chemotaxis to non-volatile and volatile attractants detected by AWC sensory neurons (PubMed:10790386, PubMed:7828815). Participates in the control of cell cycle progression at the prophase/metaphase transition in oocyte development by ensuring the activity of wee-1.3 kinase, which negatively regulates cdk-1 through its phosphorylation (PubMed:16466390). Regulates yap-1 nuclear export after heat shock treatment (PubMed:23396260).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei39ATPBy similarity1
Binding sitei81ATPBy similarity1
Binding sitei100ATPBy similarity1
Binding sitei126ATP; via amide nitrogenBy similarity1
Binding sitei371ATPBy 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 processCell cycle, Stress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-CEL-203615 eNOS activation
R-CEL-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-CEL-3371511 HSF1 activation
R-CEL-3371571 HSF1-dependent transactivation
R-CEL-5218920 VEGFR2 mediated vascular permeability
R-CEL-6798695 Neutrophil degranulation
R-CEL-844456 The NLRP3 inflammasome
R-CEL-8863795 Downregulation of ERBB2 signaling
R-CEL-8937144 Aryl hydrocarbon receptor signalling
R-CEL-8939211 ESR-mediated signaling
R-CEL-9009391 Non-genomic estrogen signaling

<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 90
Alternative name(s):
Abnormal dauer formation protein 21
<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:daf-21Imported
ORF Names:C47E8.5
<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>OrganismiCaenorhabditis elegans
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<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
  • UP000001940 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome V

Organism-specific databases

WormBase

More...
WormBasei
C47E8.5 ; CE05441 ; WBGene00000915 ; daf-21

<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

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi292E → K: Specific sensory defects and reduced fertility. 1 Publication1

<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 ‘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_00002339011 – 702Heat shock protein 90Add BLAST702

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q18688

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

More...
PaxDbi
Q18688

PeptideAtlas

More...
PeptideAtlasi
Q18688

PRoteomics IDEntifications database

More...
PRIDEi
Q18688

2D gel databases

The World-2DPAGE database

More...
World-2DPAGEi
0011:Q18688
0020:Q18688

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q18688

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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

In the embryo comma stage, expression is strongly detected in cells of the head region and less so in other areas. In early larvae, expressed in postembryonic germ cells derived from Z2 and Z3 cells and the head region, in both hermaphrodites and males. Under heat stress conditions, larval expression is not only detected in germ cells, but also all over the body. In adult hermaphrodites, expression is localized uniquely in the germ cells.1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Highly expressed throughout development.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00000915 Expressed in 10 organ(s), highest expression level in germ line (C elegans)

<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

Homodimer (PubMed:26593036).

Interacts (via TPR repeat-binding and central region) with pph-5 (via phosphatase domain); the interaction promotes pph-5 phosphatase activity (PubMed:26593036).

Interacts (via central region) with co-chaperone cdc-37 (via N-terminus); the interaction inhibits daf-21 ATPase activity (PubMed:23569206).

2 Publications

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
44973, 19 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3983 Hsp90-cdc-37-pph-5 phosphatase complex
CPX-3984 Hsp90-Cdc37 chaperone complex
CPX-4002 Hsp90-cdc-37-aha-1 complex
CPX-4003 Hsp90-sti-1 chaperone complex
CPX-4004 Hsp90-daf-41 chaperone complex

Database of interacting proteins

More...
DIPi
DIP-25037N

Protein interaction database and analysis system

More...
IntActi
Q18688, 15 interactors

Molecular INTeraction database

More...
MINTi
Q18688

STRING: functional protein association networks

More...
STRINGi
6239.C47E8.5.2

<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

1702
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q18688

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

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>Motifi698 – 702TPR 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.Sequence analysis

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

More...
HOGENOMi
HOG000031988

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q18688

KEGG Orthology (KO)

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KOi
K04079

Identification of Orthologs from Complete Genome Data

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OMAi
MRRMKEM

Database of Orthologous Groups

More...
OrthoDBi
924636at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q18688

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

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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
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

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

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

Q18688-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSENAETFAF QAEIAQLMSL IINTFYSNKE IYLRELISNA SDALDKIRYQ
60 70 80 90 100
ALTEPSELDT GKELFIKITP NKEEKTLTIM DTGIGMTKAD LVNNLGTIAK
110 120 130 140 150
SGTKAFMEAL QAGADISMIG QFGVGFYSAF LVADKVVVTS KNNDDDSYQW
160 170 180 190 200
ESSAGGSFVV RPFNDPEVTR GTKIVMHIKE DQIDFLEERK IKEIVKKHSQ
210 220 230 240 250
FIGYPIKLVV EKEREKEVED EEAVEAKDEE KKEGEVENVA DDADKKKTKK
260 270 280 290 300
IKEKYFEDEE LNKTKPIWTR NPDDISNEEY AEFYKSLSND WEDHLAVKHF
310 320 330 340 350
SVEGQLEFRA LLFVPQRAPF DLFENKKSKN SIKLYVRRVF IMENCEELMP
360 370 380 390 400
EYLNFIKGVV DSEDLPLNIS REMLQQSKIL KVIRKNLVKK CMELIDEVAE
410 420 430 440 450
DKDNFKKFYE QFGKNLKLGI HEDSTNRKKL SDFLRYSTSA GDEPTSLKEY
460 470 480 490 500
VSRMKENQTQ IYYITGESKD VVAASAFVER VKSRGFEVLY MCDPIDEYCV
510 520 530 540 550
QQLKEYDGKK LVSVTKEGLE LPETEEEKKK FEEDKVAYEN LCKVIKDILE
560 570 580 590 600
KKVEKVGVSN RLVSSPCCIV TSEYGWSANM ERIMKAQALR DSSTMGYMAA
610 620 630 640 650
KKHLEINPDH AIMKTLRDRV EVDKNDKTVK DLVVLLFETA LLASGFSLEE
660 670 680 690 700
PQSHASRIYR MIKLGLDIGD DEIEDSAVPS SCTAEAKIEG AEEDASRMEE

VD
Length:702
Mass (Da):80,283
Last modified:November 1, 1996 - v1
<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:i2B0E975A24074811
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

More...
DDBJi
Links Updated
BX284605 Genomic DNA Translation: CAA99793.1

Protein sequence database of the Protein Information Resource

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PIRi
T20019

NCBI Reference Sequences

More...
RefSeqi
NP_506626.1, NM_074225.3

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
C47E8.5.1; C47E8.5.1; WBGene00000915
C47E8.5.2; C47E8.5.2; WBGene00000915
C47E8.5.3; C47E8.5.3; WBGene00000915
C47E8.5.4; C47E8.5.4; WBGene00000915

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
179971

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cel:CELE_C47E8.5

UCSC genome browser

More...
UCSCi
C47E8.5.1 c. elegans

<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
BX284605 Genomic DNA Translation: CAA99793.1
PIRiT20019
RefSeqiNP_506626.1, NM_074225.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GQTX-ray2.15A/B1-224[»]
4I2ZX-ray2.90B693-702[»]
SMRiQ18688
ModBaseiSearch...

Protein-protein interaction databases

BioGridi44973, 19 interactors
ComplexPortaliCPX-3983 Hsp90-cdc-37-pph-5 phosphatase complex
CPX-3984 Hsp90-Cdc37 chaperone complex
CPX-4002 Hsp90-cdc-37-aha-1 complex
CPX-4003 Hsp90-sti-1 chaperone complex
CPX-4004 Hsp90-daf-41 chaperone complex
DIPiDIP-25037N
IntActiQ18688, 15 interactors
MINTiQ18688
STRINGi6239.C47E8.5.2

PTM databases

iPTMnetiQ18688

2D gel databases

World-2DPAGEi0011:Q18688
0020:Q18688

Proteomic databases

EPDiQ18688
PaxDbiQ18688
PeptideAtlasiQ18688
PRIDEiQ18688

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC47E8.5.1; C47E8.5.1; WBGene00000915
C47E8.5.2; C47E8.5.2; WBGene00000915
C47E8.5.3; C47E8.5.3; WBGene00000915
C47E8.5.4; C47E8.5.4; WBGene00000915
GeneIDi179971
KEGGicel:CELE_C47E8.5
UCSCiC47E8.5.1 c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
179971
WormBaseiC47E8.5 ; CE05441 ; WBGene00000915 ; daf-21

Phylogenomic databases

eggNOGiKOG0019 Eukaryota
KOG0020 Eukaryota
COG0326 LUCA
GeneTreeiENSGT00950000182747
HOGENOMiHOG000031988
InParanoidiQ18688
KOiK04079
OMAiMRRMKEM
OrthoDBi924636at2759
PhylomeDBiQ18688

Enzyme and pathway databases

ReactomeiR-CEL-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-CEL-203615 eNOS activation
R-CEL-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-CEL-3371511 HSF1 activation
R-CEL-3371571 HSF1-dependent transactivation
R-CEL-5218920 VEGFR2 mediated vascular permeability
R-CEL-6798695 Neutrophil degranulation
R-CEL-844456 The NLRP3 inflammasome
R-CEL-8863795 Downregulation of ERBB2 signaling
R-CEL-8937144 Aryl hydrocarbon receptor signalling
R-CEL-8939211 ESR-mediated signaling
R-CEL-9009391 Non-genomic estrogen signaling

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q18688

Gene expression databases

BgeeiWBGene00000915 Expressed in 10 organ(s), highest expression level in germ line (C elegans)

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
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
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

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
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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 nameiHSP90_CAEEL
<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: Q18688
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: November 1, 1996
Last modified: June 5, 2019
This is version 159 of the entry and version 1 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 programCaenorhabditis annotation project

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
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