Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP-dependent molecular chaperone HSP82

Gene

HSP82

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. 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. Required for growth at high temperatures.1 Publication

Miscellaneous

Present with 444943 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the ‘Function’ 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

Inhibited by geldanamycin, macbecin I and radicicol, which bind to the ATP-binding pocket. Co-chaperones CDC37, SBA1 and STI1 reduce ATPase activity. Co-chaperones AHA1 and HCH1 increase ATPase activity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei33ATPCombined sources1 Publication1
Binding sitei37ATPCombined sources1 Publication1
Binding sitei79ATPCombined sources1 Publication1
Binding sitei84ATPCombined sources1 Publication1
Binding sitei92ATPCombined sources1 Publication1
Binding sitei98ATPCombined sources1 Publication1
Binding sitei171ATPCombined sources1 Publication1
Binding sitei380ATPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi99 – 100ATPCombined sources1 Publication2
Nucleotide bindingi119 – 124ATPCombined sources1 Publication6

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

  • ATPase activity, coupled Source: SGD
  • ATP binding Source: GO_Central
  • identical protein binding Source: IntAct
  • unfolded protein binding Source: SGD

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

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-34126-MONOMER

<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:
ATP-dependent molecular chaperone HSP82
Alternative name(s):
82 kDa heat shock protein
Heat shock protein Hsp90 heat-inducible isoform
<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:HSP82
Synonyms:HSP90
Ordered Locus Names:YPL240C
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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 XVI

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000006161 HSP82

<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 Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; 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>Mutagenesisi22T → I: Induces a 6-fold increase in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. 1 Publication1
Mutagenesisi41A → V: Causes a 98% reduction in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. 1 Publication1
Mutagenesisi81G → S: Reduces client protein activation activity, leading to growth defect at high temperatures. 1 Publication1
Mutagenesisi83G → D: Abolishes ATPase activity. 1 Publication1
Mutagenesisi97A → I: Abolishes interaction with SBA1. 1 Publication1
Mutagenesisi101T → I: Causes a 90% reduction in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. 1 Publication1
Mutagenesisi107A → N: Induces a 6-fold increase in ATPase activity. 1 Publication1
Mutagenesisi170G → D: Induces a total loss of function at 34 degrees Celsius. Abolishes interaction with SBA1. 1 Publication1
Mutagenesisi313G → N or S: Reduces client protein activation activity, leading to growth defect at high temperatures. 2 Publications1
Mutagenesisi349F → A or Q: Induces a loss of ATPase activity. Can be reactivated by AHA1. 1 Publication1
Mutagenesisi380R → A: Induces a loss of ATPase activity. 1 Publication1
Mutagenesisi381E → K: Reduces client protein activation activity. Resistant to ATPase activation by AHA1. 1 Publication1
Mutagenesisi384Q → A: Induces a loss of ATPase activity. 1 Publication1
Mutagenesisi387K → A: Decreases AHA1 binding affinity, but has no effect on client protein activation activity. 1 Publication1
Mutagenesisi387K → D: Decreases AHA1 binding affinity and substantially reduces client protein activation activity. 1 Publication1
Mutagenesisi431E → K: Specifically reduces the activation of the exogenous ligand glucocorticoid receptor. 1 Publication1
Mutagenesisi485S → Y: Abolishes interaction with SBA1. 1 Publication1
Mutagenesisi525T → I: Abolishes interaction with SBA1. Reduces client protein activation activity, leading to growth defect at high temperatures. 1 Publication1
Mutagenesisi576A → T: Reduces client protein activation activity; when associated with K-579. 1 Publication1
Mutagenesisi577A → C: Enhances ATPase activity and client protein activation. 1 Publication1
Mutagenesisi577A → D: Reduces ATPase activity and client protein activation. 1 Publication1
Mutagenesisi577A → I: Enhances homodimerization, ATPase activity and client protein activation. 1 Publication1
Mutagenesisi577A → N: Reduces homodimerization, ATPase activity and client protein activation. 1 Publication1
Mutagenesisi579R → K: Reduces client protein activation activity; when associated with T-576. 1 Publication1
Mutagenesisi587A → T: No effect on ATPase activity. Reduces client protein activation activity, leading to growth defect at high temperatures. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3536

<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_00000629571 – 709ATP-dependent molecular chaperone HSP82Add BLAST709

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 residuei657PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P02829

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

More...
PaxDbi
P02829

PRoteomics IDEntifications database

More...
PRIDEi
P02829

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P02829

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P02829

<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expressed constitutively and induced by high temperatures dependent on transcription factor HSF1. According to PubMed:2674684, it is constitutively expressed at low levels, however, due to the specificity of the antibody, this result is unsure.2 Publications

<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. Interacts with the co-chaperones AHA1, CDC37, CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1. Interacts directly with the substrates GCN2, HAP1 and STE11.18 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
35923, 1614 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1276 HMC complex

Database of interacting proteins

More...
DIPi
DIP-2262N

Protein interaction database and analysis system

More...
IntActi
P02829, 381 interactors

Molecular INTeraction database

More...
MINTi
P02829

STRING: functional protein association networks

More...
STRINGi
4932.YPL240C

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P02829

<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

1709
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P02829

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

More...
SMRi
P02829

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P02829

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati221 – 22511 Publication5
Repeati226 – 23021 Publication5
Repeati231 – 23531 Publication5
Repeati237 – 24141 Publication5
Repeati250 – 25451 Publication5

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>Regioni221 – 2635 X 5 AA repeats of [DE]-[DE]-[DE]-K-K; highly charged regionAdd BLAST43

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>Motifi705 – 709TPR 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 like the co-chaperones AHA1, CDC37, CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1.

<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

Keywords - Domaini

Repeat

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153338

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000031988

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P02829

KEGG Orthology (KO)

More...
KOi
K04079

Identification of Orthologs from Complete Genome Data

More...
OMAi
VKRHSEF

Database of Orthologous Groups

More...
OrthoDBi
EOG092C1GW3

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00075 HATPase_c, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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

HAMAP database of protein families

More...
HAMAPi
MF_00505 HSP90, 1 hit

Integrated resource of protein families, domains and functional sites

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

The PANTHER Classification System

More...
PANTHERi
PTHR11528 PTHR11528, 1 hit

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF002583 Hsp90, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00775 HEATSHOCK90

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00387 HATPase_c, 1 hit

Superfamily database of structural and functional annotation

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

PROSITE; a protein domain and family database

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

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

P02829-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYKSL
60 70 80 90 100
SDPKQLETEP DLFIRITPKP EQKVLEIRDS GIGMTKAELI NNLGTIAKSG
110 120 130 140 150
TKAFMEALSA GADVSMIGQF GVGFYSLFLV ADRVQVISKS NDDEQYIWES
160 170 180 190 200
NAGGSFTVTL DEVNERIGRG TILRLFLKDD QLEYLEEKRI KEVIKRHSEF
210 220 230 240 250
VAYPIQLVVT KEVEKEVPIP EEEKKDEEKK DEEKKDEDDK KPKLEEVDEE
260 270 280 290 300
EEKKPKTKKV KEEVQEIEEL NKTKPLWTRN PSDITQEEYN AFYKSISNDW
310 320 330 340 350
EDPLYVKHFS VEGQLEFRAI LFIPKRAPFD LFESKKKKNN IKLYVRRVFI
360 370 380 390 400
TDEAEDLIPE WLSFVKGVVD SEDLPLNLSR EMLQQNKIMK VIRKNIVKKL
410 420 430 440 450
IEAFNEIAED SEQFEKFYSA FSKNIKLGVH EDTQNRAALA KLLRYNSTKS
460 470 480 490 500
VDELTSLTDY VTRMPEHQKN IYYITGESLK AVEKSPFLDA LKAKNFEVLF
510 520 530 540 550
LTDPIDEYAF TQLKEFEGKT LVDITKDFEL EETDEEKAER EKEIKEYEPL
560 570 580 590 600
TKALKEILGD QVEKVVVSYK LLDAPAAIRT GQFGWSANME RIMKAQALRD
610 620 630 640 650
SSMSSYMSSK KTFEISPKSP IIKELKKRVD EGGAQDKTVK DLTKLLYETA
660 670 680 690 700
LLTSGFSLDE PTSFASRINR LISLGLNIDE DEETETAPEA STAAPVEEVP

ADTEMEEVD
Length:709
Mass (Da):81,406
Last modified:July 21, 1986 - 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:iD7C35676D668FB63
GO

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 conflicti481A → S (PubMed:12667448).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
K01387 Unassigned RNA Translation: AAA02743.1
Z67751 Genomic DNA Translation: CAA91604.1
Z73596 Genomic DNA Translation: CAA97961.1
BK006949 Genomic DNA Translation: DAA11197.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A03313 HHBY90

NCBI Reference Sequences

More...
RefSeqi
NP_015084.1, NM_001184054.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YPL240C_mRNA; YPL240C_mRNA; YPL240C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855836

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YPL240C

<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
K01387 Unassigned RNA Translation: AAA02743.1
Z67751 Genomic DNA Translation: CAA91604.1
Z73596 Genomic DNA Translation: CAA97961.1
BK006949 Genomic DNA Translation: DAA11197.1
PIRiA03313 HHBY90
RefSeqiNP_015084.1, NM_001184054.1

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
1A4HX-ray2.50A1-220[»]
1AH6X-ray1.80A1-220[»]
1AH8X-ray2.10A/B1-220[»]
1AM1X-ray2.00A2-214[»]
1AMWX-ray1.85A1-214[»]
1BGQX-ray2.50A1-214[»]
1HK7X-ray2.50A/B273-560[»]
1US7X-ray2.30A1-214[»]
1USUX-ray2.15A273-530[»]
1USVX-ray2.70A/C/E/G272-530[»]
1ZW9X-ray1.90A1-220[»]
1ZWHX-ray1.65A1-220[»]
2AKPX-ray1.94A/B25-210[»]
2BRCX-ray1.60A1-214[»]
2BREX-ray2.00A/B1-219[»]
2CG9X-ray3.10A/B1-677[»]
2CGEX-ray3.00A/B/D273-677[»]
2CGFX-ray2.20A1-214[»]
2FXSX-ray2.00A1-220[»]
2IWSX-ray2.70A1-214[»]
2IWUX-ray2.80A1-214[»]
2IWXX-ray1.50A1-214[»]
2LSVNMR-B701-709[»]
2VW5X-ray1.90A/B/C/D1-214[»]
2VWCX-ray2.40A1-219[»]
2WEPX-ray2.00A1-220[»]
2WEQX-ray2.20A1-220[»]
2WERX-ray1.60A/B1-220[»]
2XD6X-ray2.20A1-214[»]
2XX2X-ray1.85A/B/C/D1-214[»]
2XX4X-ray2.20A1-214[»]
2XX5X-ray2.00A1-214[»]
2YGAX-ray2.37A1-220[»]
2YGEX-ray1.96A1-220[»]
2YGFX-ray2.00A1-220[»]
3C0EX-ray1.90A1-220[»]
3C11X-ray1.60A1-220[»]
3FP2X-ray1.98Q698-709[»]
4AS9X-ray2.71A1-220[»]
4ASAX-ray2.25A1-220[»]
4ASBX-ray3.08A1-220[»]
4ASFX-ray2.60A1-220[»]
4ASGX-ray2.20A1-220[»]
4CE1X-ray2.01A1-214[»]
4CE2X-ray2.38A1-214[»]
4CE3X-ray2.31A1-214[»]
5MGXX-ray2.18A/B/C/D702-709[»]
ProteinModelPortaliP02829
SMRiP02829
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35923, 1614 interactors
ComplexPortaliCPX-1276 HMC complex
DIPiDIP-2262N
IntActiP02829, 381 interactors
MINTiP02829
STRINGi4932.YPL240C

Chemistry databases

BindingDBiP02829
ChEMBLiCHEMBL3536

PTM databases

iPTMnetiP02829

2D gel databases

SWISS-2DPAGEiP02829

Proteomic databases

MaxQBiP02829
PaxDbiP02829
PRIDEiP02829

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL240C_mRNA; YPL240C_mRNA; YPL240C
GeneIDi855836
KEGGisce:YPL240C

Organism-specific databases

SGDiS000006161 HSP82

Phylogenomic databases

GeneTreeiENSGT00940000153338
HOGENOMiHOG000031988
InParanoidiP02829
KOiK04079
OMAiVKRHSEF
OrthoDBiEOG092C1GW3

Enzyme and pathway databases

BioCyciYEAST:G3O-34126-MONOMER

Miscellaneous databases

EvolutionaryTraceiP02829

Protein Ontology

More...
PROi
PR:P02829

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
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

More...
ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHSP82_YEAST
<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: P02829
Secondary accession number(s): D6W3D1
<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: July 21, 1986
Last sequence update: July 21, 1986
Last modified: December 5, 2018
This is version 214 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 programFungal 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again