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Entry version 185 (11 Dec 2019)
Sequence version 2 (01 Feb 1996)
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Protein

Heat shock protein 104

Gene

HSP104

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

Required, in concert with Hsp40 (YDJ1) and Hsp70 (SSA1) and small Hsps (HSP26), for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by components of the Hsp70/Hsp40 chaperone system. Substrate binding is ATP-dependent, and release of bound polypeptide is triggered by ATP hydrolysis. Also responsible for the maintenance of prions by dissociating prion fibrils into smaller oligomers, thereby producing transmissible seeds that can infect daughter cells during mitosis and meiosis. Loss of HSP104 can cure yeast cells of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+].25 Publications

Miscellaneous

Present with 32800 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Inhibited by micromolar concentrations of guanidinium chloride. Inhibits the ATPase activity, but does not dissociate the hexameric protein.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=170 µM for ATP (at NBD1)5 Publications
  2. KM=4.7 µM for ATP (at NBD2)5 Publications
  1. Vmax=1.25 nmol/min/µg enzyme for ATP5 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi212 – 219ATP 1Sequence analysis8
Nucleotide bindingi614 – 621ATP 2Sequence analysis8

<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

BioCyc Collection of Pathway/Genome Databases

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BioCyci
YEAST:G3O-32130-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P31539

<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 104
Alternative name(s):
Protein aggregation-remodeling factor HSP104
<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:HSP104
Ordered Locus Names:YLL026W
ORF Names:L0948
<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 XII

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
FungiDB:YLL026W

Saccharomyces Genome Database

More...
SGDi
S000003949 HSP104

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

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

Mutagenesis

Feature 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>Mutagenesisi184D → A, D, F, N, L, Q or S: Confers resistance to prion-curing by guanidine. 1 Publication1
Mutagenesisi184D → K, W or Y: Impairs prion propagation. 1 Publication1
Mutagenesisi217G → S: Largely reduces ATP hydrolysis. Alters bud morphology and causes septin mislocalization; when associated with I-499. 3 Publications1
Mutagenesisi217G → V: Completely abolishes ATP hydrolysis. 3 Publications1
Mutagenesisi218K → T: Abolishes substrate binding. Unable to confer thermotolerance. Reduces ATP hydrolysis by 98%; when associated with T-315. Comletely abolishes ATPase activity; when associated with T-620. 10 Publications1
Mutagenesisi257Y → A: Reduces thermotolerance 10-fold. 1 Publication1
Mutagenesisi285E → Q in HSP104(TRAP); completely abolishes ATP hydrolysis, but does not affect nucleotide binding, thus keeping HSP104 in an ATP-bound state; when associated with Q-687. 2 Publications1
Mutagenesisi315A → T: Reduces ATP hydrolysis by 98%; when associated with T-218. 1 Publication1
Mutagenesisi317T → A: Reduces rate of ATP hydrolysis at NBD1 nearly 10-fold. No effect on oligomerization. 2 Publications1
Mutagenesisi334R → M: Reduces ATPase activity by 80%. Impairs oligomerization. 1 Publication1
Mutagenesisi419R → M: Reduces ATPase activity by 80%. 1 Publication1
Mutagenesisi444R → M: Reduces ATPase activity by 80%. 1 Publication1
Mutagenesisi462L → R: Impairs prion propagation, but does not affect thermotolerance. 1 Publication1
Mutagenesisi495R → M: Increases ATPase activity 3-fold. 1 Publication1
Mutagenesisi499T → I: Reduces ATP hydrolysis by 50%. Alters bud morphology and causes septin mislocalization; when associated with S-217. 1 Publication1
Mutagenesisi503A → V: Increases basal level of ATPase activity and abolishes stimulation of ATP hydrolysis upon substrate binding. Inhibits growth at 37 degrees Celsius. 2 Publications1
Mutagenesisi509A → D: Reduces thermotolerance. 1 Publication1
Mutagenesisi557P → L: Impairs prion propagation, but does not affect thermotolerance. 1 Publication1
Mutagenesisi619G → V: Impairs oligomerization at low protein concentrations. 2 Publications1
Mutagenesisi620K → T: Impairs oligomerization at low protein concentrations. Reduces ATP hydrolysis rate. Unable to confer thermotolerance. Comletely abolishes ATPase activity; when associated with T-218. 9 Publications1
Mutagenesisi621T → A: Reduces ATP hydrolysis, but does not affect oligomerization. 1 Publication1
Mutagenesisi645E → K: Abolishes the ability to refold aggregated protein in vitro and to provide thermotolerance in vivo. 1 Publication1
Mutagenesisi662Y → A or K: Abolishes the ability to refold aggregated protein in vitro and to provide thermotolerance in vivo. 1 Publication1
Mutagenesisi662Y → F or W: No effect. 1 Publication1
Mutagenesisi687E → Q in HSP104(TRAP); completely abolishes ATP hydrolysis, but does not affect nucleotide binding, thus keeping HSP104 in an ATP-bound state; when associated with Q-285. 2 Publications1
Mutagenesisi704D → N: Impairs prion propagation, but does not affect thermotolerance. 1 Publication1
Mutagenesisi728N → A: Almost completely abolishes ATP hydrolysis at NBD2, but does not affect nucleotide binding, thus keeping NBD2 in an ATP-bound state. Reduces stimulation of ATP hydrolysis upon substrate binding. 4 Publications1
Mutagenesisi765R → M: Can oligomerize in the absence of nucleotides. 1 Publication1
Mutagenesisi778K → A in NLS17KA; fails to concentrate in the nucleus; when associated with A-782 and A-789. 1 Publication1
Mutagenesisi782K → A in NLS17KA; fails to concentrate in the nucleus; when associated with A-778 and A-789. 1 Publication1
Mutagenesisi789K → A in NLS17KA; fails to concentrate in the nucleus; when associated with A-778 and A-782. 1 Publication1
Mutagenesisi819Y → W: Site-specific fluorescent probe in an otherwise Trp-less HSP104. Fluorescence of this Trp changes in response to ATP and ADP binding at NBD2. Has no effect on ATP hydrolysis or protein stability. 1 Publication1
Mutagenesisi826R → M: Reduces ATP and ADP binding at NBD2 6-fold, but does not affect ATP hydrolysis at NBD2. Reduces catalytic rate at NBD1. 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_00001912121 – 908Heat shock protein 104Add BLAST908

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 residuei1N-acetylmethionineCombined sources1
Modified residuei206PhosphoserineCombined sources1
Modified residuei306PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki442Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei499PhosphothreonineCombined sources1
Modified residuei535PhosphoserineCombined sources1
Cross-linki620Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
P31539

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

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PaxDbi
P31539

PRoteomics IDEntifications database

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PRIDEi
P31539

2D gel databases

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

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SWISS-2DPAGEi
P31539

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P31539

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P31539

<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

By heat stress dependent on the heat shock transcription factor HSF1 and the general stress transcription factors MSN2 and MSN4. Expressed at a higher level in respiring cells than in fermenting cells. Expressed in stationary phase cells and spores (at protein level).5 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

Homohexamer, forming a ring with a central pore. The hexamer is stabilized by high protein concentrations and by ADP or ATP. Oligomerization influences ATP hydrolysis activity at NBD2.

Interacts with YDJ1.

Interacts (via C-terminal DDLD tetrapeptide) with CNS1, CPR7 and STI1 (via TPR repeats); under respiratory growth conditions.

8 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

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GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
31226, 471 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1861 GET4-GET5 transmembrane domain recognition complex

Database of interacting proteins

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DIPi
DIP-2252N

Protein interaction database and analysis system

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IntActi
P31539, 28 interactors

Molecular INTeraction database

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MINTi
P31539

STRING: functional protein association networks

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STRINGi
4932.YLL026W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P31539 protein

<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

1908
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
P31539

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini4 – 150Clp RPROSITE-ProRule annotationAdd BLAST147

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>Regioni7 – 76Repeat 1PROSITE-ProRule annotationAdd BLAST70
Regioni88 – 150Repeat 2PROSITE-ProRule annotationAdd BLAST63
Regioni167 – 411NBD1Add BLAST245
Regioni541 – 731NBD2Add BLAST191
Regioni905 – 908Interaction surface for TPR repeats4

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili412 – 536Sequence analysisAdd BLAST125

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>Motifi773 – 789Nuclear localization signalAdd BLAST17

<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

Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per monomer, a low-affinity, high-turnover site (NBD1) and a high-affinity site (NBD2) with a 300-fold slower rate of hydrolysis. There is allosteric regulation between the 2 sites. ATP binding to NBD1 triggers binding of polypeptides and stimulates ATP hydrolysis at NBD2. Nucleotide binding to NBD2 is crucial for oligomerization.
The C-terminal extension is involved in oligomerization.

<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 ClpA/ClpB family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000218211

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P31539

KEGG Orthology (KO)

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KOi
K03695

Identification of Orthologs from Complete Genome Data

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OMAi
KDFGQGV

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.1780.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR019489 Clp_ATPase_C
IPR004176 Clp_N
IPR036628 Clp_N_dom_sf
IPR001270 ClpA/B
IPR018368 ClpA/B_CS1
IPR028299 ClpA/B_CS2
IPR041546 ClpA/ClpB_AAA_lid
IPR027417 P-loop_NTPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00004 AAA, 1 hit
PF07724 AAA_2, 1 hit
PF17871 AAA_lid_9, 1 hit
PF02861 Clp_N, 2 hits
PF10431 ClpB_D2-small, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00300 CLPPROTEASEA

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00382 AAA, 2 hits
SM01086 ClpB_D2-small, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540 SSF52540, 2 hits
SSF81923 SSF81923, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51903 CLP_R, 1 hit
PS00870 CLPAB_1, 1 hit
PS00871 CLPAB_2, 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.

P31539-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNDQTQFTER ALTILTLAQK LASDHQHPQL QPIHILAAFI ETPEDGSVPY
60 70 80 90 100
LQNLIEKGRY DYDLFKKVVN RNLVRIPQQQ PAPAEITPSY ALGKVLQDAA
110 120 130 140 150
KIQKQQKDSF IAQDHILFAL FNDSSIQQIF KEAQVDIEAI KQQALELRGN
160 170 180 190 200
TRIDSRGADT NTPLEYLSKY AIDMTEQARQ GKLDPVIGRE EEIRSTIRVL
210 220 230 240 250
ARRIKSNPCL IGEPGIGKTA IIEGVAQRII DDDVPTILQG AKLFSLDLAA
260 270 280 290 300
LTAGAKYKGD FEERFKGVLK EIEESKTLIV LFIDEIHMLM GNGKDDAANI
310 320 330 340 350
LKPALSRGQL KVIGATTNNE YRSIVEKDGA FERRFQKIEV AEPSVRQTVA
360 370 380 390 400
ILRGLQPKYE IHHGVRILDS ALVTAAQLAK RYLPYRRLPD SALDLVDISC
410 420 430 440 450
AGVAVARDSK PEELDSKERQ LQLIQVEIKA LERDEDADST TKDRLKLARQ
460 470 480 490 500
KEASLQEELE PLRQRYNEEK HGHEELTQAK KKLDELENKA LDAERRYDTA
510 520 530 540 550
TAADLRYFAI PDIKKQIEKL EDQVAEEERR AGANSMIQNV VDSDTISETA
560 570 580 590 600
ARLTGIPVKK LSESENEKLI HMERDLSSEV VGQMDAIKAV SNAVRLSRSG
610 620 630 640 650
LANPRQPASF LFLGLSGSGK TELAKKVAGF LFNDEDMMIR VDCSELSEKY
660 670 680 690 700
AVSKLLGTTA GYVGYDEGGF LTNQLQYKPY SVLLFDEVEK AHPDVLTVML
710 720 730 740 750
QMLDDGRITS GQGKTIDCSN CIVIMTSNLG AEFINSQQGS KIQESTKNLV
760 770 780 790 800
MGAVRQHFRP EFLNRISSIV IFNKLSRKAI HKIVDIRLKE IEERFEQNDK
810 820 830 840 850
HYKLNLTQEA KDFLAKYGYS DDMGARPLNR LIQNEILNKL ALRILKNEIK
860 870 880 890 900
DKETVNVVLK KGKSRDENVP EEAEECLEVL PNHEATIGAD TLGDDDNEDS

MEIDDDLD
Length:908
Mass (Da):102,035
Last modified:February 1, 1996 - v2
<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:i4AD0E7E3AF98E318
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M67479 Genomic DNA Translation: AAA50477.1
Z73131 Genomic DNA Translation: CAA97475.1
Z73130 Genomic DNA Translation: CAA97474.1
AY693002 Genomic DNA Translation: AAT93021.1
X97560 Genomic DNA Translation: CAA66164.1
BK006945 Genomic DNA Translation: DAA09294.1

Protein sequence database of the Protein Information Resource

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PIRi
S61476

NCBI Reference Sequences

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RefSeqi
NP_013074.1, NM_001181846.1

Genome annotation databases

Ensembl fungal genome annotation project

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EnsemblFungii
YLL026W_mRNA; YLL026W; YLL026W

Database of genes from NCBI RefSeq genomes

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GeneIDi
850633

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
sce:YLL026W

<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
M67479 Genomic DNA Translation: AAA50477.1
Z73131 Genomic DNA Translation: CAA97475.1
Z73130 Genomic DNA Translation: CAA97474.1
AY693002 Genomic DNA Translation: AAT93021.1
X97560 Genomic DNA Translation: CAA66164.1
BK006945 Genomic DNA Translation: DAA09294.1
PIRiS61476
RefSeqiNP_013074.1, NM_001181846.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5KNEelectron microscopy5.64A/B/C/D/E/F6-857[»]
5U2UX-ray2.54A/B/C1-166[»]
5VJHelectron microscopy4.00A/B/C/D/E/F1-908[»]
5VY8electron microscopy4.00A/B/C/D/E/F1-908[»]
5VY9electron microscopy4.00A/B/C/D/E/F1-908[»]
5VYAelectron microscopy4.00A/B/C/D/E/F1-908[»]
5WBWX-ray2.60A/B/D4-356[»]
6AHFelectron microscopy6.78A/B/C/D/E/F1-908[»]
6AMNX-ray2.82A4-352[»]
6N8Telectron microscopy7.70A/B/C/D/E/F6-884[»]
6N8Velectron microscopy5.64A/B/C/D/E/F6-884[»]
6N8Zelectron microscopy9.30A/B/C/D/E/F6-884[»]
SMRiP31539
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi31226, 471 interactors
ComplexPortaliCPX-1861 GET4-GET5 transmembrane domain recognition complex
DIPiDIP-2252N
IntActiP31539, 28 interactors
MINTiP31539
STRINGi4932.YLL026W

PTM databases

CarbonylDBiP31539
iPTMnetiP31539

2D gel databases

SWISS-2DPAGEiP31539

Proteomic databases

MaxQBiP31539
PaxDbiP31539
PRIDEiP31539

Genome annotation databases

EnsemblFungiiYLL026W_mRNA; YLL026W; YLL026W
GeneIDi850633
KEGGisce:YLL026W

Organism-specific databases

EuPathDBiFungiDB:YLL026W
SGDiS000003949 HSP104

Phylogenomic databases

HOGENOMiHOG000218211
InParanoidiP31539
KOiK03695
OMAiKDFGQGV

Enzyme and pathway databases

BioCyciYEAST:G3O-32130-MONOMER
SABIO-RKiP31539

Miscellaneous databases

Protein Ontology

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PROi
PR:P31539
RNActiP31539 protein

Family and domain databases

Gene3Di1.10.1780.10, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR019489 Clp_ATPase_C
IPR004176 Clp_N
IPR036628 Clp_N_dom_sf
IPR001270 ClpA/B
IPR018368 ClpA/B_CS1
IPR028299 ClpA/B_CS2
IPR041546 ClpA/ClpB_AAA_lid
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00004 AAA, 1 hit
PF07724 AAA_2, 1 hit
PF17871 AAA_lid_9, 1 hit
PF02861 Clp_N, 2 hits
PF10431 ClpB_D2-small, 1 hit
PRINTSiPR00300 CLPPROTEASEA
SMARTiView protein in SMART
SM00382 AAA, 2 hits
SM01086 ClpB_D2-small, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
SSF81923 SSF81923, 1 hit
PROSITEiView protein in PROSITE
PS51903 CLP_R, 1 hit
PS00870 CLPAB_1, 1 hit
PS00871 CLPAB_2, 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 nameiHS104_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: P31539
Secondary accession number(s): D6VXX8
<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 1, 1993
Last sequence update: February 1, 1996
Last modified: December 11, 2019
This is version 185 of the entry and version 2 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, 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. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names
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