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Entry version 182 (26 Feb 2020)
Sequence version 3 (23 Jan 2007)
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Protein

Acetyl-CoA acetyltransferase

Gene

ERG10

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

Catalyzes the formation of acetoacetyl-CoA in the biosynthesis of mevalonate, an intermediate required for the biosynthesis of sterols and nonsterol isoprenoids.

Miscellaneous

Present with 60895 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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=0.16 mM for CoA1 Publication
  2. KM=0.35 mM for acetoacetyl-CoA1 Publication

    pH dependencei

    Optimum pH is 8.8.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: (R)-mevalonate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes (R)-mevalonate from acetyl-CoA.
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Acetyl-CoA acetyltransferase (ERG10)
    2. Hydroxymethylglutaryl-CoA synthase (ERG13)
    3. 3-hydroxy-3-methylglutaryl-coenzyme A reductase 2 (HMG2), 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 (HMG1)
    This subpathway is part of the pathway (R)-mevalonate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-mevalonate from acetyl-CoA, the pathway (R)-mevalonate biosynthesis and in Metabolic intermediate biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei91Acyl-thioester intermediateBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi186PotassiumBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei186Coenzyme ABy similarity1
    Binding sitei231Coenzyme ABy similarity1
    Metal bindingi248Potassium; via carbonyl oxygenBy similarity1
    Metal bindingi249Potassium; via carbonyl oxygenBy similarity1
    Metal bindingi251Potassium; via carbonyl oxygenBy similarity1
    Binding sitei252Coenzyme ABy similarity1
    Metal bindingi350Potassium; via carbonyl oxygenBy similarity1
    Active sitei354Proton acceptorPROSITE-ProRule annotation1
    Active sitei384Proton acceptorPROSITE-ProRule annotation1

    <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

    • acetyl-CoA C-acetyltransferase activity Source: SGD
    • acetyl-CoA C-acyltransferase activity Source: GO_Central
    • metal ion binding Source: UniProtKB-KW

    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 functionAcyltransferase, Transferase
    LigandMetal-binding, Potassium

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:YPL028W-MONOMER
    YEAST:YPL028W-MONOMER

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00058;UER00101

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

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Acetyl-CoA acetyltransferase (EC:2.3.1.9)
    Alternative name(s):
    Acetoacetyl-CoA thiolase
    Ergosterol biosynthesis protein 10
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:ERG10
    Ordered Locus Names:YPL028W
    ORF Names:LPB3
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XVI

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    FungiDB:YPL028W

    Saccharomyces Genome Database

    More...
    SGDi
    S000005949 ERG10

    <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

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002064162 – 398Acetyl-CoA acetyltransferaseAdd BLAST397

    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 residuei2N-acetylserineCombined sources1 Publication1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P41338

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

    More...
    PaxDbi
    P41338

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P41338

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P41338

    <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

    Induced by low intracellular sterol levels.1 Publication

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

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

    Multimeric.

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    36150, 263 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-6396N

    Protein interaction database and analysis system

    More...
    IntActi
    P41338, 9 interactors

    Molecular INTeraction database

    More...
    MINTi
    P41338

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YPL028W

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P41338 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

    1398
    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

    More...
    SMRi
    P41338

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    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

    <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

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_031026_0_1_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P41338

    KEGG Orthology (KO)

    More...
    KOi
    K00626

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    LMAGQGQ

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00751 thiolase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.47.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002155 Thiolase
    IPR016039 Thiolase-like
    IPR020615 Thiolase_acyl_enz_int_AS
    IPR020610 Thiolase_AS
    IPR020617 Thiolase_C
    IPR020613 Thiolase_CS
    IPR020616 Thiolase_N

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02803 Thiolase_C, 1 hit
    PF00108 Thiolase_N, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000429 Ac-CoA_Ac_transf, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53901 SSF53901, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01930 AcCoA-C-Actrans, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00098 THIOLASE_1, 1 hit
    PS00737 THIOLASE_2, 1 hit
    PS00099 THIOLASE_3, 1 hit

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

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

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

    P41338-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSQNVYIVST ARTPIGSFQG SLSSKTAVEL GAVALKGALA KVPELDASKD
    60 70 80 90 100
    FDEIIFGNVL SANLGQAPAR QVALAAGLSN HIVASTVNKV CASAMKAIIL
    110 120 130 140 150
    GAQSIKCGNA DVVVAGGCES MTNAPYYMPA ARAGAKFGQT VLVDGVERDG
    160 170 180 190 200
    LNDAYDGLAM GVHAEKCARD WDITREQQDN FAIESYQKSQ KSQKEGKFDN
    210 220 230 240 250
    EIVPVTIKGF RGKPDTQVTK DEEPARLHVE KLRSARTVFQ KENGTVTAAN
    260 270 280 290 300
    ASPINDGAAA VILVSEKVLK EKNLKPLAII KGWGEAAHQP ADFTWAPSLA
    310 320 330 340 350
    VPKALKHAGI EDINSVDYFE FNEAFSVVGL VNTKILKLDP SKVNVYGGAV
    360 370 380 390
    ALGHPLGCSG ARVVVTLLSI LQQEGGKIGV AAICNGGGGA SSIVIEKI
    Length:398
    Mass (Da):41,729
    Last modified:January 23, 2007 - v3
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE835A8E040629A5C
    GO

    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
    L20428 Genomic DNA Translation: AAA62378.1
    U36624 Genomic DNA Translation: AAB68159.1
    BK006949 Genomic DNA Translation: DAA11401.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A55654

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_015297.1, NM_001183842.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YPL028W_mRNA; YPL028W; YPL028W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    856079

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YPL028W

    <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
    L20428 Genomic DNA Translation: AAA62378.1
    U36624 Genomic DNA Translation: AAB68159.1
    BK006949 Genomic DNA Translation: DAA11401.1
    PIRiA55654
    RefSeqiNP_015297.1, NM_001183842.1

    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
    5XYJX-ray1.93A/B1-398[»]
    5XZ5X-ray2.20A/B1-398[»]
    SMRiP41338
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi36150, 263 interactors
    DIPiDIP-6396N
    IntActiP41338, 9 interactors
    MINTiP41338
    STRINGi4932.YPL028W

    PTM databases

    iPTMnetiP41338

    Proteomic databases

    MaxQBiP41338
    PaxDbiP41338
    PRIDEiP41338

    Genome annotation databases

    EnsemblFungiiYPL028W_mRNA; YPL028W; YPL028W
    GeneIDi856079
    KEGGisce:YPL028W

    Organism-specific databases

    EuPathDBiFungiDB:YPL028W
    SGDiS000005949 ERG10

    Phylogenomic databases

    HOGENOMiCLU_031026_0_1_1
    InParanoidiP41338
    KOiK00626
    OMAiLMAGQGQ

    Enzyme and pathway databases

    UniPathwayiUPA00058;UER00101
    BioCyciMetaCyc:YPL028W-MONOMER
    YEAST:YPL028W-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P41338
    RNActiP41338 protein

    Family and domain databases

    CDDicd00751 thiolase, 1 hit
    Gene3Di3.40.47.10, 1 hit
    InterProiView protein in InterPro
    IPR002155 Thiolase
    IPR016039 Thiolase-like
    IPR020615 Thiolase_acyl_enz_int_AS
    IPR020610 Thiolase_AS
    IPR020617 Thiolase_C
    IPR020613 Thiolase_CS
    IPR020616 Thiolase_N
    PfamiView protein in Pfam
    PF02803 Thiolase_C, 1 hit
    PF00108 Thiolase_N, 1 hit
    PIRSFiPIRSF000429 Ac-CoA_Ac_transf, 1 hit
    SUPFAMiSSF53901 SSF53901, 2 hits
    TIGRFAMsiTIGR01930 AcCoA-C-Actrans, 1 hit
    PROSITEiView protein in PROSITE
    PS00098 THIOLASE_1, 1 hit
    PS00737 THIOLASE_2, 1 hit
    PS00099 THIOLASE_3, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    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 nameiTHIL_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: P41338
    Secondary accession number(s): D6W3Y5
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 23, 2007
    Last modified: February 26, 2020
    This is version 182 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation 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, Direct protein sequencing, Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. Yeast chromosome XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    UniProt is an ELIXIR core data resource
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