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Entry version 160 (08 May 2019)
Sequence version 1 (01 Oct 1996)
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Protein

Adenine deaminase

Gene

AAH1

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 hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism. Also exhibits a low activity towards N6-substituted adenines that are commonly known as the plant hormones cytokinins.UniRule annotation4 Publications

Miscellaneous

Present with 20700 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 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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

<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=55 µM for adenine1 Publication

    pH dependencei

    Optimum pH is 7.0.1 Publication

    Temperature dependencei

    Optimum temperature is 30-37 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi16Zinc; catalyticUniRule annotation1
    Metal bindingi18Zinc; catalyticUniRule annotation1
    Metal bindingi204Zinc; catalyticUniRule annotation1
    <p>This subsection of the ‘Function’ 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 sitei207Proton donorUniRule annotation1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei228Important for catalytic activityUniRule annotation1
    Metal bindingi285Zinc; catalyticUniRule annotation1
    <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 sitei286SubstrateUniRule 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

    • adenine deaminase activity Source: SGD
    • zinc ion binding Source: UniProtKB-UniRule

    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 functionHydrolase
    Biological processNucleotide metabolism
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    YEAST:YNL141W-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.5.4.2 984
    3.5.4.4 984

    <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:
    Adenine deaminaseUniRule annotation (EC:3.5.4.2UniRule annotation)
    Short name:
    ADEUniRule annotation
    Alternative name(s):
    Adenine aminohydrolaseUniRule annotation
    Short name:
    AAHUniRule annotation
    <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:AAH1UniRule annotation
    Ordered Locus Names:YNL141W
    ORF Names:N1208, N1825
    <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 XIV

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    FungiDB:YNL141W

    Saccharomyces Genome Database

    More...
    SGDi
    S000005085 AAH1

    <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>Mutagenesisi69I → T in aah1-2; impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. 1 Publication1
    Mutagenesisi72N → K in aah1-3; impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. 1 Publication1
    Mutagenesisi219D → G in aah1-4; impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. 1 Publication1
    Mutagenesisi237E → V in aah1-6; impairs AAH1 degradation during postdiauxic growth and leads to weak interaction with SAF1. 1 Publication1
    Mutagenesisi329K → E in aah1-7; impairs AAH1 degradation during postdiauxic growth. 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_00001943601 – 347Adenine deaminaseAdd BLAST347

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Probably ubiquitinated when cells enter quiescence in response to nutrient limitation, since it is specifically degraded via a process requiring the F-box protein SAF1 and components of the SKP1-Cullin-F-box complex.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P53909

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

    More...
    PaxDbi
    P53909

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P53909

    <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

    Reduced when grown in a poor nitrogen source medium and strongly down-regulated when cells enter quiescence under nutrient-limiting conditions.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_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

    WithEntry#Exp.IntActNotes
    SAF1P383522EBI-2197,EBI-21172

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    35686, 383 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-4342N

    Protein interaction database and analysis system

    More...
    IntActi
    P53909, 4 interactors

    Molecular INTeraction database

    More...
    MINTi
    P53909

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YNL141W

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

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

    More...
    SMRi
    P53909

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00950000183113

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P53909

    KEGG Orthology (KO)

    More...
    KOi
    K01488

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    DERLMQR

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01320 ADA, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01962 Adenine_deaminase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR006650 A/AMP_deam_AS
    IPR001365 A/AMP_deaminase_dom
    IPR028892 ADE
    IPR006330 Ado/ade_deaminase
    IPR032466 Metal_Hydrolase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00962 A_deaminase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51556 SSF51556, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01430 aden_deam, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00485 A_DEAMINASE, 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.

    P53909-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MVSVEFLQEL PKCEHHLHLE GTLEPDLLFP LAKRNDIILP EGFPKSVEEL
    60 70 80 90 100
    NEKYKKFRDL QDFLDYYYIG TNVLISEQDF FDLAWAYFKK VHKQGLVHAE
    110 120 130 140 150
    VFYDPQSHTS RGISIETVTK GFQRACDKAF SEFGITSKLI MCLLRHIEPE
    160 170 180 190 200
    ECLKTIEEAT PFIKDGTISA LGLDSAEKPF PPHLFVECYG KAASLNKDLK
    210 220 230 240 250
    LTAHAGEEGP AQFVSDALDL LQVTRIDHGI NSQYDEELLD RLSRDQTMLT
    260 270 280 290 300
    ICPLSNVKLQ VVQSVSELPL QKFLDRDVPF SLNSDDPAYF GGYILDVYTQ
    310 320 330 340
    VSKDFPHWDH ETWGRIAKNA IKGSWCDDKR KNGLLSRVDE VVTKYSH
    Length:347
    Mass (Da):39,635
    Last modified:October 1, 1996 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE25573A9F9EB7BB6
    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
    Z46843 Genomic DNA Translation: CAA86885.1
    Z71417 Genomic DNA Translation: CAA96024.1
    BK006947 Genomic DNA Translation: DAA10407.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S55143

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_014258.1, NM_001182979.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YNL141W_mRNA; YNL141W_mRNA; YNL141W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    855581

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YNL141W

    <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
    Z46843 Genomic DNA Translation: CAA86885.1
    Z71417 Genomic DNA Translation: CAA96024.1
    BK006947 Genomic DNA Translation: DAA10407.1
    PIRiS55143
    RefSeqiNP_014258.1, NM_001182979.1

    3D structure databases

    SMRiP53909
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi35686, 383 interactors
    DIPiDIP-4342N
    IntActiP53909, 4 interactors
    MINTiP53909
    STRINGi4932.YNL141W

    Proteomic databases

    MaxQBiP53909
    PaxDbiP53909
    PRIDEiP53909

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYNL141W_mRNA; YNL141W_mRNA; YNL141W
    GeneIDi855581
    KEGGisce:YNL141W

    Organism-specific databases

    EuPathDBiFungiDB:YNL141W
    SGDiS000005085 AAH1

    Phylogenomic databases

    GeneTreeiENSGT00950000183113
    InParanoidiP53909
    KOiK01488
    OMAiDERLMQR

    Enzyme and pathway databases

    BioCyciYEAST:YNL141W-MONOMER
    BRENDAi3.5.4.2 984
    3.5.4.4 984

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P53909

    Family and domain databases

    CDDicd01320 ADA, 1 hit
    HAMAPiMF_01962 Adenine_deaminase, 1 hit
    InterProiView protein in InterPro
    IPR006650 A/AMP_deam_AS
    IPR001365 A/AMP_deaminase_dom
    IPR028892 ADE
    IPR006330 Ado/ade_deaminase
    IPR032466 Metal_Hydrolase
    PfamiView protein in Pfam
    PF00962 A_deaminase, 1 hit
    SUPFAMiSSF51556 SSF51556, 1 hit
    TIGRFAMsiTIGR01430 aden_deam, 1 hit
    PROSITEiView protein in PROSITE
    PS00485 A_DEAMINASE, 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 nameiADE_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: P53909
    Secondary accession number(s): D6W141
    <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: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: May 8, 2019
    This is version 160 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

    Complete proteome, Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families
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