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Entry version 205 (08 May 2019)
Sequence version 1 (01 Jan 1988)
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Protein

NAD-dependent histone deacetylase SIR2

Gene

SIR2

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

NAD-dependent deacetylase, which participates in a wide range of cellular events including chromosome silencing, chromosome segregation, DNA recombination and the determination of life span. Involved in transcriptional repression of the silent mating-type loci HML and HMR and telomeric silencing via its association with SIR3 and SIR4. Plays a central role in ribosomal DNA (rDNA) silencing via its association with the RENT complex, preventing hyperrecombination, and repressing transcription from foreign promoters, which contributes to extending life span. Probably represses transcription via the formation of heterochromatin structure, which involves the compaction of chromatin fiber into a more condensed form, although this complex in at least one case can still bind euchromatic levels of positive transcription regulators. Although it displays some NAD-dependent histone deacetylase activity on histone H3K9Ac and H3K14Ac and histone H4K16Ac in vitro, such activity is unclear in vivo and may not be essential.6 Publications

Miscellaneous

Its stability is directly linked to life span, which is extended when it is present in high dosage. Conversely, its absence shortens life span.
The reported ADP-ribosyltransferase activity of sirtuins is likely some inefficient side reaction of the deacetylase activity and may not be physiologically relevant.1 Publication
Present with 3350 molecules/cell in log phase SD medium.1 Publication

Caution

Was originally thought to be an ADP-ribosyltransferase.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+1 PublicationNote: Binds 1 zinc ion per subunit.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

Its activity is increased by calorie restriction, which slows the pace of aging and increases maximum lifespan. Activated by resveratrol (3,5,4'-trihydroxy-trans-stilbene), which is found in red wine.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=29.3 µM for NAD+1 Publication
  2. KM=239 µM for a synthetic histone H3K9 acetyllysine peptide1 Publication
  3. KM=420 µM for a synthetic histone H3K14 acetyllysine peptide1 Publication
  4. KM=140 µM for a synthetic histone H4K5 acetyllysine peptide1 Publication
  5. KM=54 µM for a synthetic histone H4K8 acetyllysine peptide1 Publication
  6. KM=105 µM for a synthetic histone H4K12 acetyllysine peptide1 Publication
  7. KM=17 µM for a synthetic histone H4K16 acetyllysine peptide1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei364Proton acceptorPROSITE-ProRule annotation1
    <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 bindingi372Zinc2 Publications1
    Metal bindingi375Zinc2 Publications1
    Metal bindingi396Zinc2 Publications1
    Metal bindingi399Zinc2 Publications1
    <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 sitei513NAD; via amide nitrogen1 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 bindingi262 – 281NAD2 PublicationsAdd BLAST20
    Nucleotide bindingi344 – 347NADBy similarity4
    Nucleotide bindingi471 – 473NAD1 Publication3
    Nucleotide bindingi496 – 498NAD1 Publication3

    <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 functionChromatin regulator, Hydrolase, Repressor
    Biological processDNA damage, DNA repair, Transcription, Transcription regulation
    LigandMetal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER3O-4152
    YEAST:MONOMER3O-4152

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-SCE-3371453 Regulation of HSF1-mediated heat shock response

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P06700

    <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:
    NAD-dependent histone deacetylase SIR2 (EC:3.5.1.-)
    Alternative name(s):
    Regulatory protein SIR2
    Silent information regulator 2
    <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:SIR2
    Synonyms:MAR1
    Ordered Locus Names:YDL042C
    ORF Names:D2714
    <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 IV

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    FungiDB:YDL042C

    Saccharomyces Genome Database

    More...
    SGDi
    S000002200 SIR2

    <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

    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>Mutagenesisi139R → K: Defects in telomeric silencing. 1 Publication1
    Mutagenesisi270G → E: Defects in telomeric silencing. 1 Publication1
    Mutagenesisi296F → L: Defects in telomeric silencing. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3275

    <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_00001102801 – 562NAD-dependent histone deacetylase SIR2Add BLAST562

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P06700

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

    More...
    PaxDbi
    P06700

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P06700

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P06700

    <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

    Homomultimer. Forms a complex with SIR3 and SIR4 (PubMed:9122169). Component of the RENT complex, at least composed of SIR2, CDC14 and NET1 (PubMed:10219244, PubMed:10219245). The RENT complex interacts with FOB1 (PubMed:12923057). Interacts with ESC8 (PubMed:12399377). Interacts with and ZDS2 (PubMed:10662670). Interacts with MCM10 (PubMed:16328881). Interacts with SLX5 (PubMed:18086879). Interacts with NSI1 (PubMed:22362748).9 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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    32017, 366 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-1669 RENT complex
    CPX-1811 Sir2-3-4 silent chromatin complex

    Database of interacting proteins

    More...
    DIPi
    DIP-596N

    Protein interaction database and analysis system

    More...
    IntActi
    P06700, 49 interactors

    Molecular INTeraction database

    More...
    MINTi
    P06700

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YDL042C

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P06700

    <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

    1562
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    2HJHX-ray1.85A/B209-562[»]
    4IAOX-ray2.90A/B87-562[»]

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

    More...
    SMRi
    P06700

    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
    P06700

    <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>Domaini245 – 529Deacetylase sirtuin-typePROSITE-ProRule annotationAdd BLAST285

    <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 sirtuin family. Class I subfamily.Curated

    Phylogenomic databases

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000159406

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000191845

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P06700

    KEGG Orthology (KO)

    More...
    KOi
    K11121

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    AINKVLC

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.1600.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029035 DHS-like_NAD/FAD-binding_dom
    IPR007654 NAD-dep_histone_deAcase_SIR2_N
    IPR003000 Sirtuin
    IPR026591 Sirtuin_cat_small_dom_sf
    IPR026590 Ssirtuin_cat_dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF04574 DUF592, 1 hit
    PF02146 SIR2, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52467 SSF52467, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50305 SIRTUIN, 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.

    P06700-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTIPHMKYAV SKTSENKVSN TVSPTQDKDA IRKQPDDIIN NDEPSHKKIK
    60 70 80 90 100
    VAQPDSLRET NTTDPLGHTK AALGEVASME LKPTNDMDPL AVSAASVVSM
    110 120 130 140 150
    SNDVLKPETP KGPIIISKNP SNGIFYGPSF TKRESLNARM FLKYYGAHKF
    160 170 180 190 200
    LDTYLPEDLN SLYIYYLIKL LGFEVKDQAL IGTINSIVHI NSQERVQDLG
    210 220 230 240 250
    SAISVTNVED PLAKKQTVRL IKDLQRAINK VLCTRLRLSN FFTIDHFIQK
    260 270 280 290 300
    LHTARKILVL TGAGVSTSLG IPDFRSSEGF YSKIKHLGLD DPQDVFNYNI
    310 320 330 340 350
    FMHDPSVFYN IANMVLPPEK IYSPLHSFIK MLQMKGKLLR NYTQNIDNLE
    360 370 380 390 400
    SYAGISTDKL VQCHGSFATA TCVTCHWNLP GERIFNKIRN LELPLCPYCY
    410 420 430 440 450
    KKRREYFPEG YNNKVGVAAS QGSMSERPPY ILNSYGVLKP DITFFGEALP
    460 470 480 490 500
    NKFHKSIRED ILECDLLICI GTSLKVAPVS EIVNMVPSHV PQVLINRDPV
    510 520 530 540 550
    KHAEFDLSLL GYCDDIAAMV AQKCGWTIPH KKWNDLKNKN FKCQEKDKGV
    560
    YVVTSDEHPK TL
    Length:562
    Mass (Da):63,262
    Last modified:January 1, 1988 - 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:i52E6937533654586
    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
    X01419 Genomic DNA Translation: CAA25667.1
    Z71781 Genomic DNA Translation: CAA96447.1
    Z74090 Genomic DNA Translation: CAA98600.1
    BK006938 Genomic DNA Translation: DAA11814.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S05891 RGBYS2

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_010242.1, NM_001180101.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YDL042C_mRNA; YDL042C_mRNA; YDL042C

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    851520

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YDL042C

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Protein Spotlight

    In vino vita? - Issue 40 of November 2003

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X01419 Genomic DNA Translation: CAA25667.1
    Z71781 Genomic DNA Translation: CAA96447.1
    Z74090 Genomic DNA Translation: CAA98600.1
    BK006938 Genomic DNA Translation: DAA11814.1
    PIRiS05891 RGBYS2
    RefSeqiNP_010242.1, NM_001180101.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2HJHX-ray1.85A/B209-562[»]
    4IAOX-ray2.90A/B87-562[»]
    SMRiP06700
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi32017, 366 interactors
    ComplexPortaliCPX-1669 RENT complex
    CPX-1811 Sir2-3-4 silent chromatin complex
    DIPiDIP-596N
    IntActiP06700, 49 interactors
    MINTiP06700
    STRINGi4932.YDL042C

    Chemistry databases

    BindingDBiP06700
    ChEMBLiCHEMBL3275

    PTM databases

    iPTMnetiP06700

    Proteomic databases

    MaxQBiP06700
    PaxDbiP06700
    PRIDEiP06700

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYDL042C_mRNA; YDL042C_mRNA; YDL042C
    GeneIDi851520
    KEGGisce:YDL042C

    Organism-specific databases

    EuPathDBiFungiDB:YDL042C
    SGDiS000002200 SIR2

    Phylogenomic databases

    GeneTreeiENSGT00940000159406
    HOGENOMiHOG000191845
    InParanoidiP06700
    KOiK11121
    OMAiAINKVLC

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER3O-4152
    YEAST:MONOMER3O-4152
    ReactomeiR-SCE-3371453 Regulation of HSF1-mediated heat shock response
    SABIO-RKiP06700

    Miscellaneous databases

    EvolutionaryTraceiP06700

    Protein Ontology

    More...
    PROi
    PR:P06700

    Family and domain databases

    Gene3Di3.30.1600.10, 1 hit
    InterProiView protein in InterPro
    IPR029035 DHS-like_NAD/FAD-binding_dom
    IPR007654 NAD-dep_histone_deAcase_SIR2_N
    IPR003000 Sirtuin
    IPR026591 Sirtuin_cat_small_dom_sf
    IPR026590 Ssirtuin_cat_dom
    PfamiView protein in Pfam
    PF04574 DUF592, 1 hit
    PF02146 SIR2, 1 hit
    SUPFAMiSSF52467 SSF52467, 1 hit
    PROSITEiView protein in PROSITE
    PS50305 SIRTUIN, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSIR2_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: P06700
    Secondary accession number(s): D6VRV4
    <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: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: May 8, 2019
    This is version 205 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. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families
    5. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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