Skip Header

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

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-Experimental evidence at protein leveli

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

Catalytic activityi

NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.PROSITE-ProRule annotation

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme 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

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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei364 – 3641Proton acceptorPROSITE-ProRule annotation
    Metal bindingi372 – 3721Zinc2 Publications
    Metal bindingi375 – 3751Zinc2 Publications
    Metal bindingi396 – 3961Zinc2 Publications
    Metal bindingi399 – 3991Zinc2 Publications
    Binding sitei513 – 5131NAD; via amide nitrogen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi262 – 28120NAD2 PublicationsAdd
    BLAST
    Nucleotide bindingi344 – 3474NADBy similarity
    Nucleotide bindingi471 – 4733NAD1 Publication
    Nucleotide bindingi496 – 4983NAD1 Publication

    GO - Molecular functioni

    • NAD+ binding Source: InterPro
    • NAD-dependent histone deacetylase activity Source: SGD
    • NAD-dependent histone deacetylase activity (H3-K14 specific) Source: SGD
    • NAD-dependent histone deacetylase activity (H3-K9 specific) Source: SGD
    • NAD-dependent histone deacetylase activity (H4-K16 specific) Source: SGD
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • chromatin assembly or disassembly Source: SGD
    • chromatin silencing at rDNA Source: SGD
    • chromatin silencing at silent mating-type cassette Source: SGD
    • chromatin silencing at telomere Source: SGD
    • chronological cell aging Source: SGD
    • DNA repair Source: UniProtKB-KW
    • histone deacetylation Source: GOC
    • histone H3 deacetylation Source: GOC
    • histone H3-K9 deacetylation Source: GOC
    • histone H3-K9 modification Source: GOC
    • histone H4 deacetylation Source: GOC
    • negative regulation of DNA recombination Source: SGD
    • negative regulation of DNA replication Source: SGD
    • replicative cell aging Source: SGD
    • transcription, DNA-templated Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    DNA damage, DNA repair, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:MONOMER3O-4152.
    ReactomeiREACT_333905. Regulation of HSF1-mediated heat shock response.
    SABIO-RKP06700.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD-dependent histone deacetylase SIR2 (EC:3.5.1.-)
    Alternative name(s):
    Regulatory protein SIR2
    Silent information regulator 2
    Gene namesi
    Name:SIR2
    Synonyms:MAR1
    Ordered Locus Names:YDL042C
    ORF Names:D2714
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome IV

    Organism-specific databases

    CYGDiYDL042c.
    EuPathDBiFungiDB:YDL042C.
    SGDiS000002200. SIR2.

    Subcellular locationi

    GO - Cellular componenti

    • chromatin silencing complex Source: SGD
    • nuclear chromosome, telomeric region Source: SGD
    • nuclear heterochromatin Source: SGD
    • nuclear telomeric heterochromatin Source: SGD
    • nucleolus Source: SGD
    • RENT complex Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi139 – 1391R → K: Defects in telomeric silencing. 1 Publication
    Mutagenesisi270 – 2701G → E: Defects in telomeric silencing. 1 Publication
    Mutagenesisi296 – 2961F → L: Defects in telomeric silencing. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 562562NAD-dependent histone deacetylase SIR2PRO_0000110280Add
    BLAST

    Proteomic databases

    MaxQBiP06700.
    PaxDbiP06700.
    PeptideAtlasiP06700.
    PRIDEiP06700.

    Expressioni

    Gene expression databases

    GenevestigatoriP06700.

    Interactioni

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC14Q006845EBI-17219,EBI-4192
    SIR4P119786EBI-17219,EBI-17237

    Protein-protein interaction databases

    BioGridi32017. 298 interactions.
    DIPiDIP-596N.
    IntActiP06700. 48 interactions.
    MINTiMINT-509141.
    STRINGi4932.YDL042C.

    Structurei

    Secondary structure

    1
    562
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi102 – 1054Combined sources
    Beta strandi111 – 1133Combined sources
    Beta strandi124 – 1263Combined sources
    Helixi132 – 15423Combined sources
    Helixi163 – 1708Combined sources
    Beta strandi173 – 1753Combined sources
    Helixi178 – 18710Combined sources
    Beta strandi213 – 2175Combined sources
    Helixi244 – 25310Combined sources
    Beta strandi255 – 2617Combined sources
    Helixi263 – 2697Combined sources
    Beta strandi274 – 2763Combined sources
    Helixi280 – 2834Combined sources
    Helixi284 – 2874Combined sources
    Helixi292 – 2965Combined sources
    Helixi298 – 3036Combined sources
    Helixi306 – 3116Combined sources
    Helixi312 – 3154Combined sources
    Helixi324 – 33411Combined sources
    Beta strandi338 – 3436Combined sources
    Helixi349 – 3524Combined sources
    Turni357 – 3593Combined sources
    Beta strandi360 – 3623Combined sources
    Beta strandi365 – 3728Combined sources
    Turni373 – 3753Combined sources
    Beta strandi378 – 3803Combined sources
    Helixi381 – 3844Combined sources
    Helixi385 – 3895Combined sources
    Turni397 – 3993Combined sources
    Helixi400 – 4067Combined sources
    Turni433 – 4364Combined sources
    Beta strandi437 – 4426Combined sources
    Helixi451 – 46010Combined sources
    Turni461 – 4633Combined sources
    Beta strandi466 – 4716Combined sources
    Helixi479 – 4813Combined sources
    Helixi482 – 4854Combined sources
    Beta strandi492 – 4987Combined sources
    Beta strandi506 – 5116Combined sources
    Helixi513 – 52412Combined sources
    Helixi533 – 5375Combined sources
    Beta strandi541 – 5477Combined sources
    Beta strandi550 – 5556Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HJHX-ray1.85A/B209-562[»]
    4IAOX-ray2.90A/B87-562[»]
    ProteinModelPortaliP06700.
    SMRiP06700. Positions 99-555.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06700.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini245 – 529285Deacetylase sirtuin-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the sirtuin family. Class I subfamily.Curated
    Contains 1 deacetylase sirtuin-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0846.
    GeneTreeiENSGT00740000115330.
    HOGENOMiHOG000191845.
    InParanoidiP06700.
    KOiK11121.
    OMAiPVKHAEF.
    OrthoDBiEOG7MWH64.

    Family and domain databases

    Gene3Di3.30.1600.10. 3 hits.
    3.40.50.1220. 3 hits.
    InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR007654. NAD-dep_histone_deAcase_SIR2_N.
    IPR003000. Sirtuin.
    IPR026591. Sirtuin_cat_small_dom.
    IPR026590. Ssirtuin_cat_dom.
    [Graphical view]
    PANTHERiPTHR11085. PTHR11085. 1 hit.
    PfamiPF04574. DUF592. 1 hit.
    PF02146. SIR2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52467. SSF52467. 2 hits.
    PROSITEiPS50305. SIRTUIN. 1 hit.
    [Graphical view]

    Sequencei

    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
    Checksum:i52E6937533654586
    GO

    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.

    Genome annotation databases

    EnsemblFungiiYDL042C; YDL042C; YDL042C.
    GeneIDi851520.
    KEGGisce:YDL042C.

    Cross-referencesi

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HJHX-ray1.85A/B209-562[»]
    4IAOX-ray2.90A/B87-562[»]
    ProteinModelPortaliP06700.
    SMRiP06700. Positions 99-555.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi32017. 298 interactions.
    DIPiDIP-596N.
    IntActiP06700. 48 interactions.
    MINTiMINT-509141.
    STRINGi4932.YDL042C.

    Chemistry

    BindingDBiP06700.
    ChEMBLiCHEMBL3275.

    Proteomic databases

    MaxQBiP06700.
    PaxDbiP06700.
    PeptideAtlasiP06700.
    PRIDEiP06700.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYDL042C; YDL042C; YDL042C.
    GeneIDi851520.
    KEGGisce:YDL042C.

    Organism-specific databases

    CYGDiYDL042c.
    EuPathDBiFungiDB:YDL042C.
    SGDiS000002200. SIR2.

    Phylogenomic databases

    eggNOGiCOG0846.
    GeneTreeiENSGT00740000115330.
    HOGENOMiHOG000191845.
    InParanoidiP06700.
    KOiK11121.
    OMAiPVKHAEF.
    OrthoDBiEOG7MWH64.

    Enzyme and pathway databases

    BioCyciYEAST:MONOMER3O-4152.
    ReactomeiREACT_333905. Regulation of HSF1-mediated heat shock response.
    SABIO-RKP06700.

    Miscellaneous databases

    EvolutionaryTraceiP06700.
    NextBioi968896.
    PROiP06700.

    Gene expression databases

    GenevestigatoriP06700.

    Family and domain databases

    Gene3Di3.30.1600.10. 3 hits.
    3.40.50.1220. 3 hits.
    InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR007654. NAD-dep_histone_deAcase_SIR2_N.
    IPR003000. Sirtuin.
    IPR026591. Sirtuin_cat_small_dom.
    IPR026590. Ssirtuin_cat_dom.
    [Graphical view]
    PANTHERiPTHR11085. PTHR11085. 1 hit.
    PfamiPF04574. DUF592. 1 hit.
    PF02146. SIR2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52467. SSF52467. 2 hits.
    PROSITEiPS50305. SIRTUIN. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Characterization of two genes required for the position-effect control of yeast mating-type genes."
      Shore D., Squire M., Nasmyth K.A.
      EMBO J. 3:2817-2823(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The sequence of a 36.7 kb segment on the left arm of chromosome IV from Saccharomyces cerevisiae reveals 20 non-overlapping open reading frames (ORFs) including SIT4, FAD1, NAM1, RNA11, SIR2, NAT1, PRP9, ACT2 and MPS1 and 11 new ORFs."
      Saren A.-M., Laamanen P., Lejarcegui J.B., Paulin L.
      Yeast 13:65-71(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Localization of Sir2p: the nucleolus as a compartment for silent information regulators."
      Gotta M., Strahl-Bolsinger S., Renauld H., Laroche T., Kennedy B.K., Grunstein M., Gasser S.M.
      EMBO J. 16:3243-3255(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    6. "An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing."
      Tanny J.C., Dowd G.J., Huang J., Hilz H., Moazed D.
      Cell 99:735-745(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY FUNCTION.
    7. "Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase."
      Imai S., Armstrong C.M., Kaeberlein M., Guarente L.
      Nature 403:795-800(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Silencing factors participate in DNA repair and recombination in Saccharomyces cerevisiae."
      Tsukamoto Y., Kato J., Ikeda H.
      Nature 388:900-903(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Silent information regulator protein complexes in Saccharomyces cerevisiae: a SIR2/SIR4 complex and evidence for a regulatory domain in SIR4 that inhibits its interaction with SIR3."
      Moazed D., Kistler A., Axelrod A., Rine J., Johnson A.D.
      Proc. Natl. Acad. Sci. U.S.A. 94:2186-2191(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIR3 AND SIR4.
    10. "Exit from mitosis is triggered by Tem1-dependent release of the protein phosphatase Cdc14 from nucleolar RENT complex."
      Shou W., Seol J.H., Shevchenko A., Baskerville C., Moazed D., Chen Z.W.S., Jang J., Shevchenko A., Charbonneau H., Deshaies R.J.
      Cell 97:233-244(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A RENT COMPLEX WITH CDC14.
    11. "Net1, a Sir2-associated nucleolar protein required for rDNA silencing and nucleolar integrity."
      Straight A.F., Shou W., Dowd G.J., Turck C.W., Deshaies R.J., Johnson A.D., Moazed D.
      Cell 97:245-256(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A RENT COMPLEX WITH NET1.
    12. "Two paralogs involved in transcriptional silencing that antagonistically control yeast life span."
      Roy N., Runge K.W.
      Curr. Biol. 10:111-114(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZDS2.
    13. "Silenced chromatin is permissive to activator binding and PIC recruitment."
      Sekinger E.A., Gross D.S.
      Cell 105:403-414(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MECHANISM OF TRANSCRIPTION REPRESSION.
    14. "The molecular biology of the SIR proteins."
      Gasser S.M., Cockell M.M.
      Gene 279:1-16(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    15. "Restoration of silencing in Saccharomyces cerevisiae by tethering of a novel Sir2-interacting protein, Esc8."
      Cuperus G., Shore D.
      Genetics 162:633-645(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ESC8.
    16. "A unique class of conditional sir2 mutants displays distinct silencing defects in Saccharomyces cerevisiae."
      Garcia S.N., Pillus L.
      Genetics 162:721-736(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-139; GLY-270 AND PHE-296.
    17. "Association of the RENT complex with nontranscribed and coding regions of rDNA and a regional requirement for the replication fork block protein Fob1 in rDNA silencing."
      Huang J., Moazed D.
      Genes Dev. 17:2162-2176(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FOB1.
    18. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    19. Cited for: ENZYME REGULATION.
    20. "Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases."
      Borra M.T., Langer M.R., Slama J.T., Denu J.M.
      Biochemistry 43:9877-9887(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    21. "Dual roles for Mcm10 in DNA replication initiation and silencing at the mating-type loci."
      Douglas N.L., Dozier S.K., Donato J.J.
      Mol. Biol. Rep. 32:197-204(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MCM10.
    22. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    23. "Slx5 promotes transcriptional silencing and is required for robust growth in the absence of Sir2."
      Darst R.P., Garcia S.N., Koch M.R., Pillus L.
      Mol. Cell. Biol. 28:1361-1372(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SLX5/HEX3.
    24. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogues and 32P-NAD."
      Du J., Jiang H., Lin H.
      Biochemistry 48:2878-2890(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    26. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Nsi1 plays a significant role in the silencing of ribosomal DNA in Saccharomyces cerevisiae."
      Ha C.W., Sung M.K., Huh W.K.
      Nucleic Acids Res. 40:4892-4903(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NSI1.
    28. "Autoregulation of the yeast Sir2 deacetylase by reaction and trapping of a pseudosubstrate motif in the active site."
      Hall B.E., Buchberger J.R., Gerber S.A., Ambrosio A.L.B., Gygi S.P., Filman D., Moazed D., Ellenberger T.
      Submitted (JUN-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 209-562 IN COMPLEX WITH ZINC AND NICOTINAMIDE.
    29. "Structural basis for allosteric stimulation of Sir2 activity by Sir4 binding."
      Hsu H.C., Wang C.L., Wang M., Yang N., Chen Z., Sternglanz R., Xu R.M.
      Genes Dev. 27:64-73(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 87-562 IN COMPLEX WITH SIR4; ADP-RIBOSE AND ZINC.

    Entry informationi

    Entry nameiSIR2_YEAST
    AccessioniPrimary (citable) accession number: P06700
    Secondary accession number(s): D6VRV4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: April 29, 2015
    This is version 168 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.