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P06700

- SIR2_YEAST

UniProt

P06700 - SIR2_YEAST

Protein

NAD-dependent histone deacetylase SIR2

Gene

SIR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    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

    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 – 3721Zinc1 PublicationPROSITE-ProRule annotation
    Metal bindingi375 – 3751Zinc1 PublicationPROSITE-ProRule annotation
    Metal bindingi396 – 3961Zinc1 PublicationPROSITE-ProRule annotation
    Metal bindingi399 – 3991Zinc1 PublicationPROSITE-ProRule annotation
    Binding sitei513 – 5131NAD; via amide nitrogenBy similarity

    Regions

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

    GO - Molecular functioni

    1. NAD+ binding Source: InterPro
    2. NAD-dependent histone deacetylase activity Source: SGD
    3. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: SGD
    4. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: SGD
    5. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: SGD
    6. protein binding Source: IntAct
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin assembly or disassembly Source: SGD
    2. chromatin silencing at rDNA Source: SGD
    3. chromatin silencing at silent mating-type cassette Source: SGD
    4. chromatin silencing at telomere Source: SGD
    5. chronological cell aging Source: SGD
    6. DNA repair Source: UniProtKB-KW
    7. histone deacetylation Source: GOC
    8. histone H3 deacetylation Source: GOC
    9. histone H4 deacetylation Source: GOC
    10. negative regulation of DNA recombination Source: SGD
    11. negative regulation of DNA replication Source: SGD
    12. replicative cell aging Source: SGD
    13. transcription, DNA-templated Source: UniProtKB-KW

    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.
    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: Chromosome IV

    Organism-specific databases

    CYGDiYDL042c.
    SGDiS000002200. SIR2.

    Subcellular locationi

    Nucleusnucleolus 1 Publication
    Note: Associated with nucleolar chromatin. Preferentially bound to the spacer regions of the rDNA repeats through its interaction with NET1.

    GO - Cellular componenti

    1. chromatin silencing complex Source: SGD
    2. nuclear chromosome, telomeric region Source: SGD
    3. nuclear heterochromatin Source: SGD
    4. nuclear telomeric heterochromatin Source: SGD
    5. nucleolus Source: SGD
    6. RENT complex Source: SGD

    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. Interacts with ESC8 and ZDS2. Component of the RENT complex, at least composed of SIR2, CDC14 and NET1. The RENT complex interacts with FOB1. Forms a complex with SIR3 and SIR4. Interacts with MCM10 and SLX5.9 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi32017. 294 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 – 1054
    Beta strandi111 – 1133
    Beta strandi124 – 1263
    Helixi132 – 15423
    Helixi163 – 1708
    Beta strandi173 – 1753
    Helixi178 – 18710
    Beta strandi213 – 2175
    Helixi244 – 25310
    Beta strandi255 – 2617
    Helixi263 – 2697
    Beta strandi274 – 2763
    Helixi280 – 2834
    Helixi284 – 2874
    Helixi292 – 2965
    Helixi298 – 3036
    Helixi306 – 3116
    Helixi312 – 3154
    Helixi324 – 33411
    Beta strandi338 – 3436
    Helixi349 – 3524
    Turni357 – 3593
    Beta strandi360 – 3623
    Beta strandi365 – 3728
    Turni373 – 3753
    Beta strandi378 – 3803
    Helixi381 – 3844
    Helixi385 – 3895
    Turni397 – 3993
    Helixi400 – 4067
    Turni433 – 4364
    Beta strandi437 – 4426
    Helixi451 – 46010
    Turni461 – 4633
    Beta strandi466 – 4716
    Helixi479 – 4813
    Helixi482 – 4854
    Beta strandi492 – 4987
    Beta strandi506 – 5116
    Helixi513 – 52412
    Helixi533 – 5375
    Beta strandi541 – 5477
    Beta strandi550 – 5556

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MTIPHMKYAV SKTSENKVSN TVSPTQDKDA IRKQPDDIIN NDEPSHKKIK    50
    VAQPDSLRET NTTDPLGHTK AALGEVASME LKPTNDMDPL AVSAASVVSM 100
    SNDVLKPETP KGPIIISKNP SNGIFYGPSF TKRESLNARM FLKYYGAHKF 150
    LDTYLPEDLN SLYIYYLIKL LGFEVKDQAL IGTINSIVHI NSQERVQDLG 200
    SAISVTNVED PLAKKQTVRL IKDLQRAINK VLCTRLRLSN FFTIDHFIQK 250
    LHTARKILVL TGAGVSTSLG IPDFRSSEGF YSKIKHLGLD DPQDVFNYNI 300
    FMHDPSVFYN IANMVLPPEK IYSPLHSFIK MLQMKGKLLR NYTQNIDNLE 350
    SYAGISTDKL VQCHGSFATA TCVTCHWNLP GERIFNKIRN LELPLCPYCY 400
    KKRREYFPEG YNNKVGVAAS QGSMSERPPY ILNSYGVLKP DITFFGEALP 450
    NKFHKSIRED ILECDLLICI GTSLKVAPVS EIVNMVPSHV PQVLINRDPV 500
    KHAEFDLSLL GYCDDIAAMV AQKCGWTIPH KKWNDLKNKN FKCQEKDKGV 550
    YVVTSDEHPK TL 562
    Length:562
    Mass (Da):63,262
    Last modified:January 1, 1988 - v1
    Checksum:i52E6937533654586
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi S05891. RGBYS2.
    RefSeqi NP_010242.1. NM_001180101.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HJH X-ray 1.85 A/B 209-562 [» ]
    4IAO X-ray 2.90 A/B 87-562 [» ]
    ProteinModelPortali P06700.
    SMRi P06700. Positions 99-555.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32017. 294 interactions.
    DIPi DIP-596N.
    IntActi P06700. 48 interactions.
    MINTi MINT-509141.
    STRINGi 4932.YDL042C.

    Chemistry

    BindingDBi P06700.
    ChEMBLi CHEMBL3275.

    Proteomic databases

    MaxQBi P06700.
    PaxDbi P06700.
    PeptideAtlasi P06700.
    PRIDEi P06700.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL042C ; YDL042C ; YDL042C .
    GeneIDi 851520.
    KEGGi sce:YDL042C.

    Organism-specific databases

    CYGDi YDL042c.
    SGDi S000002200. SIR2.

    Phylogenomic databases

    eggNOGi COG0846.
    GeneTreei ENSGT00740000115330.
    HOGENOMi HOG000191845.
    KOi K11121.
    OMAi PVKHAEF.
    OrthoDBi EOG7MWH64.

    Enzyme and pathway databases

    BioCyci YEAST:MONOMER3O-4152.
    SABIO-RK P06700.

    Miscellaneous databases

    EvolutionaryTracei P06700.
    NextBioi 968896.

    Gene expression databases

    Genevestigatori P06700.

    Family and domain databases

    Gene3Di 3.30.1600.10. 3 hits.
    3.40.50.1220. 3 hits.
    InterProi IPR029035. 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 ]
    PANTHERi PTHR11085. PTHR11085. 1 hit.
    Pfami PF04574. DUF592. 1 hit.
    PF02146. SIR2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52467. SSF52467. 2 hits.
    PROSITEi PS50305. SIRTUIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.

    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: October 1, 2014
    This is version 161 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