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P06700

- SIR2_YEAST

UniProt

P06700 - SIR2_YEAST

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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: 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 – 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. 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
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_205607. 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: 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
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. 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. 297 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 .
PIRi S05891. RGBYS2.
RefSeqi NP_010242.1. NM_001180101.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 297 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.
InParanoidi P06700.
KOi K11121.
OMAi PVKHAEF.
OrthoDBi EOG7MWH64.

Enzyme and pathway databases

BioCyci YEAST:MONOMER3O-4152.
Reactomei REACT_205607. Regulation of HSF1-mediated heat shock response.
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

« 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. "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: November 26, 2014
This is version 163 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