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P06700

- SIR2_YEAST

UniProt

P06700 - SIR2_YEAST

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Protein
NAD-dependent histone deacetylase SIR2
Gene
SIR2, MAR1, YDL042C, D2714
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.7 Publications

Catalytic activityi

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

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 peptide
  3. KM=420 µM for a synthetic histone H3K14 acetyllysine peptide
  4. KM=140 µM for a synthetic histone H4K5 acetyllysine peptide
  5. KM=54 µM for a synthetic histone H4K8 acetyllysine peptide
  6. KM=105 µM for a synthetic histone H4K12 acetyllysine peptide
  7. KM=17 µM for a synthetic histone H4K16 acetyllysine peptide

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei364 – 3641Proton acceptor By similarity
Metal bindingi372 – 3721Zinc
Metal bindingi375 – 3751Zinc
Metal bindingi396 – 3961Zinc
Metal bindingi399 – 3991Zinc
Binding sitei513 – 5131NAD; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi262 – 28120NAD
Add
BLAST
Nucleotide bindingi344 – 3474NAD By similarity
Nucleotide bindingi471 – 4733NAD By similarity
Nucleotide bindingi496 – 4983NAD By 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
Complete GO annotation...

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. chromatin assembly or disassembly Source: SGD
  3. chromatin silencing at rDNA Source: SGD
  4. chromatin silencing at silent mating-type cassette Source: SGD
  5. chromatin silencing at telomere Source: SGD
  6. chronological cell aging Source: SGD
  7. histone H3 deacetylation Source: GOC
  8. histone H4 deacetylation Source: GOC
  9. histone 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.
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
Note: Associated with nucleolar chromatin. Preferentially bound to the spacer regions of the rDNA repeats through its interaction with NET1.1 Publication

GO - Cellular componenti

  1. RENT complex Source: SGD
  2. chromatin silencing complex Source: SGD
  3. nuclear chromosome, telomeric region Source: SGD
  4. nuclear heterochromatin Source: SGD
  5. nuclear telomeric heterochromatin Source: SGD
  6. nucleolus 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 SIR2
PRO_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 SLX5.8 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi32017. 291 interactions.
DIPiDIP-596N.
IntActiP06700. 48 interactions.
MINTiMINT-509141.
STRINGi4932.YDL042C.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP06700.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini245 – 529285Deacetylase sirtuin-type
Add
BLAST

Sequence similaritiesi

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

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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...

Protein-protein interaction databases

BioGridi 32017. 291 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

« 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: June 11, 2014
This is version 160 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.

Caution

Was originally (1 Publication) thought to be an ADP-ribosyltransferase.

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

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