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Protein

NAD-dependent histone deacetylase Sir2

Gene

Sir2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

NAD-dependent histone deacetylase involved in heterochromatic silencing. Mildly suppresses the heterochromatin-mediated silencing phenomenon known as position-effect variegation (PEV). Required for epigenetic silencing of the polycomb group proteins. Has histone H4 deacetylase activity in vitro. Required maternally for establishing proper segmentation of the embryo. Involved in sex determination. May be involved in the regulation of life span.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

pH dependencei

Optimum pH is 9.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi339ZincPROSITE-ProRule annotation1
Metal bindingi342ZincPROSITE-ProRule annotation1
Metal bindingi363ZincPROSITE-ProRule annotation1
Metal bindingi366ZincPROSITE-ProRule annotation1
Binding sitei469NAD; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi229 – 248NADBy similarityAdd BLAST20
Nucleotide bindingi313 – 316NADBy similarity4
Nucleotide bindingi427 – 429NADBy similarity3
Nucleotide bindingi452 – 454NADBy similarity3

GO - Molecular functioni

  • histone deacetylase activity Source: FlyBase
  • metal ion binding Source: UniProtKB-KW
  • NAD+ binding Source: InterPro
  • NAD-dependent histone deacetylase activity Source: FlyBase
  • transcription factor binding Source: FlyBase

GO - Biological processi

  • behavioral response to ethanol Source: FlyBase
  • chromatin silencing Source: FlyBase
  • determination of adult lifespan Source: FlyBase
  • histone deacetylation Source: FlyBase
  • positive regulation of feeding behavior Source: FlyBase
  • regulation of apoptotic process Source: FlyBase
  • regulation of histone acetylation Source: FlyBase
  • regulation of transcription, DNA-templated Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

ReactomeiR-DME-3371453. Regulation of HSF1-mediated heat shock response.
R-DME-427359. SIRT1 negatively regulates rRNA Expression.

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
ORF Names:CG5216
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0024291. Sir2.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 2 Publications
  • Chromosome 1 Publication

GO - Cellular componenti

  • chromosome Source: UniProtKB-SubCell
  • cytoplasm Source: FlyBase
  • nucleoplasm Source: FlyBase
  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Causes lethality during development. Induced silencing shortens life span.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004174051 – 823NAD-dependent histone deacetylase Sir2Add BLAST823

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei618Phosphoserine1 Publication1
Modified residuei621Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VK34.
PRIDEiQ9VK34.

PTM databases

iPTMnetiQ9VK34.

Expressioni

Gene expression databases

BgeeiFBgn0024291.
GenevisibleiQ9VK34. DM.

Interactioni

Subunit structurei

Interacts with the transcriptional repressors hairy (h) and deadpan (dpn); via basic domains. Associates with the Esc/E(z) histone methyltransferase complex. Interacts directly with E(z) and Rpd3.2 Publications

GO - Molecular functioni

  • transcription factor binding Source: FlyBase

Protein-protein interaction databases

BioGridi60746. 13 interactors.
IntActiQ9VK34. 5 interactors.
MINTiMINT-318641.
STRINGi7227.FBpp0080015.

Structurei

3D structure databases

ProteinModelPortaliQ9VK34.
SMRiQ9VK34.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini212 – 485Deacetylase sirtuin-typePROSITE-ProRule annotationAdd BLAST274

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi47 – 135Glu-richAdd BLAST89
Compositional biasi508 – 522His-richAdd BLAST15

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2684. Eukaryota.
COG0846. LUCA.
GeneTreeiENSGT00850000132399.
InParanoidiQ9VK34.
KOiK11411.
OMAiQRVIECH.
OrthoDBiEOG091G07CT.
PhylomeDBiQ9VK34.

Family and domain databases

Gene3Di3.30.1600.10. 2 hits.
3.40.50.1220. 3 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026591. Sirtuin_cat_small_dom.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERiPTHR11085. PTHR11085. 3 hits.
PfamiPF02146. SIR2. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS50305. SIRTUIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VK34-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMENYEEIRL GHIRSKDLGN QVPDTTQFYP PTKFDFGAEI LASTSTEAEA
60 70 80 90 100
EAEATATTTE PATSELAGKA NGEIKTKTLA AREEQEIGAN LEHKTKNPTK
110 120 130 140 150
SMGEDEDDEE EEEEDDEEEE EDDEEGITGT SNEDEDSSSN CSSSVEPDWK
160 170 180 190 200
LRWLQREFYT GRVPRQVIAS IMPHFATGLA GDTDDSVLWD YLAHLLNEPK
210 220 230 240 250
RRNKLASVNT FDDVISLVKK SQKIIVLTGA GVSVSCGIPD FRSTNGIYAR
260 270 280 290 300
LAHDFPDLPD PQAMFDINYF KRDPRPFYKF AREIYPGEFQ PSPCHRFIKM
310 320 330 340 350
LETKGKLLRN YTQNIDTLER VAGIQRVIEC HGSFSTASCT KCRFKCNADA
360 370 380 390 400
LRADIFAQRI PVCPQCQPNK EQSVDASVAV TEEELRQLVE NGIMKPDIVF
410 420 430 440 450
FGEGLPDEYH TVMATDKDVC DLLIVIGSSL KVRPVAHIPS SIPATVPQIL
460 470 480 490 500
INREQLHHLK FDVELLGDSD VIINQICHRL SDNDDCWRQL CCDESVLTES
510 520 530 540 550
KELMPPEHSN HHLHHHLLHH RHCSSESERQ SQLDTDTQSI KSNSSADYIL
560 570 580 590 600
GSAGTCSDSG FESSTFSCGK RSTAAEAAAI ERIKTDILVE LNETTALSCD
610 620 630 640 650
RLGLEGPQTT VESYRHLSID SSKDSGIEQC DNEATPSYVR PSNLVQETKT
660 670 680 690 700
VAPSLTPIPQ QRGKRQTAAE RLQPGTFYSH TNNYSYVFPG AQVFWDNDYS
710 720 730 740 750
DDDDEEEERS HNRHSDLFGN VGHNYKDDDE DACDLNAVPL SPLLPPSLEA
760 770 780 790 800
HIVTDIVNGS NEPLPNSSPG QKRTACIIEQ QPTPAIETEI PPLKKRRPSE
810 820
ENKQQTQIER SEESPPPGQL AAV
Length:823
Mass (Da):91,837
Last modified:May 1, 2000 - v1
Checksum:i3DD1EBA975A263D3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53 – 54Missing in AAC79684 (PubMed:12663533).Curated2
Sequence conflicti104E → K in ADG03442 (Ref. 4) Curated1
Sequence conflicti290Q → QFQ in AAC79684 (PubMed:12663533).Curated1
Sequence conflicti518L → H in AAC79684 (PubMed:12663533).Curated1
Sequence conflicti746P → H in AAC79684 (PubMed:12663533).Curated1
Sequence conflicti753V → F in AAC79684 (PubMed:12663533).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068758 mRNA. Translation: AAC79684.1.
AE014134 Genomic DNA. Translation: AAF53248.1.
BT124857 mRNA. Translation: ADG03442.1.
BT133215 mRNA. Translation: AFA28456.1.
BT133274 mRNA. Translation: AFC38905.1.
RefSeqiNP_477351.1. NM_058003.4.
UniGeneiDm.415.

Genome annotation databases

EnsemblMetazoaiFBtr0080434; FBpp0080015; FBgn0024291.
GeneIDi34708.
KEGGidme:Dmel_CG5216.
UCSCiCG5216-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068758 mRNA. Translation: AAC79684.1.
AE014134 Genomic DNA. Translation: AAF53248.1.
BT124857 mRNA. Translation: ADG03442.1.
BT133215 mRNA. Translation: AFA28456.1.
BT133274 mRNA. Translation: AFC38905.1.
RefSeqiNP_477351.1. NM_058003.4.
UniGeneiDm.415.

3D structure databases

ProteinModelPortaliQ9VK34.
SMRiQ9VK34.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60746. 13 interactors.
IntActiQ9VK34. 5 interactors.
MINTiMINT-318641.
STRINGi7227.FBpp0080015.

PTM databases

iPTMnetiQ9VK34.

Proteomic databases

PaxDbiQ9VK34.
PRIDEiQ9VK34.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080434; FBpp0080015; FBgn0024291.
GeneIDi34708.
KEGGidme:Dmel_CG5216.
UCSCiCG5216-RA. d. melanogaster.

Organism-specific databases

CTDi23411.
FlyBaseiFBgn0024291. Sir2.

Phylogenomic databases

eggNOGiKOG2684. Eukaryota.
COG0846. LUCA.
GeneTreeiENSGT00850000132399.
InParanoidiQ9VK34.
KOiK11411.
OMAiQRVIECH.
OrthoDBiEOG091G07CT.
PhylomeDBiQ9VK34.

Enzyme and pathway databases

ReactomeiR-DME-3371453. Regulation of HSF1-mediated heat shock response.
R-DME-427359. SIRT1 negatively regulates rRNA Expression.

Miscellaneous databases

ChiTaRSiSir2. fly.
GenomeRNAii34708.
PROiQ9VK34.

Gene expression databases

BgeeiFBgn0024291.
GenevisibleiQ9VK34. DM.

Family and domain databases

Gene3Di3.30.1600.10. 2 hits.
3.40.50.1220. 3 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026591. Sirtuin_cat_small_dom.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERiPTHR11085. PTHR11085. 3 hits.
PfamiPF02146. SIR2. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS50305. SIRTUIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSIR2_DROME
AccessioniPrimary (citable) accession number: Q9VK34
Secondary accession number(s): D5SHQ6, O96505
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.