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Q8VDQ8 (SIR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NAD-dependent protein deacetylase sirtuin-2

EC=3.5.1.-
Alternative name(s):
Regulatory protein SIR2 homolog 2
SIR2-like protein 2
Short name=mSIR2L2
Gene names
Name:Sirt2
Synonyms:Sir2l2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length389 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins such as ACLY, PCK1 and RELA. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA By similarity.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by Sirtinol, A3 and M15 small molecules. Inhibited by nicotinamide By similarity.

Subunit structure

Interacts with HDAC6, suggesting that these proteins belong to a large complex that deacetylate the cytoskeleton By similarity.

Subcellular location

Cytoplasmcytoskeleton. Note: Colocalizes with microtubules. Ref.1

Post-translational modification

Phosphorylated at the G2/M transition of the cell cycle By similarity.

Miscellaneous

Has some ability to deacetylate histones in vitro, but seeing its subcellular location, this is unlikely in vivo By similarity.

Sequence similarities

Belongs to the sirtuin family. Class I subfamily.

Contains 1 deacetylase sirtuin-type domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
   LigandMetal-binding
NAD
Zinc
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processmitosis

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of striated muscle tissue development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-lysine deacetylation

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

ripoptosome assembly involved in necroptotic process

Inferred from mutant phenotype PubMed 23201684. Source: MGI

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionNAD+ binding

Inferred from electronic annotation. Source: InterPro

NAD-dependent histone deacetylase activity

Inferred from sequence or structural similarity. Source: UniProtKB

beta-tubulin binding

Inferred from direct assay PubMed 23201684. Source: MGI

histone acetyltransferase binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone deacetylase binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

tubulin deacetylase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AURKAO149655EBI-911012,EBI-448680From a different organism.
Cdc20Q9JJ662EBI-911012,EBI-2551389
Fzr1Q9R1K52EBI-911012,EBI-5238560

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VDQ8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8VDQ8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2-37: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 389388NAD-dependent protein deacetylase sirtuin-2
PRO_0000110259

Regions

Domain65 – 340276Deacetylase sirtuin-type
Nucleotide binding84 – 10421NAD By similarity
Nucleotide binding167 – 1704NAD By similarity
Nucleotide binding261 – 2633NAD By similarity
Nucleotide binding286 – 2883NAD By similarity

Sites

Active site1871Proton acceptor By similarity
Metal binding1951Zinc By similarity
Metal binding2001Zinc By similarity
Metal binding2211Zinc By similarity
Metal binding2241Zinc By similarity
Binding site3241NAD; via amide nitrogen By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Natural variations

Alternative sequence2 – 3736Missing in isoform 2.
VSP_008729

Experimental info

Sequence conflict2301P → L in AAG32038. Ref.1
Sequence conflict2411S → P in AAH21439. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 31, 2003. Version 2.
Checksum: 15F96635445A1BC0

FASTA38943,256
        10         20         30         40         50         60 
MAEPDPSDPL ETQAGKVQEA QDSDSDTEGG ATGGEAEMDF LRNLFTQTLG LGSQKERLLD 

        70         80         90        100        110        120 
ELTLEGVTRY MQSERCRKVI CLVGAGISTS AGIPDFRSPS TGLYANLEKY HLPYPEAIFE 

       130        140        150        160        170        180 
ISYFKKHPEP FFALAKELYP GQFKPTICHY FIRLLKEKGL LLRCYTQNID TLERVAGLEP 

       190        200        210        220        230        240 
QDLVEAHGTF YTSHCVNTSC RKEYTMGWMK EKIFSEATPR CEQCQSVVKP DIVFFGENLP 

       250        260        270        280        290        300 
SRFFSCMQSD FSKVDLLIIM GTSLQVQPFA SLISKAPLAT PRLLINKEKT GQTDPFLGMM 

       310        320        330        340        350        360 
MGLGGGMDFD SKKAYRDVAW LGDCDQGCLA LADLLGWKKE LEDLVRREHA NIDAQSGSQA 

       370        380 
PNPSTTISPG KSPPPAKEAA RTKEKEEQQ 

« Hide

Isoform 2 [UniParc].

Checksum: D88E8C48C56B3E20
Show »

FASTA35339,685

References

« Hide 'large scale' references
[1]"Cloning and characterization of two mouse genes with homology to the yeast sir2 gene."
Yang Y.H., Chen Y.H., Zhang C.Y., Nimmakayalu M.A., Ward D.C., Weissman S.
Genomics 69:355-369(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), SUBCELLULAR LOCATION.
Strain: 129/Ola.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Embryo.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Mammary tumor.
[4]Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 43-55; 58-69; 79-125; 137-153; 164-174; 213-253; 276-282 AND 348-371, MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[5]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF299337 mRNA. Translation: AAG39256.1.
AF302272 expand/collapse EMBL AC list , AF302265, AF302266, AF302267, AF302268, AF302269, AF302270, AF302271 Genomic DNA. Translation: AAG32038.1.
AK014042 mRNA. Translation: BAB29128.1.
BC021439 mRNA. Translation: AAH21439.1.
RefSeqNP_001116237.1. NM_001122765.1.
NP_001116238.1. NM_001122766.1.
NP_071877.3. NM_022432.4.
UniGeneMm.272443.

3D structure databases

ProteinModelPortalQ8VDQ8.
SMRQ8VDQ8. Positions 54-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211070. 19 interactions.
IntActQ8VDQ8. 15 interactions.
MINTMINT-4134698.

PTM databases

PhosphoSiteQ8VDQ8.

Proteomic databases

PaxDbQ8VDQ8.
PRIDEQ8VDQ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072965; ENSMUSP00000072732; ENSMUSG00000015149. [Q8VDQ8-1]
GeneID64383.
KEGGmmu:64383.
UCSCuc009fzt.2. mouse. [Q8VDQ8-1]

Organism-specific databases

CTD22933.
MGIMGI:1927664. Sirt2.

Phylogenomic databases

eggNOGCOG0846.
GeneTreeENSGT00740000115546.
HOGENOMHOG000085952.
HOVERGENHBG057095.
InParanoidQ8VDQ8.
KOK11412.
OMATICHYFM.
OrthoDBEOG7WX09C.
TreeFamTF106181.

Gene expression databases

ArrayExpressQ8VDQ8.
BgeeQ8VDQ8.
GenevestigatorQ8VDQ8.

Family and domain databases

InterProIPR003000. Sirtuin.
IPR017328. Sirtuin_class_I.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERPTHR11085. PTHR11085. 1 hit.
PfamPF02146. SIR2. 1 hit.
[Graphical view]
PIRSFPIRSF037938. SIR2_euk. 1 hit.
PROSITEPS50305. SIRTUIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSIRT2. mouse.
NextBio320059.
PROQ8VDQ8.
SOURCESearch...

Entry information

Entry nameSIR2_MOUSE
AccessionPrimary (citable) accession number: Q8VDQ8
Secondary accession number(s): Q9CXS5, Q9EQ18, Q9ERJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 31, 2003
Last modified: March 19, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot