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Q8VDQ8 (SIRT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 100. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NAD-dependent deacetylase sirtuin-2

EC=3.5.1.-
Alternative name(s):
SIR2-like protein 2
Short name=mSIR2L2
Gene names
Name:Sirt2
Synonyms:Sir2l2
OrganismMus musculus (Mouse)
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 deacetylase, which deacetylates the '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 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. Ref.5

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.

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 processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

mitosis

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-dependent

Inferred from sequence or structural similarity. Source: UniProtKB

proteasomal ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionNAD-dependent histone deacetylase activity

Inferred from sequence or structural similarity. Source: UniProtKB

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

Complete GO annotation...

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:
     1-37: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Domain65 – 340276Deacetylase sirtuin-type
Nucleotide binding84 – 10421NAD By similarity
Nucleotide binding167 – 1715NAD By similarity

Sites

Active site1871Proton acceptor By similarity
Metal binding1951Zinc By similarity
Metal binding2001Zinc By similarity
Metal binding2211Zinc By similarity
Metal binding2241Zinc By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue231Phosphoserine Ref.5
Modified residue251Phosphoserine By similarity
Modified residue3681Phosphoserine By similarity
Modified residue3721Phosphoserine By similarity

Natural variations

Alternative sequence1 – 3737Missing 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: C67B7687704CB014
Show »

FASTA35239,554

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: 11056054] [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: 16141072] [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: 15489334] [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]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, MASS SPECTROMETRY.
Tissue: Melanoma.
+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.
IPIIPI00110265.
IPI00473688.
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...

Protein-protein interaction databases

IntActQ8VDQ8. 2 interactions.
STRINGQ8VDQ8.

PTM databases

PhosphoSiteQ8VDQ8.

Proteomic databases

PRIDEQ8VDQ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072965; ENSMUSP00000072732; ENSMUSG00000015149.
GeneID64383.
KEGGmmu:64383.
NMPDRfig|10090.3.peg.16053.
UCSCuc009fzt.2. mouse.
uc009fzu.2. mouse.

Organism-specific databases

CTD22933.
MGIMGI:1927664. Sirt2.

Phylogenomic databases

GeneTreeENSGT00550000074608.
HOGENOMHBG641281.
HOVERGENHBG057095.
InParanoidQ8VDQ8.
OMASWMKEKI.
OrthoDBEOG4BVRTZ.
PhylomeDBQ8VDQ8.

Gene expression databases

ArrayExpressQ8VDQ8.
BgeeQ8VDQ8.
GenevestigatorQ8VDQ8.
GermOnlineENSMUSG00000015149. Mus musculus.

Family and domain databases

InterProIPR017328. NAD-dep_deAcase_SIR2_euk.
IPR003000. NAD-dep_deAcase_sirtuin.
[Graphical view]
KOK11412.
PANTHERPTHR11085. SIR2. 1 hit.
PfamPF02146. SIR2. 1 hit.
[Graphical view]
PIRSFPIRSF037938. SIR2_euk. 1 hit.
PROSITEPS50305. SIRTUIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio320059.
SOURCESearch...

Entry information

Entry nameSIRT2_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: January 25, 2012
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families