Q8VDQ8 (SIRT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	389 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. 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 process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding NAD Zinc
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell 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 component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB microtubule Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	NAD-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 389	388	NAD-dependent deacetylase sirtuin-2		PRO_0000110259
Regions
	Domain	65 – 340	276	Deacetylase sirtuin-type
	Nucleotide binding	84 – 104	21	NAD By similarity
	Nucleotide binding	167 – 171	5	NAD By similarity
Sites
	Active site	187	1	Proton acceptor By similarity
	Metal binding	195	1	Zinc By similarity
	Metal binding	200	1	Zinc By similarity
	Metal binding	221	1	Zinc By similarity
	Metal binding	224	1	Zinc By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	23	1	Phosphoserine Ref.5
	Modified residue	25	1	Phosphoserine By similarity
	Modified residue	368	1	Phosphoserine By similarity
	Modified residue	372	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 37	37	Missing in isoform 2.		VSP_008729
Experimental info
	Sequence conflict	230	1	P → L in AAG32038. Ref.1
	Sequence conflict	241	1	S → P in AAH21439. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 31, 2003. Version 2. Checksum: 15F96635445A1BC0	FASTA	389	43,256
	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
	Isoform 2 [UniParc]. Checksum: C67B7687704CB014	FASTA	352	39,554
	10 20 30 40 50 60 MDFLRNLFTQ TLGLGSQKER LLDELTLEGV TRYMQSERCR KVICLVGAGI STSAGIPDFR 70 80 90 100 110 120 SPSTGLYANL EKYHLPYPEA IFEISYFKKH PEPFFALAKE LYPGQFKPTI CHYFIRLLKE 130 140 150 160 170 180 KGLLLRCYTQ NIDTLERVAG LEPQDLVEAH GTFYTSHCVN TSCRKEYTMG WMKEKIFSEA 190 200 210 220 230 240 TPRCEQCQSV VKPDIVFFGE NLPSRFFSCM QSDFSKVDLL IIMGTSLQVQ PFASLISKAP 250 260 270 280 290 300 LATPRLLINK EKTGQTDPFL GMMMGLGGGM DFDSKKAYRD VAWLGDCDQG CLALADLLGW 310 320 330 340 350 KKELEDLVRR EHANIDAQSG SQAPNPSTTI SPGKSPPPAK EAARTKEKEE QQ

References

	« Hide 'large scale' referencesShow '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. , 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 , AF302265, AF302266, AF302267, AF302268, AF302269, AF302270, AF302271 Genomic DNA. Translation: AAG32038.1. AK014042 mRNA. Translation: BAB29128.1. BC021439 mRNA. Translation: AAH21439.1.
IPI	IPI00110265. IPI00473688.
RefSeq	NP_001116237.1. NM_001122765.1. NP_001116238.1. NM_001122766.1. NP_071877.3. NM_022432.4.
UniGene	Mm.272443.
3D structure databases
ProteinModelPortal	Q8VDQ8.
SMR	Q8VDQ8. Positions 54-356.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8VDQ8. 2 interactions.
STRING	Q8VDQ8.
PTM databases
PhosphoSite	Q8VDQ8.
Proteomic databases
PRIDE	Q8VDQ8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000072965; ENSMUSP00000072732; ENSMUSG00000015149.
GeneID	64383.
KEGG	mmu:64383.
NMPDR	fig|10090.3.peg.16053.
UCSC	uc009fzt.2. mouse. uc009fzu.2. mouse.
Organism-specific databases
CTD	22933.
MGI	MGI:1927664. Sirt2.
Phylogenomic databases
GeneTree	ENSGT00550000074608.
HOGENOM	HBG641281.
HOVERGEN	HBG057095.
InParanoid	Q8VDQ8.
OMA	SWMKEKI.
OrthoDB	EOG4BVRTZ.
PhylomeDB	Q8VDQ8.
Gene expression databases
ArrayExpress	Q8VDQ8.
Bgee	Q8VDQ8.
Genevestigator	Q8VDQ8.
GermOnline	ENSMUSG00000015149. Mus musculus.
Family and domain databases
InterPro	IPR017328. NAD-dep_deAcase_SIR2_euk. IPR003000. NAD-dep_deAcase_sirtuin. [Graphical view]
KO	K11412.
PANTHER	PTHR11085. SIR2. 1 hit.
Pfam	PF02146. SIR2. 1 hit. [Graphical view]
PIRSF	PIRSF037938. SIR2_euk. 1 hit.
PROSITE	PS50305. SIRTUIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	320059.
SOURCE	Search...

Entry information

Entry name

SIRT2_MOUSE

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program