[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND MUTAGENESIS OF HIS-187.
TISSUE=Testis;
DOI=10.1006/bbrc.1999.0897; PubMed=10381378 [NCBI, ExPASy, EBI, Israel, Japan]
Frye R.A.;
"Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity.";
Biochem. Biophys. Res. Commun. 260:273-279(1999).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1016/S0378-1119(99)00162-6; PubMed=10393250 [NCBI, ExPASy, EBI, Israel, Japan]
Afshar G.,
Murnane J.P.;
"Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2.";
Gene 234:161-168(1999).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
DOI=10.1046/j.1471-4159.2002.00847.x; PubMed=12065666 [NCBI, ExPASy, EBI, Israel, Japan]
De Smet C.,
Nishimori H.,
Furnari F.B.,
Boegler O.,
Huang H.-J.S.,
Cavenee W.K.;
"A novel seven transmembrane receptor induced during the early steps of astrocyte differentiation identified by differential expression.";
J. Neurochem. 81:575-588(2002).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Lennerz V.,
Fatho M.,
Gentilini C.,
Lifke A.,
Woelfel C.,
Woelfel T.;
"Response of autologous T cells to a human melanoma is dominated by individual mutant antigens.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Adrenal gland;
DOI=10.1073/pnas.160270997; PubMed=10931946 [NCBI, ExPASy, EBI, Israel, Japan]
Hu R.-M.,
Han Z.-G.,
Song H.-D.,
Peng Y.-D.,
Huang Q.-H.,
Ren S.-X.,
Gu Y.-J.,
Huang C.-H.,
Li Y.-B.,
Jiang C.-L.,
Fu G.,
Zhang Q.-H.,
Gu B.-W.,
Dai M.,
Mao Y.-F.,
Gao G.-F.,
Rong R.,
Ye M.,
Zhou J., ![]()
Xu S.-H.,
Gu J.,
Shi J.-X.,
Jin W.-R.,
Zhang C.-K.,
Wu T.-M.,
Huang G.-Y.,
Chen Z.,
Chen M.-D.,
Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
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[6]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[7]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-389 (ISOFORM 4).
TISSUE=Brain;
Mei G.,
Yu W.,
Gibbs R.A.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
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[8]
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INHIBITION BY SIRTINOL; A3 AND M15.
DOI=10.1074/jbc.M106779200; PubMed=11483616 [NCBI, ExPASy, EBI, Israel, Japan]
Grozinger C.M.,
Chao E.D.,
Blackwell H.E.,
Moazed D.,
Schreiber S.L.;
"Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening.";
J. Biol. Chem. 276:38837-38843(2001).
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[9]
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CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-187.
DOI=10.1074/jbc.M111830200; PubMed=11812793 [NCBI, ExPASy, EBI, Israel, Japan]
Borra M.T.,
O'Neill F.J.,
Jackson M.D.,
Marshall B.L.,
Verdin E.,
Foltz K.R.,
Denu J.M.;
"Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases.";
J. Biol. Chem. 277:12632-12641(2002).
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[10]
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FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HDAC6, AND MUTAGENESIS OF ASN-168 AND HIS-187.
DOI=10.1016/S1097-2765(03)00038-8; PubMed=12620231 [NCBI, ExPASy, EBI, Israel, Japan]
North B.J.,
Marshall B.L.,
Borra M.T.,
Denu J.M.,
Verdin E.;
"The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase.";
Mol. Cell 11:437-444(2003).
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[11]
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FUNCTION, DEVELOPMENTAL STAGE, PHOSPHORYLATION, AND MUTAGENESIS OF HIS-187.
DOI=10.1128/MCB.23.9.3173-3185.2003; PubMed=12697818 [NCBI, ExPASy, EBI, Israel, Japan]
Dryden S.C.,
Nahhas F.A.,
Nowak J.E.,
Goustin A.-S.,
Tainsky M.A.;
"Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle.";
Mol. Cell. Biol. 23:3173-3185(2003).
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[12]
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TISSUE SPECIFICITY.
DOI=10.1016/j.bbrc.2003.08.029; PubMed=12963026 [NCBI, ExPASy, EBI, Israel, Japan]
Hiratsuka M.,
Inoue T.,
Toda T.,
Kimura N.,
Shirayoshi Y.,
Kamitani H.,
Watanabe T.,
Ohama E.,
Tahimic C.G.T.,
Kurimasa A.,
Oshimura M.;
"Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene.";
Biochem. Biophys. Res. Commun. 309:558-566(2003).
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[13]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P.,
Lewandrowski U.,
Wiesner J.,
Wortelkamp S.,
Moebius J.,
Schuetz C.,
Walter U.,
Gambaryan S.,
Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
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[14]
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X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 34-356 IN COMPLEX WITH ZINC, AND MUTAGENESIS OF ARG-97; GLN-167; ASN-168; ASP-170 AND HIS-187.
DOI=10.1038/89668; PubMed=11427894 [NCBI, ExPASy, EBI, Israel, Japan]
Finnin M.S.,
Donigian J.R.,
Pavletich N.P.;
"Structure of the histone deacetylase SIRT2.";
Nat. Struct. Biol. 8:621-625(2001).
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- 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. Despite some ability to deacetylate histones in vitro, it is unlikely in vivo.
- CATALYTIC ACTIVITY: NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.
- COFACTOR: Binds 1 zinc ion per subunit.
- ENZYME REGULATION: Inhibited by Sirtinol, A3 and M15 small molecules. Inhibited by nicotinamide.
- SUBUNIT: Interacts with HDAC6, suggesting that these proteins belong to a large complex that deacetylate the cytoskeleton.
- INTERACTION:
Q9Y569:-; NbExp=1; IntAct=EBI-477232, EBI-1052090;
Q92830-1:GCN5L2; NbExp=1; IntAct=EBI-477232, EBI-477636;
Q92830-2:GCN5L2; NbExp=1; IntAct=EBI-477232, EBI-477641;
P13807:GYS1; NbExp=1; IntAct=EBI-477232, EBI-963094;
Q9UBN7:HDAC6; NbExp=1; IntAct=EBI-477232, EBI-301697;
Q8N1N4:KRT78; NbExp=1; IntAct=EBI-477232, EBI-1056564;
Q92831:PCAF; NbExp=2; IntAct=EBI-477232, EBI-477430;
Q99623:PHB2; NbExp=1; IntAct=EBI-477232, EBI-358348;
Q9NQC3:RTN4; NbExp=1; IntAct=EBI-477232, EBI-715945;
P49591:SARS; NbExp=1; IntAct=EBI-477232, EBI-1053431;
O43791:SPOP; NbExp=1; IntAct=EBI-477232, EBI-743549;
- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Colocalizes with microtubules.
- ALTERNATIVE PRODUCTS:
4 named isoforms [FASTA] produced by alternative splicing.
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| Name | 2 |
| Isoform ID | Q8IXJ6-2 |
| Features which should be applied to build the isoform sequence: VSP_008724. |
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| Name | 3 |
| Isoform ID | Q8IXJ6-3 |
| Note: No experimental confirmation available. |
| Features which should be applied to build the isoform sequence: VSP_008726. |
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| Name | 4 |
| Isoform ID | Q8IXJ6-4 |
| Note: No experimental confirmation available. |
| Features which should be applied to build the isoform sequence: VSP_008727, VSP_008728. |
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- TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart, brain and skeletal muscle, while it is weakly expressed in placenta and lung. Down-regulated in many gliomas suggesting that it may act as a tumor suppressor gene in human gliomas possibly through the regulation of microtubule network.
- DEVELOPMENTAL STAGE: Peaks during mitosis. After mitosis, it is probably degraded by the 26S proteasome.
- PTM: Phosphorylated at the G2/M transition of the cell cycle.
- SIMILARITY: Belongs to the sirtuin family.
- SIMILARITY: Contains 1 deacetylase sirtuin-type domain.
- SEQUENCE CAUTION:
- Sequence=AAF67015.1; Type=Frameshift; Positions=Several;
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