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Identification
HMDB Protein ID HMDBP08880
Secondary Accession Numbers
  • 14607
Name NAD-dependent protein deacetylase sirtuin-2
Synonyms
  1. SIR2-like protein 2
  2. Regulatory protein SIR2 homolog 2
Gene Name SIRT2
Protein Type Unknown
Biological Properties
General Function Involved in zinc ion binding
Specific Function NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins. 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.
Pathways Not Available
Reactions
NAD + an acetylprotein → Niacinamide + O-acetyl-ADP-ribose + a protein details
GO Classification
Biological Process
negative regulation of striated muscle tissue development
regulation of exit from mitosis
cell division
response to redox state
protein ADP-ribosylation
chromatin silencing at telomere
regulation of phosphorylation
proteasomal ubiquitin-dependent protein catabolic process
mitosis
chromatin silencing at rDNA
Cellular Component
cytoplasm
chromatin silencing complex
microtubule
Function
ion binding
cation binding
metal ion binding
binding
nucleotide binding
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
transition metal ion binding
zinc ion binding
nad or nadh binding
nad binding
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Molecular Function
NAD-dependent histone deacetylase activity
tubulin deacetylase activity
ubiquitin binding
metal ion binding
zinc ion binding
NAD+ binding
Process
metabolic process
macromolecule metabolic process
protein amino acid deacetylation
gene silencing
chromatin silencing
cellular process
biological regulation
regulation of biological process
regulation of metabolic process
regulation of macromolecule metabolic process
regulation of gene expression
regulation of transcription
post-translational protein modification
macromolecule modification
protein modification process
Cellular Location
  1. Cytoplasm
  2. cytoskeleton
Gene Properties
Chromosome Location 19
Locus 19q13
SNPs SIRT2
Gene Sequence
>1170 bp
ATGGCAGAGCCAGACCCCTCTCACCCTCTGGAGACCCAGGCAGGGAAGGTGCAGGAGGCT
CAGGACTCAGATTCAGACTCTGAGGGAGGAGCCGCTGGTGGAGAAGCAGACATGGACTTC
CTGCGGAACTTATTCTCCCAGACGCTCAGCCTGGGCAGCCAGAAGGAGCGTCTGCTGGAC
GAGCTGACCTTGGAAGGGGTGGCCCGGTACATGCAGAGCGAACGCTGTCGCAGAGTCATC
TGTTTGGTGGGAGCTGGAATCTCCACATCCGCAGGCATCCCCGACTTTCGCTCTCCATCC
ACCGGCCTCTATGACAACCTAGAGAAGTACCATCTTCCCTACCCAGAGGCCATCTTTGAG
ATCAGCTATTTCAAGAAACATCCGGAACCCTTCTTCGCCCTCGCCAAGGAACTCTATCCT
GGGCAGTTCAAGCCAACCATCTGTCACTACTTCATGCGCCTGCTGAAGGACAAGGGGCTA
CTCCTGCGCTGCTACACGCAGAACATAGATACCCTGGAGCGAATAGCCGGGCTGGAACAG
GAGGACTTGGTGGAGGCGCACGGCACCTTCTACACATCACACTGCGTCAGCGCCAGCTGC
CGGCACGAATACCCGCTAAGCTGGATGAAAGAGAAGATCTTCTCTGAGGTGACGCCCAAG
TGTGAAGACTGTCAGAGCCTGGTGAAGCCTGATATCGTCTTTTTTGGTGAGAGCCTCCCA
GCGCGTTTCTTCTCCTGTATGCAGTCAGACTTCCTGAAGGTGGACCTCCTCCTGGTCATG
GGTACCTCCTTGCAGGTGCAGCCCTTTGCCTCCCTCATCAGCAAGGCACCCCTCTCCACC
CCTCGCCTGCTCATCAACAAGGAGAAAGCTGGCCAGTCGGACCCTTTCCTGGGGATGATT
ATGGGCCTCGGAGGAGGCATGGACTTTGACTCCAAGAAGGCCTACAGGGACGTGGCCTGG
CTGGGTGAATGCGACCAGGGCTGCCTGGCCCTTGCTGAGCTCCTTGGATGGAAGAAGGAG
CTGGAGGACCTTGTCCGGAGGGAGCACGCCAGCATAGATGCCCAGTCGGGGGCGGGGGTC
CCCAACCCCAGCACTTCAGCTTCCCCCAAGAAGTCCCCGCCACCTGCCAAGGACGAGGCC
AGGACAACAGAGAGGGAGAAACCCCAGTGA
Protein Properties
Number of Residues 389
Molecular Weight 26711.565
Theoretical pI 6.524
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>NAD-dependent deacetylase sirtuin-2
MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLD
ELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFE
ISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQ
EDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLP
ARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMI
MGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWKKELEDLVRREHASIDAQSGAGV
PNPSTSASPKKSPPPAKDEARTTEREKPQ
GenBank ID Protein 13400020
UniProtKB/Swiss-Prot ID Q8IXJ6
UniProtKB/Swiss-Prot Entry Name SIRT2_HUMAN
PDB IDs
GenBank Gene ID AF083107
GeneCard ID SIRT2
GenAtlas ID SIRT2
HGNC ID HGNC:10886
References
General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed:10931946 ]
  4. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  5. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed:18088087 ]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  7. Michishita E, Park JY, Burneskis JM, Barrett JC, Horikawa I: Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol Biol Cell. 2005 Oct;16(10):4623-35. Epub 2005 Aug 3. [PubMed:16079181 ]
  8. Frye RA: 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. 1999 Jun 24;260(1):273-9. [PubMed:10381378 ]
  9. Afshar G, Murnane JP: Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2. Gene. 1999 Jun 24;234(1):161-8. [PubMed:10393250 ]
  10. De Smet C, Nishimori H, Furnari FB, Bogler O, Huang HJ, Cavenee WK: A novel seven transmembrane receptor induced during the early steps of astrocyte differentiation identified by differential expression. J Neurochem. 2002 May;81(3):575-88. [PubMed:12065666 ]
  11. Grozinger CM, Chao ED, Blackwell HE, Moazed D, Schreiber SL: Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening. J Biol Chem. 2001 Oct 19;276(42):38837-43. Epub 2001 Aug 1. [PubMed:11483616 ]
  12. Borra MT, O'Neill FJ, Jackson MD, Marshall B, Verdin E, Foltz KR, Denu JM: Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases. J Biol Chem. 2002 Apr 12;277(15):12632-41. Epub 2002 Jan 25. [PubMed:11812793 ]
  13. North BJ, Marshall BL, Borra MT, Denu JM, Verdin E: The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell. 2003 Feb;11(2):437-44. [PubMed:12620231 ]
  14. Dryden SC, Nahhas FA, Nowak JE, Goustin AS, Tainsky MA: Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol Cell Biol. 2003 May;23(9):3173-85. [PubMed:12697818 ]
  15. Hiratsuka M, Inoue T, Toda T, Kimura N, Shirayoshi Y, Kamitani H, Watanabe T, Ohama E, Tahimic CG, Kurimasa A, Oshimura M: Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene. Biochem Biophys Res Commun. 2003 Sep 26;309(3):558-66. [PubMed:12963026 ]
  16. Finnin MS, Donigian JR, Pavletich NP: Structure of the histone deacetylase SIRT2. Nat Struct Biol. 2001 Jul;8(7):621-5. [PubMed:11427894 ]