Details for: SIRT2

Gene ID: 22933

Symbol: SIRT2

Ensembl ID: ENSG00000068903

Description: sirtuin 2

Associated with

Other Information

Genular Protein ID: 3879331415

Symbol: SIR2_HUMAN

Name: NAD-dependent protein deacetylase sirtuin-2

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 10381378

Title: 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.

PubMed ID: 10381378

DOI: 10.1006/bbrc.1999.0897

PubMed ID: 10393250

Title: Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2.

PubMed ID: 10393250

DOI: 10.1016/s0378-1119(99)00162-6

PubMed ID: 12065666

Title: A novel seven transmembrane receptor induced during the early steps of astrocyte differentiation identified by differential expression.

PubMed ID: 12065666

DOI: 10.1046/j.1471-4159.2002.00847.x

PubMed ID: 24177535

Title: Constitutive nuclear localization of an alternatively spliced sirtuin-2 isoform.

PubMed ID: 24177535

DOI: 10.1016/j.jmb.2013.10.027

PubMed ID: 10931946

Title: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.

PubMed ID: 10931946

DOI: 10.1073/pnas.160270997

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 11226170

Title: A cytosolic NAD-dependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast.

PubMed ID: 11226170

DOI: 10.1093/emboj/20.1.197

PubMed ID: 11483616

Title: Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening.

PubMed ID: 11483616

DOI: 10.1074/jbc.m106779200

PubMed ID: 11812793

Title: Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases.

PubMed ID: 11812793

DOI: 10.1074/jbc.m111830200

PubMed ID: 12620231

Title: The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase.

PubMed ID: 12620231

DOI: 10.1016/s1097-2765(03)00038-8

PubMed ID: 12697818

Title: Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle.

PubMed ID: 12697818

DOI: 10.1128/mcb.23.9.3173-3185.2003

PubMed ID: 12963026

Title: Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene.

PubMed ID: 12963026

DOI: 10.1016/j.bbrc.2003.08.029

PubMed ID: 15213244

Title: Human histone deacetylase SIRT2 interacts with the homeobox transcription factor HOXA10.

PubMed ID: 15213244

DOI: 10.1093/jb/mvh084

PubMed ID: 16079181

Title: Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins.

PubMed ID: 16079181

DOI: 10.1091/mbc.e05-01-0033

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16648462

Title: SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis.

PubMed ID: 16648462

DOI: 10.1101/gad.1412706

PubMed ID: 17488717

Title: Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation.

PubMed ID: 17488717

DOI: 10.1074/jbc.m702990200

PubMed ID: 17516032

Title: Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin.

PubMed ID: 17516032

DOI: 10.1007/s11010-007-9478-6

PubMed ID: 17574768

Title: Mammalian Sir2-related protein (SIRT) 2-mediated modulation of resistance to axonal degeneration in slow Wallerian degeneration mice: a crucial role of tubulin deacetylation.

PubMed ID: 17574768

DOI: 10.1016/j.neuroscience.2007.04.059

PubMed ID: 16909107

Title: SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress.

PubMed ID: 16909107

DOI: 10.1038/sj.onc.1209857

PubMed ID: 17726514

Title: Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis.

PubMed ID: 17726514

DOI: 10.1371/journal.pone.0000784

PubMed ID: 18249187

Title: Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of p53.

PubMed ID: 18249187

DOI: 10.1016/j.bbrc.2008.01.114

PubMed ID: 18722353

Title: Acetylation of Sirt2 by p300 attenuates its deacetylase activity.

PubMed ID: 18722353

DOI: 10.1016/j.bbrc.2008.08.042

PubMed ID: 18640115

Title: SIRT2 is a negative regulator of anoxia-reoxygenation tolerance via regulation of 14-3-3 zeta and BAD in H9c2 cells.

PubMed ID: 18640115

DOI: 10.1016/j.febslet.2008.07.016

PubMed ID: 18332217

Title: The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility.

PubMed ID: 18332217

DOI: 10.1083/jcb.200707126

PubMed ID: 18995842

Title: The SIRT2 deacetylase regulates autoacetylation of p300.

PubMed ID: 18995842

DOI: 10.1016/j.molcel.2008.09.018

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19282667

Title: SIRT2 downregulation confers resistance to microtubule inhibitors by prolonging chronic mitotic arrest.

PubMed ID: 19282667

DOI: 10.4161/cc.8.8.8245

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20587414

Title: p300-mediated acetylation of histone H3 lysine 56 functions in DNA damage response in mammals.

PubMed ID: 20587414

DOI: 10.1074/jbc.m110.149393

PubMed ID: 21081649

Title: SIRT2 regulates NF-kappaB dependent gene expression through deacetylation of p65 Lys310.

PubMed ID: 21081649

DOI: 10.1242/jcs.073783

PubMed ID: 20543840

Title: Cytosolic FoxO1 is essential for the induction of autophagy and tumour suppressor activity.

PubMed ID: 20543840

DOI: 10.1038/ncb2069

PubMed ID: 22014574

Title: SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity.

PubMed ID: 22014574

DOI: 10.1016/j.ccr.2011.09.004

PubMed ID: 21791548

Title: The Sirtuin 2 microtubule deacetylase is an abundant neuronal protein that accumulates in the aging CNS.

PubMed ID: 21791548

DOI: 10.1093/hmg/ddr326

PubMed ID: 21726808

Title: Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase.

PubMed ID: 21726808

DOI: 10.1016/j.molcel.2011.04.028

PubMed ID: 21949390

Title: Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through polarity protein Par-3/atypical protein kinase C (aPKC) signaling.

PubMed ID: 21949390

DOI: 10.1073/pnas.1104969108

PubMed ID: 22771473

Title: Acetylation regulates subcellular localization of eukaryotic translation initiation factor 5A (eIF5A).

PubMed ID: 22771473

DOI: 10.1016/j.febslet.2012.06.042

PubMed ID: 22819792

Title: SIRT2 interferes with autophagy-mediated degradation of protein aggregates in neuronal cells under proteasome inhibition.

PubMed ID: 22819792

DOI: 10.1016/j.neuint.2012.07.010

PubMed ID: 22943040

Title: SIRT2 is a tumor suppressor that connects aging, acetylome, cell cycle signaling, and carcinogenesis.

PubMed ID: 22943040

PubMed ID: 23806683

Title: ERK1/2 regulates SIRT2 deacetylase activity.

PubMed ID: 23806683

DOI: 10.1016/j.bbrc.2013.06.053

PubMed ID: 23468428

Title: The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation.

PubMed ID: 23468428

DOI: 10.1101/gad.211342.112

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23932781

Title: Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth.

PubMed ID: 23932781

DOI: 10.1016/j.molcel.2013.07.002

PubMed ID: 23908241

Title: A role for SIRT2-dependent histone H3K18 deacetylation in bacterial infection.

PubMed ID: 23908241

DOI: 10.1126/science.1238858

PubMed ID: 24940000

Title: tRNA synthetase counteracts c-Myc to develop functional vasculature.

PubMed ID: 24940000

DOI: 10.7554/elife.02349

PubMed ID: 24769394

Title: Regulation of G6PD acetylation by KAT9/SIRT2 modulates NADPH homeostasis and cell survival during oxidative stress.

PubMed ID: 24769394

DOI: 10.1002/embj.201387224

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24681946

Title: SIRT2 regulates tumour hypoxia response by promoting HIF-1alpha hydroxylation.

PubMed ID: 24681946

DOI: 10.1038/onc.2014.76

PubMed ID: 27512957

Title: Oncogenic microtubule hyperacetylation through BEX4-mediated sirtuin 2 inhibition.

PubMed ID: 27512957

DOI: 10.1038/cddis.2016.240

PubMed ID: 29239724

Title: SIRT2 and lysine fatty acylation regulate the transforming activity of K-Ras4a.

PubMed ID: 29239724

DOI: 10.7554/elife.32436

PubMed ID: 32103017

Title: NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase cycle.

PubMed ID: 32103017

DOI: 10.1038/s41467-020-14893-x

PubMed ID: 11427894

Title: Structure of the histone deacetylase SIRT2.

PubMed ID: 11427894

DOI: 10.1038/89668

PubMed ID: 23454361

Title: Crystal structure analysis of human Sirt2 and its ADP-ribose complex.

PubMed ID: 23454361

DOI: 10.1016/j.jsb.2013.02.012

PubMed ID: 24389023

Title: Structural basis for potent inhibition of SIRT2 deacetylase by a macrocyclic peptide inducing dynamic structural change.

PubMed ID: 24389023

DOI: 10.1016/j.str.2013.12.001

PubMed ID: 25672491

Title: Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.

PubMed ID: 25672491

DOI: 10.1038/ncomms7263

PubMed ID: 25704306

Title: Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies.

PubMed ID: 25704306

DOI: 10.1038/srep08529

Sequence Information:

  • Length: 389
  • Mass: 43182
  • Checksum: A392442A8F6316F1
  • Sequence:
  • MAEPDPSHPL ETQAGKVQEA QDSDSDSEGG AAGGEADMDF LRNLFSQTLS LGSQKERLLD 
    ELTLEGVARY MQSERCRRVI CLVGAGISTS AGIPDFRSPS TGLYDNLEKY HLPYPEAIFE 
    ISYFKKHPEP FFALAKELYP GQFKPTICHY FMRLLKDKGL LLRCYTQNID TLERIAGLEQ 
    EDLVEAHGTF YTSHCVSASC RHEYPLSWMK EKIFSEVTPK CEDCQSLVKP DIVFFGESLP 
    ARFFSCMQSD FLKVDLLLVM GTSLQVQPFA SLISKAPLST PRLLINKEKA GQSDPFLGMI 
    MGLGGGMDFD SKKAYRDVAW LGECDQGCLA LAELLGWKKE LEDLVRREHA SIDAQSGAGV 
    PNPSTSASPK KSPPPAKDEA RTTEREKPQ

Genular Protein ID: 1424793629

Symbol: A0A0A0MRF5_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 15057824

Title: The DNA sequence and biology of human chromosome 19.

PubMed ID: 15057824

DOI: 10.1038/nature02399

Sequence Information:

  • Length: 234
  • Mass: 26712
  • Checksum: DECF52F95B7EA5C6
  • Sequence:
  • MDFLRNLFSQ TLSLGSQKER LLDELTLEGV ARYMQSERCR RVICLVGAGI STSAGIPDFR 
    SPSTGLYDNL EKYHLPYPEA IFEISYFKKH PEPFFALAKE LYPGQFKPTI CHYFMRLLKD 
    KGLLLRCYTQ NIDTLERIAG LEQEDLVEAH GTFYTSHCVS ASCRHEYPLS WMKEKIFSEV 
    TPKCEDCQSL VKPDIVFFGE SLPARFFSCM QSDFLKVDLL LVMGTSLQGR GLAG

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.