HCSGD entry for SIRT2
1. General information
| Official gene symbol | SIRT2 |
|---|---|
| Entrez ID | 22933 |
| Gene full name | sirtuin 2 |
| Other gene symbols | SIR2 SIR2L SIR2L2 |
| Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
|---|---|---|---|
| GO:0000183 | Chromatin silencing at rDNA | NAS | biological_process |
| GO:0003950 | NAD+ ADP-ribosyltransferase activity | TAS | molecular_function |
| GO:0005515 | Protein binding | IPI | molecular_function |
| GO:0005677 | Chromatin silencing complex | NAS | cellular_component |
| GO:0005737 | Cytoplasm | IDA | cellular_component |
| GO:0005874 | Microtubule | IDA | cellular_component |
| GO:0006342 | Chromatin silencing | NAS | biological_process |
| GO:0006348 | Chromatin silencing at telomere | NAS | biological_process |
| GO:0006471 | Protein ADP-ribosylation | NAS TAS | biological_process |
| GO:0006476 | Protein deacetylation | IDA | biological_process |
| GO:0007067 | Mitosis | IEA | biological_process |
| GO:0007096 | Regulation of exit from mitosis | NAS | biological_process |
| GO:0008134 | Transcription factor binding | IPI | molecular_function |
| GO:0008270 | Zinc ion binding | IDA | molecular_function |
| GO:0016458 | Gene silencing | NAS | biological_process |
| GO:0016575 | Histone deacetylation | IEA TAS | biological_process |
| GO:0017136 | NAD-dependent histone deacetylase activity | IDA | molecular_function |
| GO:0033558 | Protein deacetylase activity | IDA | molecular_function |
| GO:0034979 | NAD-dependent protein deacetylase activity | IDA | molecular_function |
| GO:0034983 | Peptidyl-lysine deacetylation | IDA | biological_process |
| GO:0035035 | Histone acetyltransferase binding | IPI | molecular_function |
| GO:0042325 | Regulation of phosphorylation | NAS | biological_process |
| GO:0042826 | Histone deacetylase binding | IPI | molecular_function |
| GO:0042903 | Tubulin deacetylase activity | IDA | molecular_function |
| GO:0043130 | Ubiquitin binding | IDA | molecular_function |
| GO:0043161 | Proteasome-mediated ubiquitin-dependent protein catabolic process | IMP | biological_process |
| GO:0045843 | Negative regulation of striated muscle tissue development | IDA | biological_process |
| GO:0045892 | Negative regulation of transcription, DNA-templated | IDA | biological_process |
| GO:0051775 | Response to redox state | NAS | biological_process |
| GO:0070403 | NAD+ binding | IDA IEA | molecular_function |
| GO:0090042 | Tubulin deacetylation | IEA | biological_process |
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4. Expression levels in datasets
- Meta-analysis result
| p-value up | p-value down | FDR up | FDR down |
|---|---|---|---|
| 0.3447122032 | 0.7434490559 | 0.9999902473 | 1.0000000000 |
- Individual experiment result
( "-" represent NA in the specific microarray platform )
( "-" represent NA in the specific microarray platform )
| Data source | Up or down | Log fold change |
|---|---|---|
| GSE11954 | Up | 0.1118829612 |
| GSE13712_SHEAR | Up | 0.0919337995 |
| GSE13712_STATIC | Down | -0.0210527463 |
| GSE19018 | Up | 0.0768642995 |
| GSE19899_A1 | Down | -0.0301745726 |
| GSE19899_A2 | Up | 0.1643694259 |
| PubMed_21979375_A1 | Down | -0.0842912170 |
| PubMed_21979375_A2 | Up | 1.0709356358 |
| GSE35957 | Down | -0.0326324721 |
| GSE36640 | Up | 0.2609368300 |
| GSE54402 | Down | -0.0367193352 |
| GSE9593 | Up | 0.1792272961 |
| GSE43922 | Up | 0.0096200484 |
| GSE24585 | Up | 0.2808762410 |
| GSE37065 | Down | -0.3674977591 |
| GSE28863_A1 | Down | -0.0780695613 |
| GSE28863_A2 | Down | -0.0265068777 |
| GSE28863_A3 | Down | -0.2193230327 |
| GSE28863_A4 | Down | -0.1000506840 |
| GSE48662 | Up | 0.3166588174 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
Not regulated by compounds
- Drugs
Not regulated by drugs
- MicroRNAs
- mirTarBase
MiRNA_name | mirBase ID | miRTarBase ID | Experiment | Support type | References (Pubmed ID) |
|---|---|---|---|---|---|
| hsa-miR-7-5p | MIMAT0000252 | MIRT025871 | Sequencing | Functional MTI (Weak) | 20371350 |
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- mirRecord
No target information from mirRecord
6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 50 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 27229617 | Increased expression of SIRT2 is a novel marker of cellular senescence and is dependent on wild type p53 status |
| 27229617 | In the present study, we now report upregulation of SIRT2 as a specific feature associated with stress induced premature senescence but not with either quiescence or cell death |
| 27229617 | Additionally, increase in SIRT2 expression was noted in different types of senescent conditions such as replicative and oncogene induced senescence using multiple cell lines |
| 27229617 | Induction of SIRT2 expression during senescence was dependent on p53 status as depletion of p53 by shRNA prevented its accumulation |
| 27229617 | Chromatin immunoprecipitation revealed the presence of p53 binding sites on the SIRT2 promoter suggesting its regulation by p53, which was also corroborated by the SEAP reporter assay |
| 27229617 | Overexpression or knockdown of SIRT2 had no effect on stress induced premature senescence, thereby indicating that SIRT2 increase is not a cause of senescence; rather it is an effect linked to senescence-associated changes |
| 27229617 | Overall, our results suggest SIRT2 as a promising marker of cellular senescence at least in cells with wild type p53 status |
| 26948035 | SIRT1 and SIRT2 are localized in the nucleus and cytoplasm |
| 26768768 | SIRT6 belongs to the mammalian homologs of Sir2 histone NAD(+)-dependent deacylase family |
| 26657715 | Sirtuin 1 (SIRT1), the mammalian ortholog of yeast longevity regulator Sir2, is a nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylase that elicits a variety of vasoprotective functions |
| 26522327 | We show that SIRT1, the human homolog of the Saccharomyces cerevisiae protein silent information regulator 2, which is involved in cellular senescence and possibly the response to inflammation, forms a stable complex with HMGB1 in murine macrophage RAW264 |
| 26414199 | The nicotinamide adenine dinucleotide-dependent protein deacetylase silent information regulator 2 (Sir2) regulates cellular lifespan in several organisms |
| 26414199 | This study shows that the expression patterns of HDAC4 and Sirtuin 1 (SIRT1; the mammalian homolog of Sir2) are positively correlated during cellular senescence |
| 25924011 | Resveratrol Induced Premature Senescence Is Associated with DNA Damage Mediated SIRT1 and SIRT2 Down-Regulation |
| 25924011 | Current study was undertaken to investigate the effects of resveratrol in human primary dermal fibroblasts (BJ) and to clarify the role of sirtuin family members in particular SIRT1 and SIRT2 that are known to be involved in cellular stress responses and cell cycle, respectively |
| 25924011 | Interestingly, at concentrations where resveratrol induced premature senescence we show a significant decrease in SIRT1 and SIRT2 levels by Western Blot and quantitative RT-PCR analysis |
| 25924011 | Conversely inhibition of SIRT1 and SIRT2 via siRNA or sirtinol treatment also induced senescence in BJ fibroblasts associated with increased SA-beta-gal activity, gamma-H2AX phosphorylation and p53, p21CIP1 and p16INK4A levels |
| 25924011 | In conclusion our data reveal that resveratrol induced premature senescence is associated with SIRT1 and SIRT2 down regulation in human dermal fibroblasts |
| 24997552 | Growth phase-dependent roles of Sir2 in oxidative stress resistance and chronological lifespan in yeast |
| 24997552 | Silent Information Regulator 2 (Sir2), a conserved NAD(+)-dependent histone deacetylase, has been implicated as one of the key factors in regulating stress response and longevity |
| 24997552 | Here, we report that the role of Sir2 in oxidative stress resistance and chronological lifespan is dependent on growth phase in yeast |
| 24997552 | Similarly, the expression of antioxidant genes, which are essential to cope with oxidative stress, was regulated by Sir2 in a growth phase-dependent manner |
| 24997552 | Collectively, our findings highlight the importance of the metabolic state of the cell in determining whether Sir2 can protect against or accelerate cellular aging of yeast |
| 24697269 | In an effort to identify small molecule inhibitors of sirtuins for potential use as chemotherapeutics as well as tools to modulate sirtuin activity, we previously identified a nonselective sirtuin inhibitor called cambinol (IC50 approximately 50 muM for SIRT1 and SIRT2) with in vitro and in vivo antilymphoma activity |
| 24697269 | 4-fold selectivity for SIRT2, and 8 with 6 |
| 24697269 | 3-fold selectivity for SIRT3 versus SIRT1 and SIRT2, respectively |
| 24697269 | In vitro cytotoxicity studies with these compounds as well as EX527, a potent and selective SIRT1 inhibitor, suggest that antilymphoma activity of this compound class may be predominantly due to SIRT2 inhibition |
| 24373458 | A common thread in many yeast replicative aging studies is the involvement of the ribosomal DNA gene repeats (rDNA), beginning with the discovery that the rDNA silencing gene, SIR2, regulates life span |
| 24025678 | Moreover, deficiencies in the H2B ubiquitylase complex Rad6/Bre1 as well as the deubiquitylase Ubp10 reduced the lifespan by altering both H3K4 and H3K79 methylation and Sir2 recruitment |
| 24025678 | Thus, these results show that low levels of H2B ubiquitylation are a prerequisite for a normal lifespan and the trans-tail regulation of histone modifications regulates age-associated Sir2 recruitment through telomeric silencing |
| 23997094 | Similarly, sirtuin expression was relatively well-preserved in aorta from both genotypes, whereas expression of SIRT1, SIRT2, SIRT3, SIRT4, and SIRT6 were significantly reduced in the aortic valve |
| 23993840 | The highly repetitive rDNA exhibits genomic instability, and the antiaging histone deacetylase gene SIR2 regulates this instability |
| 23993840 | We previously proposed that SIR2 governs lifespan by repressing rDNA noncoding transcription and rDNA instability, but the extent to which lifespan is affected by SIR2 acting at the rDNA versus other genomic regions, and the relationship between rDNA noncoding transcription/rDNA stability and lifespan have remained controversial |
| 23993840 | Here, we show that repression of noncoding transcription extends lifespan and makes SIR2 dispensable for lifespan extension |
| 23993840 | These results indicate that Sir2 maintains lifespan through repression of E-pro noncoding transcription in the rDNA cluster, rather than pleiotropically at other loci |
| 23742046 | Among many signalling mechanisms involved in altering longevity and aging, the insulin/IGF-1 pathway and the Sir2 deacetylase are highly significant |
| 23592245 | It was known that, similar to the yeast Sir2 protein, human SIRT6 deacetylates histones and regulates DNA stability and repair; however, new mechanistic insights can be derived from the discovery of the highly substrate-specific histone deacetylase activity of SIRT6 |
| 23494737 | Sirtuin 3 (SIRT3) is one of the seven mammalian sirtuins, which are homologs of the yeast Sir2 gene |
| 22932127 | SIRT2, an NAD-dependent class III histone deacetylase, contributes to H4-K16Ac deacetylation and DNA compaction in human fibroblast cell lines that assemble striking senescence-associated heterochromatin foci (SAHFs) |
| 22783411 | Mammalian SIRT1, as the closest homolog of the yeast Sir2, was extensively involved in regulating cell processes, including cell senescence, aging and neuronal protection, as well as having anti-apoptotic properties |
| 21497775 | Silent information regulator 2 (Sir2/Sirt1), a member of the sirtuin family of class III histone deacetylases, has been implicated extensively in lifespan extension and is a prominent drug target in antiaging medicine |
| 21415463 | The implication of Sir2 in replicative aging and senescence in Saccharomyces cerevisiae |
| 21415463 | In Saccharomyces cerevisiae, silent information regulator 2 (Sir2) modulates cellular senescence |
| 21415463 | Moreover, Sir2 plays a crucial role in promoting ribosomal DNA (rDNA) stability and longevity under TOR inhibition |
| 21415463 | Here we review the implication of rDNA stabilizers in longevity, discuss how Sir2 stabilizes rDNA under TOR inhibition and speculate on the link between sumoylation and Sir2-related pro-aging pathways |
| 21130086 | Lifespan extension evoked by Sir2 protein in lower organisms has attracted a large amount of interests in the last decade |
| 20829644 | Here, we focus on the sirtuins, the mammalian homologs of the yeast life-span-extending molecule, Sir2 |
| 20829644 | Among the sirtuin family proteins in mammals, the one most similar to yeast Sir2 is SIRT1, which is involved in multiple pathways, including the repair of DNA double-strand breaks |
| 20352263 | The increased sensitivity to BrdU caused by a defect in MPT5 was suppressed by a mutation in SIR2, SIR3, or SIR4, which is involved in chromatin silencing and transcriptional repression |
| 20078953 | As the most homologic homologue of silent information regulator 2 of yeast, Sirt1 gene is extensively expressed in mature tissues, and is rich in early embryo and reproductive cells |
| 19875981 | Sas2 normally prevents the Sir2/3/4 heterochromatin complex from leaving the telomere and spreading to internal euchromatic loci |
| 19736527 | Interplay between histone deacetylase SIR-2, linker histone H1 and histone methyltransferases in heterochromatin formation |
| 19736527 | The NAD(+)-dependent histone deacetylase SIR-2 and the H1 linker histone are intriguing chromatin elements that are connected to chromatin regulation and cell viability in the single cellular eukaryotic organism yeast |
| 19736527 | However, it remains an open question how SIR-2 and H1 mediate heterochromatin formation in simple multi-cellular organisms such as C |
| 19736527 | Recently we have identified SIR-2 |
| 19736527 | In addition we show that SIR-2 |
| 19736527 | Here we discuss the interplay between SIR-2, H1 histone and histone methyltransferases in modulation of chromatin structure in further detail |
| 19286634 | In yeast, CR extends the lifespan by increasing the activity of silencing information regulator 2 (Sir2), an NAD(+)-dependent deacetylase |
| 19286634 | SIRT1, a mammalian homolog of Sir2, has been reported to downregulate p53 activity and thereby prolong the lifespan of cells |
| 19067655 | We have tested this hypothesis in a cohort of preimplantation human renal allograft biopsies ( n = 75) that have been assayed by real-time polymerase chain reaction for the expression of known markers of cellular damage and biological aging, including CDKN2A, CDKN1A, SIRT2 and POT1 |
| 18691183 | Deletion of the SIR2 gene causes a decrease of lifespan, while insertion of an extra copy of SIR2 extends lifespan, indicating that like in S |
| 18691183 | Interestingly, Sir2 deletion does not result in the accumulation of extra-chromosomal rDNA molecules, but influences the retention of oxidized proteins in mother cells, suggesting that the extra-chromosomal rDNA molecules may not be associated with cellular aging in C |
| 18638538 | Whereas other laboratories have proposed that sirtuins (Sir2 and its homologs), a family of conserved proteins which are NAD(+)-dependent histone deacetylases, can extend longevity in various model organisms, we propose that one sirtuin, i |
| 18638538 | In Saccharomyces cerevisiae (yeast), the deletion of Sir2 increases DNA damage but in combination with longevity mutations in principal intracellular signal transduction mediators, or in combination with calorie restriction it causes a further increase in the chronological lifespan as well as an increase in the stress resistance and a major reduction in age-dependent genomic instability |
| 18638538 | Our recent results also provide evidence for a role of the mammalian Sir2 ortholog SirT1 in the activation of a highly conserved neuronal pathway and in the sensitization of neurons to oxidative damage |
| 18337721 | The Sir2 deacetylase regulates chromatin silencing and lifespan in Saccharomyces cerevisiae |
| 18320031 | Sir2, a NAD-dependent deacetylase, modulates lifespan in yeasts, worms and flies |
| 18320031 | The SIRT1, mammalian homologue of Sir2, regulates signaling for favoring survival in stress |
| 18203716 | Sir2, an NAD-dependent histone deacetylase, has been proven to extend life span in yeast and Caenorhabditis elegans |
| 18203716 | Mammalian Sir2 (SIRT1) has also been found to regulate premature cellular senescence induced by the tumor suppressors PML and p53 |
| 18193082 | While investigating the transcriptional repression activities of RBP1, we observed a genetic link between RBP1 and SIR2 |
| 18193082 | Further work uncovered an interaction between RBP1 family proteins and the mammalian homologue of SIR2, SIRT1 |
| 17916362 | Yeast Sir2 plays critical roles in gene silencing, stress resistance and longevity |
| 17916362 | Mammalian Sirt1 NAD(+)-dependent protein deacetylase, the closest homolog of Sir2, regulates cell cycle, cellular senescence, apoptosis and metabolism, by functional interactions with a number of biological molecules such as p53 |
| 17691205 | SIRT7 are mammalian versions of the yeast SIR2 gene |
| 17595514 | It has been reported that p53 acetylation, which promotes cellular senescence, can be regulated by the NAD(+)-dependent deacetylase SIRT1, the human homolog of yeast Sir2, a protein that modulates lifespan |
| 17202845 | All the other DSB repair proteins tested, Sir2, TRF1 and Ku80, did not show any significant differences upon aging |
| 16940753 | We found that aging in deltaNp63alpha transgenic mice and other mouse models correlated with levels of Sirt1, a mammalian SIR2 orthologue thought to extend the lifespan in lower species |
| 16546327 | Among many genes thus far reported contributing to aging process, the yeast silent information regulator-2 (SIR2) and its homologues in other species, which belong to the family of type III histone and protein deacetylases, have been the subject of active discussion |
| 16546327 | The demonstrated roles of SIRT1, the mammalian counterpart of the yeast SIR2, reveal that SIRT1 regulates important cellular processes including anti-apoptosis, neuronal protection, cellular senescence, aging and longevity |
| 16516887 | Relocalization occurs concomitantly with interaction with a subset of nuclear proteins, including PCNA, p53 and several regulators of acetylation such as the p300/CBP and PCAF histone acetyltransferases (HATs), as well as the histone deacetylases HDAC1 and hSir2 |
| 15207474 | We also demonstrate that the model can be used to gain insight into how an extra copy of the Sir2 gene might extend lifespan and we show how the model makes novel, testable predictions about patterns of age-specific mortality in yeast populations |
| 15063846 | A link between transcription and intermediary metabolism: a role for Sir2 in the control of acetyl-coenzyme A synthetase |
| 15063846 | The silent information regulator protein (Sir2) and its homologs (collectively known as sirtuins) are NAD+-dependent deacetylase enzymes involved in chromosome stability, gene silencing and cell aging in eukaryotes and archaea |
| 14522900 | Both ING1 and p53 were able to suppress AFP transcription and cause p21 induction; hSIR2, a negative regulator of the p53 protein, showed the opposite effects on the AFP promoter and, like HDAC1, repressed p21 promoter activity |
| 14522900 | In addition, we found that p33(ING1b) physically interacts with hSIR2, reverses its ability to induce the AFP promoter, and induces acetylation of p53 residues at Lys(373) and/or Lys(382) |
| 14522900 | The first is by binding to the AT-motif and excluding HNF1 binding while possibly targeting HAT activity to promoter regions, and the second is by increasing the levels of active, acetylated p53 via binding and inhibiting the ability of hSIR2 to deacetylate p53 protein |
| 12960381 | Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice |
| 12960381 | SIRT1 is a mammalian homolog of the Saccharomyces cerevisiae chromatin silencing factor Sir2 |
| 12493915 | Activation of the acetylated enzyme requires the nicotinamide adenine dinucleotide-dependent protein deacetylase activity of the CobB Sir2 protein from S |
| 12493915 | These findings extend our knowledge of the roles of Sir2 proteins in gene silencing, chromosome stability, and cell aging and imply that lysine acetylation is a common regulatory mechanism in eukaryotes and prokaryotes |
| 12220851 | Human Sir2 and the 'silencing' of p53 activity |
| 12220851 | Members of the evolutionarily conserved silent information regulator 2 (Sir2) protein family are nicotinamide adenine dinucleotide (NAD(+))-dependent histone deacetylases |
| 12220851 | In yeast, the founding Sir2 protein is known to function in transcriptional silencing processes through the deacetylation of histones H3 and H4, thus setting up a repressive chromatin structure |
| 12220851 | Yeast and Caenorhabditis elegans Sir2 are also involved in regulating the life span of these organisms |
| 12220851 | However, several recent studies have now determined a remarkable function for the human SIRT1 protein, which is the closest human homolog of yeast Sir2 |
| 12006491 | Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence |
| 12006491 | Sir2 is a conserved protein and was recently shown to regulate lifespan extension both in budding yeast and worms |
| 12006491 | Here, we show that SIRT1, the human Sir2 homolog, is recruited to the promyelocytic leukemia protein (PML) nuclear bodies of mammalian cells upon overexpression of either PML or oncogenic Ras (Ha-rasV12) |
| 11672523 | Expression of wild-type hSir2 in human cells reduces the transcriptional activity of p53 |
| 11672523 | In contrast, expression of a catalytically inactive hSir2 protein potentiates p53-dependent apoptosis and radiosensitivity |
| 11268038 | Sound silencing: the Sir2 protein and cellular senescence |
| 11268038 | The yeast protein Sir2p (Silent Information Regulator 2) is a histone deacetylase involved in transcriptional silencing and the control of genomic stability |
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