HCSGD entry for SIRT7
1. General information
| Official gene symbol | SIRT7 |
|---|---|
| Entrez ID | 51547 |
| Gene full name | sirtuin 7 |
| Other gene symbols | SIR2L7 |
| Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
|---|---|---|---|
| GO:0000122 | Negative regulation of transcription from RNA polymerase II promoter | IDA | biological_process |
| GO:0003682 | Chromatin binding | IDA | molecular_function |
| GO:0005515 | Protein binding | IPI | molecular_function |
| GO:0005730 | Nucleolus | IDA | cellular_component |
| GO:0005731 | Nucleolus organizer region | IDA | cellular_component |
| GO:0005737 | Cytoplasm | IEA | cellular_component |
| GO:0007072 | Positive regulation of transcription on exit from mitosis | IMP | biological_process |
| GO:0009303 | RRNA transcription | IMP | biological_process |
| GO:0046872 | Metal ion binding | IEA | molecular_function |
| GO:0070403 | NAD+ binding | IEA | molecular_function |
| GO:0070932 | Histone H3 deacetylation | IDA | biological_process |
| GO:0070933 | Histone H4 deacetylation | IDA | biological_process |
| GO:0097372 | NAD-dependent histone deacetylase activity (H3-K18 specific) | IDA | molecular_function |
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4. Expression levels in datasets
- Meta-analysis result
| p-value up | p-value down | FDR up | FDR down |
|---|---|---|---|
| 0.0127180274 | 0.9814790813 | 0.2819346801 | 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 | 0.5990979623 |
| GSE13712_SHEAR | Up | 1.1164979538 |
| GSE13712_STATIC | Up | 0.7130537069 |
| GSE19018 | Down | -0.3049593664 |
| GSE19899_A1 | Up | 0.1040767531 |
| GSE19899_A2 | Up | 0.9178371573 |
| PubMed_21979375_A1 | Up | 0.8308880650 |
| PubMed_21979375_A2 | Up | 0.6937706874 |
| GSE35957 | Down | -0.4451884250 |
| GSE36640 | Up | 0.5124471066 |
| GSE54402 | Up | 0.3438330213 |
| GSE9593 | Up | 0.2060593256 |
| GSE43922 | Up | 0.0852650398 |
| GSE24585 | Up | 0.1906916802 |
| GSE37065 | Down | -0.0067914289 |
| GSE28863_A1 | Down | -0.0138807657 |
| GSE28863_A2 | Down | -0.1407586858 |
| GSE28863_A3 | Up | 0.0744630216 |
| GSE28863_A4 | Up | 0.2221873509 |
| GSE48662 | Down | -0.0039770383 |
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-335-5p | MIMAT0000765 | MIRT018583 | Microarray | Functional MTI (Weak) | 18185580 |
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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: 11 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 27246221 | Molecular, Cellular, and Physiological Characterization of Sirtuin 7 (SIRT7) |
| 27246221 | Sirtuin 7 (SIRT7), a histone 3 lysine 18 (H3K18) deacetylase, functions at chromatin to suppress endoplasmic reticulum (ER) stress and mitochondrial protein folding stress (PFS(mt)), and prevent the development of fatty liver disease and hematopoietic stem cell aging |
| 27246221 | In this chapter, we provide a methodology to characterize the molecular, cellular, and physiological functions of SIRT7 |
| 26991832 | Sirtuin 7 (SIRT7) was identified as a target of miR-152 |
| 26991832 | SIRT7 was downregulated in senescent HDPSCs, whereas miR-152 inhibition upregulated SIRT7 and suppressed the senescent phenotype and SIRT7 overexpression rescued miR-152-induced senescence |
| 26991832 | Our results demonstrate that the miR-152/SIRT7 axis plays a key role in the regulation of HDPSC senescence and provide a candidate target to improve the functional and therapeutic potential of HDPSCs |
| 26948035 | Seven SIRT family members have been identified in mammals, from SIRT1, the best studied for its role in vascular aging, to SIRT7 |
| 26948035 | SIRT3, SIRT4, and SIRT5 are mitochondrial, and SIRT6 and SIRT7 are nuclear |
| 26169984 | Novel protein-protein interactions of TPPII, p53, and SIRT7 |
| 26169984 | Novel protein-protein interactions of TPPII, SIRT7, and p53 were detected by co-immunoprecipitation using both HeLa cell lysates and the cytoplasmic fraction prepared by fractionation of mouse liver tissue |
| 26169984 | The cytoplasmic interactions were likewise detected between TPPII and SIRT7 in control HEK293 and lowactTPPII HEK293 cells |
| 26169984 | The interactions of SIRT7 with p53 were confirmed in three HEK293 cell transformants as well |
| 26169984 | The cytoplasmic occurrence of SIRT7 protein was demonstrated by immunofluorescence, when both nucleolar and cytoplasmic signals were identified within HEK293 cells and primary human fibroblasts |
| 26169984 | The unique cytoplasmic localization of SIRT7 protein was discussed based on an epitope specificity of N-terminus specific SIRT7 antibodies utilized in the present study compared with C-terminus specific antibodies previously used for nuclear detection of SIRT7 by other authors |
| 26169984 | The epitope sequence of N-terminal antibodies is occurring in all three splicing variants of SIRT7 compared to the epitope of C-terminal antibody, which is specific exclusively to the splicing variant 1 |
| 26169984 | The cytoplasmic localization of p53 detected by immunofluorescence supported the results from its interactions with TPPII and SIRT7 observed by in situ PLA within model cells |
| 26169984 | Novel interactions of TPPII, p53, and SIRT7 presented in this study might contribute to the knowledge of the regulatory effects of these proteins on apoptotic pathways and to the understanding mechanisms of aging and lifespan regulation |
| 26112889 | This review focuses on the cardiovascular effects of Sirt1, Sirt3, Sirt6, and Sirt7 |
| 26112889 | Sirt7 plays a role in lipid metabolism and cardiomyopathies |
| 25970806 | Stressed SIRT7: facing a crossroad of senescence and immortality |
| 25970806 | SIRT7 with coenzyme NAD catalyzes protein de-acetylation |
| 25970806 | In stress response, SIRT7 regulates protein folding in mitochondria with unknown mechanisms |
| 25970806 | Decreases in SIRT7 entrain hematopoietic stem cell senescence, but increasing SIRT7 causes elevation of hematopoietic stem cell regenerative function |
| 25970806 | We discuss the recent findings on SIRT7 and its binding proteins, NRF1 and GABPbeta1, in decision making between the choices of inducing cell aging and immortality |
| 25792330 | Here, we identified a regulatory branch of the mitochondrial unfolded protein response (UPR(mt)), which is mediated by the interplay of SIRT7 and NRF1 and is coupled to cellular energy metabolism and proliferation |
| 25792330 | SIRT7 inactivation caused reduced quiescence, increased mitochondrial protein folding stress (PFS(mt)), and compromised regenerative capacity of hematopoietic stem cells (HSCs) |
| 25792330 | SIRT7 expression was reduced in aged HSCs, and SIRT7 up-regulation improved the regenerative capacity of aged HSCs |
| 24782448 | Comparative interactomes of SIRT6 and SIRT7: Implication of functional links to aging |
| 24782448 | Although diverse functions of sirtuins have been proposed, those functions of SIRT6 and SIRT7 that are mediated by their interacting proteins remain elusive |
| 24782448 | Our interactomes revealed 136 interacting proteins for SIRT6 and 233 for SIRT7 while confirming seven and 111 proteins identified previously for SIRT6 and SIRT7, respectively |
| 24782448 | Comparison of SIRT6 and SIRT7 interactomes under the same experimental conditions disclosed 111 shared proteins, implying related functional links |
| 24782448 | Interactions of two highly acetylated proteins, nucleophosmin (NPM1) and nucleolin, with SIRT6 and SIRT7 were confirmed by co-immunoprecipitation |
| 24782448 | NPM1 was found to be deacetylated by both SIRT6 and SIRT7 |
| 24782448 | In senescent cells, the acetylation level of NPM1 was increased in conjunction with decreased levels of SIRT6 and SIRT7, suggesting that the acetylation of NPM1 could be regulated by SIRT6 and SIRT7 in the aging process |
| 24782448 | Our comparative interactomic study of SIRT6 and SIRT7 implies important functional links to aging by their associations with interacting proteins |
| 23680022 | Intracellular distribution of human SIRT7 and mapping of the nuclear/nucleolar localization signal |
| 23680022 | Sirtuins belong to a class of NAD-dependent deacetylases, and include seven distinct isoforms, of which SIRT7 is the least studied member |
| 23680022 | In the present study, the subcellular expression of SIRT7 in primary fibroblasts undergoing senescence was evaluated by immunocytochemistry and immunoblot assay |
| 23680022 | Expression of nucleolar SIRT7 in young fibroblast was very prominent, decreased in pre-senescent cells, and became undetectable in the senescent cells |
| 23680022 | Interestingly, we observed previously unreported staining for cytoplasmic SIRT7 in fibroblasts, and report the existence of a steady-state level of SIRT7 in cytoplasm |
| 23680022 | 5 kDa) SIRT7 in the cytoplasmic fraction and the low-molecular-mass (45 kDa) SIRT7 in the nuclear fraction was observed in the immunoblot analysis of various cell types |
| 23680022 | The specificity of the N-terminal antibodies for detection of cytoplasmic SIRT7 was confirmed by RNAi and peptide competition assays |
| 23680022 | The two forms of SIRT7 showed reciprocal expression following serum starvation, nocodazole and okadaic acid treatments, and also during senescence |
| 23680022 | Using a combination of deletion constructs and site-directed mutagenesis, we defined the role of two distinct SIRT7 sequences in the N-terminal region (amino acids 61-76, LQGRSRRREGLKRRQE) and the C-terminal region (amino acids 392-400, KRTKRKKVT) for nuclear and nucleolar import, respectively |
| 23680022 | In conclusion, we report for the first time the existence of a cytoplasmic pool of SIRT7 in addition to its well-known nucleolar form, identify distinct localization signals for its nuclear/nucleolar targeting, and describe an association between loss of nucleolar SIRT7 and replicative senescence |
| 17691205 | SIRT7 are mammalian versions of the yeast SIR2 gene |
| 17003781 | Levels of SIRT7 expression were significantly increased in breast cancer (P<0 |
| 17003781 | Increased levels of SIRT3 and SIRT7 transcription were also associated with node-positive breast cancer (P<0 |
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