Primary Information |
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BoMiProt ID | Bomi7361 |
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Protein Name | NAD-dependent protein deacetylase sirtuin-7/NAD-dependent protein deacylase sirtuin-7/Regulatory protein SIR2 homolog 7/SIR2-like protein 7 |
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Organism | Bos taurus |
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Uniprot ID | Q0P595 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_001068685.1 |
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Aminoacid Length | 400 |
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Molecular Weight | 45043 |
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FASTA Sequence |
Download |
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Gene Name | SIRT7 |
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Gene ID | 505662 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | Removes acetyl groups from ATM,which is essential for dephosphorylation and deactivation of ATM during the late stages of DNA damage response.SIRT7 can decrease the protein level of SMAD4 by deacetylating and destabilizing SMAD4 protein which is AR corepressor which can inhibit the transcription of AR. PAF53 hypo-acetylation by SIRT7 correlates with increased Pol I occupancy on rDNA and transcriptional activation |
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Biochemical Properties | a class III histone deacetylase. NAD+-dependent deacetylases.Within the SIRT7 catalytic domain, serine residue 111 (S111) and histidine residue 187 (H187) are responsible for the deacetylation activity.Binds 1 zinc ion per subunit. |
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PTMs | Phosphorylation,Ubl conjugation,Methylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| NA |
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Predicted Disorder Regions | 1-48, 65-70, 348-378, 391-400 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | Methylation at Arg-388 by PRMT6 inhibits the H3K18Ac histone deacetylase activity, promoting mitochondria biogenesis and maintaining mitochondria respiration.Phosphorylated during mitosis by a CDK complex.SIRT7 is phosphorylated during cellular energy stress by 5′ AMP-activated protein kinase (AMPK), which has a crucial role in determining SIRT7 subcellular distribution and degradation.SIRT7 is modified by Lys-63-linked polyubiquitination. Ubiquitin-specific protease 7 (USP7) negatively regulates the enzymatic activity of SIRT7 through deubiquitination to control gluconeogenesis. |
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Bibliography | 1.Wu D, Li Y, Zhu KS, Wang H, Zhu WG. Advances in Cellular Characterization of the Sirtuin Isoform, SIRT7. Front Endocrinol (Lausanne). 2018 Nov 19;9:652. doi: 10.3389/fendo.2018.00652. PMID: 30510540; PMCID: PMC6253933. 2.Tang M, Li Z, Zhang C, Lu X, Tu B, Cao Z, Li Y, Chen Y, Jiang L, Wang H, Wang L, Wang J, Liu B, Xu X, Wang H, Zhu WG. SIRT7-mediated ATM deacetylation is essential for its deactivation and DNA damage repair. Sci Adv. 2019 Mar 27;5(3):eaav1118. doi: 10.1126/sciadv.aav1118. PMID: 30944854; PMCID: PMC6436926. |