PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32527012-3 2020 STRAP is acetylated at lysines 147, 148, and 156 by the acetyltransferases CREB-binding protein (CBP) and that the acetylation is reversed by the deacetylase sirtuin7 (SIRT7). Lysine 23-30 sirtuin 7 Homo sapiens 158-166 33838133-7 2021 In general, there were two pathways confirmed using tissues and cells: 1) Increased histone deacetylase sirtuin 7 (SIRT7) mediated loss of histone 3 lysine 18 acetylation (H3K18ac) at the promoter of OAT2 and inhibited its transcription. Lysine 149-155 sirtuin 7 Homo sapiens 115-120 31196136-9 2019 At the molecular level, we observed that SIRT7 interacts with and induces deacetylation of p53 at lysines 320 and 373. Lysine 98-105 sirtuin 7 Homo sapiens 41-46 30756531-1 2019 As a member of the Sirtuins family in mammals, SIRT7 locates in nucleus and is a highly specific H3K18Ac (acetylated lysine 18 of histone H3) deacetylase. Lysine 117-123 sirtuin 7 Homo sapiens 47-52 30282801-3 2018 Using co-expression in HEK293T cells and co-immunoprecipitation assays, we observed that SIRT7 deacetylates WDR77 at Lys-3 and Lys-243, which reduced of WDR77"s interaction with PRMT5. Lysine 117-120 sirtuin 7 Homo sapiens 89-94 30282801-3 2018 Using co-expression in HEK293T cells and co-immunoprecipitation assays, we observed that SIRT7 deacetylates WDR77 at Lys-3 and Lys-243, which reduced of WDR77"s interaction with PRMT5. Lysine 127-130 sirtuin 7 Homo sapiens 89-94 28426094-7 2017 SIRT7 counteracts GCN5-directed acetylation of lysine 48 within the catalytic domain of CDK9, deacetylation promoting CTD phosphorylation and transcription elongation. Lysine 47-53 sirtuin 7 Homo sapiens 0-5 30282801-6 2018 In summary, SIRT7 is a major deacetylase for WDR77, and SIRT7-mediated deacetylation of WDR77 at Lys-3 and Lys-243 weakens the WDR77-PRMT5 interaction and activity and thereby suppresses growth of cancer cells. Lysine 97-100 sirtuin 7 Homo sapiens 12-17 30282801-6 2018 In summary, SIRT7 is a major deacetylase for WDR77, and SIRT7-mediated deacetylation of WDR77 at Lys-3 and Lys-243 weakens the WDR77-PRMT5 interaction and activity and thereby suppresses growth of cancer cells. Lysine 97-100 sirtuin 7 Homo sapiens 56-61 30282801-6 2018 In summary, SIRT7 is a major deacetylase for WDR77, and SIRT7-mediated deacetylation of WDR77 at Lys-3 and Lys-243 weakens the WDR77-PRMT5 interaction and activity and thereby suppresses growth of cancer cells. Lysine 107-110 sirtuin 7 Homo sapiens 12-17 30282801-6 2018 In summary, SIRT7 is a major deacetylase for WDR77, and SIRT7-mediated deacetylation of WDR77 at Lys-3 and Lys-243 weakens the WDR77-PRMT5 interaction and activity and thereby suppresses growth of cancer cells. Lysine 107-110 sirtuin 7 Homo sapiens 56-61 28655758-7 2017 We showed that USP7 interacts with SIRT7 both in vitro and in vivo, and we further demonstrated that SIRT7 undergoes endogenous Lys-63-linked polyubiquitination, which is removed by USP7. Lysine 128-131 sirtuin 7 Homo sapiens 35-40 28655758-7 2017 We showed that USP7 interacts with SIRT7 both in vitro and in vivo, and we further demonstrated that SIRT7 undergoes endogenous Lys-63-linked polyubiquitination, which is removed by USP7. Lysine 128-131 sirtuin 7 Homo sapiens 101-106 27997115-10 2017 Knockdown of SIRT7 increased the lysine fatty acylation of several nuclear proteins based on metabolic labeling with an alkyne-tagged fatty acid analog, supporting that the defatty-acylase activity of SIRT7 is physiologically relevant. Lysine 33-39 sirtuin 7 Homo sapiens 13-18 27997115-10 2017 Knockdown of SIRT7 increased the lysine fatty acylation of several nuclear proteins based on metabolic labeling with an alkyne-tagged fatty acid analog, supporting that the defatty-acylase activity of SIRT7 is physiologically relevant. Lysine 33-39 sirtuin 7 Homo sapiens 201-206 26704979-3 2016 Here we showed that the human Dicer protein interacts with SIRT7, an NAD(+)-dependent H3K18Ac (acetylated lysine 18 of histone H3) deacetylase, and holds a proportion of SIRT7 in the cytoplasm. Lysine 106-112 sirtuin 7 Homo sapiens 59-64 26704979-3 2016 Here we showed that the human Dicer protein interacts with SIRT7, an NAD(+)-dependent H3K18Ac (acetylated lysine 18 of histone H3) deacetylase, and holds a proportion of SIRT7 in the cytoplasm. Lysine 106-112 sirtuin 7 Homo sapiens 170-175 24134843-1 2013 Sirt7 localizes in the nucleus (enriched in the nucleolus) and is an NAD(+)-dependent deacetylase with high selectivity for the acetylated lysine 18 of histone H3 (H3K18Ac). Lysine 139-145 sirtuin 7 Homo sapiens 0-5 26907567-3 2016 Here, we reported that SIRT7 can be activated by DNA to hydrolyze the acetyl group from lysine residues in vitro on histone peptides and histones in the chromatin context. Lysine 88-94 sirtuin 7 Homo sapiens 23-28 27246221-1 2016 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. Lysine 31-37 sirtuin 7 Homo sapiens 0-9 27246221-1 2016 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. Lysine 31-37 sirtuin 7 Homo sapiens 11-16 25200183-5 2014 These wide-ranging effects of SIRT7 on mitochondrial homeostasis are the consequence of the deacetylation of distinct lysine residues located in the hetero- and homodimerization domains of GABPbeta1, a master regulator of nuclear-encoded mitochondrial genes. Lysine 118-124 sirtuin 7 Homo sapiens 30-35 24536059-3 2014 SIRT7 associates with chromatin, where it catalyzes selective deacetylation of lysine 18 on histone H3 (H3K18), an emerging epigenetic biomarker of aggressive tumors and poor clinical outcome in patients with cancer. Lysine 79-85 sirtuin 7 Homo sapiens 0-5 22698398-2 2012 demonstrated that SIRT7 maintains critical features that define cancer cells by removing the acetylation mark on lysine 18 of histone H3. Lysine 113-119 sirtuin 7 Homo sapiens 18-23 22722849-3 2012 Here we show that SIRT7 is an NAD(+)-dependent H3K18Ac (acetylated lysine 18 of histone H3) deacetylase that stabilizes the transformed state of cancer cells. Lysine 67-73 sirtuin 7 Homo sapiens 18-23 35046516-7 2022 The SIRT7-mediated dessuccinylation of PRMT5 lysine 387 fails to bind to STUB1, decreasing PRMT5 ubiquitination and increasing the interaction between PRMT5 and Mep50, which promotes the formation of the PRMT5-Mep50 octamer. Lysine 45-51 sirtuin 7 Homo sapiens 4-9