PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 35453408-5 2022 A decreased interaction between sirtuin 3 and superoxide dismutase 2 (SOD2) induced SOD2 acetylation on lysine 68 and inactivation, leading to mitochondrial oxidative stress and dysfunction and hypertrophy after 24 h of Iso treatment. Lysine 104-110 superoxide dismutase 2 Homo sapiens 46-68 35453408-5 2022 A decreased interaction between sirtuin 3 and superoxide dismutase 2 (SOD2) induced SOD2 acetylation on lysine 68 and inactivation, leading to mitochondrial oxidative stress and dysfunction and hypertrophy after 24 h of Iso treatment. Lysine 104-110 superoxide dismutase 2 Homo sapiens 70-74 35453408-5 2022 A decreased interaction between sirtuin 3 and superoxide dismutase 2 (SOD2) induced SOD2 acetylation on lysine 68 and inactivation, leading to mitochondrial oxidative stress and dysfunction and hypertrophy after 24 h of Iso treatment. Lysine 104-110 superoxide dismutase 2 Homo sapiens 84-88 31160585-0 2019 Lysine 68 acetylation directs MnSOD as a tetrameric detoxification complex versus a monomeric tumor promoter. Lysine 0-6 superoxide dismutase 2 Homo sapiens 30-35 33867840-2 2021 We have previously demonstrated that MnSOD lysine-68 (K68) acetylation (K68-Ac) leads to a change in function from a superoxide-scavenging homotetramer to a peroxidase-directed monomer. Lysine 43-49 superoxide dismutase 2 Homo sapiens 37-42 33680286-6 2021 Furthermore, deletion of GCN5L1 could reduce MnSOD acetylation on lysine 68 and activate its activity, thereby scavenging excessive ROS and relieving oxidative stress-induced renal inflammation and fibrosis. Lysine 66-72 superoxide dismutase 2 Homo sapiens 45-50 25315187-8 2015 Further mass spectrometry analysis indicated that both ACAT1 and MnSOD had characterized acetylation at lysine residues, which is the first time to identify acetylation of ACAT1 and MnSOD in ccRCC. Lysine 104-110 superoxide dismutase 2 Homo sapiens 65-70 28687409-8 2017 Furthermore, the deacetylase effect of Sirt3 enhanced the MnSOD activity by deacetylation at the lysine 68 residue and therapeutic effect of UCB-MSCs on skin-wound healing was increased by EphB2 activation. Lysine 97-103 superoxide dismutase 2 Homo sapiens 58-63 27721400-7 2017 Acetylation at lysine-68 (K68) inhibits MnSOD catalytic activity and thus represents an important post-translational regulatory mechanism in human cells. Lysine 15-21 superoxide dismutase 2 Homo sapiens 40-45 26935174-4 2016 Furthermore, these tumors exhibit aberrant manganese superoxide dismutase (MnSOD) acetylation at lysine 68 and lysine 122 and have abnormally high reactive oxygen species (ROS) levels, which have been observed in many types of breast cancer. Lysine 97-103 superoxide dismutase 2 Homo sapiens 43-73 26935174-4 2016 Furthermore, these tumors exhibit aberrant manganese superoxide dismutase (MnSOD) acetylation at lysine 68 and lysine 122 and have abnormally high reactive oxygen species (ROS) levels, which have been observed in many types of breast cancer. Lysine 97-103 superoxide dismutase 2 Homo sapiens 75-80 25908444-7 2015 The lysine 68 (K68) site is the most important acetylation site contributing to SOD2 activation and plays a role in cell survival after paraquat treatment. Lysine 4-10 superoxide dismutase 2 Homo sapiens 80-84 25529796-4 2015 Genetic deletion of Sirt1 increased mitochondrial superoxide dismutase 2 (Sod2) acetylation of lysine residue 68, thereby enhancing reactive oxygen species (ROS) production and reducing SOD2 activity. Lysine 95-101 superoxide dismutase 2 Homo sapiens 74-78 25315187-8 2015 Further mass spectrometry analysis indicated that both ACAT1 and MnSOD had characterized acetylation at lysine residues, which is the first time to identify acetylation of ACAT1 and MnSOD in ccRCC. Lysine 104-110 superoxide dismutase 2 Homo sapiens 182-187 24269899-10 2014 Further studies demonstrated a significant increase in posttranslational modifications of tyrosine and lysine residues in MnSOD protein and oxidation of Cys at the active site (Cys32 and Cys35) and the regulatory site (Cys62 and Cys69) of Trx1 in high-grade PCa compared to BN tissues. Lysine 103-109 superoxide dismutase 2 Homo sapiens 122-127 21386137-4 2011 It has recently been shown that MnSOD enzymatic activity is regulated by the reversible acetylation of specific, evolutionarily conserved lysine(s) in the protein. Lysine 138-144 superoxide dismutase 2 Homo sapiens 32-37 22732184-6 2012 In this regard, we and others have shown that MnSOD is regulated, at least in part, by the deacetylation of specific conserved lysines in a reaction catalyzed by the mitochondrial sirtuin, Sirt3. Lysine 127-134 superoxide dismutase 2 Homo sapiens 46-51 22732184-7 2012 We speculate that the regulation of MnSOD activity by lysine acetylation via an electrostatic repulsion mechanism is a conserved and critical aspect of MnSOD regulation necessary to maintain mitochondrial homeostasis. Lysine 54-60 superoxide dismutase 2 Homo sapiens 36-41 22732184-7 2012 We speculate that the regulation of MnSOD activity by lysine acetylation via an electrostatic repulsion mechanism is a conserved and critical aspect of MnSOD regulation necessary to maintain mitochondrial homeostasis. Lysine 54-60 superoxide dismutase 2 Homo sapiens 152-157 22710435-5 2012 Mass spectrometry results showed a complex pattern of MnSOD-methylation at both lysine (68, 89, 122, and 202) and arginine (197 and 216) residues. Lysine 80-86 superoxide dismutase 2 Homo sapiens 54-59 22710435-7 2012 Computational-based simulations indicate that lysine and arginine methylation of MnSOD during quiescence would allow greater accessibility to the enzyme active site as well as increase the positive electrostatic potential around and within the active site. Lysine 46-52 superoxide dismutase 2 Homo sapiens 81-86 21566644-3 2011 Here, we report that SOD2 is acetylated at Lys 68 and that this acetylation decreases SOD2 activity. Lysine 43-46 superoxide dismutase 2 Homo sapiens 21-25 21566644-3 2011 Here, we report that SOD2 is acetylated at Lys 68 and that this acetylation decreases SOD2 activity. Lysine 43-46 superoxide dismutase 2 Homo sapiens 86-90 21386137-5 2011 These results, suggest for the first time, that the mitochondria contain bidirectional post-translational signaling networks, similar to that observed in the cytoplasm and nucleus, and that changes in lysine acetylation alter MnSOD enzymatic activity. Lysine 201-207 superoxide dismutase 2 Homo sapiens 226-231 11369207-12 2001 Glutamic acid substitution of the four lysine residues in the polybasic stretch at the COOH terminus of Ki-Ras completely abolishes the activation of Mn-SOD, although it does not inhibit ERK1/2-induced transcription. Lysine 39-45 superoxide dismutase 2 Homo sapiens 150-156