MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it SIRT3-dependent deacetylation exacerbates acetaminophen hepatotoxicity. SIRT3-dependent deacetylation exacerbates acetaminophen hepatotoxicity. EMBO Rep. (1469-221X) 2011 imex curation Lu Z., Bourdi M., Li JH., Aponte AM., Chen Y., Lombard DB., Gucek M., Pohl LR., Sack MN. Only protein-protein interactions mouse-liver Mus musculus liver liver anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Lu Z., Bourdi M., Li JH., Aponte AM., Chen Y., Lombard DB., Gucek M., Pohl LR., Sack MN. EMBO Rep. (1469-221X) 2011 Only protein-protein interactions imex curation SIRT3-dependent deacetylation exacerbates acetaminophen hepatotoxicity. SIRT3-dependent deacetylation exacerbates acetaminophen hepatotoxicity. EMBO Rep. (1469-221X) 2011 imex curation Lu Z., Bourdi M., Li JH., Aponte AM., Chen Y., Lombard DB., Gucek M., Pohl LR., Sack MN. Only protein-protein interactions mouse-hepa_1c1 Mus musculus hepatoma, BW7756; Derived from: Hepa-1cl, cloned from the Hepa-1 cell line hepa_1c1 mouse, C57L liver hepatoma, BW7756; Derived from: Hepa-1cl, cloned from the Hepa-1 cell line anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Lu Z., Bourdi M., Li JH., Aponte AM., Chen Y., Lombard DB., Gucek M., Pohl LR., Sack MN. EMBO Rep. (1469-221X) 2011 Only protein-protein interactions imex curation sir3_human NAD-dependent protein deacetylase sirtuin-3, mitochondrial SIRT3 SIR2L3 SIR2-like protein 3 Regulatory protein SIR2 homolog 3 protein protein human Homo sapiens Human MAFWGWRAAAALRLWGRVVERVEAGGGVGPFQACGCRLVLGGRDDVSAGLRGSHGARGEPLDPARPLQRPPRPEVPRAFRRQPRAAAPSFFFSSIKGGRRSISFSVGASSVVGSGGSSDKGKLSLQDVAELIRARACQRVVVMVGAGISTPSGIPDFRSPGSGLYSNLQQYDLPYPEAIFELPFFFHNPKPFFTLAKELYPGNYKPNVTHYFLRLLHDKGLLLRLYTQNIDGLERVSGIPASKLVEAHGTFASATCTVCQRPFPGEDIRADVMADRVPRCPVCTGVVKPDIVFFGEPLPQRFLLHVVDFPMADLLLILGTSLEVEPFASLTEAVRSSVPRLLINRDLVGPLAWHPRSRDVAQLGDVVHGVESLVELLGWTEEMRDLVQRETGKLDGPDK DIP protein Q9NTG7 original sequence version: 123 DIP protein Q9NTG7 original sequence version: 80 4BA8BD3AC5FC7901 aldh2_mouse Aldehyde dehydrogenase, mitochondrial Aldh2 Ahd-1 Ahd1 ALDH class 2 AHD-M1 ALDHI ALDH-E2 protein protein mouse Mus musculus Mouse MLRAALTTVRRGPRLSRLLSAAATSAVPAPNHQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAARAAFQLGSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS 200806F63D48F4DA sir3_mouse NAD-dependent protein deacetylase sirtuin-3 Regulatory protein SIR2 homolog 3 Sirt3 Sir2l3 SIR2-like protein 3 protein protein mouse Mus musculus Mouse MALDPLGAVVLQSIMALSGRLALAALRLWGPGGGRRPISLCVGASGGFGGGGSSEKKFSLQDVAELLRTRACSRVVVMVGAGISTPSGIPDFRSPGSGLYSNLQQYDIPYPEAIFELGFFFHNPKPFFMLAKELYPGHYRPNVTHYFLRLLHDKELLLRLYTQNIDGLERASGIPASKLVEAHGTFVTATCTVCRRSFPGEDIWADVMADRVPRCPVCTGVVKPDIVFFGEQLPARFLLHMADFALADLLLILGTSLEVEPFASLSEAVQKSVPRLLINRDLVGPFVLSPRRKDVVQLGDVVHGVERLVDLLGWTQELLDLMQRERGKLDGQDR mint NAD-dependent deacetylase. Despite some ability to deacetylate histones in vitro, it is unlikely in vivo D8C936A83C4A8AF7 aldh2_human Aldehyde dehydrogenase, mitochondrial ALDH class 2 ALDHI ALDH-E2 ALDH2 ALDM protein protein human Homo sapiens Human MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS DIP protein P05091 original sequence version: null DIP protein P05091 original sequence version: 140 E8F74D44D285A00E sirt3-aldh2 1 Sirt3 5 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role bait bait living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level Aldh2 4 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association f2c homomint mint aldh2-sirt3 1 Sirt3 5 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level Aldh2 4 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role bait bait living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association f2c homomint mint aldh2-sirt3-1 2 SIRT3 3 anti tag western anti tag western blot anti tag western predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell Q9NTG7:p.His248Tyr mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain H Y Tue Jul 12 10:19:50 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 15:49:44 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his248tyr' Tue Jun 30 19:37:45 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His248Tyr' ha tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ALDH2 6 anti tag western anti tag western blot anti tag western predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association f4b homomint mint binding of NAPQI to ALDH2 was increased after overexpression of deacetylase-competent SIRT3, and attenuated in the presence of the deacetylase-mutant SIRT3, with reduced ALDH2 acetylation correlating to the degree of NAPQI binding (Fig 4B). In parallel, the small-interfering RNA knockdown of SIRT3 in these hepatocytes diminished NAPQI binding to ALDH2 (Fig 4C)