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 http://mint.bio.uniroma2.it/mint chang-2013c-1 Acetylation of p53 stimulates miRNA processing and determines cell survival following genotoxic stress. human-hct116 Human colon carcinoma HCT116 cells hct116 Human colon carcinoma line HCT116 anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Chang J., Davis-Dusenbery B.N., Kashima R., Jiang X., Marathe N., Sessa R., Louie J., Gu W., Lagna G., Hata A. akiko.hata@ucsf.edu EMBO J. (0261-4189) 2013 Only protein-protein interactions imex curation ddx5_human Probable ATP-dependent RNA helicase DDX5 HLR1 DDX5 HELR G17P1 DEAD box protein 5 RNA helicase p68 protein protein human Homo sapiens Human MSGYSSDRDRGRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSSLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQTSFRTGNPTGTYQNGYDSTQQYGSNVPNMHNGMNQQAYAYPATAAAPMIGYPMPTGYSQ p53_human Cellular tumor antigen p53 TP53 P53 Tumor suppressor p53 Phosphoprotein p53 Antigen NY-CO-13 protein protein human Homo sapiens Human MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD rnc_human Ribonuclease 3 Ribonuclease III DROSHA p241 RNASEN RN3 RNASE3L Protein Drosha protein protein human Homo sapiens Human MMQGNTCHRMSFHPGRGCPRGRGGHGARPSAPSFRPQNLRLLHPQQPPVQYQYEPPSAPSTTFSNSPAPNFLPPRPDFVPFPPPMPPSAQGPLPPCPIRPPFPNHQMRHPFPVPPCFPPMPPPMPCPNNPPVPGAPPGQGTFPFMMPPPSMPHPPPPPVMPQQVNYQYPPGYSHHNFPPPSFNSFQNNPSSFLPSANNSSSPHFRHLPPYPLPKAPSERRSPERLKHYDDHRHRDHSHGRGERHRSLDRRERGRSPDRRRQDSRYRSDYDRGRTPSRHRSYERSRERERERHRHRDNRRSPSLERSYKKEYKRSGRSYGLSVVPEPAGCTPELPGEIIKNTDSWAPPLEIVNHRSPSREKKRARWEEEKDRWSDNQSSGKDKNYTSIKEKEPEETMPDKNEEEEEELLKPVWIRCTHSENYYSSDPMDQVGDSTVVGTSRLRDLYDKFEEELGSRQEKAKAARPPWEPPKTKLDEDLESSSESECESDEDSTCSSSSDSEVFDVIAEIKRKKAHPDRLHDELWYNDPGQMNDGPLCKCSAKARRTGIRHSIYPGEEAIKPCRPMTNNAGRLFHYRITVSPPTNFLTDRPTVIEYDDHEYIFEGFSMFAHAPLTNIPLCKVIRFNIDYTIHFIEEMMPENFCVKGLELFSLFLFRDILELYDWNLKGPLFEDSPPCCPRFHFMPRFVRFLPDGGKEVLSMHQILLYLLRCSKALVPEEEIANMLQWEELEWQKYAEECKGMIVTNPGTKPSSVRIDQLDREQFNPDVITFPIIVHFGIRPAQLSYAGDPQYQKLWKSYVKLRHLLANSPKVKQTDKQKLAQREEALQKIRQKNTMRREVTVELSSQGFWKTGIRSDVCQHAMMLPVLTHHIRYHQCLMHLDKLIGYTFQDRCLLQLAMTHPSHHLNFGMNPDHARNSLSNCGIRQPKYGDRKVHHMHMRKKGINTLINIMSRLGQDDPTPSRINHNERLEFLGDAVVEFLTSVHLYYLFPSLEEGGLATYRTAIVQNQHLAMLAKKLELDRFMLYAHGPDLCRESDLRHAMANCFEALIGAVYLEGSLEEAKQLFGRLLFNDPDLREVWLNYPLHPLQLQEPNTDRQLIETSPVLQKLTEFEEAIGVIFTHVRLLARAFTLRTVGFNHLTLGHNQRMEFLGDSIMQLVATEYLFIHFPDHHEGHLTLLRSSLVNNRTQAKVAEELGMQEYAITNDKTKRPVALRTKTLADLLESFIAALYIDKDLEYVHTFMNVCFFPRLKEFILNQDWNDPKSQLQQCCLTLRTEGKEPDIPLYKTLQTVGPSHARTYTVAVYFKGERIGCGKGPSIQQAEMGAAMDALEKYNFPQMAHQKRFIERKYRQELKEMRWEREHQEREPDETEDIKK ddx5-tp53-4 1478257 n/a 1478258 western blot western blot Immuno blot Immuno blot unspecified role unspecified role bait bait subcellular prep subcellular preparation subcellular prep physiological level physiological level endogenous level endogenous endogenous endogenous level n/a 1478259 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey subcellular prep subcellular preparation subcellular prep physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association false false false We tested whether K120 acetylation of p53 stabilizes the interaction with p68, in turn promoting p53‐dependent pri‐miRNA processing. p68 was immunoprecipitated from nuclear extracts of cells stimulated with CPT or Nut3, followed by immunoblot analysis using antibodies against total p53 or K120‐acetylated p53 (p53‐Ac‐K120) (Figure 6A). Although levels of total p53 and K382‐acetylated p53 were similar following both CPT and Nut3 treatment, only CPT increased K120 acetylation (Figure 6A, input) and the interaction between p53 and p68 (Figure 6A, IP: p68). We also confirmed that the p53 associated with p68 upon CPT treatment was K120 acetylated (Figure 6A, p53‐Ac‐K120). Lysine acetylation of p68 was not detected following CPT or Nut3 treatment (Figure 6A, Ac‐p68). f6a ddx5-tp53-5 1478257 n/a 1478258 western blot western blot Immuno blot Immuno blot unspecified role unspecified role bait bait subcellular prep subcellular preparation subcellular prep physiological level physiological level endogenous level endogenous endogenous endogenous level n/a 1478259 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed P04637:p.Lys120Arg mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false The acetyl‐K120 mimic K120Q was constitutively associated with p68 and Drosha in the absence of CPT treatment (Figure 6B), while WT p53 associated with p68 upon DNA damage stress (Figure 6A), suggesting that K120 acetylation is sufficient to promote interaction of p53 with the Drosha complex. K120R mutant of p53 was unable to interact with p68 both in the presence and absence of CPT stimulation (Figure 6B; Supplementary Figure S8). sf8 tp53-ddx5-2 1478257 n/a 1478260 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey subcellular prep subcellular preparation subcellular prep physiological level physiological level endogenous level endogenous endogenous endogenous level n/a 1478258 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey subcellular prep subcellular preparation subcellular prep physiological level physiological level endogenous level endogenous endogenous endogenous level n/a 1478259 western blot western blot Immuno blot Immuno blot unspecified role unspecified role bait bait subcellular prep subcellular preparation subcellular prep over-expressed over expressed level over-expressed P04637:p.Lys120Gln mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false The acetyl‐K120 mimic K120Q was constitutively associated with p68 and Drosha in the absence of CPT treatment (Figure 6B), while WT p53 associated with p68 upon DNA damage stress (Figure 6A), suggesting that K120 acetylation is sufficient to promote interaction of p53 with the Drosha complex. K120R mutant of p53 was unable to interact with p68 both in the presence and absence of CPT stimulation (Figure 6B; Supplementary Figure S8). f6b