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 Factors determining DNA double-strand break repair pathway choice in G2 phase. Factors determining DNA double-strand break repair pathway choice in G2 phase. EMBO J. (0261-4189) 2011 imex curation Shibata A., Conrad S., Birraux J., Geuting V., Barton O., Ismail A., Kakarougkas A., Meek K., Taucher-Scholz G., Löbrich M., Jeggo PA. Only protein-protein interactions human-a_549 Homo sapiens Caucasian lung carcinoma cell line a_549 Human Caucasian lung carcinoma fluorescence imaging fluorescence microscopy fluorescence imaging immunostaining immunostaining Shibata A., Conrad S., Birraux J., Geuting V., Barton O., Ismail A., Kakarougkas A., Meek K., Taucher-Scholz G., Löbrich M., Jeggo PA. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation Factors determining DNA double-strand break repair pathway choice in G2 phase. Factors determining DNA double-strand break repair pathway choice in G2 phase. EMBO J. (0261-4189) 2011 imex curation Shibata A., Conrad S., Birraux J., Geuting V., Barton O., Ismail A., Kakarougkas A., Meek K., Taucher-Scholz G., Löbrich M., Jeggo PA. Only protein-protein interactions human-48br Homo sapiens 48br 48br fluorescence imaging fluorescence microscopy fluorescence imaging immunostaining immunostaining Shibata A., Conrad S., Birraux J., Geuting V., Barton O., Ismail A., Kakarougkas A., Meek K., Taucher-Scholz G., Löbrich M., Jeggo PA. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation tif1b_human Transcription intermediary factor 1-beta TRIM28 KAP1 RNF96 TIF1B Tripartite motif-containing protein 28 Nuclear corepressor KAP-1 KRAB-associated protein 1 KRAB-interacting protein 1 RING finger protein 96 E3 SUMO-protein ligase TRIM28 RING-type E3 ubiquitin transferase TIF1-beta protein protein human Homo sapiens Human MAASAAAASAAAASAASGSPGPGEGSAGGEKRSTAPSAAASASASAAASSPAGGGAEALELLEHCGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCKQQCFSKDIVENYFMRDSGSKAATDAQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKSRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFASWALESDNNTALLLSKKLIYFQLHRALKMIVDPVEPHGEMKFQWDLNAWTKSAEAFGKIVAERPGTNSTGPAPMAPPRAPGPLSKQGSGSSQPMEVQEGYGFGSGDDPYSSAEPHVSGVKRSRSGEGEVSGLMRKVPRVSLERLDLDLTADSQPPVFKVFPGSTTEDYNLIVIERGAAAAATGQPGTAPAGTPGAPPLAGMAIVKEEETEAAIGAPPTATEGPETKPVLMALAEGPGAEGPRLASPSGSTSSGLEVVAPEGTSAPGGGPGTLDDSATICRVCQKPGDLVMCNQCEFCFHLDCHLPALQDVPGEEWSCSLCHVLPDLKEEDGSLSLDGADSTGVVAKLSPANQRKCERVLLALFCHEPCRPLHQLATDSTFSLDQPGGTLDLTLIRARLQEKLSPPYSSPQEFAQDVGRMFKQFNKLTEDKADVQSIIGLQRFFETRMNEAFGDTKFSAVLVEPPPMSLPGAGLSSQELSGGPGDGP DIP protein Q13263 original sequence version: 156 DIP protein Q13263 original sequence version: 154 DIP protein Q13263-1 original sequence version: 143 DIP protein Q13263 original sequence version: 198 DIP protein Q13263 original sequence version: 155 2027BABB7C94FE20 h2ax_human Histone H2AX H2AX H2AFX Histone H2A.X protein protein human Homo sapiens Human MSGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTSATVGPKAPSGGKKATQASQEY DIP protein P16104 original sequence version: 114 DIP protein P16104 original sequence version: 110 DIP protein P16104 original sequence version: 117 DIP protein P16104 original sequence version: 133 DIP protein P16104 original sequence version: 140 DIP protein P16104 original sequence version: 113 DIP protein P16104 original sequence version: 99 D4683775C2E6C3A9 tp53b_human TP53-binding protein 1 TP53BP1 protein protein human Homo sapiens Human MDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEDDSGSHFSMLSRHLPNLQTHKENPVLDVVSNPEQTAGEERGDGNSGFNEHLKENKVADPVDSSNLDTCGSISQVIEQLPQPNRTSSVLGMSVESAPAVEEEKGEELEQKEKEKEEDTSGNTTHSLGAEDTASSQLGFGVLELSQSQDVEENTVPYEVDKEQLQSVTTNSGYTRLSDVDANTAIKHEEQSNEDIPIAEQSSKDIPVTAQPSKDVHVVKEQNPPPARSEDMPFSPKASVAAMEAKEQLSAQELMESGLQIQKSPEPEVLSTQEDLFDQSNKTVSSDGCSTPSREEGGCSLASTPATTLHLLQLSGQRSLVQDSLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQEGRQDKPMDTSVLSEEGGEPFQKKLQSGEPVELENPPLLPESTVSPQASTPISQSTPVFPPGSLPIPSQPQFSHDIFIPSPSLEEQSNDGKKDGDMHSSSLTVECSKTSEIEPKNSPEDLGLSLTGDSCKLMLSTSEYSQSPKMESLSSHRIDEDGENTQIEDTEPMSPVLNSKFVPAENDSILMNPAQDGEVQLSQNDDKTKGDDTDTRDDISILATGCKGREETVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMEIKEHHPEEGSSGSEVEEIPETPCESQGEELKEENMESVPLHLSLTETQSQGLCLQKEMPKKECSEAMEVETSVISIDSPQKLAILDQELEHKEQEAWEEATSEDSSVVIVDVKEPSPRVDVSCEPLEGVEKCSDSQSWEDIAPEIEPCAENRLDTKEEKSVEYEGDLKSGTAETEPVEQDSSQPSLPLVRADDPLRLDQELQQPQTQEKTSNSLTEDSKMANAKQLSSDAEAQKLGKPSAHASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVMSESMVETHDPILGSGKGDSGAAPDVDDKLCLRMKLVSPETEASEESLQFNLEKPATGERKNGSTAVAESVASPQKTMSVLSCICEARQENEARSEDPPTTPIRGNLLHFPSSQGEEEKEKLEGDHTIRQSQQPMKPISPVKDPVSPASQKMVIQGPSSPQGEAMVTDVLEDQKEGRSTNKENPSKALIERPSQNNIGIQTMECSLRVPETVSAATQTIKNVCEQGTSTVDQNFGKQDATVQTERGSGEKPVSAPGDDTESLHSQGEEEFDMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSLHRTSSGTSLSAMHSSGSSGKGAGPLRGKTSGTEPADFALPSSRGGPGKLSPRKGVSQTGTPVCEEDGDAGLGIRQGGKAPVTPRGRGRRGRPPSRTTGTRETAVPGPLGIEDISPNLSPDDKSFSRVVPRVPDSTRRTDVGAGALRRSDSPEIPFQAAAGPSDGLDASSPGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLVEGKRKRRSNVSSPATPTASSSSSTTPTRKITESPRASMGVLSGKRKLITSEEERSPAKRGRKSATVKPGAVGAGEFVSPCESGDNTGEPSALEEQRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLPDGPTGSSEEEEEFLEIPPFNKQYTESQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH DIP protein Q12888 original sequence version: 117 DIP protein Q12888 original sequence version: 110 DIP protein Q12888 original sequence version: 113 DIP protein Q12888 original sequence version: 165 DIP protein Q12888 original sequence version: 149 DIP protein Q12888 original sequence version: 143 13E2CC8A265F9D2A rad51_human DNA repair protein RAD51 homolog 1 RAD51 RAD51A RECA RAD51 homolog A protein protein human Homo sapiens Human MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD DIP protein Q06609 original sequence version: 154 DIP protein Q06609 original sequence version: 145 DIP protein Q06609 original sequence version: 122 DIP protein Q06609 original sequence version: 121 DIP protein Q06609 original sequence version: 125 DIP protein Q06609 original sequence version: 123 DIP protein Q06609 original sequence version: 144 DIP protein Q06609 original sequence version: 167 DIP protein Q06609 original sequence version: 169 26578E6206DEDEDA h2afx-trim28 2 gH2AX 4 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell pKAP1 3 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization f2c homomint mint To facilitate quantification, we treated cells with a high concentration of Etp (150 mM) and observed B8 gH2AX foci and 6.9 pKAP-1 foci with strong co-localisation at 8 h, when the fast DSB repair process is completed (Figure 2C). h2afx-rad51 2 gH2AX 4 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell RAD51 6 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization f2e homomint mint Finally, we observed that RPA, Rad51 and gH2AX foci co-localise with pKAP-1 foci in G2 cells at 8 h after Etp treatment (Figure 2E). h2afx-rad51-1 1 gH2AX 4 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell RAD51 6 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization homomint mint sf2c h2afx-tp53bp1-3 1 gH2AX 4 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell 53BP1 5 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization sf2b homomint mint