IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell (0092-8674) 2005 imex curation Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk 18-Sep-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro enzymatic footprint enzymatic footprinting enzymatic footprint western blot western blot Immuno blot Immuno blot Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk Accepted 2014-JUL-25 by PPORRAS Cell (0092-8674) 2005 Only protein-protein interactions imex curation MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell (0092-8674) 2005 imex curation Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk 18-Sep-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. The GST fusion construct of MDC1used in this experiment is described in PMID:12607003. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk Accepted 2014-JUL-25 by PPORRAS Cell (0092-8674) 2005 Only protein-protein interactions imex curation MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell (0092-8674) 2005 imex curation Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk 18-Sep-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. The tandem BRCT domain-containing construct of MDC1used in this experiment is described in PMID:12607003. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk Accepted 2014-JUL-25 by PPORRAS Cell (0092-8674) 2005 Only protein-protein interactions imex curation MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell (0092-8674) 2005 imex curation Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk 18-Sep-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down anti tag western anti tag western blot anti tag western Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. The GFP-tagged constructs used in this experiment are described in PMID:12475977. Only a schematic representation of the deletion constructs is given but not the exact start and stop positions of the deleted regions. In this case, the positions of the required tandem BRCT domain of MDC1 are taken from interpro. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk Accepted 2014-JUL-25 by PPORRAS Cell (0092-8674) 2005 Only protein-protein interactions imex curation MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell (0092-8674) 2005 imex curation Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk 18-Sep-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk Accepted 2014-JUL-25 by PPORRAS Cell (0092-8674) 2005 Only protein-protein interactions imex curation MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell (0092-8674) 2005 imex curation Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk 18-Sep-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down ms participant Identification by mass spectrometry ms participant Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk Accepted 2014-JUL-25 by PPORRAS Cell (0092-8674) 2005 Only protein-protein interactions imex curation MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell (0092-8674) 2005 imex curation Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk 18-Sep-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., Jackson S.P. The GST fusion constructs of MDC1used in this experiment are described in PMID:12607003. ssmerdo@nimr.mrc.ac.uk,s.jackson@gurdon.cam.ac.uk Accepted 2014-JUL-25 by PPORRAS Cell (0092-8674) 2005 Only protein-protein interactions imex curation mdc1_human Mediator of DNA damage checkpoint protein 1 Nuclear factor with BRCT domains 1 MDC1 KIAA0170 NFBD1 protein protein human Homo sapiens Human MEDTQAIDWDVEEEEETEQSSESLRCNVEPVGRLHIFSGAHGPEKDFPLHLGKNVVGRMPDCSVALPFPSISKQHAEIEILAWDKAPILRDCGSLNGTQILRPPKVLSPGVSHRLRDQELILFADLLCQYHRLDVSLPFVSRGPLTVEETPRVQGETQPQRLLLAEDSEEEVDFLSERRMVKKSRTTSSSVIVPESDEEGHSPVLGGLGPPFAFNLNSDTDVEEGQQPATEEASSAARRGATVEAKQSEAEVVTEIQLEKDQPLVKERDNDTKVKRGAGNGVVPAGVILERSQPPGEDSDTDVDDDSRPPGRPAEVHLERAQPFGFIDSDTDAEEERIPATPVVIPMKKRKIFHGVGTRGPGAPGLAHLQESQAGSDTDVEEGKAPQAVPLEKSQASMVINSDTDDEEEVSAALTLAHLKESQPAIWNRDAEEDMPQRVVLLQRSQTTTERDSDTDVEEEELPVENREAVLKDHTKIRALVRAHSEKDQPPFGDSDDSVEADKSSPGIHLERSQASTTVDINTQVEKEVPPGSAIIHIKKHQVSVEGTNQTDVKAVGGPAKLLVVSLEEAWPLHGDCETDAEEGTSLTASVVADVRKSQLPAEGDAGAEWAAAVLKQERAHEVGAQGGPPVAQVEQDLPISRENLTDLVVDTDTLGESTQPQREGAQVPTGREREQHVGGTKDSEDNYGDSEDLDLQATQCFLENQGLEAVQSMEDEPTQAFMLTPPQELGPSHCSFQTTGTLDEPWEVLATQPFCLRESEDSETQPFDTHLEAYGPCLSPPRAIPGDQHPESPVHTEPMGIQGRGRQTVDKVMGIPKETAERVGPERGPLERETEKLLPERQTDVTGEEELTKGKQDREQKQLLARDTQRQESDKNGESASPERDRESLKVEIETSEEIQEKQVQKQTLPSKAFEREVERPVANRECDPAELEEKVPKVILERDTQRGEPEGGSQDQKGQASSPTPEPGVGAGDLPGPTSAPVPSGSQSGGRGSPVSPRRHQKGLLNCKMPPAEKASRIRAAEKVSRGDQESPDACLPPTVPEAPAPPQKPLNSQSQKHLAPPPLLSPLLPSIKPTVRKTRQDGSQEAPEAPLSSELEPFHPKPKIRTRKSSRMTPFPATSAAPEPHPSTSTAQPVTPKPTSQATRSRTNRSSVKTPEPVVPTAPELQPSTSTDQPVTSEPTSQVTRGRKSRSSVKTPETVVPTALELQPSTSTDRPVTSEPTSQATRGRKNRSSVKTPEPVVPTAPELQPSTSTDQPVTSEPTYQATRGRKNRSSVKTPEPVVPTAPELRPSTSTDRPVTPKPTSRTTRSRTNMSSVKTPETVVPTAPELQISTSTDQPVTPKPTSRTTRSRTNMSSVKNPESTVPIAPELPPSTSTEQPVTPEPTSRATRGRKNRSSGKTPETLVPTAPKLEPSTSTDQPVTPEPTSQATRGRTNRSSVKTPETVVPTAPELQPSTSTDQPVTPEPTSQATRGRTDRSSVKTPETVVPTAPELQASASTDQPVTSEPTSRTTRGRKNRSSVKTPETVVPAAPELQPSTSTDQPVTPEPTSRATRGRTNRSSVKTPESIVPIAPELQPSTSRNQLVTPEPTSRATRCRTNRSSVKTPEPVVPTAPEPHPTTSTDQPVTPKLTSRATRRKTNRSSVKTPKPVEPAASDLEPFTPTDQSVTPEAIAQGGQSKTLRSSTVRAMPVPTTPEFQSPVTTDQPISPEPITQPSCIKRQRAAGNPGSLAAPIDHKPCSAPLEPKSQASRNQRWGAVRAAESLTAIPEPASPQLLETPIHASQIQKVEPAGRSRFTPELQPKASQSRKRSLATMDSPPHQKQPQRGEVSQKTVIIKEEEEDTAEKPGKEEDVVTPKPGKRKRDQAEEEPNRIPSRSLRRTKLNQESTAPKVLFTGVVDARGERAVLALGGSLAGSAAEASHLVTDRIRRTVKFLCALGRGIPILSLDWLHQSRKAGFFLPPDEYVVTDPEQEKNFGFSLQDALSRARERRLLEGYEIYVTPGVQPPPPQMGEIISCCGGTYLPSMPRSYKPQRVVITCPQDFPHCSIPLRVGLPLLSPEFLLTGVLKQEAKPEAFVLSPLEMSST DIP protein Q14676 original sequence version: 135 DIP protein Q14676 original sequence version: 82 DIP protein Q14676-1 original sequence version: 100 DIP protein Q14676-1 original sequence version: 110 DIP protein Q14676 original sequence version: 110 DIP protein Q14676 original sequence version: 146 DIP protein Q14676 original sequence version: 137 DIP protein Q14676 original sequence version: 88 A8B880A25617EC96 nbn_human Nibrin Nijmegen breakage syndrome protein 1 Cell cycle regulatory protein p95 NBN NBS1 NBS P95 protein protein human Homo sapiens Human MWKLLPAAGPAGGEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEEKMQNGFSRTLKSGDGITFGVFGSKFRIEYEPLVACSSCLDVSGKTALNQAILQLGGFTVNNWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKAVESKKQPPQIESFYPPLDEPSIGSKNVDLSGRQERKQIFKGKTFIFLNAKQHKKLSSAVVFGGGEARLITEENEEEHNFFLAPGTCVVDTGITNSQTLIPDCQKKWIQSIMDMLQRQGLRPIPEAEIGLAVIFMTTKNYCDPQGHPSTGLKTTTPGPSLSQGVSVDEKLMPSAPVNTTTYVADTESEQADTWDLSERPKEIKVSKMEQKFRMLSQDAPTVKESCKTSSNNNSMVSNTLAKMRIPNYQLSPTKLPSINKSKDRASQQQQTNSIRNYFQPSTKKRERDEENQEMSSCKSARIETSCSLLEQTQPATPSLWKNKEQHLSENEPVDTNSDNNLFTDTDLKSIVKNSASKSHAAEKLRSNKKREMDDVAIEDEVLEQLFKDTKPELEIDVKVQKQEEDVNVRKRPRMDIETNDTFSDEAVPESSKISQENEIGKKRELKEDSLWSAKEISNNDKLQDDSEMLPKKLLLTEFRSLVIKNSTSRNPSGINDDYGQLKNFKKFKKVTYPGAGKLPHIIGGSDLIAHHARKNTELEEWLRQEMEVQNQHAKEESLADDLFRYNPYLKRRR DIP protein O60934 original sequence version: 65 DIP protein O60934 original sequence version: 84 DIP protein O60934 original sequence version: 96 DIP protein O60934 original sequence version: 131 DIP protein O60934 original sequence version: 133 DIP protein O60934 original sequence version: 128 DIP protein O60934 original sequence version: 99 DIP protein O60934 original sequence version: 85 CD602F09BA73DAB6 rad50_human DNA repair protein RAD50 RAD50 protein protein human Homo sapiens Human MSRIEKMSILGVRSFGIEDKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQIRLQFRDVNGELIAVQRSMVCTQKSKKTEFKTLEGVITRTKHGEKVSLSSKCAEIDREMISSLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGFERGPFSERQIKNFHKLVRERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKDIENYIQDGKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSEYVEKFYRIKKNIDQCSEIVKCSVSSLGFNVH 1F208C3817FC41FC 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 mre11_human Double-strand break repair protein MRE11 MRE11 Double-strand break repair protein MRE11A HNGS1 MRE11A Meiotic recombination 11 homolog 1 Meiotic recombination 11 homolog A protein protein human Homo sapiens Human MSTADALDDENTFKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKYCMGDRPVQFEILSDQSVNFGFSKFPWVNYQDGNLNISIPVFSIHGNHDDPTGADALCALDILSCAGFVNHFGRSMSVEKIDISPVLLQKGSTKIALYGLGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDLVIWGHEHECKIAPTKNEQQLFYISQPGSSVVTSLSPGEAVKKHVGLLRIKGRKMNMHKIPLHTVRQFFMEDIVLANHPDIFNPDNPKVTQAIQSFCLEKIEEMLENAERERLGNSHQPEKPLVRLRVDYSGGFEPFSVLRFSQKFVDRVANPKDIIHFFRHREQKEKTGEEINFGKLITKPSEGTTLRVEDLVKQYFQTAEKNVQLSLLTERGMGEAVQEFVDKEEKDAIEELVKYQLEKTQRFLKERHIDALEDKIDEEVRRFRETRQKNTNEEDDEVREAMTRARALRSQSEESASAFSADDLMSIDLAEQMANDSDDSISAATNKGRGRGRGRRGGRGQNSASRGGSQRGRADTGLETSTRSRNSKTAVSASRNMSIIDAFKSTRQQPSRNVTTKNYSEVIEVDESDVEEDIFPTTSKTDQRWSSTSSSKIMSQSQVSKGVDFESSEDDDDDPFMNTSSLRRNRR DIP protein P49959 original sequence version: 152 DIP protein P49959 original sequence version: 146 DIP protein P49959 original sequence version: 114 DIP protein P49959 original sequence version: 161 DIP protein P49959 original sequence version: 168 DIP protein P49959 original sequence version: 173 DIP protein P49959 original sequence version: 154 DIP protein P49959-1 original sequence version: 127 DIP protein P49959 original sequence version: 96 DIP protein P49959 original sequence version: 115 D94ABFBDDF6106AD parp1_human Poly [ADP-ribose] polymerase 1 PARP1 ADPRT PPOL NAD(+) ADP-ribosyltransferase 1 Poly[ADP-ribose] synthase 1 ADP-ribosyltransferase diphtheria toxin-like 1 DNA ADP-ribosyltransferase PARP1 Protein poly-ADP-ribosyltransferase PARP1 protein protein human Homo sapiens Human MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW DIP protein P09874 original sequence version: 189 DIP protein P09874 original sequence version: 183 DIP protein P09874 original sequence version: 166 DIP protein P09874 original sequence version: 117 DIP protein P09874 original sequence version: 143 DIP protein P09874 original sequence version: 136 DIP protein P09874 original sequence version: 137 DIP protein P09874 original sequence version: 147 DIP protein P09874 original sequence version: 193 DIP protein P09874 original sequence version: 202 DIP protein P09874 original sequence version: 171 DIP protein P09874 original sequence version: 153 DIP protein P09874 original sequence version: 175 6A5FC01EB91C046B h2afx-mdc1-1 6 11 unspecified role unspecified role bait bait region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain required phosphoser-140 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain Phosphorylation of ser140. chemical synthesis Chemical synthesis (Chemical synthesis) 9 unspecified role unspecified role prey prey human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 8 unspecified role unspecified role prey prey human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 10 unspecified role unspecified role prey prey human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 13 unspecified role unspecified role prey prey human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 12 unspecified role unspecified role prey prey human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 association association Fig. 1a h2afx-mdc1-2 2 11 unspecified role unspecified role bait bait region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain required phosphoser-140 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain Phosphorylation of ser140. chemical synthesis Chemical synthesis (Chemical synthesis) 8 unspecified role unspecified role prey prey human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 10 unspecified role unspecified role prey prey human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 9 unspecified role unspecified role prey prey human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 12 unspecified role unspecified role prey prey human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 association association Fig. 1b h2afx-mdc1-3 7 11 unspecified role unspecified role bait bait c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined required phosphoser-140 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain Phosphorylation of ser140. chemical synthesis Chemical synthesis (Chemical synthesis) 8 unspecified role unspecified role prey prey region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined brct domain required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 35 40 direct interaction direct interaction Fig. 1c h2afx-mdc1-4 4 8 unspecified role unspecified role prey prey brct domain required to bind necessary binding region required to bind deletion analysis deletion analysis range range range range n-terminus gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. 11 unspecified role unspecified role bait bait required phosphoser-140 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain Phosphorylation of ser140. c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined chemical synthesis Chemical synthesis (Chemical synthesis) 47 43 physical association physical association Fig. 1d mdc1-h2afx-6 3 11 unspecified role unspecified role prey prey P16104:p.Tyr143Ala mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y A Wed May 02 17:04:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr143ala' Tue Jun 30 17:23:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr143Ala' required phosphoser-140 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain Phosphorylation of ser140. P16104:p.Tyr143Leu mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y L Wed May 02 20:10:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr143leu' Tue Jun 30 16:28:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr143Leu' lig_brct_mdc1_1 motif sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 8 unspecified role unspecified role bait bait Q14676:p.Lys1936Met mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K M Wed May 02 14:27:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys1936met' Tue Jun 30 16:56:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys1936Met' brct domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) 54 57 direct interaction direct interaction Fig. 1e, Table 1 Temp = 20C H2AX peptide (residues 128-143) phosphorylated at ser140 binds with Kd = 2.3 x 10e-6 molar. A shorter H2AX peptide (residues 134-143) phosphorylated at ser140 binds with Kd = 2.2 x 10e-6 molar. H2AX peptide (residues 134-143) phosphorylated at thr137 and ser140 binds with Kd = 2.0 x 10e-6 molar. The addition of two extra ala residues to the C-terminal of the H2AX peptide (residues 134-143) disrupts binding (Kd > 500 x 10e-6 molar). The lys1936met mutation in MDC1 decreases binding of H2AX peptide (residues 134-143) phosphorylated at ser140 to Kd = 90 x 10e-6 molar. h2afx-mdc1-5 5 8 unspecified role unspecified role neutral component neutral component brct domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain selenomet-2014_2029_2086 se(s)met L-selenomethionine Delta:S(-1)Se(1) Se(S)Met Selenium replaces sulphur semetm certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) 11 unspecified role unspecified role neutral component neutral component required phosphoser-140 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain Phosphorylation of ser140. possible phosphothr-137 opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt certain certain sequence position certain certain certain sequence position certain lig_brct_mdc1_1 motif required to bind necessary binding region required to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 60 65 direct interaction direct interaction Suppl. Table S1 2.4A working 19.0%, free 24.9% h2afx-mdc1-6 2 11 unspecified role unspecified role bait bait c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain required phosphoser-140 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain Phosphorylation of ser140. region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined chemical synthesis Chemical synthesis (Chemical synthesis) 8 unspecified role unspecified role prey prey brct domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q14676:p.Thr1898Val mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain T V Wed May 02 18:11:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr1898val' Tue Jun 30 19:09:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr1898Val' region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q14676:p.Arg1933Gln mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R Q Wed May 02 19:38:18 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg1933gln' Tue Jun 30 19:55:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg1933Gln' Q14676:p.Lys1936Met mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K M Wed May 02 19:23:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys1936met' Tue Jun 30 16:55:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys1936Met' ecolx Escherichia coli 72 68 direct interaction direct interaction Fig. 4a h2afx-mdc1-7 2 8 unspecified role unspecified role prey prey human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 11 unspecified role unspecified role bait bait required phosphoser-140 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain Phosphorylation of ser140. region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 8 competitor competitor competitor prey prey Q14676:p.Lys1936Met mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K M Wed May 02 15:38:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys1936met' Tue Jun 30 15:45:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys1936Met' brct domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli physical association physical association Fig. 4b h2afx-mdc1-8 1 8 unspecified role unspecified role neutral component neutral component region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q14676:p.Lys1936Met mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K M Wed May 02 19:16:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys1936met' Tue Jun 30 18:36:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys1936Met' brct domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 11 unspecified role unspecified role neutral component neutral component lig_brct_mdc1_1 motif sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain phosphoser-140 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 91 93 direct interaction direct interaction Fig. 6b