DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264734X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264733X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264732X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro peptide array peptide array predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264739X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264730X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264731X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro peptide array peptide array predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264735X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro peptide array peptide array predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264740X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro peptide array peptide array predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264741X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro peptide array peptide array predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264736X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro peptide array peptide array predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264737X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264729X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264727X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264728X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. Structure (London, England : 1993) 2015 imex curation Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. Only protein-protein interactions in vitro In vitro peptide array peptide array predetermined predetermined participant predetermined Tong Q., Cui G., Botuyan MV., Rothbart SB., Hayashi R., Musselman CA., Singh N., Appella E., Strahl BD., Mer G., Kutateladze TG. DIP original experiment: DIP-264738X Structure (London, England : 1993) 2015 IMEx Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. h4_human Histone H4 H4-16 H4C1 H4C11 H4C12 H4C13 H4C14 H4C15 H4C2 H4C3 H4C4 H4C5 H4C6 H4C8 H4C9 H4/A H4/B H4/C H4/D H4/E H4/G H4/H H4/I H4/J H4/K H4/M H4/N H4/O H4F2 H4FA H4FB H4FC H4FD H4FE H4FG H4FH H4FI H4FJ H4FK H4FM H4FN H4FO HIST1H4A HIST1H4B HIST1H4C HIST1H4D HIST1H4E HIST1H4F HIST1H4H HIST1H4I HIST1H4J HIST1H4K HIST1H4L HIST2H4 HIST2H4A HIST2H4B HIST4H4 protein protein human Homo sapiens Human MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG DIP protein P62805 original sequence version: 68 DIP protein P62805 original sequence version: 111 DIP protein P62805 original sequence version: 94 DIP protein P62805 original sequence version: 97 DIP protein P62805 original sequence version: 116 DIP protein P62805 original sequence version: 105 DIP protein P62805 original sequence version: 120 DIP protein P62805 original sequence version: 144 DIP protein P62805 original sequence version: 150 DIP protein P62805 original sequence version: 154 DIP protein P62805 original sequence version: 156 DIP protein P62805 original sequence version: 112 DIP protein P62805 original sequence version: 121 DIP protein P62805 original sequence version: 123 DIP protein P62805 original sequence version: 126 DIP protein P62805 original sequence version: 132 DIP protein P62805 original sequence version: 136 DIP protein P62805 original sequence version: 119 A9E5DFD3F8B97598 p53_human Cellular tumor antigen p53 TP53 P53 Tumor suppressor p53 Phosphoprotein p53 Antigen NY-CO-13 protein protein human Homo sapiens Human MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD DIP protein P04637 original sequence version: 121 DIP protein P04637 original sequence version: 115 DIP protein P04637-1 original sequence version: 224 DIP protein P04637 original sequence version: 117 DIP protein P04637-1 original sequence version: 226 DIP protein P04637 original sequence version: 226 DIP protein P04637 original sequence version: 212 DIP protein P04637 original sequence version: 220 DIP protein P04637-1 original sequence version: 220 DIP protein P04637-1 original sequence version: 145 DIP protein P04637 original sequence version: 146 DIP protein P04637 original sequence version: 145 DIP protein P04637 original sequence version: 166 DIP protein P04637-1 original sequence version: 166 DIP protein P04637 original sequence version: 169 DIP protein P04637 original sequence version: 177 DIP protein P04637 original sequence version: 175 DIP protein P04637-1 original sequence version: 175 DIP protein P04637-1 original sequence version: 172 DIP protein P04637-1 original sequence version: 169 DIP protein P04637 original sequence version: 170 DIP protein P04637 original sequence version: 172 DIP protein P04637-1 original sequence version: 194 DIP protein P04637 original sequence version: 196 DIP protein P04637 original sequence version: 185 DIP protein P04637-1 original sequence version: 191 DIP protein P04637 original sequence version: 191 DIP protein P04637 original sequence version: 180 DIP protein P04637-1 original sequence version: 197 DIP protein P04637 original sequence version: 183 DIP protein P04637-1 original sequence version: 183 DIP protein P04637-1 original sequence version: 185 DIP protein P04637 original sequence version: 199 DIP protein P04637 original sequence version: 201 DIP protein P04637 original sequence version: 189 DIP protein P04637 original sequence version: 235 DIP protein P04637 original sequence version: 230 DIP protein P04637 original sequence version: 234 DIP protein P04637-1 original sequence version: 234 DIP protein P04637-1 original sequence version: 235 DIP protein P04637 original sequence version: 239 DIP protein P04637-1 original sequence version: 212 DIP protein P04637-1 original sequence version: 213 DIP protein P04637 original sequence version: 213 DIP protein P04637 original sequence version: 206 DIP protein P04637-1 original sequence version: 188 DIP protein P04637-1 original sequence version: 228 DIP protein P04637 original sequence version: 208 DIP protein P04637 original sequence version: 240 DIP protein P04637-1 original sequence version: 240 DIP protein P04637 original sequence version: 204 DIP protein P04637-1 original sequence version: 204 DIP protein P04637-1 original sequence version: 209 DIP protein P04637-1 original sequence version: 203 DIP protein P04637 original sequence version: 221 DIP protein P04637-1 original sequence version: 152 DIP protein P04637 original sequence version: 217 DIP protein P04637-1 original sequence version: 140 DIP protein P04637 original sequence version: 215 DIP protein P04637 original sequence version: 214 DIP protein P04637-1 original sequence version: 182 DIP protein P04637 original sequence version: 182 DIP protein P04637 original sequence version: 188 DIP protein P04637 original sequence version: 192 DIP protein P04637-1 original sequence version: 192 DIP protein P04637 original sequence version: 218 DIP protein P04637-1 original sequence version: 218 AD5C149FD8106131 h3tail H3 tail peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ARTKQTARKSTGGKAPRKQL q12888-1 TP53-binding protein 1 TP53BP1 protein protein human Homo sapiens Human MDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEDDSGSHFSMLSRHLPNLQTHKENPVLDVVSNPEQTAGEERGDGNSGFNEHLKENKVADPVDSSNLDTCGSISQVIEQLPQPNRTSSVLGMSVESAPAVEEEKGEELEQKEKEKEEDTSGNTTHSLGAEDTASSQLGFGVLELSQSQDVEENTVPYEVDKEQLQSVTTNSGYTRLSDVDANTAIKHEEQSNEDIPIAEQSSKDIPVTAQPSKDVHVVKEQNPPPARSEDMPFSPKASVAAMEAKEQLSAQELMESGLQIQKSPEPEVLSTQEDLFDQSNKTVSSDGCSTPSREEGGCSLASTPATTLHLLQLSGQRSLVQDSLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQEGRQDKPMDTSVLSEEGGEPFQKKLQSGEPVELENPPLLPESTVSPQASTPISQSTPVFPPGSLPIPSQPQFSHDIFIPSPSLEEQSNDGKKDGDMHSSSLTVECSKTSEIEPKNSPEDLGLSLTGDSCKLMLSTSEYSQSPKMESLSSHRIDEDGENTQIEDTEPMSPVLNSKFVPAENDSILMNPAQDGEVQLSQNDDKTKGDDTDTRDDISILATGCKGREETVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMEIKEHHPEEGSSGSEVEEIPETPCESQGEELKEENMESVPLHLSLTETQSQGLCLQKEMPKKECSEAMEVETSVISIDSPQKLAILDQELEHKEQEAWEEATSEDSSVVIVDVKEPSPRVDVSCEPLEGVEKCSDSQSWEDIAPEIEPCAENRLDTKEEKSVEYEGDLKSGTAETEPVEQDSSQPSLPLVRADDPLRLDQELQQPQTQEKTSNSLTEDSKMANAKQLSSDAEAQKLGKPSAHASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVMSESMVETHDPILGSGKGDSGAAPDVDDKLCLRMKLVSPETEASEESLQFNLEKPATGERKNGSTAVAESVASPQKTMSVLSCICEARQENEARSEDPPTTPIRGNLLHFPSSQGEEEKEKLEGDHTIRQSQQPMKPISPVKDPVSPASQKMVIQGPSSPQGEAMVTDVLEDQKEGRSTNKENPSKALIERPSQNNIGIQTMECSLRVPETVSAATQTIKNVCEQGTSTVDQNFGKQDATVQTERGSGEKPVSAPGDDTESLHSQGEEEFDMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSLHRTSSGTSLSAMHSSGSSGKGAGPLRGKTSGTEPADFALPSSRGGPGKLSPRKGVSQTGTPVCEEDGDAGLGIRQGGKAPVTPRGRGRRGRPPSRTTGTRETAVPGPLGIEDISPNLSPDDKSFSRVVPRVPDSTRRTDVGAGALRRSDSPEIPFQAAAGPSDGLDASSPGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLVEGKRKRRSNVSSPATPTASSSSSTTPTRKITESPRASMGVLSGKRKLITSEEERSPAKRGRKSATVKPGAVGAGEFVSPCESGDNTGEPSALEEQRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLPDGPTGSSEEEEEFLEIPPFNKQYTESQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH DIP protein Q12888-1 original sequence version: 117 DIP protein Q12888-1 original sequence version: 110 DIP protein Q12888-1 original sequence version: 149 DIP protein Q12888-1 original sequence version: 147 DIP protein Q12888-1 original sequence version: 164 mint 13E2CC8A265F9D2A h3(7484) Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) IAQDFKTDLRF h3(2745) Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) KSAPSTGGVKKPHRYKPGT h3(1534) Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) APRKQLATKAARKSAPSTGG h2b(124) Histone 2B peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) PEPAKSAPAPKKGSKKAVTKAQKK h3(7484)-tp53bp1-1 9 19 unspecified role unspecified role prey prey Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag 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 20 unspecified role unspecified role bait bait K5me2 K5me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain Biotin-tag Biotin-tag biotin tag biotin tag c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal in vitro In vitro direct interaction direct interaction tp53-tp53bp1-5 13 19 unspecified role unspecified role unspecified role unspecified role Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 363-377 Region 363-377 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K370me2 K370me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction h3(2745)-tp53bp1-1 1 19 unspecified role unspecified role unspecified role unspecified role Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 21 unspecified role unspecified role unspecified role unspecified role K10me2 K10me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction tp53-tp53bp1-6 6 19 unspecified role unspecified role unspecified role unspecified role Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 366-386 Region 366-386 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K370K382me2 K370K382me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction tp53-tp53bp1-7 14 19 unspecified role unspecified role unspecified role unspecified role Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 363-377 Region 363-377 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K370me2 K370me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction tp53-tp53bp1-8 3 19 unspecified role unspecified role unspecified role unspecified role Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 366-386 Region 366-386 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K370K382me2 K370K382me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction tp53-tp53bp1-9 7 19 unspecified role unspecified role prey prey Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag 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 17 unspecified role unspecified role bait bait Region 366-390 Region 366-390 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K370me2 K370me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain Biotin-tag Biotin-tag biotin tag biotin tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range K382me2 K382me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction h3(120)-tp53bp1-1 15 19 unspecified role unspecified role prey prey Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag 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 18 unspecified role unspecified role bait bait K4me2 K4me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain K9me2 K9me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain K18me2 K18me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain Biotin-tag Biotin-tag biotin tag biotin tag c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal in vitro In vitro direct interaction direct interaction hist1h4a-tp53bp1-9 10 19 unspecified role unspecified role prey prey Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag 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 16 unspecified role unspecified role bait bait Region 12-28 Region 12-28 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K21me2 K21me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain Biotin-tag Biotin-tag biotin tag biotin tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range in vitro In vitro direct interaction direct interaction tp53-tp53bp1-10 12 19 unspecified role unspecified role unspecified role unspecified role Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 376-387 Region 376-387 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K382me2 K382me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction h3(1534)-tp53bp1-1 4 19 unspecified role unspecified role prey prey Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag 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 22 unspecified role unspecified role bait bait K13me2 K13me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain Biotin-tag Biotin-tag biotin tag biotin tag c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal ecolx Escherichia coli direct interaction direct interaction tp53-tp53bp1-11 2 19 unspecified role unspecified role unspecified role unspecified role Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 376-387 Region 376-387 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K382me2 K382me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction h3(2745)-tp53bp1-2 8 19 unspecified role unspecified role prey prey Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag 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 21 unspecified role unspecified role bait bait K10me2 K10me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain Biotin-tag Biotin-tag biotin tag biotin tag c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal in vitro In vitro direct interaction direct interaction h2b(124)-tp53bp1-1 11 19 unspecified role unspecified role prey prey Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag 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 23 unspecified role unspecified role bait bait K5me2 K5me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain Biotin-tag Biotin-tag biotin tag biotin tag c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal in vitro In vitro direct interaction direct interaction tp53-tp53bp1-12 5 19 unspecified role unspecified role unspecified role unspecified role Region 1484-1603 Region 1484-1603 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 376-387 Region 376-387 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain K382me2 K382me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction