DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ tong-2015-16 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Tong Q., Mazur SJ., Rincon-Arano H., Rothbart SB., Kuznetsov DM., Cui G., Liu WH., Gete Y., Klein BJ., Jenkins L., Mer G., Kutateladze AG., Strahl BD., Groudine M., Appella E., Kutateladze TG. DIP original experiment: DIP-264780X Structure (London, England : 1993) 2015 IMEx An acetyl-methyl switch drives a conformational change in p53. Tong Q., Mazur SJ., Rincon-Arano H., Rothbart SB., Kuznetsov DM., Cui G., Liu WH., Gete Y., Klein BJ., Jenkins L., Mer G., Kutateladze AG., Strahl BD., Groudine M., Appella E., Kutateladze TG. Only protein-protein interactions imex curation tong-2015-17 in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Tong Q., Mazur SJ., Rincon-Arano H., Rothbart SB., Kuznetsov DM., Cui G., Liu WH., Gete Y., Klein BJ., Jenkins L., Mer G., Kutateladze AG., Strahl BD., Groudine M., Appella E., Kutateladze TG. DIP original experiment: DIP-264776X Structure (London, England : 1993) 2015 IMEx An acetyl-methyl switch drives a conformational change in p53. Tong Q., Mazur SJ., Rincon-Arano H., Rothbart SB., Kuznetsov DM., Cui G., Liu WH., Gete Y., Klein BJ., Jenkins L., Mer G., Kutateladze AG., Strahl BD., Groudine M., Appella E., Kutateladze TG. Only protein-protein interactions imex curation tong-2015-18 in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Tong Q., Mazur SJ., Rincon-Arano H., Rothbart SB., Kuznetsov DM., Cui G., Liu WH., Gete Y., Klein BJ., Jenkins L., Mer G., Kutateladze AG., Strahl BD., Groudine M., Appella E., Kutateladze TG. DIP original experiment: DIP-264778X Structure (London, England : 1993) 2015 IMEx An acetyl-methyl switch drives a conformational change in p53. Tong Q., Mazur SJ., Rincon-Arano H., Rothbart SB., Kuznetsov DM., Cui G., Liu WH., Gete Y., Klein BJ., Jenkins L., Mer G., Kutateladze AG., Strahl BD., Groudine M., Appella E., Kutateladze TG. Only protein-protein interactions imex curation tong-2015-19 in vitro In vitro peptide array peptide array predetermined predetermined participant predetermined Tong Q., Mazur SJ., Rincon-Arano H., Rothbart SB., Kuznetsov DM., Cui G., Liu WH., Gete Y., Klein BJ., Jenkins L., Mer G., Kutateladze AG., Strahl BD., Groudine M., Appella E., Kutateladze TG. DIP original experiment: DIP-264779X Structure (London, England : 1993) 2015 IMEx An acetyl-methyl switch drives a conformational change in p53. Tong Q., Mazur SJ., Rincon-Arano H., Rothbart SB., Kuznetsov DM., Cui G., Liu WH., Gete Y., Klein BJ., Jenkins L., Mer G., Kutateladze AG., Strahl BD., Groudine M., Appella E., Kutateladze TG. Only protein-protein interactions imex curation tong-2015-20 in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Tong Q., Mazur SJ., Rincon-Arano H., Rothbart SB., Kuznetsov DM., Cui G., Liu WH., Gete Y., Klein BJ., Jenkins L., Mer G., Kutateladze AG., Strahl BD., Groudine M., Appella E., Kutateladze TG. DIP original experiment: DIP-264777X Structure (London, England : 1993) 2015 IMEx An acetyl-methyl switch drives a conformational change in p53. Tong Q., Mazur SJ., Rincon-Arano H., Rothbart SB., Kuznetsov DM., Cui G., Liu WH., Gete Y., Klein BJ., Jenkins L., Mer G., Kutateladze AG., Strahl BD., Groudine M., Appella E., Kutateladze TG. Only protein-protein interactions imex curation tong-2015-21 in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Tong Q., Mazur SJ., Rincon-Arano H., Rothbart SB., Kuznetsov DM., Cui G., Liu WH., Gete Y., Klein BJ., Jenkins L., Mer G., Kutateladze AG., Strahl BD., Groudine M., Appella E., Kutateladze TG. DIP original experiment: DIP-264781X Structure (London, England : 1993) 2015 IMEx An acetyl-methyl switch drives a conformational change in p53. Tong Q., Mazur SJ., Rincon-Arano H., Rothbart SB., Kuznetsov DM., Cui G., Liu WH., Gete Y., Klein BJ., Jenkins L., Mer G., Kutateladze AG., Strahl BD., Groudine M., Appella E., Kutateladze TG. Only protein-protein interactions imex curation q12888-1 TP53-binding protein 1 TP53BP1 protein protein human Homo sapiens Human MDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEDDSGSHFSMLSRHLPNLQTHKENPVLDVVSNPEQTAGEERGDGNSGFNEHLKENKVADPVDSSNLDTCGSISQVIEQLPQPNRTSSVLGMSVESAPAVEEEKGEELEQKEKEKEEDTSGNTTHSLGAEDTASSQLGFGVLELSQSQDVEENTVPYEVDKEQLQSVTTNSGYTRLSDVDANTAIKHEEQSNEDIPIAEQSSKDIPVTAQPSKDVHVVKEQNPPPARSEDMPFSPKASVAAMEAKEQLSAQELMESGLQIQKSPEPEVLSTQEDLFDQSNKTVSSDGCSTPSREEGGCSLASTPATTLHLLQLSGQRSLVQDSLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQEGRQDKPMDTSVLSEEGGEPFQKKLQSGEPVELENPPLLPESTVSPQASTPISQSTPVFPPGSLPIPSQPQFSHDIFIPSPSLEEQSNDGKKDGDMHSSSLTVECSKTSEIEPKNSPEDLGLSLTGDSCKLMLSTSEYSQSPKMESLSSHRIDEDGENTQIEDTEPMSPVLNSKFVPAENDSILMNPAQDGEVQLSQNDDKTKGDDTDTRDDISILATGCKGREETVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMEIKEHHPEEGSSGSEVEEIPETPCESQGEELKEENMESVPLHLSLTETQSQGLCLQKEMPKKECSEAMEVETSVISIDSPQKLAILDQELEHKEQEAWEEATSEDSSVVIVDVKEPSPRVDVSCEPLEGVEKCSDSQSWEDIAPEIEPCAENRLDTKEEKSVEYEGDLKSGTAETEPVEQDSSQPSLPLVRADDPLRLDQELQQPQTQEKTSNSLTEDSKMANAKQLSSDAEAQKLGKPSAHASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVMSESMVETHDPILGSGKGDSGAAPDVDDKLCLRMKLVSPETEASEESLQFNLEKPATGERKNGSTAVAESVASPQKTMSVLSCICEARQENEARSEDPPTTPIRGNLLHFPSSQGEEEKEKLEGDHTIRQSQQPMKPISPVKDPVSPASQKMVIQGPSSPQGEAMVTDVLEDQKEGRSTNKENPSKALIERPSQNNIGIQTMECSLRVPETVSAATQTIKNVCEQGTSTVDQNFGKQDATVQTERGSGEKPVSAPGDDTESLHSQGEEEFDMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSLHRTSSGTSLSAMHSSGSSGKGAGPLRGKTSGTEPADFALPSSRGGPGKLSPRKGVSQTGTPVCEEDGDAGLGIRQGGKAPVTPRGRGRRGRPPSRTTGTRETAVPGPLGIEDISPNLSPDDKSFSRVVPRVPDSTRRTDVGAGALRRSDSPEIPFQAAAGPSDGLDASSPGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLVEGKRKRRSNVSSPATPTASSSSSTTPTRKITESPRASMGVLSGKRKLITSEEERSPAKRGRKSATVKPGAVGAGEFVSPCESGDNTGEPSALEEQRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLPDGPTGSSEEEEEFLEIPPFNKQYTESQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH mint p53_human Cellular tumor antigen p53 TP53 P53 Tumor suppressor p53 Phosphoprotein p53 Antigen NY-CO-13 protein protein human Homo sapiens Human MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD ep300_human Histone acetyltransferase p300 Histone butyryltransferase p300 Histone crotonyltransferase p300 Protein propionyltransferase p300 EP300 P300 E1A-associated protein p300 Protein 2-hydroxyisobutyryltransferase p300 Protein lactyltransferas p300 protein protein human Homo sapiens Human MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDINQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMPNMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQMPTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQNPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSMAQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTPTPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPSLPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSSTEVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELKTEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHLEPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNSDLNSNLSQSTLDIH 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 tp53-tp53bp1-13 3274974 N/A 3274980 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 false ecolx Escherichia coli N/A 3274981 unspecified role unspecified role unspecified role unspecified role Region 377-386 Region 377-386 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false K381ac K381ac naclys N-acetylated L-lysine NAcLys certain certain sequence position certain certain certain sequence position certain false 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 false in vitro In vitro direct interaction direct interaction false false false ep300-tp53-15 3274975 N/A 3274982 unspecified role unspecified role unspecified role unspecified role Region 1040-1161 Region 1040-1161 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3274981 unspecified role unspecified role unspecified role unspecified role Region 377-386 Region 377-386 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false K381ac K381ac naclys N-acetylated L-lysine NAcLys certain certain sequence position certain certain certain sequence position certain false in vitro In vitro direct interaction direct interaction false false false tp53-tp53bp1-14 3274976 N/A 3274980 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 false Q12888-1:p.Tyr1500Ala Y1500A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain false Q12888-1:p.Tyr1502Ala Y1502A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain false Q12888-1:p.Asp1521Ala D1521A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain false Q12888-1:p.Asp1521Tyr D1521Y mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain false Q12888-1:p.Phe1553Ala F1553A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain false Q12888-1:p.[Tyr1500Ala;Phe1553Ala] Y1500A/F1553A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3274981 unspecified role unspecified role unspecified role unspecified role Region 377-386 Region 377-386 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false K381ac K381ac naclys N-acetylated L-lysine NAcLys certain certain sequence position certain certain certain sequence position certain false 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 false in vitro In vitro direct interaction direct interaction false false false tp53-tp53bp1-15 3274977 N/A 3274980 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 false 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 false ecolx Escherichia coli N/A 3274981 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 false 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 false 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 false K381ac K381ac naclys N-acetylated L-lysine NAcLys certain certain sequence position certain certain certain sequence position certain false K386ac K386ac naclys N-acetylated L-lysine NAcLys certain certain sequence position certain certain certain sequence position certain false pS378 pS378 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 false pT377 pT377 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 false in vitro In vitro direct interaction direct interaction false false false tp53-tp53bp1-16 3274978 N/A 3274980 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 false ecolx Escherichia coli N/A 3274981 unspecified role unspecified role unspecified role unspecified role Region 377-386 Region 377-386 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false K381ac K381ac naclys N-acetylated L-lysine NAcLys certain certain sequence position certain certain certain sequence position certain false 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 false in vitro In vitro direct interaction direct interaction false false false hist1h4a-tp53bp1-10 3274979 N/A 3274980 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 false ecolx Escherichia coli N/A 3274983 unspecified role unspecified role unspecified role unspecified role Region 15-28 Region 15-28 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false 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 false in vitro In vitro direct interaction direct interaction false false false