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/ http://www.ebi.ac.uk/ tang-2008a-3 Acetylation is indispensable for p53 activation. human-h1299 Homo sapiens lung lymph node carcinoma h1299 Human lung lymph node carcinoma p53 null. These cells have also been reported to secrete the peptide hormone neuromedin B (NMB), but not gastrin releasing peptide (GRP). Also known as NCI H1299 or CRL-5803. http://www.lgcpromochem.com/atcc/ ATCC number: CRL-5803. ATCC number of the cell line is CRL-5803. ch-ip chromatin immunoprecipitation assay ch-ip primer specific pcr primer specific pcr Tang Y., Zhao W., Chen Y., Zhao Y., Gu W. Apoptosis - Interactions involving proteins with a function related to apoptosis Source of p53 taken from PMID: 17189186, ep300 from PMID: 17189186 and inferred by sequence length, CBP from PMID: 9194564 and inferred from sequence length. wg8@columbia.edu Cell (0092-8674) 2008 Only protein-protein interactions 7 imex curation Cancer - Interactions investigated in the context of cancer tang-2008a-1 Acetylation is indispensable for p53 activation. in vitro In vitro acetylase assay acetylase assay predetermined predetermined participant predetermined Tang Y., Zhao W., Chen Y., Zhao Y., Gu W. Apoptosis - Interactions involving proteins with a function related to apoptosis Source of p53 taken from PMID: 17189186, ep300 from PMID: 17189186 and inferred by sequence length, CBP from PMID: 9194564 and inferred from sequence length. wg8@columbia.edu Cell (0092-8674) 2008 Only protein-protein interactions 7 imex curation Cancer - Interactions investigated in the context of cancer tang-2008a-2 Acetylation is indispensable for p53 activation. in vitro In vitro emsa electrophoretic mobility shift assay Gel retardation assay band shift band shift Gel retardation assay emsa predetermined predetermined participant predetermined Tang Y., Zhao W., Chen Y., Zhao Y., Gu W. Apoptosis - Interactions involving proteins with a function related to apoptosis Source of p53 taken from PMID: 17189186, ep300 from PMID: 17189186 and inferred by sequence length, CBP from PMID: 9194564 and inferred from sequence length. wg8@columbia.edu Cell (0092-8674) 2008 Only protein-protein interactions 7 imex curation Cancer - Interactions investigated in the context of cancer tang-2008a-5 Acetylation is indispensable for p53 activation. in vitro In vitro pull down pull down weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Tang Y., Zhao W., Chen Y., Zhao Y., Gu W. Apoptosis - Interactions involving proteins with a function related to apoptosis Source of p53 taken from PMID: 17189186, ep300 from PMID: 17189186 and inferred by sequence length, CBP from PMID: 9194564 and inferred from sequence length. wg8@columbia.edu Cell (0092-8674) 2008 Only protein-protein interactions 7 imex curation Cancer - Interactions investigated in the context of cancer tang-2008a-8 Acetylation is indispensable for p53 activation. human-h1299 Homo sapiens lung lymph node carcinoma h1299 Human lung lymph node carcinoma p53 null. These cells have also been reported to secrete the peptide hormone neuromedin B (NMB), but not gastrin releasing peptide (GRP). Also known as NCI H1299 or CRL-5803. http://www.lgcpromochem.com/atcc/ ATCC number: CRL-5803. ATCC number of the cell line is CRL-5803. anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Tang Y., Zhao W., Chen Y., Zhao Y., Gu W. Apoptosis - Interactions involving proteins with a function related to apoptosis HA-tagged CREBBP identified using an anti-tag Ab Source of p53 taken from PMID: 17189186, ep300 from PMID: 17189186 and inferred by sequence length, CBP from PMID: 9194564 and inferred from sequence length. wg8@columbia.edu Cell (0092-8674) 2008 Only protein-protein interactions 7 imex curation Cancer - Interactions investigated in the context of cancer tang-2008a-4 Acetylation is indispensable for p53 activation. in vitro In vitro emsa supershift electrophoretic mobility supershift assay emsa supershift predetermined predetermined participant predetermined Tang Y., Zhao W., Chen Y., Zhao Y., Gu W. Apoptosis - Interactions involving proteins with a function related to apoptosis Source of p53 taken from PMID: 17189186, ep300 from PMID: 17189186 and inferred by sequence length, CBP from PMID: 9194564 and inferred from sequence length. wg8@columbia.edu Cell (0092-8674) 2008 Only protein-protein interactions 7 imex curation Cancer - Interactions investigated in the context of cancer tang-2008a-6 Acetylation is indispensable for p53 activation. in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Tang Y., Zhao W., Chen Y., Zhao Y., Gu W. Apoptosis - Interactions involving proteins with a function related to apoptosis Source of p53 taken from PMID: 17189186, ep300 from PMID: 17189186 and inferred by sequence length, CBP from PMID: 9194564 and inferred from sequence length. wg8@columbia.edu Cell (0092-8674) 2008 Only protein-protein interactions 7 imex curation Cancer - Interactions investigated in the context of cancer tang-2008a-7 Acetylation is indispensable for p53 activation. human-u2-os Human U2-OS osteosarcoma cell line u2-os U2-OS osteocaroma cell line Not in CAPRI and no primary literature reference ch-ip chromatin immunoprecipitation assay ch-ip primer specific pcr primer specific pcr Tang Y., Zhao W., Chen Y., Zhao Y., Gu W. Apoptosis - Interactions involving proteins with a function related to apoptosis Cells treated with actinomycin D (10 nM) for 0, 4, 8, 16, and 24 hrs. Source of p53 taken from PMID: 17189186, ep300 from PMID: 17189186 and inferred by sequence length, CBP from PMID: 9194564 and inferred from sequence length. wg8@columbia.edu Cell (0092-8674) 2008 Only protein-protein interactions 7 imex curation Cancer - Interactions investigated in the context of cancer p53_human Cellular tumor antigen p53 TP53 P53 Tumor suppressor p53 Phosphoprotein p53 Antigen NY-CO-13 protein protein human Homo sapiens Human MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD mdm2_human E3 ubiquitin-protein ligase Mdm2 MDM2 p53-binding protein Mdm2 Oncoprotein Mdm2 Double minute 2 protein RING-type E3 ubiquitin transferase Mdm2 protein protein human Homo sapiens Human MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP cdkn1a_human_gene Human CDKN1A gene gene gene human Homo sapiens Human cbp_mouse Histone lysine acetyltransferase CREBBP Crebbp Cbp Protein-lysine acetyltransferase CREBBP protein protein mouse Mus musculus Mouse MAENLLDGPPNPKRAKLSSPGFSANDNTDFGSLFDLENDLPDELIPNGELSLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSTNMASLGAMGKSPLNQGDSSTPNLPKQAASTSGPTPPASQALNPQAQKQVGLVTSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLMNQAQQGQAQVMNGSLGAAGRGRGAGMPYPAPAMQGATSSVLAETLTQVSPQMAGHAGLNTAQAGGMTKMGMTGTTSPFGQPFSQTGGQQMGATGVNPQLASKQSMVNSLPAFPTDIKNTSVTTVPNMSQLQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGAGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPPAHQQMRTLNALGNNPMSIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGSLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPGMAISPSRMPQPPNMMGTHANNIMAQAPTQNQFLPQNQFPSSSGAMSVNSVGMGQPAAQAGVSQGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPRSEMMEEDLQGSSQVKEETDTTEQKSEPMEVEEKKPEVKVEAKEEEENSSNDTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQNTALIAPHQIQGRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIINDYKDIFKQANEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETPEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVISTQPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVNMSPAGFPNVARTQPPTIVSAGKPTNQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRANINNGMPPGRAGMGTPGSQMTPVGLNVPRPNQVSGPVMSSMPPGQWQQAPIPQQQPMPGMPRPVMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPGHNPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNSASLAGGMAGHSQFQQPQGPGGYAPAMQQQRMQQHLPIQGSSMGQMAAPMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSMDQGHLGNPEQSAMLPQLNTPNRSALSSELSLVGDTTGDTLEKFVEGL kat5_human Histone acetyltransferase KAT5 KAT5 TIP60 HTATIP Lysine acetyltransferase 5 cPLA(2)-interacting protein Histone acetyltransferase HTATIP 60 kDa Tat-interactive protein protein protein human Homo sapiens Human MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTKNGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPKEREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPVPSETAPASVFPQNGAARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRHRLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQTILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDIVDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW tp53i3_human_gene Human TP53I3 gene gene gene human Homo sapiens Human mdm2_human_gene Human MDM2 gene gene gene human Homo sapiens Human zn363_human_gene Human RCHY1 gene gene gene human Homo sapiens Human 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 cdkn1a_human_p53bind Human CDKN1A gene - TP53 binding region dna deoxyribonucleic acid DNA deoxyribonucleic acid dna DNA deoxyribonucleic acid human Homo sapiens Human p53-mdm2-3 Binding of TP53 and MDM2 to the CDKN1A (p21) promoter 760690 N/A 760698 unspecified role unspecified role bait bait N/A 760699 unspecified role unspecified role prey prey N/A 760700 unspecified role unspecified role prey prey association association false false false P04637; Q00987 transfection Mdm2 was only present in the complex when K120, K164, K370, K372, K373, K381, K382, and K386 were all mutated to alanine, preventing acetylation suggesting that TP53 acetylation represses recruitment of MDM2 to the CDKN1A promoter. Mdm2 recruitment at the p21 promoter was strongly repressed upon treatment with the DNA-damaging reagent actinomycin D which correlated with the acetylation levels of wild-type p53 Fig. 4A, 4C, 6D p53-crebbp-8 Binding of TP53, CREBBP and HTATIP to the CDKN1A (p21) promoter 760690 N/A 760701 unspecified role unspecified role prey prey N/A 760702 unspecified role unspecified role prey prey N/A 760700 unspecified role unspecified role prey prey N/A 760698 unspecified role unspecified role bait bait association association false false false P04637; Q92993, P45481 transfection Fig. 4A, 4C p53-crebbp-9 Binding of TP53, CREBBP and HTATIP to the TP53IP (PIG3) promoter 760690 N/A 760699 unspecified role unspecified role prey prey N/A 760698 unspecified role unspecified role bait bait N/A 760701 unspecified role unspecified role prey prey N/A 760702 unspecified role unspecified role prey prey N/A 760703 unspecified role unspecified role prey prey association association false false false P04637; Q92993, P45481; Q00987 transfection Fig. 4C MDM4 (MDMX) was also observed to bid in this promoter complex but the source could not be identified. p53-crebbp-10 Binding of TP53 and CREBBP to the MDM2 promoter 760690 N/A 760699 unspecified role unspecified role prey prey N/A 760704 unspecified role unspecified role prey prey N/A-x-x-x 760698 unspecified role unspecified role bait bait N/A-x-x 760701 unspecified role unspecified role prey prey association association false false false P04637; P45481 transfection Fig. 4C, Supp. Fig. 9 Recruitment of MDM2 to the MDM2 promoteris fairly weak and requires further cycles of PCR to visualise. tp53-rchy1_gene Binding of TP53 and CREBBP to the RCHY1 (PIRH2) promoter 760690 N/A 760701 unspecified role unspecified role prey prey N/A 760698 unspecified role unspecified role bait bait region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false N/A 760705 unspecified role unspecified role prey prey association association false false false P04637; P45481 transfection Supp. Fig. 10B ep300-tp53-1 Acetylation of TP53 by EP300 760691 N/A 760698 enzyme target enzyme target substrate substrate neutral component neutral component region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false undefined mutation mutation mutation certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. N/A 760706 enzyme enzyme neutral component neutral component region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. acetylation acetylation reaction acetylation false false false Fig. 1D Acetylation of p53 on lys-164 crebbp-tp53-1 Acetylation of TP53 by CERBBP 760691 N/A 760701 enzyme enzyme neutral component neutral component human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. N/A 760698 enzyme target enzyme target substrate substrate neutral component neutral component region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false undefined mutation mutation mutation certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false P04637:p.Lys164Arg mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. acetylation acetylation reaction acetylation false false false Fig. 1D Acetylation of p53 on lys-164 p53-p21_promoter DNA binding properties of p53 760692 N/A 760700 unspecified role unspecified role bait bait promoter region sufficient to bind sufficient binding region sufficient to bind undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false N/A 760698 unspecified role unspecified role prey prey region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. direct interaction direct interaction false false false Fig. 2D P04637 transfection p53-p21_p53bind DNA binding properties of p53 760692 N/A 760698 unspecified role unspecified role prey prey region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. N/A 760699 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 false ecoli Escherichia coli (strain K12) N/A 760707 unspecified role unspecified role bait bait association association false false false Fig. 5B DNA is 32P-radiolabelled Q00987; P04637 transfection Use of the lys to arg mutant protein demonstracted that MDM2 bound preferably to the unaccetylated TP53 protein. In contrast, acetylated p53 bound DNA more strongly. mdm2-tp53-2 Interaction between MDM2 and TP53 demonstrated by pulldown 760693 N/A 760699 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false in vitro In vitro N/A 760698 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false 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 false dna binding region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false n-terminal sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false Fig. 5D mdm2-tp53-4 Interaction between MDM2 and TP53 demonstrated by pulldown 760693 N/A-x-x 760699 unspecified role unspecified role bait bait 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 false ecoli Escherichia coli (strain K12) N/A-x-x-x-x 760698 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false in vitro In vitro direct interaction direct interaction false false false Supp. Fig. 4 An interaction between MDM4 and TP53 was also demonstrated but the source of MDM4 could not be traced. tp53-crebbp Interaction between TP53 and CREBBP demonstrated by coimmunoprecipitation 760694 N/A 760701 unspecified role unspecified role prey prey region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false N/A 760698 unspecified role unspecified role bait bait region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false physical association physical association false false false Supp. Fig. 3A tp53-tip60-1 Interaction between TP53 and TIP60 demonstrated by coimmunoprecipitation 760694 N/A-x 760698 unspecified role unspecified role bait bait region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false N/A 760702 unspecified role unspecified role prey prey physical association physical association false false false Supp. Fig. 3A P04637; Q92993 transfection p53-p21_p53bind-1 DNA binding properties of p53 760695 N/A-x-x 760698 unspecified role unspecified role prey prey region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. N/A-x 760699 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 false ecoli Escherichia coli (strain K12) N/A-x 760707 unspecified role unspecified role bait bait association association false false false Fig. 5B DNA is 32P-radiolabelled Q00987; P04637 transfection The complex was supershifted by a p53-specific antibody or blocked by an Mdm2-specific antibody mdm2-tp53-3 Interaction between MDM2 and TP53 demonstrated by pulldown 760696 N/A 760698 unspecified role unspecified role prey prey human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. N/A 760699 unspecified role unspecified role bait bait 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 false ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false Fig. 5E Acetylation of TP53 inhibited this interaction An interaction between MDM4 and TP53 was also demonstrated but the source of MDM4 could not be traced. p53-mdm2-4 Binding of TP53 and MDM2 to the CDKN1A (p21) promoter 760697 N/A-x 760698 unspecified role unspecified role bait bait region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false N/A-x 760700 unspecified role unspecified role prey prey N/A-x 760699 unspecified role unspecified role prey prey association association false false false Increased TP53 acetylation due to DNA damage represses recruitment of MDM2 to the CDKN1A promoter. Fig. 6B