DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Burge S., Teufel DP., Townsley FM., Freund SM., Bycroft M., Fersht AR. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Burge S., Teufel DP., Townsley FM., Freund SM., Bycroft M., Fersht AR. DIP original experiment: DIP-133803X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Burge S., Teufel DP., Townsley FM., Freund SM., Bycroft M., Fersht AR. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Burge S., Teufel DP., Townsley FM., Freund SM., Bycroft M., Fersht AR. DIP original experiment: DIP-133805X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Burge S., Teufel DP., Townsley FM., Freund SM., Bycroft M., Fersht AR. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Burge S., Teufel DP., Townsley FM., Freund SM., Bycroft M., Fersht AR. DIP original experiment: DIP-133806X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Burge S., Teufel DP., Townsley FM., Freund SM., Bycroft M., Fersht AR. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Burge S., Teufel DP., Townsley FM., Freund SM., Bycroft M., Fersht AR. DIP original experiment: DIP-133804X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Burge S., Teufel DP., Townsley FM., Freund SM., Bycroft M., Fersht AR. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Burge S., Teufel DP., Townsley FM., Freund SM., Bycroft M., Fersht AR. DIP original experiment: DIP-217299X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Burge S., Teufel DP., Townsley FM., Freund SM., Bycroft M., Fersht AR. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Burge S., Teufel DP., Townsley FM., Freund SM., Bycroft M., Fersht AR. DIP original experiment: DIP-217298X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. 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 DIP protein Q09472 original sequence version: 193 DIP protein Q09472 original sequence version: 186 DIP protein Q09472 original sequence version: 107 DIP protein Q09472 original sequence version: 112 DIP protein Q09472 original sequence version: 181 DIP protein Q09472 original sequence version: 183 DIP protein Q09472 original sequence version: 136 DIP protein Q09472 original sequence version: 146 DIP protein Q09472 original sequence version: 165 DIP protein Q09472 original sequence version: 192 DIP protein Q09472 original sequence version: 200 DIP protein Q09472 original sequence version: 206 DIP protein Q09472 original sequence version: 194 DIP protein Q09472 original sequence version: 171 DIP protein Q09472 original sequence version: 142 DIP protein Q09472 original sequence version: 180 8E869E1F174A6FEB 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 DIP protein Q00987 original sequence version: 93 DIP protein Q00987-1 original sequence version: 192 DIP protein Q00987 original sequence version: 88 DIP protein Q00987 original sequence version: 180 DIP protein Q00987 original sequence version: 188 DIP protein Q00987 original sequence version: 189 DIP protein Q00987 original sequence version: 115 DIP protein Q00987-1 original sequence version: null DIP protein Q00987 original sequence version: 149 DIP protein Q00987 original sequence version: 146 DIP protein Q00987 original sequence version: 140 DIP protein Q00987 original sequence version: 183 DIP protein Q00987 original sequence version: 145 DIP protein Q00987 original sequence version: 182 DIP protein Q00987 original sequence version: 151 DIP protein Q00987 original sequence version: 156 DIP protein Q00987-1 original sequence version: 160 DIP protein Q00987 original sequence version: 160 DIP protein Q00987 original sequence version: 168 DIP protein Q00987 original sequence version: 186 DIP protein Q00987 original sequence version: 206 F37CE163876BC983 p73_human Tumor protein p73 TP73 P73 p53-like transcription factor p53-related protein protein protein human Homo sapiens Human MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSAKNGAASKRAFKQSPPAVPALGAGVKKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSSAATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGFDLPDCKARKQPIKEEFTEAEIH DIP protein O15350 original sequence version: 170 DIP protein O15350-1 original sequence version: 100 DIP protein O15350 original sequence version: 123 DIP protein O15350 original sequence version: 149 DIP protein O15350-1 original sequence version: 165 DIP protein O15350 original sequence version: 92 DIP protein O15350-1 original sequence version: 122 DIP protein O15350-1 original sequence version: 135 DIP protein O15350-1 original sequence version: 174 A467493C5D93EEE0 ep300-tp73-1 1 7 unspecified role unspecified role unspecified role unspecified role Region 313-433 Region 313-433 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Region 1717-1815 Region 1717-1815 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Region 564-658 Region 564-658 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Region 2039-2141 Region 2039-2141 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 1-67 Region 1-67 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ep300-tp73-2 2 7 unspecified role unspecified role unspecified role unspecified role Region 1717-1815 Region 1717-1815 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 10-40 Region 10-40 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction mdm2-tp73-2 3 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 10-40 Region 10-40 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction mdm2-tp73-3 4 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 1-67 Region 1-67 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction mdm2-tp73-4 6 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 1-67 Region 1-67 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction 1 nodeMerge04 2011-10-21 mdm2-tp73-5 5 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 10-40 Region 10-40 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction 1 nodeMerge04 2011-10-21