MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it The CH2 domain of CBP/p300 is a novel zinc finger. The CH2 domain of CBP/p300 is a novel zinc finger. FEBS Lett. (0014-5793) 2013 Park S., Martinez-Yamout MA., Dyson HJ., Wright PE. in vitro In vitro peptide array peptide array experimental particp experimental participant identification experimental particp Park S., Martinez-Yamout MA., Dyson HJ., Wright PE. FEBS Lett. (0014-5793) 2013 cbp_mouse Histone lysine acetyltransferase CREBBP Crebbp Cbp Protein-lysine acetyltransferase CREBBP protein protein mouse Mus musculus Mouse MAENLLDGPPNPKRAKLSSPGFSANDNTDFGSLFDLENDLPDELIPNGELSLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSTNMASLGAMGKSPLNQGDSSTPNLPKQAASTSGPTPPASQALNPQAQKQVGLVTSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLMNQAQQGQAQVMNGSLGAAGRGRGAGMPYPAPAMQGATSSVLAETLTQVSPQMAGHAGLNTAQAGGMTKMGMTGTTSPFGQPFSQTGGQQMGATGVNPQLASKQSMVNSLPAFPTDIKNTSVTTVPNMSQLQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGAGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPPAHQQMRTLNALGNNPMSIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGSLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPGMAISPSRMPQPPNMMGTHANNIMAQAPTQNQFLPQNQFPSSSGAMSVNSVGMGQPAAQAGVSQGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPRSEMMEEDLQGSSQVKEETDTTEQKSEPMEVEEKKPEVKVEAKEEEENSSNDTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQNTALIAPHQIQGRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIINDYKDIFKQANEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETPEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVISTQPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVNMSPAGFPNVARTQPPTIVSAGKPTNQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRANINNGMPPGRAGMGTPGSQMTPVGLNVPRPNQVSGPVMSSMPPGQWQQAPIPQQQPMPGMPRPVMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPGHNPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNSASLAGGMAGHSQFQQPQGPGGYAPAMQQQRMQQHLPIQGSSMGQMAAPMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSMDQGHLGNPEQSAMLPQLNTPNRSALSSELSLVGDTTGDTLEKFVEGL DIP protein P45481 original sequence version: 148 DIP protein P45481 original sequence version: 126 DIP protein P45481 original sequence version: 152 DIP protein P45481 original sequence version: 115 DIP protein P45481 original sequence version: 127 DIP protein P45481 original sequence version: 123 DIP protein P45481 original sequence version: 149 DIP protein P45481 original sequence version: 156 DIP protein P45481 original sequence version: 169 DIP protein P45481 original sequence version: 175 DIP protein P45481 original sequence version: 135 D89AF52B7BD33347 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 hist1h4a-crebbp 1 CBP 2 elisa enzyme linked immunosorbent assay ELISA ELISA elisa experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey purified purified 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 binding site binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-8544745]The shifted ranges (1079-1198) couldn't be applied as the new full feature sequence is different from the previous one. [EBI-8544745]1079-1198 [EBI-8544745]P45481,2 H4 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role bait bait purified purified acetylated residue ac1res monoacetylated residue Acetyl Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac) Acetylation Ac1Res certain certain sequence position certain certain certain sequence position certain prerequisite-ptm acetylated residue ac1res monoacetylated residue Acetyl Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac) Acetylation Ac1Res certain certain sequence position certain certain certain sequence position certain prerequisite-ptm binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain acetylated residue ac1res monoacetylated residue Acetyl Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac) Acetylation Ac1Res certain certain sequence position certain certain certain sequence position certain prerequisite-ptm direct interaction direct interaction homomint domino mint To determine whether the CH2 domain of CBP functions in recognition of modified histones, we screened for binding using MODifiedTM Histone Peptide arrays from Active Motif. We used the GST-tagged BRD-CH2 construct for the assay and compared the results with binding data for the isolated BRD using a GST-BRD construct. The BRD-CH2 was observed to bind preferentially to several acetylated histone H4 and H2B peptides (Fig. 5A). However, the isolated BRD binds to the same set of H4 and H2B peptides (Fig. 5A). f5a sf5 hist1h4a-crebbp-1 1 CBP 2 elisa enzyme linked immunosorbent assay ELISA ELISA elisa experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey purified purified binding site binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-8544773]The shifted ranges (1079-1198) couldn't be applied as the new full feature sequence is different from the previous one. [EBI-8544773]1079-1198 [EBI-8544773]P45481,2 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 H4 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role bait bait purified purified acetylated residue ac1res monoacetylated residue Acetyl Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac) Acetylation Ac1Res certain certain sequence position certain certain certain sequence position certain prerequisite-ptm acetylated residue ac1res monoacetylated residue Acetyl Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac) Acetylation Ac1Res certain certain sequence position certain certain certain sequence position certain prerequisite-ptm acetylated residue ac1res monoacetylated residue Acetyl Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac) Acetylation Ac1Res certain certain sequence position certain certain certain sequence position certain prerequisite-ptm acetylated residue ac1res monoacetylated residue Acetyl Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac) Acetylation Ac1Res certain certain sequence position certain certain certain sequence position certain prerequisite-ptm binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction homomint domino mint To determine whether the CH2 domain of CBP functions in recognition of modified histones, we screened for binding using MODifiedTM Histone Peptide arrays from Active Motif. We used the GST-tagged BRD-CH2 construct for the assay and compared the results with binding data for the isolated BRD using a GST-BRD construct. The BRD-CH2 was observed to bind preferentially to several acetylated histone H4 and H2B peptides (Fig. 5A). However, the isolated BRD binds to the same set of H4 and H2B peptides (Fig. 5A). f5a sf5