DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Nature 2009 imex curation Morinière J., Rousseaux S., Steuerwald U., Soler-López M., Curtet S., Vitte AL., Govin J., Gaucher J., Sadoul K., Hart DJ., Krijgsveld J., Khochbin S., Müller CW., Petosa C. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Morinière J., Rousseaux S., Steuerwald U., Soler-López M., Curtet S., Vitte AL., Govin J., Gaucher J., Sadoul K., Hart DJ., Krijgsveld J., Khochbin S., Müller CW., Petosa C. DIP original experiment: DIP-219572X Nature 2009 IMEx Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Nature 2009 imex curation Morinière J., Rousseaux S., Steuerwald U., Soler-López M., Curtet S., Vitte AL., Govin J., Gaucher J., Sadoul K., Hart DJ., Krijgsveld J., Khochbin S., Müller CW., Petosa C. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Morinière J., Rousseaux S., Steuerwald U., Soler-López M., Curtet S., Vitte AL., Govin J., Gaucher J., Sadoul K., Hart DJ., Krijgsveld J., Khochbin S., Müller CW., Petosa C. DIP original experiment: DIP-219573X Nature 2009 IMEx Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Nature 2009 imex curation Morinière J., Rousseaux S., Steuerwald U., Soler-López M., Curtet S., Vitte AL., Govin J., Gaucher J., Sadoul K., Hart DJ., Krijgsveld J., Khochbin S., Müller CW., Petosa C. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Morinière J., Rousseaux S., Steuerwald U., Soler-López M., Curtet S., Vitte AL., Govin J., Gaucher J., Sadoul K., Hart DJ., Krijgsveld J., Khochbin S., Müller CW., Petosa C. DIP original experiment: DIP-219571X Nature 2009 IMEx Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Nature 2009 imex curation Morinière J., Rousseaux S., Steuerwald U., Soler-López M., Curtet S., Vitte AL., Govin J., Gaucher J., Sadoul K., Hart DJ., Krijgsveld J., Khochbin S., Müller CW., Petosa C. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Morinière J., Rousseaux S., Steuerwald U., Soler-López M., Curtet S., Vitte AL., Govin J., Gaucher J., Sadoul K., Hart DJ., Krijgsveld J., Khochbin S., Müller CW., Petosa C. DIP original experiment: DIP-219570X Nature 2009 IMEx Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Nature 2009 imex curation Morinière J., Rousseaux S., Steuerwald U., Soler-López M., Curtet S., Vitte AL., Govin J., Gaucher J., Sadoul K., Hart DJ., Krijgsveld J., Khochbin S., Müller CW., Petosa C. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Morinière J., Rousseaux S., Steuerwald U., Soler-López M., Curtet S., Vitte AL., Govin J., Gaucher J., Sadoul K., Hart DJ., Krijgsveld J., Khochbin S., Müller CW., Petosa C. DIP original experiment: DIP-219574X Nature 2009 IMEx Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Nature 2009 imex curation Morinière J., Rousseaux S., Steuerwald U., Soler-López M., Curtet S., Vitte AL., Govin J., Gaucher J., Sadoul K., Hart DJ., Krijgsveld J., Khochbin S., Müller CW., Petosa C. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Morinière J., Rousseaux S., Steuerwald U., Soler-López M., Curtet S., Vitte AL., Govin J., Gaucher J., Sadoul K., Hart DJ., Krijgsveld J., Khochbin S., Müller CW., Petosa C. DIP original experiment: DIP-219575X Nature 2009 IMEx Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. h4r3 H4R3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) SGRGKGGKGLGKGGAKRHRK q91y44-1 Bromodomain testis-specific protein Brdt Fsrg3 Bromodomain-containing female sterile homeotic-like protein RING3-like protein protein protein mouse Mus musculus Mouse MSLPSRQTAIVNPPPPEYINTKKSGRLTNQLQFLQRVVLKALWKHGFSWPFQQPVDAVKLKLPDYYTIIKTPMDLNTIKKRLENKYYEKASECIEDFNTMFSNCYLYNKTGDDIVVMAQALEKLFMQKLSQMPQEEQVVGGKERIKKDIQQKIAVSSAKEQIPSKAAENVFKRQEIPSGLPDISLSPLNMAQEAPPICDSQSLVQITKGVKRRADTTTPTTSIAKASSESPPTLRETKPVNMPVKENTVKNVLPDSQQQHKVLKTVKVTEQLKHCSEILKEMLAKKHLPYAWPFYNPVDADALGLHNYYDVVKNPMDLGTIKGKMDNQEYKDAYEFAADVRLMFMNCYKYNPPDHEVVAMARTLQDVFELHFAKIPDEPIESMHACHLTTNSAQALSRESSSEASSGDASSEDSEDERVQHLAKLQEQLNAVHQQLQVLSQVPLRKLKKKNEKSKRAPKRKKVNNRDENPRKKPKQMKQKEKAKINQPKKKKPLLKSEEEDNAKPMNYDEKRQLSLDINKLPGDKLGRIVHIIQSREPSLRNSNPDEIEIDFETLKASTLRELEKYVLACLRKRSLKPQAKKVVRSKEELHSEKKLELERRLLDVNNQLNCRKRQTKRPAKVEKPPPPPPPPPPPPPPPELASGSRLTDSSSSSGSGSGSSSSSSGSSSSSSSSGSASSSSDSSSSDSSDSEPEIFPKFTGVKQNDLPPKENIKQIQSSVQDITSAEAPLAQQSTAPCGAPGKHSQQMLGCQVTQHLQATENTASVQTQPLSGDCKRVLLGPPVVHTSAESLTVLEPECHAPAQKDIKIKNADSWKSLGKPVKASSVLKSSDELFNQFRKAAIEKEVKARTQEQMRKHLEHNAKDPKVSQENQREPGSGLTLESLSSKVQDKSLEEDQSEQQPPSEAQDVSKLWLLKDRNLAREKEQERRRREAMAGTIDMTLQSDIMTMFENNFD DIP protein Q91Y44-1 original sequence version: 72 DIP protein Q91Y44-1 original sequence version: 59 h2b-1 Histone 2B peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) PSKSAPAPKKGSKKAISKAQ h3-5 Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) KQTARKSTGGKAPRKQLATKAARK brdt-h3-1 4 10 unspecified role unspecified role unspecified role unspecified role Region 11-20 Region 11-20 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 8 unspecified role unspecified role unspecified role unspecified role Region 257-383 Region 257-383 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction brdt-h4-1 1 7 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 8 unspecified role unspecified role unspecified role unspecified role Region 17-136 Region 17-136 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction brdt-h3-2 5 10 unspecified role unspecified role unspecified role unspecified role K6/11/15/20-ac K6/11/15/20-ac naclys N-acetylated L-lysine NAcLys certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain in vitro In vitro 8 unspecified role unspecified role unspecified role unspecified role Region 23-142 Region 23-142 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Region 257-383 Region 257-383 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction brdt-h4-2 2 7 unspecified role unspecified role unspecified role unspecified role K5/K8-ac K5/K8-ac naclys N-acetylated L-lysine NAcLys certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain in vitro In vitro 8 unspecified role unspecified role unspecified role unspecified role Region 23-142 Region 23-142 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q91Y44-1:p.Ile114Tyr I114Y/W mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain I Y Wed May 02 19:47:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile114tyr' Tue Jun 30 18:04:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile114Tyr' Q91Y44-1:p.Ile114Trp mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain I W Wed May 02 15:10:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile114trp' Tue Jun 30 18:30:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile114Trp' ecolx Escherichia coli direct interaction direct interaction brdt-h4-3 3 7 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 8 unspecified role unspecified role unspecified role unspecified role Region 17-136 Region 17-136 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction brdt-h2b-1 6 9 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 8 unspecified role unspecified role unspecified role unspecified role Region 23-142 Region 23-142 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction