DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220514X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220526X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220524X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. 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 Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220518X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220519X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220525X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220522X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. 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 Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220515X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. 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 Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220516X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. 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 Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220521X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220520X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220527X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220513X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. 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 Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220523X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones AE., MacKenzie F., Pan P., Li SS., Wang H., Min J. DIP original experiment: DIP-220517X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). h3k9-1 H3K9 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ARTKQTARKSTGGKA h1k26 Histone 1 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) KKKARKSAGAAKY eed_human Polycomb protein EED EED WD protein associating with integrin cytoplasmic tails 1 Embryonic ectoderm development protein protein protein human Homo sapiens Human MSEREVSTAPAGTDMPAAKKQKLSSDENSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR DIP protein O75530 original sequence version: 70 DIP protein O75530-1 original sequence version: 78 DIP protein O75530 original sequence version: 78 DIP protein O75530 original sequence version: 73 DIP protein O75530-1 original sequence version: 89 DIP protein O75530-1 original sequence version: 87 DIP protein O75530 original sequence version: 77 D2E0A5BA27C0499A h3k27-1 Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) QLATKAARKSAPATG h3k79 Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) EIAQDFKTDLRY h4k20ac H4-K20ac peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) GGAKRHRKVLRDNIQ h3k36-3 Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) SAPATGGVKKPHRYR eed-h3k4-1 13 16 unspecified role unspecified role unspecified role unspecified role K9me3 K9me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain Fluorescein-label Fluorescein-label fluorescein fluorescein label fluorescein n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 18 unspecified role unspecified role unspecified role unspecified role WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction eed-h3k79-1 11 20 unspecified role unspecified role unspecified role unspecified role K7me3 K7me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain Fluorescein-label Fluorescein-label fluorescein fluorescein label fluorescein n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 18 unspecified role unspecified role unspecified role unspecified role WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction eed-h1k26-1 3 17 unspecified role unspecified role unspecified role unspecified role K6me3 K6me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain in vitro In vitro 18 unspecified role unspecified role unspecified role unspecified role WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction eed-h3k27-1 15 19 unspecified role unspecified role unspecified role unspecified role K9me2 K9me2 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 K9me3 K9me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain Fluorescein-label Fluorescein-label fluorescein fluorescein label fluorescein n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 18 unspecified role unspecified role unspecified role unspecified role WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction h3k27-eed-1 12 19 unspecified role unspecified role bait bait K9me3 K9me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain Biotin-tag Biotin-tag biotin tag biotin tag n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 18 unspecified role unspecified role prey prey WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction eed-h3k4-2 1 16 unspecified role unspecified role unspecified role unspecified role K4me3 K4me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain Fluorescein-label Fluorescein-label fluorescein fluorescein label fluorescein n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal Region 1-11 Region 1-11 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 18 unspecified role unspecified role unspecified role unspecified role WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction eed-h3k4-3 6 16 unspecified role unspecified role unspecified role unspecified role K9me3 K9me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain Fluorescein-label Fluorescein-label fluorescein fluorescein label fluorescein n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 18 unspecified role unspecified role unspecified role unspecified role WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain O75530:p.Tyr148Ala Y148A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y148A'. Wed May 02 18:48:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr148ala' Tue Jun 30 15:38:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr148Ala' O75530:p.Trp364Ala W364A/L mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain W A Wed May 02 18:55:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp364ala' Tue Jun 30 16:46:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp364Ala' O75530:p.Tyr365Ala Y365A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y365A'. Wed May 02 16:07:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr365ala' Tue Jun 30 18:04:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr365Ala' O75530:p.Phe97Ala F97A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain F A This feature has been corrected as a result of our quality control procedures. The original label was 'F97A'. Wed May 02 19:56:13 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe97ala' Tue Jun 30 20:21:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe97Ala' O75530:p.Trp364Leu mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain W L Wed May 02 17:27:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp364leu' Tue Jun 30 18:18:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp364Leu' ecolx Escherichia coli direct interaction direct interaction eed-h3k27-2 4 19 unspecified role unspecified role unspecified role unspecified role K9me3 K9me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain in vitro In vitro 18 unspecified role unspecified role unspecified role unspecified role WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction eed-h3k79-2 10 20 unspecified role unspecified role unspecified role unspecified role K7me3 K7me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain in vitro In vitro 18 unspecified role unspecified role unspecified role unspecified role WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction h1k26-eed-1 2 17 unspecified role unspecified role bait bait K6me3 K6me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain Biotin-tag Biotin-tag biotin tag biotin tag n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 18 unspecified role unspecified role prey prey WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction eed-h3k36-1 5 22 unspecified role unspecified role unspecified role unspecified role K9me3 K9me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain Fluorescein-label Fluorescein-label fluorescein fluorescein label fluorescein n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 18 unspecified role unspecified role unspecified role unspecified role WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction eed-h4k20-1 7 21 unspecified role unspecified role unspecified role unspecified role K8me3 K8me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain Fluorescein-label Fluorescein-label fluorescein fluorescein label fluorescein n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 18 unspecified role unspecified role unspecified role unspecified role WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction eed-h3k4-4 8 16 unspecified role unspecified role unspecified role unspecified role K4me3 K4me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain Region 1-11 Region 1-11 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 18 unspecified role unspecified role unspecified role unspecified role WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction eed-h3k4-5 9 16 unspecified role unspecified role unspecified role unspecified role K9me3 K9me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain in vitro In vitro 18 unspecified role unspecified role unspecified role unspecified role WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction eed-h4k20-2 14 21 unspecified role unspecified role unspecified role unspecified role K8me3 K8me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain in vitro In vitro 18 unspecified role unspecified role unspecified role unspecified role WD40-repeat domain Region 40-441 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction