DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ ng-2007-5 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. DIP original experiment: DIP-253185X Nature 2007 IMEx Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. Only protein-protein interactions imex curation ng-2007-6 in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. DIP original experiment: DIP-253187X Nature 2007 IMEx Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. Only protein-protein interactions imex curation ng-2007-7 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. DIP original experiment: DIP-253191X Nature 2007 IMEx Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. Only protein-protein interactions imex curation ng-2007-8 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. DIP original experiment: DIP-253189X Nature 2007 IMEx Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. Only protein-protein interactions imex curation ng-2007-9 in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. DIP original experiment: DIP-253186X Nature 2007 IMEx Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. Only protein-protein interactions imex curation ng-2007-10 in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. DIP original experiment: DIP-253188X Nature 2007 IMEx Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. Only protein-protein interactions imex curation ng-2007-11 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. DIP original experiment: DIP-253190X Nature 2007 IMEx Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Ng SS., Kavanagh KL., McDonough MA., Butler D., Pilka ES., Lienard BM., Bray JE., Savitsky P., Gileadi O., von Delft F., Rose NR., Offer J., Scheinost JC., Borowski T., Sundstrom M., Schofield CJ., Oppermann U. Only protein-protein interactions imex curation h3k9 Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ARKSTGGK o75164-1 Lysine-specific demethylase 4A [histone H3]-trimethyl-L-lysine(36) demethylase 4A [histone H3]-trimethyl-L-lysine(9) demethylase 4A KDM4A JHDM3A JMJD2 JMJD2A KIAA0677 JmjC domain-containing histone demethylation protein 3A Jumonji domain-containing protein 2A protein protein human Homo sapiens Human MASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKNLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRKFQPERYKLWKAGKDNTVIDHTLPTPEAAEFLKESELPPRAGNEEECPEEDMEGVEDGEEGDLKTSLAKHRIGTKRHRVCLEIPQEVSQSELFPKEDLSSEQYEMTECPAALAPVRPTHSSVRQVEDGLTFPDYSDSTEVKFEELKNVKLEEEDEEEEQAAAALDLSVNPASVGGRLVFSGSKKKSSSSLGSGSSRDSISSDSETSEPLSCRAQGQTGVLTVHSYAKGDGRVTVGEPCTRKKGSAARSFSERELAEVADEYMFSLEENKKSKGRRQPLSKLPRHHPLVLQECVSDDETSEQLTPEEEAEETEAWAKPLSQLWQNRPPNFEAEKEFNETMAQQAPHCAVCMIFQTYHQVEFGGFNQNCGNASDLAPQKQRTKPLIPEMCFTSTGCSTDINLSTPYLEEDGTSILVSCKKCSVRVHASCYGVPPAKASEDWMCSRCSANALEEDCCLCSLRGGALQRANDDRWVHVSCAVAILEARFVNIAERSPVDVSKIPLPRFKLKCIFCKKRRKRTAGCCVQCSHGRCPTAFHVSCAQAAGVMMQPDDWPFVVFITCFRHKIPNLERAKGALQSITAGQKVISKHKNGRFYQCEVVRLTTETFYEVNFDDGSFSDNLYPEDIVSQDCLQFGPPAEGEVVQVRWTDGQVYGAKFVASHPIQMYQVEFEDGSQLVVKRDDVYTLDEELPKRVKSRLSVASDMRFNEIFTEKEVKQEKKRQRVINSRYREDYIEPALYRAIME h3k27 Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) AARKSAPAT h3k36 Histone 3 petide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) STGGVKKPHRY h3k9-kdm4a-1 3157895 N/A 3157902 unspecified role unspecified role unspecified role unspecified role K3me1 K3me1 n6me1lys N6-methyl-L-lysine (2S)-2-amino-6-methylaminohexanoic acid MOD_RES N6-methyllysine N(zeta)-methyllysine N6-methyl-L-lysine N6-methylated L-lysine epsilon-methyllysine Methyl Methylation N-methyl Lysyl N6Me1Lys certain certain sequence position certain certain certain sequence position certain false in vitro In vitro N/A 3157903 unspecified role unspecified role unspecified role unspecified role Region 1-359 Region 1-359 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false h3k27-kdm4a-1 3157896 N/A 3157904 enzyme target enzyme target substrate substrate 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 false h3k27:p.[Ala6Pro;Pro7Ala] A6P/P7A mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false in vitro In vitro N/A 3157903 enzyme enzyme unspecified role unspecified role Region 1-359 Region 1-359 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli demethylation demethylation reaction demethylation false false false h3k36-kdm4a-1 3157897 N/A 3157905 unspecified role unspecified role unspecified role unspecified role K36me3 K36me3 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 false in vitro In vitro N/A 3157903 unspecified role unspecified role unspecified role unspecified role Region 1-359 Region 1-359 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false h3k9-kdm4a-2 3157898 N/A 3157902 unspecified role unspecified role unspecified role unspecified role K3me2 K3me2 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 false in vitro In vitro N/A 3157903 unspecified role unspecified role unspecified role unspecified role Region 1-359 Region 1-359 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false h3k9-kdm4a-3 3157899 N/A 3157902 enzyme target enzyme target substrate substrate unspecified role unspecified role K3me3 K3me3 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 false h3k9:p.[Gly6Ala;Gly7Ala] G6A/G7A mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false pS4 pS4 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain false h3k9:p.Ser4Ala S4A mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain false in vitro In vitro N/A 3157903 enzyme enzyme unspecified role unspecified role Region 1-359 Region 1-359 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli demethylation demethylation reaction demethylation false false false h3k36-kdm4a-2 3157900 N/A 3157905 enzyme target enzyme target substrate substrate 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 false in vitro In vitro N/A 3157903 enzyme enzyme unspecified role unspecified role Region 1-359 Region 1-359 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli demethylation demethylation reaction demethylation false false false h3k9-kdm4a-4 3157901 N/A 3157902 unspecified role unspecified role unspecified role unspecified role K3me3 K3me3 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 false in vitro In vitro N/A 3157903 unspecified role unspecified role unspecified role unspecified role Region 1-359 Region 1-359 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false