DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Nature 2007 imex curation 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 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. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Nature 2007 imex curation 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 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. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Nature 2007 imex curation 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 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. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Nature 2007 imex curation 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 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. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Nature 2007 imex curation 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 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. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Nature 2007 imex curation 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 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. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Nature 2007 imex curation 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 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. h3k36 Histone 3 petide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) STGGVKKPHRY 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 DIP protein O75164-1 original sequence version: 120 DIP protein O75164 original sequence version: 66 DIP protein O75164 original sequence version: 76 DIP protein O75164-1 original sequence version: 130 DIP protein O75164-1 original sequence version: 116 h3k9 Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ARKSTGGK h3k27 Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) AARKSAPAT h3k9-kdm4a-1 2 10 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 in vitro In vitro 9 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 ecolx Escherichia coli direct interaction direct interaction h3k27-kdm4a-1 5 11 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 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 P A certain certain sequence position certain certain certain sequence position certain A P This feature has been corrected as a result of our quality control procedures. The original label was 'A6P/P7A'. Wed May 02 17:03:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala6pro,pro7ala' Tue Jun 30 18:42:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ala6Pro;Pro7Ala]' in vitro In vitro 9 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 ecolx Escherichia coli demethylation demethylation reaction demethylation h3k36-kdm4a-1 7 8 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 in vitro In vitro 9 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 ecolx Escherichia coli direct interaction direct interaction h3k9-kdm4a-2 3 10 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 in vitro In vitro 9 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 ecolx Escherichia coli direct interaction direct interaction h3k9-kdm4a-3 1 10 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 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 G A certain certain sequence position certain certain certain sequence position certain G A This feature has been corrected as a result of our quality control procedures. The original label was 'G6A/G7A'. Wed May 02 14:56:32 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly6ala,gly7ala' Tue Jun 30 18:24:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Gly6Ala;Gly7Ala]' 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 decreasing-ptm ptm decreasing an interaction decreasing-ptm 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 S A This feature has been corrected as a result of our quality control procedures. The original label was 'S4A'. Wed May 02 17:00:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser4ala' Tue Jun 30 15:40:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser4Ala' in vitro In vitro 9 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 ecolx Escherichia coli demethylation demethylation reaction demethylation h3k36-kdm4a-2 4 8 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 in vitro In vitro 9 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 ecolx Escherichia coli demethylation demethylation reaction demethylation h3k9-kdm4a-4 6 10 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 in vitro In vitro 9 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 ecolx Escherichia coli direct interaction direct interaction