DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Nature structural & molecular biology 2007 imex curation Couture JF., Collazo E., Ortiz-Tello PA., Brunzelle JS., Trievel RC. Only protein-protein interactions in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as predetermined predetermined participant predetermined Couture JF., Collazo E., Ortiz-Tello PA., Brunzelle JS., Trievel RC. DIP original experiment: DIP-68387X Nature structural & molecular biology 2007 IMEx Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Nature structural & molecular biology 2007 imex curation Couture JF., Collazo E., Ortiz-Tello PA., Brunzelle JS., Trievel RC. 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 Couture JF., Collazo E., Ortiz-Tello PA., Brunzelle JS., Trievel RC. DIP original experiment: DIP-68384X Nature structural & molecular biology 2007 IMEx Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Nature structural & molecular biology 2007 imex curation Couture JF., Collazo E., Ortiz-Tello PA., Brunzelle JS., Trievel RC. Only protein-protein interactions in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as predetermined predetermined participant predetermined Couture JF., Collazo E., Ortiz-Tello PA., Brunzelle JS., Trievel RC. DIP original experiment: DIP-68388X Nature structural & molecular biology 2007 IMEx Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Nature structural & molecular biology 2007 imex curation Couture JF., Collazo E., Ortiz-Tello PA., Brunzelle JS., Trievel RC. 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 Couture JF., Collazo E., Ortiz-Tello PA., Brunzelle JS., Trievel RC. DIP original experiment: DIP-68385X Nature structural & molecular biology 2007 IMEx Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Nature structural & molecular biology 2007 imex curation Couture JF., Collazo E., Ortiz-Tello PA., Brunzelle JS., Trievel RC. Only protein-protein interactions in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as predetermined predetermined participant predetermined Couture JF., Collazo E., Ortiz-Tello PA., Brunzelle JS., Trievel RC. DIP original experiment: DIP-68386X Nature structural & molecular biology 2007 IMEx Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. 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 kdm4d_human Lysine-specific demethylase 4D KDM4D JHDM3D JMJD2D JmjC domain-containing histone demethylation protein 3D Jumonji domain-containing protein 2D [histone H3]-trimethyl-L-lysine(9) demethylase 4D protein protein human Homo sapiens Human METMKSKANCAQNPNCNIMIFHPTKEEFNDFDKYIAYMESQGAHRAGLAKIIPPKEWKARETYDNISEILIATPLQQVASGRAGVFTQYHKKKKAMTVGEYRHLANSKKYQTPPHQNFEDLERKYWKNRIYNSPIYGADISGSLFDENTKQWNLGHLGTIQDLLEKECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHLGEPKTWYVVPPEHGQRLERLARELFPGSSRGCGAFLRHKVALISPTVLKENGIPFNRITQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGEARVTFSMDAFVRILQPERYDLWKRGQDRAVVDHMEPRVPASQELSTQKEVQLPRRAALGLRQLPSHWARHSPWPMAARSGTRCHTLVCSSLPRRSAVSGTATQPRAAAVHSSKKPSSTPSSTPGPSAQIIHPSNGRRGRGRPPQKLRAQELTLQTPAKRPLLAGTTCTASGPEPEPLPEDGALMDKPVPLSPGLQHPVKASGCSWAPVP DIP protein Q6B0I6 original sequence version: 30 DIP protein Q6B0I6 original sequence version: 76 5303A0846ECEBA58 h3k36-1 H3K36 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RKSAPATGGVKKPHRY h3k9-1 H3K9 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ARTKQTARKSTGGKA h3k9-kdm4a-5 2 9 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 6 unspecified role unspecified role neutral component neutral component 1-350 binding region 1-350 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction h3k9-kdm4d-1 3 7 enzyme enzyme neutral component neutral component 3-354 binding region 3-354 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain Q6B0I6:p.Ala292Ser A291S mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain A S Wed May 02 17:14:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala292ser' Tue Jun 30 16:37:55 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala292Ser' ecolx Escherichia coli 9 enzyme target enzyme target substrate substrate neutral component neutral component K9me3 methylation site K9me3 methylation site 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 predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain K9me2 methylation site K9me2 methylation site 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 predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) demethylation demethylation reaction demethylation h3k36-kdm4a-3 4 8 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 6 unspecified role unspecified role neutral component neutral component 1-350 binding region 1-350 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction h3k36-kdm4a-4 1 8 enzyme target enzyme target substrate substrate neutral component neutral component H3K36 methylation site H3K36 methylation site 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 predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 6 enzyme enzyme neutral component neutral component 1-350 binding region 1-350 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli demethylation demethylation reaction demethylation h3k9-kdm4a-6 5 9 enzyme target enzyme target substrate substrate neutral component neutral component h3k9-1:p.Gly12Pro G12P mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain G P This feature has been corrected as a result of our quality control procedures. The original label was 'G12P mutation'. Wed May 02 17:21:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly12pro' Tue Jun 30 19:31:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly12Pro' K9me2 methylation site K9me2 methylation site 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 predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain K9me3 methylation site K9me3 methylation site 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 predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain h3k9-1:p.Ala7Arg A7R mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain A R This feature has been corrected as a result of our quality control procedures. The original label was 'A7R mutation'. Wed May 02 20:10:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala7arg' Tue Jun 30 16:20:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala7Arg' chemical synthesis Chemical synthesis (Chemical synthesis) 6 enzyme enzyme neutral component neutral component O75164-1:p.Ser288Ala S288A mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing substitut analysis substitution analysis substitut analysis 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 'S288A mutation'. Wed May 02 16:15:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser288ala' Tue Jun 30 20:22:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser288Ala' 1-350 binding region 1-350 binding region sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli demethylation demethylation reaction demethylation