DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structure (London, England : 1993) 2013 imex curation Krishnan S., Trievel RC. Only protein-protein interactions in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Krishnan S., Trievel RC. DIP original experiment: DIP-251878X Structure (London, England : 1993) 2013 IMEx Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structure (London, England : 1993) 2013 imex curation Krishnan S., 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 Krishnan S., Trievel RC. DIP original experiment: DIP-251872X Structure (London, England : 1993) 2013 IMEx Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structure (London, England : 1993) 2013 imex curation Krishnan S., Trievel RC. Only protein-protein interactions in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Krishnan S., Trievel RC. DIP original experiment: DIP-251875X Structure (London, England : 1993) 2013 IMEx Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structure (London, England : 1993) 2013 imex curation Krishnan S., Trievel RC. Only protein-protein interactions in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Krishnan S., Trievel RC. DIP original experiment: DIP-251873X Structure (London, England : 1993) 2013 IMEx Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structure (London, England : 1993) 2013 imex curation Krishnan S., Trievel RC. Only protein-protein interactions in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Krishnan S., Trievel RC. DIP original experiment: DIP-251877X Structure (London, England : 1993) 2013 IMEx Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structure (London, England : 1993) 2013 imex curation Krishnan S., Trievel RC. Only protein-protein interactions in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Krishnan S., Trievel RC. DIP original experiment: DIP-251879X Structure (London, England : 1993) 2013 IMEx Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structure (London, England : 1993) 2013 imex curation Krishnan S., Trievel RC. Only protein-protein interactions in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Krishnan S., Trievel RC. DIP original experiment: DIP-251874X Structure (London, England : 1993) 2013 IMEx Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structure (London, England : 1993) 2013 imex curation Krishnan S., Trievel RC. Only protein-protein interactions in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Krishnan S., Trievel RC. DIP original experiment: DIP-251880X Structure (London, England : 1993) 2013 IMEx Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structure (London, England : 1993) 2013 imex curation Krishnan S., Trievel RC. Only protein-protein interactions in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Krishnan S., Trievel RC. DIP original experiment: DIP-251876X Structure (London, England : 1993) 2013 IMEx Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. 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 h3k9-1 H3K9 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ARTKQTARKSTGGKA 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 kdm4b_human Lysine-specific demethylase 4B Jumonji domain-containing protein 2B KDM4B KIAA0876 JHDM3B JMJD2B JmjC domain-containing histone demethylation protein 3B [histone H3]-trimethyl-L-lysine(9) demethylase 4B protein protein human Homo sapiens Human MGSEDHGAQNPSCKIMTFRPTMEEFKDFNKYVAYIESQGAHRAGLAKIIPPKEWKPRQTYDDIDDVVIPAPIQQVVTGQSGLFTQYNIQKKAMTVGEYRRLANSEKYCTPRHQDFDDLERKYWKNLTFVSPIYGADISGSLYDDDVAQWNIGSLRTILDMVERECGTIIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAIGFFPGSSQGCDAFLRHKMTLISPIILKKYGIPFSRITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATLRWIDYGKVATQCTCRKDMVKISMDVFVRILQPERYELWKQGKDLTVLDHTRPTALTSPELSSWSASRASLKAKLLRRSHRKRSQPKKPKPEDPKFPGEGTAGAALLEEAGGSVKEEAGPEVDPEEEEEEPQPLPHGREAEGAEEDGRGKLRPTKAKSERKKKSFGLLPPQLPPPPAHFPSEEALWLPSPLEPPVLGPGPAAMEESPLPAPLNVVPPEVPSEELEAKPRPIIPMLYVVPRPGKAAFNQEHVSCQQAFEHFAQKGPTWKEPVSPMELTGPEDGAASSGAGRMETKARAGEGQAPSTFSKLKMEIKKSRRHPLGRPPTRSPLSVVKQEASSDEEASPFSGEEDVSDPDALRPLLSLQWKNRAASFQAERKFNAAAARTEPYCAICTLFYPYCQALQTEKEAPIASLGKGCPATLPSKSRQKTRPLIPEMCFTSGGENTEPLPANSYIGDDGTSPLIACGKCCLQVHASCYGIRPELVNEGWTCSRCAAHAWTAECCLCNLRGGALQMTTDRRWIHVICAIAVPEARFLNVIERHPVDISAIPEQRWKLKCVYCRKRMKKVSGACIQCSYEHCSTSFHVTCAHAAGVLMEPDDWPYVVSITCLKHKSGGHAVQLLRAVSLGQVVITKNRNGLYYRCRVIGAASQTCYEVNFDDGSYSDNLYPESITSRDCVQLGPPSEGELVELRWTDGNLYKAKFISSVTSHIYQVEFEDGSQLTVKRGDIFTLEEELPKRVRSRLSLSTGAPQEPAFSGEEAKAAKRPRVGTPLATEDSGRSQDYVAFVESLLQVQGRPGAPF DIP protein O94953 original sequence version: 109 DIP protein O94953 original sequence version: 95 300D5CD6F2DD4330 h3k36-3 Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) SAPATGGVKKPHRYR kdm4c_human Lysine-specific demethylase 4C KDM4C GASC1 JHDM3C JMJD2C KIAA0780 Gene amplified in squamous cell carcinoma 1 protein JmjC domain-containing histone demethylation protein 3C Jumonji domain-containing protein 2C [histone H3]-trimethyl-L-lysine(9) demethylase 4C protein protein human Homo sapiens Human MEVAEVESPLNPSCKIMTFRPSMEEFREFNKYLAYMESKGAHRAGLAKVIPPKEWKPRQCYDDIDNLLIPAPIQQMVTGQSGLFTQYNIQKKAMTVKEFRQLANSGKYCTPRYLDYEDLERKYWKNLTFVAPIYGADINGSIYDEGVDEWNIARLNTVLDVVEEECGISIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAQGFFPSSSQGCDAFLRHKMTLISPSVLKKYGIPFDKITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATVRWIDYGKVAKLCTCRKDMVKISMDIFVRKFQPDRYQLWKQGKDIYTIDHTKPTPASTPEVKAWLQRRRKVRKASRSFQCARSTSKRPKADEEEEVSDEVDGAEVPNPDSVTDDLKVSEKSEAAVKLRNTEASSEEESSASRMQVEQNLSDHIKLSGNSCLSTSVTEDIKTEDDKAYAYRSVPSISSEADDSIPLSSGYEKPEKSDPSELSWPKSPESCSSVAESNGVLTEGEESDVESHGNGLEPGEIPAVPSGERNSFKVPSIAEGENKTSKSWRHPLSRPPARSPMTLVKQQAPSDEELPEVLSIEEEVEETESWAKPLIHLWQTKSPNFAAEQEYNATVARMKPHCAICTLLMPYHKPDSSNEENDARWETKLDEVVTSEGKTKPLIPEMCFIYSEENIEYSPPNAFLEEDGTSLLISCAKCCVRVHASCYGIPSHEICDGWLCARCKRNAWTAECCLCNLRGGALKQTKNNKWAHVMCAVAVPEVRFTNVPERTQIDVGRIPLQRLKLKCIFCRHRVKRVSGACIQCSYGRCPASFHVTCAHAAGVLMEPDDWPYVVNITCFRHKVNPNVKSKACEKVISVGQTVITKHRNTRYYSCRVMAVTSQTFYEVMFDDGSFSRDTFPEDIVSRDCLKLGPPAEGEVVQVKWPDGKLYGAKYFGSNIAHMYQVEFEDGSQIAMKREDIYTLDEELPKRVKARFSTASDMRFEDTFYGADIIQGERKRQRVLSSRFKNEYVADPVYRTFLKSSFQKKCQKRQ DIP protein Q9H3R0 original sequence version: 105 CBE871D4FAADD06D h3k9me3-kdm4d-1 2 11 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 10 unspecified role unspecified role unspecified role unspecified role Region 12-342 Region 12-342 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 h3k36me3-kdm4b-1 5 13 enzyme enzyme unspecified role unspecified role Region 9-357 Region 9-357 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 14 enzyme target enzyme target substrate substrate 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 demethylation demethylation reaction demethylation h3k36me3-kdm4c-1 8 14 enzyme target enzyme target substrate substrate 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 15 enzyme enzyme unspecified role unspecified role Region 1-350 Region 1-350 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 h3k9me3-kdm4a-1 7 12 enzyme enzyme unspecified role unspecified role Region 1-350 Region 1-350 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 11 enzyme target enzyme target substrate substrate 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 h3k9-1:p.Arg8Ala R8A mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R8A'. Wed May 02 18:18:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg8ala' Tue Jun 30 20:05:46 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg8Ala' h3k9-1:p.Ser10Ala S10A mutation decreasing rate mutation decreasing interaction rate mutation decreasing 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 'S10A'. Wed May 02 17:54:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser10ala' Tue Jun 30 18:17:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser10Ala' h3k9-1:p.Thr11Ala T11A mutation increasing rate mutation increasing interaction rate mutation increasing rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain T A This feature has been corrected as a result of our quality control procedures. The original label was 'T11A'. Wed May 02 15:37:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr11ala' Tue Jun 30 17:18:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr11Ala' h3k9-1:p.[Ser10Ala;Thr11Ala] S10A/T11A mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain T A 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 'S10A/T11A'. Wed May 02 15:21:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser10ala,thr11ala' Tue Jun 30 16:24:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ser10Ala;Thr11Ala]' h3k9-1:p.Thr11Ser T11S mutation increasing rate mutation increasing interaction rate mutation increasing rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain T S This feature has been corrected as a result of our quality control procedures. The original label was 'T11S'. Wed May 02 18:18:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr11ser' Tue Jun 30 17:25:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr11Ser' pT11 pT11 opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt certain certain sequence position certain certain certain sequence position certain disrupting-ptm ptm disrupting an interaction disrupting-ptm in vitro In vitro demethylation demethylation reaction demethylation h3k9me3-kdm4a-2 3 12 enzyme enzyme unspecified role unspecified role Region 1-350 Region 1-350 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain O75164-1:p.Ile71Leu I71L 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 I L This feature has been corrected as a result of our quality control procedures. The original label was 'I71L'. Wed May 02 20:24:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile71leu' Tue Jun 30 19:42:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile71Leu' ecolx Escherichia coli 11 enzyme target enzyme target substrate substrate 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 demethylation demethylation reaction demethylation h3k9me3-kdm4d-2 4 11 enzyme target enzyme target substrate substrate 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 h3k9-1:p.Arg8Ala R8A mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R8A'. Wed May 02 17:33:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg8ala' Tue Jun 30 20:16:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg8Ala' h3k9-1:p.Ser10Ala S10A mutation decreasing rate mutation decreasing interaction rate mutation decreasing 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 'S10A'. Wed May 02 18:09:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser10ala' Tue Jun 30 20:12:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser10Ala' h3k9-1:p.Thr11Ala T11A mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain T A This feature has been corrected as a result of our quality control procedures. The original label was 'T11A'. Wed May 02 19:00:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr11ala' Tue Jun 30 18:24:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr11Ala' h3k9-1:p.[Ser10Ala;Thr11Ala] S10A/T11A mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain T A 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 'S10A/T11A'. Wed May 02 17:47:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser10ala,thr11ala' Tue Jun 30 17:15:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ser10Ala;Thr11Ala]' h3k9-1:p.Thr11Ser T11S mutation increasing rate mutation increasing interaction rate mutation increasing rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain T S This feature has been corrected as a result of our quality control procedures. The original label was 'T11S'. Wed May 02 19:58:19 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr11ser' Tue Jun 30 18:46:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr11Ser' pT11 pT11 opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt certain certain sequence position certain certain certain sequence position certain disrupting-ptm ptm disrupting an interaction disrupting-ptm in vitro In vitro 10 enzyme enzyme unspecified role unspecified role Region 12-342 Region 12-342 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 h3k36me3-kdm4a-1 9 14 enzyme target enzyme target substrate substrate 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 arg13ala R40A mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain R A in vitro In vitro 12 enzyme enzyme unspecified role unspecified role Region 1-350 Region 1-350 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 h3k9me3-kdm4b-1 1 11 enzyme target enzyme target substrate substrate 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 pT11 pT11 opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt certain certain sequence position certain certain certain sequence position certain disrupting-ptm ptm disrupting an interaction disrupting-ptm in vitro In vitro 13 enzyme enzyme unspecified role unspecified role Region 9-357 Region 9-357 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 h3k9me3-kdm4c-1 6 15 enzyme enzyme unspecified role unspecified role Region 1-350 Region 1-350 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 11 enzyme target enzyme target substrate substrate 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 pT11 pT11 opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt certain certain sequence position certain certain certain sequence position certain disrupting-ptm ptm disrupting an interaction disrupting-ptm in vitro In vitro demethylation demethylation reaction demethylation