DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 2006 imex curation Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. DIP original experiment: DIP-254891X Nature 2006 IMEx Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 2006 imex curation Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. DIP original experiment: DIP-254890X Nature 2006 IMEx Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 2006 imex curation Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. DIP original experiment: DIP-254889X Nature 2006 IMEx Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 2006 imex curation Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. DIP original experiment: DIP-254895X Nature 2006 IMEx Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 2006 imex curation Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. DIP original experiment: DIP-254887X Nature 2006 IMEx Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 2006 imex curation Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. DIP original experiment: DIP-254892X Nature 2006 IMEx Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 2006 imex curation Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. DIP original experiment: DIP-254888X Nature 2006 IMEx Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 2006 imex curation Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. DIP original experiment: DIP-254894X Nature 2006 IMEx Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 2006 imex curation Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. DIP original experiment: DIP-254893X Nature 2006 IMEx Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 2006 imex curation Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. 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 Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. DIP original experiment: DIP-254885X Nature 2006 IMEx Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 2006 imex curation Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Peña PV., Davrazou F., Shi X., Walter KL., Verkhusha VV., Gozani O., Zhao R., Kutateladze TG. DIP original experiment: DIP-254886X Nature 2006 IMEx Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. ing2_mouse Inhibitor of growth protein 2 p33ING2 Inhibitor of growth 1-like protein Ing2 Ing1l protein protein mouse Mus musculus Mouse MLGQQQQQQLYSSAALLTGERSRLLSCYVQDYLECVESLPHDMQRNVSVLRELDNKYQETLKEIDDVYEKYKKEDDSNQKKRLQQHLQRALINSQELGDEKIQIVTQMLELVENRARQMELHSQCFQDPAESERASDKSKMDSSQPERSSRRPRRQRTSESRDLCHMTNGIDDCDDQPPKEKRSKSAKKKKRSKAKQEREASPVEFAIDPNEPTYCLCNQVSYGEMIGCDNEQCPIEWFHFSCVSLTYKPKGKWYCPKCRGDNEKTMDKSTEKTKKERRAR DIP protein Q9ESK4 original sequence version: 114 6D953B52822C2D8A yng2_yeast Chromatin modification-related protein YNG2 YHR090C YNG2 EAF4 NBN1 ING1 homolog 2 ESA1-associated factor 4 protein protein yeast Saccharomyces cerevisiae Baker's yeast MDPSLVLEQTIQDVSNLPSEFRYLLEEIGSNDLKLIEEKKKYEQKESQIHKFIRQQGSIPKHPQEDGLDKEIKESLLKCQSLQREKCVLANTALFLIARHLNKLEKNIALLEEDGVLAPVEEDGDMDSAAEASRESSVVSNSSVKKRRAASSSGSVPPTLKKKKTSRTSKLQNEIDVSSREKSVTPVSPSIEKKIARTKEFKNSRNGKGQNGSPENEEEDKTLYCFCQRVSFGEMVACDGPNCKYEWFHYDCVNLKEPPKGTWYCPECKIEMEKNKLKRKRN 110E0A2536547D03 110E0A2536547D03 ing1_human Inhibitor of growth protein 1 ING1 protein protein human Homo sapiens Human MSFVECPYHSPAERLVAEADEGGPSAITGMGLCFRCLLFSFSGRSGVEGGRVDLNVFGSLGLQPWIGSSRCWGGPCSSALRCGWFSSWPPPSKSAIPIGGGSRGAGRVSRWPPPHWLEAWRVSPLPLSPLSPATFGRGFIAVAVIPGLWARGRGCSSDRLPRPAGPARRQFQAASLLTRGWGRAWPWKQILKELDECYERFSRETDGAQKRRMLHCVQRALIRSQELGDEKIQIVSQMVELVENRTRQVDSHVELFEAQQELGDTAGNSGKAGADRPKGEAAAQADKPNSKRSRRQRNNENRENASSNHDHDDGASGTPKEKKAKTSKKKKRSKAKAEREASPADLPIDPNEPTYCLCNQVSYGEMIGCDNDECPIEWFHFSCVGLNHKPKGKWYCPKCRGENEKTMDKALEKSKKERAYNR DIP protein Q9UK53 original sequence version: 112 DIP protein Q9UK53-1 original sequence version: 86 03D6AEEAA6E39090 h3(112) Histone 3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ARTKQTARKSTG yng1_yeast Protein YNG1 ING1 homolog 1 YNG1 YOR29-15 YOR064C protein protein yeast Saccharomyces cerevisiae Baker's yeast MEHLANENSDSDIRYSFLSTLDHLPCELIRSLRLMQTIDLFKNEEDEPGMERACRDLLLVATYINDLVDDQIHFLKQHKKELEIQKSVTKNFNSSLENIKSKLTLEEPGAYKEPKLLLKINLKKAKSRERKESITSPTIGINQGDVTEGNNNQEEVYCFCRNVSYGPMVACDNPACPFEWFHYGCVGLKQAPKGKWYCSKDCKEIANQRSKSKRQKRRK 5232A71839E2FDA4 5232A71839E2FDA4 pho23_yeast Transcriptional regulatory protein PHO23 PHO23 N2205 YNL097C protein protein yeast Saccharomyces cerevisiae Baker's yeast MSSPANLFPGLNDITDVLEEFPLATSRYLTLLHEIDAKCVHSMPNLNERIDKFLKKDFNKDHQTQVRLLNNINKIYEELMPSLEEKMHVSSIMLDNLDRLTSRLELAYEVAIKNTEIPRGLRLGVDNHPAMHLHHELMEKIESKSNSKSSQALKSESRREAMAANRRQGEHYSASTHQQDDSKNDANYGGSRHESQDHTGNNTNSRKRANAANTNNADPETKKRKRRVATTAVSPSTISTATAVNNGRIGTSTASRGVSSVGNSNNSRISRPKTNDYGEPLYCYCNQVAYGEMVGCDGADCELEWFHLPCIGLETLPKGKWYCDDCKKKL 3BF7B519E77ED6EF 3BF7B519E77ED6EF ing5_human Inhibitor of growth protein 5 p28ING5 ING5 protein protein human Homo sapiens Human MATAMYLEHYLDSIENLPCELQRNFQLMRELDQRTEDKKAEIDILAAEYISTVKTLSPDQRVERLQKIQNAYSKCKEYSDDKVQLAMQTYEMVDKHIRRLDADLARFEADLKDKMEGSDFESSGGRGLKKGRGQKEKRGSRGRGRRTSEEDTPKKKKHKGGSEFTDTILSVHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCPIEWFHFACVDLTTKPKGKWFCPRCVQEKRKKK DIP protein Q8WYH8 original sequence version: 103 B66DA23209EE9B9E ing4_human Inhibitor of growth protein 4 ING4 p29ING4 My036 protein protein human Homo sapiens Human MAAGMYLEHYLDSIENLPFELQRNFQLMRDLDQRTEDLKAEIDKLATEYMSSARSLSSEEKLALLKQIQEAYGKCKEFGDDKVQLAMQTYEMVDKHIRRLDTDLARFEADLKEKQIESSDYDSSSSKGKKKGRTQKEKKAARARSKGKNSDEEAPKTAQKKLKLVRTSPEYGMPSVTFGSVHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCSIEWFHFACVGLTTKPRGKWFCPRCSQERKKK DIP protein Q9UNL4 original sequence version: 119 CE3FD9CC9F0CE949 ing3_human Inhibitor of growth protein 3 p47ING3 ING3 HSPC301 protein protein human Homo sapiens Human MLYLEDYLEMIEQLPMDLRDRFTEMREMDLQVQNAMDQLEQRVSEFFMNAKKNKPEWREEQMASIKKDYYKALEDADEKVQLANQIYDLVDRHLRKLDQELAKFKMELEADNAGITEILERRSLELDTPSQPVNNHHAHSHTPVEKRKYNPTSHHTTTDHIPEKKFKSEALLSTLTSDASKENTLGCRNNNSTASSNNAYNVNSSQPLGSYNIGSLSSGTGAGAITMAAAQAVQATAQMKEGRRTSSLKASYEAFKNNDFQLGKEFSMARETVGYSSSSALMTTLTQNASSSAADSRSGRKSKNNNKSSSQQSSSSSSSSSLSSCSSSSTVVQEISQQTTVVPESDSNSQVDWTYDPNEPRYCICNQVSYGEMVGCDNQDCPIEWFHYGCVGLTEAPKGKWYCPQCTAAMKRRGSRHK DIP protein Q9NXR8 original sequence version: 113 AA127416912D87F5 h3k4-ing2-1 5 15 unspecified role unspecified role bait bait 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 prerequisite-ptm prerequisite-ptm prerequisite ptm required ptm prerequisite-ptm required-ptm K4me2 K4me2 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 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 12 unspecified role unspecified role prey prey Q9ESK4:p.Tyr215Ala Y215A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning 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 'Y215A'. Wed May 02 19:07:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr215ala' Tue Jun 30 20:17:46 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr215Ala' Q9ESK4:p.[Glu237Ala;Trp238Ala] E237A/W238A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain W A certain certain sequence position certain certain certain sequence position certain E A This feature has been corrected as a result of our quality control procedures. The original label was 'E237A/W238A'. Wed May 02 15:08:44 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu237ala,trp238ala' Tue Jun 30 18:12:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu237Ala;Trp238Ala]' Region 205-265 Region 205-265 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 h3k4-ing5-1 2 18 unspecified role unspecified role unspecified role unspecified role Region 186-235 Region 186-235 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 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 in vitro In vitro direct interaction direct interaction h3k4-ing2-2 10 15 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 in vitro In vitro 12 unspecified role unspecified role unspecified role unspecified role Region 205-265 Region 205-265 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 h3k4-yng2-1 8 13 unspecified role unspecified role unspecified role unspecified role Region 222-271 Region 222-271 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 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 in vitro In vitro direct interaction direct interaction h3k4-ing4-1 6 15 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 in vitro In vitro 19 unspecified role unspecified role unspecified role unspecified role Region 196-245 Region 196-245 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 h3k4-ing3-1 1 20 unspecified role unspecified role unspecified role unspecified role Region 360-409 Region 360-409 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 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 in vitro In vitro direct interaction direct interaction h3k4-ing2-3 11 15 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 in vitro In vitro 12 unspecified role unspecified role unspecified role unspecified role Region 205-265 Region 205-265 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 h3k4-ing1-1 3 14 unspecified role unspecified role unspecified role unspecified role Region 353-402 Region 353-402 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 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 in vitro In vitro direct interaction direct interaction h3k4-ing2-4 7 15 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 K4me2 K4me2 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 K4me1 K4me1 me1lys monomethylated L-lysine Me1Lys Methyl Methylation methylk certain certain sequence position certain certain certain sequence position certain in vitro In vitro 12 unspecified role unspecified role unspecified role unspecified role Q9ESK4:p.[Glu237Ala;Trp238Ala] E237A/W238A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain W A certain certain sequence position certain certain certain sequence position certain E A This feature has been corrected as a result of our quality control procedures. The original label was 'E237A/W238A'. Wed May 02 15:01:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu237ala,trp238ala' Tue Jun 30 20:09:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu237Ala;Trp238Ala]' Q9ESK4:p.[Tyr223Ala;Glu225Ala] Y223A/E225A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain E A 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 'Y223A/E225A'. Wed May 02 17:59:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr223ala,glu225ala' Tue Jun 30 18:46:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Tyr223Ala;Glu225Ala]' Q9ESK4:p.Tyr215Ala Y215A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning 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 'Y215A'. Wed May 02 19:17:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr215ala' Tue Jun 30 20:14:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr215Ala' Q9ESK4:p.Asp230Ala D230A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain D A This feature has been corrected as a result of our quality control procedures. The original label was 'D230A'. Wed May 02 15:30:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp230ala' Tue Jun 30 19:15:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp230Ala' Region 205-265 Region 205-265 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 h3k4-pho23-1 4 17 unspecified role unspecified role unspecified role unspecified role Region 280-329 Region 280-329 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 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 in vitro In vitro direct interaction direct interaction h3k4-yng1-1 9 16 unspecified role unspecified role unspecified role unspecified role Region 155-204 Region 155-204 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 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 in vitro In vitro direct interaction direct interaction