MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Molecular functions of the TLE tetramerization domain in Wnt target gene repression. Molecular functions of the TLE tetramerization domain in Wnt target gene repression. EMBO J. (0261-4189) 2014 imex curation Chodaparambil J.V., Pate K.T., Hepler M.R., Tsai B.P., Muthurajan U.M., Luger K., Waterman M.L., Weis W.I. bill.weis@stanford.edu 21-Jul-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro far western blotting far western blotting Affinity blotting Affinity blotting predetermined predetermined participant predetermined Chodaparambil J.V., Pate K.T., Hepler M.R., Tsai B.P., Muthurajan U.M., Luger K., Waterman M.L., Weis W.I. bill.weis@stanford.edu Accepted 2014-JUL-09 by MARTA EMBO J. (0261-4189) 2014 Only protein-protein interactions imex curation Molecular functions of the TLE tetramerization domain in Wnt target gene repression. Molecular functions of the TLE tetramerization domain in Wnt target gene repression. EMBO J. (0261-4189) 2014 imex curation Chodaparambil J.V., Pate K.T., Hepler M.R., Tsai B.P., Muthurajan U.M., Luger K., Waterman M.L., Weis W.I. bill.weis@stanford.edu 21-Jul-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Chodaparambil J.V., Pate K.T., Hepler M.R., Tsai B.P., Muthurajan U.M., Luger K., Waterman M.L., Weis W.I. bill.weis@stanford.edu Accepted 2014-JUL-09 by MARTA EMBO J. (0261-4189) 2014 Only protein-protein interactions imex curation Molecular functions of the TLE tetramerization domain in Wnt target gene repression. Molecular functions of the TLE tetramerization domain in Wnt target gene repression. EMBO J. (0261-4189) 2014 imex curation Chodaparambil J.V., Pate K.T., Hepler M.R., Tsai B.P., Muthurajan U.M., Luger K., Waterman M.L., Weis W.I. bill.weis@stanford.edu 21-Jul-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Chodaparambil J.V., Pate K.T., Hepler M.R., Tsai B.P., Muthurajan U.M., Luger K., Waterman M.L., Weis W.I. bill.weis@stanford.edu Accepted 2014-JUL-09 by MARTA EMBO J. (0261-4189) 2014 Only protein-protein interactions imex curation Molecular functions of the TLE tetramerization domain in Wnt target gene repression. Molecular functions of the TLE tetramerization domain in Wnt target gene repression. EMBO J. (0261-4189) 2014 imex curation Chodaparambil J.V., Pate K.T., Hepler M.R., Tsai B.P., Muthurajan U.M., Luger K., Waterman M.L., Weis W.I. bill.weis@stanford.edu 21-Jul-2014: Contacted by IntAct-Help. 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 Chodaparambil J.V., Pate K.T., Hepler M.R., Tsai B.P., Muthurajan U.M., Luger K., Waterman M.L., Weis W.I. bill.weis@stanford.edu Accepted 2014-JUL-09 by MARTA EMBO J. (0261-4189) 2014 Only protein-protein interactions imex curation Molecular functions of the TLE tetramerization domain in Wnt target gene repression. Molecular functions of the TLE tetramerization domain in Wnt target gene repression. EMBO J. (0261-4189) 2014 imex curation Chodaparambil J.V., Pate K.T., Hepler M.R., Tsai B.P., Muthurajan U.M., Luger K., Waterman M.L., Weis W.I. bill.weis@stanford.edu 21-Jul-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Chodaparambil J.V., Pate K.T., Hepler M.R., Tsai B.P., Muthurajan U.M., Luger K., Waterman M.L., Weis W.I. bill.weis@stanford.edu Accepted 2014-JUL-09 by MARTA EMBO J. (0261-4189) 2014 Only protein-protein interactions imex curation tle1_human Transducin-like enhancer protein 1 TLE1 Enhancer of split groucho-like protein 1 E(Sp1) homolog protein protein human Homo sapiens Human MFPQSRHPTPHQAAGQPFKFTIPESLDRIKEEFQFLQAQYHSLKLECEKLASEKTEMQRHYVMYYEMSYGLNIEMHKQTEIAKRLNTICAQVIPFLSQEHQQQVAQAVERAKQVTMAELNAIIGQQQLQAQHLSHGHGPPVPLTPHPSGLQPPGIPPLGGSAGLLALSSALSGQSHLAIKDDKKHHDAEHHRDREPGTSNSLLVPDSLRGTDKRRNGPEFSNDIKKRKVDDKDSSHYDSDGDKSDDNLVVDVSNEDPSSPRASPAHSPRENGIDKNRLLKKDASSSPASTASSASSTSLKSKEMSLHEKASTPVLKSSTPTPRSDMPTPGTSATPGLRPGLGKPPAIDPLVNQAAAGLRTPLAVPGPYPAPFGMVPHAGMNGELTSPGAAYASLHNMSPQMSAAAAAAAVVAYGRSPMVGFDPPPHMRVPTIPPNLAGIPGGKPAYSFHVTADGQMQPVPFPPDALIGPGIPRHARQINTLNHGEVVCAVTISNPTRHVYTGGKGCVKVWDISHPGNKSPVSQLDCLNRDNYIRSCKLLPDGCTLIVGGEASTLSIWDLAAPTPRIKAELTSSAPACYALAISPDSKVCFSCCSDGNIAVWDLHNQTLVRQFQGHTDGASCIDISNDGTKLWTGGLDNTVRSWDLREGRQLQQHDFTSQIFSLGYCPTGEWLAVGMESSNVEVLHVNKPDKYQLHLHESCVLSLKFAYCGKWFVSTGKDNLLNAWRTPYGASIFQSKESSSVLSCDISVDDKYIVTGSGDKKATVYEVIY DIP protein Q04724 original sequence version: 119 695FD1A37410EFE5 ctnb1_mouse Catenin beta-1 Beta-catenin Ctnnb1 Catnb protein protein mouse Mus musculus Mouse MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEALGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL DIP protein Q02248 original sequence version: 128 DIP protein Q02248 original sequence version: 135 DIP protein Q02248 original sequence version: 147 DIP protein Q02248 original sequence version: 187 DIP protein Q02248 original sequence version: 140 D708F170A3FBED6E h4_human Histone H4 H4-16 H4C1 H4C11 H4C12 H4C13 H4C14 H4C15 H4C2 H4C3 H4C4 H4C5 H4C6 H4C8 H4C9 H4/A H4/B H4/C H4/D H4/E H4/G H4/H H4/I H4/J H4/K H4/M H4/N H4/O H4F2 H4FA H4FB H4FC H4FD H4FE H4FG H4FH H4FI H4FJ H4FK H4FM H4FN H4FO HIST1H4A HIST1H4B HIST1H4C HIST1H4D HIST1H4E HIST1H4F HIST1H4H HIST1H4I HIST1H4J HIST1H4K HIST1H4L HIST2H4 HIST2H4A HIST2H4B HIST4H4 protein protein human Homo sapiens Human MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG DIP protein P62805 original sequence version: 68 DIP protein P62805 original sequence version: 111 DIP protein P62805 original sequence version: 94 DIP protein P62805 original sequence version: 97 DIP protein P62805 original sequence version: 116 DIP protein P62805 original sequence version: 105 DIP protein P62805 original sequence version: 120 DIP protein P62805 original sequence version: 144 DIP protein P62805 original sequence version: 150 DIP protein P62805 original sequence version: 154 DIP protein P62805 original sequence version: 156 DIP protein P62805 original sequence version: 112 DIP protein P62805 original sequence version: 121 DIP protein P62805 original sequence version: 123 DIP protein P62805 original sequence version: 126 DIP protein P62805 original sequence version: 132 DIP protein P62805 original sequence version: 136 DIP protein P62805 original sequence version: 119 A9E5DFD3F8B97598 itf2_human Transcription factor 4 Immunoglobulin transcription factor 2 SL3-3 enhancer factor 2 ITF2 SEF2 TCF4 BHLHB19 Class B basic helix-loop-helix protein 19 protein protein human Homo sapiens Human MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQGCHQQSLLGGDMDMGNPGTLSPTKPGSQYYQYSSNNPRRRPLHSSAMEVQTKKVRKVPPGLPSSVYAPSASTADYNRDSPGYPSSKPATSTFPSSFFMQDGHHSSDPWSSSSGMNQPGYAGMLGNSSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGSGAAGSSQTGDALGKALASIYSPDHTNNSFSSNPSTPVGSPPSLSAGTAVWSRNGGQASSSPNYEGPLHSLQSRIEDRLERLDDAIHVLRNHAVGPSTAMPGGHGDMHGIIGPSHNGAMGGLGSGYGTGLLSANRHSLMVGTHREDGVALRGSHSLLPNQVPVPQLPVQSATSPDLNPPQDPYRGMPPGLQGQSVSSGSSEIKSDDEGDENLQDTKSSEDKKLDDDKKDIKSITSNNDDEDLTPEQKAEREKERRMANNARERLRVRDINEAFKELGRMVQLHLKSDKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSSEPPPLSLAGPHPGMGDASNHMGQM DIP protein P15884 original sequence version: 159 DIP protein P15884 original sequence version: 93 DIP protein P15884 original sequence version: 116 53459FC7989D9487 t7l1a_xenla Transcription factor 7-like 1-A tcf7l1-a tcf3 tcf3a HMG box transcription factor 3-A protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MPQLNSGGGDELGANDELIRFKDEGEQEEKSPGEGSAEGDLADVKSSLVNESENHSSDSDSEVERRPPPREAFEKHRDYLTEALRRQQDAAFFKGPPYAGYPFLMIPDLGGHYLPNGALSPSARTYLQMKWPLLDSPSTAGLKDARSPSPAHLSNKVPVVQHPHHMHPLTPLITYSNEHFSPGTPPGHLSPEIDPKTGIPRPPHPSELSPYYPLSPGAVGQIPHPLGWLVPPQGQPMYSIPPGGFRHPYPALAMNASMSSLVSSRFSPHMVPPPHHSLHTSGIPHPAIVSPIVKQEPSSGNISPNLHTKSNMIVKKEEEKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHSLSREEQAKYYELARKERQLHSQLYPSWSARDNYGKRKKRKREKQSPEMETHTKTKKMCVQHLPADKSCDSPASSHGSMLDSPATPSAALASPAAPAATHSEQAQPLSLTTKPEARAQLSLSHSAAFLASKSPSSSSFSGHLSSPVGSPLLSRPIPLTSSILSPSGVFPSALQALPLLQAQPLSLVTKSSD 90B24D134AE4EBDD tle1-1 4 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction st1 sf1a f1 tle1-1 3 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f1f The dimer-dimer interaction is mediated by hydrophobic side chains and buries 3,320 A2 of surface area. We confirmed that this unusual N-terminally interdigitated dimer of dimers is the solution structure by small-angle X-ray scattering (Fig 1F). tle1-1 2 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f1g The L26D/I29D mutant eluted from a size-exclusion chromatography column at a reduced apparent molecular weight corresponding to a prolate dimer relative to the wild-type tetramer (Fig 1G), and we therefore desginate this mutant the TLE120–156 dimer. tle1-1 2 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q04724:p.[Leu26Asp;Ile29Asp] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L D certain certain sequence position certain certain certain sequence position certain I D Wed May 02 16:37:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu26asp,ile29asp' Tue Jun 30 16:06:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu26Asp;Ile29Asp]' direct interaction direct interaction f1g The L26D/I29D mutant eluted from a size-exclusion chromatography column at a reduced apparent molecular weight corresponding to a prolate dimer relative to the wild-type tetramer (Fig 1G), and we therefore desginate this mutant the TLE120–156 dimer. tcf7l1_a-tle1 5 10 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f2c t1 f3b We used fluorescence anisotropy of labeled TLE120–156 to measure its affinity for purified mLEF1, hTCF1, xTCF3 and hTCF4 constructs lacking their HMG domains, a separate region that does not contribute to TLE interactions (Arce et al, 2009). TLE120-156 binds to TCF3 and TCF4 with KDs of 16 lm and 34 lM respectively, whereas it binds LEF1 and TCF1 with KDs of 195 lM and 1 mM (Fig 2C, Table 1). The TLE120–156 L26D/I29D mutant selectively disrupts the tetramer without destroying the dimeric building block (Fig 1G), so we tested whether the dimer can still interact with TCF/LEF proteins. TLE120–156 mutant dimer binds to TCF3 and TCF4 with the same affinity as the wild-type tetramer (Fig 3B). This demonstrates that the dimer confers full binding to TCF3 and TCF4, and it suggests that the stoichiometry of TLE-TCF interaction is unlikely to be 4:1 TLE:TCF as reported (Daniels & Weis, 2005). tcf4-tcf7l1_a 5 9 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f2c t1 f3b We used fluorescence anisotropy of labeled TLE120–156 to measure its affinity for purified mLEF1, hTCF1, xTCF3 and hTCF4 constructs lacking their HMG domains, a separate region that does not contribute to TLE interactions (Arce et al, 2009). TLE120-156 binds to TCF3 and TCF4 with KDs of 16 lm and 34 lM respectively, whereas it binds LEF1 and TCF1 with KDs of 195 lM and 1 mM (Fig 2C, Table 1). The TLE120–156 L26D/I29D mutant selectively disrupts the tetramer without destroying the dimeric building block (Fig 1G), so we tested whether the dimer can still interact with TCF/LEF proteins. TLE120–156 mutant dimer binds to TCF3 and TCF4 with the same affinity as the wild-type tetramer (Fig 3B). This demonstrates that the dimer confers full binding to TCF3 and TCF4, and it suggests that the stoichiometry of TLE-TCF interaction is unlikely to be 4:1 TLE:TCF as reported (Daniels & Weis, 2005). ctnnb1-tcf7l1_a-1 5 10 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 7 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association f3a Since the binding affinity is only 16 lM, we purified the b-catenin-TCF31–330 complex (KDs for b-catenin binding to the highly homologous LEF1 1–131 and TCF4 1–53 are 10 and 20 nM, respectively (Daniels and Weis, 2005; Fasolini et al, 2003; Sun and Weis, 2011)), and titrated increasing concentrations of this complex into labeled TLE120–156. The affinity of TLE120–156 for the b-catenin–TCF3 complex was 14 1 lM, essentially the same as the TLE120–156-TCF3 interaction (Fig 3A). These data demonstrate that there is no competition between b-catenin and TLE120–156 and, consistent with the domain mapping data (Table 1), that the binding regions for b-catenin and TLE120–156 on TCF3 are independent of one another. tcf7l1_a-tle1-1 1 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 8 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f4c The binding of synthetic biotinylated histone tails to the TLE120–156 tetramer and dimer mutant was analyzed using native gel shifts to obtain relative binding affinities. The TLE120–156 tetramer bound to unmodified H4 and H4 trimethylated at lysine 20 (H4K20Me3; associated with heterochromatin) tails with apparent KDs of 42 and 13 lM, respectively (Fig 4C). The dimer also bound to these tails (Fig 4D). Binding to H2A, H2B and H3 was significantly weaker for both the tetramer and dimer (Fig 4C and D). hist1h4a-tle1 1 8 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q04724:p.[Leu26Asp;Ile29Asp] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L D certain certain sequence position certain certain certain sequence position certain I D Wed May 02 16:42:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu26asp,ile29asp' Tue Jun 30 15:55:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu26Asp;Ile29Asp]' direct interaction direct interaction f4d The binding of synthetic biotinylated histone tails to the TLE120–156 tetramer and dimer mutant was analyzed using native gel shifts to obtain relative binding affinities. The TLE120–156 tetramer bound to unmodified H4 and H4 trimethylated at lysine 20 (H4K20Me3; associated with heterochromatin) tails with apparent KDs of 42 and 13 lM, respectively (Fig 4C). The dimer also bound to these tails (Fig 4D). Binding to H2A, H2B and H3 was significantly weaker for both the tetramer and dimer (Fig 4C and D). hist1h4a-tle1-1 1 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Q04724:p.[Leu26Asp;Ile29Asp] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L D certain certain sequence position certain certain certain sequence position certain I D Wed May 02 17:57:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu26asp,ile29asp' Tue Jun 30 18:40:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu26Asp;Ile29Asp]' range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 8 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain lys(me3)20 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 direct interaction direct interaction f4d The binding of synthetic biotinylated histone tails to the TLE120–156 tetramer and dimer mutant was analyzed using native gel shifts to obtain relative binding affinities. The TLE120–156 tetramer bound to unmodified H4 and H4 trimethylated at lysine 20 (H4K20Me3; associated with heterochromatin) tails with apparent KDs of 42 and 13 lM, respectively (Fig 4C). The dimer also bound to these tails (Fig 4D). Binding to H2A, H2B and H3 was significantly weaker for both the tetramer and dimer (Fig 4C and D). hist1h4a-tle1-2 1 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 8 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified lys(me3)20 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 range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f4c The binding of synthetic biotinylated histone tails to the TLE120–156 tetramer and dimer mutant was analyzed using native gel shifts to obtain relative binding affinities. The TLE120–156 tetramer bound to unmodified H4 and H4 trimethylated at lysine 20 (H4K20Me3; associated with heterochromatin) tails with apparent KDs of 42 and 13 lM, respectively (Fig 4C). The dimer also bound to these tails (Fig 4D). Binding to H2A, H2B and H3 was significantly weaker for both the tetramer and dimer (Fig 4C and D). hist1h4a-tle1-3 1 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Q04724:p.[Leu26Asp;Ile29Asp] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L D certain certain sequence position certain certain certain sequence position certain I D Wed May 02 17:03:01 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu26asp,ile29asp' Tue Jun 30 16:10:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu26Asp;Ile29Asp]' range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 8 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain acres ac1res monoacetylated residue Acetyl Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac) Acetylation Ac1Res undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined direct interaction direct interaction f4d The binding of synthetic biotinylated histone tails to the TLE120–156 tetramer and dimer mutant was analyzed using native gel shifts to obtain relative binding affinities. The TLE120–156 tetramer bound to unmodified H4 and H4 trimethylated at lysine 20 (H4K20Me3; associated with heterochromatin) tails with apparent KDs of 42 and 13 lM, respectively (Fig 4C). The dimer also bound to these tails (Fig 4D). Binding to H2A, H2B and H3 was significantly weaker for both the tetramer and dimer (Fig 4C and D). hist1h4a-tle1-4 1 8 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain acres ac1res monoacetylated residue Acetyl Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac) Acetylation Ac1Res undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 6 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f4c The binding of synthetic biotinylated histone tails to the TLE120–156 tetramer and dimer mutant was analyzed using native gel shifts to obtain relative binding affinities. The TLE120–156 tetramer bound to unmodified H4 and H4 trimethylated at lysine 20 (H4K20Me3; associated with heterochromatin) tails with apparent KDs of 42 and 13 lM, respectively (Fig 4C). The dimer also bound to these tails (Fig 4D). Binding to H2A, H2B and H3 was significantly weaker for both the tetramer and dimer (Fig 4C and D).