IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Structural insights of the specificity and catalysis of a viral histone H3 lysine 27 methyltransferase. Structural insights of the specificity and catalysis of a viral histone H3 lysine 27 methyltransferase. J. Mol. Biol. (0022-2836) 2006 imex curation Qian C., Wang X., Manzur K., Sachchidanand null., Farooq A., Zeng L., Wang R., Zhou MM. Chromatin - Epigenetic interactions resulting in chromatin modulation ming-ming.zhou@mssm.edu 23-JAN-2007: Contacted by JYOTI. orchard Only protein-protein interactions in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as ms participant Identification by mass spectrometry ms participant Qian C., Wang X., Manzur K., Sachchidanand null., Farooq A., Zeng L., Wang R., Zhou MM. Chromatin - Epigenetic interactions resulting in chromatin modulation ming-ming.zhou@mssm.edu Accepted 2007-JAN-10 by ORCHARD. 23-JAN-2007: Contacted by JYOTI. J. Mol. Biol. (0022-2836) 2006 orchard Only protein-protein interactions imex curation Structural insights of the specificity and catalysis of a viral histone H3 lysine 27 methyltransferase. Structural insights of the specificity and catalysis of a viral histone H3 lysine 27 methyltransferase. J. Mol. Biol. (0022-2836) 2006 imex curation Qian C., Wang X., Manzur K., Sachchidanand null., Farooq A., Zeng L., Wang R., Zhou MM. Chromatin - Epigenetic interactions resulting in chromatin modulation ming-ming.zhou@mssm.edu 23-JAN-2007: Contacted by JYOTI. orchard Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Qian C., Wang X., Manzur K., Sachchidanand null., Farooq A., Zeng L., Wang R., Zhou MM. Chromatin - Epigenetic interactions resulting in chromatin modulation ming-ming.zhou@mssm.edu Accepted 2007-JAN-10 by ORCHARD. 23-JAN-2007: Contacted by JYOTI. J. Mol. Biol. (0022-2836) 2006 orchard Only protein-protein interactions imex curation h3_peptide-4 conserved AA 13-33 peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) GKAPRKQLATKAARKSAPATG An amino acid sequence which is not represented in UniProt E0920C5D5052DB29 s-adenosyl-l-homocysteine S-adenosyl-l-homocysteine small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) o41094_pbcv1 A612L protein protein pbcv1 Paramecium bursaria Chlorella virus 1 (PBCV-1) MFNDRVIVKKSPLGGYGVFARKSFEKGELVEECLCIVRHNDDWGTALEDYLFSRKNMSAMALGFGAIFNHSKDPNARHELTAGLKRMRIFTIKPIAIGEEITISYGDDYWLSRPRLTQN DIP protein O41094 original sequence version: 56 9E57A5E72781E13E mek27-vset 2 3 unspecified role unspecified role neutral component neutral component h3 k27 n6me1lys N6-methyl-L-lysine (2S)-2-amino-6-methylaminohexanoic acid MOD_RES N6-methyllysine N(zeta)-methyllysine N6-methyl-L-lysine N6-methylated L-lysine epsilon-methyllysine Methyl Methylation N-methyl Lysyl N6Me1Lys certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 4 unspecified role unspecified role neutral component neutral component 5 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) physical association physical association 1, 2 and table 1 The three-dimensional structure of the tertiary complex of vSET with cofactor SAH and H3-K27me peptide. h3_peptide-vset 1 5 enzyme enzyme unspecified role unspecified role O41094:p.Tyr50Ala mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain Y A Wed May 02 14:57:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr50ala' Tue Jun 30 17:21:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr50Ala' O41094:p.Leu51Ala mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain L A Wed May 02 19:00:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu51ala' Tue Jun 30 15:58:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu51Ala' O41094:p.Tyr50Phe mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain Y F Wed May 02 18:00:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr50phe' Tue Jun 30 16:16:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr50Phe' O41094:p.Phe52Tyr mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain F Y Wed May 02 18:55:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe52tyr' Tue Jun 30 16:50:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe52Tyr' O41094:p.His78Phe mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain H F Wed May 02 17:57:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his78phe' Tue Jun 30 16:19:39 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His78Phe' O41094:p.His78Tyr mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain H Y Wed May 02 19:32:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his78tyr' Tue Jun 30 18:50:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His78Tyr' ecoli Escherichia coli (strain K12) 3 enzyme target enzyme target substrate substrate unspecified role unspecified role chemical synthesis Chemical synthesis (Chemical synthesis) methylation methylation reaction methylation 5, 6 vSET catalyzes consecutive mono, di and tri-methylation of a H3-K27 peptide (residues 15�33) with rate constants of 0.047 min−1, 0.015 min−1 and 0.005 min−1, respectively (Figure 5(b)). Our steady-state kinetics study showed that the apparent Km and kcat for the overall H3-K27 methylation by vSET are 276.2(�20.7) μM and 1.32(�0.03) s−1, Mono, di and tri methylation are observed by Mass spectrometry. Mono, di and tri-methylation of a H3-K27 peptide had rate constants of 0.047 per min, 0.015 per min and 0.005 per min, respectively. Over all Kcat of 1.32 per sec was observed. Tyr50Phe mutation became largely a mono-methylase for H3-K27 with little, if any, di or tri-methylation activity. Phe52Tyr can only mono and di but not tri-methylate H3-K27. Y50F mutation did not affect the mono-methylation with the apparent kinetic parameters being Km of 427.4 MicroMoles and kcat of 1.36 per sec. Kinetic parameters for F52Y were reaction rate of 3.9 MicroMoles.