##gff-version 3 Q03164 UniProtKB Chain 1 3969 . . . ID=PRO_0000124876;Note=Histone-lysine N-methyltransferase 2A Q03164 UniProtKB Chain 1 2718 . . . ID=PRO_0000390949;Note=MLL cleavage product N320;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12482972,ECO:0000305|PubMed:14636557;Dbxref=PMID:12482972,PMID:14636557 Q03164 UniProtKB Chain 2719 3969 . . . ID=PRO_0000390950;Note=MLL cleavage product C180;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:12482972,ECO:0000305|PubMed:14636557;Dbxref=PMID:12482972,PMID:14636557 Q03164 UniProtKB Domain 1703 1748 . . . Note=Bromo%3B divergent;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 Q03164 UniProtKB Domain 2018 2074 . . . Note=FYR N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00875 Q03164 UniProtKB Domain 3666 3747 . . . Note=FYR C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00876 Q03164 UniProtKB Domain 3829 3945 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 Q03164 UniProtKB Domain 3953 3969 . . . Note=Post-SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00155 Q03164 UniProtKB DNA binding 169 180 . . . Note=A.T hook 1 Q03164 UniProtKB DNA binding 217 227 . . . Note=A.T hook 2 Q03164 UniProtKB DNA binding 301 309 . . . Note=A.T hook 3 Q03164 UniProtKB Zinc finger 1147 1195 . . . Note=CXXC-type;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00509,ECO:0000269|PubMed:29276034;Dbxref=PMID:29276034 Q03164 UniProtKB Zinc finger 1431 1482 . . . Note=PHD-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 Q03164 UniProtKB Zinc finger 1479 1533 . . . Note=PHD-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 Q03164 UniProtKB Zinc finger 1566 1627 . . . Note=PHD-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 Q03164 UniProtKB Zinc finger 1870 1910 . . . Note=C2HC pre-PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01146 Q03164 UniProtKB Zinc finger 1931 1978 . . . Note=PHD-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01146 Q03164 UniProtKB Region 1 108 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 132 253 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 301 352 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 445 585 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 713 780 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 798 949 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 1038 1066 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 1106 1166 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 1200 1375 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 1584 1600 . . . Note=Interaction with histone H3K4me3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20677832;Dbxref=PMID:20677832 Q03164 UniProtKB Region 1663 1713 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 1806 1869 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 2081 2133 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 2145 2232 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 2275 2333 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 2373 2460 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 2475 2618 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 2647 2675 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 2713 2821 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 2961 3064 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 3166 3244 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 3464 3608 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 3620 3643 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Region 3785 3808 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Motif 6 25 . . . Note=Menin-binding motif (MBM);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22327296;Dbxref=PMID:22327296 Q03164 UniProtKB Motif 123 134 . . . Note=Integrase domain-binding motif 1 (IBM1);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25305204;Dbxref=PMID:25305204 Q03164 UniProtKB Motif 147 152 . . . Note=Integrase domain-binding motif 2 (IBM2);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25305204;Dbxref=PMID:25305204 Q03164 UniProtKB Motif 2847 2855 . . . Note=9aaTAD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17467953;Dbxref=PMID:17467953 Q03164 UniProtKB Motif 3762 3767 . . . Note=WDR5 interaction motif (WIN);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18829459,ECO:0000269|PubMed:22665483;Dbxref=PMID:18829459,PMID:22665483 Q03164 UniProtKB Compositional bias 37 58 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 81 103 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 184 203 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 204 226 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 236 253 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 325 351 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 445 495 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 535 556 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 557 576 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 713 731 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 747 780 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 798 845 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 846 898 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 1046 1061 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 1249 1272 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 1278 1302 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 1303 1317 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 1822 1847 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 2096 2118 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 2146 2174 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 2189 2232 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 2275 2320 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 2402 2418 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 2419 2445 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 2526 2594 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 2721 2746 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 2747 2784 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 2785 2821 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 3011 3064 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 3166 3183 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 3195 3222 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 3230 3244 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 3464 3530 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Compositional bias 3563 3606 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q03164 UniProtKB Binding site 1155 1155 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00509,ECO:0000269|PubMed:29276034,ECO:0007744|PDB:4NW3;Dbxref=PMID:29276034 Q03164 UniProtKB Binding site 1158 1158 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00509,ECO:0000269|PubMed:29276034,ECO:0007744|PDB:4NW3;Dbxref=PMID:29276034 Q03164 UniProtKB Binding site 1161 1161 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00509,ECO:0000269|PubMed:29276034,ECO:0007744|PDB:4NW3;Dbxref=PMID:29276034 Q03164 UniProtKB Binding site 1167 1167 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00509,ECO:0000269|PubMed:29276034,ECO:0007744|PDB:4NW3;Dbxref=PMID:29276034 Q03164 UniProtKB Binding site 1170 1170 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00509,ECO:0000269|PubMed:29276034,ECO:0007744|PDB:4NW3;Dbxref=PMID:29276034 Q03164 UniProtKB Binding site 1173 1173 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00509,ECO:0000269|PubMed:29276034,ECO:0007744|PDB:4NW3;Dbxref=PMID:29276034 Q03164 UniProtKB Binding site 1189 1189 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00509,ECO:0000269|PubMed:29276034,ECO:0007744|PDB:4NW3;Dbxref=PMID:29276034 Q03164 UniProtKB Binding site 1194 1194 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00509,ECO:0000269|PubMed:29276034,ECO:0007744|PDB:4NW3;Dbxref=PMID:29276034 Q03164 UniProtKB Binding site 3839 3839 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00190,ECO:0000269|PubMed:19187761,ECO:0000269|PubMed:26886794,ECO:0007744|PDB:2W5Y,ECO:0007744|PDB:5F5E,ECO:0007744|PDB:5F6L;Dbxref=PMID:19187761,PMID:26886794 Q03164 UniProtKB Binding site 3841 3841 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00190,ECO:0000269|PubMed:19187761,ECO:0000269|PubMed:26886794,ECO:0007744|PDB:2W5Y,ECO:0007744|PDB:5F5E,ECO:0007744|PDB:5F6L;Dbxref=PMID:19187761,PMID:26886794 Q03164 UniProtKB Binding site 3883 3883 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00190,ECO:0000269|PubMed:19187761,ECO:0000269|PubMed:26886794,ECO:0007744|PDB:2W5Z,ECO:0007744|PDB:5F5E;Dbxref=PMID:19187761,PMID:26886794 Q03164 UniProtKB Binding site 3906 3907 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:19187761,ECO:0000269|PubMed:26886794,ECO:0007744|PDB:2W5Y,ECO:0007744|PDB:5F5E,ECO:0007744|PDB:5F6L;Dbxref=PMID:19187761,PMID:26886794 Q03164 UniProtKB Binding site 3909 3909 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16990798,ECO:0000269|PubMed:19187761,ECO:0007744|PDB:2W5Y,ECO:0007744|PDB:2W5Z,ECO:0007744|PDB:5F5E,ECO:0007744|PDB:5F6L;Dbxref=PMID:16990798,PMID:19187761 Q03164 UniProtKB Binding site 3957 3957 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16990798,ECO:0000269|PubMed:19187761,ECO:0007744|PDB:2W5Y,ECO:0007744|PDB:2W5Z,ECO:0007744|PDB:5F5E,ECO:0007744|PDB:5F6L;Dbxref=PMID:16990798,PMID:19187761 Q03164 UniProtKB Binding site 3958 3958 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00190,ECO:0000269|PubMed:19187761,ECO:0000269|PubMed:26886794,ECO:0007744|PDB:2W5Y,ECO:0007744|PDB:5F5E,ECO:0007744|PDB:5F6L;Dbxref=PMID:19187761,PMID:26886794 Q03164 UniProtKB Binding site 3959 3959 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16990798,ECO:0000269|PubMed:19187761,ECO:0007744|PDB:2W5Y,ECO:0007744|PDB:2W5Z,ECO:0007744|PDB:5F5E,ECO:0007744|PDB:5F6L;Dbxref=PMID:16990798,PMID:19187761 Q03164 UniProtKB Binding site 3964 3964 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16990798,ECO:0000269|PubMed:19187761,ECO:0007744|PDB:2W5Y,ECO:0007744|PDB:2W5Z,ECO:0007744|PDB:5F6L;Dbxref=PMID:16990798,PMID:19187761 Q03164 UniProtKB Site 1334 1335 . . . Note=Breakpoint for translocation to form KMT2A-ZFYVE19 oncogene Q03164 UniProtKB Site 1362 1363 . . . Note=Breakpoint for translocation to form KMT2A-AF3P21 and KMT2A-KNL1 oncogenes Q03164 UniProtKB Site 1362 1363 . . . Note=Breakpoint for translocation to form KMT2A-CENPK oncogene Q03164 UniProtKB Site 1362 1362 . . . Note=Breakpoint for translocation to form KMT2A-FRYL fusion protein Q03164 UniProtKB Site 1406 1407 . . . Note=Breakpoint for translocation to form KMT2A-AFF4 fusion protein Q03164 UniProtKB Site 1444 1445 . . . Note=Breakpoint for translocation to form KMT2A-GAS7 oncogene Q03164 UniProtKB Site 1444 1445 . . . Note=Breakpoint for translocation to form KMT2A-LPP Q03164 UniProtKB Site 2666 2667 . . . Note=Cleavage%3B by TASP1%2C site 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14636557;Dbxref=PMID:14636557 Q03164 UniProtKB Site 2718 2719 . . . Note=Cleavage%3B by TASP1%2C site 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14636557;Dbxref=PMID:14636557 Q03164 UniProtKB Site 3765 3765 . . . Note=Important for WDR5-recognition and binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19556245;Dbxref=PMID:19556245 Q03164 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29997176;Dbxref=PMID:29997176 Q03164 UniProtKB Modified residue 142 142 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29997176;Dbxref=PMID:29997176 Q03164 UniProtKB Modified residue 153 153 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:29997176,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231,PMID:29997176 Q03164 UniProtKB Modified residue 197 197 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:20068231 Q03164 UniProtKB Modified residue 239 239 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55200 Q03164 UniProtKB Modified residue 373 373 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55200 Q03164 UniProtKB Modified residue 518 518 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q03164 UniProtKB Modified residue 636 636 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q03164 UniProtKB Modified residue 680 680 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q03164 UniProtKB Modified residue 840 840 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q03164 UniProtKB Modified residue 926 926 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 Q03164 UniProtKB Modified residue 1056 1056 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q03164 UniProtKB Modified residue 1130 1130 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q03164 UniProtKB Modified residue 1235 1235 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q03164 UniProtKB Modified residue 1837 1837 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q03164 UniProtKB Modified residue 1845 1845 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q03164 UniProtKB Modified residue 1858 1858 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19369195,ECO:0007744|PubMed:23186163;Dbxref=PMID:19369195,PMID:23186163 Q03164 UniProtKB Modified residue 2098 2098 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:23186163 Q03164 UniProtKB Modified residue 2147 2147 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q03164 UniProtKB Modified residue 2151 2151 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q03164 UniProtKB Modified residue 2201 2201 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21406692;Dbxref=PMID:21406692 Q03164 UniProtKB Modified residue 2525 2525 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q03164 UniProtKB Modified residue 2611 2611 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q03164 UniProtKB Modified residue 2796 2796 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q03164 UniProtKB Modified residue 2955 2955 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:20068231,PMID:23186163 Q03164 UniProtKB Modified residue 2958 2958 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55200 Q03164 UniProtKB Modified residue 3036 3036 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q03164 UniProtKB Modified residue 3372 3372 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:20068231 Q03164 UniProtKB Modified residue 3462 3462 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55200 Q03164 UniProtKB Modified residue 3511 3511 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q03164 UniProtKB Modified residue 3515 3515 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 Q03164 UniProtKB Modified residue 3527 3527 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q03164 UniProtKB Modified residue 3882 3882 . . . Note=S-methylcysteine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24235145;Dbxref=PMID:24235145 Q03164 UniProtKB Cross-link 2528 2528 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q03164 UniProtKB Alternative sequence 1407 1444 . . . ID=VSP_006666;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7598802;Dbxref=PMID:7598802 Q03164 UniProtKB Alternative sequence 1603 1603 . . . ID=VSP_046879;Note=In isoform 3. S->SGTE;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:10706619,ECO:0000303|PubMed:1423625;Dbxref=PMID:10706619,PMID:1423625 Q03164 UniProtKB Natural variant 30 30 . . . ID=VAR_021317;Note=A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8703835;Dbxref=dbSNP:rs9332745,PMID:8703835 Q03164 UniProtKB Natural variant 53 53 . . . ID=VAR_021318;Note=A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs9332747 Q03164 UniProtKB Natural variant 502 502 . . . ID=VAR_021319;Note=E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs9332772 Q03164 UniProtKB Natural variant 1975 1975 . . . ID=VAR_052652;Note=Q->P;Dbxref=dbSNP:rs693598 Q03164 UniProtKB Natural variant 2319 2319 . . . ID=VAR_021320;Note=S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs9332837 Q03164 UniProtKB Natural variant 2354 2354 . . . ID=VAR_021321;Note=P->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs9332838 Q03164 UniProtKB Natural variant 2387 2387 . . . ID=VAR_021322;Note=Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs9332839 Q03164 UniProtKB Natural variant 3714 3714 . . . ID=VAR_021323;Note=V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs9332859 Q03164 UniProtKB Natural variant 3773 3773 . . . ID=VAR_021324;Note=S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs9332861 Q03164 UniProtKB Mutagenesis 6 6 . . . Note=Reduced interaction with MEN1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22327296;Dbxref=PMID:22327296 Q03164 UniProtKB Mutagenesis 7 7 . . . Note=Reduced interaction with MEN1. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22327296;Dbxref=PMID:22327296 Q03164 UniProtKB Mutagenesis 8 8 . . . Note=Reduced interaction with MEN1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22327296;Dbxref=PMID:22327296 Q03164 UniProtKB Mutagenesis 9 9 . . . Note=Loss of interaction with MEN1. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22327296;Dbxref=PMID:22327296 Q03164 UniProtKB Mutagenesis 9 9 . . . Note=Reduced interaction with MEN1. F->H%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22327296;Dbxref=PMID:22327296 Q03164 UniProtKB Mutagenesis 10 10 . . . Note=Reduced interaction with MEN1. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22327296;Dbxref=PMID:22327296 Q03164 UniProtKB Mutagenesis 11 11 . . . Note=Reduced interaction with MEN1. A->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22327296;Dbxref=PMID:22327296 Q03164 UniProtKB Mutagenesis 12 12 . . . Note=Reduced interaction with MEN1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22327296;Dbxref=PMID:22327296 Q03164 UniProtKB Mutagenesis 13 13 . . . Note=Reduced interaction with MEN1. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22327296;Dbxref=PMID:22327296 Q03164 UniProtKB Mutagenesis 24 24 . . . Note=Reduced interaction with MEN1%3B when associated with E-25. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22327296;Dbxref=PMID:22327296 Q03164 UniProtKB Mutagenesis 25 25 . . . Note=Reduced interaction with MEN1%3B when associated with E-24. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22327296;Dbxref=PMID:22327296 Q03164 UniProtKB Mutagenesis 129 129 . . . Note=Weakly affects interaction with PSIP1 whereas significantly decreases interaction of KMT2A-MEN1 complex with PSIP1. Reduced interaction with PSIP1%3B when associated with A-133. F->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25082813,ECO:0000269|PubMed:25305204;Dbxref=PMID:25082813,PMID:25305204 Q03164 UniProtKB Mutagenesis 132 132 . . . Note=Reduced interaction with PSIP1%3B when associated with A-133. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29997176;Dbxref=PMID:29997176 Q03164 UniProtKB Mutagenesis 133 133 . . . Note=Reduced interaction with PSIP1%3B when associated with A-129 or A-132. F->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25082813,ECO:0000269|PubMed:29997176;Dbxref=PMID:25082813,PMID:29997176 Q03164 UniProtKB Mutagenesis 136 136 . . . Note=Phosphomimetic mutant. Significant increase in interaction with PSIP1%3B when associated with D-142. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29997176;Dbxref=PMID:29997176 Q03164 UniProtKB Mutagenesis 142 142 . . . Note=Phosphomimetic mutant. Significant increase in interaction with PSIP1%3B when associated with D-136. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29997176;Dbxref=PMID:29997176 Q03164 UniProtKB Mutagenesis 144 144 . . . Note=Loss of interaction with PSIP1%3B when associated with Q-146 and A-148. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25082813;Dbxref=PMID:25082813 Q03164 UniProtKB Mutagenesis 146 146 . . . Note=Loss of interaction with PSIP1%3B when associated with Q-144 and A-148. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25082813;Dbxref=PMID:25082813 Q03164 UniProtKB Mutagenesis 148 148 . . . Note=Reduced interaction with PSIP1. Loss of interaction with PSIP1%3B when associated with A-149 or Q-144 and Q-146. F->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25082813,ECO:0000269|PubMed:25305204;Dbxref=PMID:25082813,PMID:25305204 Q03164 UniProtKB Mutagenesis 149 149 . . . Note=Loss of interaction with PSIP1%3B when associated with A-148. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25305204;Dbxref=PMID:25305204 Q03164 UniProtKB Mutagenesis 151 151 . . . Note=Reduced interaction with PSIP1. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25082813;Dbxref=PMID:25082813 Q03164 UniProtKB Mutagenesis 1150 1150 . . . Note=Impairs DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20010842;Dbxref=PMID:20010842 Q03164 UniProtKB Mutagenesis 1151 1151 . . . Note=Impairs DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1153 1153 . . . Note=No effect on stability or DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1154 1154 . . . Note=Impairs DNA-binding. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16990798,ECO:0000269|PubMed:20010842;Dbxref=PMID:16990798,PMID:20010842 Q03164 UniProtKB Mutagenesis 1155 1155 . . . Note=Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1158 1158 . . . Note=Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1161 1161 . . . Note=Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1162 1162 . . . Note=No effect on stability or DNA-binding. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1166 1166 . . . Note=Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1167 1167 . . . Note=Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1170 1170 . . . Note=Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1172 1172 . . . Note=No effect on stability or DNA-binding. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1173 1173 . . . Note=Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1175 1175 . . . Note=Impairs DNA-binding. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1176 1176 . . . Note=Impairs DNA-binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1178 1181 . . . Note=Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. KFGG->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1178 1178 . . . Note=Impairs DNA-binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1179 1179 . . . Note=Impairs DNA-binding. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1183 1183 . . . Note=Impairs DNA-binding. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1185 1185 . . . Note=Impairs DNA-binding. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16990798,ECO:0000269|PubMed:20010842;Dbxref=PMID:16990798,PMID:20010842 Q03164 UniProtKB Mutagenesis 1186 1186 . . . Note=Impairs DNA-binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1187 1187 . . . Note=Impairs DNA-binding. Q->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16990798,ECO:0000269|PubMed:20010842;Dbxref=PMID:16990798,PMID:20010842 Q03164 UniProtKB Mutagenesis 1188 1188 . . . Note=No effect on stability or DNA-binding. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16990798,ECO:0000269|PubMed:20010842;Dbxref=PMID:16990798,PMID:20010842 Q03164 UniProtKB Mutagenesis 1188 1188 . . . Note=Abolishes DNA-binding and increases CpG methylation of the HOXA9 promoter region. Does not lead to the development of leukemia when overexpressed in mice as gene fusion with MLLT3. C->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20010842;Dbxref=PMID:20010842 Q03164 UniProtKB Mutagenesis 1189 1189 . . . Note=Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1192 1192 . . . Note=Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1193 1193 . . . Note=Impairs DNA-binding. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16990798,ECO:0000269|PubMed:20010842;Dbxref=PMID:16990798,PMID:20010842 Q03164 UniProtKB Mutagenesis 1194 1194 . . . Note=Impairs zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1195 1195 . . . Note=No effect on stability or DNA-binding. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1196 1196 . . . Note=No effect on stability or DNA-binding. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16990798;Dbxref=PMID:16990798 Q03164 UniProtKB Mutagenesis 1197 1197 . . . Note=Mildly decreases DNA-binding. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20010842;Dbxref=PMID:20010842 Q03164 UniProtKB Mutagenesis 1200 1200 . . . Note=No effect on DNA-binding. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20010842;Dbxref=PMID:20010842 Q03164 UniProtKB Mutagenesis 1581 1581 . . . Note=Decreases affinity for histone H3K4me3. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20541251;Dbxref=PMID:20541251 Q03164 UniProtKB Mutagenesis 1587 1587 . . . Note=Decreases affinity for histone H3K4me3. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20541251;Dbxref=PMID:20541251 Q03164 UniProtKB Mutagenesis 1594 1594 . . . Note=Abolishes interaction with histone H3K4me3. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20677832;Dbxref=PMID:20677832 Q03164 UniProtKB Mutagenesis 1594 1594 . . . Note=Decreases affinity for histone H3K4me3. W->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20541251;Dbxref=PMID:20541251 Q03164 UniProtKB Mutagenesis 1617 1617 . . . Note=Decreases binding affinity for PPIE. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20677832;Dbxref=PMID:20677832 Q03164 UniProtKB Mutagenesis 1619 1619 . . . Note=May perturb protein folding and thereby decrease binding affinity for PPIE. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20677832;Dbxref=PMID:20677832 Q03164 UniProtKB Mutagenesis 2666 2667 . . . Note=Reduces cleavage without abolishing it. Abolishes cleavage by TASP1%3B when associated with 2718-A--A-2720. DG->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14636557;Dbxref=PMID:14636557 Q03164 UniProtKB Mutagenesis 2718 2720 . . . Note=Abolishes cleavage by TASP1%3B when associated with 2666-A-A-2667. DGV->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12482972,ECO:0000269|PubMed:14636557;Dbxref=PMID:12482972,PMID:14636557 Q03164 UniProtKB Mutagenesis 3763 3763 . . . Note=Increased interaction with WDR5. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22665483;Dbxref=PMID:22665483 Q03164 UniProtKB Mutagenesis 3765 3765 . . . Note=Loss of interaction with the WRAD complex and WDR5. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18840606,ECO:0000269|PubMed:22665483;Dbxref=PMID:18840606,PMID:22665483 Q03164 UniProtKB Mutagenesis 3769 3769 . . . Note=Slight decrease in interaction with WDR5. H->A%2CF;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18840606;Dbxref=PMID:18840606 Q03164 UniProtKB Mutagenesis 3769 3769 . . . Note=Increased interaction with WDR5. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22665483;Dbxref=PMID:22665483 Q03164 UniProtKB Mutagenesis 3858 3858 . . . Note=Impairs methyltransferase activity toward unmodified or monomethylated H3K4me. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19187761;Dbxref=PMID:19187761 Q03164 UniProtKB Mutagenesis 3858 3858 . . . Note=Slightly affects methyltransferase activity toward unmodified or monomethylated H3K4me. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19187761;Dbxref=PMID:19187761 Q03164 UniProtKB Mutagenesis 3861 3861 . . . Note=Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5%3B when associated with L-3867. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26886794;Dbxref=PMID:26886794 Q03164 UniProtKB Mutagenesis 3861 3861 . . . Note=Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5%3B when associated with V-3867. N->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26886794;Dbxref=PMID:26886794 Q03164 UniProtKB Mutagenesis 3864 3864 . . . Note=Disrupts interaction with ASH2L and RBBP5 and nearly abolishes histone methyltransferase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26886794;Dbxref=PMID:26886794 Q03164 UniProtKB Mutagenesis 3867 3867 . . . Note=Slightly affects methyltransferase activity of the enzyme alone%2C while it impairs methyltransferase activity in complex%3B when associated with A-3871. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19187761;Dbxref=PMID:19187761 Q03164 UniProtKB Mutagenesis 3867 3867 . . . Note=Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5%3B when associated with I-3861. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26886794;Dbxref=PMID:26886794 Q03164 UniProtKB Mutagenesis 3867 3867 . . . Note=Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5%3B when associated with T-3861. Q->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26886794;Dbxref=PMID:26886794 Q03164 UniProtKB Mutagenesis 3869 3869 . . . Note=Does not affect methyltransferase activity of the enzyme alone or in complex%3B when associated with A-3872. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19187761;Dbxref=PMID:19187761 Q03164 UniProtKB Mutagenesis 3871 3871 . . . Note=Slightly affects methyltransferase activity of the enzyme alone%2C while it impairs methyltransferase activity in complex%3B when associated with A-3867. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19187761;Dbxref=PMID:19187761 Q03164 UniProtKB Mutagenesis 3872 3872 . . . Note=Does not affect methyltransferase activity of the enzyme alone or in complex%3B when associated with A-3869. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19187761;Dbxref=PMID:19187761 Q03164 UniProtKB Mutagenesis 3874 3874 . . . Note=Affects methyltransferase activity of the enzyme alone%2C while it does not affect methyltransferase activity in complex%3B when associated with A-3878. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19187761;Dbxref=PMID:19187761 Q03164 UniProtKB Mutagenesis 3878 3878 . . . Note=Affects methyltransferase activity of the enzyme alone%2C while it does not affect methyltransferase activity in complex%3B when associated with A-3874. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19187761;Dbxref=PMID:19187761 Q03164 UniProtKB Mutagenesis 3882 3882 . . . Note=Abolished auto-methylation. C->A%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24235145;Dbxref=PMID:24235145 Q03164 UniProtKB Mutagenesis 3906 3906 . . . Note=Loss of the histone H3 methyltransferase activity. Abolishes interaction with S-adenosyl-L-methionine. N->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19556245,ECO:0000269|PubMed:25561738;Dbxref=PMID:19556245,PMID:25561738 Q03164 UniProtKB Mutagenesis 3942 3942 . . . Note=Impairs methyltransferase activity toward unmodified or monomethylated H3K4me. Y->A%2CF;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19187761,ECO:0000269|PubMed:19556245;Dbxref=PMID:19187761,PMID:19556245 Q03164 UniProtKB Mutagenesis 3942 3942 . . . Note=Shifts from a specific monomethyltransferase to a di- and trimethyltransferase activity. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19187761,ECO:0000269|PubMed:19556245;Dbxref=PMID:19187761,PMID:19556245 Q03164 UniProtKB Sequence conflict 144 144 . . . Note=E->ELTTQIPCSWRTKGHIHDKKTEPFRLLAWSWCLN;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 556 556 . . . Note=Q->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 1347 1347 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 1487 1487 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 1490 1490 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 1507 1507 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 1513 1513 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 1600 1600 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 1616 1616 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 1937 1937 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 2181 2181 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 3556 3556 . . . Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 3718 3718 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 3759 3759 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 3813 3813 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Sequence conflict 3901 3901 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q03164 UniProtKB Helix 114 133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U88 Q03164 UniProtKB Beta strand 135 138 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2MTN Q03164 UniProtKB Beta strand 140 145 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6EMQ Q03164 UniProtKB Beta strand 150 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2MSR Q03164 UniProtKB Beta strand 1151 1154 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J2S Q03164 UniProtKB Beta strand 1156 1158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4NW3 Q03164 UniProtKB Helix 1159 1162 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4NW3 Q03164 UniProtKB Beta strand 1168 1170 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4NW3 Q03164 UniProtKB Helix 1171 1175 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4NW3 Q03164 UniProtKB Helix 1177 1179 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4NW3 Q03164 UniProtKB Beta strand 1183 1185 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J2S Q03164 UniProtKB Turn 1190 1192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4NW3 Q03164 UniProtKB Beta strand 1197 1200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J2S Q03164 UniProtKB Turn 1204 1206 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J2S Q03164 UniProtKB Beta strand 1566 1568 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQI Q03164 UniProtKB Turn 1570 1572 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Beta strand 1575 1577 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQI Q03164 UniProtKB Turn 1578 1582 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KYU Q03164 UniProtKB Beta strand 1585 1587 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Turn 1589 1591 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Beta strand 1594 1596 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Helix 1597 1599 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Helix 1604 1612 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Helix 1614 1617 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Turn 1622 1624 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Beta strand 1627 1629 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Helix 1631 1652 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Helix 1655 1661 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Helix 1708 1716 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Helix 1723 1740 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Helix 1745 1765 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Helix 1771 1773 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LQH Q03164 UniProtKB Helix 2847 2855 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5SVH Q03164 UniProtKB Helix 3764 3766 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ESG Q03164 UniProtKB Helix 3796 3799 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W5Y Q03164 UniProtKB Helix 3809 3811 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W5Y Q03164 UniProtKB Helix 3816 3820 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Helix 3823 3830 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Beta strand 3831 3835 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Beta strand 3837 3847 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Beta strand 3854 3857 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Beta strand 3860 3864 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Helix 3865 3867 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Helix 3868 3877 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Beta strand 3884 3886 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Beta strand 3888 3894 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Turn 3896 3898 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Helix 3901 3904 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Beta strand 3912 3920 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Beta strand 3923 3932 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Beta strand 3939 3942 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5F5E Q03164 UniProtKB Helix 3951 3953 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7W67