##gff-version 3 Q9Z148 UniProtKB Chain 1 1263 . . . ID=PRO_0000186069;Note=Histone-lysine N-methyltransferase EHMT2 Q9Z148 UniProtKB Repeat 702 731 . . . Note=ANK 1 Q9Z148 UniProtKB Repeat 737 766 . . . Note=ANK 2 Q9Z148 UniProtKB Repeat 770 799 . . . Note=ANK 3 Q9Z148 UniProtKB Repeat 803 833 . . . Note=ANK 4 Q9Z148 UniProtKB Repeat 837 866 . . . Note=ANK 5 Q9Z148 UniProtKB Repeat 870 899 . . . Note=ANK 6 Q9Z148 UniProtKB Repeat 903 932 . . . Note=ANK 7 Q9Z148 UniProtKB Domain 1025 1088 . . . Note=Pre-SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00157 Q9Z148 UniProtKB Domain 1091 1208 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 Q9Z148 UniProtKB Domain 1217 1233 . . . Note=Post-SET Q9Z148 UniProtKB Region 1 314 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z148 UniProtKB Region 332 439 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z148 UniProtKB Region 621 647 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z148 UniProtKB Region 870 872 . . . Note=Histone H3K9me binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Region 1127 1146 . . . Note=Interaction with histone H3;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Region 1207 1210 . . . Note=Interaction with histone H3;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Compositional bias 256 286 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z148 UniProtKB Compositional bias 332 347 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z148 UniProtKB Compositional bias 348 381 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z148 UniProtKB Compositional bias 391 418 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z148 UniProtKB Binding site 1027 1027 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1027 1027 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1029 1029 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1033 1033 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1033 1033 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1038 1038 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1040 1040 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1070 1070 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1070 1070 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1074 1074 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1076 1076 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1080 1080 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1101 1103 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1138 1138 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 Q9Z148 UniProtKB Binding site 1165 1166 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1168 1168 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1221 1221 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1223 1223 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Binding site 1228 1228 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Site 1120 1120 . . . Note=Histone H3K9me binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z148 UniProtKB Modified residue 40 40 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q9Z148 UniProtKB Modified residue 97 97 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Modified residue 101 101 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Modified residue 193 193 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q9Z148 UniProtKB Modified residue 239 239 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B by EHMT2%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Modified residue 239 239 . . . Note=N6%2CN6-dimethyllysine%3B by EHMT2%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Modified residue 285 285 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Modified residue 294 294 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Modified residue 298 298 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Modified residue 403 403 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Modified residue 465 465 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q9Z148 UniProtKB Modified residue 466 466 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q9Z148 UniProtKB Modified residue 608 608 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Modified residue 1257 1257 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Modified residue 1263 1263 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Cross-link 272 272 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Cross-link 282 282 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Cross-link 687 687 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96KQ7 Q9Z148 UniProtKB Alternative sequence 1 57 . . . ID=VSP_002214;Note=In isoform 2 and isoform 3. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:12130538,ECO:0000303|PubMed:15489334;Dbxref=PMID:12130538,PMID:15489334 Q9Z148 UniProtKB Alternative sequence 58 71 . . . ID=VSP_002215;Note=In isoform 2 and isoform 3. AGLTGPPVPCLPSQ->MAAAAGAAAAAAAE;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:12130538,ECO:0000303|PubMed:15489334;Dbxref=PMID:12130538,PMID:15489334 Q9Z148 UniProtKB Alternative sequence 426 459 . . . ID=VSP_002216;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12130538;Dbxref=PMID:12130538 Q9Z148 UniProtKB Mutagenesis 1120 1120 . . . Note=In GM7%3B defective in methyltransferase activity without affecting DNA methylation%3B when associated with F-1207. Y->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18818694;Dbxref=PMID:18818694 Q9Z148 UniProtKB Mutagenesis 1162 1162 . . . Note=Strongly reduces histone methyltransferase activity. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11316813;Dbxref=PMID:11316813 Q9Z148 UniProtKB Mutagenesis 1165 1168 . . . Note=Abolishes histone methyltransferase activity and subsequent repression. In GM3%3B does not form heterodimer with EHMT1 and is defective in mediating both H3K9me and DNA methylation. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12130538,ECO:0000269|PubMed:18818694;Dbxref=PMID:12130538,PMID:18818694 Q9Z148 UniProtKB Mutagenesis 1165 1166 . . . Note=In GM6%3B does not form heterodimer with EHMT1 and is defective in mediating H3K9me. NH->LE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18818694;Dbxref=PMID:18818694 Q9Z148 UniProtKB Mutagenesis 1168 1168 . . . Note=In GM4%3B defective in methyltransferase activity without affecting DNA methylation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18818694;Dbxref=PMID:18818694 Q9Z148 UniProtKB Mutagenesis 1207 1207 . . . Note=In GM7%3B defective in methyltransferase activity without affecting DNA methylation%3B when associated with V-1120. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18818694;Dbxref=PMID:18818694