##gff-version 3 Q9Z330 UniProtKB Chain 1 1622 . . . ID=PRO_0000088036;Note=DNA (cytosine-5)-methyltransferase 1 Q9Z330 UniProtKB Domain 16 109 . . . Note=DMAP1-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01260 Q9Z330 UniProtKB Domain 759 884 . . . Note=BAH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00370 Q9Z330 UniProtKB Domain 977 1105 . . . Note=BAH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00370 Q9Z330 UniProtKB Repeat 1114 1115 . . . Note=1 Q9Z330 UniProtKB Repeat 1116 1117 . . . Note=2 Q9Z330 UniProtKB Repeat 1118 1119 . . . Note=3 Q9Z330 UniProtKB Repeat 1120 1121 . . . Note=4 Q9Z330 UniProtKB Repeat 1122 1123 . . . Note=5 Q9Z330 UniProtKB Repeat 1124 1125 . . . Note=6 Q9Z330 UniProtKB Repeat 1126 1127 . . . Note=7%3B approximate Q9Z330 UniProtKB Domain 1144 1603 . . . Note=SAM-dependent MTase C5-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01016 Q9Z330 UniProtKB Zinc finger 650 696 . . . Note=CXXC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00509 Q9Z330 UniProtKB Region 1 342 . . . Note=Interaction with the PRC2/EED-EZH2 complex;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z330 UniProtKB Region 1 145 . . . Note=Interaction with DNMT3A;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z330 UniProtKB Region 100 360 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z330 UniProtKB Region 146 213 . . . Note=Interaction with DNMT3B;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z330 UniProtKB Region 304 610 . . . Note=Interaction with the PRC2/EED-EZH2 complex;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z330 UniProtKB Region 327 556 . . . Note=DNA replication foci-targeting sequence Q9Z330 UniProtKB Region 697 758 . . . Note=Autoinhibitory linker Q9Z330 UniProtKB Region 702 733 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z330 UniProtKB Region 1099 1138 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z330 UniProtKB Region 1114 1127 . . . Note=7 X 2 AA tandem repeats of K-G Q9Z330 UniProtKB Region 1126 1622 . . . Note=Interaction with the PRC2/EED-EZH2 complex;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z330 UniProtKB Region 1144 1622 . . . Note=Catalytic Q9Z330 UniProtKB Motif 173 200 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Z330 UniProtKB Compositional bias 144 168 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z330 UniProtKB Compositional bias 171 224 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z330 UniProtKB Compositional bias 232 328 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z330 UniProtKB Compositional bias 1124 1138 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z330 UniProtKB Active site 1231 1231 . . . Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01016,ECO:0000255|PROSITE-ProRule:PRU10018 Q9Z330 UniProtKB Binding site 359 359 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z330 UniProtKB Binding site 362 362 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z330 UniProtKB Binding site 420 420 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z330 UniProtKB Binding site 424 424 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z330 UniProtKB Binding site 657 657 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00509 Q9Z330 UniProtKB Binding site 660 660 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00509 Q9Z330 UniProtKB Binding site 663 663 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00509 Q9Z330 UniProtKB Binding site 668 668 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00509 Q9Z330 UniProtKB Binding site 671 671 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00509 Q9Z330 UniProtKB Binding site 674 674 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00509 Q9Z330 UniProtKB Binding site 690 690 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00509 Q9Z330 UniProtKB Binding site 695 695 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00509 Q9Z330 UniProtKB Binding site 1151 1151 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13864 Q9Z330 UniProtKB Binding site 1155 1156 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13864 Q9Z330 UniProtKB Binding site 1173 1174 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Binding site 1195 1196 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13864 Q9Z330 UniProtKB Binding site 1196 1196 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Binding site 1582 1582 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Binding site 1584 1584 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13864 Q9Z330 UniProtKB Site 515 515 . . . Note=Important for activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z330 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 Q9Z330 UniProtKB Modified residue 70 70 . . . Note=N6%2CN6-dimethyllysine%3B by EHMT2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 138 138 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13864 Q9Z330 UniProtKB Modified residue 139 139 . . . Note=N6-methyllysine%3B by SETD7;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 140 140 . . . Note=Phosphoserine%3B by PKB/AKT1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 151 151 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 163 163 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 169 169 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 304 304 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 Q9Z330 UniProtKB Modified residue 372 372 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 400 400 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 515 515 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13864 Q9Z330 UniProtKB Modified residue 555 555 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 718 718 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 Q9Z330 UniProtKB Modified residue 736 736 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 753 753 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 882 882 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 895 895 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 961 961 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 980 980 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 1116 1116 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 1118 1118 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 1120 1120 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 1122 1122 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 1124 1124 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13864 Q9Z330 UniProtKB Modified residue 1126 1126 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13864 Q9Z330 UniProtKB Modified residue 1354 1354 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Modified residue 1436 1436 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 Q9Z330 UniProtKB Cross-link 1613 1613 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26358 Q9Z330 UniProtKB Alternative sequence 1 118 . . . ID=VSP_005620;Note=In isoform 9. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z330 UniProtKB Alternative sequence 1202 1410 . . . ID=VSP_005622;Note=In isoform 6. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z330 UniProtKB Alternative sequence 1216 1504 . . . ID=VSP_005623;Note=In isoform 8. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z330 UniProtKB Alternative sequence 1218 1430 . . . ID=VSP_005621;Note=In isoform 5. QKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFRRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITMRDTMSDLPEIQNGASAPEISYKWRATVLVPEAAARVALPAHPQGPYPQVHERAGGCRM->VC;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z330 UniProtKB Alternative sequence 1226 1477 . . . ID=VSP_005624;Note=In isoform 4. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z330 UniProtKB Alternative sequence 1252 1482 . . . ID=VSP_005625;Note=In isoform 3. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z330 UniProtKB Alternative sequence 1259 1481 . . . ID=VSP_005626;Note=In isoform 7. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z330 UniProtKB Alternative sequence 1323 1403 . . . ID=VSP_005627;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z330 UniProtKB Sequence conflict 17 25 . . . Note=AGSLPDHVR->RQARPRPCP;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z330 UniProtKB Sequence conflict 189 189 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z330 UniProtKB Sequence conflict 1276 1276 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z330 UniProtKB Sequence conflict 1300 1300 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z330 UniProtKB Sequence conflict 1372 1372 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z330 UniProtKB Sequence conflict 1394 1428 . . . Note=KWRATVLVPEAAARVALPAHPQGPYPQVHERAGGC->NGEPQSWFQRQLRGSHYQPILRDHICKDMSALVAA;Ontology_term=ECO:0000305;evidence=ECO:0000305