##gff-version 3 Q8BVE8 UniProtKB Chain 1 1365 . . . ID=PRO_0000259520;Note=Histone-lysine N-methyltransferase NSD2 Q8BVE8 UniProtKB Domain 222 286 . . . Note=PWWP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00162 Q8BVE8 UniProtKB Domain 880 942 . . . Note=PWWP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00162 Q8BVE8 UniProtKB Domain 1011 1061 . . . Note=AWS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00562 Q8BVE8 UniProtKB Domain 1063 1180 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 Q8BVE8 UniProtKB Domain 1187 1203 . . . Note=Post-SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00155 Q8BVE8 UniProtKB DNA binding 453 521 . . . Note=HMG box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267 Q8BVE8 UniProtKB Zinc finger 667 713 . . . Note=PHD-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 Q8BVE8 UniProtKB Zinc finger 714 770 . . . Note=PHD-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 Q8BVE8 UniProtKB Zinc finger 831 875 . . . Note=PHD-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 Q8BVE8 UniProtKB Zinc finger 1239 1286 . . . Note=PHD-type 4%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 Q8BVE8 UniProtKB Region 149 169 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BVE8 UniProtKB Region 373 455 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BVE8 UniProtKB Region 513 567 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BVE8 UniProtKB Region 594 658 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BVE8 UniProtKB Region 1206 1232 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BVE8 UniProtKB Region 1329 1365 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BVE8 UniProtKB Compositional bias 386 400 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BVE8 UniProtKB Compositional bias 519 566 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BVE8 UniProtKB Compositional bias 602 627 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BVE8 UniProtKB Compositional bias 642 656 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BVE8 UniProtKB Binding site 1016 1016 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1018 1018 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1026 1026 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1026 1026 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1032 1032 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1041 1041 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1046 1046 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1052 1052 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1075 1075 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1115 1118 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1141 1142 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1144 1144 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1186 1186 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1191 1191 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1192 1192 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1193 1193 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Binding site 1198 1198 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Modified residue 110 110 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q8BVE8 UniProtKB Modified residue 114 114 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Modified residue 121 121 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q8BVE8 UniProtKB Modified residue 172 172 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Modified residue 376 376 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Modified residue 422 422 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O96028 Q8BVE8 UniProtKB Alternative sequence 1 661 . . . ID=VSP_044420;Note=In isoform RE-IIBP. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:18172012;Dbxref=PMID:18172012 Q8BVE8 UniProtKB Alternative sequence 1 519 . . . ID=VSP_021424;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14621295;Dbxref=PMID:14621295 Q8BVE8 UniProtKB Alternative sequence 520 522 . . . ID=VSP_021425;Note=In isoform 3. NGN->MGM;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14621295;Dbxref=PMID:14621295 Q8BVE8 UniProtKB Alternative sequence 558 558 . . . ID=VSP_021426;Note=In isoform 2 and isoform 3. K->KQ;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14621295,ECO:0000303|PubMed:15489334;Dbxref=PMID:14621295,PMID:15489334 Q8BVE8 UniProtKB Mutagenesis 1117 1117 . . . Note=Reduction in class switch recombination of the immunoglobulin heavy chain in B cells. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23241889;Dbxref=PMID:23241889 Q8BVE8 UniProtKB Mutagenesis 1138 1138 . . . Note=No methyltransferase activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18172012;Dbxref=PMID:18172012 Q8BVE8 UniProtKB Mutagenesis 1142 1142 . . . Note=No methyltransferase activity. H->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19483677;Dbxref=PMID:19483677 Q8BVE8 UniProtKB Mutagenesis 1144 1144 . . . Note=No methyltransferase activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18172012;Dbxref=PMID:18172012 Q8BVE8 UniProtKB Sequence conflict 757 757 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8BVE8 UniProtKB Sequence conflict 1019 1019 . . . Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8BVE8 UniProtKB Sequence conflict 1345 1345 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305