##gff-version 3 Q9H165 UniProtKB Chain 1 835 . . . ID=PRO_0000047102;Note=B-cell lymphoma/leukemia 11A Q9H165 UniProtKB Zinc finger 170 193 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q9H165 UniProtKB Zinc finger 377 399 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q9H165 UniProtKB Zinc finger 405 429 . . . Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q9H165 UniProtKB Zinc finger 742 764 . . . Note=C2H2-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q9H165 UniProtKB Zinc finger 770 792 . . . Note=C2H2-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q9H165 UniProtKB Zinc finger 800 823 . . . Note=C2H2-type 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 Q9H165 UniProtKB Region 1 210 . . . Note=Required for nuclear body formation and for SUMO1 recruitment;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9H165 UniProtKB Region 1 41 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H165 UniProtKB Region 323 376 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H165 UniProtKB Region 421 458 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H165 UniProtKB Region 471 512 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H165 UniProtKB Region 572 619 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H165 UniProtKB Region 678 740 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H165 UniProtKB Compositional bias 11 39 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H165 UniProtKB Compositional bias 351 374 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H165 UniProtKB Compositional bias 436 458 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H165 UniProtKB Compositional bias 479 508 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H165 UniProtKB Compositional bias 572 600 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H165 UniProtKB Compositional bias 679 699 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H165 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9QYE3 Q9H165 UniProtKB Modified residue 205 205 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19369195;Dbxref=PMID:19369195 Q9H165 UniProtKB Modified residue 271 271 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9QYE3 Q9H165 UniProtKB Modified residue 332 332 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 Q9H165 UniProtKB Modified residue 337 337 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9QYE3 Q9H165 UniProtKB Modified residue 446 446 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9QYE3 Q9H165 UniProtKB Modified residue 447 447 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9QYE3 Q9H165 UniProtKB Modified residue 608 608 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19369195;Dbxref=PMID:19369195 Q9H165 UniProtKB Modified residue 625 625 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 Q9H165 UniProtKB Modified residue 630 630 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 Q9H165 UniProtKB Modified residue 701 701 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 Q9H165 UniProtKB Cross-link 123 123 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25755297,ECO:0007744|PubMed:28112733;Dbxref=PMID:25755297,PMID:28112733 Q9H165 UniProtKB Cross-link 164 164 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q9H165 UniProtKB Cross-link 620 620 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q9H165 UniProtKB Cross-link 634 634 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9QYE3 Q9H165 UniProtKB Cross-link 833 833 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25755297,ECO:0007744|PubMed:28112733;Dbxref=PMID:25755297,PMID:28112733 Q9H165 UniProtKB Alternative sequence 129 163 . . . ID=VSP_009548;Note=In isoform 6. DKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGIC->G;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.2 Q9H165 UniProtKB Alternative sequence 129 142 . . . ID=VSP_058656;Note=In isoform 7. DKLLHWRGLSSPRS->AQTELEDVFVYLMV Q9H165 UniProtKB Alternative sequence 143 835 . . . ID=VSP_058657;Note=In isoform 7. Missing Q9H165 UniProtKB Alternative sequence 212 243 . . . ID=VSP_009550;Note=In isoform 3. GIPSGLGAECPSQPPLHGIHIADNNPFNLLRI->LHTPPFGVVPRELKMCGSFRMEAREPLSSEKI;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11719382;Dbxref=PMID:11719382 Q9H165 UniProtKB Alternative sequence 244 835 . . . ID=VSP_009552;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11719382;Dbxref=PMID:11719382 Q9H165 UniProtKB Alternative sequence 745 773 . . . ID=VSP_009554;Note=In isoform 2. EYCGKVFKNCSNLTVHRRSHTGERPYKCE->SSHTPIRRSTQRAQDVWQFSDGSSRALKF;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:11347906,ECO:0000303|PubMed:11719382,ECO:0000303|PubMed:15489334;Dbxref=PMID:11347906,PMID:11719382,PMID:15489334 Q9H165 UniProtKB Alternative sequence 774 835 . . . ID=VSP_009555;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:11347906,ECO:0000303|PubMed:11719382,ECO:0000303|PubMed:15489334;Dbxref=PMID:11347906,PMID:11719382,PMID:15489334 Q9H165 UniProtKB Natural variant 47 47 . . . ID=VAR_076921;Note=In IDPFH%3B de novo mutation%3B loss of function in transactivation of transcription%3B reduces the interaction between isoform 2 and isoform 3%3B disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3%3B does not affect the interaction of isoform 2 with TBR1. T->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27453576,ECO:0000269|PubMed:30250039;Dbxref=dbSNP:rs886037864,PMID:27453576,PMID:30250039 Q9H165 UniProtKB Natural variant 48 48 . . . ID=VAR_076922;Note=In IDPFH%3B de novo mutation%3B loss of function in transactivation of transcription%3B reduces the interaction between isoform 2 and isoform 3%3B disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3%3B does not affect the interaction of isoform 2 with TBR1. C->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27453576,ECO:0000269|PubMed:30250039;Dbxref=dbSNP:rs886037865,PMID:27453576,PMID:30250039 Q9H165 UniProtKB Natural variant 66 66 . . . ID=VAR_076923;Note=In IDPFH%3B de novo mutation%3B loss of function in transactivation of transcription%3B reduces the interaction between isoform 2 and isoform 3%3B disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3%3B does not affect the interaction of isoform 2 with TBR1. H->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27453576,ECO:0000269|PubMed:30250039;Dbxref=dbSNP:rs886037866,PMID:27453576,PMID:30250039 Q9H165 UniProtKB Natural variant 142 142 . . . ID=VAR_035553;Note=In a breast cancer sample%3B somatic mutation. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=PMID:16959974 Q9H165 UniProtKB Sequence conflict 119 119 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H165 UniProtKB Sequence conflict 316 316 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H165 UniProtKB Sequence conflict 386 386 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H165 UniProtKB Sequence conflict 522 532 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H165 UniProtKB Sequence conflict 648 648 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H165 UniProtKB Sequence conflict 653 653 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H165 UniProtKB Sequence conflict 730 730 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H165 UniProtKB Helix 739 742 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U9Q Q9H165 UniProtKB Turn 745 747 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U9Q Q9H165 UniProtKB Beta strand 750 753 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6KI6 Q9H165 UniProtKB Helix 754 765 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U9Q Q9H165 UniProtKB Beta strand 773 776 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U9Q Q9H165 UniProtKB Beta strand 778 781 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U9Q Q9H165 UniProtKB Helix 782 789 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U9Q Q9H165 UniProtKB Helix 790 792 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U9Q Q9H165 UniProtKB Beta strand 795 797 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U9Q Q9H165 UniProtKB Turn 803 805 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U9Q Q9H165 UniProtKB Beta strand 808 811 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U9Q Q9H165 UniProtKB Helix 812 822 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U9Q Q9H165 UniProtKB Natural variant 47 47 . . . ID=VAR_082936;Note=In IDPFH%2C de novo mutation%2C loss of function in transactivation of transcription%2C reduces the interaction between isoform 2 and isoform 3%2C disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3. T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305;Dbxref=dbSNP:rs886037864 Q9H165 UniProtKB Natural variant 48 48 . . . ID=VAR_082937;Note=In IDPFH%2C de novo mutation%2C loss of function in transactivation of transcription%2C reduces the interaction between isoform 2 and isoform 3%2C disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3. C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305;Dbxref=dbSNP:rs886037865 Q9H165 UniProtKB Natural variant 66 66 . . . ID=VAR_082938;Note=In IDPFH%2C de novo mutation%2C loss of function in transactivation of transcription%2C reduces the interaction between isoform 2 and isoform 3%2C disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3. H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305;Dbxref=dbSNP:rs886037866 Q9H165 UniProtKB Natural variant 47 47 . . . ID=VAR_082939;Note=In IDPFH%2C de novo mutation%2C loss of function transactivation of transcription%2C reduces the interaction between isoform 2 and isoform 3%2C disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3%2C does not affect the interaction of isoform 2 with TBR1. T->P;Ontology_term=ECO:0000305;evidence=ECO:0000305;Dbxref=dbSNP:rs886037864 Q9H165 UniProtKB Natural variant 48 48 . . . ID=VAR_082940;Note=In IDPFH%2C de novo mutation%2C loss of function in transactivation of transcription%2C reduces the interaction between isoform 2 and isoform 3%2C disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3%2C does not affect the interaction of isoform 2 with TBR1. C->F;Ontology_term=ECO:0000305;evidence=ECO:0000305;Dbxref=dbSNP:rs886037865 Q9H165 UniProtKB Natural variant 66 66 . . . ID=VAR_082941;Note=In IDPFH%2C de novo mutation%2C loss of function in transactivation of transcription%2C reduces the interaction between isoform 2 and isoform 3%2C disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3%2C does not affect the interaction of isoform 2 with TBR1. H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305;Dbxref=dbSNP:rs886037866 Q9H165 UniProtKB Cross-link 123 123 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733