##gff-version 3 Q13435 UniProtKB Chain 1 895 . . . ID=PRO_0000174328;Note=Splicing factor 3B subunit 2 Q13435 UniProtKB Domain 24 58 . . . Note=SAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00186 Q13435 UniProtKB Region 1 24 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Region 65 136 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Region 197 373 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Region 400 453 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Region 401 550 . . . Note=Required for interaction with PRMT9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25737013;Dbxref=PMID:25737013 Q13435 UniProtKB Region 691 757 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Region 844 895 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Coiled coil 140 199 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q13435 UniProtKB Compositional bias 10 24 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Compositional bias 84 136 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Compositional bias 225 251 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Compositional bias 278 300 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Compositional bias 322 338 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Compositional bias 344 359 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Compositional bias 400 429 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Compositional bias 695 712 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Compositional bias 713 732 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13435 UniProtKB Modified residue 222 222 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q13435 UniProtKB Modified residue 245 245 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q13435 UniProtKB Modified residue 247 247 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q13435 UniProtKB Modified residue 275 275 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q13435 UniProtKB Modified residue 289 289 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17525332,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:17525332,PMID:18669648,PMID:23186163 Q13435 UniProtKB Modified residue 298 298 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q13435 UniProtKB Modified residue 307 307 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231,PMID:23186163 Q13435 UniProtKB Modified residue 309 309 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231,PMID:23186163 Q13435 UniProtKB Modified residue 311 311 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:18669648,PMID:23186163,PMID:24275569 Q13435 UniProtKB Modified residue 317 317 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q13435 UniProtKB Modified residue 360 360 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 Q13435 UniProtKB Modified residue 362 362 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 Q13435 UniProtKB Modified residue 431 431 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:18318008,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:17081983,PMID:18318008,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569 Q13435 UniProtKB Modified residue 435 435 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:18318008,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:17081983,PMID:18318008,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569 Q13435 UniProtKB Modified residue 436 436 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:18318008,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:17081983,PMID:18318008,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569 Q13435 UniProtKB Modified residue 508 508 . . . Note=Omega-N-methylarginine%3B by PRMT9%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25737013;Dbxref=PMID:25737013 Q13435 UniProtKB Modified residue 508 508 . . . Note=Symmetric dimethylarginine%3B by PRMT9%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25737013;Dbxref=PMID:25737013 Q13435 UniProtKB Modified residue 515 515 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q13435 UniProtKB Modified residue 780 780 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231,PMID:23186163 Q13435 UniProtKB Modified residue 861 861 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q13435 UniProtKB Cross-link 10 10 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q13435 UniProtKB Cross-link 280 280 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q13435 UniProtKB Cross-link 400 400 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25755297,ECO:0007744|PubMed:25772364,ECO:0007744|PubMed:28112733;Dbxref=PMID:25755297,PMID:25772364,PMID:28112733 Q13435 UniProtKB Cross-link 412 412 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25218447,ECO:0007744|PubMed:28112733;Dbxref=PMID:25218447,PMID:28112733 Q13435 UniProtKB Cross-link 492 492 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q13435 UniProtKB Cross-link 543 543 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q13435 UniProtKB Cross-link 770 770 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q13435 UniProtKB Cross-link 790 790 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q13435 UniProtKB Cross-link 843 843 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q13435 UniProtKB Cross-link 857 857 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q13435 UniProtKB Natural variant 103 895 . . . ID=VAR_087086;Note=In CFM1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34344887;Dbxref=PMID:34344887 Q13435 UniProtKB Natural variant 638 895 . . . ID=VAR_087087;Note=In CFM1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34344887;Dbxref=PMID:34344887 Q13435 UniProtKB Mutagenesis 471 471 . . . Note=Does not affect methylation by PRMT9. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25737013;Dbxref=PMID:25737013 Q13435 UniProtKB Mutagenesis 495 495 . . . Note=Does not affect methylation by PRMT9. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25737013;Dbxref=PMID:25737013 Q13435 UniProtKB Mutagenesis 502 502 . . . Note=Does not affect methylation by PRMT9. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25737013;Dbxref=PMID:25737013 Q13435 UniProtKB Mutagenesis 506 506 . . . Note=Does not affect methylation by PRMT9%3B when associated with A-510. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25979344;Dbxref=PMID:25979344 Q13435 UniProtKB Mutagenesis 507 507 . . . Note=Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine%3B when associated with A-509. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25979344;Dbxref=PMID:25979344 Q13435 UniProtKB Mutagenesis 507 507 . . . Note=Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine%3B when associated with R-509. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine%3B when associated with R-508. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine%3B when associated with K-508 and R-509. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25979344;Dbxref=PMID:25979344 Q13435 UniProtKB Mutagenesis 508 508 . . . Note=Abolishes interaction with SMN1%3B Abolishes methylation by PRMT9. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine%3B when associated with R-507. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine%3B when associated with R-507. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine%3B when associated with R-507 and R-509. R->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25737013,ECO:0000269|PubMed:25979344;Dbxref=PMID:25737013,PMID:25979344 Q13435 UniProtKB Mutagenesis 509 509 . . . Note=Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine%3B when associated with A-507. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25737013;Dbxref=PMID:25737013 Q13435 UniProtKB Mutagenesis 509 509 . . . Note=Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine%3B when associated with R-507. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine%3B when associated with K-508 and R-507. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25737013;Dbxref=PMID:25737013 Q13435 UniProtKB Mutagenesis 510 510 . . . Note=Does not affect methylation by PRMT9%3B when associated with A-506. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25979344;Dbxref=PMID:25979344 Q13435 UniProtKB Mutagenesis 515 515 . . . Note=Does not affect methylation by PRMT9. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25737013;Dbxref=PMID:25737013 Q13435 UniProtKB Mutagenesis 530 530 . . . Note=Does not affect methylation by PRMT9. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25737013;Dbxref=PMID:25737013 Q13435 UniProtKB Mutagenesis 537 537 . . . Note=Does not affect methylation by PRMT9. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25737013;Dbxref=PMID:25737013 Q13435 UniProtKB Sequence conflict 602 602 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13435 UniProtKB Sequence conflict 765 765 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13435 UniProtKB Helix 29 39 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DO5 Q13435 UniProtKB Helix 47 61 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DO5 Q13435 UniProtKB Helix 454 457 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q3L Q13435 UniProtKB Helix 462 468 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q4O Q13435 UniProtKB Helix 472 474 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q4O Q13435 UniProtKB Helix 479 481 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q4O Q13435 UniProtKB Beta strand 482 484 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q4O Q13435 UniProtKB Helix 485 493 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q4O Q13435 UniProtKB Beta strand 494 496 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7EVO Q13435 UniProtKB Helix 502 505 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q4O Q13435 UniProtKB Turn 510 513 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q4O Q13435 UniProtKB Helix 514 518 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7DVQ Q13435 UniProtKB Helix 526 529 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q4O Q13435 UniProtKB Turn 530 532 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q4O Q13435 UniProtKB Helix 533 536 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q4O Q13435 UniProtKB Turn 544 546 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7DVQ Q13435 UniProtKB Helix 549 554 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7DVQ Q13435 UniProtKB Turn 555 557 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7DVQ Q13435 UniProtKB Helix 568 576 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q4O Q13435 UniProtKB Turn 593 597 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q4O Q13435 UniProtKB Helix 611 617 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7EVO Q13435 UniProtKB Beta strand 624 626 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7EVO Q13435 UniProtKB Helix 633 639 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7EVO Q13435 UniProtKB Turn 652 654 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7EVO Q13435 UniProtKB Turn 657 659 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7ONB Q13435 UniProtKB Helix 692 702 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7DVQ