##gff-version 3 P15923 UniProtKB Chain 1 654 . . . ID=PRO_0000127466;Note=Transcription factor E2-alpha P15923 UniProtKB Domain 549 602 . . . Note=BHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 P15923 UniProtKB Region 31 103 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15923 UniProtKB Region 135 205 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15923 UniProtKB Region 239 268 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15923 UniProtKB Region 292 329 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15923 UniProtKB Region 343 385 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15923 UniProtKB Region 389 425 . . . Note=Leucine-zipper P15923 UniProtKB Region 461 552 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15923 UniProtKB Region 633 654 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15923 UniProtKB Motif 19 27 . . . Note=9aaTAD P15923 UniProtKB Motif 170 176 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15923 UniProtKB Compositional bias 54 96 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15923 UniProtKB Compositional bias 139 163 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15923 UniProtKB Compositional bias 292 327 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15923 UniProtKB Compositional bias 343 366 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15923 UniProtKB Compositional bias 494 552 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15923 UniProtKB Site 483 484 . . . Note=Breakpoint for translocation to form TCF3-PBX1 oncogene P15923 UniProtKB Modified residue 134 134 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 P15923 UniProtKB Modified residue 139 139 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 P15923 UniProtKB Modified residue 355 355 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15806 P15923 UniProtKB Modified residue 359 359 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 P15923 UniProtKB Modified residue 371 371 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15806 P15923 UniProtKB Modified residue 379 379 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P15923 UniProtKB Modified residue 529 529 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P15923 UniProtKB Cross-link 498 498 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25218447,ECO:0007744|PubMed:25755297,ECO:0007744|PubMed:28112733;Dbxref=PMID:25218447,PMID:25755297,PMID:28112733 P15923 UniProtKB Cross-link 625 625 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P15923 UniProtKB Alternative sequence 49 99 . . . ID=VSP_057277;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P15923 UniProtKB Alternative sequence 528 528 . . . ID=VSP_057278;Note=In isoform 3. T->TRCQPTPRHSPPSPHQDAHVHRPHAHRTHTGRPSAGPTLFPQPHCLPLAPSRRPPH;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P15923 UniProtKB Alternative sequence 530 601 . . . ID=VSP_002155;Note=In isoform E47. PDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFKELGRMCQLHLNSEKPQTKLLILHQAVSVILN->STDEVLSLEEKDLRDRERRMANNARERVRVRDINEAFRELGRMCQMHLKSDKAQTKLLILQQAVQVILG;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:1818757,ECO:0000303|PubMed:2308859,ECO:0000303|PubMed:2493990;Dbxref=PMID:15489334,PMID:1818757,PMID:2308859,PMID:2493990 P15923 UniProtKB Natural variant 8 8 . . . ID=VAR_036396;Note=In a colorectal cancer sample%3B somatic mutation. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=dbSNP:rs376780559,PMID:16959974 P15923 UniProtKB Natural variant 120 120 . . . ID=VAR_049552;Note=L->P;Dbxref=dbSNP:rs35354874 P15923 UniProtKB Natural variant 198 198 . . . ID=VAR_049553;Note=T->A;Dbxref=dbSNP:rs11879402 P15923 UniProtKB Natural variant 270 654 . . . ID=VAR_087244;Note=In AGM8B%3B decreased protein abundance. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28532655;Dbxref=PMID:28532655 P15923 UniProtKB Natural variant 431 431 . . . ID=VAR_049554;Note=G->S;Dbxref=dbSNP:rs1052692 P15923 UniProtKB Sequence conflict 69 99 . . . Note=FDPSRTFSEGTHFTESHSSLSSSTFLGPGLG->GGGECLAWCGPSAVHRCADVGLGMVSARTAP;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15923 UniProtKB Sequence conflict 214 216 . . . Note=FYV->EFR;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15923 UniProtKB Sequence conflict 302 302 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15923 UniProtKB Sequence conflict 390 390 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15923 UniProtKB Helix 12 25 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2MH0 P15923 UniProtKB Helix 563 580 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U5V P15923 UniProtKB Helix 588 608 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3U5V P15923 UniProtKB Modified residue 531 531 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 P15923 UniProtKB Natural variant 555 555 . . . ID=VAR_082832;Note=In AGM8A%3B localizes normally to the nucleus%3B does not perform proper DNA binding%3B acts in a dominant-negative manner when coexpressed with wild-type. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24216514;Dbxref=dbSNP:rs879255271,PMID:24216514