##gff-version 3 Q16236 UniProtKB Chain 1 605 . . . ID=PRO_0000076449;Note=Nuclear factor erythroid 2-related factor 2 Q16236 UniProtKB Domain 497 560 . . . Note=BZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 Q16236 UniProtKB Region 334 449 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q16236 UniProtKB Region 499 518 . . . Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 Q16236 UniProtKB Region 522 529 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 Q16236 UniProtKB Region 571 605 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q16236 UniProtKB Region 591 596 . . . Note=Mediates interaction with CHD6 and is necessary to activate transcription;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O54968 Q16236 UniProtKB Motif 29 31 . . . Note=DLG motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60795 Q16236 UniProtKB Motif 79 82 . . . Note=ETGE motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60795 Q16236 UniProtKB Compositional bias 334 371 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q16236 UniProtKB Compositional bias 388 420 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q16236 UniProtKB Compositional bias 421 449 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q16236 UniProtKB Modified residue 40 40 . . . Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O54968 Q16236 UniProtKB Modified residue 215 215 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163 Q16236 UniProtKB Modified residue 596 596 . . . Note=N6-acetyllysine%3B by CREBBP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21196497;Dbxref=PMID:21196497 Q16236 UniProtKB Modified residue 599 599 . . . Note=N6-acetyllysine%3B by CREBBP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21196497;Dbxref=PMID:21196497 Q16236 UniProtKB Glycosylation 462 462 . . . Note=N-linked (Glc) (glycation) lysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31398338;Dbxref=PMID:31398338 Q16236 UniProtKB Glycosylation 472 472 . . . Note=N-linked (Glc) (glycation) lysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31398338;Dbxref=PMID:31398338 Q16236 UniProtKB Glycosylation 487 487 . . . Note=N-linked (Glc) (glycation) lysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31398338;Dbxref=PMID:31398338 Q16236 UniProtKB Glycosylation 499 499 . . . Note=N-linked (Glc) (glycation) arginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:31398338;Dbxref=PMID:31398338 Q16236 UniProtKB Glycosylation 569 569 . . . Note=N-linked (Glc) (glycation) arginine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:31398338;Dbxref=PMID:31398338 Q16236 UniProtKB Glycosylation 574 574 . . . Note=N-linked (Glc) (glycation) lysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31398338;Dbxref=PMID:31398338 Q16236 UniProtKB Alternative sequence 1 16 . . . ID=VSP_025045;Note=In isoform 2 and isoform 3. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|Ref.2;Dbxref=PMID:14702039 Q16236 UniProtKB Alternative sequence 135 141 . . . ID=VSP_046168;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q16236 UniProtKB Natural variant 31 31 . . . ID=VAR_080492;Note=In IMDDHH. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29018201;Dbxref=dbSNP:rs1553488015,PMID:29018201 Q16236 UniProtKB Natural variant 43 43 . . . ID=VAR_032110;Note=R->Q;Dbxref=dbSNP:rs35248500 Q16236 UniProtKB Natural variant 79 79 . . . ID=VAR_080493;Note=In IMDDHH. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29018201;Dbxref=dbSNP:rs1057519922,PMID:29018201 Q16236 UniProtKB Natural variant 80 80 . . . ID=VAR_080494;Note=In IMDDHH%3B increased protein abundance%3B increased positive regulation of transcription of target genes%3B changed cell redox homeostasis. T->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29018201;Dbxref=dbSNP:rs1553487947,PMID:29018201 Q16236 UniProtKB Natural variant 81 81 . . . ID=VAR_080495;Note=In IMDDHH. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29018201;Dbxref=dbSNP:rs1553487942,PMID:29018201 Q16236 UniProtKB Natural variant 99 99 . . . ID=VAR_020322;Note=S->P;Dbxref=dbSNP:rs5031039 Q16236 UniProtKB Natural variant 268 268 . . . ID=VAR_032111;Note=V->M;Dbxref=dbSNP:rs34154613 Q16236 UniProtKB Mutagenesis 79 82 . . . Note=Abolished interaction with KEAP1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15601839;Dbxref=PMID:15601839 Q16236 UniProtKB Mutagenesis 80 80 . . . Note=Loss of interaction with KEAP1. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16888629;Dbxref=PMID:16888629 Q16236 UniProtKB Mutagenesis 82 82 . . . Note=Abolished interaction with KEAP1. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15601839;Dbxref=PMID:15601839 Q16236 UniProtKB Mutagenesis 462 462 . . . Note=Loss of function%3B when associated with A-472%3B A-487%3B A-499%3B A-569 and A-587. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31398338;Dbxref=PMID:31398338 Q16236 UniProtKB Mutagenesis 472 472 . . . Note=Loss of function%3B when associated with A-462%3B A-487%3B A-499%3B A-569 and A-587. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31398338;Dbxref=PMID:31398338 Q16236 UniProtKB Mutagenesis 487 487 . . . Note=Loss of function%3B when associated with A-462%3B A-472%3B A-499%3B A-569 and A-587. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31398338;Dbxref=PMID:31398338 Q16236 UniProtKB Mutagenesis 499 499 . . . Note=Loss of function%3B when associated with A-462%3B A-472%3B A-487%3B A-569 and A-587. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31398338;Dbxref=PMID:31398338 Q16236 UniProtKB Mutagenesis 569 569 . . . Note=Loss of function%3B when associated with A-462%3B A-472%3B A-487%3B A-499 and A-587. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31398338;Dbxref=PMID:31398338 Q16236 UniProtKB Mutagenesis 587 587 . . . Note=Loss of function%3B when associated with A-462%3B A-472%3B A-487%3B A-499 and A-569. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31398338;Dbxref=PMID:31398338 Q16236 UniProtKB Sequence conflict 72 72 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q16236 UniProtKB Sequence conflict 92 92 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q16236 UniProtKB Sequence conflict 178 178 . . . Note=D->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q16236 UniProtKB Sequence conflict 521 521 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q16236 UniProtKB Turn 78 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2FLU Q16236 UniProtKB Beta strand 449 455 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7O7B Q16236 UniProtKB Helix 456 463 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7X5E Q16236 UniProtKB Helix 470 475 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7X5E Q16236 UniProtKB Helix 478 485 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7X5E Q16236 UniProtKB Helix 492 556 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7X5E