##gff-version 3 Q7JJ13 UniProtKB Chain 1 798 . . . ID=PRO_0000274005;Note=Bromodomain-containing protein 2 Q7JJ13 UniProtKB Domain 90 162 . . . Note=Bromo 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 Q7JJ13 UniProtKB Domain 363 435 . . . Note=Bromo 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00035 Q7JJ13 UniProtKB Domain 630 712 . . . Note=NET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00857 Q7JJ13 UniProtKB Region 1 21 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Region 53 72 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Region 267 348 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Region 454 645 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Region 736 798 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Motif 553 557 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q7JJ13 UniProtKB Compositional bias 311 335 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Compositional bias 469 484 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Compositional bias 485 509 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Compositional bias 510 524 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Compositional bias 543 561 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Compositional bias 562 578 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Compositional bias 590 617 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Compositional bias 631 645 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Compositional bias 758 798 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q7JJ13 UniProtKB Binding site 111 111 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25440 Q7JJ13 UniProtKB Binding site 154 154 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25440 Q7JJ13 UniProtKB Binding site 155 155 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25440 Q7JJ13 UniProtKB Binding site 155 155 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25440 Q7JJ13 UniProtKB Binding site 156 156 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25440 Q7JJ13 UniProtKB Binding site 159 159 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25440 Q7JJ13 UniProtKB Binding site 160 160 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25440 Q7JJ13 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25440 Q7JJ13 UniProtKB Modified residue 6 6 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25440 Q7JJ13 UniProtKB Modified residue 36 36 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25440 Q7JJ13 UniProtKB Modified residue 297 297 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17242355,ECO:0007744|PubMed:21183079;Dbxref=PMID:17242355,PMID:21183079 Q7JJ13 UniProtKB Modified residue 300 300 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17242355,ECO:0007744|PubMed:21183079;Dbxref=PMID:17242355,PMID:21183079 Q7JJ13 UniProtKB Modified residue 304 304 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q7JJ13 UniProtKB Modified residue 631 631 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25440 Q7JJ13 UniProtKB Alternative sequence 1 46 . . . ID=VSP_022601;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9693039;Dbxref=PMID:9693039 Q7JJ13 UniProtKB Mutagenesis 102 102 . . . Note=In BD1-m4 mutant%3B reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-112%2C A-154 and A-161. In m8 mutant%3B abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-112%2C A-154%2C A-161%2C A-375%2C A-385%2C A-427 and A-434. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14731392;Dbxref=PMID:14731392 Q7JJ13 UniProtKB Mutagenesis 112 112 . . . Note=In BD1-m4 mutant%3B reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-102%2C A-154 and A-161. In m8 mutant%3B abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-102%2C A-154%2C A-161%2C A-375%2C A-385%2C A-427 and A-434. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14731392;Dbxref=PMID:14731392 Q7JJ13 UniProtKB Mutagenesis 154 154 . . . Note=In BD1-m4 mutant%3B reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-102%2C A-112 and A-161. In m8 mutant%3B abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-102%2C A-112%2C A-161%2C A-375%2C A-385%2C A-427 and A-434. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14731392;Dbxref=PMID:14731392 Q7JJ13 UniProtKB Mutagenesis 154 154 . . . Note=Abolished interaction with acetylated STAT3. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28262505;Dbxref=PMID:28262505 Q7JJ13 UniProtKB Mutagenesis 161 161 . . . Note=In BD1-m4 mutant%3B reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-102%2C A-112 and A-154. In m8 mutant%3B abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-102%2C A-112%2C A-161%2C A-375%2C A-385%2C A-427 and A-434. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14731392;Dbxref=PMID:14731392 Q7JJ13 UniProtKB Mutagenesis 375 375 . . . Note=In BD2-m4 mutant%3B reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-385%2C A-427 and A-434. In m8 mutant%3B abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-102%2C A-112%2C A-154%2C A-161%2C A-385%2C A-427 and A-434. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14731392;Dbxref=PMID:14731392 Q7JJ13 UniProtKB Mutagenesis 385 385 . . . Note=In BD2-m4 mutant%3B reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-375%2C A-427 and A-434. In m8 mutant%3B abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-102%2C A-112%2C A-154%2C A-161%2C A-375%2C A-427 and A-434. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14731392;Dbxref=PMID:14731392 Q7JJ13 UniProtKB Mutagenesis 427 427 . . . Note=In BD2-m4 mutant%3B reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-375%2C A-385 and A-434. In m8 mutant%3B abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-102%2C A-112%2C A-154%2C A-161%2C A-375%2C A-385 and A-434. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14731392;Dbxref=PMID:14731392 Q7JJ13 UniProtKB Mutagenesis 427 427 . . . Note=Abolished interaction with acetylated STAT3. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28262505;Dbxref=PMID:28262505 Q7JJ13 UniProtKB Mutagenesis 434 434 . . . Note=In BD2-m4 mutant%3B reduced binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-375%2C A-385 and A-427. In m8 mutant%3B abolished binding to histone H4 acetylated at 'Lys-12' (H4K12ac)%3B when associated with A-102%2C A-112%2C A-154%2C A-161%2C A-375%2C A-385%2C and A-427434. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14731392;Dbxref=PMID:14731392 Q7JJ13 UniProtKB Sequence conflict 169 169 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q7JJ13 UniProtKB Sequence conflict 199 199 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q7JJ13 UniProtKB Sequence conflict 691 691 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q7JJ13 UniProtKB Sequence conflict 765 767 . . . Note=QVA->LVP;Ontology_term=ECO:0000305;evidence=ECO:0000305