##gff-version 3 Q15596 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19413330;Dbxref=PMID:19413330 Q15596 UniProtKB Chain 2 1464 . . . ID=PRO_0000094402;Note=Nuclear receptor coactivator 2 Q15596 UniProtKB Domain 26 83 . . . Note=BHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 Q15596 UniProtKB Domain 119 183 . . . Note=PAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00140 Q15596 UniProtKB Region 1 40 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Region 468 513 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Region 557 683 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Region 691 743 . . . Note=CASP8AP2-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61026 Q15596 UniProtKB Region 709 737 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Region 730 1121 . . . Note=Interaction with BMAL1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61026 Q15596 UniProtKB Region 973 1003 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Region 1017 1038 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Region 1051 1074 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Region 1441 1464 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Motif 641 645 . . . Note=LXXLL motif 1 Q15596 UniProtKB Motif 690 694 . . . Note=LXXLL motif 2 Q15596 UniProtKB Motif 745 749 . . . Note=LXXLL motif 3 Q15596 UniProtKB Motif 878 882 . . . Note=LXXLL motif 4 Q15596 UniProtKB Motif 1079 1087 . . . Note=LLXXLXXXL motif Q15596 UniProtKB Compositional bias 11 40 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Compositional bias 468 488 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Compositional bias 557 572 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Compositional bias 595 619 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Compositional bias 635 680 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Compositional bias 712 729 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Compositional bias 988 1003 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Compositional bias 1018 1034 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15596 UniProtKB Site 869 870 . . . Note=Breakpoint for translocation to form KAT6A-NCOA2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12676584,ECO:0000269|PubMed:15657427,ECO:0000269|PubMed:9558366;Dbxref=PMID:12676584,PMID:15657427,PMID:9558366 Q15596 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19413330;Dbxref=PMID:19413330 Q15596 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q15596 UniProtKB Modified residue 338 338 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61026 Q15596 UniProtKB Modified residue 487 487 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 Q15596 UniProtKB Modified residue 493 493 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:20068231,PMID:23186163,PMID:24275569 Q15596 UniProtKB Modified residue 499 499 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 Q15596 UniProtKB Modified residue 554 554 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q15596 UniProtKB Modified residue 565 565 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:23186163,PMID:24275569 Q15596 UniProtKB Modified residue 636 636 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61026 Q15596 UniProtKB Modified residue 640 640 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q15596 UniProtKB Modified residue 682 682 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q15596 UniProtKB Modified residue 699 699 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:23186163,PMID:24275569 Q15596 UniProtKB Modified residue 736 736 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q15596 UniProtKB Modified residue 771 771 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q15596 UniProtKB Modified residue 780 780 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q15596 UniProtKB Modified residue 785 785 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q15596 UniProtKB Modified residue 864 864 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61026 Q15596 UniProtKB Modified residue 874 874 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61026 Q15596 UniProtKB Modified residue 1173 1173 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q15596 UniProtKB Modified residue 1177 1177 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q15596 UniProtKB Modified residue 1190 1190 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q15596 UniProtKB Modified residue 1196 1196 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q15596 UniProtKB Modified residue 1203 1203 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q15596 UniProtKB Modified residue 1221 1221 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q15596 UniProtKB Modified residue 1240 1240 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61026 Q15596 UniProtKB Modified residue 1261 1261 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q15596 UniProtKB Modified residue 1266 1266 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q15596 UniProtKB Cross-link 239 239 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q15596 UniProtKB Cross-link 648 648 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q15596 UniProtKB Cross-link 705 705 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q15596 UniProtKB Cross-link 731 731 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q15596 UniProtKB Cross-link 785 785 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25218447,ECO:0007744|PubMed:28112733;Dbxref=PMID:25218447,PMID:28112733 Q15596 UniProtKB Cross-link 1454 1454 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q15596 UniProtKB Natural variant 1282 1282 . . . ID=VAR_024546;Note=M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs2228591,PMID:15489334 Q15596 UniProtKB Mutagenesis 644 645 . . . Note=By itself%2C does not affect nuclear receptor binding or transcriptional coactivation. Abrogates ligand-induced nuclear receptor binding and transactivation%3B when associated with 693-A-A-694 and 748-A-A-749. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9430642;Dbxref=PMID:9430642 Q15596 UniProtKB Mutagenesis 693 694 . . . Note=By itself%2C does not affect nuclear receptor binding or transcriptional coactivation. Abrogates ligand-induced nuclear receptor binding and transactivation%3B when associated with 644-A-A-665 and 748-A-A-749. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9430642;Dbxref=PMID:9430642 Q15596 UniProtKB Mutagenesis 748 749 . . . Note=By itself%2C does not affect nuclear receptor binding or transcriptional coactivation. Abrogates ligand-induced nuclear receptor binding and transactivation%3B when associated with 644-A-A-665 and 693-A-A-694. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9430642;Dbxref=PMID:9430642 Q15596 UniProtKB Mutagenesis 1079 1083 . . . Note=Reduces transcriptional coactivation and disrupts interaction with CREBBP/CBP. LLDQL->AADQA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9430642;Dbxref=PMID:9430642 Q15596 UniProtKB Mutagenesis 1081 1082 . . . Note=Has little effect on transcriptional coactivation. DQ->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9430642;Dbxref=PMID:9430642 Q15596 UniProtKB Helix 685 687 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5VB7 Q15596 UniProtKB Helix 689 693 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NFB Q15596 UniProtKB Beta strand 697 699 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7BK4 Q15596 UniProtKB Helix 700 711 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7APO Q15596 UniProtKB Beta strand 739 741 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1M2Z Q15596 UniProtKB Helix 743 750 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UP3