##gff-version 3 Q99966 UniProtKB Chain 1 193 . . . ID=PRO_0000144724;Note=Cbp/p300-interacting transactivator 1 Q99966 UniProtKB Region 1 26 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99966 UniProtKB Region 50 88 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99966 UniProtKB Region 106 147 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99966 UniProtKB Motif 158 167 . . . Note=Nuclear export signal Q99966 UniProtKB Compositional bias 55 72 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99966 UniProtKB Alternative sequence 1 1 . . . ID=VSP_039897;Note=In isoform 2. M->MEPSAQQLQLAASLPANLSNFCQGSEM;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.6 Q99966 UniProtKB Natural variant 96 96 . . . ID=VAR_053038;Note=H->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:19054851,ECO:0000269|PubMed:8901575,ECO:0000269|Ref.4;Dbxref=dbSNP:rs3012627,PMID:15489334,PMID:19054851,PMID:8901575 Q99966 UniProtKB Mutagenesis 16 16 . . . Note=Strongly reduces phosphorylation but does not interfere with its NES-dependent nuclear export%3B when associated with A-63%3B A-67%3B A-71 and A-137. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16864582;Dbxref=PMID:16864582 Q99966 UniProtKB Mutagenesis 63 63 . . . Note=Strongly reduces phosphorylation but does not interfere with its NES-dependent nuclear export%3B when associated with A-16%3B A-67%3B A-71 and A-137. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16864582;Dbxref=PMID:16864582 Q99966 UniProtKB Mutagenesis 67 67 . . . Note=Strongly reduces phosphorylation but does not interfere with its NES-dependent nuclear export%3B when associated with A-16%3B A-63%3B A-71 and A-137. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16864582;Dbxref=PMID:16864582 Q99966 UniProtKB Mutagenesis 71 71 . . . Note=Strongly reduces phosphorylation but does not interfere with its NES-dependent nuclear export%3B when associated with A-16%3B A-63%3B A-67 and A-137. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16864582;Dbxref=PMID:16864582 Q99966 UniProtKB Mutagenesis 91 91 . . . Note=Does not change subcellular localization%3B when associated with A-95. L->A Q99966 UniProtKB Mutagenesis 95 95 . . . Note=Does not change subcellular localization%3B when associated with A-91. M->A Q99966 UniProtKB Mutagenesis 137 137 . . . Note=Strongly reduces phosphorylation%3B when associated with A-16%3B A-63%3B A-67 and A-71. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16864582;Dbxref=PMID:16864582 Q99966 UniProtKB Mutagenesis 155 156 . . . Note=Does not inhibit interaction with ESR1 and ER-coactivation activity. EE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11581164;Dbxref=PMID:11581164 Q99966 UniProtKB Mutagenesis 157 158 . . . Note=Inhibits interaction with ESR1 and ER-coactivation activity. VL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11581164;Dbxref=PMID:11581164 Q99966 UniProtKB Mutagenesis 159 160 . . . Note=Does not inhibit interaction with ESR1 and ER-coactivation activity. MS->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11581164;Dbxref=PMID:11581164 Q99966 UniProtKB Mutagenesis 161 162 . . . Note=Does not inhibit interaction with ESR1 and ER-coactivation activity. LV->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11581164;Dbxref=PMID:11581164 Q99966 UniProtKB Mutagenesis 163 164 . . . Note=Does not inhibit interaction with ESR1 and ER-coactivation activity. VE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11581164;Dbxref=PMID:11581164 Q99966 UniProtKB Mutagenesis 165 165 . . . Note=Does not inhibit interaction with ESR1 and ER-coactivation activity. Localizes mainly in the nucleus%3B when associated with A-167. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11581164;Dbxref=PMID:11581164 Q99966 UniProtKB Mutagenesis 166 167 . . . Note=Does not inhibit interaction with ESR1 and ER-coactivation activity. Localizes mainly in the nucleus%3B when associated with A-165. GL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11581164;Dbxref=PMID:11581164 Q99966 UniProtKB Mutagenesis 176 176 . . . Note=Does not change subcellular localization%3B when associated with A-178. L->A Q99966 UniProtKB Mutagenesis 178 178 . . . Note=Does not change subcellular localization%3B when associated with A-176. L->A