##gff-version 3 O94992 UniProtKB Chain 1 359 . . . ID=PRO_0000305263;Note=Protein HEXIM1 O94992 UniProtKB Region 1 163 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O94992 UniProtKB Region 150 177 . . . Note=Basic region%3B mediates nuclear localization and interaction with 7SK snRNA and NR3C1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15941832;Dbxref=PMID:15941832 O94992 UniProtKB Region 202 205 . . . Note=Interaction with P-TEFb O94992 UniProtKB Region 210 250 . . . Note=Autoinhibitory acidic region%3B in absence of 7SK snRNA interacts with the basic region preventing interaction with P-TEFb and modulating subcellular localization O94992 UniProtKB Region 213 262 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O94992 UniProtKB Region 286 314 . . . Note=Mediates interaction with CCNT1 O94992 UniProtKB Region 310 355 . . . Note=Required for inhibition of ESR1-dependent transcription O94992 UniProtKB Coiled coil 283 349 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 O94992 UniProtKB Compositional bias 8 23 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O94992 UniProtKB Compositional bias 31 46 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O94992 UniProtKB Compositional bias 148 163 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O94992 UniProtKB Compositional bias 237 251 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O94992 UniProtKB Modified residue 97 97 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 O94992 UniProtKB Modified residue 98 98 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 O94992 UniProtKB Modified residue 233 233 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231 O94992 UniProtKB Modified residue 236 236 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231 O94992 UniProtKB Modified residue 237 237 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231 O94992 UniProtKB Modified residue 252 252 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231,PMID:21406692 O94992 UniProtKB Modified residue 260 260 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8R409 O94992 UniProtKB Mutagenesis 152 155 . . . Note=Abolishes interaction with 7SK snRNA. KHRR->ILAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201869;Dbxref=PMID:15201869 O94992 UniProtKB Mutagenesis 154 156 . . . Note=Abolishes interaction with 7SK snRNA. RRR->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16362050;Dbxref=PMID:16362050 O94992 UniProtKB Mutagenesis 203 203 . . . Note=Abolishes interaction with P-TEFb%3B when associated with D-205. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201869;Dbxref=PMID:15201869 O94992 UniProtKB Mutagenesis 205 205 . . . Note=Abolishes interaction with P-TEFb. Same effect%3B when associated with D-203. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15201869;Dbxref=PMID:15201869 O94992 UniProtKB Mutagenesis 208 208 . . . Note=Partial loss of function. F->A%2CD%2CK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15965233;Dbxref=PMID:15965233 O94992 UniProtKB Mutagenesis 271 271 . . . Note=Loss of function. Y->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15965233;Dbxref=PMID:15965233 O94992 UniProtKB Mutagenesis 287 287 . . . Note=Loss of oligomerization%3B when associated with A-294%3B A-332 and A-339. Loss of function and interaction with P-TEFb%3B when associated with A-294. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16377779;Dbxref=PMID:16377779 O94992 UniProtKB Mutagenesis 294 294 . . . Note=Loss of oligomerization%3B when associated with A-287%3B A-332 and A-339. Loss of function and interaction with P-TEFb%3B when associated with A-287. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16377779;Dbxref=PMID:16377779 O94992 UniProtKB Mutagenesis 332 332 . . . Note=Loss of oligomerization%3B when associated with A-287%3B A-294 and A-339. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16377779;Dbxref=PMID:16377779 O94992 UniProtKB Mutagenesis 339 339 . . . Note=Loss of oligomerization%3B when associated with A-287%3B A-294 and A-332. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16377779;Dbxref=PMID:16377779 O94992 UniProtKB Helix 268 280 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3S9G O94992 UniProtKB Helix 284 315 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3S9G O94992 UniProtKB Helix 319 348 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3S9G