##gff-version 3 O70133 UniProtKB Chain 1 1380 . . . ID=PRO_0000055158;Note=ATP-dependent RNA helicase A O70133 UniProtKB Domain 3 71 . . . Note=DRBM 1;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q08211,ECO:0000255|PROSITE-ProRule:PRU00266 O70133 UniProtKB Domain 182 254 . . . Note=DRBM 2;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q08211,ECO:0000255|PROSITE-ProRule:PRU00266 O70133 UniProtKB Domain 400 566 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q08211,ECO:0000255|PROSITE-ProRule:PRU00541 O70133 UniProtKB Domain 638 811 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 O70133 UniProtKB Region 1 252 . . . Note=Interaction with CREBBP;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Region 5 9 . . . Note=SiRNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Region 53 55 . . . Note=SiRNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Region 87 146 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O70133 UniProtKB Region 184 188 . . . Note=SiRNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Region 232 327 . . . Note=Interaction with BRCA1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Region 236 238 . . . Note=SiRNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Region 257 666 . . . Note=Necessary for interaction with RNA polymerase II holoenzyme;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Region 315 954 . . . Note=Necessary for interaction with H2AX;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Region 333 382 . . . Note=MTAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Region 400 811 . . . Note=Core helicase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Region 588 610 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O70133 UniProtKB Region 833 921 . . . Note=HA2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Region 960 1076 . . . Note=OB-fold;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Region 1151 1366 . . . Note=NTD region;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Region 1152 1380 . . . Note=RGG;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Motif 513 516 . . . Note=DEAH box O70133 UniProtKB Motif 588 597 . . . Note=Nuclear localization signal (NLS1);Ontology_term=ECO:0000255;evidence=ECO:0000255 O70133 UniProtKB Motif 1156 1174 . . . Note=Nuclear localization signal (NLS2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Binding site 413 421 . . . Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q08211,ECO:0000255|PROSITE-ProRule:PRU00541 O70133 UniProtKB Binding site 420 420 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Binding site 514 514 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Modified residue 127 127 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 O70133 UniProtKB Modified residue 148 148 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 O70133 UniProtKB Modified residue 148 148 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Modified residue 193 193 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Modified residue 201 201 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Modified residue 323 323 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Modified residue 451 451 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Modified residue 508 508 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Modified residue 1026 1026 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Modified residue 1167 1167 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 O70133 UniProtKB Modified residue 1176 1176 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Modified residue 1312 1312 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 O70133 UniProtKB Modified residue 1323 1323 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 O70133 UniProtKB Modified residue 1339 1339 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 O70133 UniProtKB Modified residue 1346 1346 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 O70133 UniProtKB Modified residue 1353 1353 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 O70133 UniProtKB Modified residue 1361 1361 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 O70133 UniProtKB Modified residue 1372 1372 . . . Note=Asymmetric dimethylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 O70133 UniProtKB Cross-link 699 699 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08211 O70133 UniProtKB Alternative sequence 1 216 . . . ID=VSP_014778;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14691545;Dbxref=PMID:14691545 O70133 UniProtKB Alternative sequence 123 123 . . . ID=VSP_014779;Note=In isoform 2. E->EA;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16141072;Dbxref=PMID:16141072 O70133 UniProtKB Sequence conflict 46 46 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 O70133 UniProtKB Sequence conflict 136 136 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 O70133 UniProtKB Sequence conflict 187 187 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 O70133 UniProtKB Sequence conflict 189 189 . . . Note=Q->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 O70133 UniProtKB Sequence conflict 211 211 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 O70133 UniProtKB Sequence conflict 235 235 . . . Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 O70133 UniProtKB Sequence conflict 257 257 . . . Note=V->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 O70133 UniProtKB Sequence conflict 281 281 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 O70133 UniProtKB Sequence conflict 674 674 . . . Note=N->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 O70133 UniProtKB Sequence conflict 748 748 . . . Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 O70133 UniProtKB Sequence conflict 831 831 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 O70133 UniProtKB Helix 5 14 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WHQ O70133 UniProtKB Beta strand 20 27 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WHQ O70133 UniProtKB Beta strand 29 39 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WHQ O70133 UniProtKB Beta strand 47 53 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WHQ O70133 UniProtKB Helix 54 72 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WHQ O70133 UniProtKB Turn 77 79 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WHQ O70133 UniProtKB Helix 172 175 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UIL O70133 UniProtKB Helix 180 193 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UIL O70133 UniProtKB Beta strand 201 206 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UIL O70133 UniProtKB Beta strand 212 221 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UIL O70133 UniProtKB Turn 222 225 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UIL O70133 UniProtKB Beta strand 226 231 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UIL O70133 UniProtKB Helix 237 255 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UIL O70133 UniProtKB Modified residue 137 137 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17242355,ECO:0007744|PubMed:18630941,ECO:0007744|PubMed:21183079;Dbxref=PMID:17242355,PMID:18630941,PMID:21183079