##gff-version 3 Q9H2U1 UniProtKB Chain 1 1008 . . . ID=PRO_0000247530;Note=ATP-dependent DNA/RNA helicase DHX36 Q9H2U1 UniProtKB Domain 217 387 . . . Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 Q9H2U1 UniProtKB Domain 477 647 . . . Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542 Q9H2U1 UniProtKB Region 1 200 . . . Note=Necessary for nuclear and nucleolar caps localizations;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18279852;Dbxref=PMID:18279852 Q9H2U1 UniProtKB Region 1 104 . . . Note=Required for the pre-miR-134 transport;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:D4A2Z8 Q9H2U1 UniProtKB Region 1 58 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H2U1 UniProtKB Region 1 51 . . . Note=Required for recruitment to cytoplasmic stress granules;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18854321;Dbxref=PMID:18854321 Q9H2U1 UniProtKB Region 53 105 . . . Note=Required for G4-DNA- and G4-RNA-binding;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21149580,ECO:0000269|PubMed:21846770,ECO:0000269|PubMed:24151078;Dbxref=PMID:21149580,PMID:21846770,PMID:24151078 Q9H2U1 UniProtKB Region 53 75 . . . Note=DSM (DHX36-specific motif);Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20472641,ECO:0000269|PubMed:22238380,ECO:0000269|PubMed:24369427,ECO:0000269|PubMed:26195789,ECO:0000269|PubMed:26649896;Dbxref=PMID:20472641,PMID:22238380,PMID:24369427,PMID:26195789,PMID:26649896 Q9H2U1 UniProtKB Region 106 386 . . . Note=RecA-like domain 1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Region 265 317 . . . Note=Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structure;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Region 387 628 . . . Note=RecA-like domain 2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Region 498 557 . . . Note=Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structure;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Region 629 698 . . . Note=WH domain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Region 638 697 . . . Note=Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structure;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Region 841 905 . . . Note=OB-fold-like subdomains;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Region 849 860 . . . Note=Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structure;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Region 870 900 . . . Note=Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structure;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Coiled coil 72 157 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9H2U1 UniProtKB Motif 334 337 . . . Note=DEAH box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541 Q9H2U1 UniProtKB Motif 517 528 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14731398;Dbxref=PMID:14731398 Q9H2U1 UniProtKB Binding site 233 238 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Binding site 335 335 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Binding site 337 337 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Binding site 557 557 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Binding site 602 605 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q05B79 Q9H2U1 UniProtKB Modified residue 161 161 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q9H2U1 UniProtKB Modified residue 947 947 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q9H2U1 UniProtKB Modified residue 963 963 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q9H2U1 UniProtKB Alternative sequence 517 530 . . . ID=VSP_020006;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14731398;Dbxref=PMID:14731398 Q9H2U1 UniProtKB Alternative sequence 737 765 . . . ID=VSP_020007;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q9H2U1 UniProtKB Natural variant 151 151 . . . ID=VAR_027140;Note=E->K;Dbxref=dbSNP:rs1058299 Q9H2U1 UniProtKB Natural variant 416 416 . . . ID=VAR_027141;Note=S->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12198572,ECO:0000269|PubMed:14731398,ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs9438,PMID:12198572,PMID:14731398,PMID:15489334 Q9H2U1 UniProtKB Natural variant 583 583 . . . ID=VAR_027142;Note=I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs17853513,PMID:15489334 Q9H2U1 UniProtKB Mutagenesis 54 54 . . . Note=Reduces G4-RNA binding%3B when associated with A-57%2C A-59%2C A-62 and A-63. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20472641;Dbxref=PMID:20472641 Q9H2U1 UniProtKB Mutagenesis 55 55 . . . Note=Inhibits G4-DNA-binding%3B when associated with L-59 and L-63. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26195789;Dbxref=PMID:26195789 Q9H2U1 UniProtKB Mutagenesis 57 57 . . . Note=Reduces G4-RNA-binding%3B when associated with G-54%2C A-59%2C A-62 and A-63. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20472641;Dbxref=PMID:20472641 Q9H2U1 UniProtKB Mutagenesis 59 59 . . . Note=Reduces G4-RNA-binding%3B when associated with G-54%2C A-57%2C A-62 and A-63. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20472641;Dbxref=PMID:20472641 Q9H2U1 UniProtKB Mutagenesis 59 59 . . . Note=Inhibits G4-DNA-binding%3B when associated with L-55 and L-63. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26195789;Dbxref=PMID:26195789 Q9H2U1 UniProtKB Mutagenesis 59 59 . . . Note=Greatly reduces G4-RNA-binding%3B when associated with P-63. G->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20472641;Dbxref=PMID:20472641 Q9H2U1 UniProtKB Mutagenesis 62 62 . . . Note=Reduces G4-RNA-binding%3B when associated with G-54%2C A-57%2C A-59 and A-63. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20472641;Dbxref=PMID:20472641 Q9H2U1 UniProtKB Mutagenesis 63 63 . . . Note=Reduces G4-RNA-binding%3B when associated with G-54%2C A-57%2C A-59 and A-62. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20472641;Dbxref=PMID:20472641 Q9H2U1 UniProtKB Mutagenesis 63 63 . . . Note=Inhibits G4-DNA-binding%3B when associated with L-55 and L-59. G->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26195789;Dbxref=PMID:26195789 Q9H2U1 UniProtKB Mutagenesis 63 63 . . . Note=Greatly reduces G4-RNA-binding%3B when associated with P-59. G->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20472641;Dbxref=PMID:20472641 Q9H2U1 UniProtKB Mutagenesis 65 65 . . . Note=Does not inhibit G4-DNA-binding%3B when associated with A-66. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26195789;Dbxref=PMID:26195789 Q9H2U1 UniProtKB Mutagenesis 66 66 . . . Note=Does not inhibit G4-DNA-binding%3B when associated with A-65. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26195789;Dbxref=PMID:26195789 Q9H2U1 UniProtKB Mutagenesis 335 335 . . . Note=Loss of ATPase activity%3B results in an increased in G4-DNA- and G4-RNA-binding stabilities%2C increases localization in cytoplasmic stress granules and loss of mRNA deadenylation and mRNA decay. E->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14731398,ECO:0000269|PubMed:18279852,ECO:0000269|PubMed:18854321,ECO:0000269|PubMed:21846770;Dbxref=PMID:14731398,PMID:18279852,PMID:18854321,PMID:21846770 Q9H2U1 UniProtKB Helix 60 67 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6Q6R