##gff-version 3
O00571	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:10859333,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:22223895;Dbxref=PMID:10859333,PMID:20068231,PMID:22223895	
O00571	UniProtKB	Chain	2	662	.	.	.	ID=PRO_0000055009;Note=ATP-dependent RNA helicase DDX3X	
O00571	UniProtKB	Domain	211	403	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
O00571	UniProtKB	Domain	414	575	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
O00571	UniProtKB	Region	2	139	.	.	.	Note=Required for TBK1 and IKBKE-dependent IFNB1 activation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18636090;Dbxref=PMID:18636090	
O00571	UniProtKB	Region	19	144	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O00571	UniProtKB	Region	38	44	.	.	.	Note=Interaction with EIF4E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17667941;Dbxref=PMID:17667941	
O00571	UniProtKB	Region	81	90	.	.	.	Note=Interaction with VACV protein K7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19913487;Dbxref=PMID:19913487	
O00571	UniProtKB	Region	88	123	.	.	.	Note=Involved in binding to RNA G-quadruplex;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30256975;Dbxref=PMID:30256975	
O00571	UniProtKB	Region	100	662	.	.	.	Note=Interaction with GSK3B;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18846110;Dbxref=PMID:18846110	
O00571	UniProtKB	Region	100	110	.	.	.	Note=Interaction with IKBKE	
O00571	UniProtKB	Region	139	172	.	.	.	Note=Interaction with CHUK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17667941;Dbxref=PMID:17667941	
O00571	UniProtKB	Region	250	259	.	.	.	Note=Involved in stimulation of ATPase activity by DNA and RNA%2C nucleic acid binding and unwinding and HIV-1 replication	
O00571	UniProtKB	Region	409	662	.	.	.	Note=Interaction with HCV core protein;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10329544;Dbxref=PMID:10329544	
O00571	UniProtKB	Region	536	661	.	.	.	Note=Interaction with NXF1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18596238;Dbxref=PMID:18596238	
O00571	UniProtKB	Region	601	634	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O00571	UniProtKB	Motif	12	21	.	.	.	Note=Nuclear export signal;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:30131165,ECO:0000269|PubMed:31575075;Dbxref=PMID:30131165,PMID:31575075	
O00571	UniProtKB	Motif	180	208	.	.	.	Note=Q motif	
O00571	UniProtKB	Motif	347	350	.	.	.	Note=DEAD box	
O00571	UniProtKB	Compositional bias	19	34	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O00571	UniProtKB	Compositional bias	55	89	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O00571	UniProtKB	Compositional bias	91	142	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O00571	UniProtKB	Compositional bias	603	627	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O00571	UniProtKB	Binding site	200	207	.	.	.	.	
O00571	UniProtKB	Binding site	224	231	.	.	.	.	
O00571	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:10859333,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:22223895;Dbxref=PMID:10859333,PMID:20068231,PMID:22223895	
O00571	UniProtKB	Modified residue	55	55	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q62167	
O00571	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
O00571	UniProtKB	Modified residue	86	86	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
O00571	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
O00571	UniProtKB	Modified residue	101	101	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q62167	
O00571	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine%3B by IKKE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23478265;Dbxref=PMID:23478265	
O00571	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q62167	
O00571	UniProtKB	Modified residue	110	110	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q62167	
O00571	UniProtKB	Modified residue	118	118	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861	
O00571	UniProtKB	Modified residue	131	131	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21406692;Dbxref=PMID:21406692	
O00571	UniProtKB	Modified residue	181	181	.	.	.	Note=Phosphoserine%3B by TBK1%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine%3B by TBK1;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18583960,ECO:0007744|PubMed:24275569;Dbxref=PMID:18583960,PMID:24275569	
O00571	UniProtKB	Modified residue	240	240	.	.	.	Note=Phosphoserine%3B by TBK1%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Modified residue	269	269	.	.	.	Note=Phosphoserine%3B by TBK1%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Modified residue	429	429	.	.	.	Note=Phosphoserine%3B by CSNK1E and TBK1%3B in vitro;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18583960,ECO:0000269|PubMed:29222110;Dbxref=PMID:18583960,PMID:29222110	
O00571	UniProtKB	Modified residue	438	438	.	.	.	Note=Phosphothreonine%3B by TBK1%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Modified residue	442	442	.	.	.	Note=Phosphoserine%3B by TBK1%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Modified residue	456	456	.	.	.	Note=Phosphoserine%3B by TBK1%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Modified residue	469	469	.	.	.	Note=Phosphothreonine%3B by CSNK1E%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29222110;Dbxref=PMID:29222110	
O00571	UniProtKB	Modified residue	470	470	.	.	.	Note=Phosphoserine%3B by CSNK1E%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29222110;Dbxref=PMID:29222110	
O00571	UniProtKB	Modified residue	520	520	.	.	.	Note=Phosphoserine%3B by TBK1%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Modified residue	542	542	.	.	.	Note=Phosphothreonine%3B by TBK1%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Modified residue	543	543	.	.	.	Note=Phosphoserine%3B by CSNK1E and TBK1%3B in vitro;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18583960,ECO:0000269|PubMed:29222110;Dbxref=PMID:18583960,PMID:29222110	
O00571	UniProtKB	Modified residue	592	592	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
O00571	UniProtKB	Modified residue	594	594	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
O00571	UniProtKB	Modified residue	605	605	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
O00571	UniProtKB	Modified residue	612	612	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648	
O00571	UniProtKB	Modified residue	617	617	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
O00571	UniProtKB	Modified residue	632	632	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
O00571	UniProtKB	Cross-link	215	215	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25218447,ECO:0007744|PubMed:28112733;Dbxref=PMID:25218447,PMID:28112733	
O00571	UniProtKB	Alternative sequence	35	51	.	.	.	ID=VSP_042830;Note=In isoform 2. KGRYIPPHLRNREATKG->S;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
O00571	UniProtKB	Natural variant	214	214	.	.	.	ID=VAR_075731;Note=In MRXSSB%3B loss-of-function mutation affecting regulation of Wnt signaling. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=PMID:26235985	
O00571	UniProtKB	Natural variant	233	233	.	.	.	ID=VAR_075732;Note=In MRXSSB. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=dbSNP:rs796052223,PMID:26235985	
O00571	UniProtKB	Natural variant	233	233	.	.	.	ID=VAR_075733;Note=In MRXSSB. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=PMID:26235985	
O00571	UniProtKB	Natural variant	235	235	.	.	.	ID=VAR_075734;Note=In MRXSSB. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=dbSNP:rs796052224,PMID:26235985	
O00571	UniProtKB	Natural variant	294	294	.	.	.	ID=VAR_035839;Note=In a breast cancer sample%3B somatic mutation. R->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=PMID:16959974	
O00571	UniProtKB	Natural variant	300	300	.	.	.	ID=VAR_075735;Note=In MRXSSB. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=PMID:26235985	
O00571	UniProtKB	Natural variant	326	326	.	.	.	ID=VAR_075736;Note=In MRXSSB%3B loss-of-function mutation affecting regulation of Wnt signaling. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=dbSNP:rs797045025,PMID:26235985	
O00571	UniProtKB	Natural variant	351	351	.	.	.	ID=VAR_075737;Note=In MRXSSB. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=dbSNP:rs1057518707,PMID:26235985	
O00571	UniProtKB	Natural variant	362	362	.	.	.	ID=VAR_075738;Note=In MRXSSB. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=dbSNP:rs797045026,PMID:26235985	
O00571	UniProtKB	Natural variant	376	376	.	.	.	ID=VAR_075739;Note=In MRXSSB%3B also found as a somatic mutation in medulloblastoma%3B loss of ATPase activity%3B increased interaction with CSNK1E in the absence of dsRNA%3B contrary to wild-type protein%2C strongly interacts with CSNK1A1 and CSNK1D in vivo%3B strongly increased ability to activate CSNK1E kinase activity%2C leading to increased DVL phosphorylation%2C thereby activating Wnt/beta-catenin signaling%3B increased RNA-binding%3B no effect on subcellular location. R->C;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26235985,ECO:0000269|PubMed:29222110;Dbxref=dbSNP:rs796052231,PMID:26235985,PMID:29222110	
O00571	UniProtKB	Natural variant	392	392	.	.	.	ID=VAR_075740;Note=In MRXSSB. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=dbSNP:rs796052232,PMID:26235985	
O00571	UniProtKB	Natural variant	417	417	.	.	.	ID=VAR_075741;Note=In MRXSSB. Q->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=dbSNP:rs796052233,PMID:26235985	
O00571	UniProtKB	Natural variant	475	475	.	.	.	ID=VAR_075742;Note=In MRXSSB. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=dbSNP:rs1064794574,PMID:26235985	
O00571	UniProtKB	Natural variant	480	480	.	.	.	ID=VAR_075743;Note=In MRXSSB. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=PMID:26235985	
O00571	UniProtKB	Natural variant	488	488	.	.	.	ID=VAR_075744;Note=In MRXSSB. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=dbSNP:rs796052235,PMID:26235985	
O00571	UniProtKB	Natural variant	507	507	.	.	.	ID=VAR_075745;Note=In MRXSSB%3B loss-of-function mutation affecting regulation of Wnt signaling. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=dbSNP:rs797045024,PMID:26235985	
O00571	UniProtKB	Natural variant	509	509	.	.	.	ID=VAR_075746;Note=In MRXSSB. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=PMID:26235985	
O00571	UniProtKB	Natural variant	514	514	.	.	.	ID=VAR_075747;Note=In MRXSSB. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=dbSNP:rs796052226,PMID:26235985	
O00571	UniProtKB	Natural variant	528	528	.	.	.	ID=VAR_083115;Note=In medulloblastoma%3B somatic mutation%3B loss of ATPase activity%3B interacts with CSNK1E%2C even in the presence of dsRNA%3B contrary to wild-type protein%2C strongly interacts with CSNK1A1 and CSNK1D in vivo%3B strongly increased ability to activate CSNK1E kinase activity%2C leading to increased DVL phosphorylation%2C thereby activating Wnt/beta-catenin signaling%3B no effect on RNA-binding%2C nor on subcellular location. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29222110;Dbxref=PMID:29222110	
O00571	UniProtKB	Natural variant	534	534	.	.	.	ID=VAR_075748;Note=In MRXSSB%3B loss-of-function mutation affecting regulation of Wnt signaling. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=PMID:26235985	
O00571	UniProtKB	Natural variant	560	560	.	.	.	ID=VAR_075749;Note=In MRXSSB. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=PMID:26235985	
O00571	UniProtKB	Natural variant	568	568	.	.	.	ID=VAR_075750;Note=In MRXSSB. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26235985;Dbxref=dbSNP:rs1057519430,PMID:26235985	
O00571	UniProtKB	Mutagenesis	12	21	.	.	.	Note=Impairs nuclear export and interaction with XPO1/CMR1. LDQQFAGLDL->ADQQAAGADA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31575075;Dbxref=PMID:31575075	
O00571	UniProtKB	Mutagenesis	19	21	.	.	.	Note=Impairs nuclear export and interaction with XPO1/CMR1. LDL->ADA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30131165;Dbxref=PMID:30131165	
O00571	UniProtKB	Mutagenesis	38	38	.	.	.	Note=Impaired interaction with EIF4E%3B impaired stress granule formation%2C decreased repression of cap-dependent translation and decreased ability to enhance IRES-mediated translation. No effect on translation of HIV-1 RNA%3B when associated with A-43. Y->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17667941,ECO:0000269|PubMed:21883093,ECO:0000269|PubMed:22872150;Dbxref=PMID:17667941,PMID:21883093,PMID:22872150	
O00571	UniProtKB	Mutagenesis	43	43	.	.	.	Note=Impaired interaction with EIF4E%3B decreased repression of cap-dependent translation. Fails to induce stress granule assembly and to rescue cell viability after stress. No effect on translation of HIV-1 RNA%3B when associated with A-38. L->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17667941,ECO:0000269|PubMed:21883093,ECO:0000269|PubMed:22872150;Dbxref=PMID:17667941,PMID:21883093,PMID:22872150	
O00571	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Reduces total phosphorylation by 60%25. No effect on interaction with IKBKE. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23478265;Dbxref=PMID:23478265	
O00571	UniProtKB	Mutagenesis	82	83	.	.	.	Note=Reduces total phosphorylation by 50%25. No effect on interaction with IKBKE. SS->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23478265;Dbxref=PMID:23478265	
O00571	UniProtKB	Mutagenesis	84	85	.	.	.	Note=Loss of interaction with VACV protein K7%2C IRF3 activation and IFNB1 promoter induction. FF->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19913487;Dbxref=PMID:19913487	
O00571	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Reduces total phosphorylation by 30%25. Abolishes interaction with IRF3 and fails to enhance IFNB promoter induction. No effect on interaction with IKBKE. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23478265;Dbxref=PMID:23478265	
O00571	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Interacts with IRF3 and enhances IFNB promoter induction. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23478265;Dbxref=PMID:23478265	
O00571	UniProtKB	Mutagenesis	142	144	.	.	.	Note=Loss of interaction with TRAF3%2C reduced TRAF3 'K-63'-linked autoubiquitination. PSE->ASA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27980081;Dbxref=PMID:27980081	
O00571	UniProtKB	Mutagenesis	152	152	.	.	.	Note=Reduces total phosphorylation by 60%25. No effect on interaction with IKBKE. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23478265;Dbxref=PMID:23478265	
O00571	UniProtKB	Mutagenesis	181	181	.	.	.	Note=Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFNB1 induction%3B when associated with A-183%3B A-240 and A-269. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Mutagenesis	183	183	.	.	.	Note=Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction%3B when associated with A-181%3B A-240 and A-269. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Mutagenesis	200	200	.	.	.	Note=No effect on general translation%3B when associated with A-207%3B A-230%3B A-347 and A-348. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22323517;Dbxref=PMID:22323517	
O00571	UniProtKB	Mutagenesis	207	207	.	.	.	Note=Does not promote the translation of HIV-1 RNA. No effect on general translation%3B when associated with A-200%3B A-230: A-347 and A-348. Q->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22323517,ECO:0000269|PubMed:22872150;Dbxref=PMID:22323517,PMID:22872150	
O00571	UniProtKB	Mutagenesis	230	230	.	.	.	Note=No effect on general translation%3B when associated with A-200%3B A-207%3B A-347 and A-348. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22323517;Dbxref=PMID:22323517	
O00571	UniProtKB	Mutagenesis	230	230	.	.	.	Note=Complete loss of ATPase and RNA-unwinding activities. Loss of HIV-1 mRNA nuclear export. Does not promote the translation of HIV-1 RNA. No effect on IFNB1 induction. No effect on RNA-binding. Loss of inhibition of NF-kappa-B-mediated transcriptional activity. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15507209,ECO:0000269|PubMed:18583960,ECO:0000269|PubMed:18636090,ECO:0000269|PubMed:21589879,ECO:0000269|PubMed:22872150,ECO:0000269|PubMed:27736973;Dbxref=PMID:15507209,PMID:18583960,PMID:18636090,PMID:21589879,PMID:22872150,PMID:27736973	
O00571	UniProtKB	Mutagenesis	240	240	.	.	.	Note=Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction%3B when associated with A-181%3B A-183 and A-269. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Mutagenesis	269	269	.	.	.	Note=Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction%3B when associated with A-181%3B A-183 and A-240. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Mutagenesis	275	277	.	.	.	Note=Increased NF-kappa-B-mediated transcriptional activity%2C contrary to wild-type which is inhibitory in this experimental setting. TRE->RRV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27736973;Dbxref=PMID:27736973	
O00571	UniProtKB	Mutagenesis	347	350	.	.	.	Note=Loss of ATPase activity. DEAD->AEAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21589879;Dbxref=PMID:21589879	
O00571	UniProtKB	Mutagenesis	347	347	.	.	.	Note=No effect on general translation%3B when associated with A-200%3B A-207%3B A-230 and A-348. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22323517;Dbxref=PMID:22323517	
O00571	UniProtKB	Mutagenesis	348	348	.	.	.	Note=No effect on general translation%3B when associated with A-200%3B A-207%3B A-230 and A-347. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22323517,ECO:0000269|PubMed:22872150;Dbxref=PMID:22323517,PMID:22872150	
O00571	UniProtKB	Mutagenesis	348	348	.	.	.	Note=Loss of both ATPase and RNA helicase activities%3B decreased up-regulation of CDKN1A promoter activity and HNF4A-mediated MTTP transcriptional activation%3B no effect on the repression of cap- and IRES-dependent translation%2C WNT/beta catenin signaling%2C nor on stress granule assembly. Does not promote the translation of HIV-1 RNA. E->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17667941,ECO:0000269|PubMed:21883093,ECO:0000269|PubMed:22323517,ECO:0000269|PubMed:22872150,ECO:0000269|PubMed:23413191;Dbxref=PMID:17667941,PMID:21883093,PMID:22323517,PMID:22872150,PMID:23413191	
O00571	UniProtKB	Mutagenesis	382	384	.	.	.	Note=Loss of RNA helicase%2C but not ATPase activity%3B no effect on the repression of cap- and IRES-dependent translation%2C WNT/beta catenin signaling%2C up-regulation of CDKN1A promoter activity%2C HNF4A-mediated MTTP transcriptional activation%2C nor on stress granule assembly. SAT->AAA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17667941,ECO:0000269|PubMed:21883093,ECO:0000269|PubMed:23413191,ECO:0000269|PubMed:28128295;Dbxref=PMID:17667941,PMID:21883093,PMID:23413191,PMID:28128295	
O00571	UniProtKB	Mutagenesis	382	382	.	.	.	Note=Strong decrease in ATPase activity and RNA-unwinding activity. Does not promote the translation of mRNAs containing long structured 5'UTRs%2C including that of CCNE1. No effect on the translation of HIV-1 RNA. S->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15507209,ECO:0000269|PubMed:18596238,ECO:0000269|PubMed:20837705,ECO:0000269|PubMed:22872150;Dbxref=PMID:15507209,PMID:18596238,PMID:20837705,PMID:22872150	
O00571	UniProtKB	Mutagenesis	429	429	.	.	.	Note=Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction%3B when associated with A-438%3B A-442%3B A-456 and A-520. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Mutagenesis	438	438	.	.	.	Note=Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction%3B when associated with A-429%3B A-442%3B A-456 and A-520. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Mutagenesis	442	442	.	.	.	Note=Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction%3B when associated with A-429%3B A-438%3B A-456 and A-520. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Mutagenesis	456	456	.	.	.	Note=Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction%3B when associated with A-429%3B A-438%3B A-442 and A-520. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Mutagenesis	520	520	.	.	.	Note=Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction%3B when associated with A-429%3B A-438%3B A-442 and A-456. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18583960;Dbxref=PMID:18583960	
O00571	UniProtKB	Sequence conflict	50	50	.	.	.	Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O00571	UniProtKB	Beta strand	136	138	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E7I	
O00571	UniProtKB	Helix	144	151	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E7I	
O00571	UniProtKB	Turn	158	161	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LIU	
O00571	UniProtKB	Helix	162	165	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LIU	
O00571	UniProtKB	Beta strand	168	172	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Helix	182	184	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Helix	189	198	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Helix	205	215	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Beta strand	220	223	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Helix	230	245	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Helix	249	256	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Beta strand	261	263	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PXA	
O00571	UniProtKB	Beta strand	268	272	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Helix	276	290	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Beta strand	297	300	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Beta strand	302	304	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Helix	306	313	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Beta strand	318	322	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Helix	324	332	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Beta strand	343	348	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Helix	349	354	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Turn	355	357	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7LIU	
O00571	UniProtKB	Helix	358	365	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Beta strand	367	369	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Beta strand	376	383	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Helix	387	396	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Beta strand	401	405	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I4I	
O00571	UniProtKB	Turn	411	414	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E7J	
O00571	UniProtKB	Beta strand	415	421	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Helix	424	426	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Helix	427	437	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Beta strand	444	449	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Helix	451	463	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Beta strand	468	471	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Beta strand	473	475	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E7M	
O00571	UniProtKB	Helix	477	480	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Helix	482	488	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Beta strand	491	498	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Turn	499	501	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E7I	
O00571	UniProtKB	Turn	502	504	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Beta strand	509	517	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Helix	522	529	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Beta strand	535	537	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E7I	
O00571	UniProtKB	Beta strand	539	545	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Helix	547	552	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Helix	553	562	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Helix	569	575	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JGN	
O00571	UniProtKB	Helix	578	580	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E7J