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Database: UniProt
Entry: O00571
LinkDB: O00571
Original site: O00571 
ID   DDX3X_HUMAN             Reviewed;         662 AA.
AC   O00571; A8K538; B4E3E8; O15536;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   13-NOV-2019, entry version 225.
DE   RecName: Full=ATP-dependent RNA helicase DDX3X;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 3, X-chromosomal;
DE   AltName: Full=DEAD box, X isoform;
DE   AltName: Full=Helicase-like protein 2;
DE            Short=HLP2;
GN   Name=DDX3X; Synonyms=DBX, DDX3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Hippocampus, and Liver;
RA   Chung J., Lee S.-G., Song K.;
RT   "Identification of a human homolog of a putative RNA helicase gene
RT   (mDEAD3) expressed in mouse erythroid cells.";
RL   Korean J. Biochem. 27:193-197(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (MICROBIAL
RP   INFECTION), SUBCELLULAR LOCATION, AND INTERACTION WITH HEPATITS C
RP   VIRUS/HCV CORE PROTEIN (MICROBIAL INFECTION).
RC   TISSUE=Liver;
RX   PubMed=10329544; DOI=10.1006/viro.1999.9659;
RA   Owsianka A.M., Patel A.H.;
RT   "Hepatitis C virus core protein interacts with a human DEAD box
RT   protein DDX3.";
RL   Virology 257:330-340(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=9381176; DOI=10.1126/science.278.5338.675;
RA   Lahn B.T., Page D.C.;
RT   "Functional coherence of the human Y chromosome.";
RL   Science 278:675-680(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Uterus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT SER-2.
RX   PubMed=10859333; DOI=10.1084/jem.191.12.2083;
RA   Yaguee J., Alvarez I., Rognan D., Ramos M., Vazquez J.,
RA   Lopez de Castro J.A.;
RT   "An N-acetylated natural ligand of human histocompatibility leukocyte
RT   antigen (HLA)-B39. Classical major histocompatibility complex class I
RT   proteins bind peptides with a blocked NH(2) terminus in vivo.";
RL   J. Exp. Med. 191:2083-2092(2000).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
RA   Mann M.;
RT   "Proteomic characterization of the human centrosome by protein
RT   correlation profiling.";
RL   Nature 426:570-574(2003).
RN   [10]
RP   FUNCTION (MICROBIAL INFECTION), INTERACTION WITH XPO1, INTERACTION
RP   WITH HIV-1 PROTEIN REV (MICROBIAL INFECTION), MUTAGENESIS OF LYS-230
RP   AND SER-382, AND SUBCELLULAR LOCATION.
RX   PubMed=15507209; DOI=10.1016/j.cell.2004.09.029;
RA   Yedavalli V.S., Neuveut C., Chi Y.-H., Kleiman L., Jeang K.-T.;
RT   "Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export
RT   function.";
RL   Cell 119:381-392(2004).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [12]
RP   FUNCTION, INTERACTION WITH SP1, AND SUBCELLULAR LOCATION.
RX   PubMed=16818630; DOI=10.1158/0008-5472.can-05-2415;
RA   Chao C.H., Chen C.M., Cheng P.L., Shih J.W., Tsou A.P., Lee Y.H.;
RT   "DDX3, a DEAD box RNA helicase with tumor growth-suppressive property
RT   and transcriptional regulation activity of the p21waf1/cip1 promoter,
RT   is a candidate tumor suppressor.";
RL   Cancer Res. 66:6579-6588(2006).
RN   [13]
RP   FUNCTION.
RX   PubMed=16301996; DOI=10.1038/sj.onc.1209239;
RA   Chang P.C., Chi C.W., Chau G.Y., Li F.Y., Tsai Y.H., Wu J.C.,
RA   Wu Lee Y.H.;
RT   "DDX3, a DEAD box RNA helicase, is deregulated in hepatitis virus-
RT   associated hepatocellular carcinoma and is involved in cell growth
RT   control.";
RL   Oncogene 25:1991-2003(2006).
RN   [14]
RP   FUNCTION.
RX   PubMed=17357160; DOI=10.1002/prot.21433;
RA   Franca R., Belfiore A., Spadari S., Maga G.;
RT   "Human DEAD-box ATPase DDX3 shows a relaxed nucleoside substrate
RT   specificity.";
RL   Proteins 67:1128-1137(2007).
RN   [15]
RP   ASSOCIATION WITH SPLICED MRNAS.
RX   PubMed=17095540; DOI=10.1261/rna.336807;
RA   Merz C., Urlaub H., Will C.L., Luhrmann R.;
RT   "Protein composition of human mRNPs spliced in vitro and differential
RT   requirements for mRNP protein recruitment.";
RL   RNA 13:116-128(2007).
RN   [16]
RP   FUNCTION, AND INTERACTION WITH GSK3A; GSK3B AND TNFRSF10B.
RX   PubMed=18846110; DOI=10.1038/cdd.2008.124;
RA   Sun M., Song L., Li Y., Zhou T., Jope R.S.;
RT   "Identification of an antiapoptotic protein complex at death
RT   receptors.";
RL   Cell Death Differ. 15:1887-1900(2008).
RN   [17]
RP   FUNCTION, PHOSPHORYLATION BY TBK1 AND IKBKE, AND MUTAGENESIS OF
RP   SER-181; SER-183; SER-240; SER-269; SER-429; THR-438; SER-442; SER-456
RP   AND SER-520.
RX   PubMed=18583960; DOI=10.1038/emboj.2008.126;
RA   Soulat D., Burckstummer T., Westermayer S., Goncalves A., Bauch A.,
RA   Stefanovic A., Hantschel O., Bennett K.L., Decker T.,
RA   Superti-Furga G.;
RT   "The DEAD-box helicase DDX3X is a critical component of the TANK-
RT   binding kinase 1-dependent innate immune response.";
RL   EMBO J. 27:2135-2146(2008).
RN   [18]
RP   FUNCTION, AND INTERACTION WITH VACV PROTEIN K7 (MICROBIAL INFECTION)
RP   AND IKBKE.
RX   PubMed=18636090; DOI=10.1038/emboj.2008.143;
RA   Schroder M., Baran M., Bowie A.G.;
RT   "Viral targeting of DEAD box protein 3 reveals its role in
RT   TBK1/IKKepsilon-mediated IRF activation.";
RL   EMBO J. 27:2147-2157(2008).
RN   [19]
RP   INTERACTION WITH TDRD3.
RX   PubMed=18632687; DOI=10.1093/hmg/ddn203;
RA   Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.;
RT   "TDRD3, a novel Tudor domain-containing protein, localizes to
RT   cytoplasmic stress granules.";
RL   Hum. Mol. Genet. 17:3055-3074(2008).
RN   [20]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NXF1.
RX   PubMed=18596238; DOI=10.1091/mbc.e07-12-1264;
RA   Lai M.C., Lee Y.H., Tarn W.Y.;
RT   "The DEAD-box RNA helicase DDX3 associates with export messenger
RT   ribonucleoproteins as well as tip-associated protein and participates
RT   in translational control.";
RL   Mol. Biol. Cell 19:3847-3858(2008).
RN   [21]
RP   FUNCTION, SUBCELLULAR LOCATION, AND ASSOCIATION WITH THE EIF-3
RP   COMPLEX.
RX   PubMed=18628297; DOI=10.1093/nar/gkn454;
RA   Lee C.S., Dias A.P., Jedrychowski M., Patel A.H., Hsu J.L., Reed R.;
RT   "Human DDX3 functions in translation and interacts with the
RT   translation initiation factor eIF3.";
RL   Nucleic Acids Res. 36:4708-4718(2008).
RN   [22]
RP   FUNCTION, INTERACTION WITH EIF4E, AND MUTAGENESIS OF TYR-38 AND
RP   LEU-43.
RX   PubMed=17667941; DOI=10.1038/sj.onc.1210687;
RA   Shih J.W., Tsai T.Y., Chao C.H., Wu Lee Y.H.;
RT   "Candidate tumor suppressor DDX3 RNA helicase specifically represses
RT   cap-dependent translation by acting as an eIF4E inhibitory protein.";
RL   Oncogene 27:700-714(2008).
RN   [23]
RP   FUNCTION.
RX   PubMed=18264132; DOI=10.1038/onc.2008.33;
RA   Botlagunta M., Vesuna F., Mironchik Y., Raman A., Lisok A.,
RA   Winnard P. Jr., Mukadam S., Van Diest P., Chen J.H., Farabaugh P.,
RA   Patel A.H., Raman V.;
RT   "Oncogenic role of DDX3 in breast cancer biogenesis.";
RL   Oncogene 27:3912-3922(2008).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [25]
RP   IDENTIFICATION IN A MRNP COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=19029303; DOI=10.1261/rna.1175909;
RA   Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M.,
RA   Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.;
RT   "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic
RT   RNPs.";
RL   RNA 15:104-115(2009).
RN   [26]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [27]
RP   FUNCTION, INTERACTION WITH MAVS AND DDX58, AND SUBCELLULAR LOCATION.
RX   PubMed=20127681; DOI=10.1002/eji.200940203;
RA   Oshiumi H., Sakai K., Matsumoto M., Seya T.;
RT   "DEAD/H BOX 3 (DDX3) helicase binds the RIG-I adaptor IPS-1 to up-
RT   regulate IFN-beta-inducing potential.";
RL   Eur. J. Immunol. 40:940-948(2010).
RN   [28]
RP   FUNCTION, AND INTERACTION WITH IKBKE AND TBK1.
RX   PubMed=20375222; DOI=10.1099/vir.0.020552-0;
RA   Yu S., Chen J., Wu M., Chen H., Kato N., Yuan Z.;
RT   "Hepatitis B virus polymerase inhibits RIG-I- and Toll-like receptor
RT   3-mediated beta interferon induction in human hepatocytes through
RT   interference with interferon regulatory factor 3 activation and
RT   dampening of the interaction between TBK1/IKKepsilon and DDX3.";
RL   J. Gen. Virol. 91:2080-2090(2010).
RN   [29]
RP   FUNCTION.
RX   PubMed=20837705; DOI=10.1128/mcb.00560-10;
RA   Lai M.C., Chang W.C., Shieh S.Y., Tarn W.Y.;
RT   "DDX3 regulates cell growth through translational control of cyclin
RT   E1.";
RL   Mol. Cell. Biol. 30:5444-5453(2010).
RN   [30]
RP   FUNCTION, RNA-BINDING, INTERACTION WITH MAVS, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=21170385; DOI=10.1371/journal.pone.0014258;
RA   Oshiumi H., Ikeda M., Matsumoto M., Watanabe A., Takeuchi O.,
RA   Akira S., Kato N., Shimotohno K., Seya T.;
RT   "Hepatitis C virus core protein abrogates the DDX3 function that
RT   enhances IPS-1-mediated IFN-beta induction.";
RL   PLoS ONE 5:E14258-E14258(2010).
RN   [31]
RP   FUNCTION, AND INTERACTION WITH IKBKE.
RX   PubMed=20657822; DOI=10.1371/journal.ppat.1000986;
RA   Wang H., Ryu W.S.;
RT   "Hepatitis B virus polymerase blocks pattern recognition receptor
RT   signaling via interaction with DDX3: implications for immune
RT   evasion.";
RL   PLoS Pathog. 6:E1000986-E1000986(2010).
RN   [32]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [33]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [34]
RP   FUNCTION.
RX   PubMed=21589879; DOI=10.1371/journal.pone.0019810;
RA   Garbelli A., Beermann S., Di Cicco G., Dietrich U., Maga G.;
RT   "A motif unique to the human DEAD-box protein DDX3 is important for
RT   nucleic acid binding, ATP hydrolysis, RNA/DNA unwinding and HIV-1
RT   replication.";
RL   PLoS ONE 6:E19810-E19810(2011).
RN   [35]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH NCAPH.
RX   PubMed=21730191; DOI=10.1073/pnas.1106245108;
RA   Pek J.W., Kai T.;
RT   "DEAD-box RNA helicase Belle/DDX3 and the RNA interference pathway
RT   promote mitotic chromosome segregation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12007-12012(2011).
RN   [36]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [37]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EIF4E AND PABPC1.
RX   PubMed=21883093; DOI=10.1042/bj20110739;
RA   Shih J.W., Wang W.T., Tsai T.Y., Kuo C.Y., Li H.K., Wu Lee Y.H.;
RT   "Critical roles of RNA helicase DDX3 and its interactions with
RT   eIF4E/PABP1 in stress granule assembly and stress response.";
RL   Biochem. J. 441:119-129(2012).
RN   [38]
RP   FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INDUCTION, AND
RP   INTERACTION WITH DDX5.
RX   PubMed=22034099; DOI=10.1002/jcb.23428;
RA   Choi Y.J., Lee S.G.;
RT   "The DEAD-box RNA helicase DDX3 interacts with DDX5, co-localizes with
RT   it in the cytoplasm during the G2/M phase of the cycle, and affects
RT   its shuttling during mRNP export.";
RL   J. Cell. Biochem. 113:985-996(2012).
RN   [39]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [40]
RP   FUNCTION, ASSOCIATION WITH THE RIBOSOME SMALL SUBUNIT, INTERACTION
RP   WITH EIF3C, AND MUTAGENESIS OF TYR-200; GLN-207; LYS-230; ASP-347 AND
RP   GLU-348.
RX   PubMed=22323517; DOI=10.1093/nar/gks070;
RA   Geissler R., Golbik R.P., Behrens S.E.;
RT   "The DEAD-box helicase DDX3 supports the assembly of functional 80S
RT   ribosomes.";
RL   Nucleic Acids Res. 40:4998-5011(2012).
RN   [41]
RP   FUNCTION, RNA-BINDING, INTERACTION WITH EIF4G1 AND PABPC1, AND
RP   MUTAGENESIS OF TYR-38; LEU-43; GLN-207; LYS-230; GLU-348 AND SER-382.
RX   PubMed=22872150; DOI=10.1038/emboj.2012.220;
RA   Soto-Rifo R., Rubilar P.S., Limousin T., de Breyne S., Decimo D.,
RA   Ohlmann T.;
RT   "DEAD-box protein DDX3 associates with eIF4F to promote translation of
RT   selected mRNAs.";
RL   EMBO J. 31:3745-3756(2012).
RN   [42]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-86; SER-90;
RP   SER-594 AND SER-605, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [43]
RP   FUNCTION AS SCAFFOLD PROTEIN, INTERACTION WITH IKBKE AND IRF3,
RP   PHOSPHORYLATION AT SER-102, AND MUTAGENESIS OF SER-71; 82-SER-SER-83;
RP   SER-102 AND SER-152.
RX   PubMed=23478265; DOI=10.1128/mcb.01603-12;
RA   Gu L., Fullam A., Brennan R., Schroder M.;
RT   "Human DEAD box helicase 3 couples IkappaB kinase epsilon to
RT   interferon regulatory factor 3 activation.";
RL   Mol. Cell. Biol. 33:2004-2015(2013).
RN   [44]
RP   FUNCTION, AND INTERACTION WITH CSNK1E.
RX   PubMed=23413191; DOI=10.1126/science.1231499;
RA   Cruciat C.M., Dolde C., de Groot R.E., Ohkawara B., Reinhard C.,
RA   Korswagen H.C., Niehrs C.;
RT   "RNA helicase DDX3 is a regulatory subunit of casein kinase 1 in Wnt-
RT   beta-catenin signaling.";
RL   Science 339:1436-1441(2013).
RN   [45]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [46]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-592; ARG-617 AND ARG-632,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [47]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [48]
RP   INTERACTION WITH DHX33.
RX   PubMed=26100019; DOI=10.1128/mcb.00315-15;
RA   Zhang Y., You J., Wang X., Weber J.;
RT   "The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
RL   Mol. Cell. Biol. 35:2918-2931(2015).
RN   [49]
RP   INTERACTION WITH ERCC6.
RX   PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA   Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA   Frontini M., Willems D., Prantera G., Balajee A.S.,
RA   Proietti-De-Santis L.;
RT   "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome
RT   Group B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and
RT   Chromatin Dynamics.";
RL   PLoS ONE 10:E0128558-E0128558(2015).
RN   [50]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [51]
RP   SUBUNIT.
RX   PubMed=27546789; DOI=10.1016/j.molcel.2016.07.010;
RA   Kim Y., Myong S.;
RT   "RNA remodeling activity of DEAD box proteins tuned by protein
RT   concentration, RNA length, and ATP.";
RL   Mol. Cell 63:865-876(2016).
RN   [52]
RP   INTERACTION WITH VENEZUELAN EQUINE ENCEPHALITIS VIRUS NON-STRUCTURAL
RP   PROTEIN 3 (MICROBIAL INFECTION).
RX   PubMed=27105836; DOI=10.1016/j.antiviral.2016.04.008;
RA   Amaya M., Brooks-Faulconer T., Lark T., Keck F., Bailey C., Raman V.,
RA   Narayanan A.;
RT   "Venezuelan equine encephalitis virus non-structural protein 3 (nsP3)
RT   interacts with RNA helicases DDX1 and DDX3 in infected cells.";
RL   Antiviral Res. 131:49-60(2016).
RN   [53]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [54]
RP   X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 409-580.
RX   PubMed=17401195; DOI=10.1107/s1744309107006434;
RA   Rodamilans B., Montoya G.;
RT   "Expression, purification, crystallization and preliminary X-ray
RT   diffraction analysis of the DDX3 RNA helicase domain.";
RL   Acta Crystallogr. F 63:283-286(2007).
RN   [55]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 168-582 IN COMPLEX WITH AMP.
RX   PubMed=17631897; DOI=10.1016/j.jmb.2007.06.050;
RA   Hoegbom M., Collins R., van den Berg S., Jenvert R.-M., Karlberg T.,
RA   Kotenyova T., Flores A., Karlsson Hedestam G.B., Schiavone L.H.;
RT   "Crystal structure of conserved domains 1 and 2 of the human DEAD-box
RT   helicase DDX3X in complex with the mononucleotide AMP.";
RL   J. Mol. Biol. 372:150-159(2007).
RN   [56]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 71-90 IN COMPLEX WITH VACV
RP   PROTEIN K7 (MICROBIAL INFECTION), AND MUTAGENESIS OF 84-PHE-PHE-85.
RX   PubMed=19913487; DOI=10.1016/j.str.2009.09.005;
RA   Oda S., Schroder M., Khan A.R.;
RT   "Structural basis for targeting of human RNA helicase DDX3 by poxvirus
RT   protein K7.";
RL   Structure 17:1528-1537(2009).
RN   [57]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-294.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [58]
RP   VARIANTS MRX102 THR-214; ALA-233 DEL; VAL-233; PRO-235; PHE-300;
RP   HIS-326; GLN-351; CYS-362; CYS-376; PRO-392; PRO-417; GLY-475;
RP   SER-480; HIS-488; THR-507; ILE-509; THR-514; HIS-534; LEU-560 DEL AND
RP   LEU-568, CHARACTERIZATION OF VARIANTS MRX102 THR-214; HIS-326;
RP   CYS-376; THR-507 AND HIS-534, AND INVOLVEMENT IN MRX102.
RX   PubMed=26235985; DOI=10.1016/j.ajhg.2015.07.004;
RG   DDD Study;
RA   Snijders Blok L., Madsen E., Juusola J., Gilissen C., Baralle D.,
RA   Reijnders M.R., Venselaar H., Helsmoortel C., Cho M.T., Hoischen A.,
RA   Vissers L.E., Koemans T.S., Wissink-Lindhout W., Eichler E.E.,
RA   Romano C., Van Esch H., Stumpel C., Vreeburg M., Smeets E.,
RA   Oberndorff K., van Bon B.W., Shaw M., Gecz J., Haan E., Bienek M.,
RA   Jensen C., Loeys B.L., Van Dijck A., Innes A.M., Racher H.,
RA   Vermeer S., Di Donato N., Rump A., Tatton-Brown K., Parker M.J.,
RA   Henderson A., Lynch S.A., Fryer A., Ross A., Vasudevan P., Kini U.,
RA   Newbury-Ecob R., Chandler K., Male A., Dijkstra S., Schieving J.,
RA   Giltay J., van Gassen K.L., Schuurs-Hoeijmakers J., Tan P.L.,
RA   Pediaditakis I., Haas S.A., Retterer K., Reed P., Monaghan K.G.,
RA   Haverfield E., Natowicz M., Myers A., Kruer M.C., Stein Q.,
RA   Strauss K.A., Brigatti K.W., Keating K., Burton B.K., Kim K.H.,
RA   Charrow J., Norman J., Foster-Barber A., Kline A.D., Kimball A.,
RA   Zackai E., Harr M., Fox J., McLaughlin J., Lindstrom K., Haude K.M.,
RA   van Roozendaal K., Brunner H., Chung W.K., Kooy R.F., Pfundt R.,
RA   Kalscheuer V., Mehta S.G., Katsanis N., Kleefstra T.;
RT   "Mutations in DDX3X are a common cause of unexplained intellectual
RT   disability with gender-specific effects on Wnt signaling.";
RL   Am. J. Hum. Genet. 97:343-352(2015).
CC   -!- FUNCTION: Multifunctional ATP-dependent RNA helicase. The ATPase
CC       activity can be stimulated by various ribo- and deoxynucleic acids
CC       indicative for a relaxed substrate specificity. In vitro can
CC       unwind partially double-stranded DNA with a preference for 5'-
CC       single-stranded DNA overhangs. Is involved in several steps of
CC       gene expression, such as transcription, mRNA maturation, mRNA
CC       export and translation. However, the exact mechanisms are not
CC       known and some functions may be specific for a subset of mRNAs.
CC       Involved in transcriptional regulation. Can enhance transcription
CC       from the CDKN1A/WAF1 promoter in a SP1-dependent manner. Found
CC       associated with the E-cadherin promoter and can down-regulate
CC       transcription from the promoter. Involved in regulation of
CC       translation initiation. Proposed to be involved in positive
CC       regulation of translation such as of cyclin E1/CCNE1 mRNA and
CC       specifically of mRNAs containing complex secondary structures in
CC       their 5'UTRs; these functions seem to require RNA helicase
CC       activity. Specifically promotes translation of a subset of viral
CC       and cellular mRNAs carrying a 5'proximal stem-loop structure in
CC       their 5'UTRs and cooperates with the eIF4F complex. Proposed to
CC       act prior to 43S ribosomal scanning and to locally destabilize
CC       these RNA structures to allow recognition of the mRNA cap or
CC       loading onto the 40S subunit. After association with 40S ribosomal
CC       subunits seems to be involved in the functional assembly of 80S
CC       ribosomes; the function seems to cover translation of mRNAs with
CC       structured and non-structured 5'UTRs and is independent of RNA
CC       helicase activity. Also proposed to inhibit cap-dependent
CC       translation by competetive interaction with EIF4E which can block
CC       the EIF4E:EIF4G complex formation. Proposed to be involved in
CC       stress response and stress granule assembly; the function is
CC       independent of RNA helicase activity and seems to involve
CC       association with EIF4E. May be involved in nuclear export of
CC       specific mRNAs but not in bulk mRNA export via interactions with
CC       XPO1 and NXF1. Also associates with polyadenylated mRNAs
CC       independently of NXF1. Associates with spliced mRNAs in an exon
CC       junction complex (EJC)-dependent manner and seems not to be
CC       directly involved in splicing. May be involved in nuclear mRNA
CC       export by association with DDX5 and regulating its nuclear
CC       location. Involved in innate immune signaling promoting the
CC       production of type I interferon (IFN-alpha and IFN-beta); proposed
CC       to act as viral RNA sensor, signaling intermediate and
CC       transcriptional coactivator. Involved in TBK1 and IKBKE-dependent
CC       IRF3 activation leading to IFNB induction, plays a role of
CC       scaffolding adapter that links IKBKE and IRF3 and coordinates
CC       their activation. Also found associated with IFNB promoters; the
CC       function is independent of IRF3. Can bind to viral RNAs and via
CC       association with MAVS/IPS1 and DDX58/RIG-I is thought to induce
CC       signaling in early stages of infection. Involved in regulation of
CC       apoptosis. May be required for activation of the intrinsic but
CC       inhibit activation of the extrinsic apoptotic pathway. Acts as an
CC       antiapoptotic protein through association with GSK3A/B and BIRC2
CC       in an apoptosis antagonizing signaling complex; activation of
CC       death receptors promotes caspase-dependent cleavage of BIRC2 and
CC       DDX3X and relieves the inhibition. May be involved in mitotic
CC       chromosome segregation. Is an allosteric activator of CSNK1E, it
CC       stimulates CSNK1E-mediated phosphorylation of DVL2 and is involved
CC       in the positive regulation of canonical Wnt signaling
CC       (PubMed:23413191). {ECO:0000269|PubMed:16301996,
CC       ECO:0000269|PubMed:16818630, ECO:0000269|PubMed:17357160,
CC       ECO:0000269|PubMed:17667941, ECO:0000269|PubMed:18264132,
CC       ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:18596238,
CC       ECO:0000269|PubMed:18628297, ECO:0000269|PubMed:18636090,
CC       ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:20127681,
CC       ECO:0000269|PubMed:20375222, ECO:0000269|PubMed:20657822,
CC       ECO:0000269|PubMed:20837705, ECO:0000269|PubMed:21170385,
CC       ECO:0000269|PubMed:21730191, ECO:0000269|PubMed:21883093,
CC       ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:22323517,
CC       ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:23413191,
CC       ECO:0000269|PubMed:23478265}.
CC   -!- FUNCTION: (Microbial infection) Appears to be a prime target for
CC       viral manipulations. Hepatitis B virus (HBV) polymerase and
CC       possibly vaccinia virus (VACV) protein K7 inhibit IFNB induction
CC       probably by dissociating DDX3X from TBK1 or IKBKE. Is involved in
CC       hepatitis C virus (HCV) replication; the function may involve the
CC       association with HCV core protein. HCV core protein inhibits the
CC       IPS1-dependent function in viral RNA sensing and may switch the
CC       function from a INFB inducing to a HCV replication mode. Involved
CC       in HIV-1 replication. Acts as a cofactor for XPO1-mediated nuclear
CC       export of incompletely spliced HIV-1 Rev RNAs.
CC       {ECO:0000269|PubMed:10329544, ECO:0000269|PubMed:15507209,
CC       ECO:0000269|PubMed:21589879}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Binds RNA as a monomer at low DDX3X concentrations and as
CC       a dimer at high DDX3X concentrations (PubMed:27546789). Interacts
CC       with XPO1, TDRD3, PABPC1, NXF1, EIF3C, MAVS, DDX58 and NCAPH
CC       (PubMed:15507209, PubMed:18632687, PubMed:18596238,
CC       PubMed:20127681, PubMed:21170385, PubMed:21730191,
CC       PubMed:21883093, PubMed:22323517, PubMed:22872150). Interacts with
CC       DDX5; the interaction is regulated by the phosphorylation status
CC       of both proteins (PubMed:22034099). Interacts with EIF4E; DDX3X
CC       competes with EIF4G1/EIF4G3 for interaction with EIF4E
CC       (PubMed:17667941, PubMed:21883093). Interacts with IKBKE; the
CC       interaction is direct, found to be induced upon virus infection
CC       (PubMed:20375222, PubMed:20657822, PubMed:23478265). Interacts
CC       (when phosphorylated at Ser-102) with IRF3; the interaction allows
CC       the phosphorylation and activation of IRF3 by IKBKE
CC       (PubMed:23478265). Interacts with TBK1 (PubMed:20375222).
CC       Associates with the eukaryotic translation initiation factor 3
CC       (eIF-3) complex (PubMed:18628297). Associates with the 40S
CC       ribosome (PubMed:22323517). Identified in a mRNP complex, at least
CC       composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1,
CC       PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1 (PubMed:19029303).
CC       Interacts with SP1 (PubMed:16818630). Interacts with GSK3A, GSK3B
CC       and TNFRSF10B (PubMed:18846110). Interacts with XPO1
CC       (PubMed:15507209). Interacts with CSNK1E; the interaction enhances
CC       CSNK1E recruitment to DVL2 (PubMed:23413191). Interacts with
CC       DHX33; the interaction is independent of RNA (PubMed:26100019).
CC       Interacts with ERCC6 (PubMed:26030138).
CC       {ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:16818630,
CC       ECO:0000269|PubMed:17631897, ECO:0000269|PubMed:17667941,
CC       ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18632687,
CC       ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:18846110,
CC       ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:20127681,
CC       ECO:0000269|PubMed:20375222, ECO:0000269|PubMed:20657822,
CC       ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:21730191,
CC       ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22034099,
CC       ECO:0000269|PubMed:22323517, ECO:0000269|PubMed:22872150,
CC       ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:23478265,
CC       ECO:0000269|PubMed:26030138, ECO:0000269|PubMed:26100019,
CC       ECO:0000269|PubMed:27546789}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HCV core protein.
CC       {ECO:0000269|PubMed:10329544}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus
CC       (VACV) protein K7. {ECO:0000269|PubMed:18636090,
CC       ECO:0000269|PubMed:19913487}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Rev.
CC       {ECO:0000269|PubMed:15507209}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Venezuelan equine
CC       encephalitis virus non-structural protein 3.
CC       {ECO:0000269|PubMed:27105836}.
CC   -!- INTERACTION:
CC       P26664:- (xeno); NbExp=3; IntAct=EBI-353779, EBI-9209740;
CC       P27958:- (xeno); NbExp=11; IntAct=EBI-353779, EBI-6377335;
CC       Q99IB8:- (xeno); NbExp=9; IntAct=EBI-353779, EBI-6674379;
CC       Q9WMX2:- (xeno); NbExp=4; IntAct=EBI-353779, EBI-6863754;
CC       O95786:DDX58; NbExp=2; IntAct=EBI-353779, EBI-995350;
CC       P05198:EIF2S1; NbExp=3; IntAct=EBI-353779, EBI-1056162;
CC       P55884:EIF3B; NbExp=5; IntAct=EBI-353779, EBI-366696;
CC       Q99613:EIF3C; NbExp=3; IntAct=EBI-353779, EBI-353741;
CC       Q04637:EIF4G1; NbExp=3; IntAct=EBI-353779, EBI-73711;
CC       Q14164:IKBKE; NbExp=4; IntAct=EBI-353779, EBI-307369;
CC       P68467:K7R (xeno); NbExp=6; IntAct=EBI-353779, EBI-8022707;
CC       Q7Z434:MAVS; NbExp=4; IntAct=EBI-353779, EBI-995373;
CC       Q15003:NCAPH; NbExp=2; IntAct=EBI-353779, EBI-1046410;
CC       Q9UBU9:NXF1; NbExp=5; IntAct=EBI-353779, EBI-398874;
CC       P11940:PABPC1; NbExp=10; IntAct=EBI-353779, EBI-81531;
CC       P04608:tat (xeno); NbExp=4; IntAct=EBI-353779, EBI-6164389;
CC       Q923J1:Trpm7 (xeno); NbExp=2; IntAct=EBI-353779, EBI-8010314;
CC       P68466:VACWR039 (xeno); NbExp=6; IntAct=EBI-353779, EBI-6152154;
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm. Mitochondrion
CC       outer membrane. Note=Located predominantly in nuclear speckles
CC       and, at low levels, throughout the cytoplasm. Located to the outer
CC       side of nuclear pore complexes (NPC). Shuttles between the nucleus
CC       and the cytoplasm in a XPO1 and may be also in a NFX1-dependent
CC       manner. Associated with polyadenylated mRNAs in the cytoplasm and
CC       the nucleus. Predominantly located in nucleus during G(0) phase
CC       and in the cytoplasm during G1/S phase.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O00571-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O00571-2; Sequence=VSP_042830;
CC         Note=No experimental confirmation available.;
CC   -!- INDUCTION: Regulated by the cell cycle. Maximally expressed din
CC       the cytoplasm uring G1/S phase and decreased expression during
CC       G2/M phase. {ECO:0000269|PubMed:22034099}.
CC   -!- PTM: Phosphorylated by TBK1; the phosphorylation is required to
CC       synergize with TBK1 in IFNB induction. Phosphorylated by IKBKE at
CC       Ser-102 after ssRNA viral infection; enhances the induction of
CC       INFB promoter by IRF3. The cytoplasmic form is highly
CC       phosphorylated in the G1/S phase and much lower phosphorylated in
CC       G2/M. {ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:22034099,
CC       ECO:0000269|PubMed:23478265}.
CC   -!- DISEASE: Mental retardation, X-linked 102 (MRX102) [MIM:300958]: A
CC       form of mental retardation, a disorder characterized by
CC       significantly below average general intellectual functioning
CC       associated with impairments in adaptive behavior and manifested
CC       during the developmental period. Intellectual deficiency is the
CC       only primary symptom of non-syndromic X-linked mental retardation,
CC       while syndromic mental retardation presents with associated
CC       physical, neurological and/or psychiatric manifestations. MRX102
CC       features include mild to severe intellectual disability,
CC       hypotonia, movement disorders, behavior problems, corpus callosum
CC       hypoplasia, and epilepsy. Additionally, patients manifest variable
CC       non-neurologic features such as joint hyperlaxity, skin pigmentary
CC       abnormalities, cleft lip and/or palate, hearing and visual
CC       impairment, and precocious puberty. {ECO:0000269|PubMed:26235985}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC       subfamily. {ECO:0000305}.
DR   EMBL; U50553; AAB95637.1; -; mRNA.
DR   EMBL; AF061337; AAC34298.1; -; mRNA.
DR   EMBL; AF000983; AAC51830.1; -; mRNA.
DR   EMBL; AF000982; AAC51829.1; -; mRNA.
DR   EMBL; AK291153; BAF83842.1; -; mRNA.
DR   EMBL; AK304689; BAG65460.1; -; mRNA.
DR   EMBL; AL391647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z93015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471141; EAW59402.1; -; Genomic_DNA.
DR   EMBL; CH471141; EAW59403.1; -; Genomic_DNA.
DR   EMBL; CH471141; EAW59404.1; -; Genomic_DNA.
DR   EMBL; CH471141; EAW59405.1; -; Genomic_DNA.
DR   EMBL; BC011819; AAH11819.1; -; mRNA.
DR   CCDS; CCDS43931.1; -. [O00571-1]
DR   CCDS; CCDS55404.1; -. [O00571-2]
DR   RefSeq; NP_001180345.1; NM_001193416.2.
DR   RefSeq; NP_001180346.1; NM_001193417.2. [O00571-2]
DR   RefSeq; NP_001347.3; NM_001356.4. [O00571-1]
DR   PDB; 2I4I; X-ray; 2.20 A; A=168-582.
DR   PDB; 2JGN; X-ray; 1.91 A; A/B/C=409-580.
DR   PDB; 3JRV; X-ray; 1.60 A; C/D/E=71-90.
DR   PDB; 4O2C; X-ray; 1.80 A; C=2-10.
DR   PDB; 4O2E; X-ray; 1.98 A; C/F=2-10.
DR   PDB; 4O2F; X-ray; 1.90 A; C/F=3-10.
DR   PDB; 4PX9; X-ray; 2.31 A; A/B/C=135-407.
DR   PDB; 4PXA; X-ray; 3.20 A; A=135-582.
DR   PDB; 5E7I; X-ray; 2.22 A; A/B/C=133-584.
DR   PDB; 5E7J; X-ray; 2.23 A; A=133-584.
DR   PDB; 5E7M; X-ray; 2.30 A; A=133-584.
DR   PDB; 6CZ5; X-ray; 3.00 A; A=132-607.
DR   PDB; 6O5F; X-ray; 2.50 A; A/B=132-607.
DR   PDBsum; 2I4I; -.
DR   PDBsum; 2JGN; -.
DR   PDBsum; 3JRV; -.
DR   PDBsum; 4O2C; -.
DR   PDBsum; 4O2E; -.
DR   PDBsum; 4O2F; -.
DR   PDBsum; 4PX9; -.
DR   PDBsum; 4PXA; -.
DR   PDBsum; 5E7I; -.
DR   PDBsum; 5E7J; -.
DR   PDBsum; 5E7M; -.
DR   PDBsum; 6CZ5; -.
DR   PDBsum; 6O5F; -.
DR   SMR; O00571; -.
DR   BioGrid; 108020; 284.
DR   CORUM; O00571; -.
DR   DIP; DIP-27551N; -.
DR   ELM; O00571; -.
DR   IntAct; O00571; 126.
DR   MINT; O00571; -.
DR   STRING; 9606.ENSP00000382840; -.
DR   BindingDB; O00571; -.
DR   ChEMBL; CHEMBL5553; -.
DR   TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
DR   CarbonylDB; O00571; -.
DR   iPTMnet; O00571; -.
DR   PhosphoSitePlus; O00571; -.
DR   SwissPalm; O00571; -.
DR   BioMuta; DDX3X; -.
DR   REPRODUCTION-2DPAGE; IPI00215637; -.
DR   SWISS-2DPAGE; O00571; -.
DR   EPD; O00571; -.
DR   jPOST; O00571; -.
DR   MassIVE; O00571; -.
DR   MaxQB; O00571; -.
DR   PaxDb; O00571; -.
DR   PeptideAtlas; O00571; -.
DR   PRIDE; O00571; -.
DR   ProteomicsDB; 47982; -. [O00571-1]
DR   ProteomicsDB; 47983; -. [O00571-2]
DR   Ensembl; ENST00000457138; ENSP00000392494; ENSG00000215301. [O00571-2]
DR   Ensembl; ENST00000478993; ENSP00000478443; ENSG00000215301. [O00571-1]
DR   Ensembl; ENST00000629496; ENSP00000487224; ENSG00000215301. [O00571-1]
DR   Ensembl; ENST00000629785; ENSP00000486516; ENSG00000215301. [O00571-1]
DR   Ensembl; ENST00000630255; ENSP00000486720; ENSG00000215301. [O00571-1]
DR   Ensembl; ENST00000644876; ENSP00000494040; ENSG00000215301. [O00571-1]
DR   GeneID; 1654; -.
DR   KEGG; hsa:1654; -.
DR   UCSC; uc004dfe.4; human. [O00571-1]
DR   CTD; 1654; -.
DR   DisGeNET; 1654; -.
DR   GeneCards; DDX3X; -.
DR   HGNC; HGNC:2745; DDX3X.
DR   HPA; HPA001648; -.
DR   HPA; HPA005631; -.
DR   HPA; HPA059585; -.
DR   MalaCards; DDX3X; -.
DR   MIM; 300160; gene.
DR   MIM; 300958; phenotype.
DR   neXtProt; NX_O00571; -.
DR   OpenTargets; ENSG00000215301; -.
DR   Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR   Orphanet; 3338; Toriello-Carey syndrome.
DR   Orphanet; 457260; X-linked intellectual disability-hypotonia-movement disorder syndrome.
DR   PharmGKB; PA27216; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   eggNOG; ENOG410XNTI; LUCA.
DR   GeneTree; ENSGT00940000154443; -.
DR   InParanoid; O00571; -.
DR   KO; K11594; -.
DR   OrthoDB; 595675at2759; -.
DR   PhylomeDB; O00571; -.
DR   TreeFam; TF300364; -.
DR   BRENDA; 3.6.4.13; 2681.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SIGNOR; O00571; -.
DR   ChiTaRS; DDX3X; human.
DR   EvolutionaryTrace; O00571; -.
DR   GeneWiki; DDX3X; -.
DR   GenomeRNAi; 1654; -.
DR   Pharos; O00571; -.
DR   PRO; PR:O00571; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; ENSG00000215301; Expressed in 243 organ(s), highest expression level in substantia nigra.
DR   ExpressionAtlas; O00571; baseline and differential.
DR   Genevisible; O00571; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0043186; C:P granule; IBA:GO_Central.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0043273; F:CTPase activity; IDA:AgBase.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR   GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IDA:AgBase.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:UniProtKB.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:AgBase.
DR   GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
DR   GO; GO:0043024; F:ribosomal small subunit binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR   GO; GO:0035613; F:RNA stem-loop binding; IDA:UniProtKB.
DR   GO; GO:0033592; F:RNA strand annealing activity; IDA:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
DR   GO; GO:0031369; F:translation initiation factor binding; IDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0071243; P:cellular response to arsenic-containing substance; IDA:UniProtKB.
DR   GO; GO:0071470; P:cellular response to osmotic stress; IDA:UniProtKB.
DR   GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR   GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
DR   GO; GO:0007276; P:gamete generation; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR   GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR   GO; GO:0042256; P:mature ribosome assembly; IMP:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR   GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR   GO; GO:0031333; P:negative regulation of protein complex assembly; IDA:UniProtKB.
DR   GO; GO:0017148; P:negative regulation of translation; IMP:UniProtKB.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR   GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR   GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; TAS:UniProtKB.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR   GO; GO:0032728; P:positive regulation of interferon-beta production; TAS:UniProtKB.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
DR   GO; GO:0045948; P:positive regulation of translational initiation; IMP:UniProtKB.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; IMP:AgBase.
DR   GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IMP:AgBase.
DR   GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; IDA:UniProtKB.
DR   GO; GO:0034063; P:stress granule assembly; IDA:UniProtKB.
DR   GO; GO:0006413; P:translational initiation; IMP:UniProtKB.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IMP:UniProtKB.
DR   DisProt; DP02192; -.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Apoptosis;
KW   ATP-binding; Chromosome partition; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Disease mutation; DNA-binding; Helicase;
KW   Host-virus interaction; Hydrolase; Immunity; Innate immunity;
KW   Isopeptide bond; Membrane; Mental retardation; Methylation;
KW   Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW   Ribosome biogenesis; RNA-binding; Transcription;
KW   Transcription regulation; Translation regulation; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:22223895,
FT                                ECO:0000269|PubMed:10859333}.
FT   CHAIN         2    662       ATP-dependent RNA helicase DDX3X.
FT                                /FTId=PRO_0000055009.
FT   DOMAIN      211    403       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      414    575       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     200    207       ATP.
FT   NP_BIND     224    231       ATP.
FT   REGION        2    139       Required for TBK1 and IKBKE-dependent
FT                                IFN-beta activation.
FT   REGION        2    100       Interaction with EIF4E.
FT   REGION       81     90       Required for interaction with VACV
FT                                protein K7.
FT   REGION      100    662       Interaction with GSK3B.
FT                                {ECO:0000269|PubMed:18846110}.
FT   REGION      100    110       Required for interaction with IKBKE.
FT   REGION      250    259       Involved in stimulation of ATPase
FT                                activity by DNA and RNA, nucleic acid
FT                                binding and unwinding and HIV-1
FT                                replication.
FT   REGION      260    517       Necessary for interaction with XPO1.
FT                                {ECO:0000269|PubMed:15507209}.
FT   MOTIF       180    208       Q motif.
FT   MOTIF       347    350       DEAD box.
FT   COMPBIAS    582    662       Gly/Ser-rich.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:22223895,
FT                                ECO:0000269|PubMed:10859333}.
FT   MOD_RES      55     55       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q62167}.
FT   MOD_RES      82     82       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES      86     86       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES      90     90       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     101    101       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q62167}.
FT   MOD_RES     102    102       Phosphoserine; by IKKE.
FT                                {ECO:0000269|PubMed:23478265}.
FT   MOD_RES     104    104       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q62167}.
FT   MOD_RES     110    110       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q62167}.
FT   MOD_RES     118    118       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     131    131       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     183    183       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     456    456       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q62095}.
FT   MOD_RES     592    592       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     594    594       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     605    605       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     612    612       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     617    617       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     632    632       Omega-N-methylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   CROSSLNK    215    215       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ      35     51       KGRYIPPHLRNREATKG -> S (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_042830.
FT   VARIANT     214    214       I -> T (in MRX102; loss-of-function
FT                                mutation affecting regulation of Wnt
FT                                signaling).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075731.
FT   VARIANT     233    233       A -> V (in MRX102; dbSNP:rs796052223).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075732.
FT   VARIANT     233    233       Missing (in MRX102).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075733.
FT   VARIANT     235    235       L -> P (in MRX102; dbSNP:rs796052224).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075734.
FT   VARIANT     294    294       R -> T (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035839.
FT   VARIANT     300    300       V -> F (in MRX102).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075735.
FT   VARIANT     326    326       R -> H (in MRX102; loss-of-function
FT                                mutation affecting regulation of Wnt
FT                                signaling; dbSNP:rs797045025).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075736.
FT   VARIANT     351    351       R -> Q (in MRX102; dbSNP:rs1057518707).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075737.
FT   VARIANT     362    362       R -> C (in MRX102; dbSNP:rs797045026).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075738.
FT   VARIANT     376    376       R -> C (in MRX102; loss-of-function
FT                                mutation affecting regulation of Wnt
FT                                signaling; dbSNP:rs796052231).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075739.
FT   VARIANT     392    392       L -> P (in MRX102; dbSNP:rs796052232).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075740.
FT   VARIANT     417    417       Q -> P (in MRX102; dbSNP:rs796052233).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075741.
FT   VARIANT     475    475       R -> G (in MRX102; dbSNP:rs1064794574).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075742.
FT   VARIANT     480    480       R -> S (in MRX102).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075743.
FT   VARIANT     488    488       R -> H (in MRX102; dbSNP:rs796052235).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075744.
FT   VARIANT     507    507       I -> T (in MRX102; loss-of-function
FT                                mutation affecting regulation of Wnt
FT                                signaling; dbSNP:rs797045024).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075745.
FT   VARIANT     509    509       N -> I (in MRX102).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075746.
FT   VARIANT     514    514       I -> T (in MRX102; dbSNP:rs796052226).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075747.
FT   VARIANT     534    534       R -> H (in MRX102; loss-of-function
FT                                mutation affecting regulation of Wnt
FT                                signaling).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075748.
FT   VARIANT     560    560       Missing (in MRX102).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075749.
FT   VARIANT     568    568       P -> L (in MRX102; dbSNP:rs1057519430).
FT                                {ECO:0000269|PubMed:26235985}.
FT                                /FTId=VAR_075750.
FT   MUTAGEN      38     38       Y->A: Impairs interaction with EIF4E. No
FT                                effect on translation of HIV-1 RNA; when
FT                                associated with A-43.
FT                                {ECO:0000269|PubMed:17667941,
FT                                ECO:0000269|PubMed:22872150}.
FT   MUTAGEN      43     43       L->A: Impairs interaction with EIF4E.
FT                                Fails to induce stress granule assembly
FT                                and to rescue cell viability after
FT                                stress. No effect on translation of HIV-1
FT                                RNA; when associated with A-38.
FT                                {ECO:0000269|PubMed:17667941,
FT                                ECO:0000269|PubMed:22872150}.
FT   MUTAGEN      71     71       S->A: Reduces total phosphorylation by
FT                                60%. No effect on interaction with IKBKE.
FT                                {ECO:0000269|PubMed:23478265}.
FT   MUTAGEN      82     83       SS->AA: Reduces total phosphorylation by
FT                                50%. No effect on interaction with IKBKE.
FT                                {ECO:0000269|PubMed:23478265}.
FT   MUTAGEN      84     85       FF->AA: Abolishes interaction with VACV
FT                                protein K7, IRF3 activation and IFN-beta
FT                                promoter induction.
FT                                {ECO:0000269|PubMed:19913487}.
FT   MUTAGEN     102    102       S->A: Reduces total phosphorylation by
FT                                30%. Abolishes interaction with IRF3 and
FT                                fails to enhance IFNB promoter induction.
FT                                No effect on interaction with IKBKE.
FT                                {ECO:0000269|PubMed:23478265}.
FT   MUTAGEN     102    102       S->D: Interacts with IRF3 and enhances
FT                                IFNB promoter induction.
FT                                {ECO:0000269|PubMed:23478265}.
FT   MUTAGEN     152    152       S->A: Reduces total phosphorylation by
FT                                60%. No effect on interaction with IKBKE.
FT                                {ECO:0000269|PubMed:23478265}.
FT   MUTAGEN     181    181       S->A: Greatly impairs phosphorylation by
FT                                TBK1 and fails to synergize with TBK1 in
FT                                IFN-beta induction; when associated with
FT                                A-183; A-240 and A-269.
FT                                {ECO:0000269|PubMed:18583960}.
FT   MUTAGEN     183    183       S->A: Greatly impairs phosphorylation by
FT                                TBK1 and fails to synergize with TBK1 in
FT                                IFN-beta induction; when associated with
FT                                A-181; A-240 and A-269.
FT                                {ECO:0000269|PubMed:18583960}.
FT   MUTAGEN     200    200       Y->A: No effect on general translation;
FT                                when associated with A-207; A-230; A-347
FT                                and A-348. {ECO:0000269|PubMed:22323517}.
FT   MUTAGEN     207    207       Q->A: Inhibits translation of HIV-1 RNA.
FT                                No effect on general translation; when
FT                                associated with A-200; A-230: A-347 and
FT                                A-348. {ECO:0000269|PubMed:22323517,
FT                                ECO:0000269|PubMed:22872150}.
FT   MUTAGEN     230    230       K->A: No effect on general translation;
FT                                when associated with A-200; A-207; A-347
FT                                and A-348. {ECO:0000269|PubMed:15507209,
FT                                ECO:0000269|PubMed:22323517,
FT                                ECO:0000269|PubMed:22872150}.
FT   MUTAGEN     230    230       K->E: Abolishes ATPase activity and RNA-
FT                                unwinding activity. Inhibits translation
FT                                of HIV-1 RNA.
FT                                {ECO:0000269|PubMed:15507209,
FT                                ECO:0000269|PubMed:22323517,
FT                                ECO:0000269|PubMed:22872150}.
FT   MUTAGEN     240    240       S->A: Greatly impairs phosphorylation by
FT                                TBK1 and fails to synergize with TBK1 in
FT                                IFN-beta induction; when associated with
FT                                A-181; A-183 and A-269.
FT                                {ECO:0000269|PubMed:18583960}.
FT   MUTAGEN     269    269       S->A: Greatly impairs phosphorylation by
FT                                TBK1 and fails to synergize with TBK1 in
FT                                IFN-beta induction; when associated with
FT                                A-181; A-183 and A-240.
FT                                {ECO:0000269|PubMed:18583960}.
FT   MUTAGEN     347    347       D->A: No effect on general translation;
FT                                when associated with A-200; A-207; A-230
FT                                and A-348. {ECO:0000269|PubMed:22323517}.
FT   MUTAGEN     348    348       E->A: No effect on general translation;
FT                                when associated with A-200; A-207; A-230
FT                                and A-347. {ECO:0000269|PubMed:22323517,
FT                                ECO:0000269|PubMed:22872150}.
FT   MUTAGEN     348    348       E->Q: Inhibits translation of HIV-1 RNA.
FT                                {ECO:0000269|PubMed:22323517,
FT                                ECO:0000269|PubMed:22872150}.
FT   MUTAGEN     382    382       S->L: Abolishes ATPase activity and RNA-
FT                                unwinding activity. No effect on
FT                                translation of HIV-1 RNA.
FT                                {ECO:0000269|PubMed:15507209,
FT                                ECO:0000269|PubMed:22872150}.
FT   MUTAGEN     429    429       S->A: Impairs phosphorylation by TBK1 and
FT                                fails to synergize with TBK1 in IFN-beta
FT                                induction; when associated with A-438; A-
FT                                442; A-456 and A-520.
FT                                {ECO:0000269|PubMed:18583960}.
FT   MUTAGEN     438    438       T->A: Impairs phosphorylation by TBK1 and
FT                                fails to synergize with TBK1 in IFN-beta
FT                                induction; when associated with A-429; A-
FT                                442; A-456 and A-520.
FT                                {ECO:0000269|PubMed:18583960}.
FT   MUTAGEN     442    442       S->A: Impairs phosphorylation by TBK1 and
FT                                fails to synergize with TBK1 in IFN-beta
FT                                induction; when associated with A-429; A-
FT                                438; A-456 and A-520.
FT                                {ECO:0000269|PubMed:18583960}.
FT   MUTAGEN     456    456       S->A: Impairs phosphorylation by TBK1 and
FT                                fails to synergize with TBK1 in IFN-beta
FT                                induction; when associated with A-429; A-
FT                                438; A-442 and A-520.
FT                                {ECO:0000269|PubMed:18583960}.
FT   MUTAGEN     520    520       S->A: Impairs phosphorylation by TBK1 and
FT                                fails to synergize with TBK1 in IFN-beta
FT                                induction; when associated with A-429; A-
FT                                438; A-442 and A-456.
FT                                {ECO:0000269|PubMed:18583960}.
FT   CONFLICT     50     50       K -> R (in Ref. 3; AAC51830/AAC51829).
FT                                {ECO:0000305}.
FT   STRAND      136    138       {ECO:0000244|PDB:5E7I}.
FT   HELIX       144    151       {ECO:0000244|PDB:5E7I}.
FT   STRAND      161    163       {ECO:0000244|PDB:4PXA}.
FT   STRAND      168    172       {ECO:0000244|PDB:2I4I}.
FT   HELIX       182    184       {ECO:0000244|PDB:2I4I}.
FT   HELIX       189    198       {ECO:0000244|PDB:2I4I}.
FT   HELIX       205    215       {ECO:0000244|PDB:2I4I}.
FT   STRAND      220    223       {ECO:0000244|PDB:2I4I}.
FT   HELIX       230    245       {ECO:0000244|PDB:2I4I}.
FT   HELIX       249    256       {ECO:0000244|PDB:2I4I}.
FT   STRAND      261    263       {ECO:0000244|PDB:4PXA}.
FT   STRAND      268    272       {ECO:0000244|PDB:2I4I}.
FT   HELIX       276    290       {ECO:0000244|PDB:2I4I}.
FT   STRAND      297    300       {ECO:0000244|PDB:2I4I}.
FT   STRAND      302    304       {ECO:0000244|PDB:2I4I}.
FT   HELIX       306    313       {ECO:0000244|PDB:2I4I}.
FT   STRAND      318    322       {ECO:0000244|PDB:2I4I}.
FT   HELIX       324    332       {ECO:0000244|PDB:2I4I}.
FT   STRAND      343    348       {ECO:0000244|PDB:2I4I}.
FT   HELIX       349    354       {ECO:0000244|PDB:2I4I}.
FT   HELIX       358    365       {ECO:0000244|PDB:2I4I}.
FT   STRAND      367    369       {ECO:0000244|PDB:2I4I}.
FT   STRAND      376    383       {ECO:0000244|PDB:2I4I}.
FT   HELIX       387    396       {ECO:0000244|PDB:2I4I}.
FT   STRAND      401    405       {ECO:0000244|PDB:2I4I}.
FT   TURN        411    414       {ECO:0000244|PDB:5E7J}.
FT   STRAND      415    421       {ECO:0000244|PDB:2JGN}.
FT   HELIX       424    426       {ECO:0000244|PDB:2JGN}.
FT   HELIX       427    437       {ECO:0000244|PDB:2JGN}.
FT   STRAND      444    449       {ECO:0000244|PDB:2JGN}.
FT   HELIX       451    463       {ECO:0000244|PDB:2JGN}.
FT   STRAND      468    471       {ECO:0000244|PDB:2JGN}.
FT   STRAND      473    475       {ECO:0000244|PDB:5E7M}.
FT   HELIX       477    480       {ECO:0000244|PDB:2JGN}.
FT   HELIX       482    488       {ECO:0000244|PDB:2JGN}.
FT   STRAND      491    498       {ECO:0000244|PDB:2JGN}.
FT   TURN        499    501       {ECO:0000244|PDB:5E7I}.
FT   TURN        502    504       {ECO:0000244|PDB:2JGN}.
FT   STRAND      509    517       {ECO:0000244|PDB:2JGN}.
FT   HELIX       522    529       {ECO:0000244|PDB:2JGN}.
FT   STRAND      535    537       {ECO:0000244|PDB:5E7I}.
FT   STRAND      539    545       {ECO:0000244|PDB:2JGN}.
FT   HELIX       547    552       {ECO:0000244|PDB:2JGN}.
FT   HELIX       553    562       {ECO:0000244|PDB:2JGN}.
FT   HELIX       569    575       {ECO:0000244|PDB:2JGN}.
FT   HELIX       578    580       {ECO:0000244|PDB:5E7J}.
SQ   SEQUENCE   662 AA;  73243 MW;  7074D2B8A6EBBF09 CRC64;
     MSHVAVENAL GLDQQFAGLD LNSSDNQSGG STASKGRYIP PHLRNREATK GFYDKDSSGW
     SSSKDKDAYS SFGSRSDSRG KSSFFSDRGS GSRGRFDDRG RSDYDGIGSR GDRSGFGKFE
     RGGNSRWCDK SDEDDWSKPL PPSERLEQEL FSGGNTGINF EKYDDIPVEA TGNNCPPHIE
     SFSDVEMGEI IMGNIELTRY TRPTPVQKHA IPIIKEKRDL MACAQTGSGK TAAFLLPILS
     QIYSDGPGEA LRAMKENGRY GRRKQYPISL VLAPTRELAV QIYEEARKFS YRSRVRPCVV
     YGGADIGQQI RDLERGCHLL VATPGRLVDM MERGKIGLDF CKYLVLDEAD RMLDMGFEPQ
     IRRIVEQDTM PPKGVRHTMM FSATFPKEIQ MLARDFLDEY IFLAVGRVGS TSENITQKVV
     WVEESDKRSF LLDLLNATGK DSLTLVFVET KKGADSLEDF LYHEGYACTS IHGDRSQRDR
     EEALHQFRSG KSPILVATAV AARGLDISNV KHVINFDLPS DIEEYVHRIG RTGRVGNLGL
     ATSFFNERNI NITKDLLDLL VEAKQEVPSW LENMAYEHHY KGSSRGRSKS SRFSGGFGAR
     DYRQSSGASS SSFSSSRASS SRSGGGGHGS SRGFGGGGYG GFYNSDGYGG NYNSQGVDWW
     GN
//
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