DDX3X_HUMAN
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 03-AUG-2022, entry version 239.
DE RecName: Full=ATP-dependent RNA helicase DDX3X;
DE EC=3.6.4.13 {ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:17357160, ECO:0000269|PubMed:21589879, ECO:0000269|PubMed:31300642, ECO:0000269|PubMed:31575075};
DE AltName: Full=CAP-Rf;
DE AltName: Full=DEAD box protein 3, X-chromosomal;
DE AltName: Full=DEAD box, X isoform;
DE Short=DBX;
DE AltName: Full=Helicase-like protein 2;
DE Short=HLP2;
GN Name=DDX3X; Synonyms=DBX {ECO:0000303|PubMed:15294876}, DDX3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Chung J., Lee S.-G., Song K.;
RT "Identification of a human homolog of a putative RNA helicase gene (mDEAD3)
RT expressed in mouse erythroid cells.";
RL Korean J. Biochem. 27:193-197(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH HEPATITIS C VIRUS 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 protein
RT DDX3.";
RL Virology 257:330-340(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ESCAPE FROM X-INACTIVATION.
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., 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., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., 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., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., 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., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., 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., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [10]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), INTERACTION WITH XPO1,
RP INTERACTION WITH HIV-1 PROTEIN REV (MICROBIAL INFECTION), MUTAGENESIS OF
RP LYS-230 AND SER-382, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
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 TISSUE SPECIFICITY.
RX PubMed=15294876; DOI=10.1093/hmg/ddh240;
RA Ditton H.J., Zimmer J., Kamp C., Rajpert-De Meyts E., Vogt P.H.;
RT "The AZFa gene DBY (DDX3Y) is widely transcribed but the protein is limited
RT to the male germ cells by translation control.";
RL Hum. Mol. Genet. 13:2333-2341(2004).
RN [12]
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 cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP FUNCTION, INTERACTION WITH SP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF GLU-348 AND 382-SER--THR-384.
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 and
RT transcriptional regulation activity of the p21waf1/cip1 promoter, is a
RT candidate tumor suppressor.";
RL Cancer Res. 66:6579-6588(2006).
RN [14]
RP TISSUE SPECIFICITY.
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., 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 [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 [16]
RP ASSOCIATION WITH MRNPS.
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 [17]
RP FUNCTION, INTERACTION WITH FAS; GSK3A; GSK3B; TNFRSF10A AND TNFRSF10B, AND
RP CLEAVAGE BY CASPASES.
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 receptors.";
RL Cell Death Differ. 15:1887-1900(2008).
RN [18]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), PHOSPHORYLATION AT SER-181;
RP SER-183; SER-240; SER-269; SER-429; THR-438; SER-442; SER-456; SER-520;
RP THR-542 AND SER-543, AND MUTAGENESIS OF SER-181; SER-183; LYS-230; SER-240;
RP SER-269; SER-429; THR-438; SER-442; SER-456 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., Superti-Furga G.;
RT "The DEAD-box helicase DDX3X is a critical component of the TANK-binding
RT kinase 1-dependent innate immune response.";
RL EMBO J. 27:2135-2146(2008).
RN [19]
RP FUNCTION, INTERACTION WITH VACV PROTEIN K7 (MICROBIAL INFECTION) AND IKBKE,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-230.
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 TBK1/IKKepsilon-
RT mediated IRF activation.";
RL EMBO J. 27:2147-2157(2008).
RN [20]
RP INTERACTION WITH TDRD3, AND SUBCELLULAR LOCATION.
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 cytoplasmic
RT stress granules.";
RL Hum. Mol. Genet. 17:3055-3074(2008).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF4A1; EIF2S1; NXF1 AND
RP PABPC1, ASSOCIATION WITH MRNPS, AND MUTAGENESIS OF SER-382.
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 in
RT translational control.";
RL Mol. Biol. Cell 19:3847-3858(2008).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF3B, AND ASSOCIATION
RP WITH THE EIF-3 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 translation
RT initiation factor eIF3.";
RL Nucleic Acids Res. 36:4708-4718(2008).
RN [23]
RP FUNCTION, INTERACTION WITH EIF4E, AND MUTAGENESIS OF TYR-38; LEU-43;
RP GLU-348 AND 382-SER--THR-384.
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 cap-
RT dependent translation by acting as an eIF4E inhibitory protein.";
RL Oncogene 27:700-714(2008).
RN [24]
RP FUNCTION.
RX PubMed=18264132; DOI=10.1038/onc.2008.33;
RA Botlagunta M., Vesuna F., Mironchik Y., Raman A., Lisok A., Winnard P. Jr.,
RA Mukadam S., Van Diest P., Chen J.H., Farabaugh P., Patel A.H., Raman V.;
RT "Oncogenic role of DDX3 in breast cancer biogenesis.";
RL Oncogene 27:3912-3922(2008).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, AND IDENTIFICATION BY
RP 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 [26]
RP IDENTIFICATION IN AN MRNP COMPLEX, INTERACTION WITH IGF2BP1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A.,
RA Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.";
RL RNA 15:104-115(2009).
RN [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [28]
RP FUNCTION, INTERACTION WITH IFIH1; 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-regulate
RT IFN-beta-inducing potential.";
RL Eur. J. Immunol. 40:940-948(2010).
RN [29]
RP FUNCTION, INTERACTION WITH TBK1, AND INTERACTION WITH HEPATITIS B VIRUS
RP POLYMERASE (MICROBIAL INFECTION).
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 3-
RT mediated beta interferon induction in human hepatocytes through
RT interference with interferon regulatory factor 3 activation and dampening
RT of the interaction between TBK1/IKKepsilon and DDX3.";
RL J. Gen. Virol. 91:2080-2090(2010).
RN [30]
RP FUNCTION, AND MUTAGENESIS OF SER-382.
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 E1.";
RL Mol. Cell. Biol. 30:5444-5453(2010).
RN [31]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), RNA-BINDING, INTERACTION WITH
RP MAVS, AND SUBCELLULAR LOCATION.
RX PubMed=21170385; DOI=10.1371/journal.pone.0014258;
RA Oshiumi H., Ikeda M., Matsumoto M., Watanabe A., Takeuchi O., Akira S.,
RA Kato N., Shimotohno K., Seya T.;
RT "Hepatitis C virus core protein abrogates the DDX3 function that enhances
RT IPS-1-mediated IFN-beta induction.";
RL PLoS ONE 5:E14258-E14258(2010).
RN [32]
RP FUNCTION, INTERACTION WITH IKBKE, AND INTERACTION WITH HEPATITIS B VIRUS
RP POLYMERASE (MICROBIAL INFECTION).
RX PubMed=20657822; DOI=10.1371/journal.ppat.1000986;
RA Wang H., Ryu W.S.;
RT "Hepatitis B virus polymerase blocks pattern recognition receptor signaling
RT via interaction with DDX3: implications for immune evasion.";
RL PLoS Pathog. 6:E1000986-E1000986(2010).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [34]
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., Buerckstuemmer T.,
RA 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 [35]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LYS-230 AND
RP 347-ASP--ASP-350.
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 nucleic
RT acid binding, ATP hydrolysis, RNA/DNA unwinding and HIV-1 replication.";
RL PLoS ONE 6:E19810-E19810(2011).
RN [36]
RP FUNCTION, INTERACTION WITH NCAPH, AND SUBCELLULAR LOCATION.
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 promote
RT mitotic chromosome segregation.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12007-12012(2011).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [38]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF4E AND PABPC1, AND
RP MUTAGENESIS OF LEU-43; GLU-348 AND 382-SER--THR-384.
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 eIF4E/PABP1
RT in stress granule assembly and stress response.";
RL Biochem. J. 441:119-129(2012).
RN [39]
RP SUBCELLULAR LOCATION, INTERACTION WITH DDX5, AND PHOSPHORYLATION.
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 it
RT in the cytoplasm during the G2/M phase of the cycle, and affects its
RT shuttling during mRNP export.";
RL J. Cell. Biochem. 113:985-996(2012).
RN [40]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA 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 [41]
RP FUNCTION, ASSOCIATION WITH THE RIBOSOME SMALL SUBUNIT, INTERACTION WITH
RP EIF2S1; EIF3C AND IGF2BP1/2, ASSOCIATION WITH THE EIF-3 COMPLEX, AND
RP MUTAGENESIS OF TYR-200; GLN-207; LYS-230; ASP-347 AND 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 [42]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), RNA-BINDING, INTERACTION WITH
RP EIF4G1 AND PABPC1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-38; LEU-43;
RP 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 [43]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-86; SER-90; SER-594
RP AND SER-605, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [44]
RP FUNCTION, INTERACTION WITH IKBKE AND IRF3, PHOSPHORYLATION AT SER-102, AND
RP MUTAGENESIS OF SER-71; 82-SER-SER-83; 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 interferon
RT regulatory factor 3 activation.";
RL Mol. Cell. Biol. 33:2004-2015(2013).
RN [45]
RP FUNCTION, INTERACTION WITH CSNK1E, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLU-348 AND 382-SER--THR-384.
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-beta-
RT catenin signaling.";
RL Science 339:1436-1441(2013).
RN [46]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION BY
RP 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [47]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-592; ARG-617 AND ARG-632, AND
RP 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., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA 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 [48]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY MASS
RP 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 [49]
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 [50]
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., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [51]
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., Ayoub D.,
RA 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 [52]
RP HOMOOLIGOMERIZATION.
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 [53]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH VENEZUELAN EQUINE
RP ENCEPHALITIS VIRUS NON-STRUCTURAL PROTEIN 3 (MICROBIAL INFECTION), AND
RP SUBCELLULAR LOCATION.
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 [54]
RP FUNCTION, INTERACTION WITH RELA, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-230 AND 275-THR--GLU-277.
RX PubMed=27736973; DOI=10.1371/journal.pone.0164471;
RA Xiang N., He M., Ishaq M., Gao Y., Song F., Guo L., Ma L., Sun G., Liu D.,
RA Guo D., Chen Y.;
RT "The DEAD-Box RNA Helicase DDX3 Interacts with NF-kappaB Subunit p65 and
RT Suppresses p65-Mediated Transcription.";
RL PLoS ONE 11:E0164471-E0164471(2016).
RN [55]
RP FUNCTION, INTERACTION WITH IKBKE; IRF3; MAVS; TBKBP1 AND TRAF3, AND
RP MUTAGENESIS OF 142-PRO--GLU-144.
RX PubMed=27980081; DOI=10.1042/bcj20160956;
RA Gu L., Fullam A., McCormack N., Hoehn Y., Schroeder M.;
RT "DDX3 directly regulates TRAF3 ubiquitination and acts as a scaffold to co-
RT ordinate assembly of signalling complexes downstream from MAVS.";
RL Biochem. J. 474:571-587(2017).
RN [56]
RP INTERACTION WITH CAPRIN1; EIF4E AND PABPC1, AND SUBCELLULAR LOCATION.
RX PubMed=28733330; DOI=10.1042/bcj20170354;
RA Copsey A.C., Cooper S., Parker R., Lineham E., Lapworth C., Jallad D.,
RA Sweet S., Morley S.J.;
RT "The helicase, DDX3X, interacts with poly(A)-binding protein 1 (PABP1) and
RT caprin-1 at the leading edge of migrating fibroblasts and is required for
RT efficient cell spreading.";
RL Biochem. J. 474:3109-3120(2017).
RN [57]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY MASS
RP 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-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [58]
RP FUNCTION, INTERACTION WITH TP53 AND GAMMA-TUBULIN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=28842590; DOI=10.1038/s41598-017-09779-w;
RA Chen W.J., Wang W.T., Tsai T.Y., Li H.K., Lee Y.W.;
RT "DDX3 localizes to the centrosome and prevents multipolar mitosis by
RT epigenetically and translationally modulating p53 expression.";
RL Sci. Rep. 7:9411-9411(2017).
RN [59]
RP FUNCTION, SUBCELLULAR LOCATION, AND ASSOCIATION WITH EIF4F COMPLEX.
RX PubMed=29062139; DOI=10.1038/s41598-017-14262-7;
RA Adjibade P., Grenier St-Sauveur V., Bergeman J., Huot M.E., Khandjian E.W.,
RA Mazroui R.;
RT "DDX3 regulates endoplasmic reticulum stress-induced ATF4 expression.";
RL Sci. Rep. 7:13832-13832(2017).
RN [60]
RP FUNCTION, INTERACTION WITH CREBBP; EP300; HNF4A AND NR0B2, AND MUTAGENESIS
RP OF GLU-348 AND 382-SER--THR-384.
RX PubMed=28128295; DOI=10.1038/srep41452;
RA Tsai T.Y., Wang W.T., Li H.K., Chen W.J., Tsai Y.H., Chao C.H.,
RA Wu Lee Y.H.;
RT "RNA helicase DDX3 maintains lipid homeostasis through upregulation of the
RT microsomal triglyceride transfer protein by interacting with HNF4 and
RT SHP.";
RL Sci. Rep. 7:41452-41452(2017).
RN [61]
RP FUNCTION, INTERACTION WITH MAP3K14 AND CHUK, AND SUBCELLULAR LOCATION.
RX PubMed=30341167; DOI=10.1042/bcj20180163;
RA Fullam A., Gu L., Hoehn Y., Schroeder M.;
RT "DDX3 directly facilitates IKKalpha activation and regulates downstream
RT signalling pathways.";
RL Biochem. J. 475:3595-3607(2018).
RN [62]
RP INTERACTION WITH XPO1, SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL, AND
RP MUTAGENESIS OF 19-LEU--LEU-21.
RX PubMed=30131165; DOI=10.1016/j.ejcb.2018.08.001;
RA Brennan R., Haap-Hoff A., Gu L., Gautier V., Long A., Schroeder M.;
RT "Investigating nucleo-cytoplasmic shuttling of the human DEAD-box helicase
RT DDX3.";
RL Eur. J. Cell Biol. 97:501-511(2018).
RN [63]
RP FUNCTION, INTERACTION WITH CSNK1E AND CSNK1D, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION AT SER-429; THR-469; SER-470 AND SER-543, AND
RP CHARACTERIZATION OF VARIANTS MEDULLOBLASTOMA CYS-376 AND HIS-528.
RX PubMed=29222110; DOI=10.1242/jcs.207316;
RA Dolde C., Bischof J., Grueter S., Montada A., Halekotte J., Peifer C.,
RA Kalbacher H., Baumann U., Knippschild U., Suter B.;
RT "A CK1 FRET biosensor reveals that DDX3X is an essential activator of
RT CK1epsilon.";
RL J. Cell Sci. 131:0-0(2018).
RN [64]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH TRPV4, AND SUBCELLULAR
RP LOCATION.
RX PubMed=29899501; DOI=10.1038/s41467-018-04776-7;
RA Donate-Macian P., Jungfleisch J., Perez-Vilaro G., Rubio-Moscardo F.,
RA Peralvarez-Marin A., Diez J., Valverde M.A.;
RT "The TRPV4 channel links calcium influx to DDX3X activity and viral
RT infectivity.";
RL Nat. Commun. 9:2307-2307(2018).
RN [65]
RP FUNCTION.
RX PubMed=30256975; DOI=10.1093/nar/gky861;
RA Herdy B., Mayer C., Varshney D., Marsico G., Murat P., Taylor C.,
RA D'Santos C., Tannahill D., Balasubramanian S.;
RT "Analysis of NRAS RNA G-quadruplex binding proteins reveals DDX3X as a
RT novel interactor of cellular G-quadruplex containing transcripts.";
RL Nucleic Acids Res. 46:11592-11604(2018).
RN [66]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH XPO1, SUBCELLULAR LOCATION,
RP NUCLEAR EXPORT SIGNAL, DOMAIN, AND MUTAGENESIS OF 12-LEU--LEU-21.
RX PubMed=31575075; DOI=10.3390/cells8101181;
RA Heaton S.M., Atkinson S.C., Sweeney M.N., Yang S.N.Y., Jans D.A.,
RA Borg N.A.;
RT "Exportin-1-Dependent Nuclear Export of DEAD-box Helicase DDX3X is Central
RT to its Role in Antiviral Immunity.";
RL Cells 8:0-0(2019).
RN [67]
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 [68]
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 [69]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 71-90 IN COMPLEX WITH VACV PROTEIN
RP K7 (MICROBIAL INFECTION), FUNCTION, 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 [70] {ECO:0007744|PDB:6O5F}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 132-607 IN COMPLEX WITH DSRNA,
RP HOMODIMERIZATION, AND CATALYTIC ACTIVITY.
RX PubMed=31300642; DOI=10.1038/s41467-019-11083-2;
RA Song H., Ji X.;
RT "The mechanism of RNA duplex recognition and unwinding by DEAD-box helicase
RT DDX3X.";
RL Nat. Commun. 10:3085-3085(2019).
RN [71]
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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [72]
RP VARIANTS MRXSSB THR-214; ALA-233 DEL; VAL-233; PRO-235; PHE-300; HIS-326;
RP GLN-351; CYS-362; CYS-376; PRO-392; PRO-417; GLY-475; SER-480; HIS-488;
RP THR-507; ILE-509; THR-514; HIS-534; LEU-560 DEL AND LEU-568,
RP CHARACTERIZATION OF VARIANTS MRXSSB THR-214; HIS-326; CYS-376; THR-507 AND
RP HIS-534, AND INVOLVEMENT IN MRXSSB.
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., Romano C.,
RA Van Esch H., Stumpel C., Vreeburg M., Smeets E., Oberndorff K.,
RA van Bon B.W., Shaw M., Gecz J., Haan E., Bienek M., Jensen C., Loeys B.L.,
RA Van Dijck A., Innes A.M., Racher H., Vermeer S., Di Donato N., Rump A.,
RA Tatton-Brown K., Parker M.J., Henderson A., Lynch S.A., Fryer A., Ross A.,
RA Vasudevan P., Kini U., Newbury-Ecob R., Chandler K., Male A., Dijkstra S.,
RA Schieving J., 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., Strauss K.A.,
RA Brigatti K.W., Keating K., Burton B.K., Kim K.H., Charrow J., Norman J.,
RA Foster-Barber A., Kline A.D., Kimball A., Zackai E., Harr M., Fox J.,
RA McLaughlin J., Lindstrom K., Haude K.M., van Roozendaal K., Brunner H.,
RA Chung W.K., Kooy R.F., Pfundt R., Kalscheuer V., Mehta S.G., Katsanis N.,
RA 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 (PubMed:17357160,
CC PubMed:21589879, PubMed:31575075). The ATPase activity can be
CC stimulated by various ribo-and deoxynucleic acids indicative for a
CC relaxed substrate specificity (PubMed:29222110). In vitro can unwind
CC partially double-stranded DNA with a preference for 5'-single-stranded
CC DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-
CC quadruplex (rG4s) structures, including those located in the 5'-UTR of
CC NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which
CC do not necessarily require its ATPase/helicase catalytic activities
CC (Probable). Involved in transcription regulation (PubMed:16818630,
CC PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription
CC in an SP1-dependent manner, hence inhibits cell growth. This function
CC requires its ATPase, but not helicase activity (PubMed:16818630,
CC PubMed:18264132). CDKN1A up-regulation may be cell-type specific
CC (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its
CC transcription (PubMed:18264132). Potentiates HNF4A-mediated MTTP
CC transcriptional activation; this function requires ATPase, but not
CC helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by
CC CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to
CC its response element. In addition, disrupts the interaction between
CC HNF4 and SHP that forms inactive heterodimers and enhances the
CC formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP
CC expression, may play a role in lipid homeostasis (PubMed:28128295). May
CC positively regulate TP53 transcription (PubMed:28842590). Associates
CC with mRNPs, predominantly with spliced mRNAs carrying an exon junction
CC complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the
CC regulation of translation initiation (PubMed:18628297, PubMed:17667941,
CC PubMed:22872150). Not involved in the general process of translation,
CC but promotes efficient translation of selected complex mRNAs,
CC containing highly structured 5'-untranslated regions (UTR)
CC (PubMed:20837705, PubMed:22872150). This function depends on helicase
CC activity (PubMed:20837705, PubMed:22872150). Might facilitate
CC translation by resolving secondary structures of 5'-UTRs during
CC ribosome scanning (PubMed:20837705). Alternatively, may act prior to
CC 43S ribosomal scanning and promote 43S pre-initiation complex entry to
CC mRNAs exhibiting specific RNA motifs, by performing local remodeling of
CC transcript structures located close to the cap moiety
CC (PubMed:22872150). Independently of its ATPase activity, promotes the
CC assembly of functional 80S ribosomes and disassembles from ribosomes
CC prior to the translation elongation process (PubMed:22323517).
CC Positively regulates the translation of cyclin E1/CCNE1 mRNA and
CC consequently promotes G1/S-phase transition during the cell cycle
CC (PubMed:20837705). May activate TP53 translation (PubMed:28842590).
CC Required for endoplasmic reticulum stress-induced ATF4 mRNA translation
CC (PubMed:29062139). Independently of its ATPase/helicase activity,
CC enhances IRES-mediated translation; this activity requires interaction
CC with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its
CC ATPase/helicase activity, has also been shown specifically repress cap-
CC dependent translation, possibly by acting on translation initiation
CC factor EIF4E (PubMed:17667941). Involved in innate immunity, acting as
CC a viral RNA sensor. Binds viral RNAs and promotes the production of
CC type I interferon (IFN-alpha and IFN-beta) (PubMed:31575075,
CC PubMed:20127681, PubMed:21170385). Potentiate MAVS/DDX58-mediated
CC induction of IFNB in early stages of infection (PubMed:20127681,
CC PubMed:21170385). Enhances IFNB1 expression via IRF3/IRF7 pathway and
CC participates in NFKB activation in the presence of MAVS and TBK1
CC (PubMed:18583960, PubMed:18636090, PubMed:21170385, PubMed:27980081,
CC PubMed:19913487). Involved in TBK1 and IKBKE-dependent IRF3 activation
CC leading to IFNB induction, acts as a scaffolding adapter that links
CC IKBKE and IRF3 and coordinates their activation (PubMed:23478265).
CC Involved in the TLR7/TLR8 signaling pathway leading to type I
CC interferon induction, including IFNA4 production. In this context, acts
CC as an upstream regulator of IRF7 activation by MAP3K14/NIK and
CC CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following
CC physiological activation of the TLR7 and TLR8 pathways, leading to
CC MAP3K14/CHUK-mediated activatory phosphorylation of IRF7
CC (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B
CC signaling (PubMed:30341167). Negatively regulates TNF-induced IL6 and
CC IL8 expression, via the NF-kappa-B pathway. May act by interacting with
CC RELA/p65 and trapping it in the cytoplasm (PubMed:27736973). May also
CC bind IFNB promoter; the function is independent of IRF3
CC (PubMed:18583960). Involved in both stress and inflammatory responses
CC (By similarity). Independently of its ATPase/helicase activity,
CC required for efficient stress granule assembly through its interaction
CC with EIF4E, hence promotes survival in stressed cells
CC (PubMed:21883093). Independently of its helicase activity, regulates
CC NLRP3 inflammasome assembly through interaction with NLRP3 and hence
CC promotes cell death by pyroptosis during inflammation. This function is
CC independent of helicase activity (By similarity). Therefore DDX3X
CC availability may be used to interpret stress signals and choose between
CC pro-survival stress granules and pyroptotic NLRP3 inflammasomes and
CC serve as a live-or-die checkpoint in stressed cells (By similarity). In
CC association with GSK3A/B, negatively regulates extrinsic apoptotic
CC signaling pathway via death domain receptors, including TNFRSF10B,
CC slowing down the rate of CASP3 activation following death receptor
CC stimulation (PubMed:18846110). Cleavage by caspases may inactivate
CC DDX3X and relieve the inhibition (PubMed:18846110). Independently of
CC its ATPase/helicase activity, allosteric activator of CSNK1E.
CC Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in
CC the positive regulation of Wnt/beta-catenin signaling pathway. Also
CC activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these
CC targets are physiologically relevant (PubMed:23413191,
CC PubMed:29222110). ATPase and casein kinase-activating functions are
CC mutually exclusive (PubMed:29222110). May be involved in mitotic
CC chromosome segregation (PubMed:21730191).
CC {ECO:0000250|UniProtKB:Q62167, ECO:0000269|PubMed:16818630,
CC ECO:0000269|PubMed:17095540, 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:19913487,
CC ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:20837705,
CC ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:21589879,
CC ECO:0000269|PubMed:21730191, ECO:0000269|PubMed:21883093,
CC ECO:0000269|PubMed:22323517, ECO:0000269|PubMed:22872150,
CC ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:23478265,
CC ECO:0000269|PubMed:27736973, ECO:0000269|PubMed:27980081,
CC ECO:0000269|PubMed:28128295, ECO:0000269|PubMed:28842590,
CC ECO:0000269|PubMed:29062139, ECO:0000269|PubMed:29222110,
CC ECO:0000269|PubMed:30256975, ECO:0000269|PubMed:30341167,
CC ECO:0000269|PubMed:31575075, ECO:0000305}.
CC -!- FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV)
CC replication (PubMed:29899501). During infection, HCV core protein
CC inhibits the interaction between MAVS and DDX3X and therefore impairs
CC MAVS-dependent INFB induction and might recruit DDX3X to HCV
CC replication complex (PubMed:21170385). {ECO:0000269|PubMed:21170385,
CC ECO:0000269|PubMed:29899501}.
CC -!- FUNCTION: (Microbial infection) Facilitates HIV-1 replication
CC (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150,
CC PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export
CC of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501).
CC This function is strongly stimulated in the presence of TBK1 and
CC requires DDX3X ATPase activity (PubMed:18583960).
CC {ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:18583960,
CC ECO:0000269|PubMed:21589879, ECO:0000269|PubMed:22872150,
CC ECO:0000269|PubMed:29899501}.
CC -!- FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV)
CC replication. {ECO:0000269|PubMed:29899501}.
CC -!- FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV)
CC replication. {ECO:0000269|PubMed:29899501}.
CC -!- FUNCTION: (Microbial infection) Facilitates Venezuelan equine
CC encephalitis virus (VEEV) replication. {ECO:0000269|PubMed:27105836}.
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 Evidence={ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:17357160,
CC ECO:0000269|PubMed:21589879, ECO:0000269|PubMed:31300642,
CC ECO:0000269|PubMed:31575075};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.04 mM for ATP (in the absence of nucleic acid)
CC {ECO:0000269|PubMed:17357160};
CC KM=0.03 mM for ATP (in the presence of ssDNA oligonucleoside dA200)
CC {ECO:0000269|PubMed:17357160};
CC KM=0.062 mM for ATP (in the absence of nucleic acid)
CC {ECO:0000269|PubMed:21589879};
CC KM=0.045 mM for ATP (in the presence of RNA oligo(rU)20)
CC {ECO:0000269|PubMed:21589879};
CC KM=0.047 mM for ATP (in the presence of DNA oligo(dT)20)
CC {ECO:0000269|PubMed:21589879};
CC Note=kcat is 14 min(-1) for ATP hydrolysis in the absence of nucleic
CC acid (PubMed:17357160). kcat is 36 min(-1) for ATP hydrolysis in the
CC presence of ssDNA oligonucleoside dA200 (PubMed:17357160). kcat is
CC 1.6 min(-1) for ATP hydrolysis in the absence of nucleic acid
CC (PubMed:21589879). kcat is 3.2 min(-1) for ATP hydrolysis in the
CC presence of RNA oligo(rU)20 (PubMed:21589879). kcat is 3.8 min(-1)
CC for ATP hydrolysis in the presence of DNA oligo(dT)20
CC (PubMed:21589879). {ECO:0000269|PubMed:17357160,
CC ECO:0000269|PubMed:21589879};
CC -!- SUBUNIT: Homodimer; can bind RNA as a monomer and as a dimer/oligomer
CC (PubMed:27546789, PubMed:31300642). Interacts with TDRD3
CC (PubMed:18632687). Interacts (when phosphorylated at Ser-102) with
CC IRF3; the interaction facilitates the phosphorylation and activation of
CC IRF3 by IKBKE (PubMed:23478265, PubMed:27980081). Directly interacts
CC with XPO1/CRM1 (PubMed:15507209, PubMed:30131165, PubMed:31575075). The
CC interaction with XPO1/CMR1 is dependent on the DDX3X nuclear export
CC signal motif and XPO1 interaction with GTPase RAN in its active GTP-
CC bound form (PubMed:31575075, PubMed:30131165). Weakly interacts with
CC TBKBP1/SINTBAD (PubMed:27980081). Directly interacts with TRAF3; this
CC interaction stimulates TRAF3 'Lys-63' ubiquitination (PubMed:27980081).
CC Interacts with CSNK1E in a Wnt-dependent manner; this interaction
CC greatly enhances CSNK1E affinity for ATP, stimulates its kinase
CC activity and promotes CSNK1E-mediated DVL2 phosphorylation
CC (PubMed:23413191, PubMed:29222110). In the presence of RNA, the
CC interaction is decreased (PubMed:29222110). Also interacts with CSNK1D
CC and stimulates its kinase activity (PubMed:23413191, PubMed:29222110).
CC Interacts with TRPV4; this interaction is decreased when the TRPV4
CC channel is activated, leading to DDX3X relocalization to the nucleus
CC (PubMed:29899501). Interacts with MAP3K14/NIK (PubMed:30341167).
CC Directly interacts with CHUK/IKKA after physiological activation of the
CC TLR7 and TLR8 pathways; this interaction enhances CHUK
CC autophosphorylation (PubMed:30341167). May associate with EIF4F
CC complex, composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3
CC (Probable). Directly interacts with EIF4E in an RNA-independent manner;
CC this interaction enhances EIF4E cap-binding ability (PubMed:17667941,
CC PubMed:21883093, PubMed:28733330). Directly interacts with EIF4G1 in an
CC RNA-independent manner (PubMed:22872150). DDX3X competes with EIF4G1
CC for interaction with EIF4E (PubMed:17667941, PubMed:21883093).
CC Interacts with EIF4A1 and EIF2S1 in an RNA-independent manner
CC (PubMed:18596238, PubMed:22323517). Associates with the eukaryotic
CC translation initiation factor 3 (eIF-3) complex, including with EIF3B
CC and EIF3C subunits (PubMed:18628297, PubMed:22323517). Directly
CC interacts with IKBKE/IKKE; this interaction stimulates IKBKE activating
CC autophosphorylation and is induced upon viral infection
CC (PubMed:18636090, PubMed:20657822, PubMed:23478265, PubMed:27980081).
CC Interacts with TBK1 (PubMed:20375222). Interacts with SP1; this
CC interaction potentiates SP1-induced CDKN1A/WAF1/CIP1 transcription
CC (PubMed:16818630). Interacts with GSK3A and GSK3B (PubMed:18846110).
CC Interacts with several death receptors, inclusing FAS, TNFRSF10A and
CC TNFRSF10B (PubMed:18846110). Recruited to TNFRSF10B in the absence of
CC receptor stimulation. When TNFRSF10B is stimulated, further recruited
CC to the receptor and cleaved by caspases. A large proteolytic fragment
CC remains associated with TNFRSF10B (PubMed:18846110). Interacts (via C-
CC terminus) with NXF1/TAP; this interaction may be partly involved in
CC DDX3X nuclear export and in NXF1 localization to stress granules
CC (PubMed:18596238). Identified in an mRNP complex, composed of at least
CC DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1/2, ILF3, PABPC1, PCBP2, PTBP2,
CC STAU1, STAU2, SYNCRIP and YBX1 (PubMed:19029303). The interaction with
CC IGF2BP1/2 is RNA-dependent (PubMed:22323517). Directly interacts with
CC PABPC1/PABP1 in an RNA-independent manner (PubMed:18596238,
CC PubMed:21883093, PubMed:22872150, PubMed:28733330). This interaction
CC increases in stressed cells and decreases during cell recovery
CC (PubMed:21883093). Interacts (via C-terminus) with MAVS/IPS-1; this
CC interaction occurs rapidly, but transiently after Sendai virus
CC infection (PubMed:20127681, PubMed:21170385, PubMed:27980081). The
CC interaction potentiates MAVS-mediated IFNB induction (PubMed:20127681,
CC PubMed:21170385). Interacts with ERCC6/CBS (PubMed:26030138). Interacts
CC with DHX33 in an RNA-independent manner (PubMed:26100019). Interacts
CC with DDX5 in the cytoplasm; this interaction may be more efficient when
CC both proteins are unphosphorylated (PubMed:22034099). Interacts with
CC DDX58/RIG-1 (PubMed:20127681). Interacts with IFIH1/MDA5
CC (PubMed:20127681). Interacts with NCAPH; this interaction may be
CC important for the NCAPH localization at condensing chromosomes during
CC mitosis (PubMed:21730191). Interacts with NLRP3 (via NACHT domain)
CC under inflammasome-activating conditions (By similarity). Interacts
CC with CAPRIN1 (PubMed:28733330). Interacts with HNF4A and NR0B2/SHP in
CC an RNA-independent manner; this interaction disrupts the interaction
CC between HNF4 and NR0B2 that forms inactive heterodimers and enhances
CC the formation of active HNF4 homodimers (PubMed:28128295). Interacts
CC with CREBBP/CBP (PubMed:28128295). Interacts with EP300/p300
CC (PubMed:28128295). Interacts with gamma-tubulin (PubMed:28842590).
CC Interacts with phosphorylated TP53 (PubMed:28842590). Directly
CC interacts with RELA/p65; this interaction may trap RELA in the
CC cytoplasm, impairing nuclear relocalization upon TNF activating signals
CC (PubMed:27736973). {ECO:0000250|UniProtKB:Q62167,
CC ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:16818630,
CC ECO:0000269|PubMed:17667941, ECO:0000269|PubMed:18596238,
CC ECO:0000269|PubMed:18628297, 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, ECO:0000269|PubMed:27736973,
CC ECO:0000269|PubMed:27980081, ECO:0000269|PubMed:28128295,
CC ECO:0000269|PubMed:28733330, ECO:0000269|PubMed:28842590,
CC ECO:0000269|PubMed:29222110, ECO:0000269|PubMed:29899501,
CC ECO:0000269|PubMed:30131165, ECO:0000269|PubMed:30341167,
CC ECO:0000269|PubMed:31300642, ECO:0000269|PubMed:31575075,
CC ECO:0000305|PubMed:17667941, ECO:0000305|PubMed:21883093,
CC ECO:0000305|PubMed:22872150, ECO:0000305|PubMed:28733330,
CC ECO:0000305|PubMed:29062139}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis B virus (HBV)
CC polymerase in the cytoplasm; this interaction may inhibit DDX3X
CC interaction with the IKBKE/TBK1 complex, and hence impair IKBKE/TBK1-
CC mediated increase in IFNB production. {ECO:0000269|PubMed:20375222,
CC ECO:0000269|PubMed:20657822}.
CC -!- SUBUNIT: (Microbial infection) Directly interacts with hepatitis C
CC virus (HCV) core protein in the cytoplasm.
CC {ECO:0000269|PubMed:10329544}.
CC -!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus (VACV)
CC protein K7. {ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:19913487}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 protein 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 O00571; Q8TF63: DCANP1; NbExp=3; IntAct=EBI-353779, EBI-10275670;
CC O00571; O95786: DDX58; NbExp=2; IntAct=EBI-353779, EBI-995350;
CC O00571; P05198: EIF2S1; NbExp=3; IntAct=EBI-353779, EBI-1056162;
CC O00571; P55884: EIF3B; NbExp=5; IntAct=EBI-353779, EBI-366696;
CC O00571; Q99613: EIF3C; NbExp=3; IntAct=EBI-353779, EBI-353741;
CC O00571; Q04637: EIF4G1; NbExp=3; IntAct=EBI-353779, EBI-73711;
CC O00571; Q14164: IKBKE; NbExp=4; IntAct=EBI-353779, EBI-307369;
CC O00571; Q7Z434: MAVS; NbExp=4; IntAct=EBI-353779, EBI-995373;
CC O00571; Q6P582: MZT2A; NbExp=3; IntAct=EBI-353779, EBI-2558548;
CC O00571; Q15003: NCAPH; NbExp=2; IntAct=EBI-353779, EBI-1046410;
CC O00571; Q9UBU9: NXF1; NbExp=5; IntAct=EBI-353779, EBI-398874;
CC O00571; P11940: PABPC1; NbExp=10; IntAct=EBI-353779, EBI-81531;
CC O00571; Q13148: TARDBP; NbExp=6; IntAct=EBI-353779, EBI-372899;
CC O00571; Q03403: TFF2; NbExp=3; IntAct=EBI-353779, EBI-4314702;
CC O00571; P68467: K7R; Xeno; NbExp=6; IntAct=EBI-353779, EBI-8022707;
CC O00571; P14240: L; Xeno; NbExp=2; IntAct=EBI-353779, EBI-26968662;
CC O00571; P03427: PB2; Xeno; NbExp=3; IntAct=EBI-353779, EBI-8430745;
CC O00571; P04608: tat; Xeno; NbExp=4; IntAct=EBI-353779, EBI-6164389;
CC O00571; Q923J1: Trpm7; Xeno; NbExp=2; IntAct=EBI-353779, EBI-8010314;
CC O00571; P68466: VACWR039; Xeno; NbExp=6; IntAct=EBI-353779, EBI-6152154;
CC O00571; PRO_0000037517 [P26664]; Xeno; NbExp=3; IntAct=EBI-353779, EBI-9209740;
CC O00571; PRO_0000037566 [P27958]; Xeno; NbExp=11; IntAct=EBI-353779, EBI-6377335;
CC O00571; PRO_0000037559 [Q5EG65]; Xeno; NbExp=4; IntAct=EBI-353779, EBI-9254385;
CC O00571; Q99IB8; Xeno; NbExp=9; IntAct=EBI-353779, EBI-6674379;
CC O00571; PRO_0000037541 [Q9WMX2]; Xeno; NbExp=4; IntAct=EBI-353779, EBI-6863754;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23413191,
CC ECO:0000269|PubMed:29899501}. Nucleus {ECO:0000269|PubMed:10329544,
CC ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:16818630,
CC ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18636090,
CC ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:29899501,
CC ECO:0000269|PubMed:30131165, ECO:0000269|PubMed:31575075}. Cytoplasm
CC {ECO:0000269|PubMed:10329544, ECO:0000269|PubMed:15507209,
CC ECO:0000269|PubMed:16818630, ECO:0000269|PubMed:18596238,
CC ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:20127681,
CC ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:21730191,
CC ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22034099,
CC ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:27105836,
CC ECO:0000269|PubMed:27736973, ECO:0000269|PubMed:28733330,
CC ECO:0000269|PubMed:29062139, ECO:0000269|PubMed:29222110,
CC ECO:0000269|PubMed:30131165, ECO:0000269|PubMed:30341167,
CC ECO:0000269|PubMed:31575075}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18632687,
CC ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:29062139}. Inflammasome
CC {ECO:0000250|UniProtKB:Q62167}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:28733330}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:28842590}.
CC Note=Shuttles between the nucleus and the cytosol (PubMed:15507209,
CC PubMed:18636090, PubMed:29899501, PubMed:31575075, PubMed:30131165).
CC Exported from the nucleus partly through the XPO1/CRM1 system and
CC partly through NXF1/TAP (PubMed:15507209, PubMed:18636090,
CC PubMed:18596238, PubMed:31575075, PubMed:30131165). Localizes to
CC nuclear pores on the outer side of the nuclear membrane
CC (PubMed:15507209). In the cytosol, partly colocalizes with mitochondria
CC (PubMed:20127681). At G0, predominantly located in nucleus. In G1/S
CC phase, predominantly cytoplasmic (PubMed:22034099). During
CC prophase/prometaphase, localizes in close proximity to the condensing
CC chromosomes (PubMed:30131165, PubMed:21730191). During telophase,
CC localizes around the newly synthesized nuclear membrane and in the
CC cytoplasm (PubMed:22034099). Colocalizes with TRPV4 at the plasma
CC membrane. When TRPV4 channel is activated, intracellular Ca(2+) levels
CC increase and the calmodulin/CAMKII pathway is activated, relocalizes to
CC the nucleus (PubMed:29899501). WNT3A stimulation promotes DDX3
CC recruitment to the plasma membrane (PubMed:23413191). At the leading
CC edge of migrating fibroblasts, colocalizes with CAPRIN1 and PABPC1
CC (PubMed:28733330). Localizes to centrosome throughout the cell cycle
CC and associates with TP53 at centrosome during mitosis
CC (PubMed:28842590). Translocates to the nucleus in response to HPIV-3
CC virus-mediated infection (PubMed:31575075).
CC {ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:18596238,
CC ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:20127681,
CC ECO:0000269|PubMed:21730191, ECO:0000269|PubMed:22034099,
CC ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:28733330,
CC ECO:0000269|PubMed:28842590, ECO:0000269|PubMed:29899501,
CC ECO:0000269|PubMed:30131165, ECO:0000269|PubMed:31575075}.
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 -!- TISSUE SPECIFICITY: Widely expressed (PubMed:15294876). In testis,
CC expressed in spermatids (PubMed:15294876). Expressed in epidermis and
CC liver (at protein level) (PubMed:16818630, PubMed:16301996).
CC {ECO:0000269|PubMed:15294876, ECO:0000269|PubMed:16301996,
CC ECO:0000269|PubMed:16818630}.
CC -!- DOMAIN: The C-terminus (residues 536-662) is dispensable for DDX3X
CC trafficking. {ECO:0000269|PubMed:31575075}.
CC -!- PTM: Phosphorylated by TBK1; the phosphorylation is required for the
CC synergistic induction of IFNB mediated by TBK1 and DDX3X
CC (PubMed:18583960). Phosphorylated by IKBKE at Ser-102 after ssRNA viral
CC infection; enhances the induction of INFB promoter by IRF3
CC (PubMed:18583960, PubMed:23478265). The cytoplasmic form is highly
CC phosphorylated in the G1/S phase of the cell cycle and much less at
CC G2/M (PubMed:22034099). Phosphorylation by CSNK1E may inhibit RNA-
CC stimulated ATPase activity (PubMed:29222110).
CC {ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:22034099,
CC ECO:0000269|PubMed:23478265, ECO:0000269|PubMed:29222110}.
CC -!- PTM: Upon stimulation of death receptors, including TNFRSF10B,
CC recruited to receptors and cleaved by caspases. Proteolytic fragments
CC remain associated with the receptors. This cleavage presumably
CC inactivates DDX3X anti-apoptotic function.
CC {ECO:0000269|PubMed:18846110}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic,
CC Snijders Blok type (MRXSSB) [MIM:300958]: A disorder characterized by
CC mild to severe intellectual disability, hypotonia, movement disorders,
CC behavior problems, corpus callosum hypoplasia, and epilepsy.
CC Additionally, patients manifest variable non-neurologic features such
CC as joint hyperlaxity, skin pigmentary abnormalities, cleft lip and/or
CC palate, hearing and visual impairment, and precocious puberty.
CC {ECO:0000269|PubMed:26235985}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Encoded by an chromosome X-linked gene which may escape
CC X chromosome inactivation in females. DDX3Y, its homolog on chromosome
CC Y, is located on the Y non-recombinant portion.
CC {ECO:0000269|PubMed:9381176}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: The role of the nuclear export signal (NES) motif in XPO1-
CC mediated DDX3X export is controversial (PubMed:30131165,
CC PubMed:31575075, PubMed:15507209). In one study, NES has been found
CC dispensable for DDX3X export while the helicase domain mediates the
CC interaction with XPO1 (PubMed:15507209). However, in two other studies,
CC DDX3X nuclear export is dependent on both NES and Ran in its GTP-bound
CC form while the helicase domain is not required (PubMed:30131165,
CC PubMed:31575075). {ECO:0000269|PubMed:15507209,
CC ECO:0000269|PubMed:30131165, ECO:0000269|PubMed:31575075}.
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DR EMBL; U50553; AAB95637.1; -; mRNA.
DR EMBL; AF061337; AAC34298.1; -; mRNA.
DR EMBL; AF000982; AAC51829.1; -; mRNA.
DR EMBL; AF000983; AAC51830.1; -; 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 AlphaFoldDB; O00571; -.
DR SMR; O00571; -.
DR BioGRID; 108020; 526.
DR CORUM; O00571; -.
DR DIP; DIP-27551N; -.
DR ELM; O00571; -.
DR IntAct; O00571; 153.
DR MINT; O00571; -.
DR STRING; 9606.ENSP00000382840; -.
DR BindingDB; O00571; -.
DR ChEMBL; CHEMBL5553; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR CarbonylDB; O00571; -.
DR GlyGen; O00571; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O00571; -.
DR MetOSite; 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 Antibodypedia; 463; 712 antibodies from 41 providers.
DR DNASU; 1654; -.
DR Ensembl; ENST00000457138.7; ENSP00000392494.2; ENSG00000215301.11. [O00571-2]
DR Ensembl; ENST00000478993.5; ENSP00000478443.1; ENSG00000215301.11. [O00571-1]
DR Ensembl; ENST00000629496.3; ENSP00000487224.1; ENSG00000215301.11. [O00571-1]
DR Ensembl; ENST00000629785.2; ENSP00000486516.1; ENSG00000215301.11. [O00571-1]
DR Ensembl; ENST00000630255.2; ENSP00000486720.1; ENSG00000215301.11. [O00571-1]
DR Ensembl; ENST00000644876.2; ENSP00000494040.1; ENSG00000215301.11. [O00571-1]
DR GeneID; 1654; -.
DR KEGG; hsa:1654; -.
DR MANE-Select; ENST00000644876.2; ENSP00000494040.1; NM_001356.5; NP_001347.3.
DR UCSC; uc004dfe.4; human. [O00571-1]
DR CTD; 1654; -.
DR DisGeNET; 1654; -.
DR GeneCards; DDX3X; -.
DR GeneReviews; DDX3X; -.
DR HGNC; HGNC:2745; DDX3X.
DR HPA; ENSG00000215301; Low tissue specificity.
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 VEuPathDB; HostDB:ENSG00000215301; -.
DR eggNOG; KOG0335; Eukaryota.
DR GeneTree; ENSGT00940000154443; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; O00571; -.
DR OrthoDB; 595675at2759; -.
DR PhylomeDB; O00571; -.
DR TreeFam; TF300364; -.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; O00571; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; O00571; -.
DR SIGNOR; O00571; -.
DR BioGRID-ORCS; 1654; 195 hits in 716 CRISPR screens.
DR ChiTaRS; DDX3X; human.
DR EvolutionaryTrace; O00571; -.
DR GeneWiki; DDX3X; -.
DR GenomeRNAi; 1654; -.
DR Pharos; O00571; Tchem.
DR PRO; PR:O00571; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O00571; protein.
DR Bgee; ENSG00000215301; Expressed in choroid plexus epithelium and 206 other tissues.
DR ExpressionAtlas; O00571; baseline and differential.
DR Genevisible; O00571; HS.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
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:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0072559; C:NLRP3 inflammasome complex; ISS:UniProtKB.
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:0005886; C:plasma membrane; IDA:UniProtKB.
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:ATP hydrolysis 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:0043015; F:gamma-tubulin 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:0003729; F:mRNA 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:0098586; P:cellular response to virus; 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:0055088; P:lipid homeostasis; 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:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IMP:UniProtKB.
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:0032727; P:positive regulation of interferon-alpha production; IDA:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB.
DR GO; GO:1901985; P:positive regulation of protein acetylation; IMP:UniProtKB.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0034157; P:positive regulation of toll-like receptor 7 signaling pathway; IDA:UniProtKB.
DR GO; GO:0034161; P:positive regulation of toll-like receptor 8 signaling pathway; 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:0036493; P:positive regulation of translation in response to endoplasmic reticulum stress; IMP: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:0031053; P:primary miRNA processing; IEA:Ensembl.
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:0016055; P:Wnt signaling pathway; IMP:UniProtKB.
DR DisProt; DP02192; -.
DR Gene3D; 3.40.50.300; -; 2.
DR IDEAL; IID00232; -.
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; ATP-binding;
KW Cell membrane; Cell projection; Chromosome partition; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Disease variant; DNA-binding;
KW Helicase; Host-virus interaction; Hydrolase; Immunity; Inflammasome;
KW Innate immunity; Intellectual disability; Isopeptide bond; Membrane;
KW Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; RNA-binding; Transcription;
KW Transcription regulation; Translation regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10859333,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895"
FT CHAIN 2..662
FT /note="ATP-dependent RNA helicase DDX3X"
FT /id="PRO_0000055009"
FT DOMAIN 211..403
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 414..575
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 2..139
FT /note="Required for TBK1 and IKBKE-dependent IFNB1
FT activation"
FT /evidence="ECO:0000269|PubMed:18636090"
FT REGION 19..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..44
FT /note="Interaction with EIF4E"
FT /evidence="ECO:0000269|PubMed:17667941"
FT REGION 81..90
FT /note="Interaction with VACV protein K7"
FT /evidence="ECO:0000269|PubMed:19913487"
FT REGION 88..123
FT /note="Involved in binding to RNA G-quadruplex"
FT /evidence="ECO:0000269|PubMed:30256975"
FT REGION 100..662
FT /note="Interaction with GSK3B"
FT /evidence="ECO:0000269|PubMed:18846110"
FT REGION 100..110
FT /note="Interaction with IKBKE"
FT REGION 139..172
FT /note="Interaction with CHUK"
FT /evidence="ECO:0000269|PubMed:17667941"
FT REGION 250..259
FT /note="Involved in stimulation of ATPase activity by DNA
FT and RNA, nucleic acid binding and unwinding and HIV-1
FT replication"
FT REGION 409..662
FT /note="Interaction with HCV core protein"
FT /evidence="ECO:0000269|PubMed:10329544"
FT REGION 536..661
FT /note="Interaction with NXF1"
FT /evidence="ECO:0000269|PubMed:18596238"
FT REGION 601..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 12..21
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:30131165,
FT ECO:0000269|PubMed:31575075"
FT MOTIF 180..208
FT /note="Q motif"
FT MOTIF 347..350
FT /note="DEAD box"
FT COMPBIAS 19..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 200..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 224..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10859333,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 101
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 102
FT /note="Phosphoserine; by IKKE"
FT /evidence="ECO:0000269|PubMed:23478265"
FT MOD_RES 104
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 110
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 181
FT /note="Phosphoserine; by TBK1; in vitro"
FT /evidence="ECO:0000269|PubMed:18583960"
FT MOD_RES 183
FT /note="Phosphoserine; by TBK1"
FT /evidence="ECO:0000269|PubMed:18583960,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 240
FT /note="Phosphoserine; by TBK1; in vitro"
FT /evidence="ECO:0000269|PubMed:18583960"
FT MOD_RES 269
FT /note="Phosphoserine; by TBK1; in vitro"
FT /evidence="ECO:0000269|PubMed:18583960"
FT MOD_RES 429
FT /note="Phosphoserine; by CSNK1E and TBK1; in vitro"
FT /evidence="ECO:0000269|PubMed:18583960,
FT ECO:0000269|PubMed:29222110"
FT MOD_RES 438
FT /note="Phosphothreonine; by TBK1; in vitro"
FT /evidence="ECO:0000269|PubMed:18583960"
FT MOD_RES 442
FT /note="Phosphoserine; by TBK1; in vitro"
FT /evidence="ECO:0000269|PubMed:18583960"
FT MOD_RES 456
FT /note="Phosphoserine; by TBK1; in vitro"
FT /evidence="ECO:0000269|PubMed:18583960"
FT MOD_RES 469
FT /note="Phosphothreonine; by CSNK1E; in vitro"
FT /evidence="ECO:0000269|PubMed:29222110"
FT MOD_RES 470
FT /note="Phosphoserine; by CSNK1E; in vitro"
FT /evidence="ECO:0000269|PubMed:29222110"
FT MOD_RES 520
FT /note="Phosphoserine; by TBK1; in vitro"
FT /evidence="ECO:0000269|PubMed:18583960"
FT MOD_RES 542
FT /note="Phosphothreonine; by TBK1; in vitro"
FT /evidence="ECO:0000269|PubMed:18583960"
FT MOD_RES 543
FT /note="Phosphoserine; by CSNK1E and TBK1; in vitro"
FT /evidence="ECO:0000269|PubMed:18583960,
FT ECO:0000269|PubMed:29222110"
FT MOD_RES 592
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 617
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 632
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 35..51
FT /note="KGRYIPPHLRNREATKG -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042830"
FT VARIANT 214
FT /note="I -> T (in MRXSSB; loss-of-function mutation
FT affecting regulation of Wnt signaling)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075731"
FT VARIANT 233
FT /note="A -> V (in MRXSSB; dbSNP:rs796052223)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075732"
FT VARIANT 233
FT /note="Missing (in MRXSSB)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075733"
FT VARIANT 235
FT /note="L -> P (in MRXSSB; dbSNP:rs796052224)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075734"
FT VARIANT 294
FT /note="R -> T (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035839"
FT VARIANT 300
FT /note="V -> F (in MRXSSB)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075735"
FT VARIANT 326
FT /note="R -> H (in MRXSSB; loss-of-function mutation
FT affecting regulation of Wnt signaling; dbSNP:rs797045025)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075736"
FT VARIANT 351
FT /note="R -> Q (in MRXSSB; dbSNP:rs1057518707)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075737"
FT VARIANT 362
FT /note="R -> C (in MRXSSB; dbSNP:rs797045026)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075738"
FT VARIANT 376
FT /note="R -> C (in MRXSSB; also found as a somatic mutation
FT in medulloblastoma; loss of ATPase activity; increased
FT interaction with CSNK1E in the absence of dsRNA; contrary
FT to wild-type protein, strongly interacts with CSNK1A1 and
FT CSNK1D in vivo; strongly increased ability to activate
FT CSNK1E kinase activity, leading to increased DVL
FT phosphorylation, thereby activating Wnt/beta-catenin
FT signaling; increased RNA-binding; no effect on subcellular
FT location; dbSNP:rs796052231)"
FT /evidence="ECO:0000269|PubMed:26235985,
FT ECO:0000269|PubMed:29222110"
FT /id="VAR_075739"
FT VARIANT 392
FT /note="L -> P (in MRXSSB; dbSNP:rs796052232)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075740"
FT VARIANT 417
FT /note="Q -> P (in MRXSSB; dbSNP:rs796052233)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075741"
FT VARIANT 475
FT /note="R -> G (in MRXSSB; dbSNP:rs1064794574)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075742"
FT VARIANT 480
FT /note="R -> S (in MRXSSB)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075743"
FT VARIANT 488
FT /note="R -> H (in MRXSSB; dbSNP:rs796052235)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075744"
FT VARIANT 507
FT /note="I -> T (in MRXSSB; loss-of-function mutation
FT affecting regulation of Wnt signaling; dbSNP:rs797045024)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075745"
FT VARIANT 509
FT /note="N -> I (in MRXSSB)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075746"
FT VARIANT 514
FT /note="I -> T (in MRXSSB; dbSNP:rs796052226)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075747"
FT VARIANT 528
FT /note="R -> H (in medulloblastoma; somatic mutation; loss
FT of ATPase activity; interacts with CSNK1E, even in the
FT presence of dsRNA; contrary to wild-type protein, strongly
FT interacts with CSNK1A1 and CSNK1D in vivo; strongly
FT increased ability to activate CSNK1E kinase activity,
FT leading to increased DVL phosphorylation, thereby
FT activating Wnt/beta-catenin signaling; no effect on RNA-
FT binding, nor on subcellular location)"
FT /evidence="ECO:0000269|PubMed:29222110"
FT /id="VAR_083115"
FT VARIANT 534
FT /note="R -> H (in MRXSSB; loss-of-function mutation
FT affecting regulation of Wnt signaling)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075748"
FT VARIANT 560
FT /note="Missing (in MRXSSB)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075749"
FT VARIANT 568
FT /note="P -> L (in MRXSSB; dbSNP:rs1057519430)"
FT /evidence="ECO:0000269|PubMed:26235985"
FT /id="VAR_075750"
FT MUTAGEN 12..21
FT /note="LDQQFAGLDL->ADQQAAGADA: Impairs nuclear export and
FT interaction with XPO1/CMR1."
FT /evidence="ECO:0000269|PubMed:31575075"
FT MUTAGEN 19..21
FT /note="LDL->ADA: Impairs nuclear export and interaction
FT with XPO1/CMR1."
FT /evidence="ECO:0000269|PubMed:30131165"
FT MUTAGEN 38
FT /note="Y->A: Impaired interaction with EIF4E; impaired
FT stress granule formation, decreased repression of cap-
FT dependent translation and decreased ability to enhance
FT IRES-mediated translation. No effect on translation of HIV-
FT 1 RNA; when associated with A-43."
FT /evidence="ECO:0000269|PubMed:17667941,
FT ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22872150"
FT MUTAGEN 43
FT /note="L->A: Impaired interaction with EIF4E; decreased
FT repression of cap-dependent translation. Fails to induce
FT stress granule assembly and to rescue cell viability after
FT stress. No effect on translation of HIV-1 RNA; when
FT associated with A-38."
FT /evidence="ECO:0000269|PubMed:17667941,
FT ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22872150"
FT MUTAGEN 71
FT /note="S->A: Reduces total phosphorylation by 60%. No
FT effect on interaction with IKBKE."
FT /evidence="ECO:0000269|PubMed:23478265"
FT MUTAGEN 82..83
FT /note="SS->AA: Reduces total phosphorylation by 50%. No
FT effect on interaction with IKBKE."
FT /evidence="ECO:0000269|PubMed:23478265"
FT MUTAGEN 84..85
FT /note="FF->AA: Loss of interaction with VACV protein K7,
FT IRF3 activation and IFNB1 promoter induction."
FT /evidence="ECO:0000269|PubMed:19913487"
FT MUTAGEN 102
FT /note="S->A: Reduces total phosphorylation by 30%.
FT Abolishes interaction with IRF3 and fails to enhance IFNB
FT promoter induction. No effect on interaction with IKBKE."
FT /evidence="ECO:0000269|PubMed:23478265"
FT MUTAGEN 102
FT /note="S->D: Interacts with IRF3 and enhances IFNB promoter
FT induction."
FT /evidence="ECO:0000269|PubMed:23478265"
FT MUTAGEN 142..144
FT /note="PSE->ASA: Loss of interaction with TRAF3, reduced
FT TRAF3 'K-63'-linked autoubiquitination."
FT /evidence="ECO:0000269|PubMed:27980081"
FT MUTAGEN 152
FT /note="S->A: Reduces total phosphorylation by 60%. No
FT effect on interaction with IKBKE."
FT /evidence="ECO:0000269|PubMed:23478265"
FT MUTAGEN 181
FT /note="S->A: Greatly impairs phosphorylation by TBK1 and
FT fails to synergize with TBK1 in IFNB1 induction; when
FT associated with A-183; A-240 and A-269."
FT /evidence="ECO:0000269|PubMed:18583960"
FT MUTAGEN 183
FT /note="S->A: Greatly impairs phosphorylation by TBK1 and
FT fails to synergize with TBK1 in IFN-beta induction; when
FT associated with A-181; A-240 and A-269."
FT /evidence="ECO:0000269|PubMed:18583960"
FT MUTAGEN 200
FT /note="Y->A: No effect on general translation; when
FT associated with A-207; A-230; A-347 and A-348."
FT /evidence="ECO:0000269|PubMed:22323517"
FT MUTAGEN 207
FT /note="Q->A: Does not promote the translation of HIV-1 RNA.
FT No effect on general translation; when associated with A-
FT 200; A-230: A-347 and A-348."
FT /evidence="ECO:0000269|PubMed:22323517,
FT ECO:0000269|PubMed:22872150"
FT MUTAGEN 230
FT /note="K->A: No effect on general translation; when
FT associated with A-200; A-207; A-347 and A-348."
FT /evidence="ECO:0000269|PubMed:22323517"
FT MUTAGEN 230
FT /note="K->E: Complete loss of ATPase and RNA-unwinding
FT activities. Loss of HIV-1 mRNA nuclear export. Does not
FT promote the translation of HIV-1 RNA. No effect on IFNB1
FT induction. No effect on RNA-binding. Loss of inhibition of
FT NF-kappa-B-mediated transcriptional activity."
FT /evidence="ECO:0000269|PubMed:15507209,
FT ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:18636090,
FT ECO:0000269|PubMed:21589879, ECO:0000269|PubMed:22872150,
FT ECO:0000269|PubMed:27736973"
FT MUTAGEN 240
FT /note="S->A: Greatly impairs phosphorylation by TBK1 and
FT fails to synergize with TBK1 in IFN-beta induction; when
FT associated with A-181; A-183 and A-269."
FT /evidence="ECO:0000269|PubMed:18583960"
FT MUTAGEN 269
FT /note="S->A: Greatly impairs phosphorylation by TBK1 and
FT fails to synergize with TBK1 in IFN-beta induction; when
FT associated with A-181; A-183 and A-240."
FT /evidence="ECO:0000269|PubMed:18583960"
FT MUTAGEN 275..277
FT /note="TRE->RRV: Increased NF-kappa-B-mediated
FT transcriptional activity, contrary to wild-type which is
FT inhibitory in this experimental setting."
FT /evidence="ECO:0000269|PubMed:27736973"
FT MUTAGEN 347..350
FT /note="DEAD->AEAA: Loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:21589879"
FT MUTAGEN 347
FT /note="D->A: No effect on general translation; when
FT associated with A-200; A-207; A-230 and A-348."
FT /evidence="ECO:0000269|PubMed:22323517"
FT MUTAGEN 348
FT /note="E->A: No effect on general translation; when
FT associated with A-200; A-207; A-230 and A-347."
FT /evidence="ECO:0000269|PubMed:22323517,
FT ECO:0000269|PubMed:22872150"
FT MUTAGEN 348
FT /note="E->Q: Loss of both ATPase and RNA helicase
FT activities; decreased up-regulation of CDKN1A promoter
FT activity and HNF4A-mediated MTTP transcriptional
FT activation; no effect on the repression of cap- and IRES-
FT dependent translation, WNT/beta catenin signaling, nor on
FT stress granule assembly. Does not promote the translation
FT of HIV-1 RNA."
FT /evidence="ECO:0000269|PubMed:17667941,
FT ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22323517,
FT ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:23413191"
FT MUTAGEN 382..384
FT /note="SAT->AAA: Loss of RNA helicase, but not ATPase
FT activity; no effect on the repression of cap- and IRES-
FT dependent translation, WNT/beta catenin signaling, up-
FT regulation of CDKN1A promoter activity, HNF4A-mediated MTTP
FT transcriptional activation, nor on stress granule
FT assembly."
FT /evidence="ECO:0000269|PubMed:17667941,
FT ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:23413191,
FT ECO:0000269|PubMed:28128295"
FT MUTAGEN 382
FT /note="S->L: Strong decrease in ATPase activity and RNA-
FT unwinding activity. Does not promote the translation of
FT mRNAs containing long structured 5'UTRs, including that of
FT CCNE1. No effect on the translation of HIV-1 RNA."
FT /evidence="ECO:0000269|PubMed:15507209,
FT ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:20837705,
FT ECO:0000269|PubMed:22872150"
FT MUTAGEN 429
FT /note="S->A: Impairs phosphorylation by TBK1 and fails to
FT synergize with TBK1 in IFN-beta induction; when associated
FT with A-438; A-442; A-456 and A-520."
FT /evidence="ECO:0000269|PubMed:18583960"
FT MUTAGEN 438
FT /note="T->A: Impairs phosphorylation by TBK1 and fails to
FT synergize with TBK1 in IFN-beta induction; when associated
FT with A-429; A-442; A-456 and A-520."
FT /evidence="ECO:0000269|PubMed:18583960"
FT MUTAGEN 442
FT /note="S->A: Impairs phosphorylation by TBK1 and fails to
FT synergize with TBK1 in IFN-beta induction; when associated
FT with A-429; A-438; A-456 and A-520."
FT /evidence="ECO:0000269|PubMed:18583960"
FT MUTAGEN 456
FT /note="S->A: Impairs phosphorylation by TBK1 and fails to
FT synergize with TBK1 in IFN-beta induction; when associated
FT with A-429; A-438; A-442 and A-520."
FT /evidence="ECO:0000269|PubMed:18583960"
FT MUTAGEN 520
FT /note="S->A: Impairs phosphorylation by TBK1 and fails to
FT synergize with TBK1 in IFN-beta induction; when associated
FT with A-429; A-438; A-442 and A-456."
FT /evidence="ECO:0000269|PubMed:18583960"
FT CONFLICT 50
FT /note="K -> R (in Ref. 3; AAC51830/AAC51829)"
FT /evidence="ECO:0000305"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5E7I"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:5E7I"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4PXA"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:2I4I"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2I4I"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:2I4I"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:2I4I"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:2I4I"
FT HELIX 230..245
FT /evidence="ECO:0007829|PDB:2I4I"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:2I4I"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:4PXA"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:2I4I"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:2I4I"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:2I4I"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:2I4I"
FT HELIX 306..313
FT /evidence="ECO:0007829|PDB:2I4I"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:2I4I"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:2I4I"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:2I4I"
FT HELIX 349..354
FT /evidence="ECO:0007829|PDB:2I4I"
FT HELIX 358..365
FT /evidence="ECO:0007829|PDB:2I4I"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:2I4I"
FT STRAND 376..383
FT /evidence="ECO:0007829|PDB:2I4I"
FT HELIX 387..396
FT /evidence="ECO:0007829|PDB:2I4I"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:2I4I"
FT TURN 411..414
FT /evidence="ECO:0007829|PDB:5E7J"
FT STRAND 415..421
FT /evidence="ECO:0007829|PDB:2JGN"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:2JGN"
FT HELIX 427..437
FT /evidence="ECO:0007829|PDB:2JGN"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:2JGN"
FT HELIX 451..463
FT /evidence="ECO:0007829|PDB:2JGN"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:2JGN"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:5E7M"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:2JGN"
FT HELIX 482..488
FT /evidence="ECO:0007829|PDB:2JGN"
FT STRAND 491..498
FT /evidence="ECO:0007829|PDB:2JGN"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:5E7I"
FT TURN 502..504
FT /evidence="ECO:0007829|PDB:2JGN"
FT STRAND 509..517
FT /evidence="ECO:0007829|PDB:2JGN"
FT HELIX 522..529
FT /evidence="ECO:0007829|PDB:2JGN"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:5E7I"
FT STRAND 539..545
FT /evidence="ECO:0007829|PDB:2JGN"
FT HELIX 547..552
FT /evidence="ECO:0007829|PDB:2JGN"
FT HELIX 553..562
FT /evidence="ECO:0007829|PDB:2JGN"
FT HELIX 569..575
FT /evidence="ECO:0007829|PDB:2JGN"
FT HELIX 578..580
FT /evidence="ECO:0007829|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
