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ATP-dependent RNA helicase DDX3X (EC 3.6.4.13) (DEAD box protein 3, X-chromosomal) (DEAD box, X isoform) (Helicase-like protein 2) (HLP2)

 DDX3X_HUMAN             Reviewed;         662 AA.
O00571; A8K538; B4E3E8; O15536;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 204.
RecName: Full=ATP-dependent RNA helicase DDX3X;
EC=3.6.4.13;
AltName: Full=DEAD box protein 3, X-chromosomal;
AltName: Full=DEAD box, X isoform;
AltName: Full=Helicase-like protein 2;
Short=HLP2;
Name=DDX3X; Synonyms=DBX, DDX3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Hippocampus, and Liver;
Chung J., Lee S.-G., Song K.;
"Identification of a human homolog of a putative RNA helicase gene
(mDEAD3) expressed in mouse erythroid cells.";
Korean J. Biochem. 27:193-197(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (MICROBIAL
INFECTION), SUBCELLULAR LOCATION, AND INTERACTION WITH HCV CORE
PROTEIN.
TISSUE=Liver;
PubMed=10329544; DOI=10.1006/viro.1999.9659;
Owsianka A.M., Patel A.H.;
"Hepatitis C virus core protein interacts with a human DEAD box
protein DDX3.";
Virology 257:330-340(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9381176; DOI=10.1126/science.278.5338.675;
Lahn B.T., Page D.C.;
"Functional coherence of the human Y chromosome.";
Science 278:675-680(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT SER-2.
PubMed=10859333; DOI=10.1084/jem.191.12.2083;
Yaguee J., Alvarez I., Rognan D., Ramos M., Vazquez J.,
Lopez de Castro J.A.;
"An N-acetylated natural ligand of human histocompatibility leukocyte
antigen (HLA)-B39. Classical major histocompatibility complex class I
proteins bind peptides with a blocked NH(2) terminus in vivo.";
J. Exp. Med. 191:2083-2092(2000).
[9]
FUNCTION (MICROBIAL INFECTION), IDENTIFICATION IN A COMPLEX WITH XPO1
AND REV, INTERACTION WITH XPO1, MUTAGENESIS OF LYS-230 AND SER-382,
AND SUBCELLULAR LOCATION.
PubMed=15507209; DOI=10.1016/j.cell.2004.09.029;
Yedavalli V.S., Neuveut C., Chi Y.-H., Kleiman L., Jeang K.-T.;
"Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export
function.";
Cell 119:381-392(2004).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[11]
FUNCTION, INTERACTION WITH SP1, AND SUBCELLULAR LOCATION.
PubMed=16818630; DOI=10.1158/0008-5472.CAN-05-2415;
Chao C.H., Chen C.M., Cheng P.L., Shih J.W., Tsou A.P., Lee Y.H.;
"DDX3, a DEAD box RNA helicase with tumor growth-suppressive property
and transcriptional regulation activity of the p21waf1/cip1 promoter,
is a candidate tumor suppressor.";
Cancer Res. 66:6579-6588(2006).
[12]
FUNCTION.
PubMed=16301996; DOI=10.1038/sj.onc.1209239;
Chang P.C., Chi C.W., Chau G.Y., Li F.Y., Tsai Y.H., Wu J.C.,
Wu Lee Y.H.;
"DDX3, a DEAD box RNA helicase, is deregulated in hepatitis virus-
associated hepatocellular carcinoma and is involved in cell growth
control.";
Oncogene 25:1991-2003(2006).
[13]
FUNCTION.
PubMed=17357160; DOI=10.1002/prot.21433;
Franca R., Belfiore A., Spadari S., Maga G.;
"Human DEAD-box ATPase DDX3 shows a relaxed nucleoside substrate
specificity.";
Proteins 67:1128-1137(2007).
[14]
ASSOCIATION WITH SPLICED MRNAS.
PubMed=17095540; DOI=10.1261/rna.336807;
Merz C., Urlaub H., Will C.L., Luhrmann R.;
"Protein composition of human mRNPs spliced in vitro and differential
requirements for mRNP protein recruitment.";
RNA 13:116-128(2007).
[15]
FUNCTION, AND INTERACTION WITH GSK3A; GSK3B AND TNFRSF10B.
PubMed=18846110; DOI=10.1038/cdd.2008.124;
Sun M., Song L., Li Y., Zhou T., Jope R.S.;
"Identification of an antiapoptotic protein complex at death
receptors.";
Cell Death Differ. 15:1887-1900(2008).
[16]
FUNCTION, PHOSPHORYLATION BY TBK1 AND IKBKE, AND MUTAGENESIS OF
SER-181; SER-183; SER-240; SER-269; SER-429; THR-438; SER-442; SER-456
AND SER-520.
PubMed=18583960; DOI=10.1038/emboj.2008.126;
Soulat D., Burckstummer T., Westermayer S., Goncalves A., Bauch A.,
Stefanovic A., Hantschel O., Bennett K.L., Decker T.,
Superti-Furga G.;
"The DEAD-box helicase DDX3X is a critical component of the TANK-
binding kinase 1-dependent innate immune response.";
EMBO J. 27:2135-2146(2008).
[17]
FUNCTION, AND INTERACTION WITH VACV PROTEIN K7 AND IKBKE.
PubMed=18636090; DOI=10.1038/emboj.2008.143;
Schroder M., Baran M., Bowie A.G.;
"Viral targeting of DEAD box protein 3 reveals its role in
TBK1/IKKepsilon-mediated IRF activation.";
EMBO J. 27:2147-2157(2008).
[18]
INTERACTION WITH TDRD3.
PubMed=18632687; DOI=10.1093/hmg/ddn203;
Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.;
"TDRD3, a novel Tudor domain-containing protein, localizes to
cytoplasmic stress granules.";
Hum. Mol. Genet. 17:3055-3074(2008).
[19]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NXF1.
PubMed=18596238; DOI=10.1091/mbc.E07-12-1264;
Lai M.C., Lee Y.H., Tarn W.Y.;
"The DEAD-box RNA helicase DDX3 associates with export messenger
ribonucleoproteins as well as tip-associated protein and participates
in translational control.";
Mol. Biol. Cell 19:3847-3858(2008).
[20]
FUNCTION, SUBCELLULAR LOCATION, AND ASSOCIATION WITH THE EIF-3
COMPLEX.
PubMed=18628297; DOI=10.1093/nar/gkn454;
Lee C.S., Dias A.P., Jedrychowski M., Patel A.H., Hsu J.L., Reed R.;
"Human DDX3 functions in translation and interacts with the
translation initiation factor eIF3.";
Nucleic Acids Res. 36:4708-4718(2008).
[21]
FUNCTION, INTERACTION WITH EIF4E, AND MUTAGENESIS OF TYR-38 AND
LEU-43.
PubMed=17667941; DOI=10.1038/sj.onc.1210687;
Shih J.W., Tsai T.Y., Chao C.H., Wu Lee Y.H.;
"Candidate tumor suppressor DDX3 RNA helicase specifically represses
cap-dependent translation by acting as an eIF4E inhibitory protein.";
Oncogene 27:700-714(2008).
[22]
FUNCTION.
PubMed=18264132; DOI=10.1038/onc.2008.33;
Botlagunta M., Vesuna F., Mironchik Y., Raman A., Lisok A.,
Winnard P. Jr., Mukadam S., Van Diest P., Chen J.H., Farabaugh P.,
Patel A.H., Raman V.;
"Oncogenic role of DDX3 in breast cancer biogenesis.";
Oncogene 27:3912-3922(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
IDENTIFICATION IN A MRNP COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=19029303; DOI=10.1261/rna.1175909;
Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M.,
Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.;
"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic
RNPs.";
RNA 15:104-115(2009).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[26]
FUNCTION, INTERACTION WITH MAVS AND DDX58, AND SUBCELLULAR LOCATION.
PubMed=20127681; DOI=10.1002/eji.200940203;
Oshiumi H., Sakai K., Matsumoto M., Seya T.;
"DEAD/H BOX 3 (DDX3) helicase binds the RIG-I adaptor IPS-1 to up-
regulate IFN-beta-inducing potential.";
Eur. J. Immunol. 40:940-948(2010).
[27]
FUNCTION, AND INTERACTION WITH IKBKE AND TBK1.
PubMed=20375222; DOI=10.1099/vir.0.020552-0;
Yu S., Chen J., Wu M., Chen H., Kato N., Yuan Z.;
"Hepatitis B virus polymerase inhibits RIG-I- and Toll-like receptor
3-mediated beta interferon induction in human hepatocytes through
interference with interferon regulatory factor 3 activation and
dampening of the interaction between TBK1/IKKepsilon and DDX3.";
J. Gen. Virol. 91:2080-2090(2010).
[28]
FUNCTION.
PubMed=20837705; DOI=10.1128/MCB.00560-10;
Lai M.C., Chang W.C., Shieh S.Y., Tarn W.Y.;
"DDX3 regulates cell growth through translational control of cyclin
E1.";
Mol. Cell. Biol. 30:5444-5453(2010).
[29]
FUNCTION, RNA-BINDING, INTERACTION WITH MAVS, AND SUBCELLULAR
LOCATION.
PubMed=21170385; DOI=10.1371/journal.pone.0014258;
Oshiumi H., Ikeda M., Matsumoto M., Watanabe A., Takeuchi O.,
Akira S., Kato N., Shimotohno K., Seya T.;
"Hepatitis C virus core protein abrogates the DDX3 function that
enhances IPS-1-mediated IFN-beta induction.";
PLoS ONE 5:E14258-E14258(2010).
[30]
FUNCTION, AND INTERACTION WITH IKBKE.
PubMed=20657822; DOI=10.1371/journal.ppat.1000986;
Wang H., Ryu W.S.;
"Hepatitis B virus polymerase blocks pattern recognition receptor
signaling via interaction with DDX3: implications for immune
evasion.";
PLoS Pathog. 6:E1000986-E1000986(2010).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[33]
FUNCTION.
PubMed=21589879; DOI=10.1371/journal.pone.0019810;
Garbelli A., Beermann S., Di Cicco G., Dietrich U., Maga G.;
"A motif unique to the human DEAD-box protein DDX3 is important for
nucleic acid binding, ATP hydrolysis, RNA/DNA unwinding and HIV-1
replication.";
PLoS ONE 6:E19810-E19810(2011).
[34]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH NCAPH.
PubMed=21730191; DOI=10.1073/pnas.1106245108;
Pek J.W., Kai T.;
"DEAD-box RNA helicase Belle/DDX3 and the RNA interference pathway
promote mitotic chromosome segregation.";
Proc. Natl. Acad. Sci. U.S.A. 108:12007-12012(2011).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[36]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EIF4E AND PABPC1.
PubMed=21883093; DOI=10.1042/BJ20110739;
Shih J.W., Wang W.T., Tsai T.Y., Kuo C.Y., Li H.K., Wu Lee Y.H.;
"Critical roles of RNA helicase DDX3 and its interactions with
eIF4E/PABP1 in stress granule assembly and stress response.";
Biochem. J. 441:119-129(2012).
[37]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INDUCTION, AND
INTERACTION WITH DDX5.
PubMed=22034099; DOI=10.1002/jcb.23428;
Choi Y.J., Lee S.G.;
"The DEAD-box RNA helicase DDX3 interacts with DDX5, co-localizes with
it in the cytoplasm during the G2/M phase of the cycle, and affects
its shuttling during mRNP export.";
J. Cell. Biochem. 113:985-996(2012).
[38]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[39]
FUNCTION, ASSOCIATION WITH THE RIBOSOME SMALL SUBUNIT, INTERACTION
WITH EIF3C, AND MUTAGENESIS OF TYR-200; GLN-207; LYS-230; ASP-347 AND
GLU-348.
PubMed=22323517; DOI=10.1093/nar/gks070;
Geissler R., Golbik R.P., Behrens S.E.;
"The DEAD-box helicase DDX3 supports the assembly of functional 80S
ribosomes.";
Nucleic Acids Res. 40:4998-5011(2012).
[40]
FUNCTION, RNA-BINDING, INTERACTION WITH EIF4G1 AND PABPC1, AND
MUTAGENESIS OF TYR-38; LEU-43; GLN-207; LYS-230; GLU-348 AND SER-382.
PubMed=22872150; DOI=10.1038/emboj.2012.220;
Soto-Rifo R., Rubilar P.S., Limousin T., de Breyne S., Decimo D.,
Ohlmann T.;
"DEAD-box protein DDX3 associates with eIF4F to promote translation of
selected mRNAs.";
EMBO J. 31:3745-3756(2012).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-86; SER-90;
SER-594 AND SER-605, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[42]
FUNCTION AS SCAFFOLD PROTEIN, INTERACTION WITH IKBKE AND IRF3,
PHOSPHORYLATION AT SER-102, AND MUTAGENESIS OF SER-71; 82-SER-SER-83;
SER-102 AND SER-152.
PubMed=23478265; DOI=10.1128/MCB.01603-12;
Gu L., Fullam A., Brennan R., Schroder M.;
"Human DEAD box helicase 3 couples IkappaB kinase epsilon to
interferon regulatory factor 3 activation.";
Mol. Cell. Biol. 33:2004-2015(2013).
[43]
FUNCTION, AND INTERACTION WITH CSNK1E.
PubMed=23413191; DOI=10.1126/science.1231499;
Cruciat C.M., Dolde C., de Groot R.E., Ohkawara B., Reinhard C.,
Korswagen H.C., Niehrs C.;
"RNA helicase DDX3 is a regulatory subunit of casein kinase 1 in Wnt-
beta-catenin signaling.";
Science 339:1436-1441(2013).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[45]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-592; ARG-617 AND ARG-632,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[46]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[47]
INVOLVEMENT IN MRX102, VARIANTS MRX102 THR-214; ALA-233 DEL; VAL-233;
PRO-235; PHE-300; HIS-326; GLN-351; CYS-362; CYS-376; PRO-392;
PRO-417; GLY-475; SER-480; HIS-488; THR-507; ILE-509; THR-514;
HIS-534; LEU-560 DEL AND LEU-568, AND CHARACTERIZATION OF VARIANTS
MRX102 THR-214; HIS-326; CYS-376; THR-507 AND HIS-534.
PubMed=26235985; DOI=10.1016/j.ajhg.2015.07.004;
DDD Study;
Snijders Blok L., Madsen E., Juusola J., Gilissen C., Baralle D.,
Reijnders M.R., Venselaar H., Helsmoortel C., Cho M.T., Hoischen A.,
Vissers L.E., Koemans T.S., Wissink-Lindhout W., Eichler E.E.,
Romano C., Van Esch H., Stumpel C., Vreeburg M., Smeets E.,
Oberndorff K., van Bon B.W., Shaw M., Gecz J., Haan E., Bienek M.,
Jensen C., Loeys B.L., Van Dijck A., Innes A.M., Racher H.,
Vermeer S., Di Donato N., Rump A., Tatton-Brown K., Parker M.J.,
Henderson A., Lynch S.A., Fryer A., Ross A., Vasudevan P., Kini U.,
Newbury-Ecob R., Chandler K., Male A., Dijkstra S., Schieving J.,
Giltay J., van Gassen K.L., Schuurs-Hoeijmakers J., Tan P.L.,
Pediaditakis I., Haas S.A., Retterer K., Reed P., Monaghan K.G.,
Haverfield E., Natowicz M., Myers A., Kruer M.C., Stein Q.,
Strauss K.A., Brigatti K.W., Keating K., Burton B.K., Kim K.H.,
Charrow J., Norman J., Foster-Barber A., Kline A.D., Kimball A.,
Zackai E., Harr M., Fox J., McLaughlin J., Lindstrom K., Haude K.M.,
van Roozendaal K., Brunner H., Chung W.K., Kooy R.F., Pfundt R.,
Kalscheuer V., Mehta S.G., Katsanis N., Kleefstra T.;
"Mutations in DDX3X are a common cause of unexplained intellectual
disability with gender-specific effects on Wnt signaling.";
Am. J. Hum. Genet. 97:343-352(2015).
[48]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[49]
SUBUNIT.
PubMed=27546789; DOI=10.1016/j.molcel.2016.07.010;
Kim Y., Myong S.;
"RNA remodeling activity of DEAD box proteins tuned by protein
concentration, RNA length, and ATP.";
Mol. Cell 63:865-876(2016).
[50]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[51]
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 409-580.
PubMed=17401195; DOI=10.1107/S1744309107006434;
Rodamilans B., Montoya G.;
"Expression, purification, crystallization and preliminary X-ray
diffraction analysis of the DDX3 RNA helicase domain.";
Acta Crystallogr. F 63:283-286(2007).
[52]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 168-582 IN COMPLEX WITH AMP.
PubMed=17631897; DOI=10.1016/j.jmb.2007.06.050;
Hoegbom M., Collins R., van den Berg S., Jenvert R.-M., Karlberg T.,
Kotenyova T., Flores A., Karlsson Hedestam G.B., Schiavone L.H.;
"Crystal structure of conserved domains 1 and 2 of the human DEAD-box
helicase DDX3X in complex with the mononucleotide AMP.";
J. Mol. Biol. 372:150-159(2007).
[53]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 71-90 IN COMPLEX WITH VACV
PROTEIN K7, AND MUTAGENESIS OF 84-PHE-PHE-85.
PubMed=19913487; DOI=10.1016/j.str.2009.09.005;
Oda S., Schroder M., Khan A.R.;
"Structural basis for targeting of human RNA helicase DDX3 by poxvirus
protein K7.";
Structure 17:1528-1537(2009).
[54]
VARIANT [LARGE SCALE ANALYSIS] THR-294.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Multifunctional ATP-dependent RNA helicase. The ATPase
activity can be stimulated by various ribo- and deoxynucleic acids
indicative for a relaxed substrate specificity. In vitro can
unwind partially double-stranded DNA with a preference for 5'-
single-stranded DNA overhangs. Is involved in several steps of
gene expression, such as transcription, mRNA maturation, mRNA
export and translation. However, the exact mechanisms are not
known and some functions may be specific for a subset of mRNAs.
Involved in transcriptional regulation. Can enhance transcription
from the CDKN1A/WAF1 promoter in a SP1-dependent manner. Found
associated with the E-cadherin promoter and can down-regulate
transcription from the promoter. Involved in regulation of
translation initiation. Proposed to be involved in positive
regulation of translation such as of cyclin E1/CCNE1 mRNA and
specifically of mRNAs containing complex secondary structures in
their 5'UTRs; these functions seem to require RNA helicase
activity. Specifically promotes translation of a subset of viral
and cellular mRNAs carrying a 5'proximal stem-loop structure in
their 5'UTRs and cooperates with the eIF4F complex. Proposed to
act prior to 43S ribosomal scanning and to locally destabilize
these RNA structures to allow recognition of the mRNA cap or
loading onto the 40S subunit. After association with 40S ribosomal
subunits seems to be involved in the functional assembly of 80S
ribosomes; the function seems to cover translation of mRNAs with
structured and non-structured 5'UTRs and is independent of RNA
helicase activity. Also proposed to inhibit cap-dependent
translation by competetive interaction with EIF4E which can block
the EIF4E:EIF4G complex formation. Proposed to be involved in
stress response and stress granule assembly; the function is
independent of RNA helicase activity and seems to involve
association with EIF4E. May be involved in nuclear export of
specific mRNAs but not in bulk mRNA export via interactions with
XPO1 and NXF1. Also associates with polyadenylated mRNAs
independently of NXF1. Associates with spliced mRNAs in an exon
junction complex (EJC)-dependent manner and seems not to be
directly involved in splicing. May be involved in nuclear mRNA
export by association with DDX5 and regulating its nuclear
location. Involved in innate immune signaling promoting the
production of type I interferon (IFN-alpha and IFN-beta); proposed
to act as viral RNA sensor, signaling intermediate and
transcriptional coactivator. Involved in TBK1 and IKBKE-dependent
IRF3 activation leading to IFNB induction, plays a role of
scaffolding adapter that links IKBKE and IRF3 and coordinates
their activation. Also found associated with IFNB promoters; the
function is independent of IRF3. Can bind to viral RNAs and via
association with MAVS/IPS1 and DDX58/RIG-I is thought to induce
signaling in early stages of infection. Involved in regulation of
apoptosis. May be required for activation of the intrinsic but
inhibit activation of the extrinsic apoptotic pathway. Acts as an
antiapoptotic protein through association with GSK3A/B and BIRC2
in an apoptosis antagonizing signaling complex; activation of
death receptors promotes caspase-dependent cleavage of BIRC2 and
DDX3X and relieves the inhibition. May be involved in mitotic
chromosome segregation. Is an allosteric activator of CSNK1E, it
stimulates CSNK1E-mediated phosphorylation of DVL2 and is involved
in the positive regulation of canonical Wnt signaling
(PubMed:23413191). {ECO:0000269|PubMed:16301996,
ECO:0000269|PubMed:16818630, ECO:0000269|PubMed:17357160,
ECO:0000269|PubMed:17667941, ECO:0000269|PubMed:18264132,
ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:18596238,
ECO:0000269|PubMed:18628297, ECO:0000269|PubMed:18636090,
ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:20127681,
ECO:0000269|PubMed:20375222, ECO:0000269|PubMed:20657822,
ECO:0000269|PubMed:20837705, ECO:0000269|PubMed:21170385,
ECO:0000269|PubMed:21730191, ECO:0000269|PubMed:21883093,
ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:22323517,
ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:23413191,
ECO:0000269|PubMed:23478265}.
-!- FUNCTION: (Microbial infection) Appears to be a prime target for
viral manipulations. Hepatitis B virus (HBV) polymerase and
possibly vaccinia virus (VACV) protein K7 inhibit IFNB induction
probably by dissociating DDX3X from TBK1 or IKBKE. Is involved in
hepatitis C virus (HCV) replication; the function may involve the
association with HCV core protein. HCV core protein inhibits the
IPS1-dependent function in viral RNA sensing and may switch the
function from a INFB inducing to a HCV replication mode. Involved
in HIV-1 replication. Acts as a cofactor for XPO1-mediated nuclear
export of incompletely spliced HIV-1 Rev RNAs.
{ECO:0000269|PubMed:10329544, ECO:0000269|PubMed:15507209,
ECO:0000269|PubMed:21589879}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Binds RNA as a monomer at low DDX3X concentrations and as
a dimer at high DDX3X concentrations (PubMed:27546789). Interacts
with XPO1, TDRD3, PABPC1, NXF1, EIF3C, MAVS, DDX58 and NCAPH
(PubMed:15507209, PubMed:18632687, PubMed:18596238,
PubMed:20127681, PubMed:21170385, PubMed:21730191,
PubMed:21883093, PubMed:22323517, PubMed:22872150). Interacts with
DDX5; the interaction is regulated by the phosphorylation status
of both proteins (PubMed:22034099). Interacts with EIF4E; DDX3X
competes with EIF4G1/EIF4G3 for interaction with EIF4E
(PubMed:17667941, PubMed:21883093). Interacts with IKBKE; the
interaction is direct, found to be induced upon virus infection
(PubMed:20375222, PubMed:20657822, PubMed:23478265). Interacts
(when phosphorylated at Ser-102) with IRF3; the interaction allows
the phosphorylation and activation of IRF3 by IKBKE
(PubMed:23478265). Interacts with TBK1 (PubMed:20375222).
Associates with the eukaryotic translation initiation factor 3
(eIF-3) complex (PubMed:18628297). Associates with the 40S
ribosome (PubMed:22323517). Identified in a mRNP complex, at least
composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1,
PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1 (PubMed:19029303).
Interacts with SP1 (PubMed:16818630). Interacts with GSK3A, GSK3B
and TNFRSF10B (PubMed:18846110). Interacts with HCV core protein
(PubMed:10329544). Interacts with vaccinia virus (VACV) protein K7
(PubMed:18636090, PubMed:19913487). Found in a complex with HIV-1
Rev and XPO1 (PubMed:15507209). Interacts with CSNK1E; the
interaction enhances CSNK1E recruitement to DVL2
(PubMed:23413191). {ECO:0000269|PubMed:10329544,
ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:16818630,
ECO:0000269|PubMed:17631897, ECO:0000269|PubMed:17667941,
ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18632687,
ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:18846110,
ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19913487,
ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:20375222,
ECO:0000269|PubMed:20657822, ECO:0000269|PubMed:21170385,
ECO:0000269|PubMed:21730191, ECO:0000269|PubMed:21883093,
ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:22323517,
ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:23413191,
ECO:0000269|PubMed:23478265, ECO:0000269|PubMed:27546789}.
-!- INTERACTION:
P26664:- (xeno); NbExp=3; IntAct=EBI-353779, EBI-9209740;
P27958:- (xeno); NbExp=11; IntAct=EBI-353779, EBI-6377335;
Q99IB8:- (xeno); NbExp=9; IntAct=EBI-353779, EBI-6674379;
Q9WMX2:- (xeno); NbExp=4; IntAct=EBI-353779, EBI-6863754;
O95786:DDX58; NbExp=2; IntAct=EBI-353779, EBI-995350;
P05198:EIF2S1; NbExp=3; IntAct=EBI-353779, EBI-1056162;
P55884:EIF3B; NbExp=5; IntAct=EBI-353779, EBI-366696;
Q99613:EIF3C; NbExp=3; IntAct=EBI-353779, EBI-353741;
Q04637:EIF4G1; NbExp=3; IntAct=EBI-353779, EBI-73711;
Q14164:IKBKE; NbExp=4; IntAct=EBI-353779, EBI-307369;
P68467:K7R (xeno); NbExp=6; IntAct=EBI-353779, EBI-8022707;
Q7Z434:MAVS; NbExp=4; IntAct=EBI-353779, EBI-995373;
Q15003:NCAPH; NbExp=2; IntAct=EBI-353779, EBI-1046410;
Q9UBU9:NXF1; NbExp=5; IntAct=EBI-353779, EBI-398874;
P11940:PABPC1; NbExp=10; IntAct=EBI-353779, EBI-81531;
P04608:tat (xeno); NbExp=4; IntAct=EBI-353779, EBI-6164389;
Q923J1:Trpm7 (xeno); NbExp=2; IntAct=EBI-353779, EBI-8010314;
P68466:VACWR039 (xeno); NbExp=6; IntAct=EBI-353779, EBI-6152154;
-!- SUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm. Mitochondrion
outer membrane. Note=Located predominantly in nuclear speckles
and, at low levels, throughout the cytoplasm. Located to the outer
side of nuclear pore complexes (NPC). Shuttles between the nucleus
and the cytoplasm in a XPO1 and may be also in a NFX1-dependent
manner. Associated with polyadenylated mRNAs in the cytoplasm and
the nucleus. Predominantly located in nucleus during G(0) phase
and in the cytoplasm during G1/S phase.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O00571-1; Sequence=Displayed;
Name=2;
IsoId=O00571-2; Sequence=VSP_042830;
Note=No experimental confirmation available.;
-!- INDUCTION: Regulated by the cell cycle. Maximally expressed din
the cytoplasm uring G1/S phase and decreased expression during
G2/M phase. {ECO:0000269|PubMed:22034099}.
-!- PTM: Phosphorylated by TBK1; the phosphorylation is required to
synergize with TBK1 in IFNB induction. Phosphorylated by IKBKE at
Ser-102 after ssRNA viral infection; enhances the induction of
INFB promoter by IRF3. The cytoplasmic form is highly
phosphorylated in the G1/S phase and much lower phosphorylated in
G2/M. {ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:22034099,
ECO:0000269|PubMed:23478265}.
-!- DISEASE: Mental retardation, X-linked 102 (MRX102) [MIM:300958]: A
form of mental retardation, a disorder characterized by
significantly below average general intellectual functioning
associated with impairments in adaptive behavior and manifested
during the developmental period. Intellectual deficiency is the
only primary symptom of non-syndromic X-linked mental retardation,
while syndromic mental retardation presents with associated
physical, neurological and/or psychiatric manifestations. MRX102
features include mild to severe intellectual disability,
hypotonia, movement disorders, behavior problems, corpus callosum
hypoplasia, and epilepsy. Additionally, patients manifest variable
non-neurologic features such as joint hyperlaxity, skin pigmentary
abnormalities, cleft lip and/or palate, hearing and visual
impairment, and precocious puberty. {ECO:0000269|PubMed:26235985}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U50553; AAB95637.1; -; mRNA.
EMBL; AF061337; AAC34298.1; -; mRNA.
EMBL; AF000983; AAC51830.1; -; mRNA.
EMBL; AF000982; AAC51829.1; -; mRNA.
EMBL; AK291153; BAF83842.1; -; mRNA.
EMBL; AK304689; BAG65460.1; -; mRNA.
EMBL; AL391647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z93015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471141; EAW59402.1; -; Genomic_DNA.
EMBL; CH471141; EAW59403.1; -; Genomic_DNA.
EMBL; CH471141; EAW59404.1; -; Genomic_DNA.
EMBL; CH471141; EAW59405.1; -; Genomic_DNA.
EMBL; BC011819; AAH11819.1; -; mRNA.
CCDS; CCDS43931.1; -. [O00571-1]
CCDS; CCDS55404.1; -. [O00571-2]
RefSeq; NP_001180345.1; NM_001193416.2.
RefSeq; NP_001180346.1; NM_001193417.2. [O00571-2]
RefSeq; NP_001347.3; NM_001356.4. [O00571-1]
UniGene; Hs.728563; -.
UniGene; Hs.743263; -.
PDB; 2I4I; X-ray; 2.20 A; A=168-582.
PDB; 2JGN; X-ray; 1.91 A; A/B/C=409-580.
PDB; 3JRV; X-ray; 1.60 A; C/D/E=71-90.
PDB; 4O2C; X-ray; 1.80 A; C=2-10.
PDB; 4O2E; X-ray; 1.98 A; C/F=2-10.
PDB; 4O2F; X-ray; 1.90 A; C/F=3-10.
PDB; 4PX9; X-ray; 2.31 A; A/B/C=135-407.
PDB; 4PXA; X-ray; 3.20 A; A=135-582.
PDB; 5E7I; X-ray; 2.22 A; A/B/C=133-584.
PDB; 5E7J; X-ray; 2.23 A; A=133-584.
PDB; 5E7M; X-ray; 2.30 A; A=133-584.
PDBsum; 2I4I; -.
PDBsum; 2JGN; -.
PDBsum; 3JRV; -.
PDBsum; 4O2C; -.
PDBsum; 4O2E; -.
PDBsum; 4O2F; -.
PDBsum; 4PX9; -.
PDBsum; 4PXA; -.
PDBsum; 5E7I; -.
PDBsum; 5E7J; -.
PDBsum; 5E7M; -.
ProteinModelPortal; O00571; -.
SMR; O00571; -.
BioGrid; 108020; 163.
CORUM; O00571; -.
DIP; DIP-27551N; -.
ELM; O00571; -.
IntAct; O00571; 116.
MINT; MINT-8395017; -.
STRING; 9606.ENSP00000382840; -.
BindingDB; O00571; -.
ChEMBL; CHEMBL5553; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; O00571; -.
PhosphoSitePlus; O00571; -.
SwissPalm; O00571; -.
BioMuta; DDX3X; -.
REPRODUCTION-2DPAGE; IPI00215637; -.
SWISS-2DPAGE; O00571; -.
EPD; O00571; -.
MaxQB; O00571; -.
PaxDb; O00571; -.
PeptideAtlas; O00571; -.
PRIDE; O00571; -.
Ensembl; ENST00000399959; ENSP00000382840; ENSG00000215301. [O00571-1]
Ensembl; ENST00000457138; ENSP00000392494; ENSG00000215301. [O00571-2]
Ensembl; ENST00000478993; ENSP00000478443; ENSG00000215301. [O00571-1]
Ensembl; ENST00000629496; ENSP00000487224; ENSG00000215301. [O00571-1]
Ensembl; ENST00000629785; ENSP00000486516; ENSG00000215301. [O00571-1]
Ensembl; ENST00000630255; ENSP00000486720; ENSG00000215301. [O00571-1]
GeneID; 1654; -.
KEGG; hsa:1654; -.
UCSC; uc004dfe.4; human. [O00571-1]
CTD; 1654; -.
DisGeNET; 1654; -.
EuPathDB; HostDB:ENSG00000215301.9; -.
GeneCards; DDX3X; -.
HGNC; HGNC:2745; DDX3X.
HPA; HPA001648; -.
HPA; HPA005631; -.
HPA; HPA059585; -.
MalaCards; DDX3X; -.
MIM; 300160; gene.
MIM; 300958; phenotype.
neXtProt; NX_O00571; -.
OpenTargets; ENSG00000215301; -.
Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
PharmGKB; PA27216; -.
eggNOG; KOG0335; Eukaryota.
eggNOG; ENOG410XNTI; LUCA.
GeneTree; ENSGT00900000140933; -.
HOVERGEN; HBG015893; -.
InParanoid; O00571; -.
KO; K11594; -.
PhylomeDB; O00571; -.
TreeFam; TF300364; -.
BRENDA; 3.6.4.13; 2681.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; O00571; -.
ChiTaRS; DDX3X; human.
EvolutionaryTrace; O00571; -.
GeneWiki; DDX3X; -.
GenomeRNAi; 1654; -.
PRO; PR:O00571; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000215301; -.
CleanEx; HS_DDX3X; -.
ExpressionAtlas; O00571; baseline and differential.
Genevisible; O00571; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; IDA:UniProtKB.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; IDA:UniProtKB.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0043273; F:CTPase activity; IDA:AgBase.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:AgBase.
GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:UniProtKB.
GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:AgBase.
GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
GO; GO:0043024; F:ribosomal small subunit binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0035613; F:RNA stem-loop binding; IDA:UniProtKB.
GO; GO:0033592; F:RNA strand annealing activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO; GO:0031369; F:translation initiation factor binding; IDA:UniProtKB.
GO; GO:0071243; P:cellular response to arsenic-containing substance; IDA:UniProtKB.
GO; GO:0071470; P:cellular response to osmotic stress; IDA:UniProtKB.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0042256; P:mature ribosome assembly; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0031333; P:negative regulation of protein complex assembly; IDA:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; TAS:UniProtKB.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
GO; GO:0032728; P:positive regulation of interferon-beta production; TAS:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
GO; GO:0045948; P:positive regulation of translational initiation; IMP:UniProtKB.
GO; GO:0045070; P:positive regulation of viral genome replication; IMP:AgBase.
GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IMP:AgBase.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
GO; GO:0010501; P:RNA secondary structure unwinding; IDA:UniProtKB.
GO; GO:0034063; P:stress granule assembly; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; IMP:UniProtKB.
CDD; cd00079; HELICc; 1.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
Pfam; PF00270; DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51195; Q_MOTIF; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
ATP-binding; Chromosome partition; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; DNA-binding; Helicase;
Host-virus interaction; Hydrolase; Immunity; Innate immunity;
Isopeptide bond; Membrane; Mental retardation; Methylation;
Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Ribosome biogenesis; RNA-binding; Transcription;
Transcription regulation; Translation regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:10859333}.
CHAIN 2 662 ATP-dependent RNA helicase DDX3X.
/FTId=PRO_0000055009.
DOMAIN 211 403 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 414 575 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 200 207 ATP.
NP_BIND 224 231 ATP.
REGION 2 139 Required for TBK1 and IKBKE-dependent
IFN-beta activation.
REGION 2 100 Interaction with EIF4E.
REGION 81 90 Required for interaction with VACV
protein K7.
REGION 100 662 Interaction with GSK3B.
{ECO:0000269|PubMed:18846110}.
REGION 100 110 Required for interaction with IKBKE.
REGION 250 259 Involved in stimulation of ATPase
activity by DNA and RNA, nucleic acid
binding and unwinding and HIV-1
replication.
REGION 260 517 Necessary for interaction with XPO1.
{ECO:0000269|PubMed:15507209}.
MOTIF 180 208 Q motif.
MOTIF 347 350 DEAD box.
COMPBIAS 582 662 Gly/Ser-rich.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:10859333}.
MOD_RES 55 55 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q62167}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 101 101 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q62167}.
MOD_RES 102 102 Phosphoserine; by IKKE.
{ECO:0000269|PubMed:23478265}.
MOD_RES 104 104 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q62167}.
MOD_RES 110 110 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q62167}.
MOD_RES 118 118 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 131 131 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 456 456 Phosphoserine.
{ECO:0000250|UniProtKB:Q62095}.
MOD_RES 592 592 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 594 594 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 605 605 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 612 612 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 617 617 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 632 632 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
CROSSLNK 215 215 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 35 51 KGRYIPPHLRNREATKG -> S (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042830.
VARIANT 214 214 I -> T (in MRX102; loss-of-function
mutation affecting regulation of Wnt
signaling).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075731.
VARIANT 233 233 A -> V (in MRX102; dbSNP:rs796052223).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075732.
VARIANT 233 233 Missing (in MRX102).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075733.
VARIANT 235 235 L -> P (in MRX102; dbSNP:rs796052224).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075734.
VARIANT 294 294 R -> T (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035839.
VARIANT 300 300 V -> F (in MRX102).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075735.
VARIANT 326 326 R -> H (in MRX102; loss-of-function
mutation affecting regulation of Wnt
signaling; dbSNP:rs797045025).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075736.
VARIANT 351 351 R -> Q (in MRX102).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075737.
VARIANT 362 362 R -> C (in MRX102; dbSNP:rs797045026).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075738.
VARIANT 376 376 R -> C (in MRX102; loss-of-function
mutation affecting regulation of Wnt
signaling; dbSNP:rs796052231).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075739.
VARIANT 392 392 L -> P (in MRX102; dbSNP:rs796052232).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075740.
VARIANT 417 417 Q -> P (in MRX102; dbSNP:rs796052233).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075741.
VARIANT 475 475 R -> G (in MRX102).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075742.
VARIANT 480 480 R -> S (in MRX102).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075743.
VARIANT 488 488 R -> H (in MRX102; dbSNP:rs796052235).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075744.
VARIANT 507 507 I -> T (in MRX102; loss-of-function
mutation affecting regulation of Wnt
signaling; dbSNP:rs797045024).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075745.
VARIANT 509 509 N -> I (in MRX102).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075746.
VARIANT 514 514 I -> T (in MRX102; dbSNP:rs796052226).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075747.
VARIANT 534 534 R -> H (in MRX102; loss-of-function
mutation affecting regulation of Wnt
signaling).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075748.
VARIANT 560 560 Missing (in MRX102).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075749.
VARIANT 568 568 P -> L (in MRX102).
{ECO:0000269|PubMed:26235985}.
/FTId=VAR_075750.
MUTAGEN 38 38 Y->A: Impairs interaction with EIF4E. No
effect on translation of HIV-1 RNA; when
associated with A-43.
{ECO:0000269|PubMed:17667941,
ECO:0000269|PubMed:22872150}.
MUTAGEN 43 43 L->A: Impairs interaction with EIF4E.
Fails to induce stress granule assembly
and to rescue cell viability after
stress. No effect on translation of HIV-1
RNA; when associated with A-38.
{ECO:0000269|PubMed:17667941,
ECO:0000269|PubMed:22872150}.
MUTAGEN 71 71 S->A: Reduces total phosphorylation by
60%. No effect on interaction with IKBKE.
{ECO:0000269|PubMed:23478265}.
MUTAGEN 82 83 SS->AA: Reduces total phosphorylation by
50%. No effect on interaction with IKBKE.
{ECO:0000269|PubMed:23478265}.
MUTAGEN 84 85 FF->AA: Abolishes interaction with VACV
protein K7, IRF3 activation and IFN-beta
promoter induction.
{ECO:0000269|PubMed:19913487}.
MUTAGEN 102 102 S->A: Reduces total phosphorylation by
30%. Abolishes interaction with IRF3 and
fails to enhance IFNB promoter induction.
No effect on interaction with IKBKE.
{ECO:0000269|PubMed:23478265}.
MUTAGEN 102 102 S->D: Interacts with IRF3 and enhances
IFNB promoter induction.
{ECO:0000269|PubMed:23478265}.
MUTAGEN 152 152 S->A: Reduces total phosphorylation by
60%. No effect on interaction with IKBKE.
{ECO:0000269|PubMed:23478265}.
MUTAGEN 181 181 S->A: Greatly impairs phosphorylation by
TBK1 and fails to synergize with TBK1 in
IFN-beta induction; when associated with
A-183; A-240 and A-269.
{ECO:0000269|PubMed:18583960}.
MUTAGEN 183 183 S->A: Greatly impairs phosphorylation by
TBK1 and fails to synergize with TBK1 in
IFN-beta induction; when associated with
A-181; A-240 and A-269.
{ECO:0000269|PubMed:18583960}.
MUTAGEN 200 200 Y->A: No effect on general translation;
when associated with A-207; A-230; A-347
and A-348. {ECO:0000269|PubMed:22323517}.
MUTAGEN 207 207 Q->A: Inhibits translation of HIV-1 RNA.
No effect on general translation; when
associated with A-200; A-230: A-347 and
A-348. {ECO:0000269|PubMed:22323517,
ECO:0000269|PubMed:22872150}.
MUTAGEN 230 230 K->A: No effect on general translation;
when associated with A-200; A-207; A-347
and A-348. {ECO:0000269|PubMed:15507209,
ECO:0000269|PubMed:22323517,
ECO:0000269|PubMed:22872150}.
MUTAGEN 230 230 K->E: Abolishes ATPase activity and RNA-
unwinding activity. Inhibits translation
of HIV-1 RNA.
{ECO:0000269|PubMed:15507209,
ECO:0000269|PubMed:22323517,
ECO:0000269|PubMed:22872150}.
MUTAGEN 240 240 S->A: Greatly impairs phosphorylation by
TBK1 and fails to synergize with TBK1 in
IFN-beta induction; when associated with
A-181; A-183 and A-269.
{ECO:0000269|PubMed:18583960}.
MUTAGEN 269 269 S->A: Greatly impairs phosphorylation by
TBK1 and fails to synergize with TBK1 in
IFN-beta induction; when associated with
A-181; A-183 and A-240.
{ECO:0000269|PubMed:18583960}.
MUTAGEN 347 347 D->A: No effect on general translation;
when associated with A-200; A-207; A-230
and A-348. {ECO:0000269|PubMed:22323517}.
MUTAGEN 348 348 E->A: No effect on general translation;
when associated with A-200; A-207; A-230
and A-347. {ECO:0000269|PubMed:22323517,
ECO:0000269|PubMed:22872150}.
MUTAGEN 348 348 E->Q: Inhibits translation of HIV-1 RNA.
{ECO:0000269|PubMed:22323517,
ECO:0000269|PubMed:22872150}.
MUTAGEN 382 382 S->L: Abolishes ATPase activity and RNA-
unwinding activity. No effect on
translation of HIV-1 RNA.
{ECO:0000269|PubMed:15507209,
ECO:0000269|PubMed:22872150}.
MUTAGEN 429 429 S->A: Impairs phosphorylation by TBK1 and
fails to synergize with TBK1 in IFN-beta
induction; when associated with A-438; A-
442; A-456 and A-520.
{ECO:0000269|PubMed:18583960}.
MUTAGEN 438 438 T->A: Impairs phosphorylation by TBK1 and
fails to synergize with TBK1 in IFN-beta
induction; when associated with A-429; A-
442; A-456 and A-520.
{ECO:0000269|PubMed:18583960}.
MUTAGEN 442 442 S->A: Impairs phosphorylation by TBK1 and
fails to synergize with TBK1 in IFN-beta
induction; when associated with A-429; A-
438; A-456 and A-520.
{ECO:0000269|PubMed:18583960}.
MUTAGEN 456 456 S->A: Impairs phosphorylation by TBK1 and
fails to synergize with TBK1 in IFN-beta
induction; when associated with A-429; A-
438; A-442 and A-520.
{ECO:0000269|PubMed:18583960}.
MUTAGEN 520 520 S->A: Impairs phosphorylation by TBK1 and
fails to synergize with TBK1 in IFN-beta
induction; when associated with A-429; A-
438; A-442 and A-456.
{ECO:0000269|PubMed:18583960}.
CONFLICT 50 50 K -> R (in Ref. 3; AAC51830/AAC51829).
{ECO:0000305}.
STRAND 136 138 {ECO:0000244|PDB:5E7I}.
HELIX 144 151 {ECO:0000244|PDB:5E7I}.
STRAND 161 163 {ECO:0000244|PDB:4PXA}.
STRAND 168 172 {ECO:0000244|PDB:2I4I}.
HELIX 182 184 {ECO:0000244|PDB:2I4I}.
HELIX 189 198 {ECO:0000244|PDB:2I4I}.
HELIX 205 215 {ECO:0000244|PDB:2I4I}.
STRAND 220 223 {ECO:0000244|PDB:2I4I}.
HELIX 230 245 {ECO:0000244|PDB:2I4I}.
HELIX 249 256 {ECO:0000244|PDB:2I4I}.
STRAND 261 263 {ECO:0000244|PDB:4PXA}.
STRAND 268 272 {ECO:0000244|PDB:2I4I}.
HELIX 276 290 {ECO:0000244|PDB:2I4I}.
STRAND 297 300 {ECO:0000244|PDB:2I4I}.
STRAND 302 304 {ECO:0000244|PDB:2I4I}.
HELIX 306 313 {ECO:0000244|PDB:2I4I}.
STRAND 318 322 {ECO:0000244|PDB:2I4I}.
HELIX 324 332 {ECO:0000244|PDB:2I4I}.
STRAND 343 348 {ECO:0000244|PDB:2I4I}.
HELIX 349 354 {ECO:0000244|PDB:2I4I}.
HELIX 358 365 {ECO:0000244|PDB:2I4I}.
STRAND 367 369 {ECO:0000244|PDB:2I4I}.
STRAND 376 383 {ECO:0000244|PDB:2I4I}.
HELIX 387 396 {ECO:0000244|PDB:2I4I}.
STRAND 401 405 {ECO:0000244|PDB:2I4I}.
TURN 411 414 {ECO:0000244|PDB:5E7J}.
STRAND 415 421 {ECO:0000244|PDB:2JGN}.
HELIX 424 426 {ECO:0000244|PDB:2JGN}.
HELIX 427 437 {ECO:0000244|PDB:2JGN}.
STRAND 444 449 {ECO:0000244|PDB:2JGN}.
HELIX 451 463 {ECO:0000244|PDB:2JGN}.
STRAND 468 471 {ECO:0000244|PDB:2JGN}.
STRAND 473 475 {ECO:0000244|PDB:5E7M}.
HELIX 477 480 {ECO:0000244|PDB:2JGN}.
HELIX 482 488 {ECO:0000244|PDB:2JGN}.
STRAND 491 498 {ECO:0000244|PDB:2JGN}.
TURN 499 501 {ECO:0000244|PDB:5E7I}.
TURN 502 504 {ECO:0000244|PDB:2JGN}.
STRAND 509 517 {ECO:0000244|PDB:2JGN}.
HELIX 522 529 {ECO:0000244|PDB:2JGN}.
STRAND 535 537 {ECO:0000244|PDB:5E7I}.
STRAND 539 545 {ECO:0000244|PDB:2JGN}.
HELIX 547 552 {ECO:0000244|PDB:2JGN}.
HELIX 553 562 {ECO:0000244|PDB:2JGN}.
HELIX 569 575 {ECO:0000244|PDB:2JGN}.
HELIX 578 580 {ECO:0000244|PDB:5E7J}.
SEQUENCE 662 AA; 73243 MW; 7074D2B8A6EBBF09 CRC64;
MSHVAVENAL GLDQQFAGLD LNSSDNQSGG STASKGRYIP PHLRNREATK GFYDKDSSGW
SSSKDKDAYS SFGSRSDSRG KSSFFSDRGS GSRGRFDDRG RSDYDGIGSR GDRSGFGKFE
RGGNSRWCDK SDEDDWSKPL PPSERLEQEL FSGGNTGINF EKYDDIPVEA TGNNCPPHIE
SFSDVEMGEI IMGNIELTRY TRPTPVQKHA IPIIKEKRDL MACAQTGSGK TAAFLLPILS
QIYSDGPGEA LRAMKENGRY GRRKQYPISL VLAPTRELAV QIYEEARKFS YRSRVRPCVV
YGGADIGQQI RDLERGCHLL VATPGRLVDM MERGKIGLDF CKYLVLDEAD RMLDMGFEPQ
IRRIVEQDTM PPKGVRHTMM FSATFPKEIQ MLARDFLDEY IFLAVGRVGS TSENITQKVV
WVEESDKRSF LLDLLNATGK DSLTLVFVET KKGADSLEDF LYHEGYACTS IHGDRSQRDR
EEALHQFRSG KSPILVATAV AARGLDISNV KHVINFDLPS DIEEYVHRIG RTGRVGNLGL
ATSFFNERNI NITKDLLDLL VEAKQEVPSW LENMAYEHHY KGSSRGRSKS SRFSGGFGAR
DYRQSSGASS SSFSSSRASS SRSGGGGHGS SRGFGGGGYG GFYNSDGYGG NYNSQGVDWW
GN


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EIAAB10794 ATP-dependent RNA helicase DDX42,DDX42,DEAD box protein 42,Homo sapiens,Human,RHELP,RNA helicase-like protein,RNA helicase-related protein,RNAHP,SF3b DEAD box protein,SF3b125,Splicing factor 3B-associ
EIAAB10806 Ddx5,DEAD box protein 5,DEAD box RNA helicase DEAD1,mDEAD1,Mouse,Mus musculus,Probable ATP-dependent RNA helicase DDX5,RNA helicase p68,Tnz2
EIAAB10817 ATP-dependent RNA helicase DDX54,ATP-dependent RNA helicase DP97,DDX54,DEAD box protein 54,DEAD box RNA helicase 97 kDa,Homo sapiens,Human
EIAAB10785 ATP-dependent RNA helicase DDX3Y,D1Pas1-related sequence 1,D1Pas1-rs1,Ddx3y,DEAD box protein 3, Y-chromosomal,Dead2,DEAD-box RNA helicase DEAD2,mDEAD2,Mouse,Mus musculus
EIAAB10824 ATP-dependent 61 kDa nucleolar RNA helicase,DDX21,DDX56,DEAD box protein 21,DEAD box protein 56,Homo sapiens,Human,NOH61,Probable ATP-dependent RNA helicase DDX56
EIAAB10697 ATP-dependent RNA helicase DDX19B,DBP5,DDX19,DDX19B,DEAD box protein 19B,DEAD box RNA helicase DEAD5,Homo sapiens,Human,TDBP
EIAAB12133 ATP-dependent RNA helicase DDX39A,Ddx39,Ddx39a,Ddxl,DEAD box protein 39,Nuclear RNA helicase, DECD variant of DEAD box family,Rat,Rattus norvegicus
EIAAB10759 DDX17,DEAD box protein 17,DEAD box protein p72,Homo sapiens,Human,Probable ATP-dependent RNA helicase DDX17,RNA-dependent helicase p72
EIAAB10696 ATP-dependent RNA helicase DDX19A,Ddx19,Ddx19a,DEAD box protein 19A,DEAD box RNA helicase DEAD5,Eif4a-rs1,Eukaryotic translation initiation factor 4A-related sequence 1,mDEAD5,Mouse,Mus musculus
18-003-42773 Probable ATP-dependent RNA helicase DDX6 - EC 3.6.1.-; DEAD box protein 6; ATP-dependent RNA helicase p54; Oncogene RCK Polyclonal 0.1 mg Protein A
18-003-42772 Probable ATP-dependent RNA helicase DDX5 - EC 3.6.1.-; DEAD box protein 5; RNA helicase p68 Polyclonal 0.1 mg Protein A
18-003-42771 Probable ATP-dependent RNA helicase DDX5 - EC 3.6.1.-; DEAD box protein 5; RNA helicase p68 Polyclonal 0.1 mg Protein A
18-003-42777 ATP-dependent RNA helicase DDX39 - EC 3.6.1.-; DEAD box protein 39; Nuclear RNA helicase URH49 Polyclonal 0.1 mg Protein A
18-003-42774 Spliceosome RNA helicase BAT1 - EC 3.6.1.-; DEAD box protein UAP56; 56 kDa U2AF65-associated protein; ATP-dependent RNA helicase p47; HLA-B-associated transcript-1 Polyclonal 0.05 mg Aff Pur
EIAAB10784 ATP-dependent RNA helicase DDX3Y,DBY,DDX3Y,DEAD box protein 3, Y-chromosomal,Homo sapiens,Human
EIAAB10832 ATP-dependent RNA helicase p54,Ddx6,DEAD box protein 6,Hlr2,Mouse,Mus musculus,Oncogene RCK homolog,Probable ATP-dependent RNA helicase DDX6,Rck
EIAAB10831 ATP-dependent RNA helicase p54,DDX6,DEAD box protein 6,HLR2,Homo sapiens,Human,Oncogene RCK,Probable ATP-dependent RNA helicase DDX6,RCK
EIAAB10823 ATP-dependent 61 kDa nucleolar RNA helicase,D11Ertd619e,Ddx56,DEAD box protein 56,Mouse,Mus musculus,Noh61,Probable ATP-dependent RNA helicase DDX56
EIAAB10764 Component of gems 3,DDX20,DEAD box protein 20,DEAD box protein DP 103,DP103,GEMIN3,Gemin-3,Homo sapiens,Human,Probable ATP-dependent RNA helicase DDX20
EIAAB10791 ABS,DDX41,DEAD box protein 41,DEAD box protein abstrakt homolog,Homo sapiens,Human,Probable ATP-dependent RNA helicase DDX41
EIAAB10762 ATP-dependent RNA helicase DDX18,DDX18,DEAD box protein 18,Homo sapiens,Human,MrDb,Myc-regulated DEAD box protein
EIAAB10763 Component of gems 3,Ddx20,DEAD box protein 20,DEAD box protein DP 103,Dp103,Gemin3,Gemin-3,Mouse,Mus musculus,Probable ATP-dependent RNA helicase DDX20,Regulator of steroidogenic factor 1,ROSF-1


 

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