O00571 (DDX3X_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 152. History...
Names and origin
|Protein names||Recommended name:|
ATP-dependent RNA helicase DDX3X
DEAD box protein 3, X-chromosomal
DEAD box, X isoform
Helicase-like protein 2
|Organism||Homo sapiens (Human) [Reference proteome]|
|Taxonomic identifier||9606 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo|
|Sequence length||662 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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 IFN-beta induction. Also found associated with IFN-beta 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. Appears to be a prime target for viral manipulations. Hepatitis B virus (HBV) polymerase and possibly vaccinia virus (VACV) protein K7 inhibit IFN-beta 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 INF-beta 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. Ref.2 Ref.9 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.33 Ref.34 Ref.36 Ref.37 Ref.38 Ref.39
ATP + H2O = ADP + phosphate.
Interacts with XPO1, TDRD3, PABPC1, NXF1, EIF3C, MAVS, DDX58 and NCAPH. Interacts with DDX5; the interaction is regulated by the phosphorylation status of both proteins. Interacts with EIF4E; DDX3X competes with EIF4G1/EIF4G3 for interaction with EIF4E. Interacts with IKBKE; the interaction is found to be induced upon virus infection and to be inhibited by HBV polymerase. Interacts with TBK1; the interaction is inhibited by HBV polymerase. Associates with the eukaryotic translation initiation factor 3 (eIF-3) complex. Associates with the 40S ribosome. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with HCV core protein. Interacts with vaccinia virus (VACV) protein K7. Found in a complex with HIV-1 Rev and XPO1. Ref.2 Ref.9 Ref.11 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21 Ref.24 Ref.26 Ref.27 Ref.29 Ref.30 Ref.34 Ref.36 Ref.37 Ref.38 Ref.39
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 G0 phase and in the cytoplasm during G1/S phase. Ref.2 Ref.9 Ref.11 Ref.19 Ref.20 Ref.26 Ref.29 Ref.36 Ref.37
Regulated by the cell cycle. Maximally expressed din the cytoplasm uring G1/S phase and decreased expression during G2/M phase. Ref.37
Phosphorylated by TBK1; the phosphorylation is required to synergize with TBK1 in IFN-beta induction. Probably also phosphorylated by IKBKE. The cytoplasmic form is highly phosphorylated in the G1/S phase and much lower phosphorylated in G2/M. Ref.16 Ref.37
Contains 1 helicase ATP-binding domain.
Contains 1 helicase C-terminal domain.
|This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]|
|Isoform 1 (identifier: O00571-1) |
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
|Isoform 2 (identifier: O00571-2) |
The sequence of this isoform differs from the canonical sequence as follows:
35-51: KGRYIPPHLRNREATKG → S
|Note: No experimental confirmation available.|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed Ref.8|
|Chain||2 – 662||661||ATP-dependent RNA helicase DDX3X||PRO_0000055009|
|Domain||211 – 403||193||Helicase ATP-binding|
|Domain||414 – 575||162||Helicase C-terminal|
|Nucleotide binding||200 – 207||8||ATP|
|Nucleotide binding||224 – 231||8||ATP|
|Region||2 – 139||138||Required for TBK1 and IKBKE-depenedent IFN-beta activation|
|Region||2 – 100||99||Interaction with EIF4E|
|Region||81 – 90||10||Required for interaction with VACV protein K7|
|Region||100 – 662||563||Interaction with GSK3B|
|Region||250 – 259||10||Involved in stimulation of ATPase activity by DNA and RNA, nucleic acid binding and unwinding and HIV-1 replication|
|Region||260 – 517||258||Necessary for interaction with XPO1|
|Motif||180 – 208||29||Q motif|
|Motif||347 – 350||4||DEAD box|
|Compositional bias||582 – 662||81||Gly/Ser-rich|
Amino acid modifications
|Modified residue||2||1||N-acetylserine Ref.8 Ref.31|
|Modified residue||118||1||N6-acetyllysine Ref.25|
|Modified residue||131||1||Phosphoserine Ref.35|
|Modified residue||612||1||Phosphoserine Ref.23|
|Alternative sequence||35 – 51||17||KGRYI…EATKG → S in isoform 2.||VSP_042830|
|Natural variant||294||1||R → T in a breast cancer sample; somatic mutation. Ref.43||VAR_035839|
|Mutagenesis||38||1||Y → A: Impairs interaction with EIF4E. No effect on translation of HIV-1 RNA; when associated with A-43. Ref.21 Ref.39 Ref.42|
|Mutagenesis||43||1||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. Ref.21 Ref.39 Ref.42|
|Mutagenesis||84 – 85||2||FF → AA: Abolishes interaction with VACV protein K7, IRF3 activation and IFN-beta promoter induction. Ref.42|
|Mutagenesis||181||1||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. Ref.16 Ref.42|
|Mutagenesis||183||1||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. Ref.16 Ref.42|
|Mutagenesis||200||1||Y → A: No effect on general translation; when associated with A-207; A-230; A-347 and A-348. Ref.38 Ref.42|
|Mutagenesis||207||1||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. Ref.38 Ref.39 Ref.42|
|Mutagenesis||230||1||K → A: No effect on general translation; when associated with A-200; A-207; A-347 and A-348. Ref.9 Ref.38 Ref.39 Ref.42|
|Mutagenesis||230||1||K → E: Abolishes ATPase activity and RNA-unwinding activity. Inhibits translation of HIV-1 RNA. Ref.9 Ref.38 Ref.39 Ref.42|
|Mutagenesis||240||1||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. Ref.16 Ref.42|
|Mutagenesis||269||1||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. Ref.16 Ref.42|
|Mutagenesis||347||1||D → A: No effect on general translation; when associated with A-200; A-207; A-230 and A-348. Ref.38 Ref.42|
|Mutagenesis||348||1||E → A: No effect on general translation; when associated with A-200; A-207; A-230 and A-347. Ref.38 Ref.39 Ref.42|
|Mutagenesis||348||1||E → Q: Inhibits translation of HIV-1 RNA. Ref.38 Ref.39 Ref.42|
|Mutagenesis||382||1||S → L: Abolishes ATPase activity and RNA-unwinding activity. No effect on translation of HIV-1 RNA. Ref.9 Ref.39 Ref.42|
|Mutagenesis||429||1||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. Ref.16 Ref.42|
|Mutagenesis||438||1||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. Ref.16 Ref.42|
|Mutagenesis||442||1||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. Ref.16 Ref.42|
|Mutagenesis||456||1||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. Ref.16 Ref.42|
|Mutagenesis||520||1||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. Ref.16 Ref.42|
|Sequence conflict||50||1||K → R in AAC51830. Ref.3|
|Sequence conflict||50||1||K → R in AAC51829. Ref.3|
Helix Strand Turn
|Beta strand||168 – 172||5|
|Helix||182 – 184||3|
|Helix||189 – 198||10|
|Helix||205 – 215||11|
|Beta strand||220 – 223||4|
|Helix||230 – 245||16|
|Helix||249 – 256||8|
|Beta strand||268 – 272||5|
|Helix||276 – 290||15|
|Beta strand||297 – 300||4|
|Beta strand||302 – 304||3|
|Helix||306 – 313||8|
|Beta strand||318 – 322||5|
|Helix||324 – 332||9|
|Beta strand||343 – 348||6|
|Helix||349 – 354||6|
|Helix||358 – 365||8|
|Beta strand||367 – 369||3|
|Beta strand||376 – 383||8|
|Helix||387 – 396||10|
|Beta strand||401 – 405||5|
|Beta strand||415 – 421||7|
|Helix||424 – 426||3|
|Helix||427 – 437||11|
|Beta strand||444 – 449||6|
|Helix||451 – 463||13|
|Beta strand||468 – 471||4|
|Helix||482 – 488||7|
|Beta strand||491 – 498||8|
|Helix||499 – 502||4|
|Beta strand||509 – 517||9|
|Helix||522 – 529||8|
|Beta strand||539 – 545||7|
|Helix||547 – 552||6|
|Helix||553 – 562||10|
|Helix||569 – 575||7|
|||"Identification of a human homolog of a putative RNA helicase gene (mDEAD3) expressed in mouse erythroid cells."|
Chung J., Lee S.-G., Song K.
Korean J. Biochem. 27:193-197(1995)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Hippocampus and Liver.
|||"Hepatitis C virus core protein interacts with a human DEAD box protein DDX3."|
Owsianka A.M., Patel A.H.
Virology 257:330-340(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HCV CORE PROTEIN.
|||"Functional coherence of the human Y chromosome."|
Lahn B.T., Page D.C.
Science 278:675-680(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
|||"Complete sequencing and characterization of 21,243 full-length human cDNAs."|
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. Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
|||"The DNA sequence of the human X chromosome."|
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. Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: 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. Venter J.C.|
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
|||"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."|
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
|||"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."|
Yaguee J., Alvarez I., Rognan D., Ramos M., Vazquez J., Lopez de Castro J.A.
J. Exp. Med. 191:2083-2092(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT SER-2.
|||"Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function."|
Yedavalli V.S., Neuveut C., Chi Y.-H., Kleiman L., Jeang K.-T.
Cell 119:381-392(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HIV-1 RNA EXPORT/REPLICATION, IDENTIFICATION IN A COMPLEX WITH XPO1 AND REV, INTERACTION WITH XPO1, MUTAGENESIS OF LYS-230 AND SER-382, SUBCELLULAR LOCATION.
|||"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."|
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.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
|||"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."|
Chao C.H., Chen C.M., Cheng P.L., Shih J.W., Tsou A.P., Lee Y.H.
Cancer Res. 66:6579-6588(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SP1, SUBCELLULAR LOCATION.
|||"DDX3, a DEAD box RNA helicase, is deregulated in hepatitis virus-associated hepatocellular carcinoma and is involved in cell growth control."|
Chang P.C., Chi C.W., Chau G.Y., Li F.Y., Tsai Y.H., Wu J.C., Wu Lee Y.H.
Oncogene 25:1991-2003(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|||"Human DEAD-box ATPase DDX3 shows a relaxed nucleoside substrate specificity."|
Franca R., Belfiore A., Spadari S., Maga G.
Proteins 67:1128-1137(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|||"Protein composition of human mRNPs spliced in vitro and differential requirements for mRNP protein recruitment."|
Merz C., Urlaub H., Will C.L., Luhrmann R.
RNA 13:116-128(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH SPLICED MRNAS.
|||"Identification of an antiapoptotic protein complex at death receptors."|
Sun M., Song L., Li Y., Zhou T., Jope R.S.
Cell Death Differ. 15:1887-1900(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GSK3A; GSK3B AND TNFRSF10B.
|||"The DEAD-box helicase DDX3X is a critical component of the TANK-binding kinase 1-dependent innate immune response."|
Soulat D., Burckstummer T., Westermayer S., Goncalves A., Bauch A., Stefanovic A., Hantschel O., Bennett K.L., Decker T., Superti-Furga G.
EMBO J. 27:2135-2146(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION BY TBK1 AND IKBKE, MUTAGENESIS OF SER-181; SER-183; SER-240; SER-269; SER-429; THR-438; SER-442; SER-456 AND SER-520.
|||"Viral targeting of DEAD box protein 3 reveals its role in TBK1/IKKepsilon-mediated IRF activation."|
Schroder M., Baran M., Bowie A.G.
EMBO J. 27:2147-2157(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VACV PROTEIN K7 AND IKBKE.
|||"TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules."|
Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.
Hum. Mol. Genet. 17:3055-3074(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TDRD3.
|||"The DEAD-box RNA helicase DDX3 associates with export messenger ribonucleoproteins as well as tip-associated protein and participates in translational control."|
Lai M.C., Lee Y.H., Tarn W.Y.
Mol. Biol. Cell 19:3847-3858(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NXF1.
|||"Human DDX3 functions in translation and interacts with the translation initiation factor eIF3."|
Lee C.S., Dias A.P., Jedrychowski M., Patel A.H., Hsu J.L., Reed R.
Nucleic Acids Res. 36:4708-4718(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE EIF-3 COMPLEX.
|||"Candidate tumor suppressor DDX3 RNA helicase specifically represses cap-dependent translation by acting as an eIF4E inhibitory protein."|
Shih J.W., Tsai T.Y., Chao C.H., Wu Lee Y.H.
Oncogene 27:700-714(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EIF4E, MUTAGENESIS OF TYR-38 AND LEU-43.
|||"Oncogenic role of DDX3 in breast cancer biogenesis."|
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.
Oncogene 27:3912-3922(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|||"A quantitative atlas of mitotic phosphorylation."|
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
|||"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."|
Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
|||"Lysine acetylation targets protein complexes and co-regulates major cellular functions."|
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, MASS SPECTROMETRY.
|||"DEAD/H BOX 3 (DDX3) helicase binds the RIG-I adaptor IPS-1 to up-regulate IFN-beta-inducing potential."|
Oshiumi H., Sakai K., Matsumoto M., Seya T.
Eur. J. Immunol. 40:940-948(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAVS AND DDX58, SUBCELLULAR LOCATION.
|||"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."|
Yu S., Chen J., Wu M., Chen H., Kato N., Yuan Z.
J. Gen. Virol. 91:2080-2090(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH IKBKE AND TBK1.
|||"DDX3 regulates cell growth through translational control of cyclin E1."|
Lai M.C., Chang W.C., Shieh S.Y., Tarn W.Y.
Mol. Cell. Biol. 30:5444-5453(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|||"Hepatitis C virus core protein abrogates the DDX3 function that enhances IPS-1-mediated IFN-beta induction."|
Oshiumi H., Ikeda M., Matsumoto M., Watanabe A., Takeuchi O., Akira S., Kato N., Shimotohno K., Seya T.
PLoS ONE 5:E14258-E14258(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING, INTERACTION WITH MAVS, SUBCELLULAR LOCATION.
|||"Hepatitis B virus polymerase blocks pattern recognition receptor signaling via interaction with DDX3: implications for immune evasion."|
Wang H., Ryu W.S.
PLoS Pathog. 6:E1000986-E1000986(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH IKBKE.
|||"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."|
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
|||"Initial characterization of the human central proteome."|
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
|||"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."|
Garbelli A., Beermann S., Di Cicco G., Dietrich U., Maga G.
PLoS ONE 6:E19810-E19810(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|||"DEAD-box RNA helicase Belle/DDX3 and the RNA interference pathway promote mitotic chromosome segregation."|
Pek J.W., Kai T.
Proc. Natl. Acad. Sci. U.S.A. 108:12007-12012(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NCAPH.
|||"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."|
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, MASS SPECTROMETRY.
|||"Critical roles of RNA helicase DDX3 and its interactions with eIF4E/PABP1 in stress granule assembly and stress response."|
Shih J.W., Wang W.T., Tsai T.Y., Kuo C.Y., Li H.K., Wu Lee Y.H.
Biochem. J. 441:119-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF4E AND PABPC1.
|||"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."|
Choi Y.J., Lee S.G.
J. Cell. Biochem. 113:985-996(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INDUCTION, INTERACTION WITH DDX5.
|||"The DEAD-box helicase DDX3 supports the assembly of functional 80S ribosomes."|
Geissler R., Golbik R.P., Behrens S.E.
Nucleic Acids Res. 40:4998-5011(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH THE RIBOSOME SMALL SUBUNIT, INTERACTION WITH EIF3C, MUTAGENESIS OF TYR-200; GLN-207; LYS-230; ASP-347 AND GLU-348.
|||"DEAD-box protein DDX3 associates with eIF4F to promote translation of selected mRNAs."|
Soto-Rifo R., Rubilar P.S., Limousin T., de Breyne S., Decimo D., Ohlmann T.
EMBO J. 31:3745-3756(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING, INTERACTION WITH EIF4G1 AND PABPC1, MUTAGENESIS OF TYR-38; LEU-43; GLN-207; LYS-230; GLU-348 AND SER-382.
|||"Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain."|
Rodamilans B., Montoya G.
Acta Crystallogr. F 63:283-286(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 409-580.
|||"Crystal structure of conserved domains 1 and 2 of the human DEAD-box helicase DDX3X in complex with the mononucleotide AMP."|
Hoegbom M., Collins R., van den Berg S., Jenvert R.-M., Karlberg T., Kotenyova T., Flores A., Karlsson Hedestam G.B., Schiavone L.H.
J. Mol. Biol. 372:150-159(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 168-582 IN COMPLEX WITH AMP.
|||"Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7."|
Oda S., Schroder M., Khan A.R.
Structure 17:1528-1537(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 71-90 IN COMPLEX WITH VACV PROTEIN K7, MUTAGENESIS OF 84-PHE-PHE-85.
|||"The consensus coding sequences of human breast and colorectal cancers."|
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. Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-294.
|+||Additional computationally mapped references.|
|U50553 mRNA. Translation: AAB95637.1.|
AF061337 mRNA. Translation: AAC34298.1.
AF000983 mRNA. Translation: AAC51830.1.
AF000982 mRNA. Translation: AAC51829.1.
AK291153 mRNA. Translation: BAF83842.1.
AK304689 mRNA. Translation: BAG65460.1.
AL391647 Genomic DNA. Translation: CAI41416.1.
Z93015 Genomic DNA. No translation available.
CH471141 Genomic DNA. Translation: EAW59402.1.
CH471141 Genomic DNA. Translation: EAW59403.1.
CH471141 Genomic DNA. Translation: EAW59404.1.
CH471141 Genomic DNA. Translation: EAW59405.1.
BC011819 mRNA. Translation: AAH11819.1.
|RefSeq||NP_001180346.1. NM_001193417.1. |
3D structure databases
Protein-protein interaction databases
|IntAct||O00571. 57 interactions.|
2D gel databases
Protocols and materials databases
Genome annotation databases
|Ensembl||ENST00000399959; ENSP00000382840; ENSG00000215301. |
ENST00000457138; ENSP00000392494; ENSG00000215301.
|UCSC||uc004dfe.3. human. |
|HGNC||HGNC:2745. DDX3X. |
|MIM||300160. gene. |
Gene expression databases
|GermOnline||ENSG00000124487. Homo sapiens. |
Family and domain databases
|InterPro||IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. |
|Pfam||PF00270. DEAD. 1 hit. |
PF00271. Helicase_C. 1 hit.
|SMART||SM00487. DEXDc. 1 hit. |
SM00490. HELICc. 1 hit.
|PROSITE||PS00039. DEAD_ATP_HELICASE. 1 hit. |
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
|ChiTaRS||DDX3X. human. |
|Accession||Primary (citable) accession number: O00571|
Secondary accession number(s): A8K538, B4E3E8, O15536
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
|Disclaimer||Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.|
|Human chromosome X|
Human chromosome X: entries, gene names and cross-references to MIM
|Human entries with polymorphisms or disease mutations|
List of human entries with polymorphisms or disease mutations
|Human polymorphisms and disease mutations|
Index of human polymorphisms and disease mutations
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Index of Protein Data Bank (PDB) cross-references
Index of protein domains and families