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O00571

- DDX3X_HUMAN

UniProt

O00571 - DDX3X_HUMAN

Protein

ATP-dependent RNA helicase DDX3X

Gene

DDX3X

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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. 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.24 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi200 – 2078ATP
    Nucleotide bindingi224 – 2318ATP

    GO - Molecular functioni

    1. ATPase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. ATP-dependent DNA helicase activity Source: UniProtKB
    4. ATP-dependent RNA helicase activity Source: UniProtKB
    5. DNA binding Source: UniProtKB
    6. eukaryotic initiation factor 4E binding Source: UniProtKB
    7. mRNA 5'-UTR binding Source: UniProtKB
    8. poly(A) binding Source: UniProtKB
    9. poly(A) RNA binding Source: UniProtKB
    10. protein binding Source: IntAct
    11. ribosomal small subunit binding Source: UniProtKB
    12. RNA binding Source: UniProtKB
    13. RNA stem-loop binding Source: UniProtKB
    14. transcription factor binding Source: UniProtKB
    15. translation initiation factor binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular response to arsenic-containing substance Source: UniProtKB
    3. cellular response to osmotic stress Source: UniProtKB
    4. chromosome segregation Source: UniProtKB
    5. DNA duplex unwinding Source: GOC
    6. extrinsic apoptotic signaling pathway via death domain receptors Source: UniProtKB
    7. innate immune response Source: UniProtKB
    8. intracellular signal transduction Source: UniProtKB
    9. intrinsic apoptotic signaling pathway Source: UniProtKB
    10. mature ribosome assembly Source: UniProtKB
    11. negative regulation of apoptotic process Source: UniProtKB
    12. negative regulation of cell growth Source: UniProtKB
    13. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    14. negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
    15. negative regulation of protein complex assembly Source: UniProtKB
    16. negative regulation of translation Source: UniProtKB
    17. positive regulation of apoptotic process Source: UniProtKB
    18. positive regulation of cell growth Source: UniProtKB
    19. positive regulation of chemokine (C-C motif) ligand 5 production Source: UniProtKB
    20. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    21. positive regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
    22. positive regulation of interferon-beta production Source: UniProtKB
    23. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    24. positive regulation of translation Source: UniProtKB
    25. positive regulation of translational initiation Source: UniProtKB
    26. response to virus Source: UniProtKB
    27. RNA secondary structure unwinding Source: UniProtKB
    28. stress granule assembly Source: UniProtKB
    29. transcription, DNA-templated Source: UniProtKB-KW
    30. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Apoptosis, Chromosome partition, Host-virus interaction, Immunity, Innate immunity, Ribosome biogenesis, Transcription, Transcription regulation, Translation regulation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent RNA helicase DDX3X (EC:3.6.4.13)
    Alternative name(s):
    DEAD box protein 3, X-chromosomal
    DEAD box, X isoform
    Helicase-like protein 2
    Short name:
    HLP2
    Gene namesi
    Name:DDX3X
    Synonyms:DBX, DDX3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:2745. DDX3X.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic stress granule Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. mitochondrial outer membrane Source: UniProtKB-SubCell
    5. nuclear speck Source: UniProtKB-SubCell
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381Y → A: Impairs interaction with EIF4E. No effect on translation of HIV-1 RNA; when associated with A-43. 3 Publications
    Mutagenesisi43 – 431L → 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. 3 Publications
    Mutagenesisi71 – 711S → A: Reduces total phosphorylation by 60%. No effect on interaction with IKBKE. 2 Publications
    Mutagenesisi82 – 832SS → AA: Reduces total phosphorylation by 50%. No effect on interaction with IKBKE. 1 Publication
    Mutagenesisi84 – 852FF → AA: Abolishes interaction with VACV protein K7, IRF3 activation and IFN-beta promoter induction. 1 Publication
    Mutagenesisi102 – 1021S → A: Reduces total phosphorylation by 30%. Abolishes interaction with IRF3 and fails to enhance IFNB promoter induction. No effect on interaction with IKBKE. 2 Publications
    Mutagenesisi102 – 1021S → D: Interacts with IRF3 and enhances IFNB promoter induction. 2 Publications
    Mutagenesisi152 – 1521S → A: Reduces total phosphorylation by 60%. No effect on interaction with IKBKE. 2 Publications
    Mutagenesisi181 – 1811S → 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. 2 Publications
    Mutagenesisi183 – 1831S → 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. 2 Publications
    Mutagenesisi200 – 2001Y → A: No effect on general translation; when associated with A-207; A-230; A-347 and A-348. 2 Publications
    Mutagenesisi207 – 2071Q → A: Inhibits translation of HIV-1 RNA. No effect on general translation; when associated with A-200; A-230: A-347 and A-348. 3 Publications
    Mutagenesisi230 – 2301K → A: No effect on general translation; when associated with A-200; A-207; A-347 and A-348. 4 Publications
    Mutagenesisi230 – 2301K → E: Abolishes ATPase activity and RNA-unwinding activity. Inhibits translation of HIV-1 RNA. 4 Publications
    Mutagenesisi240 – 2401S → 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. 2 Publications
    Mutagenesisi269 – 2691S → 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. 2 Publications
    Mutagenesisi347 – 3471D → A: No effect on general translation; when associated with A-200; A-207; A-230 and A-348. 2 Publications
    Mutagenesisi348 – 3481E → A: No effect on general translation; when associated with A-200; A-207; A-230 and A-347. 3 Publications
    Mutagenesisi348 – 3481E → Q: Inhibits translation of HIV-1 RNA. 3 Publications
    Mutagenesisi382 – 3821S → L: Abolishes ATPase activity and RNA-unwinding activity. No effect on translation of HIV-1 RNA. 3 Publications
    Mutagenesisi429 – 4291S → 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. 2 Publications
    Mutagenesisi438 – 4381T → 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. 2 Publications
    Mutagenesisi442 – 4421S → 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. 2 Publications
    Mutagenesisi456 – 4561S → 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. 2 Publications
    Mutagenesisi520 – 5201S → 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. 2 Publications

    Organism-specific databases

    Orphaneti99861. Precursor T-cell acute lymphoblastic leukemia.
    PharmGKBiPA27216.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 662661ATP-dependent RNA helicase DDX3XPRO_0000055009Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei55 – 551N6-acetyllysineBy similarity
    Modified residuei69 – 691Phosphotyrosine
    Modified residuei74 – 741Phosphoserine
    Modified residuei76 – 761Phosphoserine
    Modified residuei78 – 781Phosphoserine
    Modified residuei102 – 1021Phosphoserine; by IKKE1 Publication
    Modified residuei104 – 1041Phosphotyrosine
    Modified residuei118 – 1181N6-acetyllysine1 Publication
    Modified residuei125 – 1251Phosphoserine
    Modified residuei131 – 1311Phosphoserine1 Publication
    Modified residuei343 – 3431Phosphotyrosine
    Modified residuei590 – 5901Phosphoserine
    Modified residuei594 – 5941Phosphoserine
    Modified residuei612 – 6121Phosphoserine1 Publication

    Post-translational modificationi

    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.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00571.
    PaxDbiO00571.
    PeptideAtlasiO00571.
    PRIDEiO00571.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00215637.
    SWISS-2DPAGEO00571.

    PTM databases

    PhosphoSiteiO00571.

    Expressioni

    Inductioni

    Regulated by the cell cycle. Maximally expressed din the cytoplasm uring G1/S phase and decreased expression during G2/M phase.1 Publication

    Gene expression databases

    ArrayExpressiO00571.
    BgeeiO00571.
    CleanExiHS_DDX3X.
    GenevestigatoriO00571.

    Organism-specific databases

    HPAiHPA001648.
    HPA005631.

    Interactioni

    Subunit structurei

    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 direct, found to be induced upon virus infection. Interacts (when phosphorylated at Ser-102) with IRF3; the interaction allows the phosphorylation and activation of IRF3 by IKBKE. Interacts with TBK1. 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. Interacts (when phosphorylated at Ser-102) with IRF3; the interaction allows the phosphorylation and activation of IRF3 by IKBKE.21 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P266643EBI-353779,EBI-9209740From a different organism.
    P279584EBI-353779,EBI-6377335From a different organism.
    Q99IB89EBI-353779,EBI-6674379From a different organism.
    DDX58O957862EBI-353779,EBI-995350
    EIF2S1P051983EBI-353779,EBI-1056162
    EIF3BP558845EBI-353779,EBI-366696
    EIF3CQ996133EBI-353779,EBI-353741
    EIF4G1Q046373EBI-353779,EBI-73711
    IKBKEQ141644EBI-353779,EBI-307369
    K7RP684676EBI-353779,EBI-8022707From a different organism.
    MAVSQ7Z4344EBI-353779,EBI-995373
    NCAPHQ150032EBI-353779,EBI-1046410
    NXF1Q9UBU95EBI-353779,EBI-398874
    PABPC1P1194010EBI-353779,EBI-81531

    Protein-protein interaction databases

    BioGridi108020. 123 interactions.
    DIPiDIP-27551N.
    IntActiO00571. 88 interactions.
    MINTiMINT-8395017.
    STRINGi9606.ENSP00000382840.

    Structurei

    Secondary structure

    1
    662
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi168 – 1725
    Helixi182 – 1843
    Helixi189 – 19810
    Helixi205 – 21511
    Beta strandi220 – 2234
    Helixi230 – 24516
    Helixi249 – 2568
    Beta strandi268 – 2725
    Helixi276 – 29015
    Beta strandi297 – 3004
    Beta strandi302 – 3043
    Helixi306 – 3138
    Beta strandi318 – 3225
    Helixi324 – 3329
    Beta strandi343 – 3486
    Helixi349 – 3546
    Helixi358 – 3658
    Beta strandi367 – 3693
    Beta strandi376 – 3838
    Helixi387 – 39610
    Beta strandi401 – 4055
    Beta strandi415 – 4217
    Helixi424 – 4263
    Helixi427 – 43711
    Beta strandi444 – 4496
    Helixi451 – 46313
    Beta strandi468 – 4714
    Helixi482 – 4887
    Beta strandi491 – 4988
    Helixi499 – 5024
    Beta strandi509 – 5179
    Helixi522 – 5298
    Beta strandi539 – 5457
    Helixi547 – 5526
    Helixi553 – 56210
    Helixi569 – 5757

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I4IX-ray2.20A168-582[»]
    2JGNX-ray1.91A/B/C409-580[»]
    3JRVX-ray1.60C/D/E71-90[»]
    ProteinModelPortaliO00571.
    SMRiO00571. Positions 139-580.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00571.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini211 – 403193Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini414 – 575162Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 139138Required for TBK1 and IKBKE-dependent IFN-beta activationAdd
    BLAST
    Regioni2 – 10099Interaction with EIF4EAdd
    BLAST
    Regioni81 – 9010Required for interaction with VACV protein K7
    Regioni100 – 662563Interaction with GSK3BAdd
    BLAST
    Regioni100 – 11011Required for interaction with IKBKEAdd
    BLAST
    Regioni250 – 25910Involved in stimulation of ATPase activity by DNA and RNA, nucleic acid binding and unwinding and HIV-1 replication
    Regioni260 – 517258Necessary for interaction with XPO1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi180 – 20829Q motifAdd
    BLAST
    Motifi347 – 3504DEAD box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi582 – 66281Gly/Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0513.
    HOVERGENiHBG015893.
    InParanoidiO00571.
    KOiK11594.
    OMAiSFGSRND.
    OrthoDBiEOG7B5WV8.
    PhylomeDBiO00571.
    TreeFamiTF300364.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00571-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSHVAVENAL GLDQQFAGLD LNSSDNQSGG STASKGRYIP PHLRNREATK    50
    GFYDKDSSGW SSSKDKDAYS SFGSRSDSRG KSSFFSDRGS GSRGRFDDRG 100
    RSDYDGIGSR GDRSGFGKFE RGGNSRWCDK SDEDDWSKPL PPSERLEQEL 150
    FSGGNTGINF EKYDDIPVEA TGNNCPPHIE SFSDVEMGEI IMGNIELTRY 200
    TRPTPVQKHA IPIIKEKRDL MACAQTGSGK TAAFLLPILS QIYSDGPGEA 250
    LRAMKENGRY GRRKQYPISL VLAPTRELAV QIYEEARKFS YRSRVRPCVV 300
    YGGADIGQQI RDLERGCHLL VATPGRLVDM MERGKIGLDF CKYLVLDEAD 350
    RMLDMGFEPQ IRRIVEQDTM PPKGVRHTMM FSATFPKEIQ MLARDFLDEY 400
    IFLAVGRVGS TSENITQKVV WVEESDKRSF LLDLLNATGK DSLTLVFVET 450
    KKGADSLEDF LYHEGYACTS IHGDRSQRDR EEALHQFRSG KSPILVATAV 500
    AARGLDISNV KHVINFDLPS DIEEYVHRIG RTGRVGNLGL ATSFFNERNI 550
    NITKDLLDLL VEAKQEVPSW LENMAYEHHY KGSSRGRSKS SRFSGGFGAR 600
    DYRQSSGASS SSFSSSRASS SRSGGGGHGS SRGFGGGGYG GFYNSDGYGG 650
    NYNSQGVDWW GN 662
    Length:662
    Mass (Da):73,243
    Last modified:January 23, 2007 - v3
    Checksum:i7074D2B8A6EBBF09
    GO
    Isoform 2 (identifier: O00571-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         35-51: KGRYIPPHLRNREATKG → S

    Note: No experimental confirmation available.

    Show »
    Length:646
    Mass (Da):71,355
    Checksum:iA8E9EB966FC6C617
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501K → R in AAC51830. (PubMed:9381176)Curated
    Sequence conflicti50 – 501K → R in AAC51829. (PubMed:9381176)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti294 – 2941R → T in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035839

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei35 – 5117KGRYI…EATKG → S in isoform 2. 1 PublicationVSP_042830Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS43931.1. [O00571-1]
    CCDS55404.1. [O00571-2]
    RefSeqiNP_001180346.1. NM_001193417.1. [O00571-2]
    NP_001347.3. NM_001356.3. [O00571-1]
    UniGeneiHs.743263.

    Genome annotation databases

    EnsembliENST00000399959; ENSP00000382840; ENSG00000215301. [O00571-1]
    ENST00000457138; ENSP00000392494; ENSG00000215301. [O00571-2]
    GeneIDi1654.
    KEGGihsa:1654.
    UCSCiuc004dfe.3. human. [O00571-1]
    uc010nhf.1. human. [O00571-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS43931.1. [O00571-1 ]
    CCDS55404.1. [O00571-2 ]
    RefSeqi NP_001180346.1. NM_001193417.1. [O00571-2 ]
    NP_001347.3. NM_001356.3. [O00571-1 ]
    UniGenei Hs.743263.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I4I X-ray 2.20 A 168-582 [» ]
    2JGN X-ray 1.91 A/B/C 409-580 [» ]
    3JRV X-ray 1.60 C/D/E 71-90 [» ]
    ProteinModelPortali O00571.
    SMRi O00571. Positions 139-580.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108020. 123 interactions.
    DIPi DIP-27551N.
    IntActi O00571. 88 interactions.
    MINTi MINT-8395017.
    STRINGi 9606.ENSP00000382840.

    Chemistry

    BindingDBi O00571.
    ChEMBLi CHEMBL5553.

    PTM databases

    PhosphoSitei O00571.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00215637.
    SWISS-2DPAGE O00571.

    Proteomic databases

    MaxQBi O00571.
    PaxDbi O00571.
    PeptideAtlasi O00571.
    PRIDEi O00571.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000399959 ; ENSP00000382840 ; ENSG00000215301 . [O00571-1 ]
    ENST00000457138 ; ENSP00000392494 ; ENSG00000215301 . [O00571-2 ]
    GeneIDi 1654.
    KEGGi hsa:1654.
    UCSCi uc004dfe.3. human. [O00571-1 ]
    uc010nhf.1. human. [O00571-2 ]

    Organism-specific databases

    CTDi 1654.
    GeneCardsi GC0XP041192.
    HGNCi HGNC:2745. DDX3X.
    HPAi HPA001648.
    HPA005631.
    MIMi 300160. gene.
    neXtProti NX_O00571.
    Orphaneti 99861. Precursor T-cell acute lymphoblastic leukemia.
    PharmGKBi PA27216.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0513.
    HOVERGENi HBG015893.
    InParanoidi O00571.
    KOi K11594.
    OMAi SFGSRND.
    OrthoDBi EOG7B5WV8.
    PhylomeDBi O00571.
    TreeFami TF300364.

    Miscellaneous databases

    ChiTaRSi DDX3X. human.
    EvolutionaryTracei O00571.
    GeneWikii DDX3X.
    GenomeRNAii 1654.
    NextBioi 6810.
    PROi O00571.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00571.
    Bgeei O00571.
    CleanExi HS_DDX3X.
    Genevestigatori O00571.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000629. RNA-helicase_DEAD-box_CS.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00039. DEAD_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51195. Q_MOTIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. "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.
      Tissue: Liver.
    3. "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).
    4. "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.
      , 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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Uterus.
    5. "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.
      , 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.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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).
      Tissue: Skin.
    8. "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.
    9. "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.
    10. "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].
    11. "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.
    12. "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.
    13. "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.
    14. "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.
    15. "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.
    16. "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.
    17. "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.
    18. "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.
    19. "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.
    20. "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.
    21. "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.
    22. Cited for: FUNCTION.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "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.
    25. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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.
    27. "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.
    28. "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.
    29. "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.
    30. "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.
    31. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "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.
    34. "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.
    35. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "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.
    37. "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.
    38. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. "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.
    40. "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.
    41. "Human DEAD box helicase 3 couples IkappaB kinase epsilon to interferon regulatory factor 3 activation."
      Gu L., Fullam A., Brennan R., Schroder M.
      Mol. Cell. Biol. 33:2004-2015(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS SCAFFOLD PROTEIN, INTERACTION WITH IKBKE AND IRF3, PHOSPHORYLATION AT SER-102, MUTAGENESIS OF SER-71; 82-SER-SER-83; SER-102 AND SER-152.
    42. "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.
    43. "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.
    44. "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.
    45. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-294.

    Entry informationi

    Entry nameiDDX3X_HUMAN
    AccessioniPrimary (citable) accession number: O00571
    Secondary accession number(s): A8K538, B4E3E8, O15536
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 168 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3