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O00571 (DDX3X_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DDX3X
Synonyms:DBX, DDX3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length662 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. 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.39 Ref.40 Ref.41

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. 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.39 Ref.40 Ref.41

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 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

Induction

Regulated by the cell cycle. Maximally expressed din the cytoplasm uring G1/S phase and decreased expression during G2/M phase. Ref.37

Post-translational modification

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. Ref.16 Ref.37 Ref.41

Sequence similarities

Belongs to the DEAD box helicase family. DDX3/DED1 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Biological processApoptosis
Chromosome partition
Host-virus interaction
Immunity
Innate immunity
Ribosome biogenesis
Transcription
Transcription regulation
Translation regulation
   Cellular componentCytoplasm
Membrane
Mitochondrion
Mitochondrion outer membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
DNA-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.33. Source: GOC

DNA duplex unwinding

Inferred from direct assay Ref.33. Source: GOC

RNA secondary structure unwinding

Inferred from direct assay Ref.40. Source: UniProtKB

cellular response to arsenic-containing substance

Inferred from direct assay Ref.36. Source: UniProtKB

cellular response to osmotic stress

Inferred from direct assay Ref.36. Source: UniProtKB

chromosome segregation

Inferred from mutant phenotype Ref.34. Source: UniProtKB

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from mutant phenotype Ref.15. Source: UniProtKB

innate immune response

Inferred from mutant phenotype Ref.16. Source: UniProtKB

intracellular signal transduction

Inferred from direct assay Ref.17. Source: UniProtKB

intrinsic apoptotic signaling pathway

Inferred from mutant phenotype Ref.12. Source: UniProtKB

mature ribosome assembly

Inferred from mutant phenotype Ref.39. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.15. Source: UniProtKB

negative regulation of cell growth

Inferred from direct assay Ref.11. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype Ref.15. Source: UniProtKB

negative regulation of intrinsic apoptotic signaling pathway

Inferred from mutant phenotype Ref.36. Source: UniProtKB

negative regulation of protein complex assembly

Inferred from direct assay Ref.21. Source: UniProtKB

negative regulation of translation

Inferred from mutant phenotype Ref.21. Source: UniProtKB

positive regulation of G1/S transition of mitotic cell cycle

Inferred from mutant phenotype Ref.28. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype Ref.12. Source: UniProtKB

positive regulation of cell growth

Inferred from mutant phenotype Ref.20Ref.28. Source: UniProtKB

positive regulation of chemokine (C-C motif) ligand 5 production

Traceable author statement Ref.16. Source: UniProtKB

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype Ref.12. Source: UniProtKB

positive regulation of interferon-beta production

Traceable author statement Ref.16Ref.17. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.11Ref.17. Source: UniProtKB

positive regulation of translation

Inferred from direct assay Ref.19Ref.40. Source: UniProtKB

positive regulation of translational initiation

Inferred from mutant phenotype Ref.28. Source: UniProtKB

response to virus

Inferred from direct assay Ref.17. Source: UniProtKB

stress granule assembly

Inferred from direct assay Ref.36. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.2. Source: UniProtKB

cytoplasmic stress granule

Inferred from direct assay Ref.19Ref.36. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337. Source: UniProt

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Inferred from direct assay Ref.33. Source: UniProtKB

ATP-dependent RNA helicase activity

Inferred from direct assay Ref.33. Source: UniProtKB

ATPase activity

Inferred from direct assay Ref.33. Source: UniProtKB

DNA binding

Inferred from direct assay Ref.33. Source: UniProtKB

RNA binding

Inferred from direct assay Ref.33. Source: UniProtKB

RNA stem-loop binding

Inferred from direct assay Ref.40. Source: UniProtKB

eukaryotic initiation factor 4E binding

Inferred from direct assay Ref.21. Source: UniProtKB

mRNA 5'-UTR binding

Inferred from direct assay Ref.40. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

poly(A) binding

Inferred from direct assay Ref.19. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10336476Ref.19Ref.20Ref.17Ref.26Ref.30Ref.34Ref.36Ref.39PubMed 22616990Ref.40. Source: IntAct

ribosomal small subunit binding

Inferred from direct assay Ref.39. Source: UniProtKB

transcription factor binding

Inferred from direct assay Ref.11. Source: UniProtKB

translation initiation factor binding

Inferred from direct assay Ref.39Ref.40. Source: UniProtKB

Complete GO annotation...

Alternative products

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 662661ATP-dependent RNA helicase DDX3X
PRO_0000055009

Regions

Domain211 – 403193Helicase ATP-binding
Domain414 – 575162Helicase C-terminal
Nucleotide binding200 – 2078ATP
Nucleotide binding224 – 2318ATP
Region2 – 139138Required for TBK1 and IKBKE-dependent IFN-beta activation
Region2 – 10099Interaction with EIF4E
Region81 – 9010Required for interaction with VACV protein K7
Region100 – 662563Interaction with GSK3B
Region100 – 11011Required for interaction with IKBKE
Region250 – 25910Involved in stimulation of ATPase activity by DNA and RNA, nucleic acid binding and unwinding and HIV-1 replication
Region260 – 517258Necessary for interaction with XPO1
Motif180 – 20829Q motif
Motif347 – 3504DEAD box
Compositional bias582 – 66281Gly/Ser-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.8 Ref.31 Ref.38
Modified residue551N6-acetyllysine By similarity
Modified residue691Phosphotyrosine
Modified residue741Phosphoserine
Modified residue761Phosphoserine
Modified residue781Phosphoserine
Modified residue1021Phosphoserine; by IKKE Ref.41
Modified residue1041Phosphotyrosine
Modified residue1181N6-acetyllysine Ref.25
Modified residue1251Phosphoserine
Modified residue1311Phosphoserine Ref.35
Modified residue3431Phosphotyrosine
Modified residue5901Phosphoserine
Modified residue5941Phosphoserine
Modified residue6121Phosphoserine Ref.23

Natural variations

Alternative sequence35 – 5117KGRYI…EATKG → S in isoform 2.
VSP_042830
Natural variant2941R → T in a breast cancer sample; somatic mutation. Ref.45
VAR_035839

Experimental info

Mutagenesis381Y → A: Impairs interaction with EIF4E. No effect on translation of HIV-1 RNA; when associated with A-43. Ref.21 Ref.40 Ref.44
Mutagenesis431L → 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.40 Ref.44
Mutagenesis711S → A: Reduces total phosphorylation by 60%. No effect on interaction with IKBKE. Ref.41 Ref.44
Mutagenesis82 – 832SS → AA: Reduces total phosphorylation by 50%. No effect on interaction with IKBKE. Ref.44
Mutagenesis84 – 852FF → AA: Abolishes interaction with VACV protein K7, IRF3 activation and IFN-beta promoter induction. Ref.44
Mutagenesis1021S → A: Reduces total phosphorylation by 30%. Abolishes interaction with IRF3 and fails to enhance IFNB promoter induction. No effect on interaction with IKBKE. Ref.41 Ref.44
Mutagenesis1021S → D: Interacts with IRF3 and enhances IFNB promoter induction. Ref.41 Ref.44
Mutagenesis1521S → A: Reduces total phosphorylation by 60%. No effect on interaction with IKBKE. Ref.41 Ref.44
Mutagenesis1811S → 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.44
Mutagenesis1831S → 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.44
Mutagenesis2001Y → A: No effect on general translation; when associated with A-207; A-230; A-347 and A-348. Ref.39 Ref.44
Mutagenesis2071Q → 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.39 Ref.40 Ref.44
Mutagenesis2301K → A: No effect on general translation; when associated with A-200; A-207; A-347 and A-348. Ref.9 Ref.39 Ref.40 Ref.44
Mutagenesis2301K → E: Abolishes ATPase activity and RNA-unwinding activity. Inhibits translation of HIV-1 RNA. Ref.9 Ref.39 Ref.40 Ref.44
Mutagenesis2401S → 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.44
Mutagenesis2691S → 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.44
Mutagenesis3471D → A: No effect on general translation; when associated with A-200; A-207; A-230 and A-348. Ref.39 Ref.44
Mutagenesis3481E → A: No effect on general translation; when associated with A-200; A-207; A-230 and A-347. Ref.39 Ref.40 Ref.44
Mutagenesis3481E → Q: Inhibits translation of HIV-1 RNA. Ref.39 Ref.40 Ref.44
Mutagenesis3821S → L: Abolishes ATPase activity and RNA-unwinding activity. No effect on translation of HIV-1 RNA. Ref.9 Ref.40 Ref.44
Mutagenesis4291S → 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.44
Mutagenesis4381T → 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.44
Mutagenesis4421S → 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.44
Mutagenesis4561S → 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.44
Mutagenesis5201S → 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.44
Sequence conflict501K → R in AAC51830. Ref.3
Sequence conflict501K → R in AAC51829. Ref.3

Secondary structure

..................................................................... 662
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7074D2B8A6EBBF09

FASTA66273,243
        10         20         30         40         50         60 
MSHVAVENAL GLDQQFAGLD LNSSDNQSGG STASKGRYIP PHLRNREATK GFYDKDSSGW 

        70         80         90        100        110        120 
SSSKDKDAYS SFGSRSDSRG KSSFFSDRGS GSRGRFDDRG RSDYDGIGSR GDRSGFGKFE 

       130        140        150        160        170        180 
RGGNSRWCDK SDEDDWSKPL PPSERLEQEL FSGGNTGINF EKYDDIPVEA TGNNCPPHIE 

       190        200        210        220        230        240 
SFSDVEMGEI IMGNIELTRY TRPTPVQKHA IPIIKEKRDL MACAQTGSGK TAAFLLPILS 

       250        260        270        280        290        300 
QIYSDGPGEA LRAMKENGRY GRRKQYPISL VLAPTRELAV QIYEEARKFS YRSRVRPCVV 

       310        320        330        340        350        360 
YGGADIGQQI RDLERGCHLL VATPGRLVDM MERGKIGLDF CKYLVLDEAD RMLDMGFEPQ 

       370        380        390        400        410        420 
IRRIVEQDTM PPKGVRHTMM FSATFPKEIQ MLARDFLDEY IFLAVGRVGS TSENITQKVV 

       430        440        450        460        470        480 
WVEESDKRSF LLDLLNATGK DSLTLVFVET KKGADSLEDF LYHEGYACTS IHGDRSQRDR 

       490        500        510        520        530        540 
EEALHQFRSG KSPILVATAV AARGLDISNV KHVINFDLPS DIEEYVHRIG RTGRVGNLGL 

       550        560        570        580        590        600 
ATSFFNERNI NITKDLLDLL VEAKQEVPSW LENMAYEHHY KGSSRGRSKS SRFSGGFGAR 

       610        620        630        640        650        660 
DYRQSSGASS SSFSSSRASS SRSGGGGHGS SRGFGGGGYG GFYNSDGYGG NYNSQGVDWW 


GN 

« Hide

Isoform 2 [UniParc].

Checksum: A8E9EB966FC6C617
Show »

FASTA64671,355

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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. expand/collapse author list , 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
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]"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.
[23]"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, 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]"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].
[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]"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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-294.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS43931.1. [O00571-1]
CCDS55404.1. [O00571-2]
RefSeqNP_001180346.1. NM_001193417.1. [O00571-2]
NP_001347.3. NM_001356.3. [O00571-1]
UniGeneHs.743263.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I4IX-ray2.20A168-582[»]
2JGNX-ray1.91A/B/C409-580[»]
3JRVX-ray1.60C/D/E71-90[»]
ProteinModelPortalO00571.
SMRO00571. Positions 139-580.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108020. 126 interactions.
DIPDIP-27551N.
IntActO00571. 86 interactions.
MINTMINT-8395017.
STRING9606.ENSP00000382840.

Chemistry

BindingDBO00571.
ChEMBLCHEMBL5553.

PTM databases

PhosphoSiteO00571.

2D gel databases

REPRODUCTION-2DPAGEIPI00215637.
SWISS-2DPAGEO00571.

Proteomic databases

MaxQBO00571.
PaxDbO00571.
PeptideAtlasO00571.
PRIDEO00571.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000399959; ENSP00000382840; ENSG00000215301. [O00571-1]
ENST00000457138; ENSP00000392494; ENSG00000215301. [O00571-2]
GeneID1654.
KEGGhsa:1654.
UCSCuc004dfe.3. human. [O00571-1]
uc010nhf.1. human. [O00571-2]

Organism-specific databases

CTD1654.
GeneCardsGC0XP041192.
HGNCHGNC:2745. DDX3X.
HPAHPA001648.
HPA005631.
MIM300160. gene.
neXtProtNX_O00571.
Orphanet99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBPA27216.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0513.
HOVERGENHBG015893.
InParanoidO00571.
KOK11594.
OMASFGSRND.
OrthoDBEOG7B5WV8.
PhylomeDBO00571.
TreeFamTF300364.

Gene expression databases

ArrayExpressO00571.
BgeeO00571.
CleanExHS_DDX3X.
GenevestigatorO00571.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR011545. 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]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDDX3X. human.
EvolutionaryTraceO00571.
GeneWikiDDX3X.
GenomeRNAi1654.
NextBio6810.
PROO00571.
SOURCESearch...

Entry information

Entry nameDDX3X_HUMAN
AccessionPrimary (citable) accession number: O00571
Secondary accession number(s): A8K538, B4E3E8, O15536
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM