Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q62167 (DDX3X_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
D1Pas1-related sequence 2
DEAD box RNA helicase DEAD3
Short name=mDEAD3
DEAD box protein 3, X-chromosomal
Embryonic RNA helicase
Gene names
Name:Ddx3x
Synonyms:D1Pas1-rs2, Ddx3, Dead3, Erh
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity.

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. Interacts 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 By similarity.

Subcellular location

Nucleus speckle By similarity. Cytoplasm By similarity. Mitochondrion outer membrane By similarity. 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 By similarity.

Tissue specificity

Developmentally regulated.

Developmental stage

Expressed in oocytes. Ubiquitously found in 9 days post-conception embryo, at later stages it is restricted to brain and kidney.

Post-translational modification

Phosphorylated by TBK1; the phosphorylation is required to synergize with TBK1 in IFN-beta induction. Probably also phosphorylated by IKBKE By similarity.

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
Immunity
Innate immunity
Ribosome biogenesis
Transcription
Transcription regulation
Translation regulation
   Cellular componentCytoplasm
Membrane
Mitochondrion
Mitochondrion outer membrane
Nucleus
   LigandATP-binding
DNA-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity. Source: GOC

DNA duplex unwinding

Inferred from sequence or structural similarity. Source: GOC

RNA secondary structure unwinding

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to arsenic-containing substance

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to osmotic stress

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome segregation

Inferred from sequence or structural similarity. Source: UniProtKB

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from sequence or structural similarity. Source: UniProtKB

innate immune response

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

intrinsic apoptotic signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

mature ribosome assembly

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

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

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of intrinsic apoptotic signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein complex assembly

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of translation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of G1/S transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

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

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of translation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of translational initiation

Inferred from sequence or structural similarity. Source: UniProtKB

response to virus

Inferred from sequence or structural similarity. Source: UniProtKB

stress granule assembly

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic stress granule

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ATP-dependent RNA helicase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

RNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

RNA stem-loop binding

Inferred from sequence or structural similarity. Source: UniProtKB

eukaryotic initiation factor 4E binding

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA 5'-UTR binding

Inferred from sequence or structural similarity. Source: UniProtKB

poly(A) binding

Inferred from sequence or structural similarity. Source: UniProtKB

ribosomal small subunit binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

translation initiation factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TBK1Q9UHD28EBI-773173,EBI-356402From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 662661ATP-dependent RNA helicase DDX3X
PRO_0000055010

Regions

Domain211 – 403193Helicase ATP-binding
Domain414 – 575162Helicase C-terminal
Nucleotide binding200 – 2078ATP By similarity
Nucleotide binding224 – 2318ATP By similarity
Region2 – 139138Required for TBK1 and IKBKE-dependent IFN-beta activation By similarity
Region2 – 10099Interaction with EIF4E By similarity
Region100 – 662563Interaction with GSK3B By similarity
Region100 – 11011Required for interaction with IKBKE By similarity
Region250 – 25910Involved in stimulation of ATPase activity by DNA and RNA, nucleic acid binding and unwinding By similarity
Region260 – 517258Necessary for interaction with XPO1 By similarity
Motif180 – 20829Q motif
Motif347 – 3504DEAD box
Compositional bias582 – 66281Gly/Ser-rich
Compositional bias609 – 6168Poly-Ser
Compositional bias624 – 6307Poly-Gly
Compositional bias633 – 6419Poly-Gly

Amino acid modifications

Modified residue21N-acetylserine Ref.3
Modified residue551N6-acetyllysine Ref.7
Modified residue691Phosphotyrosine By similarity
Modified residue741Phosphoserine By similarity
Modified residue781Phosphoserine By similarity
Modified residue1041Phosphotyrosine Ref.5
Modified residue1181N6-acetyllysine By similarity
Modified residue1251Phosphoserine By similarity
Modified residue1311Phosphoserine Ref.6
Modified residue3431Phosphotyrosine By similarity
Modified residue5901Phosphoserine By similarity
Modified residue5941Phosphoserine By similarity
Modified residue6121Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q62167 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 216515CB00324017

FASTA66273,101
        10         20         30         40         50         60 
MSHVAVENAL GLDQQFAGLD LNSSDNQSGG STASKGRYIP PHLRNREATK GFYDKDSSGW 

        70         80         90        100        110        120 
SSSKDKDAYS SFGSRGDSRG KSSFFGDRGS GSRGRFDDRG RGDYDGIGGR 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 
QIYADGPGEA LRAMKENGRY GRRKQYPISL VLAPTRELAV QIYEEARKFS YRSRVRPCVV 

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

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

       430        440        450        460        470        480 
WVEEIDKRSF 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 LENMAFEHHY KGSSRGRSKS SRFSGGFGAR 

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


GN 

« Hide

References

« Hide 'large scale' references
[1]"The embryonic RNA helicase gene (ERH): a new member of the DEAD box family of RNA helicases."
Sowden J.C., Putt W., Morrison K., Beddington R., Edwards Y.
Biochem. J. 308:839-846(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 and DBA.
[2]"Mouse erythroid cells express multiple putative RNA helicase genes exhibiting high sequence conservation from yeast to mammals."
Gee S.L., Conboy J.G.
Gene 140:171-177(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Erythroleukemia.
[3]"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.
[4]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 535-548, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
[5]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z38117 mRNA. Translation: CAA86261.1.
L25126 mRNA. Translation: AAA53630.1.
PIRI84741.
RefSeqNP_034158.1. NM_010028.3.
UniGeneMm.289662.

3D structure databases

ProteinModelPortalQ62167.
SMRQ62167. Positions 139-580.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199084. 1 interaction.
IntActQ62167. 7 interactions.
MINTMINT-1870173.

PTM databases

PhosphoSiteQ62167.

2D gel databases

REPRODUCTION-2DPAGEQ62167.

Proteomic databases

PaxDbQ62167.
PRIDEQ62167.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000804; ENSMUSP00000000804; ENSMUSG00000000787.
GeneID13205.
KEGGmmu:13205.
UCSCuc009srl.2. mouse.

Organism-specific databases

CTD1654.
MGIMGI:103064. Ddx3x.

Phylogenomic databases

eggNOGCOG0513.
GeneTreeENSGT00740000115030.
HOGENOMHOG000268804.
HOVERGENHBG015893.
InParanoidQ62167.
KOK11594.
OMAGMSHVAV.
OrthoDBEOG7B5WV8.
PhylomeDBQ62167.
TreeFamTF300332.

Gene expression databases

ArrayExpressQ62167.
BgeeQ62167.
CleanExMM_ERH.
GenevestigatorQ62167.

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. mouse.
NextBio283364.
PROQ62167.
SOURCESearch...

Entry information

Entry nameDDX3X_MOUSE
AccessionPrimary (citable) accession number: Q62167
Secondary accession number(s): O09060, O09143
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot