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Entry version 189 (12 Aug 2020)
Sequence version 3 (23 Jan 2007)
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Protein

ATP-dependent RNA helicase DDX3X

Gene

Ddx3x

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA. Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities. Involved in transcription regulation. Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity. CDKN1A up-regulation may be cell-type specific. Binds CDH1/E-cadherin promoter and represses its transcription. Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis. May positively regulate TP53 transcription. Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC). Involved in the regulation of translation initiation. Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR). This function depends on helicase activity. Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning. Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety. Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process. Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle. May activate TP53 translation. Required for endoplasmic reticulum stress-induced ATF4 mRNA translation. Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E. Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E. Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta). Potentiate MAVS/DDX58-mediated induction of IFNB in early stages of infection (By similarity). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:30475900). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation. Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7. Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling. Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm. May also bind IFNB promoter; the function is independent of IRF3 (By similarity). Involved in both stress and inflammatory responses (PubMed:31511697). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (By similarity). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity. Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (PubMed:31511697). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation. Cleavage by caspases may inactivate DDX3X and relieve the inhibition. Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant. ATPase and casein kinase-activating functions are mutually exclusive. May be involved in mitotic chromosome segregation (By similarity).By similarity2 Publications

Miscellaneous

Encoded by an chromosome X-linked gene which escapes X chromosome inactivation (XCI) in females, but exhibits developmental- and tissue-specific differences in escape from XCI. DDX3Y, its homolog on chromosome Y, is located in the Y non-recombinant portion (By similarity). In 8 to 16 cell stage embryos, expression from paternal and maternal copies of DDX3X is detected. Paternally derived DDX3X is preferentially inactivated in extraembryonic tissues of embryos from 6.5 dpc (PubMed:27179789).By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi200 – 207ATPPROSITE-ProRule annotation8
Nucleotide bindingi224 – 231ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Helicase, Hydrolase, RNA-binding
Biological processApoptosis, Chromosome partition, Immunity, Inflammatory response, Innate immunity, Ribosome biogenesis, Transcription, Transcription regulation, Translation regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-6798695, Neutrophil degranulation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
ATP-dependent RNA helicase DDX3X (EC:3.6.4.13By similarity)
Alternative name(s):
D1Pas1-related sequence 2
DEAD box RNA helicase DEAD3
Short name:
mDEAD31 Publication
DEAD box protein 3, X-chromosomal
Embryonic RNA helicase1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Ddx3x
Synonyms:D1Pas1-rs2, Ddx3, Dead3, Erh1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:103064, Ddx3x

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Inflammasome, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

In mutant males, loss of DDX3X leads to early post-implantation lethality. In mutant females with a maternally inherited Ddx3x null allele, paternal X chromosome inactivation affects trophoblast differentiation, which leads to aberrant placental layers and defective vascularization in placental labyrinth. These placental abnormalities impair maternal blood supply to the embryo and ultimately lead to fetal growth restriction and lethality. Heterozygous females with a paternally inherited null allele are born at the expected Mendelian ratio, develop normally and are indistinguishable from their littermate controls (PubMed:27179789). Epiblast-specific knockout embryos exhibit multiple anomalies, including defective neural tube closure, underdeveloped brain, poorly developed myocardial trabeculae, which ultimately lead to embryonic lethality around 11.5 dpc (PubMed:27179789). DDX3X and DDX3Y double knockout is embryonic lethal (PubMed:30613052). DDX3X and DDX3Y double knockout germ cells can differentiate into spermatozoa (PubMed:30613052). Bone-marrow macrophage-specific knockout leads to a reduction in the expression of several cytokines, including IL1B, IL6, IL12 and IFNB1, in response to Listeria monocytogenes infection and pathogen-associated molecular patterns (PAMPs), including poly (I:C), poly (dA:dT) and LPS. This effect is more prononced in females than in male macrophages, probably due to the functional redundancy with DDX3Y gene located on chromosome Y (PubMed:30475900).3 Publications

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3751657

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000550102 – 662ATP-dependent RNA helicase DDX3XAdd BLAST661

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine1 Publication1
Modified residuei55N6-acetyllysineCombined sources1
Modified residuei82PhosphoserineBy similarity1
Modified residuei90PhosphoserineBy similarity1
Modified residuei101Omega-N-methylarginineCombined sources1
Modified residuei104PhosphotyrosineCombined sources1
Modified residuei110Omega-N-methylarginineCombined sources1
Modified residuei118N6-acetyllysineBy similarity1
Modified residuei131PhosphoserineCombined sources1
Modified residuei183PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki215Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei456PhosphoserineBy similarity1
Modified residuei592Omega-N-methylarginineBy similarity1
Modified residuei594PhosphoserineBy similarity1
Modified residuei605PhosphoserineBy similarity1
Modified residuei612PhosphoserineBy similarity1
Modified residuei617Omega-N-methylarginineBy similarity1
Modified residuei632Omega-N-methylarginineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by TBK1; the phosphorylation is required for the synergistic induction of IFNB mediated by TBK1 and DDX3X. Phosphorylated by IKBKE. Also phosphorylated by CSNK1E; this phosphorylation may inhibit RNA-stimulated ATPase activity.By similarity
Upon stimulation of death receptors, including TNFRSF10B, recruited to receptors and cleaved by caspases. Proteolytic fragments remain associated with the receptors. This cleavage presumably inactivates DDX3X anti-apoptotic function.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q62167

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q62167

MaxQB - The MaxQuant DataBase

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MaxQBi
Q62167

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q62167

PRoteomics IDEntifications database

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PRIDEi
Q62167

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
Q62167

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q62167

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q62167

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q62167

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in ovary, including in germinal vesicle immature and metaphase II (MII) stage oocytes (at protein level) (PubMed:8948440, PubMed:25050112). In the brain, expressed in the granule cells of the cerebellum and dentate gyrus, the pyramidal cells of the hippocampus, the ependymal cells lining the ventricles, choroid plexi and olfactory bulb. Also accumulates in the thalamic nuclei, the dorsal region of the colliculi and the pontine nucleus (PubMed:8948440).2 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

In oocytes, expression levels increase from germinal vesicle immature oocytes to metaphase II (MII) and decline after fertilization in 1-cell and 2-cell embryos (at protein level) (PubMed:25050112). At 7.5 dpc, highly expressed in all embryonic cells and extraembryonic tissues, including ectoplacental cone, chorion, extraembryonic endoderm and parietal endoderm (at protein level) (PubMed:27179789). At 8.5-9.5 dpc, widely expressed (PubMed:8948440). At 8.5 dpc, levels decrease in extraembryonic tissues (PubMed:27179789). As development proceeds, expression becomes more restricted. At 11.5 dpc, most abundant in the neural tube, but still expressed at moderate levels in a number of other sites, including the mesenchyme of limbs and the face and in liver. At 14.5 dpc, highly expressed in the developing brain and caudal neural tube, but absent from the marginal layer of the neural tube. Also expressed in the developing metanephros and lung. At 15.5 dpc, expressed in the brain and spinal cord, as well as in teeth primordia, the lung and in the developing limb (PubMed:8948440). At 16.5 dpc, moderate, but non-uniform expression levels in the placenta (PubMed:27179789).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000000787, Expressed in embryonic post-anal tail and 334 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q62167, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q62167, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; can bind RNA as a monomer and as a dimer/oligomer.

Interacts with TDRD3. When phosphorylated, interacts with IRF3; the interaction facilitates the phosphorylation and activation of IRF3 by IKBKE. Directly interacts with XPO1/CRM1. Weakly interacts with TBKBP1/SINTBAD. Directly interacts with TRAF3; this interaction stimulates TRAF3 'Lys-63' ubiquitination.

Interacts with CSNK1E in a Wnt-dependent manner; this interaction greatly enhances CSNK1E affinity for ATP, stimulates its kinase activity and promotes CSNK1E-mediated DVL2 phosphorylation. In the presence of RNA, the interaction is decreased.

Also interacts with CSNK1D and stimulates its kinase activity.

Interacts with TRPV4; this interaction is decreased when the TRPV4 channel is activated, leading to DDX3X relocalization to the nucleus.

Interacts with MAP3K14/NIK. Directly interacts with CHUK/IKKA after physiological activation of the TLR7 and TLR8 pathways; this interaction enhances CHUK autophosphorylation. May associate with EIF4F complex, composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. Directly interacts with EIF4E in an RNA-independent manner; this interaction enhances EIF4E cap-binding ability. Directly interacts with EIF4G1 in an RNA-independent manner. DDX3X competes with EIF4G1 for interaction with EIF4E.

Interacts with EIF4A1 and EIF2S1 in an RNA-independent manner. Associates with the eukaryotic translation initiation factor 3 (eIF-3) complex, including with EIF3B and EIF3C subunits. Directly interacts with IKBKE/IKKE; this interaction stimulates IKBKE activating autophosphorylation and is induced upon viral infection.

Interacts with TBK1.

Interacts with SP1; this interaction potentiates SP1-induced CDKN1A/WAF1/CIP1 transcription.

Interacts with GSK3A and GSK3B.

Interacts with several death receptors, inclusing FAS, TNFRSF10A and TNFRSF10B. Recruited to TNFRSF10B in the absence of receptor stimulation. When TNFRSF10B is stimulated, further recruited to the receptor and cleaved by caspases. A large proteolytic fragment remains associated with TNFRSF10B.

Interacts (via C-terminus) with NXF1/TAP; this interaction may be partly involved in DDX3X nuclear export and in NXF1 localization to stress granules.

Identified in an mRNP complex, composed of at least DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1/2, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. The interaction with IGF2BP1/2 is RNA-dependent. Directly interacts with PABPC1/PABP1 in an RNA-independent manner. This interaction increases in stressed cells and decreases during cell recovery.

Interacts (via C-terminus) with MAVS/IPS-1; this interaction potentiates MAVS-mediated IFNB induction.

Interacts with ERCC6/CBS.

Interacts with DHX33 in an RNA-independent manner.

Interacts with DDX5 in the cytoplasm; this interaction may be more efficient when both proteins are unphosphorylated.

Interacts with DDX58/RIG-1.

Interacts with IFIH1/MDA5.

Interacts with NCAPH; this interaction may be important for the NCAPH localization at condensing chromosomes during mitosis (By similarity).

Interacts with NLRP3 (via NACHT domain) under inflammasome-activating conditions (PubMed:31511697).

Interacts with CAPRIN1.

Interacts with HNF4A and NR0B2/SHP in an RNA-independent manner; this interaction disrupts the interaction between HNF4 and NR0B2 that forms inactive heterodimers and enhances the formation of active HNF4 homodimers.

Interacts with CREBBP/CBP.

Interacts with EP300/p300.

Interacts with gamma-tubulin.

Interacts with phosphorylated TP53. Directly interacts with RELA/p65; this interaction may trap RELA in the cytoplasm, impairing nuclear relocalization upon TNF activating signals (By similarity).

By similarity1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
199084, 80 interactors

Protein interaction database and analysis system

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IntActi
Q62167, 17 interactors

Molecular INTeraction database

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MINTi
Q62167

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000000804

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q62167, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q62167

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini211 – 403Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST193
Domaini414 – 575Helicase C-terminalPROSITE-ProRule annotationAdd BLAST162

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 139Required for TBK1 and IKBKE-dependent IFNB1 activationBy similarityAdd BLAST138
Regioni38 – 44Interaction with EIF4EBy similarity7
Regioni100 – 662Interaction with GSK3BBy similarityAdd BLAST563
Regioni100 – 110Interaction with IKBKEBy similarityAdd BLAST11
Regioni139 – 172Interaction with CHUKBy similarityAdd BLAST34
Regioni250 – 259Involved in stimulation of ATPase activity by DNA and RNA, nucleic acid binding and unwindingBy similarity10
Regioni260 – 517Interaction with XPO1By similarityAdd BLAST258
Regioni536 – 661Interaction with NXF1By similarityAdd BLAST126

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi180 – 208Q motifAdd BLAST29
Motifi347 – 350DEAD box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi582 – 662Gly/Ser-richAdd BLAST81
Compositional biasi609 – 616Poly-Ser8
Compositional biasi624 – 630Poly-Gly7
Compositional biasi633 – 641Poly-Gly9

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0335, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000154443

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_003041_16_3_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q62167

KEGG Orthology (KO)

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KOi
K11594

Identification of Orthologs from Complete Genome Data

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OMAi
CYRSWVR

Database of Orthologous Groups

More...
OrthoDBi
595675at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q62167

TreeFam database of animal gene trees

More...
TreeFami
TF300332

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011545, DEAD/DEAH_box_helicase_dom
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR000629, RNA-helicase_DEAD-box_CS
IPR014014, RNA_helicase_DEAD_Q_motif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00270, DEAD, 1 hit
PF00271, Helicase_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00039, DEAD_ATP_HELICASE, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS51195, Q_MOTIF, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q62167-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSHVAVENAL GLDQQFAGLD LNSSDNQSGG STASKGRYIP PHLRNREATK
60 70 80 90 100
GFYDKDSSGW SSSKDKDAYS SFGSRGDSRG KSSFFGDRGS GSRGRFDDRG
110 120 130 140 150
RGDYDGIGGR GDRSGFGKFE RGGNSRWCDK SDEDDWSKPL PPSERLEQEL
160 170 180 190 200
FSGGNTGINF EKYDDIPVEA TGNNCPPHIE SFSDVEMGEI IMGNIELTRY
210 220 230 240 250
TRPTPVQKHA IPIIKEKRDL MACAQTGSGK TAAFLLPILS QIYADGPGEA
260 270 280 290 300
LRAMKENGRY GRRKQYPISL VLAPTRELAV QIYEEARKFS YRSRVRPCVV
310 320 330 340 350
YGGAEIGQQI RDLERGCHLL VATPGRLVDM MERGKIGLDF CKYLVLDEAD
360 370 380 390 400
RMLDMGFEPQ IRRIVEQDTM PPKGVRHTMM FSATFPKEIQ MLARDFLDEY
410 420 430 440 450
IFLAVGRVGS TSENITQKVV WVEEIDKRSF LLDLLNATGK DSLTLVFVET
460 470 480 490 500
KKGADSLEDF LYHEGYACTS IHGDRSQRDR EEALHQFRSG KSPILVATAV
510 520 530 540 550
AARGLDISNV KHVINFDLPS DIEEYVHRIG RTGRVGNLGL ATSFFNERNI
560 570 580 590 600
NITKDLLDLL VEAKQEVPSW LENMAFEHHY KGSSRGRSKS SRFSGGFGAR
610 620 630 640 650
DYRQSSGASS SSFSSSRASS SRSGGGGHGG SRGFGGGGYG GFYNSDGYGG
660
NYNSQGVDWW GN
Length:662
Mass (Da):73,101
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i216515CB00324017
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
Z38117 mRNA Translation: CAA86261.1
L25126 mRNA Translation: AAA53630.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS30027.1

Protein sequence database of the Protein Information Resource

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PIRi
I84741

NCBI Reference Sequences

More...
RefSeqi
NP_034158.1, NM_010028.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000000804; ENSMUSP00000000804; ENSMUSG00000000787

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
13205

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:13205

UCSC genome browser

More...
UCSCi
uc009srl.2, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38117 mRNA Translation: CAA86261.1
L25126 mRNA Translation: AAA53630.1
CCDSiCCDS30027.1
PIRiI84741
RefSeqiNP_034158.1, NM_010028.3

3D structure databases

SMRiQ62167
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi199084, 80 interactors
IntActiQ62167, 17 interactors
MINTiQ62167
STRINGi10090.ENSMUSP00000000804

Chemistry databases

ChEMBLiCHEMBL3751657

PTM databases

iPTMnetiQ62167
PhosphoSitePlusiQ62167
SwissPalmiQ62167

2D gel databases

REPRODUCTION-2DPAGEiQ62167

Proteomic databases

EPDiQ62167
jPOSTiQ62167
MaxQBiQ62167
PaxDbiQ62167
PRIDEiQ62167

Genome annotation databases

EnsembliENSMUST00000000804; ENSMUSP00000000804; ENSMUSG00000000787
GeneIDi13205
KEGGimmu:13205
UCSCiuc009srl.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1654
MGIiMGI:103064, Ddx3x

Phylogenomic databases

eggNOGiKOG0335, Eukaryota
GeneTreeiENSGT00940000154443
HOGENOMiCLU_003041_16_3_1
InParanoidiQ62167
KOiK11594
OMAiCYRSWVR
OrthoDBi595675at2759
PhylomeDBiQ62167
TreeFamiTF300332

Enzyme and pathway databases

ReactomeiR-MMU-6798695, Neutrophil degranulation

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
13205, 7 hits in 18 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Ddx3x, mouse

Protein Ontology

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PROi
PR:Q62167
RNActiQ62167, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000000787, Expressed in embryonic post-anal tail and 334 other tissues
ExpressionAtlasiQ62167, baseline and differential
GenevisibleiQ62167, MM

Family and domain databases

InterProiView protein in InterPro
IPR011545, DEAD/DEAH_box_helicase_dom
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR000629, RNA-helicase_DEAD-box_CS
IPR014014, RNA_helicase_DEAD_Q_motif
PfamiView protein in Pfam
PF00270, DEAD, 1 hit
PF00271, Helicase_C, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00039, DEAD_ATP_HELICASE, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS51195, Q_MOTIF, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDDX3X_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q62167
Secondary accession number(s): O09060, O09143
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: August 12, 2020
This is version 189 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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