DDX3X
entrez
1654
canonical
uniprot
O00571
canonical
ensembl
ENSG00000215301
resolver
ensp
ENSP00000392494
resolver
ensp
ENSP00000494040
resolver
ensp
ENSP00000494887
resolver
ensp
ENSP00000495377
resolver
ensp
ENSP00000791194
resolver
enst
ENST00000646319
resolver
enst
ENST00000646679
resolver
genesymbol
DDX3X
resolver
genesymbol_syn
DBX
resolver
genesymbol_syn
DDX3
resolver
hgnc
HGNC:2745
resolver
uniprot
A0A2R8YDT5
resolver
uniprot
A0A2R8YFS5
resolver
uniprot
A8K538
resolver
uniprot
B4E3E8
resolver
uniprot
O15536
resolver
uniprot_entry
A0A2R8YDT5_HUMAN
resolver
uniprot_entry
A0A2R8YFS5_HUMAN
resolver
uniprot_entry
DDX3X_HUMAN
resolver
uniprot_sec
A8K538
resolver
uniprot_sec
B4E3E8
resolver
uniprot_sec
O15536
resolver
amino_acid_sequence
MSHVAVENALGLDQQFAGLDLNSSDNQSGGSTASKGRYIPPHLRNREATKGFYDKDSSGWSSSKDKDAYSSFGSRSDSRGKSSFFSDRGSGSRGRFDDRGRSDYDGIGSRGDRSGFGKFERGGNSRWCDKSDEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEESDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAYEHHYKGSSRGRSKSSRFSGGFGARDYRQSSGASSSSFSSSRASSSRSGGGGHGSSRGFGGGGYGGFYNSDGYGGNYNSQGVDWWGN
uniprot
proteins
disease_involvement
DISEASE: Intellectual developmental disorder, X-linked, syndromic, Snijders Blok type (MRXSSB) [MIM:300958]: A disorder characterized by mild to severe intellectual disability, hypotonia, movement disorders, behavior problems, corpus callosum hypoplasia, and epilepsy. Additionally, patients manifest variable non-neurologic features such as joint hyperlaxity, skin pigmentary abnormalities, cleft lip and/or palate, hearing and visual impairment, and precocious puberty. {ECO:0000269|PubMed:26235985}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.4.13
uniprot
proteins
function
FUNCTION: Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs (PubMed:17357160, PubMed:21589879). Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA (PubMed:30256975). Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities (Probable). Involved in transcription regulation (PubMed:16818630, PubMed:18264132). Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity (PubMed:16818630, PubMed:18264132). CDKN1A up-regulation may be cell-type specific (PubMed:18264132). Binds CDH1/E-cadherin promoter and represses its transcription (PubMed:18264132). 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 (PubMed:28128295). May positively regulate TP53 transcription (PubMed:28842590). Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC) (PubMed:17095540, PubMed:18596238). Involved in the regulation of translation initiation (PubMed:17667941, PubMed:18628297, PubMed:22872150). Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR) (PubMed:20837705, PubMed:22872150). This function depends on helicase activity (PubMed:20837705, PubMed:22872150). Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning (PubMed:20837705). 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 (PubMed:22872150). Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process (PubMed:22323517). Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle (PubMed:20837705). May activate TP53 translation (PubMed:28842590). Required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139). Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E (PubMed:17667941, PubMed:22323517). Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E (PubMed:17667941). 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) (PubMed:20127681, PubMed:21170385, PubMed:31575075). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (PubMed:20127681, PubMed:21170385, PubMed:33674311). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:18583960, PubMed:18636090, PubMed:19913487, PubMed:21170385, PubMed:27980081). 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 (PubMed:23478265). 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 (PubMed:30341167). Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling (PubMed:30341167). 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 (PubMed:27736973). May also bind IFNB promoter; the function is independent of IRF3 (PubMed:18583960). Involved in both stress and inflammatory responses (By similarity). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (PubMed:21883093). 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 (By similarity). 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 (By similarity). 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 (PubMed:18846110). Cleavage by caspases may inactivate DDX3X and relieve the inhibition (PubMed:18846110). 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 (PubMed:23413191, PubMed:29222110). ATPase and casein kinase-activating functions are mutually exclusive (PubMed:29222110). May be involved in mitotic chromosome segregation (PubMed:21730191). {ECO:0000250|UniProtKB:Q62167, ECO:0000269|PubMed:16818630, ECO:0000269|PubMed:17095540, ECO:0000269|PubMed:17357160, ECO:0000269|PubMed:17667941, ECO:0000269|PubMed:18264132, ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18628297, ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:19913487, ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:20837705, ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:21589879, ECO:0000269|PubMed:21730191, ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22323517, ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:23478265, ECO:0000269|PubMed:27736973, ECO:0000269|PubMed:27980081, ECO:0000269|PubMed:28128295, ECO:0000269|PubMed:28842590, ECO:0000269|PubMed:29062139, ECO:0000269|PubMed:29222110, ECO:0000269|PubMed:30256975, ECO:0000269|PubMed:30341167, ECO:0000269|PubMed:31575075, ECO:0000269|PubMed:33674311, ECO:0000305}.; FUNCTION: (Microbial infection) Facilitates hepatitis C virus (HCV) replication (PubMed:29899501). During infection, HCV core protein inhibits the interaction between MAVS and DDX3X and therefore impairs MAVS-dependent INFB induction and might recruit DDX3X to HCV replication complex (PubMed:21170385). {ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates HIV-1 replication (PubMed:15507209, PubMed:18583960, PubMed:21589879, PubMed:22872150, PubMed:29899501). Acts as a cofactor for XPO1-mediated nuclear export of HIV-1 Rev RNAs (PubMed:15507209, PubMed:18583960, PubMed:29899501). This function is strongly stimulated in the presence of TBK1 and requires DDX3X ATPase activity (PubMed:18583960). {ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:21589879, ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Zika virus (ZIKV) replication. {ECO:0000269|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Dengue virus (DENV) replication. {ECO:0000269|PubMed:29899501}.; FUNCTION: (Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication. {ECO:0000269|PubMed:27105836}.
uniprot
proteins
mass_dalton
73243
uniprot
proteins
mutagenesis
MUTAGEN 12..21; /note="LDQQFAGLDL->ADQQAAGADA: Impairs nuclear export and interaction with XPO1/CMR1."; /evidence="ECO:0000269|PubMed:31575075"; MUTAGEN 19..21; /note="LDL->ADA: Impairs nuclear export and interaction with XPO1/CMR1."; /evidence="ECO:0000269|PubMed:30131165"; MUTAGEN 38; /note="Y->A: Impaired interaction with EIF4E; impaired stress granule formation, decreased repression of cap-dependent translation and decreased ability to enhance IRES-mediated translation. No effect on translation of HIV-1 RNA; when associated with A-43."; /evidence="ECO:0000269|PubMed:17667941, ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22872150"; MUTAGEN 43; /note="L->A: Impaired interaction with EIF4E; decreased repression of cap-dependent translation. 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."; /evidence="ECO:0000269|PubMed:17667941, ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22872150"; MUTAGEN 55; /note="K->R: Partial loss of ubiquitination by RNF39."; /evidence="ECO:0000269|PubMed:33674311"; MUTAGEN 71; /note="S->A: Reduces total phosphorylation by 60%. No effect on interaction with IKBKE."; /evidence="ECO:0000269|PubMed:23478265"; MUTAGEN 82..83; /note="SS->AA: Reduces total phosphorylation by 50%. No effect on interaction with IKBKE."; /evidence="ECO:0000269|PubMed:23478265"; MUTAGEN 84..85; /note="FF->AA: Loss of interaction with VACV protein K7, IRF3 activation and IFNB1 promoter induction."; /evidence="ECO:0000269|PubMed:19913487"; MUTAGEN 102; /note="S->A: Reduces total phosphorylation by 30%. Abolishes interaction with IRF3 and fails to enhance IFNB promoter induction. No effect on interaction with IKBKE."; /evidence="ECO:0000269|PubMed:23478265"; MUTAGEN 102; /note="S->D: Interacts with IRF3 and enhances IFNB promoter induction."; /evidence="ECO:0000269|PubMed:23478265"; MUTAGEN 138; /note="K->R: Partial loss of ubiquitination by RNF39."; /evidence="ECO:0000269|PubMed:33674311"; MUTAGEN 142..144; /note="PSE->ASA: Loss of interaction with TRAF3, reduced TRAF3 'K-63'-linked autoubiquitination."; /evidence="ECO:0000269|PubMed:27980081"; MUTAGEN 152; /note="S->A: Reduces total phosphorylation by 60%. No effect on interaction with IKBKE."; /evidence="ECO:0000269|PubMed:23478265"; MUTAGEN 162; /note="K->R: Partial loss of ubiquitination by RNF39."; /evidence="ECO:0000269|PubMed:33674311"; MUTAGEN 181; /note="S->A: Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFNB1 induction; when associated with A-183; A-240 and A-269."; /evidence="ECO:0000269|PubMed:18583960"; MUTAGEN 183; /note="S->A: Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-181; A-240 and A-269."; /evidence="ECO:0000269|PubMed:18583960"; MUTAGEN 200; /note="Y->A: No effect on general translation; when associated with A-207; A-230; A-347 and A-348."; /evidence="ECO:0000269|PubMed:22323517"; MUTAGEN 207; /note="Q->A: Does not promote the translation of HIV-1 RNA. No effect on general translation; when associated with A-200; A-230: A-347 and A-348."; /evidence="ECO:0000269|PubMed:22323517, ECO:0000269|PubMed:22872150"; MUTAGEN 230; /note="K->A: No effect on general translation; when associated with A-200; A-207; A-347 and A-348."; /evidence="ECO:0000269|PubMed:22323517"; MUTAGEN 230; /note="K->E: Complete loss of ATPase and RNA-unwinding activities. Loss of HIV-1 mRNA nuclear export. Does not promote the translation of HIV-1 RNA. No effect on IFNB1 induction. No effect on RNA-binding. Loss of inhibition of NF-kappa-B-mediated transcriptional activity."; /evidence="ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:21589879, ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:27736973"; MUTAGEN 240; /note="S->A: Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-181; A-183 and A-269."; /evidence="ECO:0000269|PubMed:18583960"; MUTAGEN 269; /note="S->A: Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-181; A-183 and A-240."; /evidence="ECO:0000269|PubMed:18583960"; MUTAGEN 275..277; /note="TRE->RRV: Increased NF-kappa-B-mediated transcriptional activity, contrary to wild-type which is inhibitory in this experimental setting."; /evidence="ECO:0000269|PubMed:27736973"; MUTAGEN 347..350; /note="DEAD->AEAA: Loss of ATPase activity."; /evidence="ECO:0000269|PubMed:21589879"; MUTAGEN 347; /note="D->A: No effect on general translation; when associated with A-200; A-207; A-230 and A-348."; /evidence="ECO:0000269|PubMed:22323517"; MUTAGEN 348; /note="E->A: No effect on general translation; when associated with A-200; A-207; A-230 and A-347."; /evidence="ECO:0000269|PubMed:22323517, ECO:0000269|PubMed:22872150"; MUTAGEN 348; /note="E->Q: Loss of both ATPase and RNA helicase activities; decreased up-regulation of CDKN1A promoter activity and HNF4A-mediated MTTP transcriptional activation; no effect on the repression of cap- and IRES-dependent translation, WNT/beta catenin signaling, nor on stress granule assembly. Does not promote the translation of HIV-1 RNA."; /evidence="ECO:0000269|PubMed:17667941, ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22323517, ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:23413191"; MUTAGEN 382..384; /note="SAT->AAA: Loss of RNA helicase, but not ATPase activity; no effect on the repression of cap- and IRES-dependent translation, WNT/beta catenin signaling, up-regulation of CDKN1A promoter activity, HNF4A-mediated MTTP transcriptional activation, nor on stress granule assembly."; /evidence="ECO:0000269|PubMed:17667941, ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:28128295"; MUTAGEN 382; /note="S->L: Strong decrease in ATPase activity and RNA-unwinding activity. Does not promote the translation of mRNAs containing long structured 5'UTRs, including that of CCNE1. No effect on the translation of HIV-1 RNA."; /evidence="ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:20837705, ECO:0000269|PubMed:22872150"; MUTAGEN 429; /note="S->A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-438; A-442; A-456 and A-520."; /evidence="ECO:0000269|PubMed:18583960"; MUTAGEN 438; /note="T->A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-442; A-456 and A-520."; /evidence="ECO:0000269|PubMed:18583960"; MUTAGEN 442; /note="S->A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-438; A-456 and A-520."; /evidence="ECO:0000269|PubMed:18583960"; MUTAGEN 456; /note="S->A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-438; A-442 and A-520."; /evidence="ECO:0000269|PubMed:18583960"; MUTAGEN 520; /note="S->A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-438; A-442 and A-456."; /evidence="ECO:0000269|PubMed:18583960
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by TBK1; the phosphorylation is required for the synergistic induction of IFNB mediated by TBK1 and DDX3X (PubMed:18583960). Phosphorylated by IKBKE at Ser-102 after ssRNA viral infection; enhances the induction of INFB promoter by IRF3 (PubMed:18583960, PubMed:23478265). The cytoplasmic form is highly phosphorylated in the G1/S phase of the cell cycle and much less at G2/M (PubMed:22034099). Phosphorylation by CSNK1E may inhibit RNA-stimulated ATPase activity (PubMed:29222110). {ECO:0000269|PubMed:18583960, ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:23478265, ECO:0000269|PubMed:29222110}.; PTM: 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. {ECO:0000269|PubMed:18846110}.; PTM: Ubiquitinated by RNF39 via 'Lys-48'-linked ubiquitination; leading to proteasomal degradation. {ECO:0000269|PubMed:33674311}.
uniprot
proteins
protein_family
DDX3/DED1 subfamily
uniprot
proteins
protein_family
DEAD box helicase family
uniprot
proteins
pubmed
10329544
uniprot
proteins
pubmed
10859333
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15294876
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15507209
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16301996
uniprot
proteins
pubmed
16818630
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17095540
uniprot
proteins
pubmed
17357160
uniprot
proteins
pubmed
17401195
uniprot
proteins
pubmed
17631897
uniprot
proteins
pubmed
17667941
uniprot
proteins
pubmed
18264132
uniprot
proteins
pubmed
18583960
uniprot
proteins
pubmed
18596238
uniprot
proteins
pubmed
18628297
uniprot
proteins
pubmed
18632687
uniprot
proteins
pubmed
18636090
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18846110
uniprot
proteins
pubmed
19029303
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19913487
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20127681
uniprot
proteins
pubmed
20375222
uniprot
proteins
pubmed
20657822
uniprot
proteins
pubmed
20837705
uniprot
proteins
pubmed
21170385
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21589879
uniprot
proteins
pubmed
21730191
uniprot
proteins
pubmed
21883093
uniprot
proteins
pubmed
22034099
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22323517
uniprot
proteins
pubmed
22872150
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23413191
uniprot
proteins
pubmed
23478265
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26030138
uniprot
proteins
pubmed
26100019
uniprot
proteins
pubmed
26235985
uniprot
proteins
pubmed
27105836
uniprot
proteins
pubmed
27546789
uniprot
proteins
pubmed
27736973
uniprot
proteins
pubmed
27980081
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28128295
uniprot
proteins
pubmed
28733330
uniprot
proteins
pubmed
28842590
uniprot
proteins
pubmed
29062139
uniprot
proteins
pubmed
29222110
uniprot
proteins
pubmed
29899501
uniprot
proteins
pubmed
30131165
uniprot
proteins
pubmed
30256975
uniprot
proteins
pubmed
30341167
uniprot
proteins
pubmed
31300642
uniprot
proteins
pubmed
31575075
uniprot
proteins
pubmed
33674311
uniprot
proteins
pubmed
9381176
uniprot
proteins
sequence_length
662
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:29899501}. Nucleus {ECO:0000269|PubMed:10329544, ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:16818630, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:29899501, ECO:0000269|PubMed:30131165, ECO:0000269|PubMed:31575075}. Cytoplasm {ECO:0000269|PubMed:10329544, ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:16818630, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:21170385, ECO:0000269|PubMed:21730191, ECO:0000269|PubMed:21883093, ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:27105836, ECO:0000269|PubMed:27736973, ECO:0000269|PubMed:28733330, ECO:0000269|PubMed:29062139, ECO:0000269|PubMed:29222110, ECO:0000269|PubMed:30131165, ECO:0000269|PubMed:30341167, ECO:0000269|PubMed:31575075, ECO:0000269|PubMed:33674311}. Cytoplasm, Stress granule {ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:29062139}. Inflammasome {ECO:0000250|UniProtKB:Q62167}. Cell projection, lamellipodium {ECO:0000269|PubMed:28733330}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:28842590}. Note=Shuttles between the nucleus and the cytosol (PubMed:15507209, PubMed:18636090, PubMed:29899501, PubMed:30131165, PubMed:31575075). Exported from the nucleus partly through the XPO1/CRM1 system and partly through NXF1/TAP (PubMed:15507209, PubMed:18596238, PubMed:18636090, PubMed:30131165, PubMed:31575075). Localizes to nuclear pores on the outer side of the nuclear membrane (PubMed:15507209). In the cytosol, partly colocalizes with mitochondria (PubMed:20127681). At G0, predominantly located in nucleus. In G1/S phase, predominantly cytoplasmic (PubMed:22034099). During prophase/prometaphase, localizes in close proximity to the condensing chromosomes (PubMed:21730191, PubMed:30131165). During telophase, localizes around the newly synthesized nuclear membrane and in the cytoplasm (PubMed:22034099). Colocalizes with TRPV4 at the plasma membrane. When TRPV4 channel is activated, intracellular Ca(2+) levels increase and the calmodulin/CAMKII pathway is activated, relocalizes to the nucleus (PubMed:29899501). WNT3A stimulation promotes DDX3 recruitment to the plasma membrane (PubMed:23413191). At the leading edge of migrating fibroblasts, colocalizes with CAPRIN1 and PABPC1 (PubMed:28733330). Localizes to centrosome throughout the cell cycle and associates with TP53 at centrosome during mitosis (PubMed:28842590). Translocates to the nucleus in response to HPIV-3 virus-mediated infection (PubMed:31575075). {ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:20127681, ECO:0000269|PubMed:21730191, ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:28733330, ECO:0000269|PubMed:28842590, ECO:0000269|PubMed:29899501, ECO:0000269|PubMed:30131165, ECO:0000269|PubMed:31575075}.
uniprot
proteins