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O00571

- DDX3X_HUMAN

UniProt

O00571 - DDX3X_HUMAN

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Protein

ATP-dependent RNA helicase DDX3X

Gene
DDX3X, DBX, DDX3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Multifunctional ATP-dependent RNA helicase. The ATPase activity can be stimulated by various ribo- and deoxynucleic acids indicative for a relaxed substrate specificity. In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs. Is involved in several steps of gene expression, such as transcription, mRNA maturation, mRNA export and translation. However, the exact mechanisms are not known and some functions may be specific for a subset of mRNAs. Involved in transcriptional regulation. Can enhance transcription from the CDKN1A/WAF1 promoter in a SP1-dependent manner. Found associated with the E-cadherin promoter and can down-regulate transcription from the promoter. Involved in regulation of translation initiation. Proposed to be involved in positive regulation of translation such as of cyclin E1/CCNE1 mRNA and specifically of mRNAs containing complex secondary structures in their 5'UTRs; these functions seem to require RNA helicase activity. Specifically promotes translation of a subset of viral and cellular mRNAs carrying a 5'proximal stem-loop structure in their 5'UTRs and cooperates with the eIF4F complex. Proposed to act prior to 43S ribosomal scanning and to locally destabilize these RNA structures to allow recognition of the mRNA cap or loading onto the 40S subunit. After association with 40S ribosomal subunits seems to be involved in the functional assembly of 80S ribosomes; the function seems to cover translation of mRNAs with structured and non-structured 5'UTRs and is independent of RNA helicase activity. Also proposed to inhibit cap-dependent translation by competetive interaction with EIF4E which can block the EIF4E:EIF4G complex formation. Proposed to be involved in stress response and stress granule assembly; the function is independent of RNA helicase activity and seems to involve association with EIF4E. May be involved in nuclear export of specific mRNAs but not in bulk mRNA export via interactions with XPO1 and NXF1. Also associates with polyadenylated mRNAs independently of NXF1. Associates with spliced mRNAs in an exon junction complex (EJC)-dependent manner and seems not to be directly involved in splicing. May be involved in nuclear mRNA export by association with DDX5 and regulating its nuclear location. Involved in innate immune signaling promoting the production of type I interferon (IFN-alpha and IFN-beta); proposed to act as viral RNA sensor, signaling intermediate and transcriptional coactivator. Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, plays a role of scaffolding adapter that links IKBKE and IRF3 and coordinates their activation. Also found associated with IFNB promoters; the function is independent of IRF3. Can bind to viral RNAs and via association with MAVS/IPS1 and DDX58/RIG-I is thought to induce signaling in early stages of infection. Involved in regulation of apoptosis. May be required for activation of the intrinsic but inhibit activation of the extrinsic apoptotic pathway. Acts as an antiapoptotic protein through association with GSK3A/B and BIRC2 in an apoptosis antagonizing signaling complex; activation of death receptors promotes caspase-dependent cleavage of BIRC2 and DDX3X and relieves the inhibition. May be involved in mitotic chromosome segregation. Appears to be a prime target for viral manipulations. Hepatitis B virus (HBV) polymerase and possibly vaccinia virus (VACV) protein K7 inhibit IFNB induction probably by dissociating DDX3X from TBK1 or IKBKE. Is involved in hepatitis C virus (HCV) replication; the function may involve the association with HCV core protein. HCV core protein inhibits the IPS1-dependent function in viral RNA sensing and may switch the function from a INFB inducing to a HCV replication mode. Involved in HIV-1 replication. Acts as a cofactor for XPO1-mediated nuclear export of incompletely spliced HIV-1 Rev RNAs.24 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

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

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

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

Keywords - Ligandi

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

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:2745. DDX3X.

Subcellular locationi

Nucleus speckle. Cytoplasm. Mitochondrion outer membrane
Note: Located predominantly in nuclear speckles and, at low levels, throughout the cytoplasm. Located to the outer side of nuclear pore complexes (NPC). Shuttles between the nucleus and the cytoplasm in a XPO1 and may be also in a NFX1-dependent manner. Associated with polyadenylated mRNAs in the cytoplasm and the nucleus. Predominantly located in nucleus during G0 phase and in the cytoplasm during G1/S phase.9 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381Y → A: Impairs interaction with EIF4E. No effect on translation of HIV-1 RNA; when associated with A-43. 3 Publications
Mutagenesisi43 – 431L → A: Impairs interaction with EIF4E. Fails to induce stress granule assembly and to rescue cell viability after stress. No effect on translation of HIV-1 RNA; when associated with A-38. 3 Publications
Mutagenesisi71 – 711S → A: Reduces total phosphorylation by 60%. No effect on interaction with IKBKE. 2 Publications
Mutagenesisi82 – 832SS → AA: Reduces total phosphorylation by 50%. No effect on interaction with IKBKE. 1 Publication
Mutagenesisi84 – 852FF → AA: Abolishes interaction with VACV protein K7, IRF3 activation and IFN-beta promoter induction. 1 Publication
Mutagenesisi102 – 1021S → A: Reduces total phosphorylation by 30%. Abolishes interaction with IRF3 and fails to enhance IFNB promoter induction. No effect on interaction with IKBKE. 2 Publications
Mutagenesisi102 – 1021S → D: Interacts with IRF3 and enhances IFNB promoter induction. 2 Publications
Mutagenesisi152 – 1521S → A: Reduces total phosphorylation by 60%. No effect on interaction with IKBKE. 2 Publications
Mutagenesisi181 – 1811S → A: Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-183; A-240 and A-269. 2 Publications
Mutagenesisi183 – 1831S → A: Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-181; A-240 and A-269. 2 Publications
Mutagenesisi200 – 2001Y → A: No effect on general translation; when associated with A-207; A-230; A-347 and A-348. 2 Publications
Mutagenesisi207 – 2071Q → A: Inhibits translation of HIV-1 RNA. No effect on general translation; when associated with A-200; A-230: A-347 and A-348. 3 Publications
Mutagenesisi230 – 2301K → A: No effect on general translation; when associated with A-200; A-207; A-347 and A-348. 4 Publications
Mutagenesisi230 – 2301K → E: Abolishes ATPase activity and RNA-unwinding activity. Inhibits translation of HIV-1 RNA. 4 Publications
Mutagenesisi240 – 2401S → A: Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-181; A-183 and A-269. 2 Publications
Mutagenesisi269 – 2691S → A: Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-181; A-183 and A-240. 2 Publications
Mutagenesisi347 – 3471D → A: No effect on general translation; when associated with A-200; A-207; A-230 and A-348. 2 Publications
Mutagenesisi348 – 3481E → A: No effect on general translation; when associated with A-200; A-207; A-230 and A-347. 3 Publications
Mutagenesisi348 – 3481E → Q: Inhibits translation of HIV-1 RNA. 3 Publications
Mutagenesisi382 – 3821S → L: Abolishes ATPase activity and RNA-unwinding activity. No effect on translation of HIV-1 RNA. 3 Publications
Mutagenesisi429 – 4291S → A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-438; A-442; A-456 and A-520. 2 Publications
Mutagenesisi438 – 4381T → A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-442; A-456 and A-520. 2 Publications
Mutagenesisi442 – 4421S → A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-438; A-456 and A-520. 2 Publications
Mutagenesisi456 – 4561S → A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-438; A-442 and A-520. 2 Publications
Mutagenesisi520 – 5201S → A: Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-438; A-442 and A-456. 2 Publications

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 662661ATP-dependent RNA helicase DDX3XPRO_0000055009Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Phosphorylated by TBK1; the phosphorylation is required to synergize with TBK1 in IFNB induction. Phosphorylated by IKBKE at Ser-102 after ssRNA viral infection; enhances the induction of INFB promoter by IRF3. The cytoplasmic form is highly phosphorylated in the G1/S phase and much lower phosphorylated in G2/M.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO00571.
PaxDbiO00571.
PeptideAtlasiO00571.
PRIDEiO00571.

2D gel databases

REPRODUCTION-2DPAGEIPI00215637.
SWISS-2DPAGEO00571.

PTM databases

PhosphoSiteiO00571.

Expressioni

Inductioni

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

Gene expression databases

ArrayExpressiO00571.
BgeeiO00571.
CleanExiHS_DDX3X.
GenevestigatoriO00571.

Organism-specific databases

HPAiHPA001648.
HPA005631.

Interactioni

Subunit structurei

Interacts with XPO1, TDRD3, PABPC1, NXF1, EIF3C, MAVS, DDX58 and NCAPH. Interacts with DDX5; the interaction is regulated by the phosphorylation status of both proteins. Interacts with EIF4E; DDX3X competes with EIF4G1/EIF4G3 for interaction with EIF4E. Interacts with IKBKE; the interaction is direct, found to be induced upon virus infection. Interacts (when phosphorylated at Ser-102) with IRF3; the interaction allows the phosphorylation and activation of IRF3 by IKBKE. Interacts with TBK1. Associates with the eukaryotic translation initiation factor 3 (eIF-3) complex. Associates with the 40S ribosome. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with HCV core protein. Interacts with vaccinia virus (VACV) protein K7. Found in a complex with HIV-1 Rev and XPO1. Interacts (when phosphorylated at Ser-102) with IRF3; the interaction allows the phosphorylation and activation of IRF3 by IKBKE.19 Publications

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO00571.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini211 – 403193Helicase ATP-bindingAdd
BLAST
Domaini414 – 575162Helicase C-terminalAdd
BLAST

Region

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

Motif

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

Compositional bias

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

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

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

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

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

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

Note: No experimental confirmation available.

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

Natural variant

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei35 – 5117KGRYI…EATKG → S in isoform 2. VSP_042830Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501K → R in AAC51830. 1 Publication
Sequence conflicti50 – 501K → R in AAC51829. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U50553 mRNA. Translation: AAB95637.1.
AF061337 mRNA. Translation: AAC34298.1.
AF000983 mRNA. Translation: AAC51830.1.
AF000982 mRNA. Translation: AAC51829.1.
AK291153 mRNA. Translation: BAF83842.1.
AK304689 mRNA. Translation: BAG65460.1.
AL391647 Genomic DNA. Translation: CAI41416.1.
Z93015 Genomic DNA. No translation available.
CH471141 Genomic DNA. Translation: EAW59402.1.
CH471141 Genomic DNA. Translation: EAW59403.1.
CH471141 Genomic DNA. Translation: EAW59404.1.
CH471141 Genomic DNA. Translation: EAW59405.1.
BC011819 mRNA. Translation: AAH11819.1.
CCDSiCCDS43931.1. [O00571-1]
CCDS55404.1. [O00571-2]
RefSeqiNP_001180346.1. NM_001193417.1. [O00571-2]
NP_001347.3. NM_001356.3. [O00571-1]
UniGeneiHs.743263.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U50553 mRNA. Translation: AAB95637.1 .
AF061337 mRNA. Translation: AAC34298.1 .
AF000983 mRNA. Translation: AAC51830.1 .
AF000982 mRNA. Translation: AAC51829.1 .
AK291153 mRNA. Translation: BAF83842.1 .
AK304689 mRNA. Translation: BAG65460.1 .
AL391647 Genomic DNA. Translation: CAI41416.1 .
Z93015 Genomic DNA. No translation available.
CH471141 Genomic DNA. Translation: EAW59402.1 .
CH471141 Genomic DNA. Translation: EAW59403.1 .
CH471141 Genomic DNA. Translation: EAW59404.1 .
CH471141 Genomic DNA. Translation: EAW59405.1 .
BC011819 mRNA. Translation: AAH11819.1 .
CCDSi CCDS43931.1. [O00571-1 ]
CCDS55404.1. [O00571-2 ]
RefSeqi NP_001180346.1. NM_001193417.1. [O00571-2 ]
NP_001347.3. NM_001356.3. [O00571-1 ]
UniGenei Hs.743263.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBi O00571.
ChEMBLi CHEMBL5553.

PTM databases

PhosphoSitei O00571.

2D gel databases

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

Proteomic databases

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

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

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

Miscellaneous databases

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

Gene expression databases

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

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a human homolog of a putative RNA helicase gene (mDEAD3) expressed in mouse erythroid cells."
    Chung J., Lee S.-G., Song K.
    Korean J. Biochem. 27:193-197(1995)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Hippocampus and Liver.
  2. "Hepatitis C virus core protein interacts with a human DEAD box protein DDX3."
    Owsianka A.M., Patel A.H.
    Virology 257:330-340(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HCV CORE PROTEIN.
    Tissue: Liver.
  3. "Functional coherence of the human Y chromosome."
    Lahn B.T., Page D.C.
    Science 278:675-680(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Uterus.
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skin.
  8. "An N-acetylated natural ligand of human histocompatibility leukocyte antigen (HLA)-B39. Classical major histocompatibility complex class I proteins bind peptides with a blocked NH(2) terminus in vivo."
    Yaguee J., Alvarez I., Rognan D., Ramos M., Vazquez J., Lopez de Castro J.A.
    J. Exp. Med. 191:2083-2092(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT SER-2.
  9. "Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function."
    Yedavalli V.S., Neuveut C., Chi Y.-H., Kleiman L., Jeang K.-T.
    Cell 119:381-392(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HIV-1 RNA EXPORT/REPLICATION, IDENTIFICATION IN A COMPLEX WITH XPO1 AND REV, INTERACTION WITH XPO1, MUTAGENESIS OF LYS-230 AND SER-382, SUBCELLULAR LOCATION.
  10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "DDX3, a DEAD box RNA helicase with tumor growth-suppressive property and transcriptional regulation activity of the p21waf1/cip1 promoter, is a candidate tumor suppressor."
    Chao C.H., Chen C.M., Cheng P.L., Shih J.W., Tsou A.P., Lee Y.H.
    Cancer Res. 66:6579-6588(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SP1, SUBCELLULAR LOCATION.
  12. "DDX3, a DEAD box RNA helicase, is deregulated in hepatitis virus-associated hepatocellular carcinoma and is involved in cell growth control."
    Chang P.C., Chi C.W., Chau G.Y., Li F.Y., Tsai Y.H., Wu J.C., Wu Lee Y.H.
    Oncogene 25:1991-2003(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Human DEAD-box ATPase DDX3 shows a relaxed nucleoside substrate specificity."
    Franca R., Belfiore A., Spadari S., Maga G.
    Proteins 67:1128-1137(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Protein composition of human mRNPs spliced in vitro and differential requirements for mRNP protein recruitment."
    Merz C., Urlaub H., Will C.L., Luhrmann R.
    RNA 13:116-128(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH SPLICED MRNAS.
  15. "Identification of an antiapoptotic protein complex at death receptors."
    Sun M., Song L., Li Y., Zhou T., Jope R.S.
    Cell Death Differ. 15:1887-1900(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GSK3A; GSK3B AND TNFRSF10B.
  16. "The DEAD-box helicase DDX3X is a critical component of the TANK-binding kinase 1-dependent innate immune response."
    Soulat D., Burckstummer T., Westermayer S., Goncalves A., Bauch A., Stefanovic A., Hantschel O., Bennett K.L., Decker T., Superti-Furga G.
    EMBO J. 27:2135-2146(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION BY TBK1 AND IKBKE, MUTAGENESIS OF SER-181; SER-183; SER-240; SER-269; SER-429; THR-438; SER-442; SER-456 AND SER-520.
  17. "Viral targeting of DEAD box protein 3 reveals its role in TBK1/IKKepsilon-mediated IRF activation."
    Schroder M., Baran M., Bowie A.G.
    EMBO J. 27:2147-2157(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VACV PROTEIN K7 AND IKBKE.
  18. "TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules."
    Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.
    Hum. Mol. Genet. 17:3055-3074(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TDRD3.
  19. "The DEAD-box RNA helicase DDX3 associates with export messenger ribonucleoproteins as well as tip-associated protein and participates in translational control."
    Lai M.C., Lee Y.H., Tarn W.Y.
    Mol. Biol. Cell 19:3847-3858(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NXF1.
  20. "Human DDX3 functions in translation and interacts with the translation initiation factor eIF3."
    Lee C.S., Dias A.P., Jedrychowski M., Patel A.H., Hsu J.L., Reed R.
    Nucleic Acids Res. 36:4708-4718(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE EIF-3 COMPLEX.
  21. "Candidate tumor suppressor DDX3 RNA helicase specifically represses cap-dependent translation by acting as an eIF4E inhibitory protein."
    Shih J.W., Tsai T.Y., Chao C.H., Wu Lee Y.H.
    Oncogene 27:700-714(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EIF4E, MUTAGENESIS OF TYR-38 AND LEU-43.
  22. Cited for: FUNCTION.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
    Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
    RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  25. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "DEAD/H BOX 3 (DDX3) helicase binds the RIG-I adaptor IPS-1 to up-regulate IFN-beta-inducing potential."
    Oshiumi H., Sakai K., Matsumoto M., Seya T.
    Eur. J. Immunol. 40:940-948(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAVS AND DDX58, SUBCELLULAR LOCATION.
  27. "Hepatitis B virus polymerase inhibits RIG-I- and Toll-like receptor 3-mediated beta interferon induction in human hepatocytes through interference with interferon regulatory factor 3 activation and dampening of the interaction between TBK1/IKKepsilon and DDX3."
    Yu S., Chen J., Wu M., Chen H., Kato N., Yuan Z.
    J. Gen. Virol. 91:2080-2090(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IKBKE AND TBK1.
  28. "DDX3 regulates cell growth through translational control of cyclin E1."
    Lai M.C., Chang W.C., Shieh S.Y., Tarn W.Y.
    Mol. Cell. Biol. 30:5444-5453(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  29. "Hepatitis C virus core protein abrogates the DDX3 function that enhances IPS-1-mediated IFN-beta induction."
    Oshiumi H., Ikeda M., Matsumoto M., Watanabe A., Takeuchi O., Akira S., Kato N., Shimotohno K., Seya T.
    PLoS ONE 5:E14258-E14258(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, INTERACTION WITH MAVS, SUBCELLULAR LOCATION.
  30. "Hepatitis B virus polymerase blocks pattern recognition receptor signaling via interaction with DDX3: implications for immune evasion."
    Wang H., Ryu W.S.
    PLoS Pathog. 6:E1000986-E1000986(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IKBKE.
  31. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "A motif unique to the human DEAD-box protein DDX3 is important for nucleic acid binding, ATP hydrolysis, RNA/DNA unwinding and HIV-1 replication."
    Garbelli A., Beermann S., Di Cicco G., Dietrich U., Maga G.
    PLoS ONE 6:E19810-E19810(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  34. "DEAD-box RNA helicase Belle/DDX3 and the RNA interference pathway promote mitotic chromosome segregation."
    Pek J.W., Kai T.
    Proc. Natl. Acad. Sci. U.S.A. 108:12007-12012(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NCAPH.
  35. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "Critical roles of RNA helicase DDX3 and its interactions with eIF4E/PABP1 in stress granule assembly and stress response."
    Shih J.W., Wang W.T., Tsai T.Y., Kuo C.Y., Li H.K., Wu Lee Y.H.
    Biochem. J. 441:119-129(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF4E AND PABPC1.
  37. "The DEAD-box RNA helicase DDX3 interacts with DDX5, co-localizes with it in the cytoplasm during the G2/M phase of the cycle, and affects its shuttling during mRNP export."
    Choi Y.J., Lee S.G.
    J. Cell. Biochem. 113:985-996(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INDUCTION, INTERACTION WITH DDX5.
  38. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "The DEAD-box helicase DDX3 supports the assembly of functional 80S ribosomes."
    Geissler R., Golbik R.P., Behrens S.E.
    Nucleic Acids Res. 40:4998-5011(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH THE RIBOSOME SMALL SUBUNIT, INTERACTION WITH EIF3C, MUTAGENESIS OF TYR-200; GLN-207; LYS-230; ASP-347 AND GLU-348.
  40. "DEAD-box protein DDX3 associates with eIF4F to promote translation of selected mRNAs."
    Soto-Rifo R., Rubilar P.S., Limousin T., de Breyne S., Decimo D., Ohlmann T.
    EMBO J. 31:3745-3756(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, INTERACTION WITH EIF4G1 AND PABPC1, MUTAGENESIS OF TYR-38; LEU-43; GLN-207; LYS-230; GLU-348 AND SER-382.
  41. "Human DEAD box helicase 3 couples IkappaB kinase epsilon to interferon regulatory factor 3 activation."
    Gu L., Fullam A., Brennan R., Schroder M.
    Mol. Cell. Biol. 33:2004-2015(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS SCAFFOLD PROTEIN, INTERACTION WITH IKBKE AND IRF3, PHOSPHORYLATION AT SER-102, MUTAGENESIS OF SER-71; 82-SER-SER-83; SER-102 AND SER-152.
  42. "Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain."
    Rodamilans B., Montoya G.
    Acta Crystallogr. F 63:283-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 409-580.
  43. "Crystal structure of conserved domains 1 and 2 of the human DEAD-box helicase DDX3X in complex with the mononucleotide AMP."
    Hoegbom M., Collins R., van den Berg S., Jenvert R.-M., Karlberg T., Kotenyova T., Flores A., Karlsson Hedestam G.B., Schiavone L.H.
    J. Mol. Biol. 372:150-159(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 168-582 IN COMPLEX WITH AMP.
  44. "Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7."
    Oda S., Schroder M., Khan A.R.
    Structure 17:1528-1537(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 71-90 IN COMPLEX WITH VACV PROTEIN K7, MUTAGENESIS OF 84-PHE-PHE-85.
  45. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-294.

Entry informationi

Entry nameiDDX3X_HUMAN
AccessioniPrimary (citable) accession number: O00571
Secondary accession number(s): A8K538, B4E3E8, O15536
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 167 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3

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