O00571 (DDX3X_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DDX3X
Synonyms:	DBX, DDX3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	662 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Multifunctional ATP-dependent RNA helicase. The ATPase activity can be stimulated by various ribo- and deoxynucleic acids indicative for a relaxed substrate specificity. In vitro can unwind partially double stranded DNA with a preference for 5'-single stranded DNA overhangs. Is involved in several steps of gene expression, such as transcription, mRNA maturation, mRNA export and translation. However, the exact mechanisms are not known and some functions may be specific for a subset of mRNAs. Involved in transcriptional regulation. Can enhance transcription from the CDKN1A/WAF1 promoter in a SP1-dependent manner. Found associated with the E-cadherin promoter and can down-regulate transcription from the promoter. Involved in regulation of translation initiation. Proposed to be involved in positive regulation of translation such as of cyclin E1/CCNE1 mRNA and specifically of mRNAs containing complex secondary structures in their 5'UTRs; these functions seem to require RNA helicase activity. Specifically promotes translation of a subset of viral and cellular mRNAs carrying a 5'proximal stem-loop structure in their 5'UTRs and cooperates with the eIF4F complex. Proposed to act prior to 43S ribosomal scanning and to locally destabilize these RNA structures to allow recognition of the mRNA cap or loading onto the 40S subunit. After association with 40S ribosomal subunits seems to be involved in the functional assembly of 80S ribosomes; the function seems to cover translation of mRNAs with structured and non-structured 5'UTRs and is independent of RNA helicase activity. Also proposed to inhibit cap-dependent translation by competetive interaction with EIF4E which can block the EIF4E:EIF4G complex formation. Proposed to be involved in stress response and stress granule assembly; the function is independent of RNA helicase activity and seems to involve association with EIF4E. May be involved in nuclear export of specific mRNAs but not in bulk mRNA export via interactions with XPO1 and NXF1. Also associates with polyadenylated mRNAs independently of NXF1. Associates with spliced mRNAs in an exon junction complex (EJC)-dependent manner and seems not to be directly involved in splicing. May be involved in nuclear mRNA export by association with DDX5 and regulating its nuclear location. Involved in innate immune signaling promoting the production of type I interferon (IFN-alpha and IFN-beta); proposed to act as viral RNA sensor, signaling intermediate and transcriptional coactivator. Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFN-beta induction. Also found associated with IFN-beta 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 IFN-beta 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 INF-beta inducing to a HCV replication mode. Involved in HIV-1 replication. Acts as a cofactor for XPO1-mediated nuclear export of incompletely spliced HIV-1 Rev RNAs. Ref.2 Ref.9 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.33 Ref.34 Ref.36 Ref.37 Ref.38 Ref.39
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Interacts with XPO1, TDRD3, PABPC1, NXF1, EIF3C, MAVS, DDX58 and NCAPH. Interacts with DDX5; the interaction is regulated by the phosphorylation status of both proteins. Interacts with EIF4E; DDX3X competes with EIF4G1/EIF4G3 for interaction with EIF4E. Interacts with IKBKE; the interaction is found to be induced upon virus infection and to be inhibited by HBV polymerase. Interacts with TBK1; the interaction is inhibited by HBV polymerase. 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. Ref.2 Ref.9 Ref.11 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21 Ref.24 Ref.26 Ref.27 Ref.29 Ref.30 Ref.34 Ref.36 Ref.37 Ref.38 Ref.39
Subcellular location	Nucleus speckle. Cytoplasm. Mitochondrion outer membrane. Note: Located predominantly in nuclear speckles and, at low levels, throughout the cytoplasm. Located to the outer side of nuclear pore complexes (NPC). Shuttles between the nucleus and the cytoplasm in a XPO1 and may be also in a NFX1-dependent manner. Associated with polyadenylated mRNAs in the cytoplasm and the nucleus. Predominantly located in nucleus during G0 phase and in the cytoplasm during G1/S phase. Ref.2 Ref.9 Ref.11 Ref.19 Ref.20 Ref.26 Ref.29 Ref.36 Ref.37
Induction	Regulated by the cell cycle. Maximally expressed din the cytoplasm uring G1/S phase and decreased expression during G2/M phase. Ref.37
Post-translational modification	Phosphorylated by TBK1; the phosphorylation is required to synergize with TBK1 in IFN-beta induction. Probably also phosphorylated by IKBKE. The cytoplasmic form is highly phosphorylated in the G1/S phase and much lower phosphorylated in G2/M. Ref.16 Ref.37
Sequence similarities	Belongs to the DEAD box helicase family. DDX3/DED1 subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.

Ontologies

Keywords
Biological process	Apoptosis Chromosome partition Host-virus interaction Immunity Innate immunity Ribosome biogenesis Transcription Transcription regulation Translation regulation
Cellular component	Cytoplasm Membrane Mitochondrion Mitochondrion outer membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA secondary structure unwinding Inferred from direct assay Ref.39. Source: UniProtKB cellular response to arsenic-containing substance Inferred from direct assay Ref.36. Source: UniProtKB cellular response to osmotic stress Inferred from direct assay Ref.36. Source: UniProtKB chromosome segregation Inferred from mutant phenotype Ref.34. Source: UniProtKB extrinsic apoptotic signaling pathway via death domain receptors Inferred from mutant phenotype Ref.15. Source: UniProtKB innate immune response Inferred from mutant phenotype Ref.16. Source: UniProtKB intracellular protein kinase cascade Inferred from direct assay Ref.17. Source: UniProtKB intrinsic apoptotic signaling pathway Inferred from mutant phenotype Ref.12. Source: UniProtKB mature ribosome assembly Inferred from mutant phenotype Ref.38. Source: UniProtKB negative regulation of apoptotic process Inferred from mutant phenotype Ref.15. Source: UniProtKB negative regulation of cell growth Inferred from direct assay Ref.11. Source: UniProtKB negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from mutant phenotype Ref.15. Source: UniProtKB negative regulation of intrinsic apoptotic signaling pathway Inferred from mutant phenotype Ref.36. Source: UniProtKB negative regulation of protein complex assembly Inferred from direct assay Ref.21. Source: UniProtKB negative regulation of translation Inferred from mutant phenotype Ref.21. Source: UniProtKB positive regulation of G1/S transition of mitotic cell cycle Inferred from mutant phenotype Ref.28. Source: UniProtKB positive regulation of apoptotic process Inferred from mutant phenotype Ref.12. Source: UniProtKB positive regulation of cell growth Inferred from mutant phenotype Ref.20Ref.28. Source: UniProtKB positive regulation of chemokine (C-C motif) ligand 5 production Traceable author statement Ref.16. Source: UniProtKB positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from mutant phenotype Ref.12. Source: UniProtKB positive regulation of interferon-beta production Traceable author statement Ref.16Ref.17. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.11Ref.17. Source: UniProtKB positive regulation of translational initiation Inferred from mutant phenotype Ref.28. Source: UniProtKB response to virus Inferred from direct assay Ref.17. Source: UniProtKB stress granule assembly Inferred from direct assay Ref.36. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasmic stress granule Inferred from direct assay Ref.19Ref.36. Source: UniProtKB mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent DNA helicase activity Inferred from direct assay Ref.33. Source: UniProtKB ATP-dependent RNA helicase activity Inferred from direct assay Ref.33. Source: UniProtKB DNA binding Inferred from direct assay Ref.33. Source: UniProtKB RNA stem-loop binding Inferred from direct assay Ref.39. Source: UniProtKB eukaryotic initiation factor 4E binding Inferred from direct assay Ref.21. Source: UniProtKB mRNA 5'-UTR binding Inferred from direct assay Ref.39. Source: UniProtKB poly(A) RNA binding Inferred from direct assay Ref.19. Source: UniProtKB ribosomal small subunit binding Inferred from direct assay Ref.38. Source: UniProtKB transcription factor binding Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDX58	O95786	2	EBI-353779,EBI-995350
EIF2S1	P05198	3	EBI-353779,EBI-1056162
EIF3B	P55884	5	EBI-353779,EBI-366696
EIF3CL	Q99613	3	EBI-353779,EBI-353741
MAVS	Q7Z434	4	EBI-353779,EBI-995373
NCAPH	Q15003	2	EBI-353779,EBI-1046410
NXF1	Q9UBU9	5	EBI-353779,EBI-398874
PABPC1	P11940	9	EBI-353779,EBI-81531

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O00571-1)

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

Isoform 2 (identifier: O00571-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 662

661

ATP-dependent RNA helicase DDX3X

PRO_0000055009

Regions

Domain

211 – 403

193

Helicase ATP-binding

Domain

414 – 575

162

Helicase C-terminal

Nucleotide binding

200 – 207

8

ATP

Nucleotide binding

224 – 231

8

ATP

Region

2 – 139

138

Required for TBK1 and IKBKE-depenedent IFN-beta activation

Region

2 – 100

99

Interaction with EIF4E

Region

81 – 90

10

Required for interaction with VACV protein K7

Region

100 – 662

563

Interaction with GSK3B

Region

250 – 259

10

Involved in stimulation of ATPase activity by DNA and RNA, nucleic acid binding and unwinding and HIV-1 replication

Region

260 – 517

258

Necessary for interaction with XPO1

Motif

180 – 208

29

Q motif

Motif

347 – 350

4

DEAD box

Compositional bias

582 – 662

81

Gly/Ser-rich

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.8 Ref.31

Modified residue

69

1

Phosphotyrosine

Modified residue

74

1

Phosphoserine

Modified residue

76

1

Phosphoserine

Modified residue

78

1

Phosphoserine

Modified residue

104

1

Phosphotyrosine

Modified residue

118

1

N6-acetyllysine Ref.25

Modified residue

125

1

Phosphoserine

Modified residue

131

1

Phosphoserine Ref.35

Modified residue

343

1

Phosphotyrosine

Modified residue

590

1

Phosphoserine

Modified residue

594

1

Phosphoserine

Modified residue

612

1

Phosphoserine Ref.23

Natural variations

Alternative sequence

35 – 51

17

KGRYI…EATKG → S in isoform 2.

VSP_042830

Natural variant

294

1

R → T in a breast cancer sample; somatic mutation. Ref.43

VAR_035839

Experimental info

Mutagenesis

38

1

Y → A: Impairs interaction with EIF4E. No effect on translation of HIV-1 RNA; when associated with A-43. Ref.21 Ref.39 Ref.42

Mutagenesis

43

1

L → A: Impairs interaction with EIF4E. Fails to induce stress granule assembly and to rescue cell viability after stress. No effect on translation of HIV-1 RNA; when associated with A-38. Ref.21 Ref.39 Ref.42

Mutagenesis

84 – 85

2

FF → AA: Abolishes interaction with VACV protein K7, IRF3 activation and IFN-beta promoter induction. Ref.42

Mutagenesis

181

1

S → A: Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-183; A-240 and A-269. Ref.16 Ref.42

Mutagenesis

183

1

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. Ref.16 Ref.42

Mutagenesis

200

1

Y → A: No effect on general translation; when associated with A-207; A-230; A-347 and A-348. Ref.38 Ref.42

Mutagenesis

207

1

Q → A: Inhibits translation of HIV-1 RNA. No effect on general translation; when associated with A-200; A-230: A-347 and A-348. Ref.38 Ref.39 Ref.42

Mutagenesis

230

1

K → A: No effect on general translation; when associated with A-200; A-207; A-347 and A-348. Ref.9 Ref.38 Ref.39 Ref.42

Mutagenesis

230

1

K → E: Abolishes ATPase activity and RNA-unwinding activity. Inhibits translation of HIV-1 RNA. Ref.9 Ref.38 Ref.39 Ref.42

Mutagenesis

240

1

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. Ref.16 Ref.42

Mutagenesis

269

1

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. Ref.16 Ref.42

Mutagenesis

347

1

D → A: No effect on general translation; when associated with A-200; A-207; A-230 and A-348. Ref.38 Ref.42

Mutagenesis

348

1

E → A: No effect on general translation; when associated with A-200; A-207; A-230 and A-347. Ref.38 Ref.39 Ref.42

Mutagenesis

348

1

E → Q: Inhibits translation of HIV-1 RNA. Ref.38 Ref.39 Ref.42

Mutagenesis

382

1

S → L: Abolishes ATPase activity and RNA-unwinding activity. No effect on translation of HIV-1 RNA. Ref.9 Ref.39 Ref.42

Mutagenesis

429

1

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. Ref.16 Ref.42

Mutagenesis

438

1

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. Ref.16 Ref.42

Mutagenesis

442

1

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. Ref.16 Ref.42

Mutagenesis

456

1

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. Ref.16 Ref.42

Mutagenesis

520

1

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. Ref.16 Ref.42

Sequence conflict

50

1

K → R in AAC51830. Ref.3

Sequence conflict

50

1

K → R in AAC51829. Ref.3

Secondary structure

1

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662

Helix Strand Turn

Details...

Beta strand

168 – 172

5

Helix

182 – 184

3

Helix

189 – 198

10

Helix

205 – 215

11

Beta strand

220 – 223

4

Helix

230 – 245

16

Helix

249 – 256

8

Beta strand

268 – 272

5

Helix

276 – 290

15

Beta strand

297 – 300

4

Beta strand

302 – 304

3

Helix

306 – 313

8

Beta strand

318 – 322

5

Helix

324 – 332

9

Beta strand

343 – 348

6

Helix

349 – 354

6

Helix

358 – 365

8

Beta strand

367 – 369

3

Beta strand

376 – 383

8

Helix

387 – 396

10

Beta strand

401 – 405

5

Beta strand

415 – 421

7

Helix

424 – 426

3

Helix

427 – 437

11

Beta strand

444 – 449

6

Helix

451 – 463

13

Beta strand

468 – 471

4

Helix

482 – 488

7

Beta strand

491 – 498

8

Helix

499 – 502

4

Beta strand

509 – 517

9

Helix

522 – 529

8

Beta strand

539 – 545

7

Helix

547 – 552

6

Helix

553 – 562

10

Helix

569 – 575

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 7074D2B8A6EBBF09	FASTA	662	73,243
	10 20 30 40 50 60 MSHVAVENAL GLDQQFAGLD LNSSDNQSGG STASKGRYIP PHLRNREATK GFYDKDSSGW 70 80 90 100 110 120 SSSKDKDAYS SFGSRSDSRG KSSFFSDRGS GSRGRFDDRG RSDYDGIGSR GDRSGFGKFE 130 140 150 160 170 180 RGGNSRWCDK SDEDDWSKPL PPSERLEQEL FSGGNTGINF EKYDDIPVEA TGNNCPPHIE 190 200 210 220 230 240 SFSDVEMGEI IMGNIELTRY TRPTPVQKHA IPIIKEKRDL MACAQTGSGK TAAFLLPILS 250 260 270 280 290 300 QIYSDGPGEA LRAMKENGRY GRRKQYPISL VLAPTRELAV QIYEEARKFS YRSRVRPCVV 310 320 330 340 350 360 YGGADIGQQI RDLERGCHLL VATPGRLVDM MERGKIGLDF CKYLVLDEAD RMLDMGFEPQ 370 380 390 400 410 420 IRRIVEQDTM PPKGVRHTMM FSATFPKEIQ MLARDFLDEY IFLAVGRVGS TSENITQKVV 430 440 450 460 470 480 WVEESDKRSF LLDLLNATGK DSLTLVFVET KKGADSLEDF LYHEGYACTS IHGDRSQRDR 490 500 510 520 530 540 EEALHQFRSG KSPILVATAV AARGLDISNV KHVINFDLPS DIEEYVHRIG RTGRVGNLGL 550 560 570 580 590 600 ATSFFNERNI NITKDLLDLL VEAKQEVPSW LENMAYEHHY KGSSRGRSKS SRFSGGFGAR 610 620 630 640 650 660 DYRQSSGASS SSFSSSRASS SRSGGGGHGS SRGFGGGGYG GFYNSDGYGG NYNSQGVDWW GN
	Isoform 2 [UniParc]. Checksum: A8E9EB966FC6C617	FASTA	646	71,355
	10 20 30 40 50 60 MSHVAVENAL GLDQQFAGLD LNSSDNQSGG STASSFYDKD SSGWSSSKDK DAYSSFGSRS 70 80 90 100 110 120 DSRGKSSFFS DRGSGSRGRF DDRGRSDYDG IGSRGDRSGF GKFERGGNSR WCDKSDEDDW 130 140 150 160 170 180 SKPLPPSERL EQELFSGGNT GINFEKYDDI PVEATGNNCP PHIESFSDVE MGEIIMGNIE 190 200 210 220 230 240 LTRYTRPTPV QKHAIPIIKE KRDLMACAQT GSGKTAAFLL PILSQIYSDG PGEALRAMKE 250 260 270 280 290 300 NGRYGRRKQY PISLVLAPTR ELAVQIYEEA RKFSYRSRVR PCVVYGGADI GQQIRDLERG 310 320 330 340 350 360 CHLLVATPGR LVDMMERGKI GLDFCKYLVL DEADRMLDMG FEPQIRRIVE QDTMPPKGVR 370 380 390 400 410 420 HTMMFSATFP KEIQMLARDF LDEYIFLAVG RVGSTSENIT QKVVWVEESD KRSFLLDLLN 430 440 450 460 470 480 ATGKDSLTLV FVETKKGADS LEDFLYHEGY ACTSIHGDRS QRDREEALHQ FRSGKSPILV 490 500 510 520 530 540 ATAVAARGLD ISNVKHVINF DLPSDIEEYV HRIGRTGRVG NLGLATSFFN ERNINITKDL 550 560 570 580 590 600 LDLLVEAKQE VPSWLENMAY EHHYKGSSRG RSKSSRFSGG FGARDYRQSS GASSSSFSSS 610 620 630 640 RASSSRSGGG GHGSSRGFGG GGYGGFYNSD GYGGNYNSQG VDWWGN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a human homolog of a putative RNA helicase gene (mDEAD3) expressed in mouse erythroid cells." Chung J., Lee S.-G., Song K. Korean J. Biochem. 27:193-197(1995) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Hippocampus and Liver.
[2]	"Hepatitis C virus core protein interacts with a human DEAD box protein DDX3." Owsianka A.M., Patel A.H. Virology 257:330-340(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HCV CORE PROTEIN. Tissue: Liver.
[3]	"Functional coherence of the human Y chromosome." Lahn B.T., Page D.C. Science 278:675-680(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin.
[8]	"An N-acetylated natural ligand of human histocompatibility leukocyte antigen (HLA)-B39. Classical major histocompatibility complex class I proteins bind peptides with a blocked NH(2) terminus in vivo." Yaguee J., Alvarez I., Rognan D., Ramos M., Vazquez J., Lopez de Castro J.A. J. Exp. Med. 191:2083-2092(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT SER-2.
[9]	"Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function." Yedavalli V.S., Neuveut C., Chi Y.-H., Kleiman L., Jeang K.-T. Cell 119:381-392(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HIV-1 RNA EXPORT/REPLICATION, IDENTIFICATION IN A COMPLEX WITH XPO1 AND REV, INTERACTION WITH XPO1, MUTAGENESIS OF LYS-230 AND SER-382, SUBCELLULAR LOCATION.
[10]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"DDX3, a DEAD box RNA helicase with tumor growth-suppressive property and transcriptional regulation activity of the p21waf1/cip1 promoter, is a candidate tumor suppressor." Chao C.H., Chen C.M., Cheng P.L., Shih J.W., Tsou A.P., Lee Y.H. Cancer Res. 66:6579-6588(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SP1, SUBCELLULAR LOCATION.
[12]	"DDX3, a DEAD box RNA helicase, is deregulated in hepatitis virus-associated hepatocellular carcinoma and is involved in cell growth control." Chang P.C., Chi C.W., Chau G.Y., Li F.Y., Tsai Y.H., Wu J.C., Wu Lee Y.H. Oncogene 25:1991-2003(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Human DEAD-box ATPase DDX3 shows a relaxed nucleoside substrate specificity." Franca R., Belfiore A., Spadari S., Maga G. Proteins 67:1128-1137(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Protein composition of human mRNPs spliced in vitro and differential requirements for mRNP protein recruitment." Merz C., Urlaub H., Will C.L., Luhrmann R. RNA 13:116-128(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH SPLICED MRNAS.
[15]	"Identification of an antiapoptotic protein complex at death receptors." Sun M., Song L., Li Y., Zhou T., Jope R.S. Cell Death Differ. 15:1887-1900(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH GSK3A; GSK3B AND TNFRSF10B.
[16]	"The DEAD-box helicase DDX3X is a critical component of the TANK-binding kinase 1-dependent innate immune response." Soulat D., Burckstummer T., Westermayer S., Goncalves A., Bauch A., Stefanovic A., Hantschel O., Bennett K.L., Decker T., Superti-Furga G. EMBO J. 27:2135-2146(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION BY TBK1 AND IKBKE, MUTAGENESIS OF SER-181; SER-183; SER-240; SER-269; SER-429; THR-438; SER-442; SER-456 AND SER-520.
[17]	"Viral targeting of DEAD box protein 3 reveals its role in TBK1/IKKepsilon-mediated IRF activation." Schroder M., Baran M., Bowie A.G. EMBO J. 27:2147-2157(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH VACV PROTEIN K7 AND IKBKE.
[18]	"TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules." Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J. Hum. Mol. Genet. 17:3055-3074(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TDRD3.
[19]	"The DEAD-box RNA helicase DDX3 associates with export messenger ribonucleoproteins as well as tip-associated protein and participates in translational control." Lai M.C., Lee Y.H., Tarn W.Y. Mol. Biol. Cell 19:3847-3858(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NXF1.
[20]	"Human DDX3 functions in translation and interacts with the translation initiation factor eIF3." Lee C.S., Dias A.P., Jedrychowski M., Patel A.H., Hsu J.L., Reed R. Nucleic Acids Res. 36:4708-4718(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE EIF-3 COMPLEX.
[21]	"Candidate tumor suppressor DDX3 RNA helicase specifically represses cap-dependent translation by acting as an eIF4E inhibitory protein." Shih J.W., Tsai T.Y., Chao C.H., Wu Lee Y.H. Oncogene 27:700-714(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EIF4E, MUTAGENESIS OF TYR-38 AND LEU-43.
[22]	"Oncogenic role of DDX3 in breast cancer biogenesis." Botlagunta M., Vesuna F., Mironchik Y., Raman A., Lisok A., Winnard P. Jr., Mukadam S., Van Diest P., Chen J.H., Farabaugh P., Patel A.H., Raman V. Oncogene 27:3912-3922(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[32]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]	"A motif unique to the human DEAD-box protein DDX3 is important for nucleic acid binding, ATP hydrolysis, RNA/DNA unwinding and HIV-1 replication." Garbelli A., Beermann S., Di Cicco G., Dietrich U., Maga G. PLoS ONE 6:E19810-E19810(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[34]	"DEAD-box RNA helicase Belle/DDX3 and the RNA interference pathway promote mitotic chromosome segregation." Pek J.W., Kai T. Proc. Natl. Acad. Sci. U.S.A. 108:12007-12012(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH NCAPH.
[35]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, MASS SPECTROMETRY.
[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]	"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.
[39]	"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.
[40]	"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.
[41]	"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.
[42]	"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.
[43]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-294.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U50553 mRNA. Translation: AAB95637.1.
AF061337 mRNA. Translation: AAC34298.1.
AF000983 mRNA. Translation: AAC51830.1.
AF000982 mRNA. Translation: AAC51829.1.
AK291153 mRNA. Translation: BAF83842.1.
AK304689 mRNA. Translation: BAG65460.1.
AL391647 Genomic DNA. Translation: CAI41416.1.
Z93015 Genomic DNA. No translation available.
CH471141 Genomic DNA. Translation: EAW59402.1.
CH471141 Genomic DNA. Translation: EAW59403.1.
CH471141 Genomic DNA. Translation: EAW59404.1.
CH471141 Genomic DNA. Translation: EAW59405.1.
BC011819 mRNA. Translation: AAH11819.1.

IPI

IPI00215637.
IPI00985384.

RefSeq

NP_001180346.1. NM_001193417.1.
NP_001347.3. NM_001356.3.

UniGene

Hs.380774.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2I4I	X-ray	2.20	A	168-581	[»]
2JGN	X-ray	1.91	A/B/C	409-579	[»]
3JRV	X-ray	1.60	C/D/E	71-90	[»]

ProteinModelPortal

O00571.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27551N.

IntAct

O00571. 57 interactions.

MINT

MINT-93217.

STRING

9606.ENSP00000382840.

PTM databases

PhosphoSite

O00571.

2D gel databases

REPRODUCTION-2DPAGE

IPI00215637.

SWISS-2DPAGE

O00571.

Proteomic databases

PaxDb

O00571.

PeptideAtlas

O00571.

PRIDE

O00571.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000399959; ENSP00000382840; ENSG00000215301.
ENST00000457138; ENSP00000392494; ENSG00000215301.

GeneID

1654.

KEGG

hsa:1654.

UCSC

uc004dfe.3. human.

Organism-specific databases

CTD

1654.

GeneCards

GC0XP041192.

HGNC

HGNC:2745. DDX3X.

HPA

HPA001648.
HPA005631.

MIM

300160. gene.

neXtProt

NX_O00571.

PharmGKB

PA27216.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0513.

HOVERGEN

HBG015893.

InParanoid

O00571.

KO

K11594.

OMA

KYERGGN.

OrthoDB

EOG47D9FV.

PhylomeDB

O00571.

Gene expression databases

ArrayExpress

O00571.

Bgee

O00571.

CleanEx

HS_DDX3X.

Genevestigator

O00571.

GermOnline

ENSG00000124487. Homo sapiens.

Family and domain databases

InterPro

IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]

Pfam

PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

PROSITE

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]

ProtoNet

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Other

BindingDB

O00571.

ChEMBL

CHEMBL5553.

ChiTaRS

DDX3X. human.

EvolutionaryTrace

O00571.

GenomeRNAi

1654.

NextBio

6810.

SOURCE

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Entry information

Entry name

DDX3X_HUMAN

Accession

Primary (citable) accession number: O00571
Secondary accession number(s): A8K538, B4E3E8, O15536

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 152 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.