DDX3X: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''ATP-dependent [[:en:Helicase#RNA helicases|RNA helicase]] DDX3X''' is an [[enzyme]] that in humans is encoded by the ''DDX3X'' [[gene]].<ref name="pmid9381176">{{cite journal | vauthors = Lahn BT, Page DC | title = Functional coherence of the human Y chromosome | journal = Science | volume = 278 | issue = 5338 | pages = 675–80 | date = October 1997 | pmid = 9381176 | pmc =  | doi = 10.1126/science.278.5338.675 }}</ref><ref name="pmid9730595">{{cite journal | vauthors = Park SH, Lee SG, Kim Y, Song K | title = Assignment of a human putative RNA helicase gene, DDX3, to human X chromosome bands p11.3→p11.23 | journal = Cytogenetics and Cell Genetics | volume = 81 | issue = 3–4 | pages = 178–9 | date = Oct 1998 | pmid = 9730595 | pmc = | doi = 10.1159/000015022 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DDX3X DEAD (Asp-Glu-Ala-Asp) box polypeptide 3, X-linked| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1654 }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_DDX3X_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2i4i.
| PDB = {{PDB2|2i4i}}
| Name = DEAD (Asp-Glu-Ala-Asp) box polypeptide 3, X-linked
| HGNCid = 2745
| Symbol = DDX3X
| AltSymbols =; DBX; DDX14; DDX3; HLP2
| OMIM = 300160
| ECnumber = 
| Homologene = 3425
| MGIid = 103064
| GeneAtlas_image1 = PBB_GE_DDX3X_201210_at_tn.png
| GeneAtlas_image2 = PBB_GE_DDX3X_201211_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_DDX3X_212514_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0004004 |text = ATP-dependent RNA helicase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1654
    | Hs_Ensembl = ENSG00000124487
    | Hs_RefseqProtein = XP_001129278
    | Hs_RefseqmRNA = XM_001129278
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = X
    | Hs_GenLoc_start = 41077595
    | Hs_GenLoc_end = 41108669
    | Hs_Uniprot = O00571
    | Mm_EntrezGene = 13205
    | Mm_Ensembl = ENSMUSG00000000787
    | Mm_RefseqmRNA = XM_981517
    | Mm_RefseqProtein = XP_986611
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = X
    | Mm_GenLoc_start = 12437997
    | Mm_GenLoc_end = 12449573
    | Mm_Uniprot = Q3TQX5
  }}
}}
'''DEAD (Asp-Glu-Ala-Asp) box polypeptide 3, X-linked''', also known as '''DDX3X''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DDX3X DEAD (Asp-Glu-Ala-Asp) box polypeptide 3, X-linked| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1654| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[DExD/H box proteins|DEAD box proteins]], characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA [[helicase]]s. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as [[Eukaryotic translation#initiation|translation initiation]], nuclear and mitochondrial [[RNA splicing|splicing]], and [[ribosome]] and [[spliceosome]] assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which interacts specifically with hepatitis C virus core protein resulting a change in intracellular location. This gene has a homolog located in the nonrecombining region of the Y chromosome. The protein sequence is 91% identical between this gene and the Y-linked homolog.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which interacts specifically with hepatitis C virus core protein resulting a change in intracellular location. This gene has a homolog located in the nonrecombining region of the Y chromosome. The protein sequence is 91% identical between this gene and the Y-linked homolog.<ref name="entrez">{{cite web | title = Entrez Gene: DDX3X DEAD (Asp-Glu-Ala-Asp) box polypeptide 3, X-linked| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1654| accessdate = }}</ref>
}}


==References==
== Role in cancer ==
{{reflist|2}}
 
==Further reading==
DDX3X is involved in many different types of cancer. For example, it is abnormally expressed in breast epithelial cancer cells in which its expression is activated by [[:en:HIF1A|HIF1A]] during [[:en:Tumor hypoxia|hypoxia]].<ref name=":0">{{cite journal | vauthors = Botlagunta M, Krishnamachary B, Vesuna F, Winnard PT, Bol GM, Patel AH, Raman V | title = Expression of DDX3 is directly modulated by hypoxia inducible factor-1 alpha in breast epithelial cells | journal = PLOS One | volume = 6 | issue = 3 | pages = e17563 | date = March 2011 | pmid = 21448281 | doi = 10.1371/journal.pone.0017563 | website =  | publisher = PLOS One | pmc=3063174}}</ref> Increased expression of DDX3X by HIF1A in hypoxia is initiated by the direct binding of HIF1A to the HIF1A [[:en:Transcription factor#Response elements|response element]],<ref name=":0" /> as verified with [[:en:Chromatin immunoprecipitation|chromatin immunoprecipitation]] and [[:en:Luciferase|luciferase reporter assay]]. Since the expression of DDX3X is affected by the activity of HIF1A, the co-localization of these proteins has also been demonstrated in [[MDA-MB-231]] [[:en:Xenograft|xenograft]] tumor samples.<ref name=":0" />
 
In [[:en:HeLa|HeLa cells]] DDX3X is reported to control cell cycle progression through [[:en:Cyclin E1|Cyclin E1]].<ref name=":1">{{cite journal | vauthors = Lai MC, Chang WC, Shieh SY, Tarn WY | title = DDX3 regulates cell growth through translational control of cyclin E1 | journal = Molecular and Cellular Biology | volume = 30 | issue = 22 | pages = 5444–53 | date = November 2010 | pmid = 20837705 | doi = 10.1128/MCB.00560-10 | url = http://mcb.asm.org/content/30/22/5444.long | website =  | publisher = Molecular and Cellular Biology | pmc=2976371}}</ref> More specifically, DDX3X was shown to directly bind to the [[:en:Five prime untranslated region|5´ UTR]] of Cyclin E1 and thereby facilitating the translation of the protein. Increased protein levels of Cyclin E1 was demonstrated to mediate the transition of [[:en:S phase|S phase]] entry.<ref name=":1" />
 
== Clinical significance ==
 
Mutations of the ''DDX3X'' gene are also associated with [[medulloblastoma]].<ref>{{cite journal | vauthors = Robinson G, Parker M, Kranenburg TA, Lu C, Chen X, Ding L, Phoenix TN, Hedlund E, Wei L, Zhu X, Chalhoub N, Baker SJ, Huether R, Kriwacki R, Curley N, Thiruvenkatam R, Wang J, Wu G, Rusch M, Hong X, Becksfort J, Gupta P, Ma J, Easton J, Vadodaria B, Onar-Thomas A, Lin T, Li S, Pounds S, Paugh S, Zhao D, Kawauchi D, Roussel MF, Finkelstein D, Ellison DW, Lau CC, Bouffet E, Hassall T, Gururangan S, Cohn R, Fulton RS, Fulton LL, Dooling DJ, Ochoa K, Gajjar A, Mardis ER, Wilson RK, Downing JR, Zhang J, Gilbertson RJ | display-authors = 6 | title = Novel mutations target distinct subgroups of medulloblastoma | journal = Nature | volume = 488 | issue = 7409 | pages = 43–8 | date = August 2012 | pmid = 22722829 | doi = 10.1038/nature11213 | pmc=3412905}}</ref><ref>{{cite journal | vauthors = Jones DT, Jäger N, Kool M, Zichner T, Hutter B, Sultan M, Cho YJ, Pugh TJ, Hovestadt V, Stütz AM, Rausch T, Warnatz HJ, Ryzhova M, Bender S, Sturm D, Pleier S, Cin H, Pfaff E, Sieber L, Wittmann A, Remke M, Witt H, Hutter S, Tzaridis T, Weischenfeldt J, Raeder B, Avci M, Amstislavskiy V, Zapatka M, Weber UD, Wang Q, Lasitschka B, Bartholomae CC, Schmidt M, von Kalle C, Ast V, Lawerenz C, Eils J, Kabbe R, Benes V, van Sluis P, Koster J, Volckmann R, Shih D, Betts MJ, Russell RB, Coco S, Tonini GP, Schüller U, Hans V, Graf N, Kim YJ, Monoranu C, Roggendorf W, Unterberg A, Herold-Mende C, Milde T, Kulozik AE, von Deimling A, Witt O, Maass E, Rössler J, Ebinger M, Schuhmann MU, Frühwald MC, Hasselblatt M, Jabado N, Rutkowski S, von Bueren AO, Williamson D, Clifford SC, McCabe MG, Collins VP, Wolf S, Wiemann S, Lehrach H, Brors B, Scheurlen W, Felsberg J, Reifenberger G, Northcott PA, Taylor MD, Meyerson M, Pomeroy SL, Yaspo ML, Korbel JO, Korshunov A, Eils R, Pfister SM, Lichter P | display-authors = 6 | title = Dissecting the genomic complexity underlying medulloblastoma | journal = Nature | volume = 488 | issue = 7409 | pages = 100–5 | date = August 2012 | pmid = 22832583 | pmc = 3662966 | doi = 10.1038/nature11284 }}</ref><ref>{{cite journal | vauthors = Pugh TJ, Weeraratne SD, Archer TC, Pomeranz Krummel DA, Auclair D, Bochicchio J, Carneiro MO, Carter SL, Cibulskis K, Erlich RL, Greulich H, Lawrence MS, Lennon NJ, McKenna A, Meldrim J, Ramos AH, Ross MG, Russ C, Shefler E, Sivachenko A, Sogoloff B, Stojanov P, Tamayo P, Mesirov JP, Amani V, Teider N, Sengupta S, Francois JP, Northcott PA, Taylor MD, Yu F, Crabtree GR, Kautzman AG, Gabriel SB, Getz G, Jäger N, Jones DT, Lichter P, Pfister SM, Roberts TM, Meyerson M, Pomeroy SL, Cho YJ | display-authors = 6 | title = Medulloblastoma exome sequencing uncovers subtype-specific somatic mutations | journal = Nature | volume = 488 | issue = 7409 | pages = 106–10 | date = August 2012 | pmid = 22820256 | pmc = 3413789 | doi = 10.1038/nature11329 }}</ref>
 
== See also ==
 
*[[Eukaryotic translation]]
*[[DExD/H box proteins]]
*[[DHX29]]
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Li L, Li HS, Pauza CD, Bukrinsky M, Zhao RY | title = Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions | journal = Cell Research | volume = 15 | issue = 11–12 | pages = 923–34 | year = 2006 | pmid = 16354571 | doi = 10.1038/sj.cr.7290370 }}
| citations =
* {{cite journal | vauthors = Owsianka AM, Patel AH | title = Hepatitis C virus core protein interacts with a human DEAD box protein DDX3 | journal = Virology | volume = 257 | issue = 2 | pages = 330–40 | date = May 1999 | pmid = 10329544 | doi = 10.1006/viro.1999.9659 }}
*{{cite journal | author=Li L, Li HS, Pauza CD, ''et al.'' |title=Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions. |journal=Cell Res. |volume=15 |issue= 11-12 |pages= 923-34 |year= 2006 |pmid= 16354571 |doi= 10.1038/sj.cr.7290370 }}
* {{cite journal | vauthors = Mamiya N, Worman HJ | title = Hepatitis C virus core protein binds to a DEAD box RNA helicase | journal = The Journal of Biological Chemistry | volume = 274 | issue = 22 | pages = 15751–6 | date = May 1999 | pmid = 10336476 | doi = 10.1074/jbc.274.22.15751 }}
*{{cite journal | author=Lahn BT, Page DC |title=Functional coherence of the human Y chromosome. |journal=Science |volume=278 |issue= 5338 |pages= 675-80 |year= 1997 |pmid= 9381176 |doi=  }}
* {{cite journal | vauthors = Yagüe J, Alvarez I, Rognan D, Ramos M, Vázquez J, de Castro JA | title = 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 | journal = The Journal of Experimental Medicine | volume = 191 | issue = 12 | pages = 2083–92 | date = June 2000 | pmid = 10859333 | pmc = 2193201 | doi = 10.1084/jem.191.12.2083 }}
*{{cite journal  | author=Park SH, Lee SG, Kim Y, Song K |title=Assignment of a human putative RNA helicase gene, DDX3, to human X chromosome bands p11.3-->p11.23. |journal=Cytogenet. Cell Genet. |volume=81 |issue= 3-4 |pages= 178-9 |year= 1998 |pmid= 9730595 |doi=  }}
* {{cite journal | vauthors = Kim YS, Lee SG, Park SH, Song K | title = Gene structure of the human DDX3 and chromosome mapping of its related sequences | journal = Molecules and Cells | volume = 12 | issue = 2 | pages = 209–14 | date = October 2001 | pmid = 11710523 | doi =  }}
*{{cite journal  | author=Owsianka AM, Patel AH |title=Hepatitis C virus core protein interacts with a human DEAD box protein DDX3. |journal=Virology |volume=257 |issue= 2 |pages= 330-40 |year= 1999 |pmid= 10329544 |doi= 10.1006/viro.1999.9659 }}
* {{cite journal | vauthors = Li J, Hawkins IC, Harvey CD, Jennings JL, Link AJ, Patton JG | title = Regulation of alternative splicing by SRrp86 and its interacting proteins | journal = Molecular and Cellular Biology | volume = 23 | issue = 21 | pages = 7437–47 | date = November 2003 | pmid = 14559993 | pmc = 207616 | doi = 10.1128/MCB.23.21.7437-7447.2003 }}
*{{cite journal | author=Mamiya N, Worman HJ |title=Hepatitis C virus core protein binds to a DEAD box RNA helicase. |journal=J. Biol. Chem. |volume=274 |issue= 22 |pages= 15751-6 |year= 1999 |pmid= 10336476 |doi= }}
* {{cite journal | vauthors = Shu H, Chen S, Bi Q, Mumby M, Brekken DL | title = Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line | journal = Molecular & Cellular Proteomics | volume = 3 | issue = 3 | pages = 279–86 | date = March 2004 | pmid = 14729942 | doi = 10.1074/mcp.D300003-MCP200 }}
*{{cite journal | author=Yagüe J, Alvarez I, Rognan D, ''et al.'' |title=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. |journal=J. Exp. Med. |volume=191 |issue= 12 |pages= 2083-92 |year= 2000 |pmid= 10859333 |doi= }}
* {{cite journal | vauthors = Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G | title = A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway | journal = Nature Cell Biology | volume = 6 | issue = 2 | pages = 97–105 | date = February 2004 | pmid = 14743216 | doi = 10.1038/ncb1086 }}
*{{cite journal | author=Kim YS, Lee SG, Park SH, Song K |title=Gene structure of the human DDX3 and chromosome mapping of its related sequences. |journal=Mol. Cells |volume=12 |issue= 2 |pages= 209-14 |year= 2002 |pmid= 11710523 |doi=  }}
* {{cite journal | vauthors = Yedavalli VS, Neuveut C, Chi YH, Kleiman L, Jeang KT | title = Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function | journal = Cell | volume = 119 | issue = 3 | pages = 381–92 | date = October 2004 | pmid = 15507209 | doi = 10.1016/j.cell.2004.09.029 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Dayton AI | title = Within you, without you: HIV-1 Rev and RNA export | journal = Retrovirology | volume = 1 | issue =  | pages = 35 | date = October 2004 | pmid = 15516266 | pmc = 526764 | doi = 10.1186/1742-4690-1-35 }}
*{{cite journal  | author=Li J, Hawkins IC, Harvey CD, ''et al.'' |title=Regulation of alternative splicing by SRrp86 and its interacting proteins. |journal=Mol. Cell. Biol. |volume=23 |issue= 21 |pages= 7437-47 |year= 2003 |pmid= 14559993 |doi= }}
* {{cite journal | vauthors = Krishnan V, Zeichner SL | title = Alterations in the expression of DEAD-box and other RNA binding proteins during HIV-1 replication | journal = Retrovirology | volume = 1 | issue =  | pages = 42 | date = December 2004 | pmid = 15588285 | pmc = 543576 | doi = 10.1186/1742-4690-1-42 }}
*{{cite journal | author=Shu H, Chen S, Bi Q, ''et al.'' |title=Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line. |journal=Mol. Cell Proteomics |volume=3 |issue= 3 |pages= 279-86 |year= 2004 |pmid= 14729942 |doi= 10.1074/mcp.D300003-MCP200 }}
* {{cite journal | vauthors = Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ | title = Immunoaffinity profiling of tyrosine phosphorylation in cancer cells | journal = Nature Biotechnology | volume = 23 | issue = 1 | pages = 94–101 | date = January 2005 | pmid = 15592455 | doi = 10.1038/nbt1046 }}
*{{cite journal | author=Bouwmeester T, Bauch A, Ruffner H, ''et al.'' |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97-105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 }}
* {{cite journal | vauthors = Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R | title = Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry | journal = Nature Methods | volume = 2 | issue = 8 | pages = 591–8 | date = August 2005 | pmid = 16094384 | doi = 10.1038/nmeth776 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
* {{cite journal | vauthors = Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J | title = Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC | journal = Proteomics | volume = 5 | issue = 14 | pages = 3589–99 | date = September 2005 | pmid = 16097034 | doi = 10.1002/pmic.200401217 }}
*{{cite journal  | author=Yedavalli VS, Neuveut C, Chi YH, ''et al.'' |title=Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function. |journal=Cell |volume=119 |issue= 3 |pages= 381-92 |year= 2004 |pmid= 15507209 |doi= 10.1016/j.cell.2004.09.029 }}
* {{cite journal | vauthors = Chang PC, Chi CW, Chau GY, Li FY, Tsai YH, Wu JC, Wu Lee YH | title = DDX3, a DEAD box RNA helicase, is deregulated in hepatitis virus-associated hepatocellular carcinoma and is involved in cell growth control | journal = Oncogene | volume = 25 | issue = 14 | pages = 1991–2003 | date = March 2006 | pmid = 16301996 | doi = 10.1038/sj.onc.1209239 }}
*{{cite journal | author=Dayton AI |title=Within you, without you: HIV-1 Rev and RNA export. |journal=Retrovirology |volume=1 |issue=  |pages= 35 |year= 2006 |pmid= 15516266 |doi= 10.1186/1742-4690-1-35 }}
*{{cite journal | author=Krishnan V, Zeichner SL |title=Alterations in the expression of DEAD-box and other RNA binding proteins during HIV-1 replication. |journal=Retrovirology |volume=1 |issue=  |pages= 42 |year= 2006 |pmid= 15588285 |doi= 10.1186/1742-4690-1-42 }}
*{{cite journal | author=Rush J, Moritz A, Lee KA, ''et al.'' |title=Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. |journal=Nat. Biotechnol. |volume=23 |issue= 1 |pages= 94-101 |year= 2005 |pmid= 15592455 |doi= 10.1038/nbt1046 }}
*{{cite journal | author=Tao WA, Wollscheid B, O'Brien R, ''et al.'' |title=Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. |journal=Nat. Methods |volume=2 |issue= 8 |pages= 591-8 |year= 2005 |pmid= 16094384 |doi= 10.1038/nmeth776 }}
*{{cite journal | author=Gevaert K, Staes A, Van Damme J, ''et al.'' |title=Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. |journal=Proteomics |volume=5 |issue= 14 |pages= 3589-99 |year= 2006 |pmid= 16097034 |doi= 10.1002/pmic.200401217 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Chang PC, Chi CW, Chau GY, ''et al.'' |title=DDX3, a DEAD box RNA helicase, is deregulated in hepatitis virus-associated hepatocellular carcinoma and is involved in cell growth control. |journal=Oncogene |volume=25 |issue= 14 |pages= 1991-2003 |year= 2006 |pmid= 16301996 |doi= 10.1038/sj.onc.1209239 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=1654}}
{{WikiDoc Sources}}

Latest revision as of 09:05, 5 March 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

ATP-dependent RNA helicase DDX3X is an enzyme that in humans is encoded by the DDX3X gene.[1][2][3]

Function

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which interacts specifically with hepatitis C virus core protein resulting a change in intracellular location. This gene has a homolog located in the nonrecombining region of the Y chromosome. The protein sequence is 91% identical between this gene and the Y-linked homolog.[3]

Role in cancer

DDX3X is involved in many different types of cancer. For example, it is abnormally expressed in breast epithelial cancer cells in which its expression is activated by HIF1A during hypoxia.[4] Increased expression of DDX3X by HIF1A in hypoxia is initiated by the direct binding of HIF1A to the HIF1A response element,[4] as verified with chromatin immunoprecipitation and luciferase reporter assay. Since the expression of DDX3X is affected by the activity of HIF1A, the co-localization of these proteins has also been demonstrated in MDA-MB-231 xenograft tumor samples.[4]

In HeLa cells DDX3X is reported to control cell cycle progression through Cyclin E1.[5] More specifically, DDX3X was shown to directly bind to the 5´ UTR of Cyclin E1 and thereby facilitating the translation of the protein. Increased protein levels of Cyclin E1 was demonstrated to mediate the transition of S phase entry.[5]

Clinical significance

Mutations of the DDX3X gene are also associated with medulloblastoma.[6][7][8]

See also

References

  1. ↑ Lahn BT, Page DC (October 1997). "Functional coherence of the human Y chromosome". Science. 278 (5338): 675–80. doi:10.1126/science.278.5338.675. PMID 9381176.
  2. ↑ Park SH, Lee SG, Kim Y, Song K (Oct 1998). "Assignment of a human putative RNA helicase gene, DDX3, to human X chromosome bands p11.3→p11.23". Cytogenetics and Cell Genetics. 81 (3–4): 178–9. doi:10.1159/000015022. PMID 9730595.
  3. ↑ 3.0 3.1 "Entrez Gene: DDX3X DEAD (Asp-Glu-Ala-Asp) box polypeptide 3, X-linked".
  4. ↑ 4.0 4.1 4.2 Botlagunta M, Krishnamachary B, Vesuna F, Winnard PT, Bol GM, Patel AH, Raman V (March 2011). "Expression of DDX3 is directly modulated by hypoxia inducible factor-1 alpha in breast epithelial cells". PLOS One. PLOS One. 6 (3): e17563. doi:10.1371/journal.pone.0017563. PMC 3063174. PMID 21448281.
  5. ↑ 5.0 5.1 Lai MC, Chang WC, Shieh SY, Tarn WY (November 2010). "DDX3 regulates cell growth through translational control of cyclin E1". Molecular and Cellular Biology. Molecular and Cellular Biology. 30 (22): 5444–53. doi:10.1128/MCB.00560-10. PMC 2976371. PMID 20837705.
  6. ↑ Robinson G, Parker M, Kranenburg TA, Lu C, Chen X, Ding L, et al. (August 2012). "Novel mutations target distinct subgroups of medulloblastoma". Nature. 488 (7409): 43–8. doi:10.1038/nature11213. PMC 3412905. PMID 22722829.
  7. ↑ Jones DT, Jäger N, Kool M, Zichner T, Hutter B, Sultan M, et al. (August 2012). "Dissecting the genomic complexity underlying medulloblastoma". Nature. 488 (7409): 100–5. doi:10.1038/nature11284. PMC 3662966. PMID 22832583.
  8. ↑ Pugh TJ, Weeraratne SD, Archer TC, Pomeranz Krummel DA, Auclair D, Bochicchio J, et al. (August 2012). "Medulloblastoma exome sequencing uncovers subtype-specific somatic mutations". Nature. 488 (7409): 106–10. doi:10.1038/nature11329. PMC 3413789. PMID 22820256.

Further reading

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