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'''ATP-dependent RNA helicase DDX39''' is an [[enzyme]] that in humans is encoded by the ''DDX39'' [[gene]].<ref name="pmid7601445">{{cite journal | vauthors = Peelman LJ, Chardon P, Nunes M, Renard C, Geffrotin C, Vaiman M, Van Zeveren A, Coppieters W, van de Weghe A, Bouquet Y | title = The BAT1 gene in the MHC encodes an evolutionarily conserved putative nuclear RNA helicase of the DEAD family | journal = Genomics | volume = 26 | issue = 2 | pages = 210–8 |date=Aug 1995 | pmid = 7601445 | pmc = | doi =10.1016/0888-7543(95)80203-X |display-authors=etal}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DDX39 DEAD (Asp-Glu-Ala-Asp) box polypeptide 39| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10212| accessdate = }}</ref> | |||
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| summary_text = This gene encodes a member of the DEAD box protein family. These proteins are characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD) and 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 the DEAD box protein family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division.<ref name="entrez" | | summary_text = This gene encodes a member of the DEAD box protein family. These proteins are characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD) and 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 the DEAD box protein family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division.<ref name="entrez" /> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{cite journal | vauthors=Andersen JS, Lyon CE, Fox AH |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1–11 |year= 2002 |pmid= 11790298 |doi=10.1016/S0960-9822(01)00650-9 |display-authors=etal}} | ||
*{{cite journal | vauthors=Strässer K, Masuda S, Mason P |title=TREX is a conserved complex coupling transcription with messenger RNA export. |journal=Nature |volume=417 |issue= 6886 |pages= 304–8 |year= 2002 |pmid= 11979277 |doi= 10.1038/nature746 |display-authors=etal}} | |||
*{{cite journal | | *{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 | pmc=139241 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Lehner B, Semple JI, Brown SE |title=Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region. |journal=Genomics |volume=83 |issue= 1 |pages= 153–67 |year= 2004 |pmid= 14667819 |doi=10.1016/S0888-7543(03)00235-0 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Pryor A, Tung L, Yang Z |title=Growth-regulated expression and G0-specific turnover of the mRNA that encodes URH49, a mammalian DExH/D box protein that is highly related to the mRNA export protein UAP56. |journal=Nucleic Acids Res. |volume=32 |issue= 6 |pages= 1857–65 |year= 2004 |pmid= 15047853 |doi= 10.1093/nar/gkh347 | pmc=390356 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Leaw CL, Ren EC, Choong ML |title=Hcc-1 is a novel component of the nuclear matrix with growth inhibitory function. |journal=Cell. Mol. Life Sci. |volume=61 |issue= 17 |pages= 2264–73 |year= 2004 |pmid= 15338056 |doi= 10.1007/s00018-004-4205-x }} | ||
*{{cite journal | | *{{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |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 | pmc=528928 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Andersen JS, Lam YW, Leung AK |title=Nucleolar proteome dynamics. |journal=Nature |volume=433 |issue= 7021 |pages= 77–83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Rual JF, Venkatesan K, Hao T |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 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Kapadia F, Pryor A, Chang TH, Johnson LF |title=Nuclear localization of poly(A)+ mRNA following siRNA reduction of expression of the mammalian RNA helicases UAP56 and URH49. |journal=Gene |volume=384 |issue= |pages= 37–44 |year= 2007 |pmid= 16949217 |doi= 10.1016/j.gene.2006.07.010 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Sugiura T, Sakurai K, Nagano Y |title=Intracellular characterization of DDX39, a novel growth-associated RNA helicase. |journal=Exp. Cell Res. |volume=313 |issue= 4 |pages= 782–90 |year= 2007 |pmid= 17196963 |doi= 10.1016/j.yexcr.2006.11.014 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Quaresma AJ, Sievert R, Nickerson JA |title=Regulation of mRNA export by the PI3 kinase/AKT signal transduction pathway. |journal=Mol. Biol. Cell |volume= 24|issue= 8 |pages= 1208–21 |year= 2013 |pmid= 23427269 |doi= 10.1091/mbc.E12-06-0450 | pmc=3623641 }} | ||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{ | ==External links== | ||
{{ | * {{UCSC genome browser|DDX39A}} | ||
* {{UCSC gene details|DDX39A}} | |||
{{PDB Gallery|geneid=10212}} | |||
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Species | Human | Mouse | |||||
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ATP-dependent RNA helicase DDX39 is an enzyme that in humans is encoded by the DDX39 gene.[1][2]
This gene encodes a member of the DEAD box protein family. These proteins are characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD) and 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 the DEAD box protein family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division.[2]
References
- ↑ Peelman LJ, Chardon P, Nunes M, Renard C, Geffrotin C, Vaiman M, Van Zeveren A, Coppieters W, van de Weghe A, Bouquet Y, et al. (Aug 1995). "The BAT1 gene in the MHC encodes an evolutionarily conserved putative nuclear RNA helicase of the DEAD family". Genomics. 26 (2): 210–8. doi:10.1016/0888-7543(95)80203-X. PMID 7601445.
- ↑ 2.0 2.1 "Entrez Gene: DDX39 DEAD (Asp-Glu-Ala-Asp) box polypeptide 39".
Further reading
- Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
- Strässer K, Masuda S, Mason P, et al. (2002). "TREX is a conserved complex coupling transcription with messenger RNA export". Nature. 417 (6886): 304–8. doi:10.1038/nature746. PMID 11979277.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Lehner B, Semple JI, Brown SE, et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Pryor A, Tung L, Yang Z, et al. (2004). "Growth-regulated expression and G0-specific turnover of the mRNA that encodes URH49, a mammalian DExH/D box protein that is highly related to the mRNA export protein UAP56". Nucleic Acids Res. 32 (6): 1857–65. doi:10.1093/nar/gkh347. PMC 390356. PMID 15047853.
- Leaw CL, Ren EC, Choong ML (2004). "Hcc-1 is a novel component of the nuclear matrix with growth inhibitory function". Cell. Mol. Life Sci. 61 (17): 2264–73. doi:10.1007/s00018-004-4205-x. PMID 15338056.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Kapadia F, Pryor A, Chang TH, Johnson LF (2007). "Nuclear localization of poly(A)+ mRNA following siRNA reduction of expression of the mammalian RNA helicases UAP56 and URH49". Gene. 384: 37–44. doi:10.1016/j.gene.2006.07.010. PMID 16949217.
- Sugiura T, Sakurai K, Nagano Y (2007). "Intracellular characterization of DDX39, a novel growth-associated RNA helicase". Exp. Cell Res. 313 (4): 782–90. doi:10.1016/j.yexcr.2006.11.014. PMID 17196963.
- Quaresma AJ, Sievert R, Nickerson JA (2013). "Regulation of mRNA export by the PI3 kinase/AKT signal transduction pathway". Mol. Biol. Cell. 24 (8): 1208–21. doi:10.1091/mbc.E12-06-0450. PMC 3623641. PMID 23427269.
External links
- DDX39A human gene location in the UCSC Genome Browser.
- DDX39A human gene details in the UCSC Genome Browser.
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