DDX5

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,{{cite journal |last1=Legrand |first1=JMD |last2=Chan |first2=AL |last3=La |first3=HM |last4=Rossello |first4=FJ |last5=Änkö |first5=ML |last6=Fuller-Pace |first6=FV |last7=Hobbs |first7=RM |title=DDX5 plays essential transcriptional and post-transcriptional roles in the maintenance and function of spermatogonia. |journal=Nature Communications |date=23 May 2019 |volume=10 |issue=1 |pages=2278 |doi=10.1038/s41467-019-09972-7 |pmid=31123254|pmc=6533336 |bibcode=2019NatCo..10.2278L }} and cellular growth and division. This gene encodes a DEAD box protein, which is an RNA-dependent ATPase, and also a proliferation-associated nuclear antigen, specifically reacting with the simian virus 40 tumor antigen. This gene consists of 13 exons, and alternatively spliced transcripts containing several intron sequences have been detected, but no isoforms encoded by these transcripts have been identified.

DDX5 has been shown to interact with:

• AKAP8,{{cite journal | vauthors = Akileswaran L, Taraska JW, Sayer JA, Gettemy JM, Coghlan VM | title = A-kinase-anchoring protein AKAP95 is targeted to the nuclear matrix and associates with p68 RNA helicase | journal = J. Biol. Chem. | volume = 276 | issue = 20 | pages = 17448–54 |date=May 2001 | pmid = 11279182 | doi = 10.1074/jbc.M101171200 | doi-access = free }}
• DDX17 (p72),{{cite journal | vauthors = Ogilvie VC, Wilson BJ, Nicol SM, Morrice NA, Saunders LR, Barber GN, Fuller-Pace FV | title = The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells | journal = Nucleic Acids Res. | volume = 31 | issue = 5 | pages = 1470–80 |date=March 2003 | pmid = 12595555 | pmc = 149829 | doi = 10.1093/nar/gkg236 }}
• DHX9 (RNA helicase A),{{cite journal | vauthors = Wilson BJ, Giguère V | title = Identification of novel pathway partners of p68 and p72 RNA helicases through Oncomine meta-analysis | journal = BMC Genomics | volume = 8| pages = 419 | year = 2007 | pmid = 18005418 | doi = 10.1186/1471-2164-8-419 | pmc=3225811 | doi-access = free }}
• Estrogen receptor alpha,{{cite journal | vauthors = Rossow KL, Janknecht R | title = Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300 | journal = Oncogene | volume = 22 | issue = 1 | pages = 151–6 |date=January 2003 | pmid = 12527917 | doi = 10.1038/sj.onc.1206067 | doi-access = free }}
• Fibrillarin,{{cite journal | vauthors = Nicol SM, Causevic M, Prescott AR, Fuller-Pace FV | title = The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase | journal = Exp. Cell Res. | volume = 257 | issue = 2 | pages = 272–80 |date=June 2000 | pmid = 10837141 | doi = 10.1006/excr.2000.4886 }}
• HDAC1,{{cite journal | vauthors = Wilson BJ, Bates GJ, Nicol SM, Gregory DJ, Perkins ND, Fuller-Pace FV | title = The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner | journal = BMC Mol. Biol. | volume = 5| pages = 11 |date=August 2004 | pmid = 15298701 | pmc = 514542 | doi = 10.1186/1471-2199-5-11 | doi-access = free }}
• p53,{{cite journal | vauthors = Bates GJ, Nicol SM, Wilson BJ, Jacobs AM, Bourdon JC, Wardrop J, Gregory DJ, Lane DP, Perkins ND, Fuller-Pace FV | title = The DEAD box protein p68: a novel transcriptional coactivator of the p53 tumour suppressor | journal = EMBO J. | volume = 24 | issue = 3 | pages = 543–53 |date=February 2005 | pmid = 15660129 | pmc = 548656 | doi = 10.1038/sj.emboj.7600550 }}
• CTCF.{{cite journal | vauthors = Yao H, Brick K, Evrard Y, Xiao T, Camerini-Otero RD, Felsenfeld G | title = Mediation of CTCF transcriptional insulation by DEAD-box RNA-binding protein p68 and steroid receptor RNA activator SRA | journal = Genes Dev | volume = 24 | issue = 22 | pages = 2543–2555 | year = 2010 |pmid = 20966046 | pmc = 2975930| doi = 10.1101/gad.1967810 }}

{{reflist}}

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• {{cite journal | vauthors=Rössler OG, Hloch P, Schütz N |title=Structure and expression of the human p68 RNA helicase gene |journal=Nucleic Acids Res. |volume=28 |issue= 4 |pages= 932–9 |year= 2000 |pmid= 10648785 |doi=10.1093/nar/28.4.932 | pmc=102575 |display-authors=etal}}
• {{cite journal | vauthors=Nicol SM, Causevic M, Prescott AR, Fuller-Pace FV |title=The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase |journal=Exp. Cell Res. |volume=257 |issue= 2 |pages= 272–80 |year= 2000 |pmid= 10837141 |doi= 10.1006/excr.2000.4886 }}
• {{cite journal | vauthors=Akileswaran L, Taraska JW, Sayer JA |title=A-kinase-anchoring protein AKAP95 is targeted to the nuclear matrix and associates with p68 RNA helicase |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 17448–54 |year= 2001 |pmid= 11279182 |doi= 10.1074/jbc.M101171200 |display-authors=etal|doi-access=free }}
• {{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 |s2cid=14132033 |display-authors=etal|doi-access=free |bibcode=2002CBio...12....1A }}
• {{cite journal | vauthors=Jurica MS, Licklider LJ, Gygi SR |title=Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis |journal=RNA |volume=8 |issue= 4 |pages= 426–39 |year= 2002 |pmid= 11991638 |doi=10.1017/S1355838202021088 | pmc=1370266 |display-authors=etal}}
• {{cite journal | author=Liu ZR |title=p68 RNA Helicase Is an Essential Human Splicing Factor That Acts at the U1 snRNA-5′ Splice Site Duplex |journal=Mol. Cell. Biol. |volume=22 |issue= 15 |pages= 5443–50 |year= 2002 |pmid= 12101238 |doi=10.1128/MCB.22.15.5443-5450.2002 | pmc=133941 }}
• {{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 |bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }}
• {{cite journal | vauthors=Rossow KL, Janknecht R |title=Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300 |journal=Oncogene |volume=22 |issue= 1 |pages= 151–6 |year= 2003 |pmid= 12527917 |doi= 10.1038/sj.onc.1206067 |doi-access= free }}
• {{cite journal | vauthors=Guil S, Gattoni R, Carrascal M |title=Roles of hnRNP A1, SR Proteins, and p68 Helicase in c-H-ras Alternative Splicing Regulation |journal=Mol. Cell. Biol. |volume=23 |issue= 8 |pages= 2927–41 |year= 2003 |pmid= 12665590 |doi=10.1128/MCB.23.8.2927-2941.2003 | pmc=152554 |display-authors=etal}}
• {{cite journal | vauthors=Fujita T, Kobayashi Y, Wada O |title=Full activation of estrogen receptor alpha activation function-1 induces proliferation of breast cancer cells |journal=J. Biol. Chem. |volume=278 |issue= 29 |pages= 26704–14 |year= 2003 |pmid= 12738788 |doi= 10.1074/jbc.M301031200 |display-authors=etal|doi-access=free }}
• {{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|doi-access=free }}

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{{Acid anhydride hydrolases}}

{{Enzymes}}

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Category:EC 3.6.4