Biology:DDX5
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Short description: Protein-coding gene in Homo sapiens
 Generic protein structure example |
Probable ATP-dependent RNA helicase DDX5 also known as DEAD box protein 5 or RNA helicase p68 is an enzyme that in humans is encoded by the DDX5 gene.[1]
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,[2] 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.[1]
Interactions
DDX5 has been shown to interact with:
- AKAP8,[3]
- DDX17 (p72),[4]
- DHX9 (RNA helicase A),[5]
- Estrogen receptor alpha,[6][7]
- Fibrillarin,[8]
- HDAC1,[9]
- Nuclear receptor coactivator 1,[10]
- Nuclear receptor coactivator 2,[10]
- Nuclear receptor coactivator 3,[10]
- p53,[11]
- CTCF.[12]
References
- ↑ 1.0 1.1 "Entrez Gene: DDX5 DEAD (Asp-Glu-Ala-Asp) box polypeptide 5". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1655.
- ↑ Legrand, JMD; Chan, AL; La, HM; Rossello, FJ; Änkö, ML; Fuller-Pace, FV; Hobbs, RM (23 May 2019). "DDX5 plays essential transcriptional and post-transcriptional roles in the maintenance and function of spermatogonia.". Nature Communications 10 (1): 2278. doi:10.1038/s41467-019-09972-7. PMID 31123254. Bibcode: 2019NatCo..10.2278L.
- ↑ "A-kinase-anchoring protein AKAP95 is targeted to the nuclear matrix and associates with p68 RNA helicase". J. Biol. Chem. 276 (20): 17448–54. May 2001. doi:10.1074/jbc.M101171200. PMID 11279182.
- ↑ "The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells". Nucleic Acids Res. 31 (5): 1470–80. March 2003. doi:10.1093/nar/gkg236. PMID 12595555.
- ↑ "Identification of novel pathway partners of p68 and p72 RNA helicases through Oncomine meta-analysis". BMC Genomics 8: 419. 2007. doi:10.1186/1471-2164-8-419. PMID 18005418.
- ↑ "Purification and Identification of p68 RNA Helicase Acting as a Transcriptional Coactivator Specific for the Activation Function 1 of Human Estrogen Receptor α". Mol. Cell. Biol. 19 (8): 5363–72. August 1999. doi:10.1128/MCB.19.8.5363. PMID 10409727.
- ↑ "Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300". Oncogene 22 (1): 151–6. January 2003. doi:10.1038/sj.onc.1206067. PMID 12527917.
- ↑ "The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase". Exp. Cell Res. 257 (2): 272–80. June 2000. doi:10.1006/excr.2000.4886. PMID 10837141.
- ↑ "The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner". BMC Mol. Biol. 5: 11. August 2004. doi:10.1186/1471-2199-5-11. PMID 15298701.
- ↑ 10.0 10.1 10.2 "A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor α coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA". EMBO J. 20 (6): 1341–52. March 2001. doi:10.1093/emboj/20.6.1341. PMID 11250900.
- ↑ "The DEAD box protein p68: a novel transcriptional coactivator of the p53 tumour suppressor". EMBO J. 24 (3): 543–53. February 2005. doi:10.1038/sj.emboj.7600550. PMID 15660129.
- ↑ "Mediation of CTCF transcriptional insulation by DEAD-box RNA-binding protein p68 and steroid receptor RNA activator SRA". Genes Dev 24 (22): 2543–2555. 2010. doi:10.1101/gad.1967810. PMID 20966046.
Further reading
- "p68 RNA helicase: identification of a nucleolar form and cloning of related genes containing a conserved intron in yeasts". Mol. Cell. Biol. 11 (3): 1326–33. 1991. doi:10.1128/MCB.11.3.1326. PMID 1996094.
- "Complete cDNA sequence of the human p68 protein". Nucleic Acids Res. 18 (10): 3045. 1990. doi:10.1093/nar/18.10.3045. PMID 2349099.
- "Nuclear protein with sequence homology to translation initiation factor eIF-4A". Nature 332 (6166): 736–8. 1988. doi:10.1038/332736a0. PMID 2451786. Bibcode: 1988Natur.332..736F.
- "Chromosome mapping of the human gene encoding the 68-kDa nuclear antigen (p68) by using the polymerase chain reaction". Proc. Natl. Acad. Sci. U.S.A. 86 (16): 6211–4. 1989. doi:10.1073/pnas.86.16.6211. PMID 2762324. Bibcode: 1989PNAS...86.6211I.
- "Regulation of p68 RNA helicase by calmodulin and protein kinase C". J. Biol. Chem. 269 (47): 29367–70. 1994. doi:10.1016/S0021-9258(18)43885-9. PMID 7525583.
- "Construction of a transcription map surrounding the BRCA1 locus of human chromosome 17". Genomics 25 (1): 238–47. 1995. doi:10.1016/0888-7543(95)80131-5. PMID 7774924. https://zenodo.org/record/1258609.
- "Purification and Identification of p68 RNA Helicase Acting as a Transcriptional Coactivator Specific for the Activation Function 1 of Human Estrogen Receptor α". Mol. Cell. Biol. 19 (8): 5363–72. 1999. doi:10.1128/MCB.19.8.5363. PMID 10409727.
- "Structure and expression of the human p68 RNA helicase gene". Nucleic Acids Res. 28 (4): 932–9. 2000. doi:10.1093/nar/28.4.932. PMID 10648785.
- "The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase". Exp. Cell Res. 257 (2): 272–80. 2000. doi:10.1006/excr.2000.4886. PMID 10837141.
- "A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor α coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA". EMBO J. 20 (6): 1341–52. 2001. doi:10.1093/emboj/20.6.1341. PMID 11250900.
- "A-kinase-anchoring protein AKAP95 is targeted to the nuclear matrix and associates with p68 RNA helicase". J. Biol. Chem. 276 (20): 17448–54. 2001. doi:10.1074/jbc.M101171200. PMID 11279182.
- "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. 2002. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
- "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". RNA 8 (4): 426–39. 2002. doi:10.1017/S1355838202021088. PMID 11991638.
- Liu ZR (2002). "p68 RNA Helicase Is an Essential Human Splicing Factor That Acts at the U1 snRNA-5′ Splice Site Duplex". Mol. Cell. Biol. 22 (15): 5443–50. doi:10.1128/MCB.22.15.5443-5450.2002. PMID 12101238.
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300". Oncogene 22 (1): 151–6. 2003. doi:10.1038/sj.onc.1206067. PMID 12527917.
- "Roles of hnRNP A1, SR Proteins, and p68 Helicase in c-H-ras Alternative Splicing Regulation". Mol. Cell. Biol. 23 (8): 2927–41. 2003. doi:10.1128/MCB.23.8.2927-2941.2003. PMID 12665590.
- "Full activation of estrogen receptor alpha activation function-1 induces proliferation of breast cancer cells". J. Biol. Chem. 278 (29): 26704–14. 2003. doi:10.1074/jbc.M301031200. PMID 12738788.
- "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.
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