WD repeat-containing protein 77
(Redirected from WDR77)
An Error has occurred retrieving Wikidata item for infobox Methylosome protein 50 is a protein that in humans is encoded by the WDR77 gene.[1][2][3]
Interactions
WD repeat-containing protein 77 has been shown to interact with CTDP1[4] and Protein arginine methyltransferase 5.[1]
References
- ^ a b Friesen WJ, Wyce A, Paushkin S, Abel L, Rappsilber J, Mann M, Dreyfuss G (Mar 2002). "A novel WD repeat protein component of the methylosome binds Sm proteins". J Biol Chem. 277 (10): 8243–7. doi:10.1074/jbc.M109984200. PMID 11756452.
- ^ Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Jun 1996). "A "double adaptor" method for improved shotgun library construction". Anal Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
- ^ "Entrez Gene: WDR77 WD repeat domain 77".
- ^ Licciardo, Paolo; Amente Stefano; Ruggiero Luca; Monti Maria; Pucci Piero; Lania Luigi; Majello Barbara (Feb 2003). "The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP". Nucleic Acids Res. England. 31 (3): 999–1005. doi:10.1093/nar/gkg197. PMC 149217. PMID 12560496.
Further reading
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Licciardo P, Amente S, Ruggiero L, et al. (2003). "The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP". Nucleic Acids Res. 31 (3): 999–1005. doi:10.1093/nar/gkg197. PMC 149217. PMID 12560496.
- 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.
- Yamada S, Ohira M, Horie H, et al. (2004). "Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas". Oncogene. 23 (35): 5901–11. doi:10.1038/sj.onc.1207782. PMID 15221005.
- Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
- 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.
- Amente S, Napolitano G, Licciardo P, et al. (2005). "Identification of proteins interacting with the RNAPII FCP1 phosphatase: FCP1 forms a complex with arginine methyltransferase PRMT5 and it is a substrate for PRMT5-mediated methylation". FEBS Lett. 579 (3): 683–9. doi:10.1016/j.febslet.2004.12.045. PMID 15670829.
- Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
- Furuno K, Masatsugu T, Sonoda M, et al. (2006). "Association of Polycomb group SUZ12 with WD-repeat protein MEP50 that binds to histone H2A selectively in vitro". Biochem. Biophys. Res. Commun. 345 (3): 1051–8. doi:10.1016/j.bbrc.2006.05.014. PMID 16712789.
- Zhou L, Wu H, Lee P, Wang Z (2007). "Roles of the androgen receptor cofactor p44 in the growth of prostate epithelial cells". J. Mol. Endocrinol. 37 (2): 283–300. doi:10.1677/jme.1.02062. PMID 17032745.
- Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
- Liang JJ, Wang Z, Chiriboga L, et al. (2007). "The expression and function of androgen receptor coactivator p44 and protein arginine methyltransferase 5 in the developing testis and testicular tumors". J. Urol. 177 (5): 1918–22. doi:10.1016/j.juro.2007.01.017. PMID 17437848.
- Rengasamy, M, Zhang, F, Vashisht, A, Song, WM, et al. (2017). "The PRMT5/WDR77 complex regulates alternative splicing through ZNF326 in breast cancer". Nucleic Acids Res. 45 (19): 11106–11120. doi:10.1093/nar/gkx727. PMC 5737218. PMID 28977470.
External links
- Overview of all the structural information available in the PDB for UniProt: Q9BQA1 (Methylosome protein 50) at the PDBe-KB.
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