PRMT6
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An Error has occurred retrieving Wikidata item for infobox Protein arginine N-methyltransferase 6 is an enzyme that in humans is encoded by the PRMT6 gene.[1][2]
Protein arginine N-methyltransferases, such as PRMT6, catalyze the sequential transfer of a methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins to form methylated arginine derivatives and S-adenosyl-L-homocysteine.[supplied by OMIM][2]
References
- ^ Frankel A, Yadav N, Lee J, Branscombe TL, Clarke S, Bedford MT (Jan 2002). "The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity". J Biol Chem. 277 (5): 3537–43. doi:10.1074/jbc.M108786200. PMID 11724789.
- ^ a b "Entrez Gene: PRMT6 protein arginine methyltransferase 6".
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.
- 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.
- 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.
- 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.
- Boulanger MC, Liang C, Russell RS, et al. (2005). "Methylation of Tat by PRMT6 Regulates Human Immunodeficiency Virus Type 1 Gene Expression". J. Virol. 79 (1): 124–31. doi:10.1128/JVI.79.1.124-131.2005. PMC 538702. PMID 15596808.
- Sgarra R, Lee J, Tessari MA, et al. (2006). "The AT-hook of the chromatin architectural transcription factor high mobility group A1a is arginine-methylated by protein arginine methyltransferase 6". J. Biol. Chem. 281 (7): 3764–72. doi:10.1074/jbc.M510231200. PMID 16293633.
- Willemsen NM, Hitchen EM, Bodetti TJ, et al. (2007). "Protein methylation is required to maintain optimal HIV-1 infectivity". Retrovirology. 3: 92. doi:10.1186/1742-4690-3-92. PMC 1766367. PMID 17169163.
- Invernizzi CF, Xie B, Richard S, Wainberg MA (2007). "PRMT6 diminishes HIV-1 Rev binding to and export of viral RNA". Retrovirology. 3: 93. doi:10.1186/1742-4690-3-93. PMC 1779295. PMID 17176473.
- Xie B, Invernizzi CF, Richard S, Wainberg MA (2007). "Arginine Methylation of the Human Immunodeficiency Virus Type 1 Tat Protein by PRMT6 Negatively Affects Tat Interactions with both Cyclin T1 and the Tat Transactivation Region". J. Virol. 81 (8): 4226–34. doi:10.1128/JVI.01888-06. PMC 1866113. PMID 17267505.
- Guccione E, Bassi C, Casadio F, et al. (2007). "Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive". Nature. 449 (7164): 933–7. Bibcode:2007Natur.449..933G. doi:10.1038/nature06166. PMID 17898714. S2CID 4341782.
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