PRMT6

Protein arginine methyltransferase 6, also known as PRMT6, is a human gene.cite web | title = Entrez Gene: PRMT6 protein arginine methyltransferase 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55170| accessdate = ]

PBB_Summary
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summary_text = 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] cite web | title = Entrez Gene: PRMT6 protein arginine methyltransferase 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55170| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Frankel A, Yadav N, Lee J, "et al." |title=The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. |journal=J. Biol. Chem. |volume=277 |issue= 5 |pages= 3537–43 |year= 2002 |pmid= 11724789 |doi= 10.1074/jbc.M108786200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |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
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |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
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |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
*cite journal | author=Boulanger MC, Liang C, Russell RS, "et al." |title=Methylation of Tat by PRMT6 regulates human immunodeficiency virus type 1 gene expression. |journal=J. Virol. |volume=79 |issue= 1 |pages= 124–31 |year= 2005 |pmid= 15596808 |doi= 10.1128/JVI.79.1.124-131.2005
*cite journal | author=Sgarra R, Lee J, Tessari MA, "et al." |title=The AT-hook of the chromatin architectural transcription factor high mobility group A1a is arginine-methylated by protein arginine methyltransferase 6. |journal=J. Biol. Chem. |volume=281 |issue= 7 |pages= 3764–72 |year= 2006 |pmid= 16293633 |doi= 10.1074/jbc.M510231200
*cite journal | author=Willemsen NM, Hitchen EM, Bodetti TJ, "et al." |title=Protein methylation is required to maintain optimal HIV-1 infectivity. |journal=Retrovirology |volume=3 |issue= |pages= 92 |year= 2007 |pmid= 17169163 |doi= 10.1186/1742-4690-3-92
*cite journal | author=Invernizzi CF, Xie B, Richard S, Wainberg MA |title=PRMT6 diminishes HIV-1 Rev binding to and export of viral RNA. |journal=Retrovirology |volume=3 |issue= |pages= 93 |year= 2007 |pmid= 17176473 |doi= 10.1186/1742-4690-3-93
*cite journal | author=Xie B, Invernizzi CF, Richard S, Wainberg MA |title=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. |journal=J. Virol. |volume=81 |issue= 8 |pages= 4226–34 |year= 2007 |pmid= 17267505 |doi= 10.1128/JVI.01888-06
*cite journal | author=Guccione E, Bassi C, Casadio F, "et al." |title=Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive. |journal=Nature |volume=449 |issue= 7164 |pages= 933–7 |year= 2007 |pmid= 17898714 |doi= 10.1038/nature06166

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