PRMT6

Protein arginine N-methyltransferase 6 is an enzyme that in humans is encoded by the PRMT6 gene.[5][6]

PRMT6
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4HC4, 4QPP, 4QQK, 4Y2H, 4Y30, 5EGS, 5E8R, 5HZM
Identifiers
Aliases	PRMT6, HRMT1L6, protein arginine methyltransferase 6
External IDs	OMIM: 608274 MGI: 2139971 HomoloGene: 10024 GeneCards: PRMT6
EC number	2.1.1.321
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p13.3 Start 107,056,674 bp[1] End 107,067,636 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 F3 Start 110,246,109 bp[2] End 110,250,998 bp[2]
Gene ontology Molecular function • methyltransferase activity • transferase activity • histone methyltransferase activity • protein-arginine omega-N monomethyltransferase activity • histone methyltransferase activity (H4-R3 specific) • histone binding • protein-arginine omega-N asymmetric methyltransferase activity • chromatin binding • histone methyltransferase activity (H2A-R3 specific) • histone methyltransferase activity (H3-R2 specific) • GO:0001948 protein binding • protein-arginine N-methyltransferase activity • histone-arginine N-methyltransferase activity Cellular component • nucleoplasm • cell nucleus • nucleolus • cytosol Biological process • regulation of transcription, DNA-templated • negative regulation of transcription from RNA polymerase II promoter • transcription, DNA-templated • cellular response to DNA damage stimulus • cellular senescence • methylation • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine • histone methylation • GO:0022415 viral process • negative regulation of transcription, DNA-templated • DNA repair • base-excision repair • protein methylation • histone H4-R3 methylation • regulation of megakaryocyte differentiation • chromatin organization • histone H3-R2 methylation • peptidyl-arginine N-methylation • negative regulation of histone H3-K4 methylation • regulation of signal transduction by p53 class mediator • histone arginine methylation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	55170	99890
Ensembl	ENSG00000198890	ENSMUSG00000049300
UniProt	Q96LA8	Q6NZB1
RefSeq (mRNA)	NM_018137	NM_178891
RefSeq (protein)	NP_060607	NP_849222
Location (UCSC)	Chr 1: 107.06 – 107.07 Mb	Chr 3: 110.25 – 110.25 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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][6]

References

1. GRCh38: Ensembl release 89: ENSG00000198890 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000049300 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "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. 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. doi:10.1038/nature06166. PMID 17898714.