PRMT6

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

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) Band 1p13.3 Start 107,056,674 bp End 107,067,636 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 F3 Start 110,153,425 bp End 110,158,314 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in islet of Langerhans palpebral conjunctiva metanephros left adrenal gland prefrontal cortex kidney body of pancreas stromal cell of endometrium hypothalamus retinal pigment epithelium Top expressed in renal corpuscle medullary collecting duct spermatocyte endocardial cushion primitive streak yolk sac neural tube cumulus cell morula ganglionic eminence More reference expression data BioGPS n/a
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) protein binding protein-arginine N-methyltransferase activity histone-arginine N-methyltransferase activity Cellular component nucleoplasm nucleus nucleolus cytosol Biological process regulation of transcription, DNA-templated negative regulation of transcription by RNA polymerase II transcription, DNA-templated cellular response to DNA damage stimulus cellular senescence methylation peptidyl-arginine methylation, to asymmetrical-dimethyl arginine histone methylation 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: 110.15 – 110.16 Mb PubMed search
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]

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. hdl:11577/1565364. 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.