PRMT6

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	MGI: 2139971 HomoloGene: 10024 GeneCards: PRMT6
EC number	2.1.1.125
Gene location (Human)
Chr.	Chromosome 1 (human)[1]
End	107,059,294 bp[1]
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)[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); • 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; • 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
	55170
	99890
	ENSG00000198890
	ENSMUSG00000049300
	Q96LA8
	Q6NZB1
	NM_018137
	NM_178891
	NP_060607
	NP_849222
	Wikidata
View/Edit Human	View/Edit Mouse

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

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 2 3 GRCh38: Ensembl release 89: ENSG00000198890 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000049300 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
1 2 "Entrez Gene: PRMT6 protein arginine methyltransferase 6".

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000198890 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000049300 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid11724789-5] 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.

[entrez-6] 1 2 "Entrez Gene: PRMT6 protein arginine methyltransferase 6".

PRMT6

References

Further reading