CARM1, PRMT6 methylate arginine-3 of histone H3 (H3R2)

Stable Identifier
Reaction [transition]
Homo sapiens
CARM1, PRMT6 methylate arginine-3 of histone H3
Locations in the PathwayBrowser
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PRMT6 (Guccione et al. 2007, Hyllus et al. 2007) and CARM1 (PRMT4) (Schurter et al. 2001, Torres-Padilla et al. 2007) can methylate arginine-3 of histone H3 (H3R2). PRMT6 predominantly asymmetrically dimethylates H3R2 and is the major cellular H3R2 methyltransferase. It has higher activity toward the monomethylated form of the peptide than the unmethylated form (Hyllus et al. 2007).
Literature References
PubMed ID Title Journal Year
17215844 Histone arginine methylation regulates pluripotency in the early mouse embryo

Parfitt, DE, Zernicka-Goetz, M, Kouzarides, T, Torres-Padilla, ME

Nature 2007
17898714 Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive

Guccione, E, Cesaroni, M, Casadio, F, Bassi, C, Amati, B, L├╝scher, B, Martinato, F, Schuchlautz, H

Nature 2007
11341840 Methylation of histone H3 by coactivator-associated arginine methyltransferase 1

Koh, SS, Stallcup, MR, Henschen-Edman, A, Hanson, BL, Harp, JM, Chen, D, Aswad, DW, Schurter, BT, Mackay, DR, Bunick, GJ

Biochemistry 2001
18079182 PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

Schnabel, K, Schiltz, E, Bauer, UM, Stein, C, Hsieh, J, Imhof, A, Dou, Y, Hyllus, D

Genes Dev. 2007
Catalyst Activity

protein-arginine N-methyltransferase activity of CARM1, PRMT6 [nucleoplasm]

Orthologous Events
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