PRMT1 arginine-methylates RUNX1

Stable Identifier
Reaction [transition]
Homo sapiens
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Protein arginine methyltransferase 1 (PRMT1) methylates arginine residues R206 and R210 of RUNX1. Methylation of R206 and R210 inhibits binding of co-repressors to RUNX1, thus enhancing RUNX1 transcriptional activity (Zhao et al. 2008). In mice, arginine methylation seems to be dispensable for the function of RUNX1 in definitive hematopoiesis and steady-state platelet production, but is needed for the maintenance of the peripheral population of CD4+ T cells (Mizutani et al. 2015).

Literature References
PubMed ID Title Journal Year
18316480 Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity

Menendez, S, Tempst, P, Xiao, A, Nimer, SD, Allis, CD, Erdjument-Bromage, H, Zhao, X, Pardanani, A, Jankovic, V, Zhang, J, Dunne, R, Gural, A, Huang, G

Genes Dev. 2008
26010396 Loss of RUNX1/AML1 arginine-methylation impairs peripheral T cell homeostasis

Okuda, T, Zhao, X, Yoshida, T, Taniwaki, M, Nimer, SD, Mizutani, S

Br. J. Haematol. 2015
Catalyst Activity

protein-arginine N-methyltransferase activity of RUNX1:CBFB:PRMT1 [nucleoplasm]

Orthologous Events
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