Reactome | COPRS:CCND1:CDK4:PRMT5:pT5-WDR77 methylates arginine-4 of histone H4 (H4R3)

COPRS:CCND1:CDK4:PRMT5:pT5-WDR77 methylates arginine-4 of histone H4 (H4R3)

Stable Identifier

R-HSA-5205861

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

Synonyms

COPRS:CCND1:CDK4:PRMT5:pT5-WDR77 methylates arginine-4 of histone H4

ReviewStatus

5/5

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COPRS:CCND1:CDK4:PRMT5:pT5-WDR77 methylates arginine-4 of histone H4 (H4R3)

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PRMT5 can methylate histone H4 at arginine-4 (H4R3)and histone H2A at arginine-4 (H2AR3) (Pal et al. 2004). Symmetric dimethylation of histone H4 arginine-4 (H4R3me2s) by PRMT5 is required for subsequent DNA methylation. The histone-binding protein Cooperator of PRMT5 (COPRS) guides PRMT5:WDR77 to methylate histone H4 arginine-4 (H4R3) rather than histone H3 arginine-9 (H3R8) (Lacroix et al. 2008). H4R3me2s serves as a direct binding target for the DNA methyltransferase DNMT3A, which interacts through the ADD domain, which contains a PHD motif (Zhao et al. 2009).

Literature References

PubMed ID	Title	Journal	Year
18404153	The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5 Rodier, G, Le Cam, A, Fabbrizio, E, Sardet, C, El Messaoudi, S, Lacroix, M	EMBO Rep.	2008
15485929	Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes Vishwanath, SN, Pal, S, Sif, S, Tempst, P, Erdjument-Bromage, H	Mol. Cell. Biol.	2004