PRMT3 transfers 3xCH3 from 3xAdoMet to RPS2

Stable Identifier
R-HSA-8879123
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
Protein arginine methyltransferase 3 (PRMT3) is a cytosolic enzyme that catalyzes the formation of omega-mono- or asymmetric dimethylarginine (Tang et al. 1998). It has a unique substrate binding N-terminal C2H2 Zn finger domain and a catalytic C-terminal domain that is homologous to other PRMTs (Zhang et al. 2000). PRMT3 associates with ribosomes in the cytosol, which contain its main in vivo substrate, the small ribosomal subunit Ribosomal protein S2 (RPS2). PRMT3 methylates arginines in the RG-rich N-terminal tail of RPS2 forming asymmetric dimethylarginines (Swiercz et al. 2005). Prmt3–null mice show developmental delay during embryogenesis and have embryos that are markedly smaller than wt , though size at birth is normal suggesting that PRMT3 loss can be compensated for in most cell types but may not be in under conditions that demand extremely fast protein synthesis (Swiercz et al. 2007).
Literature References
Participants
Participates
Catalyst Activity

protein-arginine N-methyltransferase activity of PRMT3 [cytosol]

Orthologous Events
Authored
Reviewed
Created
Cite Us!