We are using a number of approaches to identify novel PRMT substrates, including TAP-tag affinity purification using catalytic-inactive PRMTs as bait, bio-ID, bio-orthogonal profiling and the isolation of methylated proteins via purification by symmetric dimethyl reader domains. We combine this with quantitative proteomics to help better understand how the substrate repertoire of PRMTs is altered after DNA damage, or in cancer cells compared to their non-transformed counterparts. In doing so, we hope that new cellular functions for arginine methylation will be discovered that will help explain its contribution to both physiological and pathological processes.