Set1 is the catalytic subunit of an evolutionarily conserved complex, SET1C or COMPASS, which methylates histone H3 at lysine 4 and serves as a scaffold for the association of seven tightly bound polypeptides: Swd1, Swd2, Swd3, Bre2, Sdc1, Spp1, and Shg1. Our results reveal that Set1 interacts with several importins as well as RGG motif-containing proteins, providing new insights into the mechanisms by which Set1 moves between cytoplasmic and nuclear compartments. We uncover that SET1C likely cooperates with other chromatin regulators, particularly via the Snf2 component of the SWI/SNF complex. Here to further investigate Snf2 methylation by Set1C in vivo, we purified Snf2-GFP and its subunits with GFP nanobodies in the presence or absence of Set1. The protein composition of the complex was determined by mass spectrometry in the presence of absence of Set1.