Palmitoylation is the post-translational addition of lipids to proteins though thioester bonds and acts to promote association with membranes. Palmitoylation also acts to target proteins to specific membrane compartments, control residence in and movement between membrane microdomains and regulate protein conformation and activity. Palmitoylation is unique among lipid modifications of proteins as it is reversible, allowing for dynamic control over all palmitoylation dependent processes. Palmitoylation cannot be predicted from protein sequence and as a result is understudied when compared with other post-translational modifications. We recently published a proteomic analysis of palmitoylation in plants and increased the number of proposed palmitoylated proteins in plants from ~30 to over 500. The wide range of identified proteins indicates that palmitoylation is likely important for a variety of different functions in plants. Many supposedly well characterized proteins were identified as palmitoylated and our new data provides novel insight into regulatory mechanisms and potential explanations for observed phenomena. These data represent a new resource for plant biologist and will allow the study of palmitoylated proteins in plants to expand and move forward.