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SUMOylation is a post-translational modification that regulates a multitude of cellular processes, including replication, cell-cycle progression, protein transport and the DNA damage response. Similar to ubiquitin, SUMO (small ubiquitin-like modifier) is covalently attached to target proteins in a reversible process via an enzymatic cascade. SUMOylation is essential for nearly all eukaryotic organisms, and deregulation of the SUMO system is associated with human diseases such as cancer and neurodegenerative diseases. Therefore, it is of great interest to understand the regulation and dynamics of this post-translational modification. Within the last decade, mass spectrometry analyses of SUMO proteomes have overcome several obstacles, greatly expanding the number of known SUMO target proteins. In this review, we briefly outline the basic concepts of the SUMO system, and discuss the potential of proteomic approaches to decipher SUMOylation patterns in order to understand the role of SUMO in health and disease.Small Ubiquitin-like Modifiers (SUMO) are covalently attached to lysines in target proteins. In recent years, SUMO proteomes have extensively been studied using mass spectrometry, greatly expanding the number of known SUMO target proteins and precise SUMOylation sites. These proteomic approaches decipher dynamic SUMOylation patterns in response to diverse stimuli, to enable understanding the role of SUMO in health and disease.