SUMOylation is a post-translational modification that is involved in the regulation of proteins of different cellular processes. Dependent on the transient, small SUMOylated portion of most target proteins, it is difficult to identify and characterize this modification and its functions, and it is even more difficult to study the interplay between SUMOylation and other modifications on a specific protein. To facilitate the analysis of protein SUMOylation and its interplay with other protein modifications, the UFDS (Ubc9 fusion-directed SUMOylation) system has been developed. The identification of new SUMOylation substrates and the elucidation of the interplay between STAT1 (signal transducer and activator of transcription 1) phosphorylation and SUMOylation demonstrate UFDS as a useful tool for analysing protein SUMOylation.

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