Amino acid preferences at neddylation sites

Neddylation is a dynamic post-translational modification in which NEDD8 proteins are covalently attached to the target site lysine residue. Neddylation may affect a target protein’s localization, binding partners and structure. Targets of this modification have commonly found in nucleus and the most well characterized target family is cullins, which is modulating ubiquitination and proteosomal degradation system in a cell. Disruptions in neddylation pathway implicated in various diseases such as Alzheimer’s, Parkinson’s and cancer. Therefore, understanding neddylation site recognition bears a huge importance in understanding the complete functional mechanism of this post-translational modification and revealing the mechanisms of associated diseases towards a cure. However, there is no study in literature investigating whether a common neddylation site motif exists or not. In this work, we have identified various amino acid preferences and hydrophobicity patterns seen in neddylation sites, differing from not neddylated lysine residues.