Lysine methylation of non-histone proteins

Abstract

Proteomics, or the large-scale study of protein structure and function, has contributed greatly to our understanding of cellular biology and disease. Over time, it has become apparent that the proteome is spatially, temporally, and chemically dynamic allowing for the same protein to perform very different functions and fulfil completely unrelated roles in a cell through small chemical changes. This can be described as epiproteomics (just as epigenetic are changes to DNA not encoded in the DNA sequence) and mainly covers Post-Translational Modifications (PTMs) such as phosphorylation, ubiquitination, acetylation or methylation, among over 200 or more [1]. These vary depending on cell type, signalling, stress condition, micro-environment and so on, leading to some sort of change in protein properties, which consequently, either directly or indirectly, alters the function