Abstract: Post-translational modification by ubiquitin and ubiquitin-like modifiers(Ubls) is one of the most important mechanisms regulating a wide range of cellular processes in eukaryotes. Previous research shows that, through covalently modification by ubiquitin or ubls, the substrate proteins can be regulated in many different ways like stability, subcellular localization, enzymatic activity, protein-protein interaction, etc.. Therefore, we can imagine, ubiquitin and ubls are playing very important roles in cellular and biological processes by modifying plenty of proteins. To better understand the ubiquitin and ubls system, proteomic approaches have been developed to purify and identify more protein substrates. Large-scale idendification of ubiquitin/ubls - modification sites by mass spectrometry is particularly important for understanding the molecular mechanism and function of ubiquitin/ubls modification. Until now, more and more scientists are getting interested and participating in proteomics research of ubiquitin/Ubl modifications. This review summarizes the rencent works in this field.