Through covalent modification of residues in proteins, post-translational modification (PTM) greatly expands the proteome diversity and regulates the dynamic functions of proteins. Recently, lysine was discovered as a hot spot amino acid for the PTM. Besides relatively well-studied PTMs such as methylation, acetylation and ubiquitination, a number of new PTMs were discovered to modify lysine residue, for example, butyrylation, crotonylation and succinylation. Although the detailed regulatory mechanisms are far from understanding, it is anticipated that these PTMs play critical roles in various biological processes. Here, We reported an integrated database of CPLM (Compendium of Protein Lysine Modification) or protein lysine modifications (PLMs). In total, 203,972 modification events on 189,919 modified lysines of 45,748 proteins for 11 types of PTMs were manually collected, including acetylation, ubiquitination, methylation, sumoylation, propionylation, butyrylation, succinylation, crotonylation, glycation, malonylation, and pupylation. With the dataset, we totally identified 76 types of co-occurrences of various PLMs on the same lysine residues, and the most abundant PLM crosstalk is between acetylation and ubiquitination. Up to 53.5% of acetylation and 33.1% of ubiquitination events co-occur at 10,746 lysine sites. Thus, the various PLM crosstalks suggested that a considerable proportion of lysines were competitively and dynamically regulated in a complicated manner. Since these various lysine modifications attracted great attention recently, we anticipate that such a comprehensive resource will be useful for the research community. The CPLM database is free to all users at: http://cplm.biocuckoo.org (1).