• Bo Sun, Menghuan Zhang, Peng Cui, Hong Li, Jia Jia, Yixue Li, and Lu Xie.
• School of Life Science and Biotechnology, Shanghai Jiao Tong University, 800 Dong Chuan Road, Shanghai 200240, China ; Shanghai Center for Bioinformation Technology, Shanghai Academy of Science and Technology, 1278 Ke Yuan Road, Shanghai 201203, China.
• Comput Math Methods Med. 2015 Jan 1; 2015: 124630.

AbstractProtein posttranslational modifications (PTMs) play key roles in a variety of protein activities and cellular processes. Different PTMs show distinct impacts on protein functions, and normal protein activities are consequences of all kinds of PTMs working together. With the development of high throughput technologies such as tandem mass spectrometry (MS/MS) and next generation sequencing, more and more nonsynonymous single-nucleotide variations (nsSNVs) that cause variation of amino acids have been identified, some of which result in the damage of PTMs. The damaged PTMs could be the reason of the development of some human diseases. In this study, we elucidated the proteome wide relationship of eight damaged PTMs to human inherited diseases and cancers. Some human inherited diseases or cancers may be the consequences of the interactions of damaged PTMs, rather than the result of single damaged PTM site.

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