Nonsynonymous Single-Nucleotide Variations on Some Posttranslational Modifications of Human Proteins and the Association with Diseases.
Protein 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.
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.
Bo
B
Sun
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.
Menghuan
M
Zhang
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.
Peng
P
Cui
Shanghai Center for Bioinformation Technology, Shanghai Academy of Science and Technology, 1278 Ke Yuan Road, Shanghai 201203, China.
Hong
H
Li
Shanghai Center for Bioinformation Technology, Shanghai Academy of Science and Technology, 1278 Ke Yuan Road, Shanghai 201203, China.
Jia
J
Jia
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.
Yixue
Y
Li
Shanghai Center for Bioinformation Technology, Shanghai Academy of Science and Technology, 1278 Ke Yuan Road, Shanghai 201203, China.
Lu
L
Xie
D030562:Databases, Protein / Q000706:statistics & numerical data; D056726:Genetic Association Studies / Q000706:statistics & numerical data; D030342:Genetic Diseases, Inborn / Q000235:genetics / Q000378:metabolism; D006801:Humans; D050505:Mutant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D009369:Neoplasms / Q000235:genetics / Q000378:metabolism; D020641:Polymorphism, Single Nucleotide; D060066:Protein Interaction Maps; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D040901:Proteomics / Q000379:methods / Q000706:statistics & numerical data; D053719:Tandem Mass Spectrometry
D050505:Mutant Proteins; D011506:Proteins