Predicting Protein Post-translational Modifications Using Meta-analysis of Proteome Scale Data Sets
Predicting Protein Post-translational Modifications Using Meta-analysis of Proteome Scale Data Sets
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DOI：
10.1074/mcp.m800332-mcp200
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发表时间：
2009-02-01
影响因子：
7
通讯作者：
Church, George M.
中科院分区：
文献类型：
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作者：
Schwartz, Daniel;Chou, Michael F.;Church, George M.
蛋白质翻译后修饰是一种重要的生物学调控机制，利用高通量技术发现蛋白质翻译后修饰的速度正在迅速增加。为了利用这些丰富的序列数据，我们引入了一种新的通用策略，旨在预测多种生物体中的各种翻译后修饰。我们使用motif-x程序来确定酵母、苍蝇、小鼠和人类的磷酸化基序以及人类的赖氨酸乙酰化基序，然后使用新开发的称为scan-x的工具对蛋白质组序列数据扫描这些基序，以全局预测这些生物体中的其他潜在修饰位点。10-使用折叠交叉验证（foldcross-validation）来确定每组预测的灵敏度和最小特异性，所有这些都显示出相对于其它可用的磷酸预测工具的改进。新基序的发现是这种方法的副产品，磷酸化基序分析为已知和新型激酶基序的进化保守性提供了强有力的证据。Molecular & Cellular Proteomics 8：365-379，2009.
Protein post-translational modifications are an important biological regulatory mechanism, and the rate of their discovery using high throughput techniques is rapidly increasingly. To make use of this wealth of sequence data, we introduce a new general strategy designed to predict a variety of post-translational modifications in several organisms. We used the motif-x program to determine phosphorylation motifs in yeast, fly, mouse, and man and lysine acetylation motifs in man. These motifs were then scanned against proteomic sequence data using a newly developed tool called scan-x to globally predict other potential modification sites within these organisms. 10-fold cross-validation was used to determine the sensitivity and minimum specificity for each set of predictions, all of which showed improvement over other available tools for phosphoprediction. New motif discovery is a byproduct of this approach, and the phosphorylation motif analyses provide strong evidence of evolutionary conservation of both known and novel kinase motifs. Molecular & Cellular Proteomics 8:365-379, 2009.