Department of Proteomics and Signal Transduction, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.
Bioinformatics. 2010 Jul 1;26(13):1666-8. doi: 10.1093/bioinformatics/btq260. Epub 2010 May 26.
Lysine acetylation is a post-translational protein modification and a primary regulatory mechanism that controls many cell signaling processes. Lysine acetylation sites are recognized by acetyltransferases and deacetylases through sequence patterns (motifs). Recently, we used high-resolution mass spectrometry to identify 3600 lysine acetylation sites on 1750 human proteins covering most of the previously annotated sites and providing the most comprehensive acetylome so far. This dataset should provide an excellent source to train support vector machines (SVMs) allowing the high accuracy in silico prediction of acetylated lysine residues.
We developed a SVM to predict acetylated residues. The precision of our acetylation site predictor is 78% at 78% recall on input data containing equal numbers of modified and non-modified residues.
The online predictor is available at http://www.phosida.com
赖氨酸乙酰化是一种翻译后蛋白质修饰，也是控制许多细胞信号转导过程的主要调控机制。赖氨酸乙酰化位点通过序列模式（基序）被乙酰转移酶和去乙酰化酶识别。最近，我们使用高分辨率质谱法在 1750 个人类蛋白质上鉴定了 3600 个赖氨酸乙酰化位点，这些位点覆盖了大多数先前注释的位点，并提供了迄今为止最全面的乙酰组。该数据集应该为训练支持向量机（SVM）提供一个极好的资源，从而可以在包含等量修饰和非修饰残基的输入数据上进行高精度的计算乙酰化赖氨酸残基的预测。
我们开发了一种 SVM 来预测乙酰化残基。在包含等量修饰和非修饰残基的输入数据上，我们的乙酰化位点预测器的精度为 78%，召回率为 78%。
在线预测器可在 http://www.phosida.com 上获得。
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