Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database
Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database
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DOI：
10.1038/srep00090
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发表时间：
2011-09-13
影响因子：
4.6
通讯作者：
Floudas, Christodoulos A.
中科院分区：
文献类型：
--
作者：
Khoury, George A.;Baliban, Richard C.;Floudas, Christodoulos A.
翻译后修饰（ptm）广泛地促进了最近蛋白质组学数据的爆炸式增长，并且具有超过蛋白质设计的复杂性。ptm是蛋白质翻译后的化学修饰，具有广泛的作用，拓宽了蛋白质的功能范围。根据以前的估计，人们普遍认为超过一半的蛋白质是糖蛋白。虽然每个位点只能发生一次突变，但不同形式的翻译后修饰可能串联发生。随着修饰的数量和丰度不断被发现，没有办法轻易地评估它们的相对水平。在这里，我们报告了从高质量的人工整理的蛋白质组数据中通过实验和推测发现的每个PTM的相对丰度，并表明最多只有不到五分之一的蛋白质被糖基化。我们向学术界提供一个持续更新的资源（http://selene.princeton.edu/PTMCuration），其中包含统计数据，以便科学家可以评估每种PTM存在的“数量”。
Post-translational modifications (PTMs) broadly contribute to the recent explosion of proteomic data and possess a complexity surpassing that of protein design. PTMs are the chemical modification of a protein after its translation, and have wide effects broadening its range of functionality. Based on previous estimates, it is widely believed that more than half of proteins are glycoproteins. Whereas mutations can only occur once per position, different forms of post-translational modifications may occur in tandem. With the number and abundances of modifications constantly being discovered, there is no method to readily assess their relative levels. Here we report the relative abundances of each PTM found experimentally and putatively, from high-quality, manually curated, proteome-wide data, and show that at best, less than one-fifth of proteins are glycosylated. We make available to the academic community a continuously updated resource (http://selene.princeton.edu/PTMCuration) containing the statistics so scientists can assess "how many'' of each PTM exists.