Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.
Sci Signal. 2010 Aug 31;3(137):rs2. doi: 10.1126/scisignal.2001099.
Although various databases have been established that are designed to compile an ever-growing list of protein phosphorylation sites in plants and animals, no such repository exists for viruses. Here, we developed the viral posttranslational modification (virPTM) database, which contains a comprehensive list of 329 accurately localized phosphorylation sites in proteins from 52 human viruses published between 1986 and the present. Additionally, to aid in the detection of new viral phosphorylation sites, we used the scan-x tool to make thousands of high-specificity serine, threonine, and tyrosine phosphorylation predictions in 229 viruses that replicate in human cells. By cross-validating our prediction results with the literature-based entries in the virPTM database, we highlight the effectiveness of the scan-x tool with viral data and extrapolate the existence of at least 4000 as yet unidentified phosphorylation sites on hundreds of viral proteins. Together, these results imply a substantial role for human kinases in mediating viral protein functions and suggest, more generally, that viral primary structure may provide important clues to aid in the rational design of therapeutic agents.
尽管已经建立了各种数据库，旨在编译动植物中不断增长的蛋白质磷酸化位点列表，但对于病毒却没有这样的存储库。在这里，我们开发了病毒翻译后修饰（virPTM）数据库，其中包含了 52 种人类病毒在 1986 年至现在发表的蛋白质中 329 个准确定位的磷酸化位点的综合列表。此外，为了帮助检测新的病毒磷酸化位点，我们使用 scan-x 工具在 229 种在人类细胞中复制的病毒中进行了数千次高特异性丝氨酸、苏氨酸和酪氨酸磷酸化预测。通过将我们的预测结果与 virPTM 数据库中基于文献的条目进行交叉验证，我们突出了 scan-x 工具在病毒数据中的有效性，并推断出数百种病毒蛋白上至少存在 4000 个尚未确定的磷酸化位点。这些结果共同表明，人类激酶在介导病毒蛋白功能方面发挥着重要作用，并更普遍地表明，病毒的一级结构可能提供重要线索，有助于合理设计治疗剂。
