Minguez Pablo, Bork Peer
Department of Genetics and Genomics, Instituto de Investigacion Sanitaria-University Hospital Fundacion Jimenez Diaz (IIS-FJD), Avda. Reyes Católicos 2, 28040, Madrid, Spain.
European Molecular Biology Laboratory, Structural and Computational Biology Unit, 69117, Heidelberg, Germany.
Methods Mol Biol. 2017;1558:303-320. doi: 10.1007/978-1-4939-6783-4_14.
Post-translational modifications (PTMs) are an important source of protein regulation; they fine-tune the function, localization, and interaction with other molecules of the majority of proteins and are partially responsible for their multifunctionality. Usually, proteins have several potential modification sites, and their patterns of occupancy are associated with certain functional states. These patterns imply cross talk among PTMs within and between proteins, the majority of which are still to be discovered. Several methods detect associations between PTMs; these have recently combined into a global resource, the PTMcode database, which contains already known and predicted functional associations between pairs of PTMs from more than 45,000 proteins in 19 eukaryotic species.
翻译后修饰（PTMs）是蛋白质调控的重要来源；它们对大多数蛋白质的功能、定位以及与其他分子的相互作用进行微调，并部分地决定了它们的多功能性。通常，蛋白质有多个潜在的修饰位点，其占据模式与特定的功能状态相关。这些模式意味着蛋白质内部和之间的PTMs存在相互作用，其中大部分仍有待发现。有几种方法可检测PTMs之间的关联；这些方法最近整合到了一个全球资源——PTMcode数据库中，该数据库包含了19种真核生物中45000多种蛋白质的PTM对之间已知和预测的功能关联。
