DisProt Database: A Central Repository of Information on Intrinsically Disordered Proteins

这个奖项是根据2009年美国复苏和再投资法案(公法第111-5条)资助的。印第安纳大学被授予扩大和改进可公开访问的蛋白质数据库(http://www.DisProt.org).)的赠款该数据库现在包含约500个蛋白质条目的序列和功能信息，这些条目具有1000多个经过实验表征的固有无序区域。这项将得到资助的工作将极大地扩大这个数据库中蛋白质的数量，扩大各种蛋白质的信息阵列，改善这个数据库的特点和可用性，发现与无序蛋白质和区域相关的新功能，并开始开发内在无序蛋白质的本体。本质上无序的蛋白质执行各种各样的功能。最近的一项生物信息学研究表明，至少~1/3的蛋白质相关功能依赖于蛋白质的紊乱。这些无序依赖的功能是关键细胞过程的基础，如基因调控、细胞分裂、蛋白质-蛋白质相互作用网络的组织、决定功能的信号通路的形成和调控等。DisProt数据库的开发将证实，许多被怀疑依赖于蛋白质紊乱的特定生物功能实际上确实依赖于紊乱，将显示许多特定紊乱例子的共性，将导致发现依赖于紊乱的生物功能的新例子，并将首次提供对紊乱在细胞中的作用的全面评估。关于内在无序蛋白质的中央信息库有可能改变细胞、分子、化学和系统生物学、生物化学和生物物理学的整个领域，通过揭示各种基本重要的生物过程对蛋白质无序的共同和关键依赖。

"This award is funded under the American Recovery and Reinvestment Act of 2009 (Public Law 111-5)."Indiana University is awarded a grant to expand and improve a publicly accessible Database of Protein (http://www.DisProt.org). This database now contains sequence and functional information for ~ 500 protein entries that have more than 1000 experimentally characterized regions of intrinsic disorder. The work to be funded will greatly expand the number of proteins in this database, will enlarge the array of information for the various proteins, will improve the features and usability of this database, will discover new functions associated with disordered proteins and regions, and will begin the development of an ontology for intrinsically disordered protein. Intrinsically disordered proteins carry out a wide variety of functions. A recent bioinformatics study suggests that, at a minimum, ~ 1/3 of protein-associated functions depend on protein disorder. These disorder-dependent functions underlie critical cellular processes such as gene regulation, cell division, organization of protein-protein interaction networks, formation and regulation of function-determining signaling pathways, and so on. Development of the DisProt Database will confirm that many particular biological functions suspected to depend on protein disorder actually do depend on disorder, will show the generality of many particular disorder examples, will lead to the discovery of new examples of disorder-dependent biological functions, and will provide for the first time a comprehensive evaluation of the roles of disorder in the cell. A central repository of information on intrinsically disordered proteins has the potential of transforming the entire fields of cellular, molecular, chemical, and systems biology; biochemistry; and biophysics by revealing the common and critical dependence on protein disorder for a wide variety of fundamentally important biological processes.