O-GlcNAcAtlas: A database of experimentally identified O-GlcNAc sites and proteins
O-GlcNAcAtlas: A database of experimentally identified O-GlcNAc sites and proteins
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DOI：
10.1093/glycob/cwab003
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发表时间：
2021-01-12
期刊：
影响因子：
4.3
通讯作者：
Wu, Ci
中科院分区：
文献类型：
--
作者：
Ma, Junfeng;Li, Yaoxiang;Wu, Ci
O-连接的β-N-乙酰葡糖胺（O-GlcNAc）是一种翻译后修饰（即，O-GlcNAc酰化）作用于蛋白质的丝氨酸/苏氨酸残基。蛋白质O-GlcNAc酰化作为一种独特的细胞内单糖修饰，在几乎所有的生物化学过程中起着重要的作用。异常的O-GlcNAc酰化是许多慢性疾病病因的基础。随着研究技术的不断进步，人们已经发现了数千种具有O-GlcNAc位点的蛋白质沿着被发现。然而，到目前为止，几乎没有专门的数据库来容纳这种信息的快速积累。因此，创建O-GlcNAcAtlas以整合所有实验识别的O-GlcNAc位点和蛋白质。O-GlcNAc图谱由两个数据集组成（数据集-I和数据集-II，分别用于明确识别的位点和模糊识别的位点），代表了1984年至2019年12月31日研究的所有种属中共计4571种O-GlcNAc修饰蛋白。对于每种蛋白质，提供了全面的信息（包括种属、样品类型、基因符号、修饰肽和/或修饰位点、位点作图方法和参考文献）。为了解决从不同来源收集的数据之间的异质性，将这些报道的O-GlcNAc肽的序列同一性映射到UniProtKB蛋白条目。据我们所知，O-GlcNAc图谱是一个高度全面和严格管理的数据库，涵盖了过去35年中发现的所有O-GlcNAc位点和蛋白质。我们期望O-GlcNAcAtlas将是一个有用的资源，以促进O-GlcNAc的研究和蛋白质O-GlcNAcylation的计算分析。O-GlcNAcAtlas的网络界面的公开版本可以在http://oglcnac.org/找到。
O-linked beta-N-acetylglucosamine (O-GlcNAc) is a post-translational modification (i.e., O-GlcNAcylation) on the serine/threonine residues of proteins. As a unique intracellular monosaccharide modification, protein O-GlcNAcylation plays important roles in almost all biochemical processes examined. Aberrant O-GlcNAcylation underlies the etiologies of a number of chronic diseases. With the tremendous improvement of techniques, thousands of proteins along with their O-GlcNAc sites have been reported. However, until now, there are few databases dedicated to accommodate the rapid accumulation of such information. Thus, O-GlcNAcAtlas is created to integrate all experimentally identified O-GlcNAc sites and proteins. O-GlcNAcAtlas consists of two datasets (Dataset-I and Dataset-II, for unambiguously identified sites and ambiguously identified sites, respectively), representing a total number of 4571 O-GlcNAc modified proteins from all species studied from 1984 to 31 Dec 2019. For each protein, comprehensive information (including species, sample type, gene symbol, modified peptides and/or modification sites, site mapping methods and literature references) is provided. To solve the heterogeneity among the data collected from different sources, the sequence identity of these reported O-GlcNAc peptides are mapped to the UniProtKB protein entries. To our knowledge, O-GlcNAcAtlas is a highly comprehensive and rigorously curated database encapsulating all O-GlcNAc sites and proteins identified in the past 35 years. We expect that O-GlcNAcAtlas will be a useful resource to facilitate O-GlcNAc studies and computational analyses of protein O-GlcNAcylation. The public version of the web interface to the O-GlcNAcAtlas can be found at http://oglcnac.org/.