Department of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University Medical Center, Washington, DC 20057, USA.
Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, Liaoning 116023, China.
Glycobiology. 2021 Aug 7;31(7):719-723. doi: 10.1093/glycob/cwab003.
O-linked β-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/.
O-连接的β-N-乙酰氨基葡萄糖（O-GlcNAc）是蛋白质丝氨酸/苏氨酸残基上的一种翻译后修饰（即 O-GlcNAcylation）。作为一种独特的细胞内单糖修饰，蛋白质 O-GlcNAcylation 在几乎所有已研究的生化过程中都发挥着重要作用。异常的 O-GlcNAcylation 是许多慢性疾病的病因之一。随着技术的巨大进步，已经报道了数千种蛋白质及其 O-GlcNAc 位点。然而，到目前为止，还没有专门的数据库来容纳这些信息的快速积累。因此，创建了 O-GlcNAcAtlas 来整合所有实验鉴定的 O-GlcNAc 位点和蛋白质。O-GlcNAcAtlas 由两个数据集（Dataset-I 和 Dataset-II，分别用于明确鉴定的位点和模糊鉴定的位点）组成，代表了自 1984 年至 2019 年 12 月 31 日所有研究物种中共有 4571 种 O-GlcNAc 修饰蛋白。对于每个蛋白质，都提供了全面的信息（包括物种、样本类型、基因符号、修饰肽和/或修饰位点、位点映射方法和文献参考）。为了解决从不同来源收集的数据的异质性，这些报道的 O-GlcNAc 肽的序列同一性被映射到 UniProtKB 蛋白质条目。据我们所知，O-GlcNAcAtlas 是一个高度全面和严格编辑的数据库，包含了过去 35 年中鉴定的所有 O-GlcNAc 位点和蛋白质。我们希望 O-GlcNAcAtlas 将成为一个有用的资源，促进 O-GlcNAc 研究和蛋白质 O-GlcNAcylation 的计算分析。O-GlcNAcAtlas 的公共网络界面版本可在 http://oglcnac.org/ 找到。
