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bioRxiv · 10.1101/2020.11.25.397042

O-GlcNAcAtlas: A Database of Experimentally Identified O-GlcNAc Sites and Proteins

Abstract

O-linked {beta}-N-acetylglucosamine (O-GlcNAc) is a post-translational modification (i.e., O-GlcNAcylation) on 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 (including cancer, diabetes, and neurodegenerative disease). With the tremendous improvement of techniques, thousands of proteins along with their O-GlcNAc sites have been reported. However, until now there is no database dedicated to accommodate the rapid accumulation of such information. Thus, O-GlcNAcAtlas is created to integrate all experimentally identified O-GlcNAc sites and proteins from 1984 to Dec, 2019. 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. For each protein, comprehensive information (including gene name, organism, 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 the comprehensive and 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 which will facilitate site-specific O-GlcNAc functional studies and computational analyses of protein O-GlcNAcylation. The public version of the web interface to the O-GlcNAcAtlas can be found at https://oglcnac.org.

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BibTeXRIS

Ma, J., Li, Y., Hou, C., Wu, C.. 2020-11-26. O-GlcNAcAtlas: A Database of Experimentally Identified O-GlcNAc Sites and Proteins. https://doi.org/10.1101/2020.11.25.397042

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