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O-linked β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) is a monosaccharide modification on proteins predominantly inside cells. It is widely appreciated that spatiotemporal protein O-GlcNAcylation regulates a plethora of biological processes. High-throughput analytical techniques, particularly site-specific O-GlcNAc proteomics, have tremendously advanced the profiling of O-GlcNAc proteomes. Recently we established O-GlcNAcAtlas, a highly curated database of O-GlcNAc proteins/peptides/sites from experiments reported in the past forty years. However, a resource for O-GlcNAcylation quantification information is not available yet. Herein, we provide an updated database O-GlcNAcAtlas 4.0 by incorporating information of O-GlcNAcylation quantification. Exhaustive curation of published literature yielded a total of about 5,400 quantification events for 3,130 unique O-GlcNAc sites. The quantification vales were then systematically integrated with the specific O-GlcNAc sites and catalogued in O-GlcNAcAtlas, with key experimental details (including sample sources, conditions and methods) presented. Taken together, we present O-GlcNAcAtlas 4.0, a unique database hosting qualitative and quantitative data of O-GlcNAcylation on proteins. As a comprehensive repository supplemented with protein O-GlcNAcylation dynamics, the updated database will further facilitate related functional investigations by the biomedical community. O-GlcNAcAtlas 4.0 is freely accessible at https://oglcnac.org/atlas/.

O-linked β-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. 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 Dec. 31, 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/.