Protein O-GlcNAcylation has been documented in all metazoans (including animals, insects, and plants), some bacteria, fungi, and viruses. O-GlcNAcylation occurs on many proteins in nuclear, cytosolic, and mitochondria. As a critical modification, O-GlcNAc functions in a species-, tissue-/cell-, protein-, and site-specific manner.If you find this resource helpful, please cite our paper (Ma J., et al. O-GlcNAcAtlas: A database of experimentally identified O-GlcNAc sites and proteins. Glycobiology 2021, 31, 7, 719-723. DOI: 10.1093/glycob/cwab003 ) in your publications.
(Regarding the basics and latest advances in characterization of O-GlcNAcylation and O-GlcNAc proteins, please feel free to explore more @ Ma J. et al., Analytical and biochemical perspectives of protein O-GlcNAcylation. Chemical Reviews 2021, 121, 3, 1513-1581. DOI: 10.1021/acs.chemrev.0c00884).
(Regarding a systems perspective of O-GlcNAcylation and O-GlcNAcylated proteins/sites, please feel free to explore more @ Ma J. et al., Demystifying the O‑GlcNAc Code: A Systems View. Chemical Reviews 2022. DOI:10.1021/acs.chemrev.1c01006 ).
The current version: O-GlcNAcAtalas_2.0