The human O-GlcNAcome database and meta-analysis
Abstract Over the past 35 years, ~1700 articles have characterized protein O-GlcNAcylation. Found in almost all living organisms, this post-translational modification of serine and threonine residues is highly conserved and key to biological processes. With half of the primary research articles usin...
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2021
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oai:doaj.org-article:8c8aa8966a2e44bf99d37ac7766f02122021-12-02T15:23:29ZThe human O-GlcNAcome database and meta-analysis10.1038/s41597-021-00810-42052-4463https://doaj.org/article/8c8aa8966a2e44bf99d37ac7766f02122021-01-01T00:00:00Zhttps://doi.org/10.1038/s41597-021-00810-4https://doaj.org/toc/2052-4463Abstract Over the past 35 years, ~1700 articles have characterized protein O-GlcNAcylation. Found in almost all living organisms, this post-translational modification of serine and threonine residues is highly conserved and key to biological processes. With half of the primary research articles using human models, the O-GlcNAcome recently reached a milestone of 5000 human proteins identified. Herein, we provide an extensive inventory of human O-GlcNAcylated proteins, their O-GlcNAc sites, identification methods, and corresponding references ( www.oglcnac.mcw.edu ). In the absence of a comprehensive online resource for O-GlcNAcylated proteins, this list serves as the only database of O-GlcNAcylated proteins. Based on the thorough analysis of the amino acid sequence surrounding 7002 O-GlcNAc sites, we progress toward a more robust semi-consensus sequence for O-GlcNAcylation. Moreover, we offer a comprehensive meta-analysis of human O-GlcNAcylated proteins for protein domains, cellular and tissue distribution, and pathways in health and diseases, reinforcing that O-GlcNAcylation is a master regulator of cell signaling, equal to the widely studied phosphorylation.Eugenia Wulff-FuentesRex R. BerendtLogan MassmanLaura DannerFlorian MalardJeet VoraRobel KahsayStephanie Olivier-Van StichelenNature PortfolioarticleScienceQENScientific Data, Vol 8, Iss 1, Pp 1-11 (2021) |
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Science Q Eugenia Wulff-Fuentes Rex R. Berendt Logan Massman Laura Danner Florian Malard Jeet Vora Robel Kahsay Stephanie Olivier-Van Stichelen The human O-GlcNAcome database and meta-analysis |
description |
Abstract Over the past 35 years, ~1700 articles have characterized protein O-GlcNAcylation. Found in almost all living organisms, this post-translational modification of serine and threonine residues is highly conserved and key to biological processes. With half of the primary research articles using human models, the O-GlcNAcome recently reached a milestone of 5000 human proteins identified. Herein, we provide an extensive inventory of human O-GlcNAcylated proteins, their O-GlcNAc sites, identification methods, and corresponding references ( www.oglcnac.mcw.edu ). In the absence of a comprehensive online resource for O-GlcNAcylated proteins, this list serves as the only database of O-GlcNAcylated proteins. Based on the thorough analysis of the amino acid sequence surrounding 7002 O-GlcNAc sites, we progress toward a more robust semi-consensus sequence for O-GlcNAcylation. Moreover, we offer a comprehensive meta-analysis of human O-GlcNAcylated proteins for protein domains, cellular and tissue distribution, and pathways in health and diseases, reinforcing that O-GlcNAcylation is a master regulator of cell signaling, equal to the widely studied phosphorylation. |
format |
article |
author |
Eugenia Wulff-Fuentes Rex R. Berendt Logan Massman Laura Danner Florian Malard Jeet Vora Robel Kahsay Stephanie Olivier-Van Stichelen |
author_facet |
Eugenia Wulff-Fuentes Rex R. Berendt Logan Massman Laura Danner Florian Malard Jeet Vora Robel Kahsay Stephanie Olivier-Van Stichelen |
author_sort |
Eugenia Wulff-Fuentes |
title |
The human O-GlcNAcome database and meta-analysis |
title_short |
The human O-GlcNAcome database and meta-analysis |
title_full |
The human O-GlcNAcome database and meta-analysis |
title_fullStr |
The human O-GlcNAcome database and meta-analysis |
title_full_unstemmed |
The human O-GlcNAcome database and meta-analysis |
title_sort |
human o-glcnacome database and meta-analysis |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/8c8aa8966a2e44bf99d37ac7766f0212 |
work_keys_str_mv |
AT eugeniawulfffuentes thehumanoglcnacomedatabaseandmetaanalysis AT rexrberendt thehumanoglcnacomedatabaseandmetaanalysis AT loganmassman thehumanoglcnacomedatabaseandmetaanalysis AT lauradanner thehumanoglcnacomedatabaseandmetaanalysis AT florianmalard thehumanoglcnacomedatabaseandmetaanalysis AT jeetvora thehumanoglcnacomedatabaseandmetaanalysis AT robelkahsay thehumanoglcnacomedatabaseandmetaanalysis AT stephanieoliviervanstichelen thehumanoglcnacomedatabaseandmetaanalysis AT eugeniawulfffuentes humanoglcnacomedatabaseandmetaanalysis AT rexrberendt humanoglcnacomedatabaseandmetaanalysis AT loganmassman humanoglcnacomedatabaseandmetaanalysis AT lauradanner humanoglcnacomedatabaseandmetaanalysis AT florianmalard humanoglcnacomedatabaseandmetaanalysis AT jeetvora humanoglcnacomedatabaseandmetaanalysis AT robelkahsay humanoglcnacomedatabaseandmetaanalysis AT stephanieoliviervanstichelen humanoglcnacomedatabaseandmetaanalysis |
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