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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Autores principales: Eugenia Wulff-Fuentes, Rex R. Berendt, Logan Massman, Laura Danner, Florian Malard, Jeet Vora, Robel Kahsay, Stephanie Olivier-Van Stichelen
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/8c8aa8966a2e44bf99d37ac7766f0212
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spelling 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)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle 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
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