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Find out if your protein is O-GlcNAc modified: The O-GlcNAc database. FASEB J 2022 May;36 Suppl 1

Date

05/14/2022

Pubmed ID

35555657

DOI

10.1096/fasebj.2022.36.S1.R4178

Scopus ID

2-s2.0-85130007238

Abstract

Post-translational modifications (PTMs) are ubiquitous and essential for protein function and signaling, motivating the need for sustainable benefit and open models of web databases. Highly conserved O-GlcNAcylation is a case example of one of the most recently discovered PTMs, investigated by a growing community. Historically, details about O-GlcNAcylated proteins and sites were dispersed across literature and in non-O-GlcNAc-focused, rapidly outdated or now defunct web databases. In a first effort to fill the gap, we recently published a human O-GlcNAcome catalog with a basic web interface. Based on the enthusiasm generated by this first resource, we extended our O-GlcNAcome catalog to include data from 42 distinct organisms and released the O-GlcNAc Database v1.2. In this version, more than 14 500 O-GlcNAcylated proteins and 11 000 O-GlcNAcylation sites are referenced from the curation of 2200 publications. Here, we present the extensive features of the O-GlcNAc Database, including the user-friendly interface, back-end and client-server interactions. Finally, this database system can be administrated with little to no programming skills and is meant to be an example of a useful, sustainable and cost-efficient resource, which exclusively relies on free open-source software elements (www.oglcnac.mcw.edu).

Author List

Olivier-Van Stichelen S, Malard F, Berendt R, Wulff-Fuentes E, Danner L

Author

Stephanie Olivier-Van Stichelen PhD Assistant Professor in the Biochemistry department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Acetylglucosamine
Databases, Factual
Humans
Protein Processing, Post-Translational
Proteins
Software