OGP (O-glycoprotein) database was designed and built as a comprehensive knowledgebase for O-glycoproteins. It also includes a module for O-glycosylation site prediction based on the current available glycosylated sites data.
Statistical analysis module provides an overview of the database status: number of recorded proteins, sites and site-specific glycans; distribution of recorded species and pathway analysis or disease clustering for human source recorded O-glycosylated proteins.
Database search module is designed for users to search with parameters like UniProt protein accession number, protein name, gene name, or glycan. Useful links to UniProt for registered proteins and to NCBI PubMed for related reference are also provided.
Site prediction module includes an inherent example of site prediction model. Users can submit ordered sequence (11 amino acid with S/T in the middle of the sequence) of fasta-type protein sequence to get site prediction results.
Data submission module allows users to submit high confident O-glycosylation data that consists well annotated mass spectral data with clear site determination evidence or fragment ions to make this database more comprehensive.
1. OGP is a comprehensive repository of experimentally characterized O-glycoproteins. There is also a prediction tool for O-glycosylated sites based on currently recorded O-glycosylation data. This database will surely facilitate research in O-glycosylation research.
2. pGlycoQuant: a collaborative development new tool, designed for precise and minuscule-missing-value quantitative glycoproteomics. Downloading page: http://www.oglyp.org/pglycoquant/
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Recent Advances in Software Tools for More Generic and Precise Intact Glycopeptide Analysis. Cao W, Liu M, Kong S, Wu M, Zhang Y, Yang P. Molecular & Cellular Proteomics. 2021 Feb; 100060.
Fast and comprehensive N- and O-glycoproteomics analysis with MSFragger-Glyco. Daniel A. Polasky, Fengchao Yu, Guo Ci Teo & Alexey I. Nesvizhskii. Nat Methods. 2020 Nov; 17(11): 1125–1132.
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Oxidative release of natural glycans for functional glycomics. Song X, Ju H, Lasanajak Y, Kudelka MR, Smith DF, Cummings RD. Nat Methods. 2016 Jun;13(6):528-34.
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