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Protein Glycosylation

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...

Oligosaccharide Assembly

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

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Related Experiment Video

Updated: Apr 16, 2026

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

Glycomic analysis using KEGG GLYCAN.

Kiyoko F Aoki-Kinoshita¹, Minoru Kanehisa

¹Department of Bioinformatics, Faculty of Engineering, Soka University, 1-236 Tangi-machi, Hachioji, Tokyo, 192-8577, Japan, kkiyoko@soka.ac.jp.

Methods in Molecular Biology (Clifton, N.J.)

|March 11, 2015

Summary

The KEGG GLYCAN database offers comprehensive glycan structures and their connections to various biological entities and processes within KEGG. It also provides analytical tools for exploring these complex carbohydrate data.

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Area of Science:

Glycomics
Bioinformatics
Systems Biology

Background:

The KEGG GLYCAN database is a key component of the KEGG resource, focusing on carbohydrate structures.
Glycans play crucial roles in various biological processes, necessitating a structured database for their study.

Purpose of the Study:

To describe the KEGG GLYCAN database and its integrated features.
To introduce the analytical tools available for glycan data exploration.

Main Methods:

Description of the KEGG GLYCAN database structure and content.
Explanation of the interconnections between KEGG GLYCAN and other KEGG databases.
Overview of analytical tools such as Composite Structure Map (CSM), KegDraw, KCam, and GECS.

Main Results:

KEGG GLYCAN provides detailed glycan structures linked to genes, orthologs, reactions, pathways, drugs, and diseases.
Integration with other KEGG resources allows for a systems-level understanding of glycans.
Availability of specialized tools facilitates the analysis and visualization of glycan data.

Conclusions:

KEGG GLYCAN serves as a valuable resource for glycomics research.
The database and its associated tools support the investigation of glycan functions in health and disease.
Enhanced accessibility and analytical capabilities promote further research in carbohydrate science.