<?xml version="1.0" encoding="UTF-8" standalone="yes"?>

<!-- Copyright (c) 2004-2026 Broad Institute, Inc., Massachusetts Institute of Technology, and Regents of the University of California.  All rights reserved.
     See license terms at www.gsea-msigdb.org/gsea/license_terms_list. Please note that certain gene sets have special access terms.
-->
<MSIGDB BUILD_DATE="Jan 29, 2026" VERSION="2026.1.Hs" NAME="export">
    <GENESET STANDARD_NAME="KEGG_GLYCOSAMINOGLYCAN_BIOSYNTHESIS_CHONDROITIN_SULFATE" SYSTEMATIC_NAME="M19166" HISTORICAL_NAMES="" PMID="" AUTHORS="" GEOID="" EXACT_SOURCE="hsa00532" GENESET_LISTING_URL="" EXTERNAL_DETAILS_URL="http://www.genome.jp/pathway/hsa00532" CHIP="Human_NCBI_Gene_ID" CONTRIBUTOR="KEGG" CONTRIBUTOR_ORG="Kyoto Encyclopedia of Genes and Genomes" DESCRIPTION_BRIEF="Glycosaminoglycan biosynthesis - chondroitin sulfate" DESCRIPTION_FULL="Glycosaminoglycans (GAGs) are linear polysaccharide chains consisting of repeating disaccharide units and form proteglycans by covalently attaching to their core proteins. Chondroitin sulfate (CS) is a glycosaminoglycan with the disaccharide unit GalNAc(b1-4)GlcA(b1-3), modified with ester-linked sulfate at certain positions. Dermatan sulfate (DS) is a modified form of CS, in which a portion of D-glucuronate residues is epimerized to L-iduronates. CS and DS are linked to serine residues in core proteins via a linkage tetrasaccharide formed by the transfer of xylose and three more residues. The assembly process of CS is initiated by the transfer of N-acetylgalactosamine to the linkage tetrasaccharide. The polymerization step is catalyzed by bifunctional enzymes (chondroitin synthases) that have both b13 glucuronosyltransferase and b14 N-acetylgalactosaminyltransferase activities. Chondroitin polymerization also requires the action of the chondroitin polymerizing factor. Sulfation of chondroitin in vertebrates is a complex process, with multiple sulfotransferases involved in 4-O sulfation and 6-O sulfation of N-acetylgalactosamine residues. Additional enzymes exist for epimerization of glucuronic acid to iduronic acid in DS, sulfation at the C-2 position of the uronic acids, and other patterns of sulfation found in unusual species of chondroitin." TAGS="" MEMBERS="10090,11285,113189,126792,135152,166012,22856,26229,27087,29940,337876,50515,51363,54480,55454,55501,55790,56548,64131,64132,79586,9469" MEMBERS_SYMBOLIZED="B3GALT6,B3GAT1,B3GAT2,B3GAT3,B4GALT7,CHPF,CHPF2,CHST11,CHST12,CHST13,CHST14,CHST15,CHST3,CHST7,CHSY1,CHSY3,CSGALNACT1,CSGALNACT2,DSE,UST,XYLT1,XYLT2" MEMBERS_EZID="10090,11285,113189,126792,135152,166012,22856,26229,27087,29940,337876,50515,51363,54480,55454,55501,55790,56548,64131,64132,79586,9469" MEMBERS_MAPPING="10090,UST,10090|11285,B4GALT7,11285|113189,CHST14,113189|126792,B3GALT6,126792|135152,B3GAT2,135152|166012,CHST13,166012|22856,CHSY1,22856|26229,B3GAT3,26229|27087,B3GAT1,27087|29940,DSE,29940|337876,CHSY3,337876|50515,CHST11,50515|51363,CHST15,51363|54480,CHPF2,54480|55454,CSGALNACT2,55454|55501,CHST12,55501|55790,CSGALNACT1,55790|56548,CHST7,56548|64131,XYLT1,64131|64132,XYLT2,64132|79586,CHPF,79586|9469,CHST3,9469" FILTERED_BY_SIMILARITY="" FOUNDER_NAMES="" REFINEMENT_DATASETS="" VALIDATION_DATASETS="" CATEGORY_CODE="C2" ORGANISM="Homo sapiens" SUB_CATEGORY_CODE="CP:KEGG_LEGACY"/>
</MSIGDB>
