Carbohydrate (chondroitin 4) sulfotransferase 13

CHST13
Identifiers
Aliases	CHST13, C4ST3, carbohydrate sulfotransferase 13, Carbohydrate (chondroitin 4) sulfotransferase 13
External IDs	OMIM: 610124 MGI: 1919047 HomoloGene: 44360 GeneCards: CHST13
Gene location (Human) Chr. Chromosome 3 (human) Band 3q21.3 Start 126,524,155 bp End 126,543,291 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6|6 D1 Start 90,285,331 bp End 90,302,167 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver monocyte tibia blood spleen kidney bone marrow oocyte duodenum right uterine tube Top expressed in yolk sac bone marrow liver left lobe of liver blastocyst proximal tubule calvaria spermatocyte body of femur cervix More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity N-acetylgalactosamine 4-O-sulfotransferase activity sulfotransferase activity chondroitin 4-sulfotransferase activity Cellular component integral component of membrane Golgi membrane Golgi apparatus membrane Biological process chondroitin sulfate biosynthetic process carbohydrate biosynthetic process carbohydrate metabolic process proteoglycan biosynthetic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 166012 71797 Ensembl ENSG00000180767 ENSMUSG00000056643 UniProt Q8NET6 D3Z6E3 RefSeq (mRNA) NM_152889 NM_027928 RefSeq (protein) NP_690849 NP_082204 Location (UCSC) Chr 3: 126.52 – 126.54 Mb Chr 6: 90.29 – 90.3 Mb PubMed search
Wikidata
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Carbohydrate (chondroitin 4) sulfotransferase 13 is a protein that is encoded in humans by the CHST13 gene.

Function

The protein encoded by this gene belongs to the sulfotransferase 2 family. It is localized to the golgi membrane, and catalyzes the transfer of sulfate to the C4 hydroxyl of beta-1,4-linked N-acetylgalactosamine (GalNAc) flanked by glucuronic acid residue in chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices.

Further reading

• Kang HG, Evers MR, Xia G, Baenziger JU, Schachner M (September 2002). "Molecular cloning and characterization of chondroitin-4-O-sulfotransferase-3. A novel member of the HNK-1 family of sulfotransferases". The Journal of Biological Chemistry. 277 (38): 34766–72. doi:10.1074/jbc.M204907200. PMID 12080076.
• Valente B, Campos PA, do Rosário VE, Silveira H (October 2010). "Natural frequency of polymorphisms linked to the chondroitin 4-sulfotransferase genes and its association with placental malaria". Transactions of the Royal Society of Tropical Medicine and Hygiene. 104 (10): 687–9. doi:10.1016/j.trstmh.2010.05.005. PMID 20580388.
• Hiraoka N, Nakagawa H, Ong E, Akama TO, Fukuda MN, Fukuda M (June 2000). "Molecular cloning and expression of two distinct human chondroitin 4-O-sulfotransferases that belong to the HNK-1 sulfotransferase gene family". The Journal of Biological Chemistry. 275 (26): 20188–96. doi:10.1074/jbc.M002443200. PMID 10781601.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.