CHST2

Carbohydrate sulfotransferase 2 is an enzyme that in humans is encoded by the CHST2 gene.

CHST2
Identifiers
Aliases	CHST2, C6ST, GST-2, GST2, Gn6ST-1, HEL-S-75, glcNAc6ST-1, carbohydrate sulfotransferase 2
External IDs	OMIM: 603798; MGI: 1891160; HomoloGene: 3150; GeneCards: CHST2; OMA:CHST2 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3q24 Start 143,119,771 bp End 143,124,014 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9|9 E3.3 Start 95,281,345 bp End 95,288,775 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in decidua lateral nuclear group of thalamus hair follicle trabecular bone cartilage tissue spinal cord C1 segment olfactory bulb granulocyte subthalamic nucleus Top expressed in supraoptic nucleus olfactory tubercle habenula ascending aorta medial geniculate nucleus aortic valve subiculum lateral septal nucleus lateral geniculate nucleus medial dorsal nucleus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity sulfotransferase activity N-acetylglucosamine 6-O-sulfotransferase activity Cellular component integral component of membrane Golgi membrane trans-Golgi network intrinsic component of Golgi membrane membrane Golgi apparatus Biological process multicellular organism development sulfur compound metabolic process inflammatory response keratan sulfate biosynthetic process N-acetylglucosamine metabolic process carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9435 54371 Ensembl ENSG00000175040 ENSMUSG00000033350 UniProt Q9Y4C5 Q80WV3 RefSeq (mRNA) NM_004267 NM_018763 RefSeq (protein) NP_004258 NP_061233 Location (UCSC) Chr 3: 143.12 – 143.12 Mb Chr 9: 95.28 – 95.29 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

External links

• Human CHST2 genome location and CHST2 gene details page in the UCSC Genome Browser.

Further reading

• Bernstein HB, Compans RW (1992). "Sulfation of the human immunodeficiency virus envelope glycoprotein". J. Virol. 66 (12): 6953–9. doi:10.1128/JVI.66.12.6953-6959.1992. PMC 240329. PMID 1433500.
• Shilatifard A, Merkle RK, Helland DE, et al. (1993). "Complex-type N-linked oligosaccharides of gp120 from human immunodeficiency virus type 1 contain sulfated N-acetylglucosamine". J. Virol. 67 (2): 943–52. doi:10.1128/JVI.67.2.943-952.1993. PMC 237448. PMID 8419650.
• Uchimura K, Muramatsu H, Kadomatsu K, et al. (1998). "Molecular cloning and characterization of an N-acetylglucosamine-6-O-sulfotransferase". J. Biol. Chem. 273 (35): 22577–83. doi:10.1074/jbc.273.35.22577. PMID 9712885.
• Uchimura K, Muramatsu H, Kaname T, et al. (1998). "Human N-acetylglucosamine-6-O-sulfotransferase involved in the biosynthesis of 6-sulfo sialyl Lewis X: molecular cloning, chromosomal mapping, and expression in various organs and tumor cells". J. Biochem. 124 (3): 670–8. doi:10.1093/oxfordjournals.jbchem.a022164. PMID 9722682.
• Tu L, Murphy PG, Li X, Tedder TF (1999). "L-selectin ligands expressed by human leukocytes are HECA-452 antibody-defined carbohydrate epitopes preferentially displayed by P-selectin glycoprotein ligand-1". J. Immunol. 163 (9): 5070–8. doi:10.4049/jimmunol.163.9.5070. PMID 10528213.
• Sakaguchi H, Kitagawa H, Sugahara K (2000). "Functional expression and genomic structure of human N-acetylglucosamine-6-O-sulfotransferase that transfers sulfate to beta-N-acetylglucosamine at the nonreducing end of an N-acetyllactosamine sequence". Biochim. Biophys. Acta. 1523 (2–3): 269–76. doi:10.1016/s0304-4165(00)00136-7. PMID 11042394.
• Okuda T, Mita S, Yamauchi S, et al. (2001). "Molecular cloning, expression, and chromosomal mapping of human chondroitin 4-sulfotransferase, whose expression pattern in human tissues is different from that of chondroitin 6-sulfotransferase". J. Biochem. 128 (5): 763–70. doi:10.1093/oxfordjournals.jbchem.a022813. PMID 11056388.
• Li X, Tu L, Murphy PG, et al. (2001). "CHST1 and CHST2 sulfotransferase expression by vascular endothelial cells regulates shear-resistant leukocyte rolling via L-selectin". J. Leukoc. Biol. 69 (4): 565–74. doi:10.1189/jlb.69.4.565. PMID 11310842. S2CID 8888883.
• Uchimura K, El-Fasakhany FM, Hori M, et al. (2002). "Specificities of N-acetylglucosamine-6-O-sulfotransferases in relation to L-selectin ligand synthesis and tumor-associated enzyme expression". J. Biol. Chem. 277 (6): 3979–84. doi:10.1074/jbc.M106587200. PMID 11726653.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Grunwell JR, Rath VL, Rasmussen J, et al. (2003). "Characterization and mutagenesis of Gal/GlcNAc-6-O-sulfotransferases". Biochemistry. 41 (52): 15590–600. doi:10.1021/bi0269557. PMID 12501187.
• de Graffenried CL, Bertozzi CR (2003). "Golgi localization of carbohydrate sulfotransferases is a determinant of L-selectin ligand biosynthesis". J. Biol. Chem. 278 (41): 40282–95. doi:10.1074/jbc.M304928200. PMID 12855678.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• de Graffenried CL, Bertozzi CR (2004). "The stem region of the sulfotransferase GlcNAc6ST-1 is a determinant of substrate specificity". J. Biol. Chem. 279 (38): 40035–43. doi:10.1074/jbc.M405709200. PMID 15220337.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Chen L, Ichihara-Tanaka K, Muramatsu T (2005). "Role of the carboxyl-terminal region in the activity of N-acetylglucosamine 6-o-sulfotransferase-1". J. Biochem. 136 (5): 659–64. doi:10.1093/jb/mvh162. PMID 15632306.
• Kanoh A, Seko A, Ideo H, et al. (2007). "Ectopic expression of N-acetylglucosamine 6-O-sulfotransferase 2 in chemotherapy-resistant ovarian adenocarcinomas". Glycoconj. J. 23 (5–6): 453–60. doi:10.1007/s10719-006-6979-6. PMID 16897186. S2CID 22628478.