CHST2

Carbohydrate sulfotransferase 2 is an enzyme that in humans is encoded by the CHST2 gene.[4][5]

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
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3q24 Start 143,119,771 bp[1] End 143,124,014 bp[1]
RNA expression pattern 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	n/a
UniProt	Q9Y4C5	Q80WV3
RefSeq (mRNA)	NM_004267	NM_018763
RefSeq (protein)	NP_004258	NP_061233
Location (UCSC)	Chr 3: 143.12 – 143.12 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCh38: Ensembl release 89: ENSG00000175040 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Li X, Tedder TF (May 1999). "CHST1 and CHST2 sulfotransferases expressed by human vascular endothelial cells: cDNA cloning, expression, and chromosomal localization". Genomics. 55 (3): 345–7. doi:10.1006/geno.1998.5653. PMID 10049591.
5. "Entrez Gene: CHST2 carbohydrate (N-acetylglucosamine-6-O) sulfotransferase 2".

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. 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. 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. 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. PMID 11310842.
• 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. 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.