CHST7

Carbohydrate sulfotransferase 7 is an enzyme that in humans is encoded by the CHST7 gene.[5][6]

CHST7
Identifiers
Aliases	CHST7, C6ST-2, GST-5, carbohydrate sulfotransferase 7
External IDs	OMIM: 300375 MGI: 1891767 HomoloGene: 10531 GeneCards: CHST7
Gene location (Human) Chr. X chromosome (human)[1] Band Xp11.3 Start 46,573,765 bp[1] End 46,598,496 bp[1]
Gene location (Mouse) Chr. X chromosome (mouse)[2] Band X|X A1.3 Start 20,059,560 bp[2] End 20,097,521 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • sulfotransferase activity • N-acetylglucosamine 6-O-sulfotransferase activity • chondroitin 6-sulfotransferase activity Cellular component • integral component of membrane • Golgi membrane • Golgi apparatus • membrane • trans-Golgi network Biological process • sulfur compound metabolic process • chondroitin sulfate biosynthetic process • N-acetylglucosamine metabolic process • polysaccharide metabolic process • carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	56548	60322
Ensembl	ENSG00000147119	ENSMUSG00000037347
UniProt	Q9NS84	Q9EP78
RefSeq (mRNA)	NM_019886	NM_021715
RefSeq (protein)	NP_063939	NP_068361
Location (UCSC)	Chr X: 46.57 – 46.6 Mb	Chr X: 20.06 – 20.1 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene belongs to the sulfotransferase gene family. Sulfotransferases generate sulfated glycosaminoglycan (GAG) moieties during chondroitin sulfate biosynthesis. They create considerable structural diversity among chondroitin sulfates by transferring sulfate with remarkable specificity for the underlying oligosaccharide substrate. This gene product mainly transfers sulfate to N-acetylgalactosamine. The regulated expression of each member of this gene family may be an important determinant of sulfated GAGs expression and the associated function of chondroitin sulfates as regulators of many biologic processes. This gene is part of a gene cluster on chromosome Xp11.23.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000147119 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000037347 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Kitagawa H, Fujita M, Ito N, Sugahara K (Aug 2000). "Molecular cloning and expression of a novel chondroitin 6-O-sulfotransferase". J Biol Chem. 275 (28): 21075–80. doi:10.1074/jbc.M002101200. PMID 10781596.
6. "Entrez Gene: CHST7 carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 7".

External links

• Human CHST7 genome location and CHST7 gene details page in the UCSC Genome Browser.

Further reading

• Liu T, Qian WJ, Gritsenko MA, et al. (2006). "Human Plasma N-Glycoproteome Analysis by Immunoaffinity Subtraction, Hydrazide Chemistry, and Mass Spectrometry". J. Proteome Res. 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952.
• Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome". Nature. 434 (7031): 325–37. doi:10.1038/nature03440. PMC 2665286. PMID 15772651.
• 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.
• 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.
• Thiselton DL, McDowall J, Brandau O, et al. (2002). "An integrated, functionally annotated gene map of the DXS8026-ELK1 interval on human Xp11.3-Xp11.23: potential hotspot for neurogenetic disorders". Genomics. 79 (4): 560–72. doi:10.1006/geno.2002.6733. PMID 11944989.
• Bhakta S, Bartes A, Bowman KG, et al. (2001). "Sulfation of N-acetylglucosamine by chondroitin 6-sulfotransferase 2 (GST-5)". J. Biol. Chem. 275 (51): 40226–34. doi:10.1074/jbc.M006414200. PMID 10956661.
• Uchimura K, Fasakhany F, Kadomatsu K, et al. (2000). "Diversity of N-acetylglucosamine-6-O-sulfotransferases: molecular cloning of a novel enzyme with different distribution and specificities". Biochem. Biophys. Res. Commun. 274 (2): 291–6. doi:10.1006/bbrc.2000.3141. PMID 10913333.
• 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.
• Bernstein HB, Compans RW (1992). "Sulfation of the human immunodeficiency virus envelope glycoprotein". J. Virol. 66 (12): 6953–9. PMC 240329. PMID 1433500.