CHST7

CHST7
Identifiers
AliasesCHST7, C6ST-2, GST-5, carbohydrate sulfotransferase 7
External IDsMGI: 1891767 HomoloGene: 10531 GeneCards: CHST7
Gene location (Human)
Chr.X chromosome (human)[1]
BandXp11.3Start46,573,784 bp[1]
End46,598,408 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
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 MbChr X: 20.06 – 20.1 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

Function

This gene belongs to the sulfotransferase gene family. Sulfotransferases generate sulfated glycosaminoglycan (GAG) moities 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. 1 2 3 GRCh38: Ensembl release 89: ENSG00000147119 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000037347 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  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. 1 2 "Entrez Gene: CHST7 carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 7".

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.


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