CHST7

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 19,925,799 bp [2] End 19,963,760 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Stromal cell of endometrium left ventricle canal of the cervix left coronary artery subcutaneous adipose tissue monocyte gastric mucosa spleen blood right lobe of liver Top expressed in proximal tubule primitive streak interventricular septum secondary oocyte kidney atrioventricular valve endocardial cushion calvaria soleus muscle left lung More reference expression data BioGPS 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: 19.93 – 19.96 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/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) 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. Bibcode:2005Natur.434..325R. 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. Bibcode:2002PNAS...9916899M. 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. doi:10.1128/JVI.67.2.943-952.1993. PMC   237448 . PMID   8419650.
• 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.