CHST2

Protein-coding gene in the species Homo sapiens
CHST2
Identifiers
AliasesCHST2, C6ST, GST-2, GST2, Gn6ST-1, HEL-S-75, glcNAc6ST-1, carbohydrate sulfotransferase 2
External IDsOMIM: 603798; MGI: 1891160; HomoloGene: 3150; GeneCards: CHST2; OMA:CHST2 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for CHST2
Genomic location for CHST2
Band3q24Start143,119,771 bp[1]
End143,124,014 bp[1]
Gene location (Mouse)
Chromosome 9 (mouse)
Chr.Chromosome 9 (mouse)[2]
Chromosome 9 (mouse)
Genomic location for CHST2
Genomic location for CHST2
Band9|9 E3.3Start95,281,345 bp[2]
End95,288,775 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 9: 95.28 – 95.29 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Carbohydrate sulfotransferase 2 is an enzyme that in humans is encoded by the CHST2 gene.[5][6]


References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000175040 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033350 – 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. ^ 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.
  6. ^ "Entrez Gene: CHST2 carbohydrate (N-acetylglucosamine-6-O) sulfotransferase 2".

External links

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.


  • v
  • t
  • e