CHST2

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)
End	143,124,014 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	95,288,775 bp
RNA expression pattern
	Top expressed in
	hair follicle; ; cancellous bone; ; spinal cord; ; olfactory bulb; ; subthalamic nucleus; ; internal globus pallidus; ; medulla oblongata; ; cerebellar vermis; ; trigeminal ganglion; ; inferior olivary nucleus;
	Top expressed in
	supraoptic nucleus; ; olfactory tubercle; ; habenula; ; ascending aorta; ; medial geniculate nucleus; ; aortic valve; ; subiculum; ; lateral geniculate nucleus; ; medial dorsal nucleus; ; hippocampus proper;
	More reference expression data
	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
	9435
	54371
	ENSG00000175040
	ENSMUSG00000033350
	Q9Y4C5
	Q80WV3
	NM_004267
	NM_018763
	NP_004258
	NP_061233
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 04, 2023

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

Related Research Articles

Selectin P ligand, also known as SELPLG or CD162, is a human gene.

Carbohydrate sulfotransferase 6 is an enzyme that in humans is encoded by the CHST6 gene.

Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the GCNT1 gene.

Carbohydrate sulfotransferase 4 is an enzyme that in humans is encoded by the CHST4 gene.

Carbohydrate sulfotransferase 1 is an enzyme that in humans is encoded by the CHST1 gene.

N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase is an enzyme that in humans is encoded by the NAGPA gene.

Carbohydrate sulfotransferase 15 is an enzyme that in humans is encoded by the CHST15 gene. It belongs to the N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase enzyme class.

Galactose-3-O-sulfotransferase 2 is an enzyme that in humans is encoded by the GAL3ST2 gene.

Carbohydrate sulfotransferase 5 is an enzyme that in humans is encoded by the CHST5 gene.

Carbohydrate sulfotransferase 11 is an enzyme that in humans is encoded by the CHST11 gene.

Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 is an enzyme that in humans is encoded by the HS3ST3A1 gene.

Disintegrin and metalloproteinase domain-containing protein 28 is an enzyme that in humans is encoded by the ADAM28 gene.

Carbohydrate sulfotransferase 12 is an enzyme that in humans is encoded by the CHST12 gene.

Heparan sulfate 2-O-sulfotransferase 1 is an enzyme that in humans is encoded by the HS2ST1 gene.

Heparan sulfate glucosamine 3-O-sulfotransferase 3B1 is an enzyme that in humans is encoded by the HS3ST3B1 gene. Heparan sulfate biosynthetic enzymes are key components in generating myriad distinct heparan sulfate fine structures that carry out multiple biologic activities. The enzyme encoded by this gene is a member of the heparan sulfate biosynthetic enzyme family. It is a type II integral membrane protein and possesses heparan sulfate glucosaminyl 3-O-sulfotransferase activity ( HS3ST3A1). The Sulfotransferase domain of this enzyme is highly similar to the same domain of heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1 and these two enzymes sulfate an identical disaccharide. This gene is widely expressed, with the most abundant expression in liver and placenta.

Carbohydrate sulfotransferase 7 is an enzyme that in humans is encoded by the CHST7 gene.

Galactose-3-O-sulfotransferase 3 is an enzyme that in humans is encoded by the GAL3ST3 gene.

Carbohydrate sulfotransferase 10 is an enzyme that in humans is encoded by the CHST10 gene.

<span class="mw-page-title-main">Carbohydrate sulfotransferase</span>

Carbohydrate sulfotransferases are sulfotransferase enzymes that transfer sulfate to carbohydrate groups in glycoproteins and glycolipids. Carbohydrates are used by cells for a wide range of functions from structural purposes to extracellular communication. Carbohydrates are suitable for such a wide variety of functions due to the diversity in structure generated from monosaccharide composition, glycosidic linkage positions, chain branching, and covalent modification. Possible covalent modifications include acetylation, methylation, phosphorylation, and sulfation. Sulfation, performed by carbohydrate sulfotransferases, generates carbohydrate sulfate esters. These sulfate esters are only located extracellularly, whether through excretion into the extracellular matrix (ECM) or by presentation on the cell surface. As extracellular compounds, sulfated carbohydrates are mediators of intercellular communication, cellular adhesion, and ECM maintenance.

Carbohydrate sulfotransferase 13 is a protein that is encoded in humans by the CHST13 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000175040 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033350 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ "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 .

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. 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000175040 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid10049591-5] 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.

[entrez-6] "Entrez Gene: CHST2 carbohydrate (N-acetylglucosamine-6-O) sulfotransferase 2".

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CHST2

Contents

Related Research Articles

References

External links

Further reading