HS3ST2

Heparan sulfate glucosamine 3-O-sulfotransferase 2 is an enzyme that in humans is encoded by the HS3ST2 gene.[5][6]

HS3ST2
Identifiers
Aliases	HS3ST2, 30ST2, 3OST2, heparan sulfate-glucosamine 3-sulfotransferase 2
External IDs	OMIM: 604056 MGI: 1333802 HomoloGene: 21220 GeneCards: HS3ST2
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p12.2 Start 22,814,162 bp[1] End 22,916,338 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7 F2|7 65.07 cM Start 121,391,859 bp[2] End 121,501,770 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • sulfotransferase activity • [heparan sulfate-glucosamine 3-sulfotransferase 2 activity] • [heparan sulfate-glucosamine 3-sulfotransferase 1 activity] • heparan sulfate sulfotransferase activity Cellular component • integral component of membrane • Golgi membrane • Golgi apparatus • membrane Biological process • circadian rhythm • glycosaminoglycan biosynthetic process • heparan sulfate proteoglycan biosynthetic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9956	195646
Ensembl	ENSG00000122254	ENSMUSG00000046321
UniProt	Q9Y278	Q673U1
RefSeq (mRNA)	NM_006043	NM_001081327 NM_177575
RefSeq (protein)	NP_006034	NP_001074796
Location (UCSC)	Chr 16: 22.81 – 22.92 Mb	Chr 7: 121.39 – 121.5 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Heparan sulfate biosynthetic enzymes are key components in generating a myriad of 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. This gene is expressed predominantly in brain and may play a role in the nervous system.[6]

Role in breast cancer The HS3ST2 promoter is hypermethylated in breast cancer tissue compared to normal breast ducts, suggesting a potential involvement in the pathogenesis of the disease.[7] Functional analysis revealed that upregulation of HS3ST2 in human breast cancer cells resulted in altered invasiveness, which was due to changes in Mitogen-activated protein kinase signaling and matrix metalloproteinase expression.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000122254 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000046321 - 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. Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD (Mar 1999). "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci". J Biol Chem. 274 (8): 5170–84. doi:10.1074/jbc.274.8.5170. PMID 9988767.
6. "Entrez Gene: HS3ST2 heparan sulfate (glucosamine) 3-O-sulfotransferase 2".
7. Dietrich, Dimo (2009). "Analysis of DNA Methylation of Multiple Genes in Microdissected Cells From Formalin-fixed and Paraffin-embedded Tissues". Journal of Histochemistry and Cytochemistry. 57 (5): 477–489. doi:10.1369/jhc.2009.953026. PMC 2674771. PMID 19153192.
8. Vijaya Kumar, Archana (2014). "HS3ST2 modulates breast cancer cell invasiveness via MAP kinase- and Tcf4 (Tcf7l2)-dependent regulation of protease and cadherin expression". International Journal of Cancer. 135 (11): 2579–92. doi:10.1002/ijc.28921. PMID 24752740.

Further reading

• Lawrence R, Yabe T, Hajmohammadi S, et al. (2007). "The principal neuronal gD-type 3-O-sulfotransferases and their products in central and peripheral nervous system tissues". Matrix Biol. 26 (6): 442–55. doi:10.1016/j.matbio.2007.03.002. PMC 1993827. PMID 17482450.
• O'Donnell CD, Tiwari V, Oh MJ, Shukla D (2006). "A role for heparan sulfate 3-O-sulfotransferase isoform 2 in herpes simplex virus type 1 entry and spread". Virology. 346 (2): 452–9. doi:10.1016/j.virol.2005.11.003. PMID 16336986.
• 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.
• Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
• Miyamoto K, Asada K, Fukutomi T, et al. (2003). "Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers". Oncogene. 22 (2): 274–80. doi:10.1038/sj.onc.1206146. PMID 12527896.
• 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.
• Liu J, Shworak NW, Sinaÿ P, et al. (1999). "Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities". J. Biol. Chem. 274 (8): 5185–92. doi:10.1074/jbc.274.8.5185. PMID 9988768.
• Razi N, Lindahl U (1995). "Biosynthesis of heparin/heparan sulfate. The D-glucosaminyl 3-O-sulfotransferase reaction: target and inhibitor saccharides". J. Biol. Chem. 270 (19): 11267–75. doi:10.1074/jbc.270.19.11267. PMID 7744762.