HS3ST3B1

Heparan sulfate (glucosamine) 3-O-sulfotransferase 3B1, also known as HS3ST3B1, is a human gene.cite web | title = Entrez Gene: HS3ST3B1 heparan sulfate (glucosamine) 3-O-sulfotransferase 3B1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9953| accessdate = ] PBB_Summary
section_title =
summary_text = 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. 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.cite web | title = Entrez Gene: HS3ST3B1 heparan sulfate (glucosamine) 3-O-sulfotransferase 3B1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9953| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Razi N, Lindahl U |title=Biosynthesis of heparin/heparan sulfate. The D-glucosaminyl 3-O-sulfotransferase reaction: target and inhibitor saccharides. |journal=J. Biol. Chem. |volume=270 |issue= 19 |pages= 11267–75 |year= 1995 |pmid= 7744762 |doi=
*cite journal | author=Shworak NW, Liu J, Petros LM, "et al." |title=Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci. |journal=J. Biol. Chem. |volume=274 |issue= 8 |pages= 5170–84 |year= 1999 |pmid= 9988767 |doi=
*cite journal | author=Liu J, Shworak NW, Sinaÿ P, "et al." |title=Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities. |journal=J. Biol. Chem. |volume=274 |issue= 8 |pages= 5185–92 |year= 1999 |pmid= 9988768 |doi=
*cite journal | author=Shukla D, Liu J, Blaiklock P, "et al." |title=A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. |journal=Cell |volume=99 |issue= 1 |pages= 13–22 |year= 1999 |pmid= 10520990 |doi=
*cite journal | author=Salehi LB, Mangino M, De Serio S, "et al." |title=Assignment of a locus for autosomal dominant idiopathic scoliosis (IS) to human chromosome 17p11. |journal=Hum. Genet. |volume=111 |issue= 4-5 |pages= 401–4 |year= 2002 |pmid= 12384783 |doi= 10.1007/s00439-002-0785-4
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Moon AF, Edavettal SC, Krahn JM, "et al." |title=Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1. |journal=J. Biol. Chem. |volume=279 |issue= 43 |pages= 45185–93 |year= 2004 |pmid= 15304505 |doi= 10.1074/jbc.M405013200
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504

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