| 释义 |
- References
- Further reading
{{Infobox_gene}}Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 is an enzyme that in humans is encoded by the HS3ST3A1 gene.[1][2]{{PBB_Summary
| section_title =
| summary_text = 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. 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.[2]
}}References1. ^{{cite journal |vauthors=Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD | 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 |date=Mar 1999 | pmid = 9988767 | pmc = | doi =10.1074/jbc.274.8.5170 }}
2. ^1 {{cite web | title = Entrez Gene: HS3ST3A1 heparan sulfate (glucosamine) 3-O-sulfotransferase 3A1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9955| accessdate = }}
Further reading{{refbegin | 2}}- {{cite journal |vauthors=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=10.1074/jbc.270.19.11267 }}
- {{cite journal |vauthors=Liu J, Shworak NW, Sinaÿ P, etal |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=10.1074/jbc.274.8.5185 }}
- {{cite journal |vauthors=Shukla D, Liu J, Blaiklock P, etal |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=10.1016/S0092-8674(00)80058-6 }}
- {{cite journal |vauthors=Liu J, Shriver Z, Blaiklock P, etal |title=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues. |journal=J. Biol. Chem. |volume=274 |issue= 53 |pages= 38155–62 |year= 2000 |pmid= 10608887 |doi=10.1074/jbc.274.53.38155 }}
- {{cite journal |vauthors=Salehi LB, Mangino M, De Serio S, etal |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 |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 }}
- {{cite journal |vauthors=Clark HF, Gurney AL, Abaya E, etal |title=The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265–70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 | pmc=403697 }}
- {{cite journal |vauthors=Moon AF, Edavettal SC, Krahn JM, etal |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 |pmc=4114238 |doi= 10.1074/jbc.M405013200 }}
- {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 | pmc=528928 }}
{{refend}}{{PDB Gallery|geneid=9955}}{{gene-17-stub}} |