HS3ST3B1
From Wikipedia, the free encyclopedia
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Heparan sulfate (glucosamine) 3-O-sulfotransferase 3B1
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| PDB rendering based on 1t8t. | ||||||||||||||
| Available structures: 1t8t, 1t8u | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbol(s) | HS3ST3B1; 30ST3B1; 3OST3B1 | |||||||||||||
| External IDs | OMIM: 604058 MGI: 1333853 HomoloGene: 88576 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 9953 | 54710 | ||||||||||||
| Ensembl | ENSG00000125430 | ENSMUSG00000070407 | ||||||||||||
| Uniprot | Q9Y662 | Q3TA92 | ||||||||||||
| Refseq | NM_006041 (mRNA) NP_006032 (protein) |
NM_018805 (mRNA) NP_061275 (protein) |
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| Location | Chr 17: 14.15 - 14.19 Mb | Chr 11: 63.7 - 63.74 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Heparan sulfate (glucosamine) 3-O-sulfotransferase 3B1, also known as HS3ST3B1, is a human gene.[1] 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.[1]
[edit] References
[edit] Further reading
- 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. PMID 7744762.
- Shworak NW, Liu J, Petros LM, et al. (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. PMID 9988767.
- 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. PMID 9988768.
- Shukla D, Liu J, Blaiklock P, et al. (1999). "A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry.". Cell 99 (1): 13–22. PMID 10520990.
- Salehi LB, Mangino M, De Serio S, et al. (2002). "Assignment of a locus for autosomal dominant idiopathic scoliosis (IS) to human chromosome 17p11.". Hum. Genet. 111 (4-5): 401–4. doi:. PMID 12384783.
- 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:. PMID 12477932.
- 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:. PMID 14702039.
- Moon AF, Edavettal SC, Krahn JM, et al. (2004). "Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1.". J. Biol. Chem. 279 (43): 45185–93. doi:. PMID 15304505.
- 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:. PMID 15489334.

