HS3ST3A1

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Heparan sulfate (glucosamine) 3-O-sulfotransferase 3A1
PDB rendering based on 1t8t.
Available structures: 1t8t, 1t8u
Identifiers
Symbol(s) HS3ST3A1; 30ST3A1; 3OST3A1
External IDs OMIM: 604057 MGI: 1333861 HomoloGene: 88735
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 9955 15478
Ensembl ENSG00000153976 ENSMUSG00000047759
Uniprot Q9Y663 Q52KJ0
Refseq NM_006042 (mRNA)
NP_006033 (protein)		 NM_178870 (mRNA)
NP_849201 (protein)
Location Chr 17: 13.34 - 13.45 Mb Chr 11: 64.25 - 64.34 Mb
Pubmed search [1] [2]

Heparan sulfate (glucosamine) 3-O-sulfotransferase 3A1, also known as HS3ST3A1, 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

  1. ^ a b Entrez Gene: HS3ST3A1 heparan sulfate (glucosamine) 3-O-sulfotransferase 3A1.

[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. 
  • Liu J, Shriver Z, Blaiklock P, et al. (2000). "Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues.". J. Biol. Chem. 274 (53): 38155–62. PMID 10608887. 
  • 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:10.1007/s00439-002-0785-4. 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:10.1073/pnas.242603899. PMID 12477932. 
  • 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. PMID 12975309. 
  • 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:10.1074/jbc.M405013200. 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:10.1101/gr.2596504. PMID 15489334. 
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