HS3ST1

From Wikipedia, the free encyclopedia


Heparan sulfate (glucosamine) 3-O-sulfotransferase 1
PDB rendering based on 1vkj.
Available structures: 1vkj, 1zrh
Identifiers
Symbol(s) HS3ST1; 3OST; 3OST1
External IDs OMIM: 603244 MGI1201606 HomoloGene3751
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 9957 15476
Ensembl ENSG00000002587 ENSMUSG00000051022
Uniprot O14792 O35310
Refseq NM_005114 (mRNA)
NP_005105 (protein)
NM_010474 (mRNA)
NP_034604 (protein)
Location Chr 4: 11.01 - 11.04 Mb Chr 5: 39.9 - 39.93 Mb
Pubmed search [1] [2]

Heparan sulfate (glucosamine) 3-O-sulfotransferase 1, also known as HS3ST1, 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 possesses both heparan sulfate glucosaminyl 3-O-sulfotransferase activity, anticoagulant heparan sulfate conversion activity, and is a rate limiting enzyme for synthesis of anticoagulant heparan. This enzyme is an intraluminal Golgi resident protein.[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. 
  • Liu J, Shworak NW, Fritze LM, et al. (1996). "Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase.". J. Biol. Chem. 271 (43): 27072–82. PMID 8900198. 
  • Shworak NW, Liu J, Fritze LM, et al. (1997). "Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase.". J. Biol. Chem. 272 (44): 28008–19. PMID 9346953. 
  • 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. 
  • Hernaiz M, Liu J, Rosenberg RD, Linhardt RJ (2000). "Enzymatic modification of heparan sulfate on a biochip promotes its interaction with antithrombin III.". Biochem. Biophys. Res. Commun. 276 (1): 292–7. doi:10.1006/bbrc.2000.3453. PMID 11006120. 
  • 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. 
  • 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:10.1038/ng1285. PMID 14702039. 
  • Edavettal SC, Carrick K, Shah RR, et al. (2004). "A conformational change in heparan sulfate 3-O-sulfotransferase-1 is induced by binding to heparan sulfate.". Biochemistry 43 (16): 4680–8. doi:10.1021/bi0499112. PMID 15096036. 
  • 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.