HS2ST1
Heparan sulfate 2-O-sulfotransferase 1 | |||||||||||||
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Identifiers | |||||||||||||
Symbols | HS2ST1 ; dJ604K5.2 | ||||||||||||
External IDs | OMIM: 604844 MGI: 1346049 HomoloGene: 8025 GeneCards: HS2ST1 Gene | ||||||||||||
EC number | 2.8.2.- | ||||||||||||
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Orthologs | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | 9653 | 23908 | |||||||||||
Ensembl | ENSG00000153936 | ENSMUSG00000040151 | |||||||||||
UniProt | Q7LGA3 | Q8R3H7 | |||||||||||
RefSeq (mRNA) | NM_001134492 | NM_011828 | |||||||||||
RefSeq (protein) | NP_001127964 | NP_035958 | |||||||||||
Location (UCSC) |
Chr 1: 86.91 – 87.11 Mb |
Chr 3: 144.43 – 144.57 Mb | |||||||||||
PubMed search | |||||||||||||
Heparan sulfate 2-O-sulfotransferase 1 is an enzyme that in humans is encoded by the HS2ST1 gene.[1][2]
Heparan sulfate biosynthetic enzymes are key components in generating a myriad of distinct heparan sulfate fine structures that carry out multiple biologic activities. This gene encodes heparan sulfate 2-O-sulfotransferase, a member of the heparan sulfate biosynthetic enzyme family. This family member transfers sulfate to the 2 position of the iduronic acid residue of heparan sulfate. The disruption of this gene resulted in no kidney formation in knockout embryonic mice, indicating that the absence of this enzyme may interfere with the signaling required for kidney formation.[2]
References
- ↑ Seki N, Ohira M, Nagase T, Ishikawa K, Miyajima N, Nakajima D, Nomura N, Ohara O (Feb 1998). "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain". DNA Res 4 (5): 345–9. doi:10.1093/dnares/4.5.345. PMID 9455484.
- 1 2 "Entrez Gene: HS2ST1 heparan sulfate 2-O-sulfotransferase 1".
Further reading
- Muramatsu T (2000). "Essential roles of carbohydrate signals in development, immune response and tissue functions, as revealed by gene targeting". J. Biochem. 127 (2): 171–6. doi:10.1093/oxfordjournals.jbchem.a022590. PMID 10731680.
- Rong J, Habuchi H, Kimata K, et al. (2000). "Expression of heparan sulphate L-iduronyl 2-O-sulphotransferase in human kidney 293 cells results in increased D-glucuronyl 2-O-sulphation". Biochem. J. 346 (2): 463–8. doi:10.1042/0264-6021:3460463. PMC 1220874. PMID 10677367.
- 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. PMC 139241. 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.
- Aquino RS, Landeira-Fernandez AM, Valente AP, et al. (2005). "Occurrence of sulfated galactans in marine angiosperms: evolutionary implications". Glycobiology 15 (1): 11–20. doi:10.1093/glycob/cwh138. PMID 15317737.
- 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. PMC 528928. PMID 15489334.
- Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
- Xu D, Song D, Pedersen LC, Liu J (2007). "Mutational study of heparan sulfate 2-O-sulfotransferase and chondroitin sulfate 2-O-sulfotransferase". J. Biol. Chem. 282 (11): 8356–67. doi:10.1074/jbc.M608062200. PMID 17227754.
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