GAL3ST3
| GAL3ST3 | ||||||
|---|---|---|---|---|---|---|
| Identifiers | ||||||
| Aliases | GAL3ST3, GAL3ST-3, GAL3ST2, galactose-3-O-sulfotransferase 3 | |||||
| External IDs | MGI: 3617843 HomoloGene: 57198 GeneCards: GAL3ST3 | |||||
| Orthologs | ||||||
| Species | Human | Mouse | ||||
| Entrez | ||||||
| Ensembl | ||||||
| UniProt | ||||||
| RefSeq (mRNA) | ||||||
| RefSeq (protein) | ||||||
| Location (UCSC) | Chr 11: 66.04 – 66.05 Mb | Chr 19: 5.3 – 5.31 Mb | ||||
| PubMed search | [1] | [2] | ||||
| Wikidata | ||||||
| View/Edit Human | View/Edit Mouse |
Galactose-3-O-sulfotransferase 3 is an enzyme that in humans is encoded by the GAL3ST3 gene.[3][4][5]
This gene encodes a member of the galactose-3-O-sulfotransferase protein family. The product of this gene catalyzes sulfonation by transferring a sulfate group to the 3' position of galactose in N-acetyllactosamine in both type 2 (Gal-beta-1-4GlcNAc-R) oligosaccharides and core-2-branched O-glycans, but not on type 1 or core-1-branched structures. This gene, which has also been referred to as GAL3ST2, is different from the GAL3ST2 gene located on chromosome 2 that encodes a related enzyme with distinct tissue distribution and substrate specificities, compared to galactose-3-O-sulfotransferase 3.[5]
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ Suzuki A, Hiraoka N, Suzuki M, Angata K, Misra AK, McAuliffe J, Hindsgaul O, Fukuda M (Jun 2001). "Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans". J Biol Chem. 276 (26): 24388–95. doi:10.1074/jbc.M103135200. PMID 11323440.
- ↑ El-Fasakhany FM, Uchimura K, Kannagi R, Muramatsu T (Jul 2001). "A novel human Gal-3-O-sulfotransferase: molecular cloning, characterization, and its implications in biosynthesis of (SO(4)-3)Galbeta1-4(Fucalpha1-3)GlcNAc". J Biol Chem. 276 (29): 26988–94. doi:10.1074/jbc.M100348200. PMID 11356829.
- 1 2 "Entrez Gene: GAL3ST3 galactose-3-O-sulfotransferase 3".
Further reading
- 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. - Chandrasekaran EV, Lakhaman SS, Chawda R, et al. (2004). "Identification of physiologically relevant substrates for cloned Gal: 3-O-sulfotransferases (Gal3STs): distinct high affinity of Gal3ST-2 and LS180 sulfotransferase for the globo H backbone, Gal3ST-3 for N-glycan multiterminal Galbeta1, 4GlcNAcbeta units and 6-sulfoGalbeta1, 4GlcNAcbeta, and Gal3ST-4 for the mucin core-2 trisaccharide". J. Biol. Chem. 279 (11): 10032–41. doi:10.1074/jbc.M311989200. PMID 14701868.
- 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.
- Seko A, Hara-Kuge S, Yamashita K (2001). "Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1-->3galNAc residue in O-glycans". J. Biol. Chem. 276 (28): 25697–704. doi:10.1074/jbc.M101558200. PMID 11333265.
- Chandrasekaran EV, Jain RK, Rhodes JM, et al. (2000). "Characterization of distinct Gal:3-O-sulfotransferase activities in human tumor epithelial cell lines and of calf lymph node GlcNAc : 6-O-sulfotransferase activity". Glycoconj. J. 16 (9): 523–36. doi:10.1023/A:1007074005371. PMID 10815989.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
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