GAL3ST3

GAL3ST3
Identifiers
AliasesGAL3ST3, GAL3ST-3, GAL3ST2, galactose-3-O-sulfotransferase 3
External IDsMGI: 3617843 HomoloGene: 57198 GeneCards: GAL3ST3
Gene location (Human)
Chr.Chromosome 11 (human)[1]
Band11q13.1Start66,041,952 bp[1]
End66,049,180 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

89792

545276

Ensembl

ENSG00000175229

ENSMUSG00000047658

UniProt

Q96A11

P61315

RefSeq (mRNA)

NM_033036

NM_001024717

RefSeq (protein)

NP_149025

NP_001019888

Location (UCSC)Chr 11: 66.04 – 66.05 MbChr 19: 5.3 – 5.31 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Galactose-3-O-sulfotransferase 3 is an enzyme that in humans is encoded by the GAL3ST3 gene.[5][6][7]

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.[7]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000175229 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000047658 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ 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.
  6. ↑ 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.
  7. 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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