ST3GAL3

The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. This protein is a member of glycosyltransferase family 29. Multiple transcript variants encoding several different isoforms have been found for this gene.

Mutations in the ST3GAL3 gene was recently shown to be the cause of autosomal recessive mental retardation 12. Since the mutations disrupt a glycosylation pathway, this disorder may be considered a congenital disorder of glycosylation.

• Sialyltransferase

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• {{cite journal | vauthors = Kitagawa H, Paulson JC | title = Differential expression of five sialyltransferase genes in human tissues | journal = The Journal of Biological Chemistry | volume = 269 | issue = 27 | pages = 17872–8 | date = Jul 1994 | doi = 10.1016/S0021-9258(17)32390-6 | pmid = 8027041 | doi-access = free }}
• {{cite journal | vauthors = Kitagawa H, Paulson JC | title = Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase | journal = Biochemical and Biophysical Research Communications | volume = 194 | issue = 1 | pages = 375–82 | date = Jul 1993 | pmid = 8333853 | doi = 10.1006/bbrc.1993.1830 }}
• {{cite journal | vauthors = Burger PC, Lötscher M, Streiff M, Kleene R, Kaissling B, Berger EG | title = Immunocytochemical localization of alpha2,3(N)-sialyltransferase (ST3Gal III) in cell lines and rat kidney tissue sections: evidence for golgi and post-golgi localization | journal = Glycobiology | volume = 8 | issue = 3 | pages = 245–57 | date = Mar 1998 | pmid = 9451034 | doi = 10.1093/glycob/8.3.245 | doi-access = free }}
• {{cite journal | vauthors = Taniguchi A, Morishima T, Tsujita Y, Matsumoto Y, Matsumoto K | title = Genomic structure, expression, and transcriptional regulation of human Gal beta 1,3 GalNAc alpha 2,3-sialyltransferase gene | journal = Biochemical and Biophysical Research Communications | volume = 300 | issue = 2 | pages = 570–6 | date = Jan 2003 | pmid = 12504121 | doi = 10.1016/S0006-291X(02)02899-1 }}
• {{cite journal | vauthors = Taniguchi A, Saito K, Kubota T, Matsumoto K | title = Characterization of the promoter region of the human Galbeta1,3(4)GlcNAc alpha2,3-sialyltransferase III (hST3Gal III) gene | journal = Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression | volume = 1626 | issue = 1–3 | pages = 92–6 | date = Apr 2003 | pmid = 12697334 | doi = 10.1016/s0167-4781(03)00021-6 }}
• {{cite journal | vauthors = Saito S, Aoki H, Ito A, Ueno S, Wada T, Mitsuzuka K, Satoh M, Arai Y, Miyagi T | title = Human alpha2,3-sialyltransferase (ST3Gal II) is a stage-specific embryonic antigen-4 synthase | journal = The Journal of Biological Chemistry | volume = 278 | issue = 29 | pages = 26474–9 | date = Jul 2003 | pmid = 12716912 | doi = 10.1074/jbc.M213223200 | doi-access = free }}
• {{cite journal | vauthors = Grahn A, Barkhordar GS, Larson G | title = Cloning and sequencing of nineteen transcript isoforms of the human alpha2,3-sialyltransferase gene, ST3Gal III; its genomic organisation and expression in human tissues | journal = Glycoconjugate Journal | volume = 19 | issue = 3 | pages = 197–210 | date = Mar 2002 | pmid = 12815231 | doi = 10.1023/A:1024253808424 | s2cid = 23897339 }}
• {{cite journal | vauthors = Gretschel S, Haensch W, Schlag PM, Kemmner W | title = Clinical relevance of sialyltransferases ST6GAL-I and ST3GAL-III in gastric cancer | journal = Oncology | volume = 65 | issue = 2 | pages = 139–45 | year = 2003 | pmid = 12931020 | doi = 10.1159/000072339 | s2cid = 6438454 }}
• {{cite journal | vauthors = Jeanneau C, Chazalet V, Augé C, Soumpasis DM, Harduin-Lepers A, Delannoy P, Imberty A, Breton C | title = Structure-function analysis of the human sialyltransferase ST3Gal I: role of n-glycosylation and a novel conserved sialylmotif | journal = The Journal of Biological Chemistry | volume = 279 | issue = 14 | pages = 13461–8 | date = Apr 2004 | pmid = 14722111 | doi = 10.1074/jbc.M311764200 | doi-access =free }}
• {{cite journal | vauthors = Grahn A, Barkhordar GS, Larson G | title = Identification of seven new alpha2,3-sialyltransferase III, ST3Gal III, transcripts from human foetal brain | journal = Glycoconjugate Journal | volume = 20 | issue = 7–8 | pages = 493–500 | year = 2005 | pmid = 15316282 | doi = 10.1023/B:GLYC.0000038295.87747.0b | s2cid = 1544031 }}
• {{cite journal | vauthors = Van Dyken SJ, Green RS, Marth JD | title = Structural and mechanistic features of protein O glycosylation linked to CD8+ T-cell apoptosis | journal = Molecular and Cellular Biology | volume = 27 | issue = 3 | pages = 1096–111 | date = Feb 2007 | pmid = 17101770 | pmc = 1800694 | doi = 10.1128/MCB.01750-06 }}
• {{cite journal | vauthors = Hu H, Eggers K, Chen W, Garshasbi M, Motazacker MM, Wrogemann K, Kahrizi K, Tzschach A, Hosseini M, Bahman I, Hucho T, Mühlenhoff M, Gerardy-Schahn R, Najmabadi H, Ropers HH, Kuss AW | title = ST3GAL3 mutations impair the development of higher cognitive functions | journal = American Journal of Human Genetics | volume = 89 | issue = 3 | pages = 407–14 | date = Sep 2011 | doi = 10.1016/j.ajhg.2011.08.008 | pmid = 21907012 | pmc=3169827}}
• {{cite journal |vauthors=Szabo R, Skropeta D, etal |title=Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities. |journal=Med. Res. Rev. |volume=37 |issue=2 |pages= 210–270 |year= 2017 |doi= 10.1002/med.21407 |url=http://ro.uow.edu.au/cgi/viewcontent.cgi?article=5226&context=smhpapers |pmid=27678392|s2cid=26280291 }}

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