[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/fut6-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/fut6-wikipedia\/","headline":"FUT6 – Wikipedia","name":"FUT6 – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Protein-coding gene in the species Homo sapiens Alpha-(1,3)-fucosyltransferase is an enzyme that in","datePublished":"2018-10-05","dateModified":"2018-10-05","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","url":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","height":"1","width":"1"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/fut6-wikipedia\/","about":["Wiki"],"wordCount":4279,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Protein-coding gene in the species Homo sapiensAlpha-(1,3)-fucosyltransferase is an enzyme that in humans is encoded by the FUT6 gene.[3][4][5]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4The alpha-1,3-fucosyltransferases constitute a large family of glycosyltransferases with a high degree of homology. The enzymes of this family comprise 3 main activity patterns called myeloid, plasma, and Lewis, based on their capacity to transfer alpha-L-fucose to distinct oligosaccharide acceptors, their sensitivity to N-ethylmaleimide inhibition, their cation requirements, and their tissue-specific expression patterns. The different categories of alpha-1,3-fucosyltransferases are sequentially expressed during embryo-fetal development.[supplied by OMIM][5]References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000156413 – Ensembl, May 2017^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ Koszdin KL, Bowen BR (Oct 1992). “The cloning and expression of a human alpha-1,3 fucosyltransferase capable of forming the E-selectin ligand”. Biochem Biophys Res Commun. 187 (1): 152\u20137. doi:10.1016\/S0006-291X(05)81472-X. PMID\u00a01520296.^ McCurley RS, Recinos A III, Olsen AS, Gingrich JC, Szczepaniak D, Cameron HS, Krauss R, Weston BW (Jul 1995). “Physical maps of human alpha (1,3)fucosyltransferase genes FUT3-FUT6 on chromosomes 19p13.3 and 11q21”. Genomics. 26 (1): 142\u20136. doi:10.1016\/0888-7543(95)80094-3. PMID\u00a07782074.^ a b “Entrez Gene: FUT6 fucosyltransferase 6 (alpha (1,3) fucosyltransferase)”.Further reading[edit]Weston BW, Smith PL, Kelly RJ, Lowe JB (1992). “Molecular cloning of a fourth member of a human alpha (1,3)fucosyltransferase gene family. Multiple homologous sequences that determine expression of the Lewis x, sialyl Lewis x, and difucosyl sialyl Lewis x epitopes”. J. Biol. Chem. 267 (34): 24575\u201384. doi:10.1016\/S0021-9258(18)35803-4. PMID\u00a01339443.Cameron HS, Szczepaniak D, Weston BW (1995). “Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms”. J. Biol. Chem. 270 (34): 20112\u201322. doi:10.1074\/jbc.270.34.20112. PMID\u00a07650030.Maruyama K, Sugano S (1994). “Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene. 138 (1\u20132): 171\u20134. doi:10.1016\/0378-1119(94)90802-8. PMID\u00a08125298.Mollicone R, Reguigne I, Fletcher A,  et\u00a0al. (1994). “Molecular basis for plasma alpha(1,3)-fucosyltransferase gene deficiency (FUT6)”. J. Biol. Chem. 269 (17): 12662\u201371. doi:10.1016\/S0021-9258(18)99927-8. PMID\u00a08175676.Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K,  et\u00a0al. (1997). “Construction and characterization of a full length-enriched and a 5′-end-enriched cDNA library”. Gene. 200 (1\u20132): 149\u201356. doi:10.1016\/S0378-1119(97)00411-3. PMID\u00a09373149.Borsig L, Imbach T, H\u00f6chli M, Berger EG (2000). “alpha1,3Fucosyltransferase VI is expressed in HepG2 cells and codistributed with beta1,4galactosyltransferase I in the golgi apparatus and monensin-induced swollen vesicles”. Glycobiology. 9 (11): 1273\u201380. doi:10.1093\/glycob\/9.11.1273. PMID\u00a010536043.Schnyder-Candrian S, Borsig L, Moser R, Berger EG (2000). “Localization of alpha 1,3-fucosyltransferase VI in Weibel-Palade bodies of human endothelial cells”. Proc. Natl. Acad. Sci. U.S.A. 97 (15): 8369\u201374. Bibcode:2000PNAS…97.8369S. doi:10.1073\/pnas.97.15.8369. PMC\u00a026954. PMID\u00a010900002.Kami\u0144ska J, Musielak M, Nowicka A,  et\u00a0al. (2001). “Neutrophils promote the release of alpha-6-fucosyltransferase from blood platelets through the action of cathepsin G and elastase”. Biochimie. 83 (8): 739\u201342. doi:10.1016\/S0300-9084(01)01306-2. PMID\u00a011530205.Roos C, Kolmer M, Mattila P, Renkonen R (2002). “Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism”. J. Biol. Chem. 277 (5): 3168\u201375. doi:10.1074\/jbc.M107927200. PMID\u00a011698403.Strausberg RL, Feingold EA, Grouse LH,  et\u00a0al. (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\u2013903. Bibcode:2002PNAS…9916899M. doi:10.1073\/pnas.242603899. PMC\u00a0139241. PMID\u00a012477932.Kanoh A, Ota M, Narimatsu H, Irimura T (2003). “Expression levels of FUT6 gene transfected into human colon carcinoma cells switch two sialyl-Lewis X-related carbohydrate antigens with distinct properties in cell adhesion”. Biochem. Biophys. Res. Commun. 303 (3): 896\u2013901. doi:10.1016\/S0006-291X(03)00420-0. PMID\u00a012670495.Martinez-Duncker I, Michalski JC, Bauvy C,  et\u00a0al. (2004). “Activity and tissue distribution of splice variants of alpha6-fucosyltransferase in human embryogenesis”. Glycobiology. 14 (1): 13\u201325. doi:10.1093\/glycob\/cwh006. PMID\u00a014514715.Ota T, Suzuki Y, Nishikawa T,  et\u00a0al. (2004). “Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40\u20135. doi:10.1038\/ng1285. PMID\u00a014702039.Kimura K, Wakamatsu A, Suzuki Y,  et\u00a0al. (2006). “Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes”. Genome Res. 16 (1): 55\u201365. doi:10.1101\/gr.4039406. PMC\u00a01356129. PMID\u00a016344560.Higai K, Miyazaki N, Azuma Y, Matsumoto K (2007). “Interleukin-1beta induces sialyl Lewis X on hepatocellular carcinoma HuH-7 cells via enhanced expression of ST3Gal IV and FUT VI gene”. FEBS Lett. 580 (26): 6069\u201375. doi:10.1016\/j.febslet.2006.09.073. PMID\u00a017054948. S2CID\u00a09731951.       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