[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/galnt6-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/galnt6-wikipedia\/","headline":"GALNT6 – Wikipedia","name":"GALNT6 – Wikipedia","description":"From Wikipedia, the free encyclopedia Protein-coding gene in the species Homo sapiens Polypeptide N-acetylgalactosaminyltransferase 6 is an enzyme that in","datePublished":"2021-01-07","dateModified":"2021-01-07","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\/galnt6-wikipedia\/","wordCount":2834,"articleBody":"From Wikipedia, the free encyclopediaProtein-coding gene in the species Homo sapiensPolypeptide N-acetylgalactosaminyltransferase 6 is an enzyme that in humans is encoded by the GALNT6 gene.[4][5]This gene encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal\/GalNAc transferase motif, and a C-terminal ricin\/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. The encoded protein is capable of glycosylating fibronectin peptide in vitro and is expressed in a fibroblast cell line, indicating that it may be involved in the synthesis of oncofetal fibronectin.[5]References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000139629 – Ensembl, May 2017^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ Bennett EP, Hassan H, Mandel U, Hollingsworth MA, Akisawa N, Ikematsu Y, Merkx G, van Kessel AG, Olofsson S, Clausen H (Oct 1999). “Cloning and characterization of a close homologue of human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy”. J Biol Chem. 274 (36): 25362\u201370. doi:10.1074\/jbc.274.36.25362. PMID\u00a010464263.^ a b “Entrez Gene: GALNT6 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 6 (GalNAc-T6)”.Further reading[edit]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.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.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.Arg\u00fceso P, Tisdale A, Mandel U, et\u00a0al. (2003). “The cell-layer- and cell-type-specific distribution of GalNAc-transferases in the ocular surface epithelia is altered during keratinization”. Invest. Ophthalmol. Vis. Sci. 44 (1): 86\u201392. doi:10.1167\/iovs.02-0181. PMID\u00a012506059.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.Gerhard DS, Wagner L, Feingold EA, et\u00a0al. (2004). “The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121\u20137. doi:10.1101\/gr.2596504. PMC\u00a0528928. PMID\u00a015489334.Otsuki T, Ota T, Nishikawa T, et\u00a0al. (2007). “Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries”. DNA Res. 12 (2): 117\u201326. doi:10.1093\/dnares\/12.2.117. PMID\u00a016303743.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. "},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/galnt6-wikipedia\/#breadcrumbitem","name":"GALNT6 – Wikipedia"}}]}]