GALNT6

GALNT6
Identifiers
Aliases	GALNT6 , GALNAC-T6, GalNAcT6, polypeptide N-acetylgalactosaminyltransferase 6
External IDs	OMIM: 605148; MGI: 1891640; HomoloGene: 5218; GeneCards: GALNT6; OMA:GALNT6 - orthologs
Gene location (Human) Chr. Chromosome 12 (human) [1] Band 12q13.13 Start 51,351,247 bp [1] End 51,392,867 bp [1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in parotid gland trachea corpus epididymis bronchial epithelial cell pylorus jejunal mucosa duodenum stromal cell of endometrium monocyte corpus callosum n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function carbohydrate binding glycosyltransferase activity metal ion binding transferase activity polypeptide N-acetylgalactosaminyltransferase activity Cellular component membrane perinuclear region of cytoplasm Golgi membrane integral component of membrane Golgi apparatus Biological process O-glycan processing protein O-linked glycosylation protein glycosylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11226 207839 Ensembl ENSG00000139629 n/a UniProt Q8NCL4 Q8C7U7 RefSeq (mRNA) NM_007210 NM_001161767 NM_001161768 NM_172451 RefSeq (protein) NP_009141 NP_001155239 NP_001155240 NP_766039 Location (UCSC) Chr 12: 51.35 – 51.39 Mb n/a PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Polypeptide 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

1. GRCh38: Ensembl release 89: ENSG00000139629 – Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. 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): 25362–70. doi: 10.1074/jbc.274.36.25362 . hdl: 2066/184726 . PMID   10464263.
5. "Entrez Gene: GALNT6 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 6 (GalNAc-T6)".

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• 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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Argüeso P, Tisdale A, Mandel U, et al. (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): 86–92. doi: 10.1167/iovs.02-0181 . PMID   12506059.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID   14702039.
• 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.
• Otsuki T, Ota T, Nishikawa T, et al. (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): 117–26. doi: 10.1093/dnares/12.2.117 . PMID   16303743.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC   1356129 . PMID   16344560.