Protein-coding gene in humans
GALNT6 |
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Identifiers |
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Aliases | GALNT6, GALNAC-T6, GalNAcT6, polypeptide N-acetylgalactosaminyltransferase 6 |
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External IDs | OMIM: 605148; MGI: 1891640; HomoloGene: 5218; GeneCards: GALNT6; OMA:GALNT6 - orthologs |
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Gene location (Human) |
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![Chromosome 12 (human)](//upload.wikimedia.org/wikipedia/commons/thumb/e/e7/Ideogram_human_chromosome_12.svg/300px-Ideogram_human_chromosome_12.svg.png) | Chr. | Chromosome 12 (human)[1] |
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| Band | 12q13.13 | Start | 51,351,247 bp[1] |
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End | 51,392,867 bp[1] |
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RNA expression pattern |
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Bgee | Human | Mouse (ortholog) |
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Top expressed in | - parotid gland
- trachea
- corpus epididymis
- bronchial epithelial cell
- pylorus
- jejunal mucosa
- duodenum
- stromal cell of endometrium
- monocyte
- corpus callosum
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| | More reference expression data |
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BioGPS | ![](//upload.wikimedia.org/wikipedia/commons/thumb/9/9c/PBB_GE_GALNT6_219956_at_fs.png/250px-PBB_GE_GALNT6_219956_at_fs.png) | More reference expression data |
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Gene ontology |
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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 |
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Orthologs |
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Species | Human | Mouse |
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Entrez | | |
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Ensembl | | |
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UniProt | | |
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RefSeq (mRNA) | | |
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NM_001161767 NM_001161768 NM_172451 |
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RefSeq (protein) | | |
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NP_001155239 NP_001155240 NP_766039 |
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Location (UCSC) | Chr 12: 51.35 – 51.39 Mb | n/a |
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PubMed search | [2] | [3] |
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Wikidata |
View/Edit Human | View/Edit Mouse |
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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
- ^ 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): 25362–70. doi:10.1074/jbc.274.36.25362. hdl:2066/184726. PMID 10464263.
- ^ a b "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.