GALNT14

GALNT14
Identifiers
Aliases	GALNT14 , GALNT15, GalNac-T10, GalNac-T14, polypeptide N-acetylgalactosaminyltransferase 14
External IDs	OMIM: 608225; MGI: 1918935; HomoloGene: 56997; GeneCards: GALNT14; OMA:GALNT14 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) [1] Band 2p23.1 Start 30,910,467 bp [1] End 31,155,202 bp [1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in kidney tubule renal medulla human kidney nasal epithelium glomerulus lateral nuclear group of thalamus metanephric glomerulus endothelial cell epithelium of esophagus periodontal fiber n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function glycosyltransferase activity transferase activity metal ion binding carbohydrate binding polypeptide N-acetylgalactosaminyltransferase activity Cellular component integral component of membrane Golgi apparatus membrane Golgi membrane Biological process protein glycosylation O-glycan processing Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 79623 71685 Ensembl ENSG00000158089 n/a UniProt Q96FL9 Q8BVG5 RefSeq (mRNA) NM_001253826 NM_001253827 NM_024572 NM_001329095 NM_001329096 NM_001329097 NM_027864 RefSeq (protein) NP_001240755 NP_001240756 NP_001316024 NP_001316025 NP_001316026 NP_078848 NP_082140 Location (UCSC) Chr 2: 30.91 – 31.16 Mb n/a PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Polypeptide N-acetylgalactosaminyltransferase 14 is an enzyme that in humans is encoded by the GALNT14 gene. ^{[4] [5]}

GALNT14 (EC 2.4.1.41) belongs to a large subfamily of glycosyltransferases residing in the Golgi apparatus. GALNT enzymes catalyze the first step in the O-glycosylation of mammalian proteins by transferring N-acetyl-D-galactosamine (GalNAc) to peptide substrates.[supplied by OMIM] ^[5]

SNPs on GALNT14 have been shown to be associated to the chemotherapy responses of patients with advanced hepatocellular carcinoma. ^{[6] [7] [8] [9]}

References

1. GRCh38: Ensembl release 89: ENSG00000158089 – 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. Wang H, Tachibana K, Zhang Y, Iwasaki H, Kameyama A, Cheng L, Guo J, Hiruma T, Togayachi A, Kudo T, Kikuchi N, Narimatsu H (Dec 2002). "Cloning and characterization of a novel UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, pp-GalNAc-T14". Biochem Biophys Res Commun. 300 (3): 738–44. doi:10.1016/S0006-291X(02)02908-X. PMID   12507512.
5. "Entrez Gene: GALNT14 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 14 (GalNAc-T14)".
6. Liang KH, Lin CC, Yeh CT (Jul 2011). "GALNT14 SNP as a potential predictor of response to combination chemotherapy using 5-FU, mitoxantrone and cisplatin in advanced HCC". Pharmacogenomics. 12 (7): 1061–73. doi:10.2217/pgs.11.43. PMID   21635146.
7. Yeh CT, Liang KH, Lin CC, Chang ML, Hsu CL, Hung CF (Mar 2014). "A single nucleotide polymorphism on the GALNT14 gene as an effective predictor of response to chemotherapy in advanced hepatocellular carcinoma". Int J Cancer. 134 (5): 1214–1224. doi: 10.1002/ijc.28439 . PMID   23959947. S2CID   1262943.
8. Liang KH, Yang PC, Yeh CT (Nov 2014). "Genotyping the GALNT14 gene by joint analysis of two linked single nucleotide polymorphisms using liver tissues for clinical and geographical comparisons". Oncol Lett. 8 (5): 2215–2220. doi:10.3892/ol.2014.2507. PMC   4186602 . PMID   25295111.
9. Lin WR, Hsu CW, Chen YC, Chang ML, Liang KH, Huang YH, Yeh CT (Jul 2014). "GALNT14 genotype, α-fetoprotein and therapeutic side effects predict post-chemotherapy survival in patients with advanced hepatocellular carcinoma". Mol Clin Oncol. 2 (4): 630–640. doi:10.3892/mco.2014.294. PMC   4051573 . PMID   24940508.

Further reading

• Wu C, Yao G, Zou M, et al. (2007). "N-Acetylgalactosaminyltransferase 14, a novel insulin-like growth factor binding protein-3 binding partner". Biochem. Biophys. Res. Commun. 357 (2): 360–5. doi:10.1016/j.bbrc.2007.03.153. PMID   17434446.
• 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.
• 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.
• Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC   403697 . PMID   12975309.
• 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.
• 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.
• 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.