Gene Association: GALNT17
UniProt Search:
GALNT17 (PROTEIN_CODING)
Function Description: polypeptide N-acetylgalactosaminyltransferase 17
found 2 associated metabolites with current gene based on the text mining result from the pubmed database.
UDP-α-D-N-Acetylglucosamine disodium
Uridine diphosphate-N-acetylglucosamine (uridine 5-diphosphate-GlcNAc, or UDP-Glc-NAc) is an acetylated aminosugar nucleotide. UDP-GlcNAc is the donor substrate for modification of nucleocytoplasmic proteins at serine and threonine residues with N-acetylglucosamine (O-GlcNAc). Nutrient sensing in mammals is done through the hexosamine biosynthetic pathway (HSP), which produces uridine 5-diphospho-N-acetylglucosamine (UDP-Glc-NAc) as its end product. Mammals respond to nutrient excess by activating O-GlcNAcylation (addition of O-linked N-acetylglucosamine). O-GlcNAc addition (and removal) is key to histone remodeling, transcription, proliferation, apoptosis, and proteasomal degradation. This nutrient-responsive signaling pathway also modulates important cellular pathways, including the insulin signaling cascade in. Alterations in O-GlcNAc metabolism are associated with various human diseases including diabetes mellitus and neurodegeneration. (PMID: 16317114) Due to the chemical makeup of UDP-GlcNAc, it is well positioned to serve as a glucose sensor in that it is a high-energy compound that requires and/or responds to glucose, amino acid, fatty acid and nucleotide metabolism for synthesis. Elevated levels of O-GlcNAc have an effect on insulin-stimulated glucose uptake. (PMID: 12678487). Uridine 5-diphosphate-GlcNAc (UDP-Glc-NAc )respond to nutrient excess to activate O-GlcNAcylation (addition of O-linked N-acetylglucosamine) in the hexosamine signaling pathway (HSP). O-GlcNAc addition (and removal) is key to histone remodeling, transcription, proliferation, apoptosis, and proteasomal degradation. This nutrient-responsive signaling pathway also modulates important cellular pathways, including the insulin signaling cascade in. Alterations in O-GlcNAc metabolism are associated with various human diseases including diabetes mellitus and neurodegeneration. (PMID: 16317114) Acquisition and generation of the data is financially supported in part by CREST/JST.
Uridine diphosphate-N-acetylgalactosamine
Uridine diphosphate-N-acetylgalactosamine (UDP-GalNAc) is a sugar donor metabolite, transferring N-acetylgalactosamine (GalNAc, an O-glycan) from UDP-GalNAc to serine and threonine residues, forming an alpha-anomeric linkage in a reaction catalyzed by enzymes known as UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferases. The addition of GalNAc to serine or threonine represents the first committed step in mucin biosynthesis. O-Glycans impart unique structural features to mucin glycoproteins and numerous membrane receptors, and resistance to thermal change and proteolytic attack in a number of diverse proteins. O-Linked carbohydrate side chains function as ligands for receptors, lymphocyte and leukocyte homing, and as signals for protein sorting (PMID: 12634319). Animal studies suggest that overactivity of the hexosamine pathway, resulting in increased UDP-hexosamines (i.e. UDP-GalNAc) is an important mechanism by which hyperglycemia causes insulin resistance. However, to date, human studies concerning the role of the hexosamine pathway in hyperglycemia-induced insulin resistance are scarce and restricted to measurements of glutamine fructose-6-phosphate amidotransferase (GFAT) enzyme activity. Both positive and negative correlations between GFAT activity in human muscle tissue from patients with type 2 DM and glucose disposal rate have been reported (PMID: 12414889). Uridine diphosphate-N-acetylgalactosamine (UDP-GalNAc) is a sugar donor metabolite, transferring N-acetylgalactosamine (GalNAc, an O-glycan) from UDP-GalNAc to serine and threonine residues, forming an alpha anomeric linkage in a reaction catalyzed by enzymes known as UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferases; addition of GalNAc to serine or threonine represents the first committed step in mucin biosynthesis. O-glycans impart unique structural features to mucin glycoproteins and numerous membrane receptors, and resistance to thermal change and proteolytic attack in a number of diverse proteins. O-linked carbohydrate side chains function as ligands for receptors; lymphocyte and leukocyte homing and as signals for protein sorting. (PMID: 12634319)
