2.4.1.41 additional information involved in development, necessary for viability 2.4.1.41 additional information pp-GalNAc-T13 is specifically expressed in neurons and synthesizes Tn antigen 2.4.1.41 additional information UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase catalyzes the first step in the mucin-type O-glycan biosynthesis pathway by transferring GalNAc to Ser or Thr residues in a protein from the sugar donor UDP-GalNAc 2.4.1.41 additional information UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases transfer GalNAc from UDP-GalNAc to the Ser and Thr residues of polypeptide acceptors, and initiate and regulate mucin-type O-glycosylation 2.4.1.41 additional information no activity with 2'-deoxy-alpha-D-galactosamine or 2'-oxymethyl-alpha-D-galactosamine 2.4.1.41 UDP-N-acetyl-alpha-D-galactosamine + polypeptide - 2.4.1.41 UDP-N-acetyl-alpha-D-galactosamine + polypeptide EA2 sequence PTTDSTTPAPTTK 2.4.1.41 UDP-N-acetyl-alpha-D-galactosamine + polypeptide Muc1 - 2.4.1.41 UDP-N-acetyl-alpha-D-galactosamine + polypeptide MUC13 isoform GALNT14 contributes to the glycosylation of peptide MUC13, which is significantly higher in ovarian cancer cells compared with the normal/benign ovary tissues 2.4.1.41 UDP-N-acetyl-D-galactosamine + bone sialoprotein preferred substrate of isozyme ppGalNAcT-1, glycosylation of Thr101, Ser131, Thr199, and Ser214, glycosylation pattern, overview 2.4.1.41 UDP-N-acetyl-D-galactosamine + fibronectin fibronectin is a physiological substrate for GalNAc-T3 2.4.1.41 UDP-N-acetyl-D-galactosamine + kappa-casein glycosylation of kappa-casein occurs after casein micelle formation triggered by the accumulation of Ca2+ in vivo 2.4.1.41 UDP-N-acetyl-D-galactosamine + osteopontin preferred substrate of isozyme ppGalNAcT-1, glycosylation pattern, overview 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide - 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide diversely regulated ppGaNTase family may play a role in the various processes governing development 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide ppGalNAc-T13: synthesis of O-glycan, specifically the Tn antigen in neurons 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide key role in O-linked glycosylation, catalyzes first step in the assembly 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide GalNAc-T1 glycosylates unmodified polypeptides in vivo 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide GalNAc-T7: functions as a follow-up enzyme in the initiation step of O-glycosylation 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide different enzyme activities are involved in the initiation of GalNAc O-glycosylation and these are differentially expressed in cells and organs 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide ppGalNAc-T14 may be involved in O-glycosylation in kidney 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide catalyzes the first step in biosynthesis of O-linked oligosaccharides in many glycoproteins 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide GalNAc-T9 catalyzes O-glycosylation in brain 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide first step in biosynthesis of O-linked oligosaccharides in submaxillary gland 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide catalyzes in vivo glycosylation of both threonine and serine 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide initial step of mucin-type O-glycosylation 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide O-glycosylation by ppGaNTase-Ts of multisite substrates may proceed in a specific hierarchical manner 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide post-translational, initial reaction in O-linked oligosaccharide biosynthesis 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide key role in overall control of O-glycosylation 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide ppGalNAc-T2: initiation of O-glycosylation in the IgA1 hinge region 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide primary step in the production of mucin-type O-linked oligosaccharide groups in glycoproteins 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide can participate in the biosynthesis of O-glycosylated parasite proteins exposed at the interface between Echinococcus granulosus and its hosts 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide initiates the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine from UDP-GalNAc to Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-alpha-1-O-Ser/Thr) 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide the enzyme is involved in the normal development of the brain through O-glycosylation of proteins in the neurons 2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide mucin-type O-linked glycosylation of serine or threonine residues 2.4.1.41 UDP-N-acetyl-D-galactosamine + syndecan-3 syndecan-3 may be a natural substrate for GalNAc-T13