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UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 13

GalNAc-T13
The GALNT13 protein is a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAcT; EC 2.4.1.41) family, which initiate O-linked glycosylation of mucins (see MUC3A, MIM 158371) by the initial transfer of N-acetylgalactosamine (GalNAc) with an alpha-linkage to a serine or threonine residue.[supplied by OMIM, Apr 2004] (from NCBI)
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Top mentioned proteins: ACID, GalNAc-T, GalNAc-T4, Arp2, MG2
Papers on GalNAc-T13
Genome-wide association study in NSAID-induced acute urticaria/angioedema in Spanish and Han Chinese populations.
Lee et al., Málaga, Spain. In Pharmacogenomics, 2013
Five regions showed suggestive associations after meta-analysis: HLF, RAD51L1, COL24A1, GalNAc-T13 and FBXL7.
UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases: completion of the family tree.
Tabak et al., Bethesda, United States. In Glycobiology, 2012
We have also identified and characterized enzymatically active splice variants of GalNAc-T13 that differ in the sequence of their lectin domain.
pp-GalNAc-T13 induces high metastatic potential of murine Lewis lung cancer by generating trimeric Tn antigen.
Furukawa et al., Nagoya, Japan. In Biochem Biophys Res Commun, 2012
Consequently, pp-GalNAc-T13 gene was identified as up-regulated genes in the high metastatic sublines.
Differential gene expression profiles of normal human parotid and submandibular glands.
Wang et al., Beijing, China. In Oral Dis, 2008
Ninety-eight transcripts were upregulated at least twofold in the submandibular gland compared with the parotid gland, including the chloride channel CFTR and mucin-associated genes that belong to the starch and sucrose metabolism pathway (GalNAc-T4, GalNAc-T7 and GalNAc-T13).
Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.
GeneRIF
Narimatsu et al., Tsukuba, Japan. In J Biol Chem, 2003
cloning and characterization of pp-GalNAc-T13; expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes
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