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UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 7

GalNAc-T7, ppGaNTase-T7
This gene encodes GalNAc transferase 7, a member of the GalNAc-transferase family. The enzyme encoded by this gene controls the initiation step of mucin-type O-linked protein glycosylation and transfer of N-acetylgalactosamine to serine and threonine amino acid residues. This enzyme is a type II transmembrane protein and shares common sequence motifs with other family members. Unlike other family members, this enzyme shows exclusive specificity for partially GalNAc-glycosylated acceptor substrates and shows no activity with non-glycosylated peptides. This protein may function as a follow-up enzyme in the initiation step of O-glycosylation. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: GalNAc-T, HAD, ACID, CACNA1A, Arp2
Papers on GalNAc-T7
MicroRNA-214 suppresses growth and invasiveness of cervical cancer cells by targeting UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 7.
Tang et al., Tianjin, China. In J Biol Chem, 2012
miR-214 is a new regulator of GALNT7, and both miR-214 and GALNT7 play important roles in the pathogenesis of cervical cancer
miR-30b/30d regulation of GalNAc transferases enhances invasion and immunosuppression during metastasis.
Hernando et al., New York City, United States. In Cancer Cell, 2011
Ectopic expression of miR-30b/30d promoted the metastatic behavior of melanoma cells by directly targeting the GalNAc transferase GALNT7.
MicroRNA miR-378 regulates nephronectin expression modulating osteoblast differentiation by targeting GalNT-7.
Yang et al., Toronto, Canada. In Plos One, 2008
MicroRNA miR-378 regulates nephronectin expression modulating osteoblast differentiation by targeting GalNT-7
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).
All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases.
Tabak et al., Bethesda, United States. In Glycobiology, 2003
In vitro assays suggest that a subset of the ppGaNTases have overlapping substrate specificities, but at least two ppGaNTases (ppGaNTase-T7 and -T9 [now designated -T10]) appear to require the prior addition of GalNAc to a synthetic peptide before they can catalyze sugar transfer to this substrate.
Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T10.
Narimatsu et al., Tsukuba, Japan. In Febs Lett, 2002
A novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) gene family was cloned as a homolog of human pp-GalNAc-T7, and designated pp-GalNAc-T10.
Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila.
Clausen et al., Copenhagen, Denmark. In J Biol Chem, 2002
In support of this hypothesis, we provide evidence that distinctive functional properties of Drosophila and human GalNAc-transferase isoforms were exhibited by evolutionarily conserved members of two subfamilies (dGalNAc-T1 (l(2)35Aa) and GalNAc-T11; dGalNAc-T2 (CG6394) and GalNAc-T7).
Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9.
Tabak et al., Rochester, United States. In J Biol Chem, 2001
The activity of this glycopeptide transferase is distinguished from that of ppGaNTase-T7 in that it forms a tetra-glycopeptide species from the MUC5AC tri-glycopeptide substrate, whereas ppGaNTase-T7 forms a hexa-glycopeptide species.
A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates.
Clausen et al., Copenhagen, Denmark. In Febs Lett, 1999
A novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed.
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