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Protein O-linked mannose beta1,2-N-acetylglucosaminyltransferase

The protein encoded by this gene is a type II transmembrane protein that resides in the golgi. It participates in O-mannosyl glycosylation, and is specific for alpha linked terminal mannose. Mutations in this gene are associated with muscle-eye-brain (MEB) disease. Alternatively spliced transcript variants have been found for this gene.[provided by RefSeq, Oct 2008] (from NCBI)
Top mentioned proteins: fukutin, POMT2, HAD, glycosyltransferase, CAN
Papers on POMGnT1
Generalization of Rare Variant Association Tests for Longitudinal Family Studies.
Chiu et al., Taipei, Taiwan. In Genet Epidemiol, Feb 2016
When the proposed tests were applied to data from the Diabetes Heart Study, we found exome variants of POMGNT1 and JAK1 genes were associated with type 2 diabetes.
Role of glycosyltransferase PomGnT1 in glioblastoma progression.
Qiu et al., Shanghai, China. In Neuro Oncol, Feb 2015
We reported previously that levels of peptide-O-linked mannose β-1,2-N-acetylglucosaminyltransferase 1 (PomGnT1) in glioma specimens correlated with tumor grade.
POMGNT1 Is Glycosylated by Mucin-Type O-Glycans.
Endo et al., Tokyo, Japan. In Biol Pharm Bull, 2014
Protein O-linked mannose β1,2-N-acetylglucosaminyltransferase 1 (POMGNT1) is a Golgi glycosyltransferase that catalyzes the formation of the N-acetylglucosamine (GlcNAc) β1→2Man linkage of O-mannosyl glycan.
Dystroglycanopathy with two novel POMT1 mutations in a Chinese boy with developmental delay and muscular dystrophy.
Lam et al., Hong Kong, Hong Kong. In Eur J Paediatr Neurol, 2014
Alpha-dystroglycanopathies are a group of diseases due to reduced glycosylation of alpha-dystroglycan, which commonly result from mutations in POMT1, POMT2, and POMGnT1.
Adeno-associated virus-mediated overexpression of LARGE rescues α-dystroglycan function in dystrophic mice with mutations in the fukutin-related protein.
Lu et al., Charlotte, United States. In Hum Gene Ther Methods, 2014
Multiple genes (e.g., POMT1, POMT2, POMGnT1, ISPD, GTDC2, B3GALNT2, FKTN, FKRP, and LARGE) are known to be involved in the glycosylation pathway of α-dystroglycan (α-DG).
Golgi phosphoprotein 3 mediates the Golgi localization and function of protein O-linked mannose β-1,2-N-acetlyglucosaminyltransferase 1.
Song et al., Singapore, Singapore. In J Biol Chem, 2014
Through the use of a T7 phage display, we discovered a novel interaction between GOLPH3 and a mammalian glycosyltransferase, POMGnT1, which is involved in the O-mannosylation of α-dystroglycan.
Clinical, radiological, and genetic survey of patients with muscle-eye-brain disease caused by mutations in POMGNT1.
Kurul et al., İzmir, Turkey. In Pediatr Neurol, 2014
All of the patients had mutations in the POMGNT1 gene.
Clinical features and molecular characterization of a patient with muscle-eye-brain disease: a novel mutation in the POMGNT1 gene.
Cruces et al., Madrid, Spain. In J Child Neurol, 2014
There was no glycosylation of α-dystroglycan and the genetic screening revealed a novel truncating mutation, c.1545delC (p.Tyr516Thrfs*21), and a previously identified missense mutation, c.1469G>A (p.Cys490Tyr), in the protein O-mannose beta-1,2-N-acetylglucosaminyltransferase 1 (POMGNT1) gene.
160 kb deletion in ISPD unmasking a recessive mutation in a patient with Walker-Warburg syndrome.
Wieczorek et al., Essen, Germany. In Eur J Med Genet, 2013
The disease family of muscular dystrophy-dystroglycanopathy (MDDG) contains a spectrum of severe to mild disorders, designated as MDDG type A to C. WWS, as the most severe manifestation, corresponds to MDDG type A. Defects in the genes POMT1, POMT2, POMGNT1, FKTN, FKRP, LARGE, GTDC2, G3GALNT2, GMPPB, B3GNT1, TMEM5 and COL4A1 and ISPD have been described as causal for several types of MDDG including WWS, but can only be confirmed in about 60-70% of the clinically diagnosed individuals.
Intragenic rearrangements in LARGE and POMGNT1 genes in severe dystroglycanopathies.
Seta et al., Paris, France. In Neuromuscul Disord, 2011
This study demonistreated that Intragenic rearrangements in POMGNT1 gene in muscle-eye-brain disease.
[Recent Advances in α-dystroglycanopathy].
Toda et al., Kōbe, Japan. In Brain Nerve, 2011
POMT1/2 and POMGnT1, protein products of causative genes of WWS and MEB, respectively, are enzymes that directly catalyze the biosynthesis of this glycan.
Effects of length and amino acid sequence of O-mannosyl peptides on substrate specificity of protein O-linked mannose β1,2-N-acetylglucosaminyltransferase 1 (POMGnT1).
Endo et al., Tokyo, Japan. In Biochem Biophys Res Commun, 2011
these results show that the amino acid sequence affects POMGnT1 activity.
Glycomic analyses of mouse models of congenital muscular dystrophy.
Wells et al., Athens, United States. In J Biol Chem, 2011
classical beta1,2-elongation and beta1,6-GlcNAc branching of O-mannose glycan structures are dependent upon the POMGnT1 enzyme and O-mannosylation is not limited solely to alpha-DG in the brain
Biochemical correlation of activity of the α-dystroglycan-modifying glycosyltransferase POMGnT1 with mutations in muscle-eye-brain disease.
Flitsch et al., Manchester, United Kingdom. In Biochem J, 2011
This study gives a comprehensive biochemical evaluation of all clinically relevant POMGnT1 point mutations known to date, which have been linked to muscle-eye-brain disease or similar conditions.
Reactive gliosis of astrocytes and Müller glial cells in retina of POMGnT1-deficient mice.
Takahashi et al., Chiba, Japan. In Mol Cell Neurosci, 2011
Results describe the effect of altered glycosylation of alpha-dystroglycan caused by inactivation of POMGnT1 in the retina.
[Pathomechanism and therapeutic strategy of Fukuyama congenital muscular dystrophy and related disorders].
Toda, Kōbe, Japan. In Rinsho Shinkeigaku, 2009
We previously identified the genes for Fukuyama congenital muscular dystrophy (FCMD) and muscle-eye-brain disease (MEB).
A 649 kb microduplication in 1p34.1, including POMGNT1, in a patient with microcephaly, coloboma and laryngomalacia; and a review of the literature.
van Ravenswaaij-Arts et al., Groningen, Netherlands. In Eur J Med Genet, 2009
Ten known genes are located in the duplicated region, including the POMGNT1 gene encoding for O-mannose beta-1,2-N-acetylglucosaminyltransferase.
Muscular dystrophies due to glycosylation defects.
Brockington et al., London, United Kingdom. In Neurotherapeutics, 2008
In the last few years, muscular dystrophies due to reduced glycosylation of alpha-dystroglycan (ADG) have emerged as a common group of conditions, now referred to as dystroglycanopathies. Mutations in six genes (POMT1, POMT2, POMGnT1, Fukutin, FKRP and LARGE) have so far been identified in patients with a dystroglycanopathy.
Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies.
Campbell et al., Iowa City, United States. In Nature, 2002
The FCMD gene, fukutin, shares some homology with fringe-like glycosyltransferases, and the MEB gene, POMGnT1, seems to be a new glycosyltransferase.
Congenital Muscular Dystrophy Overview
Pegoraro et al., Seattle, United States. In Unknown Journal, 2001
The main CMD subtypes, grouped by involved protein function and gene in which causative mutations occur, are laminin alpha-2 (merosin) deficiency (MDC1A), collagen VI-deficient CMD, the dystroglycanopathies (caused by mutations in POMT1, POMT2, FKTN, FKRP, LARGE, POMGNT1, and ISPD), SEPN1-related CMD (previously known as rigid spine syndrome, RSMD1) and LMNA-related CMD (L-CMD).
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