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Asparagine-linked glycosylation 12, alpha-1,6-mannosyltransferase homolog

ALG12, hALG12
This gene encodes a member of the glycosyltransferase 22 family. The encoded protein catalyzes the addition of the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation. Mutations in this gene have been associated with congenital disorder of glycosylation type Ig (CDG-Ig)characterized by abnormal N-glycosylation. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: MT1, HAD, Alpha-1, CD45, CAN
Papers on ALG12
A novel phenotype in N-glycosylation disorders: Gillessen-Kaesbach-Nishimura skeletal dysplasia due to pathogenic variants in ALG9.
Grigelioniene et al., Stockholm, Sweden. In Eur J Hum Genet, Feb 2016
The skeletal features overlap with that previously reported for ALG3- and ALG12-CDG, suggesting that this subset of glycosylation disorders constitutes a new diagnostic group of skeletal dysplasias.
Diagnosis of ALG12-CDG by exome sequencing in a case of severe skeletal dysplasia.
Campeau et al., Houston, United States. In Mol Genet Metab Rep, 2013
Congenital Disorder of Glycosylation type Ig (ALG12-CDG) is part of a group of autosomal recessive conditions caused by deficiency of proteins involved in the assembly of dolichol-oligosaccharides used for protein N-glycosylation.
Characterization of the 5'-flanking region of the mouse asparagine-linked glycosylation 12 homolog gene.
Kiuchi et al., Gifu, Japan. In Cell Mol Biol Lett, 2013
Recently, we characterized multiple roles of the endoplasmic reticulum stress responsive element (ERSE) in the promotion of a unique head-to-head gene pair: mammalian asparagine-linked glycosylation 12 homolog (ALG12) and cysteine-rich with EGF-like domains 2 (CRELD2).
Molecular and phenotypic characterization of ring chromosome 22 in two unrelated patients.
Saad et al., Sousse, Tunisia. In Cytogenet Genome Res, 2012
Nevertheless, phenotypic severity and occurrence of additional features in the first patient suggest a potential involvement of one or more specific gene(s) located proximally to SHANK3 (as PLXNB2, PANX2, ALG12 or MLC1), acting either independently of it or by regulating or promoting its expression and thus disrupting its function when deleted.
Evolutionarily conserved glycan signal to degrade aberrant brassinosteroid receptors in Arabidopsis.
Li et al., Ann Arbor, United States. In Proc Natl Acad Sci U S A, 2012
By contrast, overexpression of EBS4 in ebs3-1 bri1-9, which encodes the Arabidopsis ortholog of the yeast ALG12 catalyzing the ER luminal α1,6 Man addition, adds an α1,6 Man to the truncated N-glycan precursor accumulated in ebs3-1 bri1-9, promotes the bri1-9 ERAD, and neutralizes the ebs3-1 suppressor phenotype.
Mutations of an alpha1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis.
Li et al., United States. In Plant Cell, 2009
Here, we show that loss-of-function mutations in the Arabidopsis thaliana homolog of the yeast ALG12 result in transfer of incompletely assembled glycans to polypeptides.
Role of an ER stress response element in regulating the bidirectional promoter of the mouse CRELD2 - ALG12 gene pair.
Kiuchi et al., Gifu, Japan. In Bmc Genomics, 2009
Interestingly, the CRELD2 and asparagine-linked glycosylation 12 homolog (ALG12) genes are arranged as a bidirectional (head-to-head) gene pair and are separated by less than 400 bp.
Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides.
Hennet et al., Zürich, Switzerland. In Hum Mutat, 2009
This review sets the state of the art by listing all mutations identified in the 15 genes (PMM2, MPI, DPAGT1, ALG1, ALG2, ALG3, ALG9, ALG12, ALG6, ALG8, DOLK, DPM1, DPM3, MPDU1, and RFT1) that yield a deficiency of dolichol-linked oligosaccharide biosynthesis.
Expanding spectrum of congenital disorder of glycosylation Ig (CDG-Ig): sibs with a unique skeletal dysplasia, hypogammaglobulinemia, cardiomyopathy, genital malformations, and early lethality.
Freeze et al., Los Angeles, United States. In Am J Med Genet A, 2007
Both sibs were compound heterozygotes for a novel 301 G > A (G101R) mutation and a previously described 437 G > A (R146Q) mutation in ALG12.
Nuclear pore complex function in Saccharomyces cerevisiae is influenced by glycosylation of the transmembrane nucleoporin Pom152p.
Davis et al., New York City, United States. In Genetics, 2005
We have identified loss-of-function alleles of ALG12, encoding a mannosyltransferase, as suppressors of a temperature-sensitive mutation in the gene encoding the FXFG-nucleoporin NUP1.
Hydrophobic Man-1-P derivatives correct abnormal glycosylation in Type I congenital disorder of glycosylation fibroblasts.
Freeze et al., Los Angeles, United States. In Glycobiology, 2005
C-II also corrected impaired LLO biosynthesis in cells from a Dolichol (Dol)-P-Man deficient patient (CDG-Ie) and partially corrected LLO in cells from an ALG12 mannosyltransferase-deficient patient (CDG-Ig), whereas cells from an ALG3-deficient patient (CDG-Id) and from an MPDU1-deficient patient (CDG-If) were not corrected.
Molecular and clinical description of the first US patients with congenital disorder of glycosylation Ig.
Freeze et al., Los Angeles, United States. In Mol Genet Metab, 2005
Labeling of the patients' lipid-linked oligosaccharides suggested mutations in the hALG12 gene, encoding a mannosyltransferase.
Transposon mutagenesis of Trypanosoma brucei identifies glycosylation mutants resistant to concanavalin A.
Cross et al., New York City, United States. In J Biol Chem, 2004
As a proof of principle, we isolated and characterized two independent clones that were resistant to the cytotoxic action of concanavalin A. In both clones, the transposon had integrated into the locus encoding a homologue of human ALG12, which encodes a dolichyl-P-Man: Man(7)GlcNAc(2)-PP-dolichyl-alpha6-mannosyltransferase.
Screening for new yeast mutants affected in mannosylphosphorylation of cell wall mannoproteins.
Larriba et al., Badajoz, Spain. In Yeast, 2003
Within groups I, II and III, we found some genes known to be involved in oligosaccharide biosynthesis (ALG9, ALG12, HOC1), secretion (BRE5, COD4/COG5, VPS53), transcription (YOL072w/THP1, ELP2, STB1, SNF11), cell polarity (SEP7, RDG1), mitochondrial function (YFH1), cell metabolism, as well as orphan genes.
Abnormal glycosylation of red cell membrane band 3 in the congenital disorder of glycosylation Ig.
Delaunay et al., Le Kremlin-Bicêtre, France. In Pediatr Res, 2003
It has been shown that the condition stems from a homozygous mutation within the human ortholog of yeast ALG12 gene, which encodes a dolichol-P-mannose:Man7GlcNAc2-PP-dolichol alpha,1-6 mannosyltransferase of the endoplasmic reticulum.
Deficiency of dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl mannosyltransferase causes congenital disorder of glycosylation type Ig.
Körner et al., Göttingen, Germany. In Biochem J, 2002
this enzyme has a role in glycosylation and its deficiency causes congenital disorder of glycosylation type Ig
Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase.
Moore et al., Villejuif, France. In J Biol Chem, 2002
deficiency results in congenital disorders of glycosylation type Ig
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