Cloned (Comment) | Organism |
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expression of the human ALG12 cDNA under the control of the GPD promoter in Dalg12wbp12 yeasts. Growth of Dalg12wbp12 yeasts is restored by expression of this cDNA, thus establishing the function of the corresponding protein. The two mutant ALG12 alleles found in the congenital disorder of glycosylation patient, namely ALG12[T67M] and ALG12[R146Q], do very weakly restore growth to the levels reached with the normal human ALG12 cDNA | Homo sapiens |
Protein Variants | Comment | Organism |
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R146Q | congenital disorder of glycosylation type lg is identified in a child presenting with psychomotor retardation, hypotonia, growth retardation, dysmorphic features and anorexia. In the patients fibroblasts, the biosynthetic intermediate GlcNAc2Man7 oligosaccharide is detected both on the lipid carrier dolichyl pyrophosphate and on newly synthesized glycoproteins, pointing to a defect in the dolichyl pyrophosphateGlcNAc2Man7-dependent ALG12 alpha1,6 mannosyltransferase. Analysis of the ALG12 cDNA in the CDG patient revealed compound heterozygosity for two point mutations that result in the amino acid substitutions T67M and R146Q, respectively. The impact of these mutations on ALG12 protein function is investigated in the Saccharomyces cerevisiae alg12 glycosylation mutant by showing that the yeast ALG12 gene bearing the homologous mutations T61M and R161Q and the human mutant ALG12 cDNA alleles fail to normalize the growth defect phenotype of the alg12 yeast model, whereas expression of the normal ALG12 cDNA complements the yeast mutation. The ALG12 mannosyltransferase defect defines a type of congenital disorder of glycosylation, designated CDG-Ig | Homo sapiens |
T67M | congenital disorder of glycosylation type lg is identified in a child presenting with psychomotor retardation, hypotonia, growth retardation, dysmorphic features and anorexia. In the patients fibroblasts, the biosynthetic intermediate GlcNAc2Man7 oligosaccharide is detected both on the lipid carrier dolichyl pyrophosphate and on newly synthesized glycoproteins, pointing to a defect in the dolichyl pyrophosphateGlcNAc2Man7-dependent ALG12 alpha1,6 mannosyltransferase. Analysis of the ALG12 cDNA in the CDG patient revealed compound heterozygosity for two point mutations that result in the amino acid substitutions T67M and R146Q, respectively. The impact of these mutations on ALG12 protein function is investigated in the Saccharomyces cerevisiae alg12 glycosylation mutant by showing that the yeast ALG12 gene bearing the homologous mutations T61M and R161Q and the human mutant ALG12 cDNA alleles fail to normalize the growth defect phenotype of the alg12 yeast model, whereas expression of the normal ALG12 cDNA complements the yeast mutation. The ALG12 mannosyltransferase defect defines a type of congenital disorder of glycosylation, designated CDG-Ig | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9BV10 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
fibroblast | primary fibroblasts obtained from skin biopsies | Homo sapiens | - |
Synonyms | Comment | Organism |
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ALG12 alpha1,6mannosyltransferase | - |
Homo sapiens |
ALG12 mannosyltransferase | - |
Homo sapiens |