4388 lines
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Entry
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- *613228 - ASPARTYLGLUCOSAMINIDASE; AGA
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- OMIM
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<p>
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<span class="h4">*613228</span>
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<br />
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<strong>Table of Contents</strong>
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<a href="#title"><strong>Title</strong></a>
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<a href="#geneMap"><strong>Gene-Phenotype Relationships</strong></a>
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<a href="#text"><strong>Text</strong></a>
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<a href="#description">Description</a>
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<li role="presentation" style="margin-left: 1em">
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<a href="#cloning">Cloning and Expression</a>
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<li role="presentation" style="margin-left: 1em">
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<a href="#biochemicalFeatures">Biochemical Features</a>
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<a href="#mapping">Mapping</a>
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<a href="#molecularGenetics">Molecular Genetics</a>
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<a href="#allelicVariants"><strong>Allelic Variants</strong></a>
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<li role="presentation" style="margin-left: 1em">
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<a href="/allelicVariants/613228">Table View</a>
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<li role="presentation">
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<a href="#seeAlso"><strong>See Also</strong></a>
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</li>
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<li role="presentation">
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<a href="#references"><strong>References</strong></a>
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<a href="#creationDate"><strong>Creation Date</strong></a>
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<li role="presentation">
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<a href="#editHistory"><strong>Edit History</strong></a>
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<div id="mimExternalLinksToggleTriangle" class="small" style="color: white; display: table-cell;">▼</div>
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<div style="display: table-cell;">External Links</div>
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</div>
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</a>
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</h4>
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</div>
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</div>
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<a href="#mimGenomeLinksFold" id="mimGenomeLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<span id="mimGenomeLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5">►</span> Genome
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</a>
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<div id="mimGenomeLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel" aria-labelledby="genome">
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<div><a href="https://www.ensembl.org/Homo_sapiens/Location/View?db=core;g=ENSG00000038002;t=ENST00000264595" class="mim-tip-hint" title="Genome databases for vertebrates and other eukaryotic species." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Ensembl', 'domain': 'ensembl.org'})">Ensembl</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/genome/gdv/browser/gene/?id=175" class="mim-tip-hint" title="Detailed views of the complete genomes of selected organisms from vertebrates to protozoa." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI Genome Viewer', 'domain': 'ncbi.nlm.nih.gov'})">NCBI Genome Viewer</a></div>
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<div><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&hgFind=omimGeneAcc&position=613228" class="mim-tip-hint" title="UCSC Genome Browser; reference sequences and working draft assemblies for a large collection of genomes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UCSC Genome Browser', 'domain': 'genome.ucsc.edu'})">UCSC Genome Browser</a></div>
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<span id="mimDnaLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5">►</span> DNA
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</a>
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<div id="mimDnaLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://www.ensembl.org/Homo_sapiens/Transcript/Sequence_cDNA?db=core;g=ENSG00000038002;t=ENST00000264595" class="mim-tip-hint" title="Transcript-based views for coding and noncoding DNA." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Ensembl', 'domain': 'ensembl.org'})">Ensembl (MANE Select)</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/nuccore/NM_000027,NM_001171988,NR_033655,XM_047449722" class="mim-tip-hint" title="A collection of genome, gene, and transcript sequence data from several sources, including GenBank, RefSeq." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI RefSeq', 'domain': 'ncbi.nlm.nih'})">NCBI RefSeq</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/nuccore/NM_000027" class="mim-tip-hint" title="A collection of genome, gene, and transcript sequence data from several sources, including GenBank, RefSeq." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI RefSeq (MANE)', 'domain': 'ncbi.nlm.nih'})">NCBI RefSeq (MANE Select)</a></div>
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<div><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&hgFind=omimGeneAcc&position=613228" class="mim-tip-hint" title="UCSC Genome Browser; reference sequences and working draft assemblies for a large collection of genomes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UCSC Genome Browser', 'domain': 'genome.ucsc.edu'})">UCSC Genome Browser</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimProtein">
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<span class="panel-title">
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<span class="small">
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<a href="#mimProteinLinksFold" id="mimProteinLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<span id="mimProteinLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5">►</span> Protein
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</a>
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</span>
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<div id="mimProteinLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://hprd.org/summary?hprd_id=01949&isoform_id=01949_1&isoform_name=Isoform_1" class="mim-tip-hint" title="The Human Protein Reference Database; manually extracted and visually depicted information on human proteins." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'HPRD', 'domain': 'hprd.org'})">HPRD</a></div>
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<div><a href="https://www.proteinatlas.org/search/AGA" class="mim-tip-hint" title="The Human Protein Atlas contains information for a large majority of all human protein-coding genes regarding the expression and localization of the corresponding proteins based on both RNA and protein data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'HumanProteinAtlas', 'domain': 'proteinatlas.org'})">Human Protein Atlas</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/protein/34760,183309,183311,183330,183334,187586,287793,312228,553306,732508,4164585,4262124,15214539,49456391,63990788,119625117,119625118,119625119,119625120,189066569,194382514,285002251,285002253,288558804,2217349253,2462595387" class="mim-tip-hint" title="NCBI protein data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI Protein', 'domain': 'ncbi.nlm.nih.gov'})">NCBI Protein</a></div>
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<div><a href="https://www.uniprot.org/uniprotkb/P20933" class="mim-tip-hint" title="Comprehensive protein sequence and functional information, including supporting data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UniProt', 'domain': 'uniprot.org'})">UniProt</a></div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimGeneInfo">
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<span class="panel-title">
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<span class="small">
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<a href="#mimGeneInfoLinksFold" id="mimGeneInfoLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<div style="display: table-row">
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<div id="mimGeneInfoLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5; display: table-cell;">►</div>
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<div style="display: table-cell;">Gene Info</div>
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</div>
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</a>
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</span>
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</span>
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<div id="mimGeneInfoLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="http://biogps.org/#goto=genereport&id=175" class="mim-tip-hint" title="The Gene Portal Hub; customizable portal of gene and protein function information." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'BioGPS', 'domain': 'biogps.org'})">BioGPS</a></div>
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<div><a href="https://www.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000038002;t=ENST00000264595" class="mim-tip-hint" title="Orthologs, paralogs, regulatory regions, and splice variants." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Ensembl', 'domain': 'ensembl.org'})">Ensembl</a></div>
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<div><a href="https://www.genecards.org/cgi-bin/carddisp.pl?gene=AGA" class="mim-tip-hint" title="The Human Genome Compendium; web-based cards integrating automatically mined information on human genes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GeneCards', 'domain': 'genecards.org'})">GeneCards</a></div>
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<div><a href="http://amigo.geneontology.org/amigo/search/annotation?q=AGA" class="mim-tip-hint" title="Terms, defined using controlled vocabulary, representing gene product properties (biologic process, cellular component, molecular function) across species." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GeneOntology', 'domain': 'amigo.geneontology.org'})">Gene Ontology</a></div>
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<div><a href="https://www.genome.jp/dbget-bin/www_bget?hsa+175" class="mim-tip-hint" title="Kyoto Encyclopedia of Genes and Genomes; diagrams of signaling pathways." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'KEGG', 'domain': 'genome.jp'})">KEGG</a></div>
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<dd><a href="http://v1.marrvel.org/search/gene/AGA" class="mim-tip-hint" title="Model organism Aggregated Resources for Rare Variant ExpLoration." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MARRVEL', 'domain': 'marrvel.org'})">MARRVEL</a></dd>
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<dd><a href="https://monarchinitiative.org/NCBIGene:175" class="mim-tip-hint" title="Monarch Initiative." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Monarch', 'domain': 'monarchinitiative.org'})">Monarch</a></dd>
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<div><a href="https://www.ncbi.nlm.nih.gov/gene/175" class="mim-tip-hint" title="Gene-specific map, sequence, expression, structure, function, citation, and homology data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI Gene', 'domain': 'ncbi.nlm.nih.gov'})">NCBI Gene</a></div>
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<div><a href="https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_chrom=chr4&hgg_gene=ENST00000264595.7&hgg_start=177430774&hgg_end=177442437&hgg_type=knownGene" class="mim-tip-hint" title="UCSC Genome Bioinformatics; gene-specific structure and function information with links to other databases." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UCSC', 'domain': 'genome.ucsc.edu'})">UCSC</a></div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimClinicalResources">
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<span class="panel-title">
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<span class="small">
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<a href="#mimClinicalResourcesLinksFold" id="mimClinicalResourcesLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<div style="display: table-row">
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<div id="mimClinicalResourcesLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5; display: table-cell;">►</div>
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<div style="display: table-cell;">Clinical Resources</div>
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</div>
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</a>
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</span>
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</span>
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</div>
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<div id="mimClinicalResourcesLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel" aria-labelledby="clinicalResources">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://search.clinicalgenome.org/kb/gene-dosage/HGNC:318" class="mim-tip-hint" title="A ClinGen curated resource of genes and regions of the genome that are dosage sensitive and should be targeted on a cytogenomic array." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'ClinGen Dosage', 'domain': 'dosage.clinicalgenome.org'})">ClinGen Dosage</a></div>
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<div><a href="https://search.clinicalgenome.org/kb/genes/HGNC:318" class="mim-tip-hint" title="A ClinGen curated resource of ratings for the strength of evidence supporting or refuting the clinical validity of the claim(s) that variation in a particular gene causes disease." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'ClinGen Validity', 'domain': 'search.clinicalgenome.org'})">ClinGen Validity</a></div>
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<div><a href="https://medlineplus.gov/genetics/gene/aga" class="mim-tip-hint" title="Consumer-friendly information about the effects of genetic variation on human health." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MedlinePlus Genetics', 'domain': 'medlineplus.gov'})">MedlinePlus Genetics</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/gtr/all/tests/?term=613228[mim]" class="mim-tip-hint" title="Genetic Testing Registry." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GTR', 'domain': 'ncbi.nlm.nih.gov'})">GTR</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimVariation">
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<span class="panel-title">
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<span class="small">
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<a href="#mimVariationLinksFold" id="mimVariationLinksToggle" class=" mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<span id="mimVariationLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5">▼</span> Variation
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</a>
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</span>
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</span>
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</div>
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<div id="mimVariationLinksFold" class="panel-collapse collapse in mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://www.ncbi.nlm.nih.gov/clinvar?term=613228[MIM]" class="mim-tip-hint" title="ClinVar aggregates information about sequence variation and its relationship to human health." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">ClinVar</a></div>
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<div><a href="https://www.deciphergenomics.org/gene/AGA/overview/clinical-info" class="mim-tip-hint" title="DECIPHER" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'DECIPHER', 'domain': 'DECIPHER'})">DECIPHER</a></div>
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<div><a href="https://gnomad.broadinstitute.org/gene/ENSG00000038002" class="mim-tip-hint" title="The Genome Aggregation Database (gnomAD), Broad Institute." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'gnomAD', 'domain': 'gnomad.broadinstitute.org'})">gnomAD</a></div>
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<div><a href="https://www.ebi.ac.uk/gwas/search?query=AGA" class="mim-tip-hint" title="GWAS Catalog; NHGRI-EBI Catalog of published genome-wide association studies." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GWAS Catalog', 'domain': 'gwascatalog.org'})">GWAS Catalog </a></div>
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<div><a href="https://www.gwascentral.org/search?q=AGA" class="mim-tip-hint" title="GWAS Central; summary level genotype-to-phenotype information from genetic association studies." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GWAS Central', 'domain': 'gwascentral.org'})">GWAS Central </a></div>
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<div><a href="http://www.hgmd.cf.ac.uk/ac/gene.php?gene=AGA" class="mim-tip-hint" title="Human Gene Mutation Database; published mutations causing or associated with human inherited disease; disease-associated/functional polymorphisms." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'HGMD', 'domain': 'hgmd.cf.ac.uk'})">HGMD</a></div>
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<div><a href="https://evs.gs.washington.edu/EVS/PopStatsServlet?searchBy=Gene+Hugo&target=AGA&upstreamSize=0&downstreamSize=0&x=0&y=0" class="mim-tip-hint" title="National Heart, Lung, and Blood Institute Exome Variant Server." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NHLBI EVS', 'domain': 'evs.gs.washington.edu'})">NHLBI EVS</a></div>
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<div><a href="https://www.pharmgkb.org/gene/PA24615" class="mim-tip-hint" title="Pharmacogenomics Knowledge Base; curated and annotated information regarding the effects of human genetic variations on drug response." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PharmGKB', 'domain': 'pharmgkb.org'})">PharmGKB</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimAnimalModels">
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<span class="panel-title">
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<span class="small">
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<a href="#mimAnimalModelsLinksFold" id="mimAnimalModelsLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<div style="display: table-row">
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<div id="mimAnimalModelsLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5; display: table-cell;">►</div>
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<div style="display: table-cell;">Animal Models</div>
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</div>
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</a>
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</span>
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</span>
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</div>
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<div id="mimAnimalModelsLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://www.alliancegenome.org/gene/HGNC:318" class="mim-tip-hint" title="Search Across Species; explore model organism and human comparative genomics." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Alliance Genome', 'domain': 'alliancegenome.org'})">Alliance Genome</a></div>
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<div><a href="https://flybase.org/reports/FBgn0033431.html" class="mim-tip-hint" title="A Database of Drosophila Genes and Genomes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'FlyBase', 'domain': 'flybase.org'})">FlyBase</a></div>
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<div><a href="https://www.mousephenotype.org/data/genes/MGI:104873" class="mim-tip-hint" title="International Mouse Phenotyping Consortium." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'IMPC', 'domain': 'knockoutmouse.org'})">IMPC</a></div>
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<div><a href="http://v1.marrvel.org/search/gene/AGA#HomologGenesPanel" class="mim-tip-hint" title="Model organism Aggregated Resources for Rare Variant ExpLoration." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MARRVEL', 'domain': 'marrvel.org'})">MARRVEL</a></div>
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<div><a href="http://www.informatics.jax.org/marker/MGI:104873" class="mim-tip-hint" title="Mouse Genome Informatics; international database resource for the laboratory mouse, including integrated genetic, genomic, and biological data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MGI Mouse Gene', 'domain': 'informatics.jax.org'})">MGI Mouse Gene</a></div>
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<div><a href="https://www.mmrrc.org/catalog/StrainCatalogSearchForm.php?search_query=" class="mim-tip-hint" title="Mutant Mouse Resource & Research Centers." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MMRRC', 'domain': 'mmrrc.org'})">MMRRC</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/gene/175/ortholog/" class="mim-tip-hint" title="Orthologous genes at NCBI." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI Orthologs', 'domain': 'ncbi.nlm.nih.gov'})">NCBI Orthologs</a></div>
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<div><a href="https://www.orthodb.org/?ncbi=175" class="mim-tip-hint" title="Hierarchical catalogue of orthologs." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'OrthoDB', 'domain': 'orthodb.org'})">OrthoDB</a></div>
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<div><a href="https://wormbase.org/db/gene/gene?name=WBGene00019867;class=Gene" class="mim-tip-hint" title="Database of the biology and genome of Caenorhabditis elegans and related nematodes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name'{'name': 'Wormbase Gene', 'domain': 'wormbase.org'})">Wormbase Gene</a></div>
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<div><a href="https://zfin.org/ZDB-GENE-040426-2311" class="mim-tip-hint" title="The Zebrafish Model Organism Database." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'ZFin', 'domain': 'zfin.org'})">ZFin</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
|
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<div class="panel-heading mim-panel-heading" role="tab" id="mimCellularPathways">
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<span class="panel-title">
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<span class="small">
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<a href="#mimCellularPathwaysLinksFold" id="mimCellularPathwaysLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
|
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<div style="display: table-row">
|
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<div id="mimCellularPathwaysLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5; display: table-cell;">►</div>
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<div style="display: table-cell;">Cellular Pathways</div>
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</div>
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</a>
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</span>
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</span>
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</div>
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<div id="mimCellularPathwaysLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+hsa:175" class="mim-tip-hint" title="Kyoto Encyclopedia of Genes and Genomes; diagrams of signaling pathways." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'KEGG', 'domain': 'genome.jp'})">KEGG</a></div>
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<div><a href="https://reactome.org/content/query?q=AGA&species=Homo+sapiens&types=Reaction&types=Pathway&cluster=true" class="definition" title="Protein-specific information in the context of relevant cellular pathways." target="_blank" onclick="gtag('event', 'mim_outbound', {{'name': 'Reactome', 'domain': 'reactome.org'}})">Reactome</a></div>
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</div>
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</div>
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</div>
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</div>
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</div>
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</div>
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<span>
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<span class="mim-tip-bottom" qtip_title="<strong>Looking for this gene or this phenotype in other resources?</strong>" qtip_text="Select a related resource from the dropdown menu and click for a targeted link to information directly relevant.">
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</span>
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</span>
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</div>
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<div class="col-lg-8 col-lg-pull-2 col-md-8 col-md-pull-2 col-sm-8 col-sm-pull-2 col-xs-12">
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<div>
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<a id="title" class="mim-anchor"></a>
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<div>
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<a id="number" class="mim-anchor"></a>
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<div class="text-right">
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<a href="#" class="mim-tip-icd" qtip_title="<strong>ICD+</strong>" qtip_text="
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<strong>SNOMEDCT:</strong> 54954004<br />
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<strong>ICD10CM:</strong> E77.1<br />
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">ICD+</a>
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</div>
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<div>
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<span class="h3">
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<span class="mim-font mim-tip-hint" title="Gene description">
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<span class="text-danger"><strong>*</strong></span>
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613228
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</span>
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</span>
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</div>
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</div>
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<div>
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<a id="preferredTitle" class="mim-anchor"></a>
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<h3>
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<span class="mim-font">
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ASPARTYLGLUCOSAMINIDASE; AGA
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</span>
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</h3>
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</div>
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<div>
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<br />
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</div>
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<div>
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<a id="alternativeTitles" class="mim-anchor"></a>
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<div>
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<p>
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<span class="mim-font">
|
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<em>Alternative titles; symbols</em>
|
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</span>
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</p>
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</div>
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<div>
|
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<h4>
|
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<span class="mim-font">
|
|
GLYCOSYLASPARAGINASE
|
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</span>
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</h4>
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</div>
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</div>
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<div>
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<br />
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</div>
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</div>
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<div>
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<a id="approvedGeneSymbols" class="mim-anchor"></a>
|
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<p>
|
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<span class="mim-text-font">
|
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<strong><em>HGNC Approved Gene Symbol: <a href="https://www.genenames.org/tools/search/#!/genes?query=AGA" class="mim-tip-hint" title="HUGO Gene Nomenclature Committee." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'HGNC', 'domain': 'genenames.org'})">AGA</a></em></strong>
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</span>
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</p>
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</div>
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<div>
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<a id="cytogeneticLocation" class="mim-anchor"></a>
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<p>
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<span class="mim-text-font">
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<strong>
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<em>
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Cytogenetic location: <a href="/geneMap/4/694?start=-3&limit=10&highlight=694">4q34.3</a>
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Genomic coordinates <span class="small">(GRCh38)</span> : <a href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&position=chr4:177430774-177442437&dgv=pack&knownGene=pack&omimGene=pack" class="mim-tip-hint" title="UCSC Genome Browser; reference sequences and working draft assemblies for a large collection of genomes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UCSC Genome Browser', 'domain': 'genome.ucsc.edu'})">4:177,430,774-177,442,437</a> </span>
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</em>
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</strong>
|
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<a href="https://www.ncbi.nlm.nih.gov/" target="_blank" class="small"> (from NCBI) </a>
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</span>
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</p>
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</div>
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<div>
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<br />
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</div>
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<div>
|
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<a id="geneMap" class="mim-anchor"></a>
|
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<div style="margin-bottom: 10px;">
|
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<span class="h4 mim-font">
|
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<strong>Gene-Phenotype Relationships</strong>
|
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</span>
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</div>
|
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<div>
|
|
<table class="table table-bordered table-condensed table-hover small mim-table-padding">
|
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<thead>
|
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<tr class="active">
|
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<th>
|
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Location
|
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</th>
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<th>
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Phenotype
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</th>
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<th>
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Phenotype <br /> MIM number
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</th>
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<th>
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Inheritance
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</th>
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<th>
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Phenotype <br /> mapping key
|
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</th>
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</tr>
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</thead>
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<tbody>
|
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<tr>
|
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<td rowspan="1">
|
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<span class="mim-font">
|
|
<a href="/geneMap/4/694?start=-3&limit=10&highlight=694">
|
|
4q34.3
|
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</a>
|
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</span>
|
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</td>
|
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|
|
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<td>
|
|
<span class="mim-font">
|
|
Aspartylglucosaminuria
|
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</span>
|
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</td>
|
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<td>
|
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<span class="mim-font">
|
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|
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<a href="/entry/208400"> 208400 </a>
|
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|
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</span>
|
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</td>
|
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<td>
|
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<span class="mim-font">
|
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<abbr class="mim-tip-hint" title="Autosomal recessive">AR</abbr>
|
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</span>
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</td>
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<td>
|
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<span class="mim-font">
|
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<abbr class="mim-tip-hint" title="3 - The molecular basis of the disorder is known">3</abbr>
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</span>
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</td>
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</tr>
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</tbody>
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</table>
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</div>
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</div>
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<div>
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<div class="btn-group">
|
|
<button type="button" class="btn btn-success dropdown-toggle" data-toggle="dropdown" aria-haspopup="true" aria-expanded="false">
|
|
PheneGene Graphics <span class="caret"></span>
|
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</button>
|
|
<ul class="dropdown-menu" style="width: 17em;">
|
|
<li><a href="/graph/linear/613228" target="_blank" onclick="gtag('event', 'mim_graph', {'destination': 'Linear'})"> Linear </a></li>
|
|
<li><a href="/graph/radial/613228" target="_blank" onclick="gtag('event', 'mim_graph', {'destination': 'Radial'})"> Radial </a></li>
|
|
</ul>
|
|
</div>
|
|
<span class="glyphicon glyphicon-question-sign mim-tip-hint" title="OMIM PheneGene graphics depict relationships between phenotypes, groups of related phenotypes (Phenotypic Series), and genes.<br /><a href='/static/omim/pdf/OMIM_Graphics.pdf' target='_blank'>A quick reference overview and guide (PDF)</a>"></span>
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</div>
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<div>
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<br />
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</div>
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<div>
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<p>Aspartylglucosaminidase (AGA; <a href="https://enzyme.expasy.org/EC/3.5.1.26" target="_blank" onclick="gtag(\'event\', \'mim_outbound\', {\'name\': \'EC\', \'domain\': \'expasy.org\'})">EC 3.5.1.26</a>) is a key enzyme in the catabolism of N-linked oligosaccharides of glycoproteins. It cleaves the asparagine from the residual N-acetylglucosamines as one of the final steps in the lysosomal breakdown of glycoproteins (summary by <a href="#12" class="mim-tip-reference" title="Ikonen, E., Baumann, M., Gron, K., Syvanen, A.-C., Enomaa, N., Halila, R., Aula, P., Peltonen, L. <strong>Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.</strong> EMBO J. 10: 51-58, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1703489/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1703489</a>] [<a href="https://doi.org/10.1002/j.1460-2075.1991.tb07920.x" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1703489">Ikonen et al., 1991</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=1703489" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p><a href="#7" class="mim-tip-reference" title="Fisher, K. J., Tollersrud, O. K., Aronson, N. N., Jr. <strong>Cloning and sequence analysis of a cDNA for human glycosylasparaginase: a single gene encodes the subunits of this lysosomal amidase.</strong> FEBS Lett. 269: 440-444, 1990. Note: Erratum. FEBS Lett. 276: 232 only, 1990.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2401370/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2401370</a>] [<a href="https://doi.org/10.1016/0014-5793(90)81211-6" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="2401370">Fisher et al. (1990)</a> cloned and sequenced a cDNA for the enzyme deficient in this disorder, which they referred to as glycosylasparaginase. <a href="#25" class="mim-tip-reference" title="Tollersrud, O. K., Aronson, N. N., Jr. <strong>Purification and characterization of rat liver glycosylasparaginase.</strong> Biochem. J. 260: 101-108, 1989.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2775174/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2775174</a>] [<a href="https://doi.org/10.1042/bj2600101" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="2775174">Tollersrud and Aronson (1989)</a> purified glycosylasparaginase to homogeneity from rat liver and found it to have a native molecular mass of 49 kD and to comprise 2 subunits of 24 and 20 kD. From study of a cDNA for the human enzyme, <a href="#7" class="mim-tip-reference" title="Fisher, K. J., Tollersrud, O. K., Aronson, N. N., Jr. <strong>Cloning and sequence analysis of a cDNA for human glycosylasparaginase: a single gene encodes the subunits of this lysosomal amidase.</strong> FEBS Lett. 269: 440-444, 1990. Note: Erratum. FEBS Lett. 276: 232 only, 1990.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2401370/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2401370</a>] [<a href="https://doi.org/10.1016/0014-5793(90)81211-6" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="2401370">Fisher et al. (1990)</a> found that it is encoded as a 34.6-kD polypeptide that is posttranslationally processed to generate 2 subunits of approximately 19.5 (the alpha subunit) and 15 (the beta subunit) kD. The AGA cDNA encodes a deduced 436-amino acid protein. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=2401370+2775174" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#12" class="mim-tip-reference" title="Ikonen, E., Baumann, M., Gron, K., Syvanen, A.-C., Enomaa, N., Halila, R., Aula, P., Peltonen, L. <strong>Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.</strong> EMBO J. 10: 51-58, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1703489/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1703489</a>] [<a href="https://doi.org/10.1002/j.1460-2075.1991.tb07920.x" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1703489">Ikonen et al. (1991)</a> cloned and sequenced a full-length cDNA for human AGA and studied its transient expression in COS-1 cells. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=1703489" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p><a href="#21" class="mim-tip-reference" title="Oinonen, C., Tikkanen, R., Rouvinen, J., Peltonen, L. <strong>Three-dimensional structure of human lysosomal aspartylglucosaminidase.</strong> Nature Struct. Biol. 2: 1102-1108, 1995.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8846222/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8846222</a>] [<a href="https://doi.org/10.1038/nsb1295-1102" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="8846222">Oinonen et al. (1995)</a> determined the high resolution crystal structure of human lysosomal aspartylglucosaminidase. The enzyme is synthesized as a single polypeptide precursor that is immediately posttranslationally cleaved into alpha- and beta-subunits. Two alpha- and beta-chains were found to pack together forming the final heterotetrameric structure. The catalytically essential residue, the N-terminal threonine of the beta-chain, is situated in the deep pocket of the funnel-shaped active site. On the basis of the structure of the enzyme-product complex, <a href="#21" class="mim-tip-reference" title="Oinonen, C., Tikkanen, R., Rouvinen, J., Peltonen, L. <strong>Three-dimensional structure of human lysosomal aspartylglucosaminidase.</strong> Nature Struct. Biol. 2: 1102-1108, 1995.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8846222/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8846222</a>] [<a href="https://doi.org/10.1038/nsb1295-1102" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="8846222">Oinonen et al. (1995)</a> presented a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum. The 3-dimensional structure also allowed the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=8846222" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p>By analysis of somatic cell hybrids, <a href="#1" class="mim-tip-reference" title="Aula, P., Astrin, K. H., Francke, U., Desnick, R. J. <strong>Assignment of the structural gene encoding human aspartylglucosaminidase to the long arm of chromosome 4 (4q21-4qter).</strong> Am. J. Hum. Genet. 36: 1215-1224, 1984.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/6517050/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">6517050</a>]" pmid="6517050">Aula et al. (1984)</a> assigned the structural gene for aspartylglucosaminidase to chromosome 4q21-qter. <a href="#9" class="mim-tip-reference" title="Halal, F., Vekemans, M., Chitayat, D. <strong>Interstitial tandem direct duplication of the long arm of chromosome 4 (q23-q27) and possible assignment of the structural gene encoding human aspartylglucosaminidase to this segment.</strong> Am. J. Med. Genet. 39: 418-421, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1877620/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1877620</a>] [<a href="https://doi.org/10.1002/ajmg.1320390412" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1877620">Halal et al. (1991)</a> presented observations they interpreted as indicating a narrowing of the assignment of the gene to 4q23-q27: a girl with a de novo direct tandem duplication of 4q23-q27 had increased activity of AGA enzyme in cultured fibroblasts. <a href="#20" class="mim-tip-reference" title="Morris, C., Heisterkamp, N., Groffen, J., Williams, J. C., Mononen, I. <strong>Chromosomal localization of the human glycoasparaginase gene to 4q32-q33.</strong> Hum. Genet. 88: 295-297, 1992.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1733831/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1733831</a>] [<a href="https://doi.org/10.1007/BF00197262" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1733831">Morris et al. (1992)</a> concluded from in situ hybridization studies that the localization is 4q32-q33. <a href="#5" class="mim-tip-reference" title="Engelen, J., Hamers, A., Schrander-Stumpel, C., Mulder, H., Poorthuis, B. <strong>Assignment of the aspartylglucosaminidase gene (AGA) to 4q33-q35 based on decreased activity in a girl with a 46,XX,del(4)(q33) karyotype.</strong> Cytogenet. Cell Genet. 60: 208-209, 1992.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1505217/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1505217</a>] [<a href="https://doi.org/10.1159/000133338" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1505217">Engelen et al. (1992)</a> found reduced activity of the enzyme in a patient with deletion of 4q33-qter. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=1733831+6517050+1505217+1877620" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#24" class="mim-tip-reference" title="Tenhunen, K., Laan, M., Manninen, T., Palotie, A., Peltonen, L., Jalanko, A. <strong>Molecular cloning, chromosomal assignment, and expression of the mouse aspartylglucosaminidase gene.</strong> Genomics 30: 244-250, 1995.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8586423/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8586423</a>] [<a href="https://doi.org/10.1006/geno.1995.9881" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="8586423">Tenhunen et al. (1995)</a> found that the Aga gene in the mouse is located in the central area of the B region of chromosome 8 in the region that shows homology of synteny to the telomeric region of human 4q. The mouse gene spans an 11-kb genomic region and contains 9 exons, which is analogous to the human gene. Furthermore, the exon/intron boundaries of the mouse and human genes are identically positioned. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=8586423" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p>In Finnish patients with aspartylglucosaminuria (AGU; <a href="/entry/208400">208400</a>), <a href="#12" class="mim-tip-reference" title="Ikonen, E., Baumann, M., Gron, K., Syvanen, A.-C., Enomaa, N., Halila, R., Aula, P., Peltonen, L. <strong>Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.</strong> EMBO J. 10: 51-58, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1703489/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1703489</a>] [<a href="https://doi.org/10.1002/j.1460-2075.1991.tb07920.x" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1703489">Ikonen et al. (1991)</a> and <a href="#8" class="mim-tip-reference" title="Fisher, K. J., Tollersrud, O. K., Aronson, N. N., Jr. <strong>Molecular genetics of aspartylglucosaminuria. (Abstract)</strong> Nucleic Acids Res. Symp. 23: 8 only, 1991."None>Fisher et al. (1991)</a> independently identified homozygosity for a cys163-to-ser (C163S; <a href="#0001">613228.0001</a>) mutation in the AGA gene. The C163S mutation is responsible for 98% of the cases of AGU in Finland (<a href="#15" class="mim-tip-reference" title="Isoniemi, A., Hietala, M., Aula, P., Jalanko, A., Peltonen, L. <strong>Identification of a novel mutation causing aspartylglucosaminuria reveals a mutation hotspot region in the aspartylglucosaminidase gene.</strong> Hum. Mutat. 5: 318-326, 1995.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/7627186/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">7627186</a>] [<a href="https://doi.org/10.1002/humu.1380050408" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="7627186">Isoniemi et al., 1995</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?term=7627186+1703489" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#13" class="mim-tip-reference" title="Ikonen, E., Enomaa, N., Ulmanen, I., Peltonen, L. <strong>In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation.</strong> Genomics 11: 206-211, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1765378/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1765378</a>] [<a href="https://doi.org/10.1016/0888-7543(91)90120-4" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1765378">Ikonen et al. (1991)</a> described the spectrum of 10 AGA mutations found in 12 unrelated patients of non-Finnish origin with AGU. Since 11 of the 12 were homozygotes, consanguinity appeared to be a common denominator in most AGU families, although consanguinity could be confirmed in only 2 of the families. Screening for the unknown gene defects was done using single-strand conformation polymorphism (SSCP) analysis. The mutations were distributed over the entire coding region of the AGA cDNA, except in the carboxyl-terminal 17-kD subunit in which they were clustered within a 46-amino acid region. Based on the character of the mutations, <a href="#13" class="mim-tip-reference" title="Ikonen, E., Enomaa, N., Ulmanen, I., Peltonen, L. <strong>In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation.</strong> Genomics 11: 206-211, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1765378/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1765378</a>] [<a href="https://doi.org/10.1016/0888-7543(91)90120-4" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1765378">Ikonen et al. (1991)</a> concluded that most of the mutations probably affected the folding and stability of the molecule and did not directly affect the active site of the enzyme. There were 3 non-Finnish patients who had the 'Finnish' C163S mutation but 2 of them were Norwegian and 1 was Swedish. These patients presumably had Finnish ancestry (<a href="#4" class="mim-tip-reference" title="Borud, O., Torp, K. H. <strong>Aspartylglycosaminuria in northern Norway (Letter)</strong> Lancet 307: 1082-1083, 1976. Note: Originally Volume I.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/57494/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">57494</a>] [<a href="https://doi.org/10.1016/s0140-6736(76)92266-2" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="57494">Borud and Torp, 1976</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?term=57494+1765378" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#26" class="mim-tip-reference" title="Tollersrud, O. K., Nilssen, O., Tranebjaerg, L., Borud, O. <strong>Aspartylglucosaminuria in northern Norway: a molecular and genealogical study.</strong> J. Med. Genet. 31: 360-363, 1994.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8064811/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8064811</a>] [<a href="https://doi.org/10.1136/jmg.31.5.360" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="8064811">Tollersrud et al. (1994)</a> reported 9 patients from 7 families identified in northern Norway. All were homozygous for the most prevalent Finnish mutation, cys163-to-ser. Genealogic investigation of 9 parents proved Finnish ancestry in all pedigrees. These Finnish immigrants originated in the main from the Tornio valley in northern Finland in a continuous immigration movement from 1700 to 1900. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=8064811" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#14" class="mim-tip-reference" title="Ikonen, E., Peltonen, L. <strong>Mutations causing aspartylglucosaminuria (AGU): a lysosomal accumulation disease.</strong> Hum. Mutat. 1: 361-365, 1992.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1301945/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1301945</a>] [<a href="https://doi.org/10.1002/humu.1380010503" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1301945">Ikonen and Peltonen (1992)</a> reviewed a total of 11 AGA mutations published to that time. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=1301945" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#16" class="mim-tip-reference" title="Laitinen, A., Hietala, M., Haworth, J. C., Schroeder, M. L., Seargeant, L. E., Greenberg, C. R., Aula, P. <strong>Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation.</strong> Clin. Genet. 51: 174-178, 1997.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9137882/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9137882</a>] [<a href="https://doi.org/10.1111/j.1399-0004.1997.tb02448.x" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9137882">Laitinen et al. (1997)</a> demonstrated that 2 Canadian sibs of non-Finnish extraction had AGU on the basis of compound heterozygosity at the AGA locus: a 299G-A transition caused a gly100-to-glu substitution and a 404T-C transition caused a phe135-to-ser substitution in the enzyme. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=9137882" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#15" class="mim-tip-reference" title="Isoniemi, A., Hietala, M., Aula, P., Jalanko, A., Peltonen, L. <strong>Identification of a novel mutation causing aspartylglucosaminuria reveals a mutation hotspot region in the aspartylglucosaminidase gene.</strong> Hum. Mutat. 5: 318-326, 1995.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/7627186/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">7627186</a>] [<a href="https://doi.org/10.1002/humu.1380050408" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="7627186">Isoniemi et al. (1995)</a> found 7 Finnish AGU patients to be compound heterozygotes for the C163S mutation and another mutation, namely a 2-bp deletion in the second exon of the AGA cDNA, causing a shift of the reading frame and a premature termination of the polypeptide chain. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=7627186" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#23" class="mim-tip-reference" title="Saarela, J., Laine, M., Oinonen, C., von Schantz, C., Jalanko, A., Rouvinen, J., Peltonen, L. <strong>Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations.</strong> Hum. Molec. Genet. 10: 983-995, 2001.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/11309371/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">11309371</a>] [<a href="https://doi.org/10.1093/hmg/10.9.983" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="11309371">Saarela et al. (2001)</a> used the 3-dimensional structure of AGA to predict structural consequences of AGU mutations, including 6 novel mutations, and to characterize the effect of mutations on intracellular stability, maturation, transport, and the activity of AGA. Most mutations are substitutions replacing the original amino acid with a bulkier residue. Mutations of the dimer interface prevent dimerization in the endoplasmic reticulum, whereas active site mutations not only destroy the activity but also affect maturation of the precursor. Depending on their effects on the stability of the AGA polypeptide, the authors categorized mutations as mild, moderate, or severe. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=11309371" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<strong>ALLELIC VARIANTS (<a href="/help/faq#1_4"></strong>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=613228[MIM]" class="btn btn-default mim-tip-hint" role="button" title="ClinVar aggregates information about sequence variation and its relationship to human health." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">ClinVar</a>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown"><span class="text-primary">●</span> rs121964904 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs121964904;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://gnomad.broadinstitute.org/variant/rs121964904?dataset=gnomad_r2_1" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'gnomad.broadinstitute.org'})" style="padding-left: 8px;"><span class="text-primary">●</span> gnomAD</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs121964904" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs121964904" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000000243 OR RCV000410114" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000000243, RCV000410114" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000000243...</a>
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<p>By direct sequencing of PCR-amplified AGA cDNA from a patient with aspartylglucosaminuria (AGU; <a href="/entry/208400">208400</a>), <a href="#13" class="mim-tip-reference" title="Ikonen, E., Enomaa, N., Ulmanen, I., Peltonen, L. <strong>In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation.</strong> Genomics 11: 206-211, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1765378/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1765378</a>] [<a href="https://doi.org/10.1016/0888-7543(91)90120-4" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1765378">Ikonen et al. (1991)</a> found a G-to-C mutation resulting in the substitution of serine for cysteine-163 (C163S). This mutation was found in all of 20 analyzed Finnish AGU patients, and in heterozygous form in all 53 carriers, and in none of 67 control individuals. The mutation produces a change in the predicted flexibility of the AGA polypeptide chain and removes an intramolecular S-S bridge. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=1765378" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#8" class="mim-tip-reference" title="Fisher, K. J., Tollersrud, O. K., Aronson, N. N., Jr. <strong>Molecular genetics of aspartylglucosaminuria. (Abstract)</strong> Nucleic Acids Res. Symp. 23: 8 only, 1991."None>Fisher et al. (1991)</a> independently found the G-to-C transversion in DNA from Finnish AGU fibroblasts; however, they found a second G-to-A transition that resulted in an arginine-to-glutamine substitution as well. The 2 substitutions were present in all 3 Finnish cases studied and in none of 2 non-Finnish AGU fibroblast lines. In non-Finnish AGU fibroblasts, <a href="#8" class="mim-tip-reference" title="Fisher, K. J., Tollersrud, O. K., Aronson, N. N., Jr. <strong>Molecular genetics of aspartylglucosaminuria. (Abstract)</strong> Nucleic Acids Res. Symp. 23: 8 only, 1991."None>Fisher et al. (1991)</a> found deletions as the apparent cause of the AGA deficiency. <a href="#19" class="mim-tip-reference" title="Mononen, I., Heisterkamp, N., Kaartinen, V., Williams, J. C., Yates, J. R., III, Griffin, P. R., Hood, L. E., Groffen, J. <strong>Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.</strong> Proc. Nat. Acad. Sci. 88: 2941-2945, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2011603/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2011603</a>] [<a href="https://doi.org/10.1073/pnas.88.7.2941" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="2011603">Mononen et al. (1991)</a> likewise found 2 mutations, R161Q and C163S. Both mutations resulted in novel restriction endonuclease sites and were present in all 8 Finnish AGU patients studied, but they were absent from Finnish and non-Finnish controls and a non-Finnish case of AGU. Both amino acid changes would be expected to modify the structure of the protein profoundly: the replacement of an arginine by glutamine represents the substitution of a basic amino acid for one containing an uncharged polar group; the replacement of cysteine by serine may abolish a disulfide bridge. Whether both mutations are involved in the pathologic consequences or whether one mutation is a polymorphism was uncertain. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=2011603" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#13" class="mim-tip-reference" title="Ikonen, E., Enomaa, N., Ulmanen, I., Peltonen, L. <strong>In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation.</strong> Genomics 11: 206-211, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1765378/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1765378</a>] [<a href="https://doi.org/10.1016/0888-7543(91)90120-4" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1765378">Ikonen et al. (1991)</a> showed by in vitro mutagenesis studies that the C163S mutation is responsible for enzyme deficiency, whereas the arg161-to-gln (R161Q) substitution, which accompanies the other mutation in 98% of AGU alleles in Finland, represents a rare polymorphism. Cysteine-163 was shown to participate in an S-S bridge. The absence of this covalent crosslink in the mutated protein probably results in disturbed folding of the polypeptide chain and consequent decrease in its intracellular stability. <a href="#6" class="mim-tip-reference" title="Fisher, K. J., Aronson, N. N., Jr. <strong>Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients: amino acid substitution cys163-to-ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits.</strong> J. Biol. Chem. 266: 12105-12113, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1904874/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1904874</a>]" pmid="1904874">Fisher and Aronson (1991)</a> likewise found the 482G-A transition and the 488G-C transversion and demonstrated that only the latter was responsible for deficiency of glycosylasparaginase activity. The substitution prevented the normal posttranslational processing of the precursor polypeptide into its alpha and beta subunits. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=1765378+1904874" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>The C163S mutation is responsible for 98% of the cases of AGU in Finland (<a href="#15" class="mim-tip-reference" title="Isoniemi, A., Hietala, M., Aula, P., Jalanko, A., Peltonen, L. <strong>Identification of a novel mutation causing aspartylglucosaminuria reveals a mutation hotspot region in the aspartylglucosaminidase gene.</strong> Hum. Mutat. 5: 318-326, 1995.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/7627186/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">7627186</a>] [<a href="https://doi.org/10.1002/humu.1380050408" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="7627186">Isoniemi et al., 1995</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=7627186" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<strong>.0002 ASPARTYLGLUCOSAMINURIA</strong>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000000244" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000000244" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000000244</a>
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<p>In a 10-year-old Turkish child with aspartylglucosaminuria (AGU; <a href="/entry/208400">208400</a>), <a href="#11" class="mim-tip-reference" title="Ikonen, E., Aula, P., Gron, K., Tollersrud, O., Halila, R., Manninen, T., Syvanen, A.-C., Peltonen, L. <strong>Spectrum of mutations in aspartylglucosaminuria.</strong> Proc. Nat. Acad. Sci. 88: 11222-11226, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1722323/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1722323</a>] [<a href="https://doi.org/10.1073/pnas.88.24.11222" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1722323">Ikonen et al. (1991)</a> found a G-to-A substitution at nucleotide 904 of the AGA gene, resulting in substitution of arginine for glycine-302 (G302R). The patient was homozygous for the mutation and showed fibroblast AGA activity about 7% of normal. The parents were first cousins. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=1722323" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown"><span class="text-primary">●</span> rs121964906 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs121964906;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://gnomad.broadinstitute.org/variant/rs121964906?dataset=gnomad_r2_1" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'gnomad.broadinstitute.org'})" style="padding-left: 8px;"><span class="text-primary">●</span> gnomAD</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs121964906" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs121964906" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<span class="mim-text-font">
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000000245" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000000245" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000000245</a>
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<p>In a 16-year-old white American patient with aspartylglucosaminuria (AGU; <a href="/entry/208400">208400</a>), <a href="#11" class="mim-tip-reference" title="Ikonen, E., Aula, P., Gron, K., Tollersrud, O., Halila, R., Manninen, T., Syvanen, A.-C., Peltonen, L. <strong>Spectrum of mutations in aspartylglucosaminuria.</strong> Proc. Nat. Acad. Sci. 88: 11222-11226, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1722323/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1722323</a>] [<a href="https://doi.org/10.1073/pnas.88.24.11222" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1722323">Ikonen et al. (1991)</a> found by the SSCP method a T-to-C change at nucleotide 916 of the AGA gene, resulting in substitution of arginine for cysteine-306 (C306R). <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=1722323" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<a id="0004" class="mim-anchor"></a>
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<strong>.0004 ASPARTYLGLUCOSAMINURIA</strong>
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AGA, GLY60ASP
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown">rs121964907 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs121964907;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs121964907" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs121964907" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<span class="mim-text-font">
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000000246" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000000246" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000000246</a>
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</span>
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<span class="mim-text-font">
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<p>In a 3-year-old German child with aspartylglucosaminuria (AGU; <a href="/entry/208400">208400</a>), previously reported by <a href="#27" class="mim-tip-reference" title="Ziegler, R., Schmidt, H., Sewell, A. C., Weglage, J., v. Lengerke, J. H., Ullrich, K. <strong>Aspartylglucosaminurie: Klinische Beschreibung von zwei deutschen Patienten.</strong> Mschr. Kinderheilk. 137: 454-457, 1989.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2811876/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2811876</a>]" pmid="2811876">Ziegler et al. (1989)</a>, <a href="#11" class="mim-tip-reference" title="Ikonen, E., Aula, P., Gron, K., Tollersrud, O., Halila, R., Manninen, T., Syvanen, A.-C., Peltonen, L. <strong>Spectrum of mutations in aspartylglucosaminuria.</strong> Proc. Nat. Acad. Sci. 88: 11222-11226, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1722323/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1722323</a>] [<a href="https://doi.org/10.1073/pnas.88.24.11222" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1722323">Ikonen et al. (1991)</a> found a G-to-A substitution at nucleotide 179 of the AGA gene, resulting in substitution of the negatively charged aspartic acid for uncharged glycine at residue 60 (G60D). <a href="https://pubmed.ncbi.nlm.nih.gov/?term=1722323+2811876" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<a id="0005" class="mim-anchor"></a>
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<h4>
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<span class="mim-font">
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<strong>.0005 ASPARTYLGLUCOSAMINURIA</strong>
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</span>
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</h4>
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AGA, ALA101VAL
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown"><span class="text-primary">●</span> rs121964908 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs121964908;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://gnomad.broadinstitute.org/variant/rs121964908?dataset=gnomad_r2_1" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'gnomad.broadinstitute.org'})" style="padding-left: 8px;"><span class="text-primary">●</span> gnomAD</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs121964908" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs121964908" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<span class="mim-text-font">
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000000247 OR RCV001532508 OR RCV004698463" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000000247, RCV001532508, RCV004698463" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000000247...</a>
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</span>
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<span class="mim-text-font">
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<p>In a 1-year-old Italian child with aspartylglucosaminuria (AGU; <a href="/entry/208400">208400</a>), <a href="#11" class="mim-tip-reference" title="Ikonen, E., Aula, P., Gron, K., Tollersrud, O., Halila, R., Manninen, T., Syvanen, A.-C., Peltonen, L. <strong>Spectrum of mutations in aspartylglucosaminuria.</strong> Proc. Nat. Acad. Sci. 88: 11222-11226, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1722323/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1722323</a>] [<a href="https://doi.org/10.1073/pnas.88.24.11222" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1722323">Ikonen et al. (1991)</a> found a C-to-T transition at nucleotide 302 of the AGA gene, resulting in a change changed alanine-101 to valine (A101V). The patient was homozygous for this mutation, which was discovered by the SSCP method. The same mutation was found in a compound heterozygous state in an English patient (see <a href="#0006">613228.0006</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=1722323" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<div>
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<a id="0006" class="mim-anchor"></a>
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<h4>
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<span class="mim-font">
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<strong>.0006 ASPARTYLGLUCOSAMINURIA</strong>
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</span>
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</h4>
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</div>
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<span class="mim-text-font">
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<div style="float: left;">
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AGA, 7-BP DEL, NT102
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</div>
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</span>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown">rs386833417 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs386833417;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs386833417" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs386833417" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<span class="mim-text-font">
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000000248" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000000248" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000000248</a>
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</span>
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</div>
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<div>
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<span class="mim-text-font">
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<p>In a 5-year-old English child with aspartylglucosaminuria (AGU; <a href="/entry/208400">208400</a>), <a href="#11" class="mim-tip-reference" title="Ikonen, E., Aula, P., Gron, K., Tollersrud, O., Halila, R., Manninen, T., Syvanen, A.-C., Peltonen, L. <strong>Spectrum of mutations in aspartylglucosaminuria.</strong> Proc. Nat. Acad. Sci. 88: 11222-11226, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1722323/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1722323</a>] [<a href="https://doi.org/10.1073/pnas.88.24.11222" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1722323">Ikonen et al. (1991)</a> found compound heterozygosity for the A101V mutation (<a href="#0005">613228.0005</a>) and a 7-nucleotide deletion (102_108delfs34Ter) in the AGA gene. The gene deletion would be predicted to result in the formation of a truncated polypeptide chain of only 33 amino acids. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=1722323" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<a id="0007" class="mim-anchor"></a>
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<h4>
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<span class="mim-font">
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<strong>.0007 ASPARTYLGLUCOSAMINURIA</strong>
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</span>
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</h4>
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</div>
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<span class="mim-text-font">
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<div style="float: left;">
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AGA, 1-BP INS, 800T
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown"><span class="text-primary">●</span> rs386833436 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs386833436;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://gnomad.broadinstitute.org/variant/rs386833436?dataset=gnomad_r2_1" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'gnomad.broadinstitute.org'})" style="padding-left: 8px;"><span class="text-primary">●</span> gnomAD</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs386833436" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs386833436" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<span class="mim-text-font">
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000000249 OR RCV002512599 OR RCV004721239" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000000249, RCV002512599, RCV004721239" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000000249...</a>
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</span>
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<span class="mim-text-font">
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<p>In a 17-year-old Spanish American patient with aspartylglucosaminuria (AGU; <a href="/entry/208400">208400</a>), <a href="#11" class="mim-tip-reference" title="Ikonen, E., Aula, P., Gron, K., Tollersrud, O., Halila, R., Manninen, T., Syvanen, A.-C., Peltonen, L. <strong>Spectrum of mutations in aspartylglucosaminuria.</strong> Proc. Nat. Acad. Sci. 88: 11222-11226, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1722323/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1722323</a>] [<a href="https://doi.org/10.1073/pnas.88.24.11222" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1722323">Ikonen et al. (1991)</a> found insertion of a single thymidine after nucleotide 800 in the AGA gene, resulting in a shift in the reading frame and a premature stop codon causing a truncated polypeptide chain with 318 amino acids of which the first 267 amino acids represented the normal AGA polypeptide (800_801insfs319Ter). <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=1722323" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<a id="0008" class="mim-anchor"></a>
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<h4>
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<span class="mim-font">
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<strong>.0008 ASPARTYLGLUCOSAMINURIA</strong>
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</span>
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</h4>
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</div>
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<span class="mim-text-font">
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<div style="float: left;">
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AGA, 6-BP INS, NT127
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown">rs386833418 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs386833418;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs386833418" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs386833418" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<span class="mim-text-font">
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000000250" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000000250" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000000250</a>
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</span>
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</div>
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<p>In a 3-year-old Tunisian child with aspartylglucosaminuria (AGU; <a href="/entry/208400">208400</a>), the offspring of first-cousin parents, <a href="#13" class="mim-tip-reference" title="Ikonen, E., Enomaa, N., Ulmanen, I., Peltonen, L. <strong>In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation.</strong> Genomics 11: 206-211, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1765378/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1765378</a>] [<a href="https://doi.org/10.1016/0888-7543(91)90120-4" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1765378">Ikonen et al. (1991)</a> found homozygosity for a 6-nucleotide insertion (ATGCGG) after nucleotide 127 in the AGA gene, causing an in-frame insertion of aspartic acid and alanine after amino acid 42. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=1765378" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000000251" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000000251" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000000251</a>
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<p>In a 12-year-old black American patient with aspartylglucosaminuria (AGU; <a href="/entry/208400">208400</a>) (<a href="#10" class="mim-tip-reference" title="Hreidarsson, S., Thomas, G. H., Valle, D. L., Stevenson, R. E., Taylor, H., McCarty, J., Coker, S. B., Green, W. R. <strong>Aspartylglucosaminuria in the United States.</strong> Clin. Genet. 23: 427-435, 1983.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/6883788/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">6883788</a>] [<a href="https://doi.org/10.1111/j.1399-0004.1983.tb01977.x" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="6883788">Hreidarsson et al., 1983</a>; Camden number GM03560), <a href="#11" class="mim-tip-reference" title="Ikonen, E., Aula, P., Gron, K., Tollersrud, O., Halila, R., Manninen, T., Syvanen, A.-C., Peltonen, L. <strong>Spectrum of mutations in aspartylglucosaminuria.</strong> Proc. Nat. Acad. Sci. 88: 11222-11226, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1722323/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1722323</a>] [<a href="https://doi.org/10.1073/pnas.88.24.11222" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1722323">Ikonen et al. (1991)</a> found homozygosity for a deletion of nucleotides 807-940 in the AGA gene. Further sequence analysis of both cDNA and genomic DNA confirmed that a 134-bp exon was missing from the cDNA and that a G-to-T substitution had occurred in the adjacent 3-prime intron at position +1 of the splice donor site; the authors thus concluded that this was a splicing mutation. The mutation resulted in a transcript that was 134-bp shorter than normal. The mutation also resulted in the shift of the reading frame and a premature termination codon at the beginning of the following exon. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=1722323+6883788" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown">rs794728009 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs794728009;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs794728009" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs794728009" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000000252" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000000252" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000000252</a>
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<p>In an 8-year-old Dutch child with aspartylglucosaminuria (AGU; <a href="/entry/208400">208400</a>), <a href="#13" class="mim-tip-reference" title="Ikonen, E., Enomaa, N., Ulmanen, I., Peltonen, L. <strong>In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation.</strong> Genomics 11: 206-211, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1765378/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1765378</a>] [<a href="https://doi.org/10.1016/0888-7543(91)90120-4" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="1765378">Ikonen et al. (1991)</a> found deletion of 1 nucleotide, thymidine-336, in the AGA gene. This resulted in a frameshift and premature termination of the polypeptide chain after 126 amino acids. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=1765378" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown">rs121964909 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs121964909;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs121964909" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs121964909" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000000253" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000000253" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000000253</a>
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<p><a href="#22" class="mim-tip-reference" title="Peltola, M., Tikkanen, R., Peltonen, L., Jalanko, A. <strong>Ser72pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation.</strong> Hum. Molec. Genet. 5: 737-743, 1996.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8776587/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8776587</a>] [<a href="https://doi.org/10.1093/hmg/5.6.737" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="8776587">Peltola et al. (1996)</a> reported that a T-to-C change at codon 214 in the AGA gene, leading to a ser72-to-pro (S72P) substitution, occurred in affected members of 4 Arab families with aspartylglucosaminuria (AGU; <a href="/entry/208400">208400</a>). They noted that this mutation is the first naturally occurring AGA mutation that involves an active site and is apparently the second most common AGA mutation worldwide. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=8776587" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<a href="#Aula1984" class="mim-tip-reference" title="Aula, P., Rapola, J., von Koskull, H., Ammala, P. <strong>Prenatal diagnosis and fetal pathology of aspartylglucosaminuria.</strong> Am. J. Med. Genet. 19: 359-367, 1984.">Aula et al. (1984)</a>; <a href="#Aula1984" class="mim-tip-reference" title="Aula, P., Rapola, J., von Koskull, H., Ammala, P. <strong>Prenatal diagnosis and fetal pathology of aspartylglucosaminuria.</strong> Am. J. Med. Genet. 19: 359-367, 1984.">Aula et al. (1984)</a>; <a href="#Mononen1993" class="mim-tip-reference" title="Mononen, I., Fisher, K. J., Kaartinen, V., Aronson, N. N., Jr. <strong>Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation.</strong> FASEB J. 7: 1247-1256, 1993.">Mononen et al. (1993)</a>; <a href="#Mononen1992" class="mim-tip-reference" title="Mononen, I., Heisterkamp, N., Kaartinen, V., Mononen, T., Williams, J. C., Groffen, J. <strong>Aspartylglycosaminuria in a non-Finnish patient caused by a donor splice mutation in the glycoasparaginase gene.</strong> J. Biol. Chem. 267: 3196-3199, 1992.">Mononen et al. (1992)</a>
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Aula, P., Astrin, K. H., Francke, U., Desnick, R. J.
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<strong>Assignment of the structural gene encoding human aspartylglucosaminidase to the long arm of chromosome 4 (4q21-4qter).</strong>
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Am. J. Hum. Genet. 36: 1215-1224, 1984.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/6517050/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">6517050</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=6517050" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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<strong>Assignment of the structural gene encoding human aspartylglucosaminidase to the long arm of chromosome 4 (4q21-4qter). (Abstract)</strong>
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Am. J. Hum. Genet. 36: 201S only, 1984.
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Aula, P., Rapola, J., von Koskull, H., Ammala, P.
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<strong>Prenatal diagnosis and fetal pathology of aspartylglucosaminuria.</strong>
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Am. J. Med. Genet. 19: 359-367, 1984.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/6507482/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">6507482</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=6507482" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1002/ajmg.1320190218" target="_blank">Full Text</a>]
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Borud, O., Torp, K. H.
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<strong>Aspartylglycosaminuria in northern Norway (Letter)</strong>
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Lancet 307: 1082-1083, 1976. Note: Originally Volume I.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/57494/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">57494</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=57494" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1016/s0140-6736(76)92266-2" target="_blank">Full Text</a>]
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Engelen, J., Hamers, A., Schrander-Stumpel, C., Mulder, H., Poorthuis, B.
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<strong>Assignment of the aspartylglucosaminidase gene (AGA) to 4q33-q35 based on decreased activity in a girl with a 46,XX,del(4)(q33) karyotype.</strong>
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Cytogenet. Cell Genet. 60: 208-209, 1992.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/1505217/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">1505217</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=1505217" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1159/000133338" target="_blank">Full Text</a>]
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Fisher, K. J., Aronson, N. N., Jr.
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<strong>Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients: amino acid substitution cys163-to-ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits.</strong>
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</p>
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<strong>Cloning and sequence analysis of a cDNA for human glycosylasparaginase: a single gene encodes the subunits of this lysosomal amidase.</strong>
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[<a href="https://doi.org/10.1016/0014-5793(90)81211-6" target="_blank">Full Text</a>]
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<strong>Interstitial tandem direct duplication of the long arm of chromosome 4 (q23-q27) and possible assignment of the structural gene encoding human aspartylglucosaminidase to this segment.</strong>
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[<a href="https://doi.org/10.1002/ajmg.1320390412" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1111/j.1399-0004.1983.tb01977.x" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1073/pnas.88.24.11222" target="_blank">Full Text</a>]
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<strong>Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.</strong>
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[<a href="https://doi.org/10.1002/j.1460-2075.1991.tb07920.x" target="_blank">Full Text</a>]
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<strong>In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation.</strong>
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[<a href="https://doi.org/10.1016/0888-7543(91)90120-4" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1002/humu.1380010503" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1002/humu.1380050408" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1111/j.1399-0004.1997.tb02448.x" target="_blank">Full Text</a>]
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Mononen, I., Fisher, K. J., Kaartinen, V., Aronson, N. N., Jr.
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[<a href="https://doi.org/10.1096/fasebj.7.13.8405810" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1073/pnas.88.7.2941" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1007/BF00197262" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1038/nsb1295-1102" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1093/hmg/5.6.737" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1093/hmg/10.9.983" target="_blank">Full Text</a>]
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<a id="24" class="mim-anchor"></a>
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<a id="Tenhunen1995" class="mim-anchor"></a>
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<div class="">
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<p class="mim-text-font">
|
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Tenhunen, K., Laan, M., Manninen, T., Palotie, A., Peltonen, L., Jalanko, A.
|
|
<strong>Molecular cloning, chromosomal assignment, and expression of the mouse aspartylglucosaminidase gene.</strong>
|
|
Genomics 30: 244-250, 1995.
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|
|
[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8586423/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8586423</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=8586423" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1006/geno.1995.9881" target="_blank">Full Text</a>]
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</p>
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</div>
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</li>
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<li>
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<a id="25" class="mim-anchor"></a>
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<a id="Tollersrud1989" class="mim-anchor"></a>
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<div class="">
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<p class="mim-text-font">
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Tollersrud, O. K., Aronson, N. N., Jr.
|
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<strong>Purification and characterization of rat liver glycosylasparaginase.</strong>
|
|
Biochem. J. 260: 101-108, 1989.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2775174/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2775174</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=2775174" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1042/bj2600101" target="_blank">Full Text</a>]
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</p>
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</div>
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</li>
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<li>
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<a id="26" class="mim-anchor"></a>
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<a id="Tollersrud1994" class="mim-anchor"></a>
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<div class="">
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<p class="mim-text-font">
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Tollersrud, O. K., Nilssen, O., Tranebjaerg, L., Borud, O.
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|
<strong>Aspartylglucosaminuria in northern Norway: a molecular and genealogical study.</strong>
|
|
J. Med. Genet. 31: 360-363, 1994.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8064811/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8064811</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=8064811" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1136/jmg.31.5.360" target="_blank">Full Text</a>]
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</p>
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</div>
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</li>
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<li>
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<a id="27" class="mim-anchor"></a>
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<a id="Ziegler1989" class="mim-anchor"></a>
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<div class="">
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<p class="mim-text-font">
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Ziegler, R., Schmidt, H., Sewell, A. C., Weglage, J., v. Lengerke, J. H., Ullrich, K.
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<strong>Aspartylglucosaminurie: Klinische Beschreibung von zwei deutschen Patienten.</strong>
|
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Mschr. Kinderheilk. 137: 454-457, 1989.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2811876/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2811876</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=2811876" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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</p>
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</li>
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</ol>
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<div>
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<br />
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</div>
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<div>
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<a id="creationDate" class="mim-anchor"></a>
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<div class="row">
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<div class="col-lg-2 col-md-2 col-sm-4 col-xs-4">
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<span class="text-nowrap mim-text-font">
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Creation Date:
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</span>
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</div>
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<div class="col-lg-6 col-md-6 col-sm-6 col-xs-6">
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<span class="mim-text-font">
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Carol A. Bocchini : 1/21/2010
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</span>
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</div>
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</div>
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</div>
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<div>
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<a id="editHistory" class="mim-anchor"></a>
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<div class="row">
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<div class="col-lg-2 col-md-2 col-sm-4 col-xs-4">
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<span class="text-nowrap mim-text-font">
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<a href="#mimCollapseEditHistory" role="button" data-toggle="collapse"> Edit History: </a>
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</span>
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</div>
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<div class="col-lg-6 col-md-6 col-sm-6 col-xs-6">
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<span class="mim-text-font">
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alopez : 11/07/2018
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</span>
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</div>
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</div>
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<div class="row collapse" id="mimCollapseEditHistory">
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<div class="col-lg-offset-2 col-md-offset-2 col-sm-offset-4 col-xs-offset-4 col-lg-6 col-md-6 col-sm-6 col-xs-6">
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<span class="mim-text-font">
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carol : 07/07/2015<br>carol : 5/13/2015<br>mcolton : 5/5/2015<br>terry : 1/28/2010<br>carol : 1/28/2010<br>terry : 1/22/2010<br>carol : 1/21/2010
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</span>
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</div>
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</div>
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</div>
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<div class="container visible-print-block">
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<div class="col-md-8 col-md-offset-1">
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<div>
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<div>
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<h3>
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<span class="mim-font">
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<strong>*</strong> 613228
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</span>
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</h3>
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</div>
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<div>
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<h3>
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<span class="mim-font">
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ASPARTYLGLUCOSAMINIDASE; AGA
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</span>
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</h3>
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</div>
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<div>
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<br />
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</div>
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<div>
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<div >
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<p>
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<span class="mim-font">
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<em>Alternative titles; symbols</em>
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</span>
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</p>
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</div>
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<div>
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<h4>
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<span class="mim-font">
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GLYCOSYLASPARAGINASE
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</span>
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</h4>
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</div>
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</div>
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<div>
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<br />
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</div>
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</div>
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<div>
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<p>
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<span class="mim-text-font">
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<strong><em>HGNC Approved Gene Symbol: AGA</em></strong>
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</span>
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</p>
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</div>
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<div>
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<p>
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<span class="mim-text-font">
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<strong>SNOMEDCT:</strong> 54954004;
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<strong>ICD10CM:</strong> E77.1;
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</span>
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</p>
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</div>
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<div>
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<br />
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</div>
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<div>
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<p>
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<span class="mim-text-font">
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<strong>
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<em>
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Cytogenetic location: 4q34.3
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Genomic coordinates <span class="small">(GRCh38)</span> : 4:177,430,774-177,442,437 </span>
|
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</em>
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</strong>
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<span class="small">(from NCBI)</span>
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</span>
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</p>
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</div>
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<div>
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<br />
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</div>
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<div>
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<h4>
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<span class="mim-font">
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<strong>Gene-Phenotype Relationships</strong>
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</span>
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</h4>
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<div>
|
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<table class="table table-bordered table-condensed small mim-table-padding">
|
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<thead>
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<tr class="active">
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<th>
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Location
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</th>
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<th>
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Phenotype
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</th>
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<th>
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Phenotype <br /> MIM number
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</th>
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<th>
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Inheritance
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</th>
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<th>
|
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Phenotype <br /> mapping key
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</th>
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</tr>
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</thead>
|
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<tbody>
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<tr>
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<td rowspan="1">
|
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<span class="mim-font">
|
|
4q34.3
|
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</span>
|
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</td>
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<td>
|
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<span class="mim-font">
|
|
Aspartylglucosaminuria
|
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</span>
|
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</td>
|
|
<td>
|
|
<span class="mim-font">
|
|
208400
|
|
</span>
|
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</td>
|
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<td>
|
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<span class="mim-font">
|
|
Autosomal recessive
|
|
</span>
|
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</td>
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<td>
|
|
<span class="mim-font">
|
|
3
|
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</span>
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</td>
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</tr>
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</tbody>
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</table>
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</div>
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</div>
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<div>
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<br />
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</div>
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<div>
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<h4>
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<span class="mim-font">
|
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<strong>TEXT</strong>
|
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</span>
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</h4>
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<div>
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<h4>
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<span class="mim-font">
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<strong>Description</strong>
|
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</span>
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</h4>
|
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</div>
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<span class="mim-text-font">
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<p>Aspartylglucosaminidase (AGA; EC 3.5.1.26) is a key enzyme in the catabolism of N-linked oligosaccharides of glycoproteins. It cleaves the asparagine from the residual N-acetylglucosamines as one of the final steps in the lysosomal breakdown of glycoproteins (summary by Ikonen et al., 1991). </p>
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</span>
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<div>
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<br />
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</div>
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<div>
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<h4>
|
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<span class="mim-font">
|
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<strong>Cloning and Expression</strong>
|
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</span>
|
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</h4>
|
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</div>
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<span class="mim-text-font">
|
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<p>Fisher et al. (1990) cloned and sequenced a cDNA for the enzyme deficient in this disorder, which they referred to as glycosylasparaginase. Tollersrud and Aronson (1989) purified glycosylasparaginase to homogeneity from rat liver and found it to have a native molecular mass of 49 kD and to comprise 2 subunits of 24 and 20 kD. From study of a cDNA for the human enzyme, Fisher et al. (1990) found that it is encoded as a 34.6-kD polypeptide that is posttranslationally processed to generate 2 subunits of approximately 19.5 (the alpha subunit) and 15 (the beta subunit) kD. The AGA cDNA encodes a deduced 436-amino acid protein. </p><p>Ikonen et al. (1991) cloned and sequenced a full-length cDNA for human AGA and studied its transient expression in COS-1 cells. </p>
|
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</span>
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<div>
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<br />
|
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</div>
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<div>
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<h4>
|
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<span class="mim-font">
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<strong>Biochemical Features</strong>
|
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</span>
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</h4>
|
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</div>
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<span class="mim-text-font">
|
|
<p>Oinonen et al. (1995) determined the high resolution crystal structure of human lysosomal aspartylglucosaminidase. The enzyme is synthesized as a single polypeptide precursor that is immediately posttranslationally cleaved into alpha- and beta-subunits. Two alpha- and beta-chains were found to pack together forming the final heterotetrameric structure. The catalytically essential residue, the N-terminal threonine of the beta-chain, is situated in the deep pocket of the funnel-shaped active site. On the basis of the structure of the enzyme-product complex, Oinonen et al. (1995) presented a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum. The 3-dimensional structure also allowed the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria. </p>
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</span>
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<div>
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<br />
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</div>
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<div>
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<h4>
|
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<span class="mim-font">
|
|
<strong>Mapping</strong>
|
|
</span>
|
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</h4>
|
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</div>
|
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<span class="mim-text-font">
|
|
<p>By analysis of somatic cell hybrids, Aula et al. (1984) assigned the structural gene for aspartylglucosaminidase to chromosome 4q21-qter. Halal et al. (1991) presented observations they interpreted as indicating a narrowing of the assignment of the gene to 4q23-q27: a girl with a de novo direct tandem duplication of 4q23-q27 had increased activity of AGA enzyme in cultured fibroblasts. Morris et al. (1992) concluded from in situ hybridization studies that the localization is 4q32-q33. Engelen et al. (1992) found reduced activity of the enzyme in a patient with deletion of 4q33-qter. </p><p>Tenhunen et al. (1995) found that the Aga gene in the mouse is located in the central area of the B region of chromosome 8 in the region that shows homology of synteny to the telomeric region of human 4q. The mouse gene spans an 11-kb genomic region and contains 9 exons, which is analogous to the human gene. Furthermore, the exon/intron boundaries of the mouse and human genes are identically positioned. </p>
|
|
</span>
|
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<div>
|
|
<br />
|
|
</div>
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<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>Molecular Genetics</strong>
|
|
</span>
|
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</h4>
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</div>
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<span class="mim-text-font">
|
|
<p>In Finnish patients with aspartylglucosaminuria (AGU; 208400), Ikonen et al. (1991) and Fisher et al. (1991) independently identified homozygosity for a cys163-to-ser (C163S; 613228.0001) mutation in the AGA gene. The C163S mutation is responsible for 98% of the cases of AGU in Finland (Isoniemi et al., 1995). </p><p>Ikonen et al. (1991) described the spectrum of 10 AGA mutations found in 12 unrelated patients of non-Finnish origin with AGU. Since 11 of the 12 were homozygotes, consanguinity appeared to be a common denominator in most AGU families, although consanguinity could be confirmed in only 2 of the families. Screening for the unknown gene defects was done using single-strand conformation polymorphism (SSCP) analysis. The mutations were distributed over the entire coding region of the AGA cDNA, except in the carboxyl-terminal 17-kD subunit in which they were clustered within a 46-amino acid region. Based on the character of the mutations, Ikonen et al. (1991) concluded that most of the mutations probably affected the folding and stability of the molecule and did not directly affect the active site of the enzyme. There were 3 non-Finnish patients who had the 'Finnish' C163S mutation but 2 of them were Norwegian and 1 was Swedish. These patients presumably had Finnish ancestry (Borud and Torp, 1976). </p><p>Tollersrud et al. (1994) reported 9 patients from 7 families identified in northern Norway. All were homozygous for the most prevalent Finnish mutation, cys163-to-ser. Genealogic investigation of 9 parents proved Finnish ancestry in all pedigrees. These Finnish immigrants originated in the main from the Tornio valley in northern Finland in a continuous immigration movement from 1700 to 1900. </p><p>Ikonen and Peltonen (1992) reviewed a total of 11 AGA mutations published to that time. </p><p>Laitinen et al. (1997) demonstrated that 2 Canadian sibs of non-Finnish extraction had AGU on the basis of compound heterozygosity at the AGA locus: a 299G-A transition caused a gly100-to-glu substitution and a 404T-C transition caused a phe135-to-ser substitution in the enzyme. </p><p>Isoniemi et al. (1995) found 7 Finnish AGU patients to be compound heterozygotes for the C163S mutation and another mutation, namely a 2-bp deletion in the second exon of the AGA cDNA, causing a shift of the reading frame and a premature termination of the polypeptide chain. </p><p>Saarela et al. (2001) used the 3-dimensional structure of AGA to predict structural consequences of AGU mutations, including 6 novel mutations, and to characterize the effect of mutations on intracellular stability, maturation, transport, and the activity of AGA. Most mutations are substitutions replacing the original amino acid with a bulkier residue. Mutations of the dimer interface prevent dimerization in the endoplasmic reticulum, whereas active site mutations not only destroy the activity but also affect maturation of the precursor. Depending on their effects on the stability of the AGA polypeptide, the authors categorized mutations as mild, moderate, or severe. </p>
|
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</span>
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<div>
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<br />
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</div>
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</div>
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<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>ALLELIC VARIANTS</strong>
|
|
</span>
|
|
<strong>12 Selected Examples):</strong>
|
|
</span>
|
|
</h4>
|
|
<div>
|
|
<p />
|
|
</div>
|
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<div>
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<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0001 ASPARTYLGLUCOSAMINURIA, FINNISH TYPE</strong>
|
|
</span>
|
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</h4>
|
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</div>
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<div>
|
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<span class="mim-text-font">
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|
|
AGA, CYS163SER
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<br />
|
|
|
|
SNP: rs121964904,
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|
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gnomAD: rs121964904,
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|
|
ClinVar: RCV000000243, RCV000410114
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</span>
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</div>
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<div>
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<span class="mim-text-font">
|
|
<p>By direct sequencing of PCR-amplified AGA cDNA from a patient with aspartylglucosaminuria (AGU; 208400), Ikonen et al. (1991) found a G-to-C mutation resulting in the substitution of serine for cysteine-163 (C163S). This mutation was found in all of 20 analyzed Finnish AGU patients, and in heterozygous form in all 53 carriers, and in none of 67 control individuals. The mutation produces a change in the predicted flexibility of the AGA polypeptide chain and removes an intramolecular S-S bridge. </p><p>Fisher et al. (1991) independently found the G-to-C transversion in DNA from Finnish AGU fibroblasts; however, they found a second G-to-A transition that resulted in an arginine-to-glutamine substitution as well. The 2 substitutions were present in all 3 Finnish cases studied and in none of 2 non-Finnish AGU fibroblast lines. In non-Finnish AGU fibroblasts, Fisher et al. (1991) found deletions as the apparent cause of the AGA deficiency. Mononen et al. (1991) likewise found 2 mutations, R161Q and C163S. Both mutations resulted in novel restriction endonuclease sites and were present in all 8 Finnish AGU patients studied, but they were absent from Finnish and non-Finnish controls and a non-Finnish case of AGU. Both amino acid changes would be expected to modify the structure of the protein profoundly: the replacement of an arginine by glutamine represents the substitution of a basic amino acid for one containing an uncharged polar group; the replacement of cysteine by serine may abolish a disulfide bridge. Whether both mutations are involved in the pathologic consequences or whether one mutation is a polymorphism was uncertain. </p><p>Ikonen et al. (1991) showed by in vitro mutagenesis studies that the C163S mutation is responsible for enzyme deficiency, whereas the arg161-to-gln (R161Q) substitution, which accompanies the other mutation in 98% of AGU alleles in Finland, represents a rare polymorphism. Cysteine-163 was shown to participate in an S-S bridge. The absence of this covalent crosslink in the mutated protein probably results in disturbed folding of the polypeptide chain and consequent decrease in its intracellular stability. Fisher and Aronson (1991) likewise found the 482G-A transition and the 488G-C transversion and demonstrated that only the latter was responsible for deficiency of glycosylasparaginase activity. The substitution prevented the normal posttranslational processing of the precursor polypeptide into its alpha and beta subunits. </p><p>The C163S mutation is responsible for 98% of the cases of AGU in Finland (Isoniemi et al., 1995). </p>
|
|
</span>
|
|
</div>
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|
<div>
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|
<br />
|
|
</div>
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|
|
|
</div>
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|
<div>
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|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0002 ASPARTYLGLUCOSAMINURIA</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
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|
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|
<div>
|
|
<span class="mim-text-font">
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|
|
|
AGA, GLY302ARG
|
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|
<br />
|
|
|
|
SNP: rs121964905,
|
|
|
|
|
|
|
|
ClinVar: RCV000000244
|
|
|
|
|
|
</span>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In a 10-year-old Turkish child with aspartylglucosaminuria (AGU; 208400), Ikonen et al. (1991) found a G-to-A substitution at nucleotide 904 of the AGA gene, resulting in substitution of arginine for glycine-302 (G302R). The patient was homozygous for the mutation and showed fibroblast AGA activity about 7% of normal. The parents were first cousins. </p>
|
|
</span>
|
|
</div>
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<div>
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|
<br />
|
|
</div>
|
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</div>
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|
<div>
|
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<div>
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|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0003 ASPARTYLGLUCOSAMINURIA</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
|
|
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|
<div>
|
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<span class="mim-text-font">
|
|
|
|
AGA, CYS306ARG
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<br />
|
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|
|
SNP: rs121964906,
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|
|
|
gnomAD: rs121964906,
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|
|
ClinVar: RCV000000245
|
|
|
|
|
|
</span>
|
|
</div>
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|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In a 16-year-old white American patient with aspartylglucosaminuria (AGU; 208400), Ikonen et al. (1991) found by the SSCP method a T-to-C change at nucleotide 916 of the AGA gene, resulting in substitution of arginine for cysteine-306 (C306R). </p>
|
|
</span>
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|
</div>
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|
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<div>
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|
<br />
|
|
</div>
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|
</div>
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<div>
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|
<div>
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|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0004 ASPARTYLGLUCOSAMINURIA</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
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<div>
|
|
<span class="mim-text-font">
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|
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|
AGA, GLY60ASP
|
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|
<br />
|
|
|
|
SNP: rs121964907,
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|
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|
|
|
|
ClinVar: RCV000000246
|
|
|
|
|
|
</span>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In a 3-year-old German child with aspartylglucosaminuria (AGU; 208400), previously reported by Ziegler et al. (1989), Ikonen et al. (1991) found a G-to-A substitution at nucleotide 179 of the AGA gene, resulting in substitution of the negatively charged aspartic acid for uncharged glycine at residue 60 (G60D). </p>
|
|
</span>
|
|
</div>
|
|
|
|
|
|
|
|
<div>
|
|
<br />
|
|
</div>
|
|
|
|
</div>
|
|
|
|
|
|
<div>
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0005 ASPARTYLGLUCOSAMINURIA</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
|
|
|
|
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
|
|
AGA, ALA101VAL
|
|
|
|
|
|
<br />
|
|
|
|
SNP: rs121964908,
|
|
|
|
|
|
gnomAD: rs121964908,
|
|
|
|
|
|
ClinVar: RCV000000247, RCV001532508, RCV004698463
|
|
|
|
|
|
</span>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In a 1-year-old Italian child with aspartylglucosaminuria (AGU; 208400), Ikonen et al. (1991) found a C-to-T transition at nucleotide 302 of the AGA gene, resulting in a change changed alanine-101 to valine (A101V). The patient was homozygous for this mutation, which was discovered by the SSCP method. The same mutation was found in a compound heterozygous state in an English patient (see 613228.0006). </p>
|
|
</span>
|
|
</div>
|
|
|
|
|
|
|
|
<div>
|
|
<br />
|
|
</div>
|
|
|
|
</div>
|
|
|
|
|
|
<div>
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0006 ASPARTYLGLUCOSAMINURIA</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
|
|
|
|
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
|
|
AGA, 7-BP DEL, NT102
|
|
|
|
|
|
<br />
|
|
|
|
SNP: rs386833417,
|
|
|
|
|
|
|
|
ClinVar: RCV000000248
|
|
|
|
|
|
</span>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In a 5-year-old English child with aspartylglucosaminuria (AGU; 208400), Ikonen et al. (1991) found compound heterozygosity for the A101V mutation (613228.0005) and a 7-nucleotide deletion (102_108delfs34Ter) in the AGA gene. The gene deletion would be predicted to result in the formation of a truncated polypeptide chain of only 33 amino acids. </p>
|
|
</span>
|
|
</div>
|
|
|
|
|
|
|
|
<div>
|
|
<br />
|
|
</div>
|
|
|
|
</div>
|
|
|
|
|
|
<div>
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0007 ASPARTYLGLUCOSAMINURIA</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
|
|
|
|
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
|
|
AGA, 1-BP INS, 800T
|
|
|
|
|
|
<br />
|
|
|
|
SNP: rs386833436,
|
|
|
|
|
|
gnomAD: rs386833436,
|
|
|
|
|
|
ClinVar: RCV000000249, RCV002512599, RCV004721239
|
|
|
|
|
|
</span>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In a 17-year-old Spanish American patient with aspartylglucosaminuria (AGU; 208400), Ikonen et al. (1991) found insertion of a single thymidine after nucleotide 800 in the AGA gene, resulting in a shift in the reading frame and a premature stop codon causing a truncated polypeptide chain with 318 amino acids of which the first 267 amino acids represented the normal AGA polypeptide (800_801insfs319Ter). </p>
|
|
</span>
|
|
</div>
|
|
|
|
|
|
|
|
<div>
|
|
<br />
|
|
</div>
|
|
|
|
</div>
|
|
|
|
|
|
<div>
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0008 ASPARTYLGLUCOSAMINURIA</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
|
|
|
|
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
|
|
AGA, 6-BP INS, NT127
|
|
|
|
|
|
<br />
|
|
|
|
SNP: rs386833418,
|
|
|
|
|
|
|
|
ClinVar: RCV000000250
|
|
|
|
|
|
</span>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In a 3-year-old Tunisian child with aspartylglucosaminuria (AGU; 208400), the offspring of first-cousin parents, Ikonen et al. (1991) found homozygosity for a 6-nucleotide insertion (ATGCGG) after nucleotide 127 in the AGA gene, causing an in-frame insertion of aspartic acid and alanine after amino acid 42. </p>
|
|
</span>
|
|
</div>
|
|
|
|
|
|
|
|
<div>
|
|
<br />
|
|
</div>
|
|
|
|
</div>
|
|
|
|
|
|
<div>
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0009 ASPARTYLGLUCOSAMINURIA</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
|
|
|
|
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
|
|
AGA, IVS8DS, G-T, +1
|
|
|
|
|
|
<br />
|
|
|
|
|
|
|
|
ClinVar: RCV000000251
|
|
|
|
|
|
</span>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In a 12-year-old black American patient with aspartylglucosaminuria (AGU; 208400) (Hreidarsson et al., 1983; Camden number GM03560), Ikonen et al. (1991) found homozygosity for a deletion of nucleotides 807-940 in the AGA gene. Further sequence analysis of both cDNA and genomic DNA confirmed that a 134-bp exon was missing from the cDNA and that a G-to-T substitution had occurred in the adjacent 3-prime intron at position +1 of the splice donor site; the authors thus concluded that this was a splicing mutation. The mutation resulted in a transcript that was 134-bp shorter than normal. The mutation also resulted in the shift of the reading frame and a premature termination codon at the beginning of the following exon. </p>
|
|
</span>
|
|
</div>
|
|
|
|
|
|
|
|
<div>
|
|
<br />
|
|
</div>
|
|
|
|
</div>
|
|
|
|
|
|
<div>
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0010 ASPARTYLGLUCOSAMINURIA</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
|
|
|
|
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
|
|
AGA, 1-BP DEL, 336T
|
|
|
|
|
|
<br />
|
|
|
|
SNP: rs794728009,
|
|
|
|
|
|
|
|
ClinVar: RCV000000252
|
|
|
|
|
|
</span>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In an 8-year-old Dutch child with aspartylglucosaminuria (AGU; 208400), Ikonen et al. (1991) found deletion of 1 nucleotide, thymidine-336, in the AGA gene. This resulted in a frameshift and premature termination of the polypeptide chain after 126 amino acids. </p>
|
|
</span>
|
|
</div>
|
|
|
|
|
|
|
|
<div>
|
|
<br />
|
|
</div>
|
|
|
|
</div>
|
|
|
|
|
|
<div>
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-text-font">
|
|
<strong>.0011 MOVED TO 613228.0009</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<br />
|
|
</div>
|
|
|
|
</div>
|
|
|
|
|
|
<div>
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0012 ASPARTYLGLUCOSAMINURIA</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
|
|
|
|
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
|
|
AGA, SER72PRO
|
|
|
|
|
|
<br />
|
|
|
|
SNP: rs121964909,
|
|
|
|
|
|
|
|
ClinVar: RCV000000253
|
|
|
|
|
|
</span>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>Peltola et al. (1996) reported that a T-to-C change at codon 214 in the AGA gene, leading to a ser72-to-pro (S72P) substitution, occurred in affected members of 4 Arab families with aspartylglucosaminuria (AGU; 208400). They noted that this mutation is the first naturally occurring AGA mutation that involves an active site and is apparently the second most common AGA mutation worldwide. </p>
|
|
</span>
|
|
</div>
|
|
|
|
|
|
|
|
<div>
|
|
<br />
|
|
</div>
|
|
|
|
</div>
|
|
|
|
|
|
|
|
</div>
|
|
|
|
|
|
|
|
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>See Also:</strong>
|
|
</span>
|
|
</h4>
|
|
<span class="mim-text-font">
|
|
Aula et al. (1984); Aula et al. (1984); Mononen et al. (1993);
|
|
Mononen et al. (1992)
|
|
</span>
|
|
<div>
|
|
<br />
|
|
</div>
|
|
</div>
|
|
|
|
|
|
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>REFERENCES</strong>
|
|
</span>
|
|
</h4>
|
|
<div>
|
|
<p />
|
|
</div>
|
|
|
|
<div>
|
|
<ol>
|
|
|
|
<li>
|
|
<p class="mim-text-font">
|
|
Aula, P., Astrin, K. H., Francke, U., Desnick, R. J.
|
|
<strong>Assignment of the structural gene encoding human aspartylglucosaminidase to the long arm of chromosome 4 (4q21-4qter).</strong>
|
|
Am. J. Hum. Genet. 36: 1215-1224, 1984.
|
|
|
|
|
|
[PubMed: 6517050]
|
|
|
|
|
|
|
|
</p>
|
|
</li>
|
|
|
|
<li>
|
|
<p class="mim-text-font">
|
|
Aula, P., Astrin, K. H., Francke, U., Desnick, R. J.
|
|
<strong>Assignment of the structural gene encoding human aspartylglucosaminidase to the long arm of chromosome 4 (4q21-4qter). (Abstract)</strong>
|
|
Am. J. Hum. Genet. 36: 201S only, 1984.
|
|
|
|
</p>
|
|
</li>
|
|
|
|
<li>
|
|
<p class="mim-text-font">
|
|
Aula, P., Rapola, J., von Koskull, H., Ammala, P.
|
|
<strong>Prenatal diagnosis and fetal pathology of aspartylglucosaminuria.</strong>
|
|
Am. J. Med. Genet. 19: 359-367, 1984.
|
|
|
|
|
|
[PubMed: 6507482]
|
|
|
|
|
|
[Full Text: https://doi.org/10.1002/ajmg.1320190218]
|
|
|
|
|
|
</p>
|
|
</li>
|
|
|
|
<li>
|
|
<p class="mim-text-font">
|
|
Borud, O., Torp, K. H.
|
|
<strong>Aspartylglycosaminuria in northern Norway (Letter)</strong>
|
|
Lancet 307: 1082-1083, 1976. Note: Originally Volume I.
|
|
|
|
|
|
[PubMed: 57494]
|
|
|
|
|
|
[Full Text: https://doi.org/10.1016/s0140-6736(76)92266-2]
|
|
|
|
|
|
</p>
|
|
</li>
|
|
|
|
<li>
|
|
<p class="mim-text-font">
|
|
Engelen, J., Hamers, A., Schrander-Stumpel, C., Mulder, H., Poorthuis, B.
|
|
<strong>Assignment of the aspartylglucosaminidase gene (AGA) to 4q33-q35 based on decreased activity in a girl with a 46,XX,del(4)(q33) karyotype.</strong>
|
|
Cytogenet. Cell Genet. 60: 208-209, 1992.
|
|
|
|
|
|
[PubMed: 1505217]
|
|
|
|
|
|
[Full Text: https://doi.org/10.1159/000133338]
|
|
|
|
|
|
</p>
|
|
</li>
|
|
|
|
<li>
|
|
<p class="mim-text-font">
|
|
Fisher, K. J., Aronson, N. N., Jr.
|
|
<strong>Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients: amino acid substitution cys163-to-ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits.</strong>
|
|
J. Biol. Chem. 266: 12105-12113, 1991.
|
|
|
|
|
|
[PubMed: 1904874]
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