Total submissions: 6
Submitter | RCV | SCV | Clinical significance | Condition | Last evaluated | Review status | Method | Comment |
---|---|---|---|---|---|---|---|---|
Genomic Diagnostic Laboratory, |
RCV000202814 | SCV000258207 | uncertain significance | not specified | 2015-06-25 | criteria provided, single submitter | clinical testing | |
Ambry Genetics | RCV002310718 | SCV000319646 | pathogenic | Familial thoracic aortic aneurysm and aortic dissection | 2015-05-08 | criteria provided, single submitter | clinical testing | The p.R105C pathogenic mutation (also known as c.313C>T), located in coding exon 2 of the SLC2A10 gene, results from a C to T substitution at nucleotide position 313. The arginine at codon 105 is replaced by cysteine, an amino acid with highly dissimilar properties. This variant has been described in a consanguineous Saudi Arabian family in which one individual was affected with arterial tortuosity syndrome (ATS). The affected individual was homozygous for the variant and both of his unaffected parents were confirmed to be heterozygous (Faiyaz-Ul-Haque M et al. Atherosclerosis 2009;203(2):466-71). This alteration has also been reported in a second individual with ATS in the compound heterozygous state with the recurrent SLC2A10 nonsense mutation p.G445Efs*40 (Hardin JS et al. Ophthalmic Genet. 2018;39:29-34). Based on the supporting evidence, this alteration is interpreted as a disease-causing mutation. |
Invitae | RCV000202447 | SCV000644163 | pathogenic | Arterial tortuosity syndrome | 2023-10-13 | criteria provided, single submitter | clinical testing | This sequence change replaces arginine, which is basic and polar, with cysteine, which is neutral and slightly polar, at codon 105 of the SLC2A10 protein (p.Arg105Cys). This variant is present in population databases (rs767864243, gnomAD 0.009%). This missense change has been observed in individuals with clinical features of arterial tortuosity syndrome (PMID: 18774132, 28726533; Invitae). ClinVar contains an entry for this variant (Variation ID: 161104). Advanced modeling of protein sequence and biophysical properties (such as structural, functional, and spatial information, amino acid conservation, physicochemical variation, residue mobility, and thermodynamic stability) performed at Invitae indicates that this missense variant is expected to disrupt SLC2A10 protein function. This variant disrupts the p.Arg105 amino acid residue in SLC2A10. Other variant(s) that disrupt this residue have been observed in individuals with SLC2A10-related conditions (PMID: 28726533), which suggests that this may be a clinically significant amino acid residue. For these reasons, this variant has been classified as Pathogenic. |
Ce |
RCV000997782 | SCV001153486 | likely pathogenic | not provided | 2019-05-01 | criteria provided, single submitter | clinical testing | |
Baylor Genetics | RCV000202447 | SCV001521671 | likely pathogenic | Arterial tortuosity syndrome | criteria provided, single submitter | clinical testing | ||
Gene |
RCV000202447 | SCV000195658 | not provided | Arterial tortuosity syndrome | no assertion provided | literature only |