Total submissions: 3
Submitter | RCV | SCV | Clinical significance | Condition | Last evaluated | Review status | Method | Comment |
---|---|---|---|---|---|---|---|---|
Gene |
RCV000520714 | SCV000619145 | pathogenic | not provided | 2017-07-20 | criteria provided, single submitter | clinical testing | The G329R variant in the COL1A1 gene has not been reported previously as a pathogenic variant nor as a benign variant, to our knowledge. G329R occurs in the triple helical domain and replaces the Glycine in the canonical Gly-X-Y repeat. Variants in these Glycines result in poor winding of the collagen triple helix and a less functional protein. The G329R variant is not observed in large population cohorts (Lek et al., 2016; 1000 Genomes Consortium et al., 2015; Exome Variant Server). The G329R variant is a non-conservative amino acid substitution, which is likely to impact secondary protein structure as these residues differ in polarity, charge, size and/or other properties. This substitution occurs at a position that is conserved across species, and in silico analysis predicts this variant is probably damaging to the protein structure/function. Missense variants in nearby Glycine residues (G326D, G332R, G332A) have been reported in the Human Gene Mutation Database in association with osteogenesis imperfecta (Stenson et al., 2014), supporting the functional importance of this region of the protein. Therefore, we interpret G329R as a pathogenic variant. |
Fulgent Genetics, |
RCV000763012 | SCV000893457 | likely pathogenic | Osteogenesis imperfecta with normal sclerae, dominant form; Postmenopausal osteoporosis; Osteogenesis imperfecta, perinatal lethal; Osteogenesis imperfecta type III; Infantile cortical hyperostosis; Ehlers-Danlos syndrome, arthrochalasia type; Osteogenesis imperfecta type I | 2018-10-31 | criteria provided, single submitter | clinical testing | |
Athena Diagnostics | RCV000520714 | SCV001143195 | pathogenic | not provided | 2018-11-09 | criteria provided, single submitter | clinical testing | The variant disrupts a glycine residue in the canonical Gly-X-Y repeats of the triple helix domain, which are required for stability and structure of this protein. Therefore it is expected to severely affect the function of the protein. Found in at least one symptomatic patient, and not found in general population data. |