Total submissions: 2
Submitter | RCV | SCV | Clinical significance | Condition | Last evaluated | Review status | Method | Comment |
---|---|---|---|---|---|---|---|---|
Baylor Genetics | RCV001334142 | SCV001526894 | uncertain significance | 3-methylcrotonyl-CoA carboxylase 2 deficiency | 2018-07-11 | criteria provided, single submitter | clinical testing | This variant was determined to be of uncertain significance according to ACMG Guidelines, 2015 [PMID:25741868]. This variant has been previously reported in one patient with 3-methylcrotonoyl-CoA carboxylase 2 deficiency and the functional study showed that this variant has about 4% of the activity produced by wild type allele [PMID: 11181649] An allelic change affecting the same amino acid, c.578G>A (p.R193H), has also been previously reported in patients with with 3-methylcrotonoyl-CoA carboxylase 2 [PMID: 16835865] The c.955G>A (p.G319R) variant has been previously reported in one patient with 3-methylcrotonoyl-CoA carboxylase 2 deficiency [PMID: 25382614] |
Labcorp Genetics |
RCV001334142 | SCV003525831 | likely pathogenic | 3-methylcrotonyl-CoA carboxylase 2 deficiency | 2022-08-20 | criteria provided, single submitter | clinical testing | In summary, the currently available evidence indicates that the variant is pathogenic, but additional data are needed to prove that conclusively. Therefore, this variant has been classified as Likely Pathogenic. This sequence change replaces glycine, which is neutral and non-polar, with arginine, which is basic and polar, at codon 319 of the MCCC2 protein (p.Gly319Arg). This variant is present in population databases (no rsID available, gnomAD 0.0009%). This missense change has been observed in individual(s) with MCCC2-related conditions (PMID: 25382614). In at least one individual the data is consistent with being in trans (on the opposite chromosome) from a pathogenic variant. ClinVar contains an entry for this variant (Variation ID: 1032131). 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 MCCC2 protein function. |