Total submissions: 2
Submitter | RCV | SCV | Clinical significance | Condition | Last evaluated | Review status | Method | Comment |
---|---|---|---|---|---|---|---|---|
Labcorp Genetics |
RCV001916136 | SCV002179358 | pathogenic | Familial melanoma | 2024-01-26 | criteria provided, single submitter | clinical testing | This variant, c.95_112del, results in the deletion of 6 amino acid(s) of the CDKN2A (p16INK4a) protein (p.Leu32_Leu37del), but otherwise preserves the integrity of the reading frame. This variant is not present in population databases (gnomAD no frequency). This variant has been observed in individual(s) with melanoma (PMID: 33050356). ClinVar contains an entry for this variant (Variation ID: 1409909). Experimental studies and prediction algorithms are not available or were not evaluated, and the functional significance of this variant is currently unknown. This variant disrupts a region of the CDKN2A (p16INK4a) protein in which other variant(s) (p.Gly35Ala) have been determined to be pathogenic (PMID: 8595405, 9425228, 12072543, 12556369, 19260062, 19759551, 21462282, 22841127). This suggests that this is a clinically significant region of the protein, and that variants that disrupt it are likely to be disease-causing. For these reasons, this variant has been classified as Pathogenic. |
Ambry Genetics | RCV002370509 | SCV002688236 | pathogenic | Hereditary cancer-predisposing syndrome | 2021-02-18 | criteria provided, single submitter | clinical testing | The c.95_112del18 pathogenic mutation (also known as p.L32_L37del) is located in coding exon 1 of the CDKN2A gene, results from an in-frame TGGAGGCGGGGGCGCTGC deletion at nucleotide positions 95 to 112. This results in the in-frame deletion of 6 amino acid residues at codons 32 to 37. This alteration was identified in a Czech female diagnosed with early-onset melanoma and gastric cancer, and a family history of melanoma and breast, colorectal, gastric, and lung cancers (Stolarova L et al. Biomedicines. 2020 Oct;8:). This variant impacts a region that is known to be critical to protein function based on overlap with known likely pathogenic missense mutations. In addition, based on internal structural analysis, this variant disrupts protein structure (Byeon IJ et al. Mol Cell. 1998 Feb;1:421-31). As such, this alteration is interpreted as a disease-causing mutation. |