| Date | Panel | Item | Activity | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Mendeliome v2.0 | RPN1 | Gene migrated from ENSG00000163902 to ENSG00000163902 (gene set migration) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mendeliome v1.4931 | RPN1 | Krithika Murali Marked gene: RPN1 as ready | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mendeliome v1.4931 | RPN1 | Krithika Murali Gene: rpn1 has been classified as Red List (Low Evidence). | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mendeliome v1.4931 | RPN1 |
Krithika Murali gene: RPN1 was added gene: RPN1 was added to Mendeliome. Sources: Literature Mode of inheritance for gene: RPN1 was set to BIALLELIC, autosomal or pseudoautosomal Publications for gene: RPN1 were set to 41935956 Phenotypes for gene: RPN1 were set to Syndromic disease, MONDO:0002254 Review for gene: RPN1 was set to RED Added comment: RPN1 encodes ribophorin I, a subunit of the oligosaccharyltransferase complex that mediates N‑linked protein glycosylation. PMID 41935956 report two affected siblings from a consanguineous family harbouring a homozygous nonsense variant c.1654C>T (p.Gln552*) who present with a congenital disorder of glycosylation characterised by neurodevelopmental delay, dysmorphic features and a type I transferrin profile. Biochemical analyses show a truncated RPN1 protein and reduced OST complex components, and CRISPR knock‑in of the variant in HEK293 cells reproduces the glycosylation defect, supporting a loss‑of‑function mechanism. Sources: Literature |
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||