rs72645357
From SNPedia
| Orientation | minus |
| Stabilized | minus |
| Geno | Mag | Summary |
|---|---|---|
| (G;G) | 0 | common in clinvar |
| Make rs72645357(A;A) |
| Make rs72645357(A;G) |
| Reference | GRCh38 38.1/141 |
| Chromosome | 17 |
| Position | 50196163 |
| Gene | COL1A1 |
| is a | snp |
| is | mentioned by |
| dbSNP | rs72645357 |
| dbSNP (classic) | rs72645357 |
| ClinGen | rs72645357 |
| ebi | rs72645357 |
| HLI | rs72645357 |
| Exac | rs72645357 |
| Gnomad | rs72645357 |
| Varsome | rs72645357 |
| LitVar | rs72645357 |
| Map | rs72645357 |
| PheGenI | rs72645357 |
| Biobank | rs72645357 |
| 1000 genomes | rs72645357 |
| hgdp | rs72645357 |
| ensembl | rs72645357 |
| geneview | rs72645357 |
| scholar | rs72645357 |
| rs72645357 | |
| pharmgkb | rs72645357 |
| gwascentral | rs72645357 |
| openSNP | rs72645357 |
| 23andMe | rs72645357 |
| SNPshot | rs72645357 |
| SNPdbe | rs72645357 |
| MSV3d | rs72645357 |
| GWAS Ctlg | rs72645357 |
| Max Magnitude | 0 |
| ClinVar | |
|---|---|
| Risk | rs72645357(A;A) |
| Alt | rs72645357(A;A) |
| Reference | Rs72645357(G;G) |
| Significance | Pathogenic |
| Disease | Osteogenesis imperfecta type III Osteogenesis imperfecta not provided Osteogenesis imperfecta with normal sclerae |
| Variation | info |
| Gene | COL1A1 |
| CLNDBN | Osteogenesis imperfecta type III Osteogenesis imperfecta not provided Osteogenesis imperfecta with normal sclerae, dominant form |
| Reversed | 1 |
| HGVS | NC_000017.10:g.48273524C>T |
| CLNSRC | OMIM Allelic Variant |
| CLNACC | RCV000018853.27, RCV000029586.1, RCV000480634.1, RCV000490676.1, |
[PMID 2037280] Osteogenesis imperfecta due to recurrent point mutations at CpG dinucleotides in the COL1A1 gene of type I collagen.
[PMID 8669434] Substitution of arginine for glycine at position 154 of the alpha 1 chain of type I collagen in a variant of osteogenesis imperfecta: comparison to previous cases with the same mutation.
[PMID 17078022
] Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans.
