de Winter et al. (1998) analyzed the FANCG gene in two sibs (a male and a female) from a consanguineous Lebanese family. De Winter et al. (1998) concluded that complementation group G Fanconi anemia was caused in these patients by homozygosity for a splice acceptor site G-C substitution at IVS13-1, which results in a truncated protein.

Tamary et al. (2004) investigated the molecular basis of Fanconi anemia (FANCA and FANCG) in three consanguineous families with nine patients and an additional unrelated patient. In one consanguineous family with three affected individuals, Tamary et al. (2004) applied SSCP analysis coupled with RT-PCR and DNA sequencing for the exons of the FANCG gene and identified a unique disease-causing splice-site IVS4+3A-G mutation. cDNA analysis of the mutation suggested exon 4 skipping in FANCG gene that caused an out-of-frame mRNA which predicted a new termination codon (TAA, at new codon 107), probably resulting in a truncated protein.

Ghazwani et al. (2016) reviewed Fanconi anemia (FA) patients at a Saudi Arabian hospital to determine their underlying genetic mutations.  Ten FA patients from consanguineous families were identified for the study.  Of these, a 21-year-old Saudi female was found to have a homozygous c.637_643del in the FANCG gene, resulting in a p.Tyr213Lysfs*6 substitution.  This mutation was not found in 50 ethnically-matched, non-FA controls.  The patient’s symptoms included micrognathia, café au lait spots, a short stature and an ectopic kidney.  She suffered from severe aplastic anemia and eventually, acute myeloid leukemia.  This mutation had been found to be frequent in sub-Saharan African FA patients and has been associated with an increased risk of hematological malignancy.  The authors also noted that, unlike FANCG, most Saudi mutations were found in downstream FA pathway genes. The FANCD2 protein monoubiquitination assay would thus be unable to detect most Saudi FA cases.