Background and Objectives: 3' untranslated region (3'UTR) single nucleotide polymorphisms (SNPs) represent genetic variations that may potentially affect binding of miRNA to coding genes, potentially leading to complex disorders. We aimed to perform in silico analysis of the potential phenotypic effect of 3'UTR SNPs on human astrocyte elevated gene-1 (AEG-1), a newly identified candidate cancer gene.Methods: We gathered a list of all 3'UTR SNPs located in the human AEG-1 gene from the SNP database. Analysis of the potential effects was done using MirSNP and MicroSNiper.Results: Analysis by the MirSNP estimated that rs187728237 might increase the affinity of two miRNAs and decrease the affinity of 10 other miRNAs to the AEG-1 transcript. Moreover, MicroSNiPer showed that rs80320514 might affect 24 putative miRNA binding sites in the 3'UTR of AEG-1.Conclusion: Based on our findings, it can be concluded that the 3'UTR SNPs located in the human AEG-1 gene may be within the miRNA targets of the transcript, therefore affecting the stability of putative miRNA-target interactions.
Background and Objectives: Non-synonymous single nucleotide polymorphisms are typical genetic variations that may potentially affect the structure or function of expressed proteins, and therefore could be involved in complex disorders. A computationalbased analysis has been done to evaluate the phenotypic effect of non-synonymous single nucleotide polymorphisms in the gene encoding the human hypoxanthine-guanine phosphoribosyltransferase (HGPRT-1). HGPRT-1 is an enzyme involved in purine recycling pathway and its deficiency is associated with several human genetic disorders. Methods: We provide a list of all amino acid replacements in the human HGPRT-1 from the dbSNP, Uniprot and dbEST databases. Sorting intolerant from tolerant (SIFT) and PolyPhen softwares were also used in our study. Results: Of 94 amino acid substitutions, rs 267606863 was predicted to be the most deleterious. Substitutions of S110L and S104A in flexible loop and D194N, D201Y, H204R, Y195C, F199V and H204D in hood domain were predicted as functionally damaging. Conclusion: It could be concluded that these intolerant changes may lie within a functional region of the protein and may affect the stability and folding of HGPRT-1. These variants could be used for future functional and molecular epidemiology studies of HGPRT-1related disorders.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.