%0 Journal Article
%T Phosphorylation states of cell cycle and DNA repair proteins can be altered by the nsSNPs
%A Sevtap Savas
%A Hilmi Ozcelik
%J BMC Cancer
%D 2005
%I BioMed Central
%R 10.1186/1471-2407-5-107
%X In this study, we used the web-based NetPhos tool to predict candidate nsSNPs that either introduce or remove putative phosphorylation sites in proteins that act in DNA repair and cell cycle pathways.Our results demonstrated that a total of 15 nsSNPs (16.9%) were likely to alter the putative phosphorylation patterns of 14 proteins. Three of these SNPs (CDKN1A-S31R, OGG1-S326C, and XRCC3-T241M) have already found to be associated with altered cancer risk. We believe that this set of nsSNPs constitutes an excellent resource for further molecular and genetic analyses.The novel systematic approach used in this study will accelerate the understanding of how naturally occurring human SNPs may alter protein function through the modification of phosphorylation mechanisms and contribute to disease susceptibility.Phosphorylation is a common, reversible post-translational modification that occurs at serine (S), threonine (T), and tyrosine (Y) residues in proteins [1]. Overall, phosphorylation can alter the structure, function, interaction, stability, and the sub-cellular location of the proteins [2-4], and therefore play an indispensable role in regulation of the cellular processes such as signal transduction, gene expression, cytoskeletal regulation, apoptosis, homeostasis, cell cycle, and DNA damage recognition and repair [5-11]. The phosphorylation state of a protein is determined by the opposing actions of kinases and phosphatases [12]. Proteins may contain multiple phosphorylation sites, which may be targeted by different kinases/phosphatases [2]. The activity of kinases and phosphatases at different times and/or upon different stimuli provides a means of powerful control over the protein phosphorylation state and thus the biological processes the protein is involved in.In the post-genomic era, there is an expanding interest in identification of the single nucleotide polymorphisms (SNPs) that might affect the protein function and thus contribute to the disease susceptibil
%U http://www.biomedcentral.com/1471-2407/5/107