Phosphorylation states of cell cycle and DNA repair proteins can be altered by the nsSNPs

<p>Abstract</p> <p>Background</p> <p>Phosphorylation is a reversible post-translational modification that affects the intrinsic properties of proteins, such as structure and function. Non-synonymous single nucleotide polymorphisms (nsSNPs) result in the substitution of...

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Main Authors: Savas Sevtap, Ozcelik Hilmi
Format: Article
Language:English
Published: BMC 2005-08-01
Series:BMC Cancer
Online Access:http://www.biomedcentral.com/1471-2407/5/107
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spelling doaj-b93d620e51fa4470aeb9a6cf721a57a42020-11-24T21:17:07ZengBMCBMC Cancer1471-24072005-08-015110710.1186/1471-2407-5-107Phosphorylation states of cell cycle and DNA repair proteins can be altered by the nsSNPsSavas SevtapOzcelik Hilmi<p>Abstract</p> <p>Background</p> <p>Phosphorylation is a reversible post-translational modification that affects the intrinsic properties of proteins, such as structure and function. Non-synonymous single nucleotide polymorphisms (nsSNPs) result in the substitution of the encoded amino acids and thus are likely to alter the phosphorylation motifs in the proteins.</p> <p>Methods</p> <p>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.</p> <p>Results</p> <p>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.</p> <p>Conclusion</p> <p>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.</p> http://www.biomedcentral.com/1471-2407/5/107
collection DOAJ
language English
format Article
sources DOAJ
author Savas Sevtap
Ozcelik Hilmi
spellingShingle Savas Sevtap
Ozcelik Hilmi
Phosphorylation states of cell cycle and DNA repair proteins can be altered by the nsSNPs
BMC Cancer
author_facet Savas Sevtap
Ozcelik Hilmi
author_sort Savas Sevtap
title Phosphorylation states of cell cycle and DNA repair proteins can be altered by the nsSNPs
title_short Phosphorylation states of cell cycle and DNA repair proteins can be altered by the nsSNPs
title_full Phosphorylation states of cell cycle and DNA repair proteins can be altered by the nsSNPs
title_fullStr Phosphorylation states of cell cycle and DNA repair proteins can be altered by the nsSNPs
title_full_unstemmed Phosphorylation states of cell cycle and DNA repair proteins can be altered by the nsSNPs
title_sort phosphorylation states of cell cycle and dna repair proteins can be altered by the nssnps
publisher BMC
series BMC Cancer
issn 1471-2407
publishDate 2005-08-01
description <p>Abstract</p> <p>Background</p> <p>Phosphorylation is a reversible post-translational modification that affects the intrinsic properties of proteins, such as structure and function. Non-synonymous single nucleotide polymorphisms (nsSNPs) result in the substitution of the encoded amino acids and thus are likely to alter the phosphorylation motifs in the proteins.</p> <p>Methods</p> <p>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.</p> <p>Results</p> <p>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.</p> <p>Conclusion</p> <p>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.</p>
url http://www.biomedcentral.com/1471-2407/5/107
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