<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Chi, An</style></author><author><style face="normal" font="default" size="100%">Huttenhower, Curtis</style></author><author><style face="normal" font="default" size="100%">Geer, Lewis Y</style></author><author><style face="normal" font="default" size="100%">Coon, Joshua J</style></author><author><style face="normal" font="default" size="100%">Syka, John E P</style></author><author><style face="normal" font="default" size="100%">Bai, Dina L</style></author><author><style face="normal" font="default" size="100%">Shabanowitz, Jeffrey</style></author><author><style face="normal" font="default" size="100%">Burke, Daniel J</style></author><author><style face="normal" font="default" size="100%">Troyanskaya, Olga G</style></author><author><style face="normal" font="default" size="100%">Hunt, Donald F</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</style></title><secondary-title><style face="normal" font="default" size="100%">Proceedings of the National Academy of Sciences of the United States of America</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2007 Feb 13</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">104</style></volume><pages><style face="normal" font="default" size="100%">2193-8</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">We present a strategy for the analysis of the yeast phosphoproteome that uses endo-Lys C as the proteolytic enzyme, immobilized metal affinity chromatography for phosphopeptide enrichment, a 90-min nanoflow-HPLC/electrospray-ionization MS/MS experiment for phosphopeptide fractionation and detection, gas phase ion/ion chemistry, electron transfer dissociation for peptide fragmentation, and the Open Mass Spectrometry Search Algorithm for phosphoprotein identification and assignment of phosphorylation sites. From a 30-microg (approximately 600 pmol) sample of total yeast protein, we identify 1,252 phosphorylation sites on 629 proteins. Identified phosphoproteins have expression levels that range from &lt;50 to 1,200,000 copies per cell and are encoded by genes involved in a wide variety of cellular processes. We identify a consensus site that likely represents a motif for one or more uncharacterized kinases and show that yeast kinases, themselves, contain a disproportionately large number of phosphorylation sites. Detection of a pHis containing peptide from the yeast protein, Cdc10, suggests an unexpected role for histidine phosphorylation in septin biology. From diverse functional genomics data, we show that phosphoproteins have a higher number of interactions than an average protein and interact with each other more than with a random protein. They are also likely to be conserved across large evolutionary distances.</style></abstract><issue><style face="normal" font="default" size="100%">7</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/17287358?dopt=Abstract</style></custom1></record></records></xml>
