<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Hegemann B</submitter><funding>Austrian Science Fund FWF</funding><funding>NIEHS NIH HHS</funding><funding>NCI NIH HHS</funding><funding>NIGMS NIH HHS</funding><pagination>rs12</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4206221</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>4(198)</volume><pubmed_abstract>Progression through mitosis depends on a large number of protein complexes that regulate the major structural and physiological changes necessary for faithful chromosome segregation. Most, if not all, of the mitotic processes are regulated by a set of mitotic protein kinases that control protein activity by phosphorylation. Although many mitotic phosphorylation events have been identified in proteome-scale mass spectrometry studies, information on how these phosphorylation sites are distributed within mitotic protein complexes and which kinases generate these phosphorylation sites is largely lacking. We used systematic protein-affinity purification combined with mass spectrometry to identify 1818 phosphorylation sites in more than 100 mitotic protein complexes. In many complexes, the phosp</pubmed_abstract><journal>Science signaling</journal><pubmed_title>Systematic phosphorylation analysis of human mitotic protein complexes.</pubmed_title><pmcid>PMC4206221</pmcid><funding_grant_id>CA-112967</funding_grant_id><funding_grant_id>P50 GM068762</funding_grant_id><funding_grant_id>GM-60594</funding_grant_id><funding_grant_id>R01 GM060594</funding_grant_id><funding_grant_id>GM-68762</funding_grant_id><funding_grant_id>ES-015339</funding_grant_id><funding_grant_id>U54 CA112967</funding_grant_id><funding_grant_id>F 3407</funding_grant_id><funding_grant_id>R01 ES015339</funding_grant_id><pubmed_authors>Hudecz O</pubmed_authors><pubmed_authors>Mazanek M</pubmed_authors><pubmed_authors>Heriche JK</pubmed_authors><pubmed_authors>Rameseder J</pubmed_authors><pubmed_authors>Hyman AA</pubmed_authors><pubmed_authors>Yaffe MB</pubmed_authors><pubmed_authors>Poser I</pubmed_authors><pubmed_authors>Liu S</pubmed_authors><pubmed_authors>Mechtler K</pubmed_authors><pubmed_authors>Lenart P</pubmed_authors><pubmed_authors>Kraut N</pubmed_authors><pubmed_authors>Novatchkova M</pubmed_authors><pubmed_authors>Hegemann B</pubmed_authors><pubmed_authors>Sykora MM</pubmed_authors><pubmed_authors>Hutchins JR</pubmed_authors><pubmed_authors>Peters JM</pubmed_authors></additional><is_claimable>false</is_claimable><name>Systematic phosphorylation analysis of human mitotic protein complexes.</name><description>Progression through mitosis depends on a large number of protein complexes that regulate the major structural and physiological changes necessary for faithful chromosome segregation. Most, if not all, of the mitotic processes are regulated by a set of mitotic protein kinases that control protein activity by phosphorylation. Although many mitotic phosphorylation events have been identified in proteome-scale mass spectrometry studies, information on how these phosphorylation sites are distributed within mitotic protein complexes and which kinases generate these phosphorylation sites is largely lacking. We used systematic protein-affinity purification combined with mass spectrometry to identify 1818 phosphorylation sites in more than 100 mitotic protein complexes. In many complexes, the phosp</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Nov</publication><modification>2025-07-11T03:04:02.795Z</modification><creation>2025-07-11T03:04:02.795Z</creation></dates><accession>S-EPMC4206221</accession><cross_references><pubmed>22067460</pubmed><doi>10.1126/scisignal.2001993</doi></cross_references></HashMap>