{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hegemann B"],"funding":["Austrian Science Fund FWF","NIEHS NIH HHS","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["rs12"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4206221"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["4(198)"],"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"],"journal":["Science signaling"],"pubmed_title":["Systematic phosphorylation analysis of human mitotic protein complexes."],"pmcid":["PMC4206221"],"funding_grant_id":["CA-112967","P50 GM068762","GM-60594","R01 GM060594","GM-68762","ES-015339","U54 CA112967","F 3407","R01 ES015339"],"pubmed_authors":["Hudecz O","Mazanek M","Heriche JK","Rameseder J","Hyman AA","Yaffe MB","Poser I","Liu S","Mechtler K","Lenart P","Kraut N","Novatchkova M","Hegemann B","Sykora MM","Hutchins JR","Peters JM"],"additional_accession":[]},"is_claimable":false,"name":"Systematic phosphorylation analysis of human mitotic protein complexes.","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","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Nov","modification":"2025-07-11T03:04:02.795Z","creation":"2025-07-11T03:04:02.795Z"},"accession":"S-EPMC4206221","cross_references":{"pubmed":["22067460"],"doi":["10.1126/scisignal.2001993"]}}