Dataset Information

MitoCheck (www.mitocheck.org) - Systematic phosphorylation analysis of human mitotic protein complexes

ABSTRACT: MitoCheck Mm Bub1b NB LAP CHY LC-FTICR-MSA

INSTRUMENT(S): Qtrap, FTICR

SUBMITTER: Otto Hudecz

LAB HEAD: Otto Hudecz

PROVIDER: PRD000214 | Pride | 2013-06-19

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	PRIDE_Exp_Complete_Ac_11797.pride.mgf.gz	Mgf
	PRIDE_Exp_Complete_Ac_11797.pride.mztab.gz	Mztab
	PRIDE_Exp_Complete_Ac_11797.xml.gz	Xml
	PRIDE_Exp_Complete_Ac_11798.pride.mgf.gz	Mgf
	PRIDE_Exp_Complete_Ac_11798.pride.mztab.gz	Mztab

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Publications

Systematic phosphorylation analysis of human mitotic protein complexes.

Hegemann Björn B Hutchins James R A JR Hudecz Otto O Novatchkova Maria M Rameseder Jonathan J Sykora Martina M MM Liu Sihan S Mazanek Michael M Lénárt Péter P Hériché Jean-Karim JK Poser Ina I Kraut Norbert N Hyman Anthony A AA Yaffe Michael B MB Mechtler Karl K Peters Jan-Michael JM

Science signaling 20111108 198

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 ...[more]

PMID: 22067460

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Project description:Pilotexp_IMAC_TiO2_eluate_ATM_ATR_dep_phos_15min_postIR: Proteins were isolated from 4 different conditions of Arabidopsis thaliana plants: wild type untreated, wild type irradiated, atm/atr mutant untreated, atm/atr mutant irradiated The proteins were tryptically digested and labelled each with one channel ofthe iTRAQ4plex reagent. The samples were mixed and subjected to phosphopeptide enrichment by IMAC followed by TiO2. The enriched phosphopeptides were separated by SCX and each fraction was analysed by nano-reversed phase HPLC coupled online to a LTQ Orbitrap Velos. Each peptide was fragmented both by CID (MSA) and HCD, using the iontrap-MS analyser for CID and the Orbitrap detector for HCD scans. IMAC_TiO2_eluate_ATM_ATR_dep_phos_15min_postIR: Proteins were isolated from 4 different conditions of Arabidopsis thaliana plants: wild type untreated, wild type irradiated, atm/atr mutant untreated, atm/atr mutant irradiated The proteins were tryptically digested and labelled each with one channel ofthe iTRAQ4plex reagent. The samples were mixed and subjected to phosphopeptide enrichment by IMAC followed by TiO2. The enriched phosphopeptides were separated by SCX and each fraction was analysed by nano-reversed phase HPLC coupled online to a LTQ Orbitrap Velos. Each peptide was fragmented both by CID (MSA) and HCD, using the iontrap-MS analyser for CID and the Orbitrap detector for HCD scans. IMAC_TiO2_FT_ATM_ATR_dep_phos_15min_postIR: Proteins were isolated from 4 different conditions of Arabidopsis thaliana plants: wild type untreated, wild type irradiated, atm/atr mutant untreated, atm/atr mutant irradiated The proteins were tryptically digested and labelled each with one channel ofthe iTRAQ4plex reagent. The samples were mixed and subjected to phosphopeptide enrichment by IMAC followed by TiO2. The unphosphorylated peptides found in the flowthrough of the TiO2 column were separated by SCX and each fraction was analysed by nano-reversed phase HPLC coupled online to a LTQ Orbitrap Velos. Each peptide was fragmented both by CID and HCD, using the iontrap-MS analyser for CID and the Orbitrap detector for HCD scans. The iTRAQ ratio obtained for the unmodified peptides from this flowthrough sample was used to calculate protein ratios for the 4 different conditions.