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Tissue atlas Arabidopsis - ProteomicsDB

Phosphorylation in Arabidopsis thaliana

36525 modifications in 28028 peptides, found in 18074 proteins

Experiment Details

Exp 114


Experimental Setup
TissueAtlas of 30 tissues
ConditionControl conditions
PTM EnrichmentIMAC
MS InstrumentQ Exactive HF
MS/MS Search Parameters
Protein DatabaseAraport11
Decoy StrategyReverse decoy database
FDR ThresholdFDR < 0.1%
Search Algorithm(s)MaxQuant (version 1.5.8.3)
Precursor Mass Tolerance20 ppm
PTM Site AllocationPTM Score
Identification ScoreMaxQuant score
ProteaseTrypsin
Fixed ModificationsCarbamidomethyl (C)
Variable ModificationsOxidation (M)
Phosphorylation (STY)
N-terminal acetylation (Protein N-terminus)
Other Information
CommentsSupplemental Dataset 1. We combined all phosphorylation sites for the 30 tissues in 1 experiment along with MaxQuant identification metrics. For more detailed info on relative abundance within a specific tissue please consult the original dataset.


Publication Information

Mergner et al., 2020

PubMed ID: 32188942

ProteomeXchange: PXD013868

Abstract

Nature. 2020 Mar;579(7799):409-414. doi: 10.1038/s41586-020-2094-2. Epub 2020 
Mar 11.

Mass-spectrometry-based draft of the Arabidopsis proteome.

Mergner J(1), Frejno M(1), List M(2), Papacek M(3), Chen X(4), Chaudhary A(4), 
Samaras P(1), Richter S(5), Shikata H(6)(7), Messerer M(8), Lang D(8), Altmann 
S(9), Cyprys P(10), Zolg DP(1), Mathieson T(11), Bantscheff M(11), Hazarika 
RR(12)(13), Schmidt T(1), Dawid C(14), Dunkel A(14), Hofmann T(14), Sprunck 
S(10), Falter-Braun P(9)(15), Johannes F(12)(13), Mayer KFX(8)(16), Jürgens 
G(5), Wilhelm M(1), Baumbach J(2), Grill E(3), Schneitz K(4), Schwechheimer 
C(6), Kuster B(17)(18)(19).

Author information:
(1)Chair of Proteomics and Bioanalytics, Technical University of Munich (TUM), 
Freising, Germany.
(2)Chair of Experimental Bioinformatics, Technical University of Munich (TUM), 
Freising, Germany.
(3)Chair of Botany, Technical University of Munich (TUM), Freising, Germany.
(4)Plant Developmental Biology, Technical University of Munich (TUM), Freising, 
Germany.
(5)Center for Plant Molecular Biology, University of Tübingen, Tübingen, 
Germany.
(6)Chair of Plant Systems Biology, Technical University of Munich (TUM), 
Freising, Germany.
(7)Devision of Plant Environmental Responses, National Institute for Basic 
Biology, Okazaki, Japan.
(8)Plant Genome and Systems Biology, Helmholtz Center Munich, German Research 
Center for Environmental Health, Munich-Neuherberg, Germany.
(9)Institute of Network Biology (INET), Helmholtz Center Munich, German Research 
Center for Environmental Health, Munich-Neuherberg, Germany.
(10)Cell Biology and Plant Biochemistry, University of Regensburg, Regensburg, 
Germany.
(11)Cellzome GmbH, Heidelberg, Germany.
(12)Population Epigenetics and Epigenomics, Technical University of Munich 
(TUM), Freising, Germany.
(13)Institute of Advanced Study (IAS), Technical University of Munich (TUM), 
Freising, Germany.
(14)Chair of Food Chemistry and Molecular Sensory Science, Technical University 
of Munich (TUM), Freising, Germany.
(15)Chair of Microbe-Host Interactions, Ludwigs-Maximilians-University (LMU), 
Munich, Germany.
(16)Plant Genome Biology, Technical University of Munich (TUM), Freising, 
Germany.
(17)Chair of Proteomics and Bioanalytics, Technical University of Munich (TUM), 
Freising, Germany. kuster@tum.de.
(18)Institute of Advanced Study (IAS), Technical University of Munich (TUM), 
Freising, Germany. kuster@tum.de.
(19)Bavarian Biomolecular Mass Spectrometry Center (BayBioMS), Technical 
University of Munich (TUM), Freising, Germany. kuster@tum.de.

Comment in
    Sci Data. 2020 Oct 9;7(1):334.

Plants are essential for life and are extremely diverse organisms with unique 
molecular capabilities1. Here we present a quantitative atlas of the 
transcriptomes, proteomes and phosphoproteomes of 30 tissues of the model plant 
Arabidopsis thaliana. Our analysis provides initial answers to how many genes 
exist as proteins (more than 18,000), where they are expressed, in which 
approximate quantities (a dynamic range of more than six orders of magnitude) 
and to what extent they are phosphorylated (over 43,000 sites). We present 
examples of how the data may be used, such as to discover proteins that are 
translated from short open-reading frames, to uncover sequence motifs that are 
involved in the regulation of protein production, and to identify 
tissue-specific protein complexes or phosphorylation-mediated signalling events. 
Interactive access to this resource for the plant community is provided by the 
ProteomicsDB and ATHENA databases, which include powerful bioinformatics tools 
to explore and characterize Arabidopsis proteins, their modifications and 
interactions.

DOI: 10.1038/s41586-020-2094-2
PMID: 32188942 [Indexed for MEDLINE]