ArticleFrontiers in plant science2012
P(3)DB: An Integrated Database for Plant Protein Phosphorylation.
Article in Frontiers in plant science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Multimodal knowledge expansion widget powered by plant protein phosphorylation database and ChatGPT.Frontiers in bioinformatics · 2025Article
- Protein phosphorylation regulation of key genes in oral squamous cell carcinoma and their role in the immune microenvironment.Frontiers in immunology · 2025Article
- Deep Learning in Phosphoproteomics: Methods and Application in Cancer Drug Discovery.Proteomes · 2023Review
- Dynamics of Protein Phosphorylation duringInternational journal of molecular sciences · 2022Article
- Regulation of PaRBOH1-mediated ROS production in Norway spruce by CaFrontiers in plant science · 2022Article
- Novel Translational and Phosphorylation Modification Regulation Mechanisms of Tomato (International journal of molecular sciences · 2021Article
- Comparative phosphoproteomic analysis of BR-defective mutant reveals a key role of GhSK13 in regulating cotton fiber development.Science China. Life sciences · 2020Article
- Global Quantitative Proteomics Studies Revealed Tissue-Preferential Expression and Phosphorylation of Regulatory Proteins inInternational journal of molecular sciences · 2020Article
- Bioinformatics Resources for Plant Abiotic Stress Responses: State of the Art and Opportunities in the Fast Evolving -Omics Era.Plants (Basel, Switzerland) · 2020Review
- Article
- Genome-wide identification, structural and gene expression analysis of the bZIP transcription factor family in sweet potato wild relative Ipomoea trifida.BMC genetics · 2019Article
- Global Phosphoproteomic Analysis Reveals the Defense and Response Mechanisms ofInternational journal of molecular sciences · 2019Article
- G protein subunit phosphorylation as a regulatory mechanism in heterotrimeric G protein signaling in mammals, yeast, and plants.The Biochemical journal · 2018Review
- Evidence that thePlant biotechnology (Tokyo, Japan) · 2018Article
- Structural disorder in plant proteins: where plasticity meets sessility.Cellular and molecular life sciences : CMLS · 2017Review
- The Kinase Activity of Calcineurin B-like Interacting Protein Kinase 26 (CIPK26) Influences Its Own Stability and that of the ABA-regulated Ubiquitin Ligase, Keep on Going (KEG).Frontiers in plant science · 2017Article
- Dynamic Phosphoproteome Analysis of Seedling Leaves in Brachypodium distachyon L. Reveals Central Phosphorylated Proteins Involved in the Drought Stress Response.Scientific reports · 2016Article
- Quantitative phosphoproteomics reveals the role of the AMPK plant ortholog SnRK1 as a metabolic master regulator under energy deprivation.Scientific reports · 2016Article
- The global phosphoproteome of Chlamydomonas reinhardtii reveals complex organellar phosphorylation in the flagella and thylakoid membrane.Molecular & cellular proteomics : MCP · 2014Article
- Quantitative phosphoproteomic profiling of fiber differentiation and initiation in a fiberless mutant of cotton.BMC genomics · 2014Article
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5 authors.
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Abstract
Protein phosphorylation is widely recognized as the most widespread, enzyme-catalyzed post-translational modification in eukaryotes. In particular, plants have appropriated this signaling mechanism as evidenced by the twofold higher frequency of protein kinases within the genome compared to other eukaryotes. While all aspects of plant protein phosphorylation research have grown in the past 10 years; phosphorylation site mapping using high-resolution mass spectrometry has grown exponentially. In Arabidopsis alone there are thousands of experimentally determined phosphorylation sites. To archive these events in a user-intuitive format we have developed P(3)DB, the Plant Protein Phosphorylation Database (p3db.org). This database is a repository for plant protein phosphorylation site data, currently hosting information on 32,963 non-redundant sites collated from 23 experimental studies from six plant species. These data can be queried for a protein-of-interest using an integrated BLAST module to query similar sequences with known phosphorylation sites among the multiple plants currently investigated. The paper demonstrates how this resource can help identify functionally conserved phosphorylation sites in plants using a multi-system approach.
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