Database Commons
Database Commons

a catalog of worldwide biological databases

Database Profile

PlantsP

General information

URL: http://plantsp.sdsc.edu
Full name: PlantsP
Description: Here, we describe the identification of more than 300 phosphorylation sites from Arabidopsis thaliana plasma membrane proteins.We present an analysis of the characteristics of phosphorylation sites, their conservation among orthologs and paralogs, and the existence of putative motifs surrounding the sites. These analyses yield general principles for predicting other phosphorylation sites in plants and provide indications of specificity determinants for responsible kinases.All data are deposited in a new searchable database for plant phosphorylation sites maintained by PlantsP (http://plantsp.sdsc.edu)
Year founded: 2001
Last update: 2011
Version:
Accessibility:
Accessible
Country/Region: United Kingdom

Classification & Tag

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Contact information

University/Institution: Sainsbury Laboratory, John Ines Centre
Address:
City:
Province/State:
Country/Region: United Kingdom
Contact name (PI/Team): Scott C. Peck
Contact email (PI/Helpdesk): scott.peck@sainsbury-laboratory.ac.uk

Publications

15308754
Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database. [PMID: 15308754]
Nühse TS, Stensballe A, Jensen ON, Peck SC.

Functional genomic technologies are generating vast amounts of data describing the presence of transcripts or proteins in plant cells. Together with classical genetics, these approaches broaden our understanding of the gene products required for specific responses. Looking to the future, the focus of research must shift to the dynamic aspects of biology: molecular mechanisms of function and regulation. Phosphorylation is a key regulatory factor in all aspects of plant biology; but it is difficult, if not impossible, for most researchers to identify in vivo phosphorylation sites within their proteins of interest. We have developed a large-scale strategy for the isolation of phosphopeptides and identification by mass spectrometry (Nühse et al., 2003b). Here, we describe the identification of more than 300 phosphorylation sites from Arabidopsis thaliana plasma membrane proteins. These data will be a valuable resource for many fields of plant biology and overcome a major impediment to the elucidation of signal transduction pathways. We present an analysis of the characteristics of phosphorylation sites, their conservation among orthologs and paralogs, and the existence of putative motifs surrounding the sites. These analyses yield general principles for predicting other phosphorylation sites in plants and provide indications of specificity determinants for responsible kinases. In addition, more than 50 sites were mapped on receptor-like kinases and revealed an unexpected complexity of regulation. Finally, the data also provide empirical evidence on the topology of transmembrane proteins. This information indicates that prediction programs incorrectly identified the cytosolic portion of the protein in 25% of the transmembrane proteins found in this study. All data are deposited in a new searchable database for plant phosphorylation sites maintained by PlantsP (http://plantsp.sdsc.edu) that will be updated as the project expands to encompass additional tissues and organelles.

Plant Cell. 2004:16(9) | 311 Citations (from Europe PMC, 2025-04-19)
11125063
PlantsP: a functional genomics database for plant phosphorylation. [PMID: 11125063]
Gribskov M, Fana F, Harper J, Hope DA, Harmon AC, Smith DW, Tax FE, Zhang G.

The PlantsP database is a curated database that combines information derived from sequences with experimental functional genomics information. PlantsP focuses on plant protein kinases and protein phosphatases. The database will specifically provide a resource for information on a collection of T-DNA insertion mutants (knockouts) in each protein kinase and phosphatase in Arabidopsis thaliana. PlantsP also provides a curated view of each protein that includes a comprehensive annotation of functionally related sequence motifs, sequence family definitions, alignments and phylogenetic trees, and descriptive information drawn directly from the literature. PlantsP is available at http://PlantsP.sdsc.edu.

Nucleic Acids Res. 2001:29(1) | 41 Citations (from Europe PMC, 2025-04-19)

Ranking

All databases:
776/6278 (87.655%)
Modification:
47/300 (84.667%)
776
Total Rank
325
Citations
14.13
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Record metadata

Created on: 2018-02-10
Curated by:
huma shireen [2018-09-03]
Hao Zhang [2018-03-03]