PHOSIDA: Difference between revisions

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==Technology {{HelpIcon|Help:Databases}}==
==Technology {{HelpIcon|Help:Databases}}==
===Web Services/API===
===Web Services/API===
The underlying database of PHOSIDA is based on mySQL. In addition, we used C#/ASP.NET to generate the dynamic web application.


==Discussion {{HelpIcon|Help:Databases}}==
==Discussion {{HelpIcon|Help:Databases}}==

Revision as of 20:38, 17 March 2008

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Link/URL:

http://www.phosida.de/

What:

Phosida - Phosphorylation Site Database

Who:

Florian Gnad and Matthias Mann

Updates:

Genome Annotation Section

Upcoming events:

Inclusion of additional phosphoproteomes of various organisms

Web Services:
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See Help:Database_table for how to add or edit information in this section of EcoliWiki.

About PHOSIDA

Add general information here

PHOSIDA, the phosphorylation site database, integrates thousands of high-confidence in-vivo phosphosites identified by mass spectrometry-based proteomics in various species. It includes phosphoproteomes of organisms, which cover the entire phylogenetic tree representatively, ranging from bacteria such as Escherichia coli and Bacillus subtilis to eukaryotes such as yeast and human. It contains 81 phosphorylation sites on 79 E.coli proteins, for example.
E.coli results are described in Macek and Gnad et al.[1].

Content

PHOSIDA contains phosphoproteomes of the following prokaryotes:

Escherichia coli (79 phosphoproteins, 81 phosphosites)

Bacillus subtilis (78 phosphoproteins, 78 phosphosites)

edit table


Using PHOSIDA

Browsing

The web user is able to search for any protein of interest within a specified organism. In the case of human, it is possible to search via IPI accession number, Swissprot identifier, gene symbol, protein name, peptide sequence, protein sequence or any substring that matches with the description of a given protein, for example.

Searching

For each protein, the user is presented with general features such as isoelectric point (pI), molecular weight, sequence, and description at the protein level in addition to corresponding GO accession numbers, which are directly hyperlinked to the detailed description of the annotation at the Gene Ontology website. In addition, a hyperlink to the Reactome database is provided, if the specified protein is annotated in Reactome (www.reactome.org).


Furthermore, annotated protein features such as active sites, binding sites, domains, and signal sequences are derived from the Swissprot database and illustrated for eukaryotic phosphoproteins, when clicking the ‘motifs/domains’ button. In the case of human, protein assignments were based on the IPI database, which is cross-referenced with the Swissprot database by PHOSIDA. Entries of both databases that correspond to the same proteins were aligned to derive the exact positions of these protein features. Already annotated phosphosites derived from Swissprot are transferred to the IPI sequences in the same way and listed when clicking the ‘sites (other sources)’ button. The aligned regions can be visualized via ‘check alignment’ buttons. Furthermore, corresponding literature is also provided.


Moreover, all phosphorylated sites that have been identified in our laboratory are displayed on the left panel. This presentment allows to check immediately whether phosphorylation sites occur within known domains or signaling sequence regions. Additionally, it becomes instantly clear whether a known biologically functional site such as binding sites is phosphorylated. In such cases, one can link the phosphorylation event to its functional impact. If the localization probability is lower than 0.995, it is enclosed in round brackets. When users click on any of the displayed phosphosites, the surrounding sequence and matching kinase motifs are shown.
Often, several phosphopeptides covering the same phosphosite are measured by mass spectrometry. These peptides are also listed along with their localization probabilities, Mascot scores, and MSQuant/PTM scores for each instance. In many cases, for example, the growth factor treatment, PHOSIDA contains quantitative and time-resolved data for the relative abundance of each phosphopeptide. These data are listed separately for peptides as a function of their sequences, degrees of phosphorylation, and further categories, such as experimental design or fraction. When moving the mouse over the ‘occurences’ button, protein entries sharing the same phosphopeptide of interest are listed along with the number of unique peptides that have been measured in one experimental assay. Each peptide is color coded according to the protein assignment: if the peptide sequence is marked in green, the selected protein has the maximum number of peptides in comparison to all other proteins that contain the same peptide. If the protein assignment is ambiguous because of another protein with the same number of identified peptides, the peptide is highlighted in blue. Red indicates that other proteins exceed the number of detected peptides in comparison to the selected phosphoprotein. Each feature of PHOSIDA is explained in the help menu, which is accessible via the ‘background’ menu or via clicking on the ‘question mark’ button at the page of interest.


Usage examples

Add links to additional pages describing success stories here.

Other sites with related content

Technology

Web Services/API

The underlying database of PHOSIDA is based on mySQL. In addition, we used C#/ASP.NET to generate the dynamic web application.

Discussion

References

  1. ↑ Macek, B et al. (2008) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol. Cell Proteomics 7 299-307 PubMed

External Links

PHOSIDA (Phosphorylation Site Database): http://www.phosida.com
MAPU (Max-Planck Unified Proteome Database): http://www.mapuproteome.com


Discussion of PHOSIDA on other websites