Phospho.ELM

a database of experimentally verified phosphorylation sites in eukaryotic proteins

Francesca Diella, Scott Cameron, Christine Gemünd, Rune Linding, Allegra Via, Bernhard Kuster, Thomas Sicheritz-Pontén, Nikolaj Blom, Toby J. Gibson

    Research output: Contribution to journalArticle

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    Abstract

    BACKGROUND: Post-translational phosphorylation is one of the most common protein modifications. Phosphoserine, threonine and tyrosine residues play critical roles in the regulation of many cellular processes. The fast growing number of research reports on protein phosphorylation points to a general need for an accurate database dedicated to phosphorylation to provide easily retrievable information on phosphoproteins.

    DESCRIPTION: Phospho.ELM http://phospho.elm.eu.org is a new resource containing experimentally verified phosphorylation sites manually curated from the literature and is developed as part of the ELM (Eukaryotic Linear Motif) resource. Phospho.ELM constitutes the largest searchable collection of phosphorylation sites available to the research community. The Phospho.ELM entries store information about substrate proteins with the exact positions of residues known to be phosphorylated by cellular kinases. Additional annotation includes literature references, subcellular compartment, tissue distribution, and information about the signaling pathways involved as well as links to the molecular interaction database MINT. Phospho.ELM version 2.0 contains 1703 phosphorylation site instances for 556 phosphorylated proteins.

    CONCLUSION: Phospho.ELM will be a valuable tool both for molecular biologists working on protein phosphorylation sites and for bioinformaticians developing computational predictions on the specificity of phosphorylation reactions.

    Original languageEnglish
    Article number79
    Number of pages5
    JournalBMC Bioinformatics
    Volume5
    DOIs
    Publication statusPublished - 22 Jun 2004

    Fingerprint

    Phosphorylation
    Databases
    Proteins
    Protein
    Protein Phosphorylation
    Resources
    Signaling Pathways
    Chemical Databases
    Phosphoserine
    Specificity
    Annotation
    Molecular interactions
    Phosphoproteins
    Tissue Distribution
    Threonine
    Substrate
    Tyrosine
    Phosphotransferases
    Prediction
    Tissue

    Cite this

    Diella, Francesca ; Cameron, Scott ; Gemünd, Christine ; Linding, Rune ; Via, Allegra ; Kuster, Bernhard ; Sicheritz-Pontén, Thomas ; Blom, Nikolaj ; Gibson, Toby J. / Phospho.ELM : a database of experimentally verified phosphorylation sites in eukaryotic proteins. In: BMC Bioinformatics. 2004 ; Vol. 5.
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    abstract = "BACKGROUND: Post-translational phosphorylation is one of the most common protein modifications. Phosphoserine, threonine and tyrosine residues play critical roles in the regulation of many cellular processes. The fast growing number of research reports on protein phosphorylation points to a general need for an accurate database dedicated to phosphorylation to provide easily retrievable information on phosphoproteins.DESCRIPTION: Phospho.ELM http://phospho.elm.eu.org is a new resource containing experimentally verified phosphorylation sites manually curated from the literature and is developed as part of the ELM (Eukaryotic Linear Motif) resource. Phospho.ELM constitutes the largest searchable collection of phosphorylation sites available to the research community. The Phospho.ELM entries store information about substrate proteins with the exact positions of residues known to be phosphorylated by cellular kinases. Additional annotation includes literature references, subcellular compartment, tissue distribution, and information about the signaling pathways involved as well as links to the molecular interaction database MINT. Phospho.ELM version 2.0 contains 1703 phosphorylation site instances for 556 phosphorylated proteins.CONCLUSION: Phospho.ELM will be a valuable tool both for molecular biologists working on protein phosphorylation sites and for bioinformaticians developing computational predictions on the specificity of phosphorylation reactions.",
    author = "Francesca Diella and Scott Cameron and Christine Gem{\"u}nd and Rune Linding and Allegra Via and Bernhard Kuster and Thomas Sicheritz-Pont{\'e}n and Nikolaj Blom and Gibson, {Toby J.}",
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    Diella, F, Cameron, S, Gemünd, C, Linding, R, Via, A, Kuster, B, Sicheritz-Pontén, T, Blom, N & Gibson, TJ 2004, 'Phospho.ELM: a database of experimentally verified phosphorylation sites in eukaryotic proteins', BMC Bioinformatics, vol. 5, 79. https://doi.org/10.1186/1471-2105-5-79

    Phospho.ELM : a database of experimentally verified phosphorylation sites in eukaryotic proteins. / Diella, Francesca; Cameron, Scott; Gemünd, Christine; Linding, Rune; Via, Allegra; Kuster, Bernhard; Sicheritz-Pontén, Thomas; Blom, Nikolaj; Gibson, Toby J.

    In: BMC Bioinformatics, Vol. 5, 79, 22.06.2004.

    Research output: Contribution to journalArticle

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    T2 - a database of experimentally verified phosphorylation sites in eukaryotic proteins

    AU - Diella, Francesca

    AU - Cameron, Scott

    AU - Gemünd, Christine

    AU - Linding, Rune

    AU - Via, Allegra

    AU - Kuster, Bernhard

    AU - Sicheritz-Pontén, Thomas

    AU - Blom, Nikolaj

    AU - Gibson, Toby J.

    PY - 2004/6/22

    Y1 - 2004/6/22

    N2 - BACKGROUND: Post-translational phosphorylation is one of the most common protein modifications. Phosphoserine, threonine and tyrosine residues play critical roles in the regulation of many cellular processes. The fast growing number of research reports on protein phosphorylation points to a general need for an accurate database dedicated to phosphorylation to provide easily retrievable information on phosphoproteins.DESCRIPTION: Phospho.ELM http://phospho.elm.eu.org is a new resource containing experimentally verified phosphorylation sites manually curated from the literature and is developed as part of the ELM (Eukaryotic Linear Motif) resource. Phospho.ELM constitutes the largest searchable collection of phosphorylation sites available to the research community. The Phospho.ELM entries store information about substrate proteins with the exact positions of residues known to be phosphorylated by cellular kinases. Additional annotation includes literature references, subcellular compartment, tissue distribution, and information about the signaling pathways involved as well as links to the molecular interaction database MINT. Phospho.ELM version 2.0 contains 1703 phosphorylation site instances for 556 phosphorylated proteins.CONCLUSION: Phospho.ELM will be a valuable tool both for molecular biologists working on protein phosphorylation sites and for bioinformaticians developing computational predictions on the specificity of phosphorylation reactions.

    AB - BACKGROUND: Post-translational phosphorylation is one of the most common protein modifications. Phosphoserine, threonine and tyrosine residues play critical roles in the regulation of many cellular processes. The fast growing number of research reports on protein phosphorylation points to a general need for an accurate database dedicated to phosphorylation to provide easily retrievable information on phosphoproteins.DESCRIPTION: Phospho.ELM http://phospho.elm.eu.org is a new resource containing experimentally verified phosphorylation sites manually curated from the literature and is developed as part of the ELM (Eukaryotic Linear Motif) resource. Phospho.ELM constitutes the largest searchable collection of phosphorylation sites available to the research community. The Phospho.ELM entries store information about substrate proteins with the exact positions of residues known to be phosphorylated by cellular kinases. Additional annotation includes literature references, subcellular compartment, tissue distribution, and information about the signaling pathways involved as well as links to the molecular interaction database MINT. Phospho.ELM version 2.0 contains 1703 phosphorylation site instances for 556 phosphorylated proteins.CONCLUSION: Phospho.ELM will be a valuable tool both for molecular biologists working on protein phosphorylation sites and for bioinformaticians developing computational predictions on the specificity of phosphorylation reactions.

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