Database Commons

a catalog of biological databases

e.g., animal; RNA; Methylation; China

Database information

Phospho.ELM (A database of experimentally verified phosphorylation sites in eukaryotic proteins)

General information

Description: Phospho.ELM is a database of experimentally verified phosphorylation sites in eukaryotic proteins.
Year founded: 2004
Last update: 2010-08-06
Version: v1.0
Real time : Checking...
Country/Region: Germany
Data type:
Data object:
Database category:
Major organism:

Contact information

University/Institution: European Molecular Biology Laboratory
Address: Meyerhofstraße 1, 69117 Heidelberg, Germany
City: Heidelberg
Country/Region: Germany
Contact name (PI/Team): Toby Gibson
Contact email (PI/Helpdesk):

Record metadata

Created on: 2015-06-20
Curated by:
pei wang [2018-01-27]
Shixiang Sun [2016-03-25]
Mengwei Li [2016-02-21]
Mengwei Li [2016-02-20]
Shixiang Sun [2015-11-21]
Jian SA [2015-07-01]
Shixiang Sun [2015-06-28]
Shixiang Sun [2015-06-26]


All databases:
197/4549 (95.691%)
8/185 (96.216%)
Total Rank

Community reviews

Not Rated
Data quality & quantity:
Content organization & presentation
System accessibility & reliability:

Word cloud


Phospho.ELM: a database of phosphorylation sites--update 2011. [PMID: 21062810]
Dinkel H, Chica C, Via A, Gould CM, Jensen LJ, Gibson TJ, Diella F.

The Phospho.ELM resource ( is a relational database designed to store in vivo and in vitro phosphorylation data extracted from the scientific literature and phosphoproteomic analyses. The resource has been actively developed for more than 7 years and currently comprises 42,574 serine, threonine and tyrosine non-redundant phosphorylation sites. Several new features have been implemented, such as structural disorder/order and accessibility information and a conservation score. Additionally, the conservation of the phosphosites can now be visualized directly on the multiple sequence alignment used for the score calculation. Finally, special emphasis has been put on linking to external resources such as interaction networks and other databases.

Nucleic Acids Res. 2011:39(Database issue) | 247 Citations (from Europe PMC, 2020-02-15)
Phospho.ELM: a database of phosphorylation sites--update 2008. [PMID: 17962309]
Diella F, Gould CM, Chica C, Via A, Gibson TJ.

Phospho.ELM is a manually curated database of eukaryotic phosphorylation sites. The resource includes data collected from published literature as well as high-throughput data sets. The current release of Phospho.ELM (version 7.0, July 2007) contains 4078 phospho-protein sequences covering 12 025 phospho-serine, 2362 phospho-threonine and 2083 phospho-tyrosine sites. The entries provide information about the phosphorylated proteins and the exact position of known phosphorylated instances, the kinases responsible for the modification (where known) and links to bibliographic references. The database entries have hyperlinks to easily access further information from UniProt, PubMed, SMART, ELM, MSD as well as links to the protein interaction databases MINT and STRING. A new BLAST search tool, complementary to retrieval by keyword and UniProt accession number, allows users to submit a protein query (by sequence or UniProt accession) to search against the curated data set of phosphorylated peptides. Phospho.ELM is available on line at:

Nucleic Acids Res. 2008:36(Database issue) | 147 Citations (from Europe PMC, 2020-02-08)
Phospho.ELM: a database of experimentally verified phosphorylation sites in eukaryotic proteins. [PMID: 15212693]
Diella F, Cameron S, Gemünd C, Linding R, Via A, Kuster B, Sicheritz-Pontén T, Blom N, Gibson TJ.

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. Phospho.ELM 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. 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.

BMC Bioinformatics. 2004:5() | 195 Citations (from Europe PMC, 2020-02-15)