Phospho.ELM: a database of phosphorylation sites update 2008
Open Access
- 23 December 2007
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 36 (Databae) , D240-D244
- https://doi.org/10.1093/nar/gkm772
Abstract
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: http://phospho.elm.eu.org.Keywords
This publication has 26 references indexed in Scilit:
- Systematic Discovery of In Vivo Phosphorylation NetworksCell, 2007
- Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling NetworksCell, 2006
- Phosphoproteome analysis of the human mitotic spindleProceedings of the National Academy of Sciences, 2006
- Kinomics: methods for deciphering the kinomeNature Methods, 2004
- Multiplexed Protein Quantitation in Saccharomyces cerevisiae Using Amine-reactive Isobaric Tagging ReagentsMolecular & Cellular Proteomics, 2004
- Large-scale characterization of HeLa cell nuclear phosphoproteinsProceedings of the National Academy of Sciences, 2004
- Robust Phosphoproteomic Profiling of Tyrosine Phosphorylation Sites from Human T Cells Using Immobilized Metal Affinity Chromatography and Tandem Mass SpectrometryAnalytical Chemistry, 2004
- Stable Isotope Labeling by Amino Acids in Cell Culture, SILAC, as a Simple and Accurate Approach to Expression ProteomicsMolecular & Cellular Proteomics, 2002
- Signaling—2000 and BeyondCell, 2000
- Quantitative analysis of complex protein mixtures using isotope-coded affinity tagsNature Biotechnology, 1999