Additional information about the substrate protein, which contains the phosphorylation site, pattern of expression, interaction partners and interaction network(s) (where available).
Link to UniPROT/Ensembl entry.
- Interaction Network(s)
Links to STRING to allow retrieval of interacting genes/proteins and\or NetworKIN to allow the user to browse/search which kinase families are predicted to phosphorylate experimentally identified phosphorylation sites in vivo.
- External Source(s)
Links to PHOSIDA
- MINT Interaction(s)
Links to the Molecular INTeractions database for the interaction partners of the substrate.
- GO Terms
Gene Ontology Terms (cellular component, molecular function, biological process) annotated for the particular sequence.
Phosphorylated residue (S/T/Y)
Position of the S/T/Y phosphorylation site within the UniPROT/TrEMBL sequence. (NB. position may differ from that given in literature due to differences in sequence entry).
Amino acid sequence of region flanking the modified residue (+/- 10 amino acids).
List of kinases which modify the given residue.
Link to PubMed entry(s) for publications reporting the evidence from which the data was collected. (NB. Site position quoted in literature may differ from that given in Phospho.ELM due to differences in sequence entry and annotation).
High Throughput Data (HTP); Low Throughput Data (LTP)
The Conservation Score quantifies the conservation of each phospho-site. Values range between 0 and 1, where 1 indicates highest conservation.
Link to ELM server entry for the given phosphorylation and/or binding motif.
- Binding Domain
The phosphorylation of the given residue creates a binding motif for a domain involved in signaling (e.g. SH2, 14-3-3, PTB).
Note of any SMART domain predictions in which the phosphorylation instance resides.
- IUPRED score
Prediction of protein disorder by IUPRED. Score ranges from 0 to 1; a score above 0.5 is considered as disordered.
Link to a macromolecular structure database PDBe entry containing a relevant structure covering the phosphorylated site.
- P3D Acc.
Surface accessibility score calculated by Phospho3D - a database of three-dimensional structures of protein phosphorylation sites. A link to the Phospho3D entry is provided for each calculated value. The accessibility data should always be interpreted in the context of the structure!
The PhosphoELM database can also be accessed via URL as follows:
- by substrate name:
- by Uniprot ID:
- by Uniprot IDand Position
- by ENSEMBL IDand multiple Positions
- by Uniprot name:
- by Kinase:
- by Binding domain:
- retrieve a stored Sequence:
- retrieve data as CSV
- retrieve data for a single positionas CSV
- retrieve data for multipleIDs as CSV
- using web-services: