RF-Phos: Random Forest based Predictor for Protein Phosphorylation Sites

Protein phosphorylation, mediated by protein kinases, is the most common posttranslational modification in eukaryotes. Phosphorylation can impact the biological function of a given cellular protein by modulating parameters such as enzymatic activity, protein-protein interactions, subcellular localization and protein stability. In eukaryotes, phosphorylation typically occurs on three amino acids, namely serine, threonine and tyrosine. RF-Phos is a general computational phosphosite predictor that annotates putative phosphorylation sites in a protein given only the primary amino acid sequence of the protein as an input.
Query sequence

Enter a single valid protein sequence in fasta format(click to paste example sequence)

Select residues

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Supporting publications

  1. Ismail, H., Jones, A., Kim, J.H., Newman R.H., KC D.B. "Phosphorylation sites prediction using Random Forest", ICCABS, 2015, 2015 IEEE 5th International Conference on Computational Advances in Bio and Medical Sciences (ICCABS), 2015 IEEE 5th International Conference on Computational Advances in Bio and Medical Sciences (ICCABS) 2015, pp. 1-6, doi:10.1109/ICCABS.2015.7344726
  2. Ismail, H., Jones, A., Kim, J.H., Newman R.H., KC D.B. "RF-Phos: Random forest-based prediction of phosphorylation sites," in Bioinformatics and Biomedicine (BIBM), 2015 IEEE International Conference on , vol., no., pp.135-140, 9-12 Nov. 2015 doi: 10.1109/BIBM.2015.7359670 URL: URL: http://ieeexplore.ieee.org/stamp/stamp.jsp?tp=&arnumber=7359670&isnumber=7359638

Contact: hdismail@ncat.edu -- Copyright © 2015 KC Lab