TY - JOUR
T1 - RF-Phos: A Novel General Phosphorylation Site Prediction Tool Based on Random Forest
AU - Ismail, Hamid D
AU - Jones, Ahoi
AU - Kim, Jung H.
AU - Newman, Robert H
AU - Kc, Dukka B.
PY - 2016/1/1
Y1 - 2016/1/1
N2 - Protein phosphorylation is one of the most widespread regulatory mechanisms in eukaryotes. Over the past decade, phosphorylation site prediction has emerged as an important problem in the field of bioinformatics. Here, we report a new method, termed Random Forest-based Phosphosite predictor 2.0 (RF-Phos 2.0), to predict phosphorylation sites given only the primary amino acid sequence of a protein as input. RF-Phos 2.0, which uses random forest with sequence and structural features, is able to identify putative sites of phosphorylation across many protein families. In side-by-side comparisons based on 10-fold cross validation and an independent dataset, RF-Phos 2.0 compares favorably to other popular mammalian phosphosite prediction methods, such as PhosphoSVM, GPS2.1, and Musite.
AB - Protein phosphorylation is one of the most widespread regulatory mechanisms in eukaryotes. Over the past decade, phosphorylation site prediction has emerged as an important problem in the field of bioinformatics. Here, we report a new method, termed Random Forest-based Phosphosite predictor 2.0 (RF-Phos 2.0), to predict phosphorylation sites given only the primary amino acid sequence of a protein as input. RF-Phos 2.0, which uses random forest with sequence and structural features, is able to identify putative sites of phosphorylation across many protein families. In side-by-side comparisons based on 10-fold cross validation and an independent dataset, RF-Phos 2.0 compares favorably to other popular mammalian phosphosite prediction methods, such as PhosphoSVM, GPS2.1, and Musite.
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U2 - 10.1155/2016/3281590
DO - 10.1155/2016/3281590
M3 - Article
C2 - 27066500
SN - 2314-6133
VL - 2016
JO - BioMed Research International
JF - BioMed Research International
IS - Special Issue
M1 - 3281590
ER -