The mitochondrion is a key organelle of eukaryotic cell that provides the energy for cellular activities. Correctly identifying submitochondria locations of proteins can provide plentiful information for understanding their functions. However, using web-experimental methods to recognize submitochondria locations of proteins are time-consuming and costly. Thus, it is highly desired to develop a bioinformatics method to predict the submitochondria locations of mitochondrion proteins. In this work, a novel method based on support vector machine was developed to predict the submitochondria locations of mitochondrion proteins by using over-represented tetrapeptides selected by using binomial distribution. A reliable and rigorous benchmark dataset including 495 mitochondrion proteins with sequence identity ≤25% was constructed for testing and evaluating the proposed model. Jackknife cross-validated results showed that the 91.1% of the 495 mitochondrion proteins can be correctly predicted. Subsequently, our model was estimated by three existing benchmark datasets. The overall accuracies are 94.0, 94.7 and 93.4%, respectively, suggesting that the proposed model is potentially useful in the realm of mitochondrion proteome research. Based on this model, we built a predictor called TetraMito which is freely available at http://lin.uestc.edu.cn/server/TetraMito.
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http://dx.doi.org/10.1007/s10441-013-9181-9 | DOI Listing |
Iran J Biotechnol
August 2018
Department of Computer Engineering, Science and Research branch, Islamic Azad University, Tehran, Iran.
Background: Prediction of the protein localization is among the most important issues in the bioinformatics that is used for the prediction of the proteins in the cells and organelles such as mitochondria. In this study, several machine learning algorithms are applied for the prediction of the intracellular protein locations. These algorithms use the features extracted from protein sequences.
View Article and Find Full Text PDFActa Biotheor
June 2013
Key Laboratory for NeuroInformation of Ministry of Education, Center of Bioinformatics, School of Life Science and Technology, University of Electronic Science and Technology of China, Chengdu, China.
The mitochondrion is a key organelle of eukaryotic cell that provides the energy for cellular activities. Correctly identifying submitochondria locations of proteins can provide plentiful information for understanding their functions. However, using web-experimental methods to recognize submitochondria locations of proteins are time-consuming and costly.
View Article and Find Full Text PDFJ Theor Biol
October 2012
Software College, Shenyang Normal University, Shenyang, China.
Recent years have witnessed much progress in computational modeling for protein subcellular localization. However, there are far few computational models for predicting plant protein subcellular multi-localization. In this paper, we propose a multi-label multi-kernel transfer learning model for predicting multiple subcellular locations of plant proteins (MLMK-TLM).
View Article and Find Full Text PDFPLoS One
December 2012
Software College, Shenyang Normal University, Shenyang, China.
Recent years have witnessed much progress in computational modelling for protein subcellular localization. However, the existing sequence-based predictive models demonstrate moderate or unsatisfactory performance, and the gene ontology (GO) based models may take the risk of performance overestimation for novel proteins. Furthermore, many human proteins have multiple subcellular locations, which renders the computational modelling more complicated.
View Article and Find Full Text PDFAmino Acids
August 2012
Department of Physics, School of Physical Science and Technology, Inner Mongolia University, Hohhot 010021, China.
Knowledge of the submitochondria location of protein is integral to understanding its function and a necessity in the proteomics era. In this work, a new submitochondria data set is constructed, and an approach for predicting protein submitochondria locations is proposed by combining the amino acid composition, dipeptide composition, reduced physicochemical properties, gene ontology, evolutionary information, and pseudo-average chemical shift. The overall prediction accuracy is 93.
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