• Proceedings of the Korean Information Science Society Conference
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• 2005.07b
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• pp.283-285
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• 2005

단백질들이 어느 세포내 소기관에 위치하는지에 대한 지식은 그들의 기능을 예측하는데 있어서 중요한 정보를 제공한다. 하지만 실험적으로 세포내 소기관 위치를 분석하는 작업은 않은 비용과 시간을 요구한다. 따라서 지금까지 단백질의 세포내 소기관 위치 예측을 위한 다양한 계산적 방법들이 개발되었으나, 효율적인 학습 데이터의 생성에 있어서 문제점을 가지고 있다. 본 논문은 기계학습 기법을 이용하여 주요 서열 구성을 선택함으로써 예측의 성능을 최대화 하는 방법을 제안하고자 한다. 실험은 효모의 단백질의 세포 내 소기관 위치 예측에 있어서 주요 아미노산 서열들을 선택함으로써 예측의 성능을 향상시키는 결과를 보이고 있다.

• Journal of the Korea Institute of Information and Communication Engineering
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• v.18 no.10
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• pp.2562-2570
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• 2014

One of the important hints for inferring the function of unknown proteins is the knowledge about protein subcellular localization. Recently, there are considerable researches on the prediction of subcellular localization of proteins which simultaneously exist at multiple subcellular localization. In this paper, label power-set classification is improved for the accurate prediction of multiple subcellular localization. The predicted multi-labels from the label power-set classifier are combined with their prediction probability to give the final result. To find the accurate probability estimates of multi-classes, this paper employs pair-wise comparison and error-correcting output codes frameworks. Prediction experiments on protein subcellular localization show significant performance improvement.

• Proceedings of the Korea Contents Association Conference
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• 2007.11a
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• pp.12-16
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• 2007

The function of a protein is closely co-related with its subcellular location(s). Given a protein sequence, therefore, how to determine its subcellular location is a vitally important problem. We have developed a new prediction method for protein subcellular location(s), which is based on n-gram feature extraction and k-nearest neighbor (kNN) classification algorithm. It classifies a protein sequence to one or more subcellular compartments based on the locations of top k sequences which show the highest similarity weights against the input sequence. The similarity weight is a kind of similarity measure which is determined by comparing n-gram features between two sequences. Currently our method extract penta-grams as features of protein sequences, computes scores of the potential localization site(s) using kNN algorithm, and finally presents the locations and their associated scores. We constructed a large-scale data set of protein sequences with known subcellular locations from the SWISS-PROT database. This data set contains 51,885 entries with one or more known subcellular locations. Our method show very high prediction precision of about 93% for this data set, and compared with other method, it also showed comparable prediction improvement for a test collection used in a previous work.

• Journal of the Korea Institute of Information and Communication Engineering
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• v.18 no.7
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• pp.1749-1756
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• 2014

Knowledge about protein subcellular localization provides important information about protein function. This paper improves a label power-set multi-label classification for the accurate prediction of subcellular localization of proteins which simultaneously exist at multiple subcellular locations. Among multi-label classification methods, label power-set method can effectively model the correlation between subcellular locations of proteins performing certain biological function. With constrained optimization, this paper calculates combination weights which are used in the linear combination representation of a multi-label by other multi-labels. Using these weights, the prediction probabilities of multi-labels are combined to give final prediction results. Experimental results on human protein dataset show that the proposed method achieves higher performance than other prediction methods for protein subcellular localization. This shows that the proposed method can successfully enrich the prediction probability of multi-labels by exploiting the overlapping information between multi-labels.

• Journal of KIISE:Software and Applications
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• v.37 no.11
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• pp.803-811
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• 2010

Since protein subcellular location and biological function are highly correlated, the prediction of protein subcellular localization can provide information about the function of a protein. In order to enhance the prediction performance, external information other than amino acids sequence information is actively exploited in many researches. This paper compares the prediction capabilities resided in amino acid sequence similarity, protein profile, gene ontology, motif, and textual information. In the experiments using PLOC dataset which has proteins less than 80% sequence similarity, sequence similarity information and gene ontology are effective information, achieving a classification accuracy of 94.8%. In the experiments using BaCelLo IDS dataset with low sequence similarity less than 30%, using gene ontology gives the best prediction accuracies, 93.2% for animals and 86.6% for fungi.

• Journal of the Korea Institute of Information and Communication Engineering
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• v.18 no.4
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• pp.992-999
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• 2014

This paper presents an extensive experimental comparison of a variety of multi-label learning methods for the accurate prediction of subcellular localization of proteins which simultaneously exist at multiple subcellular locations. We compared several methods from three categories of multi-label classification algorithms: algorithm adaptation, problem transformation, and meta learning. Experimental results are analyzed using 12 multi-label evaluation measures to assess the behavior of the methods from a variety of view-points. We also use a new summarization measure to find the best performing method. Experimental results show that the best performing methods are power-set method pruning a infrequently occurring subsets of labels and classifier chains modeling relevant labels with an additional feature. futhermore, ensembles of many classifiers of these methods enhance the performance further. The recommendation from this study is that the correlation of subcellular locations is an effective clue for classification, this is because the subcellular locations of proteins performing certain biological function are not independent but correlated.

• Journal of KIISE:Software and Applications
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• v.37 no.1
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• pp.74-79
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• 2010

The amino acid composition of a protein provides basic information for solving many problems in bioinformatics. We propose a new method that uses biologically relevant similarity between amino acids to determine the amino acid composition, where the BOLOSUM matrix is exploited to define a similarity measure between amino acids. Futhermore, to extract more information from a protein sequence than conventional methods for determining amino acid composition, we exploit the concepts of spectral analysis of signals such as radar and speech signals-the concepts of time-dependent analysis, time resolution, and frequency resolution. The proposed method was applied to predict subcellular localization of proteins, and showed significantly improved performance over previous methods for amino acid composition estimation.

• Journal of the Korea Society of Computer and Information
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• v.14 no.3
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• pp.193-207
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• 2009

Intracellular signal transduction is achieved by protein-protein interaction. In this paper, we suggest high performance algorithm based on Yeast protein-protein interaction and protein location information. We compare if pathways predicted with high valued weights indicate similar tendency with pathways provided in KEGG. Furthermore, we suggest extracted results, which can imply a discovery of new signaling pathways that is yet proven through experiments. This will be a good basis for research to discover new protein signaling pathways and unknown functions of established proteins.

• Journal of KIISE:Software and Applications
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• v.34 no.7
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• pp.595-602
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• 2007

This paper proposes a method that discriminates signal peptide and predicts the cleavage site of the secretory proteins cleaved by the signal peptidase I. The preprocessing stage uses hydrophobicity scales of amino acids in order to predict the presence of signal sequence and the cleavage site. The preprocessing enhances the performance of the prediction method by eliminating the non-secretory proteins in the early stage of prediction. for the effective use of support vector machine for the signal sequence prediction, the biologically relevant distance between the amino acid sequences is defined by using the hydrophobicity and substitution matrix; the hydrophobicity can be used to Predict the location of amino acid in a cell and the substitution matrix represents the evolutionary relationships of amino acids. The proposed method showed 98.9% discrimination rates from signal sequences and 88% correct rate of the cleavage site prediction on Swiss-Prot release 50 protein database using the 5-fold-cross-validation. In the comparison tests, the proposed method has performed significantly better than other prediction methods.