Literature DB >> 26432000

Prediction of sumoylation sites in proteins using linear discriminant analysis.

Yan Xu1, Ya-Xin Ding1, Nai-Yang Deng2, Li-Ming Liu3.   

Abstract

Sumoylation is a multifunctional post-translation modification (PTM) in proteins by the small ubiquitin-related modifiers (SUMOs), which have relations to ubiquitin in molecular structure. Sumoylation has been found to be involved in some cellular processes. It is very significant to identify the exact sumoylation sites in proteins for not only basic researches but also drug developments. Comparing with time exhausting experiment methods, it is highly desired to develop computational methods for prediction of sumoylation sites as a complement to experiment in the post-genomic age. In this work, three feature constructions (AAIndex, position-specific amino acid propensity and modification of composition of k-space amino acid pairs) and five different combinations of them were used to construct features. At last, 178 features were selected as the optimal features according to the Mathew's correlation coefficient values in 10-fold cross validation based on linear discriminant analysis. In 10-fold cross-validation on the benchmark dataset, the accuracy and Mathew's correlation coefficient were 86.92% and 0.6845. Comparing with those existing predictors, SUMO_LDA showed its better performance.
Copyright © 2015. Published by Elsevier B.V.

Keywords:  F-score; Post-translational modification; Pseudo amino acid

Mesh:

Substances:

Year:  2015        PMID: 26432000     DOI: 10.1016/j.gene.2015.09.072

Source DB:  PubMed          Journal:  Gene        ISSN: 0378-1119            Impact factor:   3.688


  1 in total

1.  Identifying Acetylation Protein by Fusing Its PseAAC and Functional Domain Annotation.

Authors:  Wang-Ren Qiu; Ao Xu; Zhao-Chun Xu; Chun-Hua Zhang; Xuan Xiao
Journal:  Front Bioeng Biotechnol       Date:  2019-12-06
  1 in total

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