Abstract
A post-translational modification (PTM) named lysine formylation discovered recently is a reversible and dynamic biological process primarily found on histone proteins of the organism that plays strong roles on modulation of chromatin conformations and the process of gene activation. A large number of traditional laboratory-based experimental methods and computational methods are currently available for identifying the formylated lysine residues. But the experimental methods are more costly and time consuming than computational methods. In order to predict formylated lysine sites, the existing computational methods are not satisfactory to select reliable non-formylated sites for balancing the training samples. A useful bioinformatics model named PLF_RNS is developed in this study by using various sequence-based features with support vector machine algorithm and F-score feature selection method. For this purpose, the verified formylated lysine samples are labeled as positive and reliable negative samples that are filtered from remaining samples using evolutionary information based on BLOSUM62 matrix are labeled as negative samples. The experimental result shows that PLF_RNS has acquired an average accuracy of 95.09% on tenfold cross validation, which is better compared to other currently available models. Therefore, it may be helpful for a better understanding of those types of molecular mechanisms and the development of drugs for related diseases.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Yu B, Yu Z, Chen C et al (2020) DNNAce: prediction of prokaryote lysine acetylation sites through deep neural networks with multi-information fusion. Chemom Intell Lab Syst 200(5):103999–104014. https://doi.org/10.1016/j.chemolab.2020.103999
Ning Q, Ma Z, Zhao X (2019) dForml(KNN)-PseAAC: detecting formylation sites from protein sequences using K-nearest neighbor algorithm via Chou’s 5-step rule and pseudo components. J Theor Bio 470(7):43–49. https://doi.org/10.1016/j.jtbi.2019.03.011
Ju Z, Wang S (2020) Prediction of lysine formylation sites using the composition of k-spaced amino acid pairs via Chou’s 5-steps rule and general pseudo components. Genomics 112(1):859–866. https://doi.org/10.1016/j.ygeno.2019.05.027
Jia C, Zhang M, Fan C et al (2019) Formator: predicting lysine formylation sites based on the most distant undersampling and safe-level synthetic minority oversampling. IEEE/ACM Trans Computat Biol Bioinf. https://doi.org/10.1109/tcbb.2019.2957758
Jiang T, Zhou X, Taghizadeh K et al (2006) N-formylation of lysine in histone proteins as a secondary modification arising from oxidative DNA damage. Proc Nat Acad Sci 104(1):60–65. https://doi.org/10.1073/pnas.0606775103
Machida Y, Chiba T, Takayanagi A et al (2005) Common anti-apoptotic roles of parkin and α-synuclein in human dopaminergic cells. Biochem Biophys Res Commun 332(1):233–240. https://doi.org/10.1016/j.bbrc.2005.04.124
Sohrawordi M, Hasan M (2020) LyFor: prediction of lysine formylation sites from sequence based features using support vector machine. 2020 IEEE Region 10 Symp (TENSYMP), 250–253. https://doi.org/10.1109/tensymp50017.2020.9230689
Blagus R, Lusa L (2013) SMOTE for high-dimensional class-imbalanced data. BMC Bioinf. https://doi.org/10.1186/1471-2105-14-106
Xu H, Zhou J, Lin S et al (2017) PLMD: an updated data resource of protein lysine modifications. J Genet Genomics 44(5):243–250. https://doi.org/10.1016/j.jgg.2017.03.007
Bairoch A, Apweiler R, Wu CH et al (2009) The universal protein resource (UniProt) in 2010. Nucleic Acids Res 38(1):D138–D142. https://doi.org/10.1093/nar/gkp846
Huang K, Lee T, Kao H et al (2018) dbPTM in 2019: exploring disease association and cross-talk of post-translational modifications. Nucleic Acids Res 47(D1):D298–D308. https://doi.org/10.1093/nar/gky1074
Fu L, Niu B, Zhu Z et al (2012) CD-HIT: accelerated for clustering the next-generation sequencing data. Bioinformatics 28(23):3150–3152. https://doi.org/10.1093/bioinformatics/bts565
Zhang L, Dong B, Teng Z et al (2020) Identification of human enzymes using amino acid composition and the composition of k-spaced amino acid pairs. BioMed Res Int 1–11. https://doi.org/10.1155/2020/9235920
Li S, Yu K, Wu G et al (2021) Pcysmod: prediction of multiple cysteine modifications based on deep learning framework. Front Cell Dev Biol. https://doi.org/10.3389/fcell.2021.617366
Ning Q, Zhao X, Bao L et al (2018) Detecting succinylation sites from protein sequences using ensemble support vector machine. BMC Bioinf 19(1):237–235. https://doi.org/10.1186/s12859-018-2249-4
Liu Y, Yu Z, Chen C et al (2020) Prediction of protein crotonylation sites through LightGBM classifier based on SMOTE and elastic net. Anal Biochem 609:113903–113910. https://doi.org/10.1016/j.ab.2020.113903
Gupta S, Mittal P, Madhu M, Sharma VK (2017) IL17eScan: a tool for the identification of peptides inducing IL-17 response. Front Immunol. https://doi.org/10.3389/fimmu.2017.01430
Liu M-L, Su W, Wang J-S et al (2020) Predicting preference of transcription factors for methylated DNA using sequence information. Mol Therapy Nucleic Acids. https://doi.org/10.1016/j.omtn.2020.07.035
Atanaki F, Behrouzi S, Ariaeenejad S et al (2020) BIPEP: sequence-based prediction of biofilm inhibitory peptides using a combination of NMR and physicochemical descriptors. ACS Omega 5:7290–7297. https://doi.org/10.1021/acsomega.9b04119
Yahav S, Bhole G (2020) Learning from imbalanced data in classification. Int J Recent Technol Eng 8:1907–1916. https://doi.org/10.35940/ijrte.e628 6.018520
Chawla N, Bowyer K, Hall L, Kegelmeyer W (2002) SMOTE: synthetic minority over-sampling technique. J Artif Intell Res 16:321–357. https://doi.org/10.1613/jair.953
Wang M, Cui X, Yu B et al (2020) SulSite-GTB: identification of protein S-sulfenylation sites by fusing multiple feature information and gradient tree boosting. Neural Comput Appl 32:13843–13862. https://doi.org/10.1007/s00521-020-04792-z
Kumari C, Abulaish M, Subbarao N (2020) Using SMOTE to deal with class-imbalance problem in bioactivity data to predict mTOR inhibitors. SN Comput Sci 1. https://doi.org/10.1007/s42979-020-00156-5
Wu L, Gao C, Xiang P et al (2020) CT-imaging based analysis of invasive lung adenocarcinoma presenting as ground glass nodules using peri- and intra-nodular radiomic features. Front Oncol 10. https://doi.org/10.3389/fonc.2020.00838
Mishra S, Mallick PK, Jena L, Chae G-S (2020) Optimization of skewed data using sampling-based preprocessing approach. Front Public Health 8. https://doi.org/10.3389/fpubh.2020.00274
Cortes C, Vapnik V (1995) Support-vector networks. Mach Learn 20:273–297. https://doi.org/10.1007/bf00994018
Ccrvantes J, Garcia-Lamont F, Rodriguez-Mazahua L, Lopez A (2020) A comprehensive survey on support vector machine classification: applications, challenges and trends. Neurocomputing 408:189–215. https://doi.org/10.1016/j.neucom.2019.10.118
Atasever S, Aydin Z, Erbay H, Sabzekar M (2019) Sample reduction strategies for protein secondary structure prediction. Appl Sci 9:4429. https://doi.org/10.3390/app9204429
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2022 The Author(s), under exclusive license to Springer Nature Singapore Pte Ltd.
About this paper
Cite this paper
Sohrawordi, M., Ali Hossain, M. (2022). Incorporation of Kernel Support Vector Machine for Effective Prediction of Lysine Formylation from Class Imbalance Samples. In: Arefin, M.S., Kaiser, M.S., Bandyopadhyay, A., Ahad, M.A.R., Ray, K. (eds) Proceedings of the International Conference on Big Data, IoT, and Machine Learning. Lecture Notes on Data Engineering and Communications Technologies, vol 95. Springer, Singapore. https://doi.org/10.1007/978-981-16-6636-0_15
Download citation
DOI: https://doi.org/10.1007/978-981-16-6636-0_15
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-16-6635-3
Online ISBN: 978-981-16-6636-0
eBook Packages: EngineeringEngineering (R0)