Bioactive peptides are typically small functional peptides with 2–20 amino acid residues and play versatile roles in metabolic and biological processes. Bioactive peptides are multi-functional, so it is vastly challenging to accurately detect all their functions simultaneously. We proposed a convolution neural network (CNN) and bi-directional long short-term memory (Bi-LSTM)-based deep learning method (called MPMABP) for recognizing multi-activities of bioactive peptides. The MPMABP stacked five CNNs at different scales, and used the residual network to preserve the information from loss. The empirical results showed that the MPMABP is superior to the state-of-the-art methods. Analysis on the distribution of amino acids indicated that the lysine preferred to appear in the anti-cancer peptide, the leucine in the anti-diabetic peptide, and the proline in the anti-hypertensive peptide. The method and analysis are beneficial to recognize multi-activities of bioactive peptides.

Lysine succinylation is a typical protein post‐translational modification and plays a crucial role of regulation in the cellular process. Identifying succinylation sites is fundamental to explore its functions. Although many computational methods were developed to deal with this challenge, few considered semantic relationship between residues. We combined long short‐term memory (LSTM) and convolutional neural network (CNN) into a deep learning method for predicting succinylation site. The proposed method obtained a Matthews correlation coefficient of 0.2508 on the independent test, outperforming state of the art methods. We also performed the enrichment analysis of succinylation proteins. The results showed that functions of succinylation were conserved across species but differed to a certain extent with species. On basis of the proposed method, we developed a user‐friendly web server for predicting succinylation sites.