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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
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The Ideal Transformer01:26

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In single-phase two-winding transformers, two windings are coiled around a magnetic core characterized by cross-sectional area A and magnetic permeability μ. A phasor current i1 enters the left winding while i2 exits the right winding, establishing the fundamental working of the transformer through electromagnetic principles.
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Per-Unit Sequence Models01:26

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Types Of Transformers01:16

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Transformers can provide desired voltages to a circuit by modifying the number of turns in the secondary windings.
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Related Experiment Video

Updated: Sep 26, 2025

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TransPhos: A Deep-Learning Model for General Phosphorylation Site Prediction Based on Transformer-Encoder

Xun Wang1,2, Zhiyuan Zhang1, Chaogang Zhang1

  • 1College of Computer Science and Technology, China University of Petroleum, Qingdao 266555, China.

International Journal of Molecular Sciences
|April 23, 2022
PubMed
Summary

TransPhos, a novel deep learning predictor, enhances protein phosphorylation site prediction using transformer encoders and CNNs. This computational tool outperforms existing methods, improving accuracy for Serine, Threonine, and Tyrosine phosphorylation sites.

Keywords:
phosphorylation site predictionpost-translational modificationstransformer

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Area of Science:

  • Biochemistry and Molecular Biology
  • Computational Biology
  • Bioinformatics

Background:

  • Protein phosphorylation is a critical post-translational modification in eukaryotes, regulating numerous biological processes.
  • Accurate prediction of phosphorylation sites is essential for understanding protein function and signaling pathways.
  • Existing computational predictors often rely on domain knowledge or feature selection, limiting their generalizability.

Purpose of the Study:

  • To develop a novel deep learning-based predictor, TransPhos, for accurate phosphorylation site prediction.
  • To evaluate the performance of TransPhos against established deep learning models and state-of-the-art prediction tools.
  • To assess the model's efficacy across different phosphorylation sites (Serine, Threonine, Tyrosine).

Main Methods:

  • TransPhos utilizes a transformer encoder combined with densely connected convolutional neural network (CNN) blocks.
  • Model performance was evaluated on the PPA (version 3.0) and Phospho.ELM datasets.
  • 10-fold cross-validation was employed to assess prediction accuracy.

Main Results:

  • TransPhos demonstrated superior performance compared to various deep learning models (CNN, LSTM, RNN, FCNN) and existing tools (GPS2.1, NetPhos, DeepPhos, etc.).
  • The model achieved high AUC values: 0.8579 for Serine (S), 0.8335 for Threonine (T), and 0.6953 for Tyrosine (Y).
  • TransPhos significantly outperformed competing predictors in general phosphorylation site prediction.

Conclusions:

  • TransPhos represents a significant advancement in computational phosphorylation site prediction.
  • The deep learning architecture effectively captures complex patterns for improved prediction accuracy.
  • This tool offers a robust and accurate solution for researchers studying protein phosphorylation.