Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.7K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.7K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.4K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.4K
Regulated Protein Degradation02:58

Regulated Protein Degradation

8.8K
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
8.8K
The Proteasome01:13

The Proteasome

1.6K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.6K
The Proteasome02:18

The Proteasome

10.1K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
10.1K
Conserved Binding Sites01:49

Conserved Binding Sites

5.0K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Cardiomyopathy-associated and basic residue mutations in myopalladin alter actin binding, bundling, and structural stability.

Protein science : a publication of the Protein Society·2026
Same author

The Role of Linker Length and Composition in Actin Binding and Bundling by Palladin.

bioRxiv : the preprint server for biology·2025
Same author

Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS.

Protein science : a publication of the Protein Society·2025
Same author

Prediction of human O-linked glycosylation sites using stacked generalization and embeddings from pre-trained protein language model.

Bioinformatics (Oxford, England)·2024
Same author

Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS.

bioRxiv : the preprint server for biology·2024
Same author

SumoPred-PLM: human SUMOylation and SUMO2/3 sites Prediction using Pre-trained Protein Language Model.

NAR genomics and bioinformatics·2024
Same journal

metaLoc: protein localisation prediction workflow.

Bioinformatics advances·2026
Same journal

Fuscan: a robust DNA fusion caller for targeted sequencing data in cancer diagnostics.

Bioinformatics advances·2026
Same journal

Correction to: Pathogenicity patterns in cytochrome P450 family.

Bioinformatics advances·2026
Same journal

Region-aware bridge modeling enables interpretable mesoscale representation of spatial transcriptomic tissue sections.

Bioinformatics advances·2026
Same journal

Microbiome differential abundance methodologies to detect relevant taxa associated with chemotherapy toxicity rate in colorectal cancer.

Bioinformatics advances·2026
Same journal

maldipickr dereplicates microbial MALDI-TOF spectra to facilitate multiplexed isolation.

Bioinformatics advances·2026
See all related articles

Related Experiment Video

Updated: Jan 18, 2026

Detection of Protein Ubiquitination
09:00

Detection of Protein Ubiquitination

Published on: August 19, 2009

43.6K

Multimodal deep learning for predicting protein ubiquitination sites.

Subash C Pakhrin1,2, Moriah R Beck3, Punjan Subedi2

  • 1School of Computing, Wichita State University, Wichita, KS 67260, United States.

Bioinformatics Advances
|September 8, 2025
PubMed
Summary
This summary is machine-generated.

A new deep learning tool, the Multimodal Ubiquitination Predictor, accurately identifies ubiquitination sites across various datasets. This advancement enhances understanding of protein ubiquitination and its biological roles.

More Related Videos

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
11:54

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

10.2K
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.5K

Related Experiment Videos

Last Updated: Jan 18, 2026

Detection of Protein Ubiquitination
09:00

Detection of Protein Ubiquitination

Published on: August 19, 2009

43.6K
Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
11:54

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

10.2K
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.5K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioinformatics

Background:

  • Ubiquitination is a critical post-translational modification regulating protein degradation, signal transduction, and cellular homeostasis.
  • Accurate identification of ubiquitination sites is vital for understanding these biological processes.
  • Existing prediction tools often struggle with generalizability across diverse datasets.

Purpose of the Study:

  • To develop a robust deep learning model for predicting ubiquitination sites.
  • To enhance the accuracy and generalizability of ubiquitination site prediction across different datasets.
  • To provide a valuable resource for ubiquitination site discovery in research and applications.

Main Methods:

  • Developed a deep learning-based approach named Multimodal Ubiquitination Predictor.
  • Integrated diverse protein sequence representations: one-hot encoding, embeddings, and physicochemical properties.
  • Utilized a unified deep-learning framework for enhanced prediction accuracy and robustness.

Main Results:

  • Achieved superior performance on general, human-specific, and plant-specific datasets.
  • Demonstrated 77.25% accuracy, 74.98% sensitivity, 80.67% specificity, MCC of 0.54, and AUC of 0.87 on an independent human dataset.
  • Outperformed existing methods, showing enhanced reliability in ubiquitination site prediction.

Conclusions:

  • The Multimodal Ubiquitination Predictor offers enhanced accuracy and robustness for ubiquitination site prediction.
  • The developed predictor and dataset serve as valuable resources for future research in ubiquitination.
  • The tool is publicly available, facilitating broader research and application in the field.