Related Experiment Video
Updated: Jul 15, 2026

09:00
Detection of Protein Ubiquitination
Published on: August 19, 2009
UbiProt: a database of ubiquitylated proteins
Alexander L Chernorudskiy1, Alejandro Garcia, Eugene V Eremin
1Nizhny Novgorod State University, Nizhny Novgorod, Russia. chalbio@mail.ru <chalbio@mail.ru>
BMC Bioinformatics
|April 20, 2007
Summary
The UbiProt Database consolidates information on ubiquitylated proteins, addressing a critical need for systematized data in ubiquitylation research. This resource aids scientists studying protein ubiquitylation and its role in human diseases.
Area of Science:
- Molecular Biology
- Biochemistry
- Genomics
Background:
- Ubiquitylation, a key post-translational modification, significantly impacts cellular pathways and disease pathogenesis.
- While many eukaryotic proteins are ubiquitylated, data remains fragmented.
- Understanding ubiquitylation is crucial for advancing biological and medical research.
Purpose of the Study:
- To create a centralized, systematized knowledge base for ubiquitylated proteins.
- To address the need for organized experimental data on ubiquitylation.
- To provide a comprehensive resource for researchers in the ubiquitin field.
Main Methods:
- Development of the UbiProt Database, a novel resource for ubiquitylated proteins.
- Systematization of experimental data on protein ubiquitylation.
- Inclusion of protein characteristics, ubiquitylation sites, and related machinery.
Main Results:
- The UbiProt Database offers retrievable information on protein ubiquitylation.
- It includes details on ubiquitylation features, machinery, and supporting literature.
- The database is publicly accessible at http://ubiprot.org.ru.
Conclusions:
- UbiProt serves as a valuable public resource for comprehensive ubiquitylated protein information.
- It benefits researchers studying the ubiquitin system and specific ubiquitylated proteins.
- Ongoing development of UbiProt is anticipated to be of broad interest to the research community.
Related Concept Videos
Covalently Linked Protein Regulators
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.
These groups modify specific amino acids in a protein.
Protein Networks
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
The Proteasome
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 (ubiquitin...
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 (ubiquitin...
The Proteasome
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...
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...
Protein-protein Interfaces
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 polypeptide...
Proteomics
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

