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Covalently Linked Protein Regulators

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.

Covalently Linked Protein Regulators

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.

The Proteasome

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...

The Proteasome

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...

The Proteasome

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...

Bacterial Protein Maturation

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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Related Experiment Video

Updated: May 27, 2026

Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications

Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications

Published on: April 21, 2023

TopFIND 2.0--linking protein termini with proteolytic processing and modifications altering protein function.

Philipp F Lange¹, Pitter F Huesgen, Christopher M Overall

¹Centre for Blood Research, Department of Oral Biological and Medical Sciences, University of British Columbia, Vancouver, BC, Canada V6T 1Z3. philipp.lange@ubc.ca

Nucleic Acids Research

|November 22, 2011

Summary

This summary is machine-generated.

TopFIND 2.0 is a knowledgebase for protein termini, modifications, and proteolytic processing. It aids in understanding protein function by analyzing cleavage events and termini across multiple species.

More Related Videos

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

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Last Updated: May 27, 2026

Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications

Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications

Published on: April 21, 2023

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Area of Science:

Proteomics
Biochemistry
Bioinformatics

Background:

Protein termini (N- and C-termini) are crucial for understanding protein function and modifications.
Advances in proteomics enable large-scale analysis of protein termini (terminomes).
Information on in vivo protein termini, post-translational modifications, and proteolytic processing is rapidly growing.

Purpose of the Study:

To present TopFIND version 2.0, a comprehensive knowledgebase for protein termini.
To consolidate information on protein termini, modifications, and proteolytic processing.
To facilitate the investigation of protein function through terminus analysis.

Main Methods:

Developed TopFIND 2.0, a protein-centric knowledgebase.
Integrated data from community submissions, publications, UniProtKB, and MEROPS.
Incorporated detailed evidence classification for cleavage sites, termini, and modifications.
Implemented filtering options for supporting evidence.
Developed dynamic network visualizations for protease-substrate-inhibitor relationships and cleavage site specificities.

Main Results:

TopFIND 2.0 covers five species: human, mouse, *Arabidopsis thaliana*, yeast, and *E. coli*.
The knowledgebase provides detailed evidence for identified cleavage sites, termini, and modifications.
Includes network visualizations for exploring protease activities and specificities.

Conclusions:

TopFIND 2.0 offers a valuable resource for in-depth investigation of protein termini.
Facilitates hypothesis generation on protein function by linking cleavage events to domains and mutations.
Supports the global analysis of terminomes and proteolytic processing.