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Phosphorylation

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Related Experiment Video

Updated: Jul 19, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

Protein N-terminal modifications: molecular machineries and biological implications.

Hanne Øye¹, Malin Lundekvam¹, Alessia Caiella¹

¹Department of Biomedicine, University of Bergen, Bergen, Norway.

Trends in Biochemical Sciences

|January 21, 2025

Summary

Eukaryotic proteins undergo N-terminal (Nt) modifications by enzymes, impacting protein function and biological processes. This review covers Nt modifications, their enzymes, and their roles in health and disease.

Keywords:

acetylation arginylation methylation myristoylation oxidation ubiquitylation

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Last Updated: Jul 19, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

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Published on: December 27, 2016

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications

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Published on: May 18, 2017

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:

Biochemistry
Molecular Biology
Proteomics

Background:

Most eukaryotic proteins are modified at their N-terminus (Nt).
These modifications are enzyme-mediated and sequence-dependent.
Nt modifications are crucial for regulating protein function and cellular processes.

Purpose of the Study:

To provide an overview of protein N-terminal modifications.
To discuss the enzymes involved in Nt modifications.
To highlight the biological impact and disease relevance of Nt modifications.

Main Methods:

Literature review of N-terminal modification enzymes.
Analysis of co- and post-translational modification mechanisms.
Compilation of biological roles and disease associations.

Main Results:

Identified diverse Nt modifications including acetylation, methylation, and oxidation.
Cataloged enzymes such as peptidases, transferases, oxygenases, and ligases.
Demonstrated Nt modifications' roles in protein targeting, stability, and complex formation.

Conclusions:

N-terminal modifications are fundamental to proteome complexity and biological regulation.
Dysregulation of Nt-modifying enzymes is linked to human diseases.
Understanding Nt modifications is vital for comprehending cellular functions and disease mechanisms.