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Related Concept Videos

Covalently Linked Protein Regulators02:04

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.
Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Proteomics01:33

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...
Regulation of Expression at Multiple Steps01:23

Regulation of Expression at Multiple Steps

The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the addition of a...

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Related Experiment Video

Updated: May 20, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Deciphering a global network of functionally associated post-translational modifications.

Pablo Minguez1, Luca Parca, Francesca Diella

  • 1Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.

Molecular Systems Biology
|July 19, 2012
PubMed
Summary
This summary is machine-generated.

Post-translational modifications (PTMs) are interconnected, forming a global regulatory network. This study reveals extensive PTM interplay, impacting thousands of human proteins and their functions.

More Related Videos

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
09:29

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

Published on: May 18, 2017

Related Experiment Videos

Last Updated: May 20, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
09:29

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

Published on: May 18, 2017

Area of Science:

  • Molecular Biology
  • Proteomics
  • Bioinformatics

Background:

  • Post-translational modifications (PTMs) regulate eukaryotic protein function.
  • Co-regulation of different PTMs within and between proteins is known.
  • A global understanding of PTM interplay is lacking.

Purpose of the Study:

  • To investigate the global interplay between different PTM types.
  • To compare the evolutionary rates of various PTMs.
  • To develop a method for measuring PTM co-evolution within proteins.

Main Methods:

  • Collected data for 13 frequent PTM types across 8 eukaryotes.
  • Compared evolutionary speeds of PTMs.
  • Developed a co-occurrence-based method to measure PTM co-evolution within proteins.

Main Results:

  • PTM types are vastly interconnected, forming a global network.
  • This network involves >50,000 residues in ~6000 human proteins.
  • Significant PTM interplay is predicted in secreted/membrane proteins, protein domains, and short-linear motifs.

Conclusions:

  • The global network of co-evolving PTM types suggests complex post-translational regulation.
  • This intricate regulation likely governs multiple functional states of eukaryotic proteins.
  • PTM interplay is a fundamental aspect of protein regulation.