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Protein Networks

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,...

Protein-protein Interfaces

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...

Protein-Protein Interfaces

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...

Tagging and Fusion Proteins

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...

Proteomics

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...

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Related Experiment Video

Updated: Jun 28, 2026

Mass Spectrometry-Based Proteomics Analyses Using the OpenProt Database to Unveil Novel Proteins Translated from Non-Canonical Open Reading Frames

Mass Spectrometry-Based Proteomics Analyses Using the OpenProt Database to Unveil Novel Proteins Translated from Non-Canonical Open Reading Frames

Published on: April 11, 2019

InterPro: the integrative protein signature database.

Sarah Hunter¹, Rolf Apweiler, Teresa K Attwood

¹EMBL Outstation European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge, UK. hunter@ebi.ac.uk

Nucleic Acids Research

|October 23, 2008

Summary

This summary is machine-generated.

The InterPro database integrates protein signatures from multiple sources, enhancing protein family and functional site analysis. Recent updates improve data accessibility and expand coverage of the UniProtKB database.

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Last Updated: Jun 28, 2026

Mass Spectrometry-Based Proteomics Analyses Using the OpenProt Database to Unveil Novel Proteins Translated from Non-Canonical Open Reading Frames

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Published on: April 11, 2019

An Integrated Approach for Microprotein Identification and Sequence Analysis

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Identifying Protein-protein Interaction Sites Using Peptide Arrays

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Area of Science:

Bioinformatics
Computational Biology
Proteomics

Background:

The InterPro database integrates protein signatures from diverse source databases, including Pfam, PROSITE, and SMART.
These signatures represent protein domains, families, and functional sites, aiding in protein characterization.

Purpose of the Study:

To describe recent developments and updates to the InterPro database and its associated resources.
To highlight improvements in data integration, accessibility, and coverage.

Main Methods:

Manual integration of protein signatures from source databases into InterPro entries.
Development of new XML files for non-signature data and inclusion of matchless UniProtKB proteins.
Enhancement of the InterPro web interface with new links and viewers.

Main Results:

Approximately 58,000 signatures are available, with about half integrated into InterPro entries.
The latest release (v18.0) covers 79.8% of UniProtKB (v14.1) and contains 16,549 entries.
New features include display of un-integrated signatures, structural data, and links to external databases.

Conclusions:

InterPro provides a comprehensive resource for protein signature analysis.
Ongoing development ensures improved data coverage, integration, and accessibility for researchers.