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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...

Protein Families

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism. Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members. If these new proteins contain similar amino acids in key...

Protein Families

Protein Families

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

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 Networks

Protein Networks

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Updated: Mar 11, 2026

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

The neXtProt knowledgebase on human proteins: 2017 update.

Pascale Gaudet^1,2, Pierre-André Michel³, Monique Zahn-Zabal³

¹CALIPHO group, SIB Swiss Institute of Bioinformatics, Geneva, Switzerland, 1206 pascale.gaudet@sib.swiss.

Nucleic Acids Research

|December 1, 2016

Summary

This summary is machine-generated.

The neXtProt knowledgebase now offers extensive proteomics data for human proteins and genetic variations linked to hereditary diseases. This update enhances resources for proteomics researchers and genetic studies.

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Area of Science:

Bioinformatics
Genomics
Proteomics

Background:

The neXtProt human protein knowledgebase is a comprehensive resource for protein information.
Continuous updates are essential to incorporate the latest research findings and data.

Purpose of the Study:

To present the recent updates and new features of the neXtProt knowledgebase.
To highlight the expanded proteomics and genetic variation data available.

Main Methods:

Integration of proteomics data for over 85% of human proteins.
Inclusion of over 8000 phenotypic observations for genetic variations.
Development of new tools specifically for the proteomics community.

Main Results:

neXtProt now covers a significant portion of human proteins with proteomics data.
Detailed phenotypic information is available for thousands of genetic variations.
New, specialized tools are accessible to proteomics researchers.

Conclusions:

The latest neXtProt release significantly enhances its utility for proteomics and genetic variation studies.
Data accessibility is maintained through user interfaces, FTP, API, and SPARQL endpoints.