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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

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-Protein Interfaces

Protein-Protein Interfaces

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...

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....

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Related Experiment Video

Updated: Apr 18, 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: current status.

Pascale Gaudet¹, Pierre-André Michel², Monique Zahn-Zabal²

¹CALIPHO group, SIB Swiss Institute of Bioinformatics, Geneva, Switzerland, 1211 Department of Human Protein Sciences, Faculty of Medicine, University of Geneva, Geneva, Switzerland, 1211 pascale.gaudet@isb-sib.ch.

Nucleic Acids Research

|January 17, 2015

Summary

This summary is machine-generated.

neXtProt is a comprehensive human protein knowledgebase. Recent updates enhance proteomics data representation, human variant information, and introduce advanced semantic search capabilities for better biological research.

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Last Updated: Apr 18, 2026

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Published on: April 11, 2019

Area of Science:

Bioinformatics
Human Proteomics
Molecular Biology

Background:

neXtProt is a specialized knowledgebase for human proteins.
It aims to represent human biology with comprehensive data and precise annotations.
Traceable data provenance and an intuitive web interface are key features.

Purpose of the Study:

To present significant advances in the neXtProt knowledgebase.
To highlight improvements in proteomics data representation.
To detail enhanced human variant information and advanced search functionalities.

Main Methods:

Development of advanced data representation models for proteomics.
Expansion of human variant data capture and annotation.
Implementation of semantic technologies for enhanced search capabilities.

Main Results:

Improved representation of proteomics data within neXtProt.
Extended and more detailed information on human protein variants.
A new advanced search functionality leveraging semantic web technologies.

Conclusions:

neXtProt continues to evolve as a state-of-the-art resource for human protein information.
The recent updates significantly enhance its utility for researchers in human biology and proteomics.
Advanced search and data representation facilitate more comprehensive biological inquiry.