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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

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 form...
Conservation of Protein Domains02:26

Conservation of Protein Domains

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 form...
Exon Recombination02:32

Exon Recombination

The evolution of new genes is critical for speciation. Exon recombination, also known as exon shuffling or domain shuffling, is an important means of new gene formation. It is observed across vertebrates, invertebrates, and in some plants such as potatoes and sunflowers. During exon recombination, exons from the same or different genes recombine and produce new exon-intron combinations, which might evolve into new genes. 
Exon shuffling follows “splice frame rules.” Each exon has three reading...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...

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Updated: May 21, 2026

Identification of Functional Protein Regions Through Chimeric Protein Construction
11:39

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

Novel domain combinations in proteins encoded by chimeric transcripts.

Milana Frenkel-Morgenstern1, Alfonso Valencia

  • 1Structural Biology and BioComputing Program, Spanish National Cancer Research Centre (CNIO), 28029 Madrid, Spain.

Bioinformatics (Oxford, England)
|June 13, 2012
PubMed
Summary
This summary is machine-generated.

Chimeric proteins, formed from rearranged genes, often contain complete functional domains. This suggests they may disrupt normal cell functions by competing with existing proteins.

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Last Updated: May 21, 2026

Identification of Functional Protein Regions Through Chimeric Protein Construction
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Area of Science:

  • Genomics
  • Proteomics
  • Molecular Biology

Background:

  • Chimeric RNAs arise from trans-splicing, translocations, or gene fusions.
  • Some chimeric transcripts yield functional chimeric proteins.

Purpose of the Study:

  • Investigate design principles of chimeric proteins.
  • Analyze domain composition in human chimeric RNAs.

Main Methods:

  • Analyzed 7,424 human chimeric RNAs.
  • Used genomic alignments and gene-gene junction analysis.
  • Predicted protein domains and compared permutations.

Main Results:

  • Chimeras frequently contain complete protein domains, more than random sets.
  • Eight domain types are over-represented in chimeras.
  • Identified novel domain combinations and predicted dominant-negative effects.

Conclusions:

  • Chimeric proteins offer combinatorial diversity, potentially impacting gene function and protein interactions.
  • Complete domains in chimeras suggest functional roles and potential for dominant-negative activity.