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Related Concept Videos

Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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...
Protein Networks02:26

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.
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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...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...

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A Protocol for Computer-Based Protein Structure and Function Prediction
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Published on: November 3, 2011

Predicting protein subnuclear localization using GO-amino-acid composition features.

Wen-Lin Huang1, Chun-Wei Tung, Hui-Ling Huang

  • 1Department of Management Information System, Chin Min Institute of Technology, Miaoli, Taiwan.

Bio Systems
|July 9, 2009
PubMed
Summary
This summary is machine-generated.

Predicting protein subnuclear localization is crucial for understanding cell functions. This study introduces PGAC, a method using Gene Ontology (GO) terms and amino acid composition to accurately predict protein locations within the nucleus.

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Area of Science:

  • Molecular Biology
  • Bioinformatics
  • Computational Biology

Background:

  • Nuclear proteins concentrate in subnuclear compartments, making their localization critical for understanding nuclear construction and function.
  • Gene Ontology (GO) annotation aids in predicting subnuclear localization, but challenges exist for sequence-based predictions without accession numbers or GO terms.

Purpose of the Study:

  • To develop an effective sequence-based method for predicting protein subnuclear localization, particularly for proteins lacking accession numbers or GO terms.
  • To leverage informative Gene Ontology (GO) terms and amino acid composition for improved prediction accuracy.

Main Methods:

  • Utilized BLAST to find protein homologies and retrieve GO terms for query proteins.
  • Developed the PGAC (Protein Gene Ontology Annotation Classifier) method, a support vector machine-based classifier.
  • Integrated informative GO terms with amino acid composition features for prediction.

Main Results:

  • PGAC identified 55 informative GO terms.
  • Achieved training accuracy of 85.7% and test accuracy of 76.3% on the SNL_35 dataset.
  • PGAC demonstrated superior performance over Nuc-PLoc, with 81.1% cross-validation accuracy compared to 67.4% on the SNL_80 dataset.

Conclusions:

  • Informative Gene Ontology (GO) terms are effective features for protein subnuclear localization prediction.
  • The PGAC method offers a robust approach for predicting protein subnuclear localization using sequence information.
  • A prediction server for PGAC is publicly available for use.