Related Experiment Video
Updated: Jul 17, 2026

Enriching Subcellular Proteins in Leptospira Using a Triton X-114-Based Fractionation Approach
Published on: August 8, 2025
Using motifs in the prediction of eukaryotic protein subcellular localization
1Department of Electronic Science and Technology, University of Science and Technology of China, Hefei, P R, China.
Abstract:
Subcellular location of a protein is one of the key functional characters as proteins must be localized correctly at the subcellular level to have normal biological functions. In this paper, all motifs in PROSITE were examined and those that are indicative to eukaryotic protein subcellular localizations were picked out. A corresponding motif module was built and combined to our former work: LOCSVMPSI. Prediction results of this combined method were compared to LOCSVMPSI as well as several other existing methods for subcellular localization. The combined method achieved highest overall prediction accuracy among all listed methods and improved the over-all and each-location accuracies of LOCSVMPSI by 3%-8%. Further analysis indicates the combined motif method is very effective in eukaryotic protein subcellular localization prediction.
Related Concept Videos
Nuclear Protein Sorting
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...
Directing Proteins to the Rough Endoplasmic Reticulum
Nuclear Localization Signals and Import
Conserved Binding Sites
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...
Regulated mRNA Transport
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
