Related Experiment Video
Updated: Dec 27, 2025
Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells
Published on: June 30, 2018
SCLpred-EMS: subcellular localization prediction of endomembrane system and secretory pathway proteins by Deep N-to-1
Manaz Kaleel1,2, Yandan Zheng3, Jialiang Chen3
1School of Computer Science.
Motivation:
The subcellular location of a protein can provide useful information for protein function prediction and drug design. Experimentally determining the subcellular location of a protein is an expensive and time-consuming task. Therefore, various computer-based tools have been developed, mostly using machine learning algorithms, to predict the subcellular location of proteins.
Results:
Here, we present a neural network-based algorithm for protein subcellular location prediction. We introduce SCLpred-EMS a subcellular localization predictor powered by an ensemble of Deep N-to-1 Convolutional Neural Networks. SCLpred-EMS predicts the subcellular location of a protein into two classes, the endomembrane system and secretory pathway versus all others, with a Matthews correlation coefficient of 0.75-0.86 outperforming the other state-of-the-art web servers we tested.
Availability And Implementation:
SCLpred-EMS is freely available for academic users at http://distilldeep.ucd.ie/SCLpred2/.
Contact:
catherine.mooney@ucd.ie.
Related Concept Videos
01:45ER Retrieval Pathway
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
01:12Clathrin Coated Vesicles
01:17Role of ER in the Secretory Pathway
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
01:46Nuclear Localization Signals and Import
01:26Insertion of Single-pass Transmembrane Proteins in the RER
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
01:29Insertion of Multi-pass Transmembrane Proteins in the RER
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...