SignalP - 5.0

Signal peptide and cleavage sites in gram+, gram- and eukaryotic amino acid sequences

The SignalP 5.0 server predicts the presence of signal peptides and the location of their cleavage sites in proteins from Archaea, Gram-positive Bacteria, Gram-negative Bacteria and Eukarya. In Bacteria and Archaea, SignalP 5.0 can discriminate between three types of signal peptides:

• Sec/SPI: "standard" secretory signal peptides transported by the Sec translocon and cleaved by Signal Peptidase I (Lep)
• Sec/SPII: lipoprotein signal peptides transported by the Sec translocon and cleaved by Signal Peptidase II (Lsp)
• Tat/SPI: Tat signal peptides transported by the Tat translocon and cleaved by Signal Peptidase I (Lep)

SignalP 5.0 is based on a deep convolutional and recurrent neural network architecture including a conditional random field.

History paper Click here to read "A Brief History of Protein Sorting Prediction", The Protein Journal, 2019

DeepLoc Remember, the presence or absence of a signal peptide is not the whole story about the localization of a protein! If you want to find out more about the sorting of your eukaryotic proteins, try the protein subcellular localization predictor.

Behind the paper Check out the blog post about the SignalP 5.0 publication.

NOTE: This is not the newest version of SignalP. To use the current version, please go to the main SignalP site!

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