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SignalP - 6.0

Signal peptides and their cleavage sites in all domains of life

The SignalP 6.0 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 6.0 can discriminate between five 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)
  • Tat/SPII: Tat lipoprotein signal peptides transported by the Tat translocon and cleaved by Signal Peptidase II (Lsp)
  • Sec/SPIII: Pilin and pilin-like signal peptides transported by the Sec translocon and cleaved by Signal Peptidase III (PilD/PibD)
Additionally, SignalP 6.0 predicts the regions of signal peptides. Depending on the type, the positions of n-, h- and c-regions as well as of other distinctive features are predicted.
SignalP 6.0 is based on a transformer protein language model with a conditional random field for structured prediction.

Behind the Paper: Check out the blog post about the SignalP 6.0 publication in the Nature Portfolio Bioengineering Community.

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

Eukaryotic proteins: 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 DeepLoc. You may also want to check whether proteins with signal peptides have GPI anchors that keep them attached to the outer face of the plasma membrane using the predictor NetGPI.



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