Prediction of proprotein convertase cleavage sites

Protein Eng Des Sel. 2004 Jan;17(1):107-12. doi: 10.1093/protein/gzh013.


Many secretory proteins and peptides are synthesized as inactive precursors that in addition to signal peptide cleavage undergo post-translational processing to become biologically active polypeptides. Precursors are usually cleaved at sites composed of single or paired basic amino acid residues by members of the subtilisin/kexin-like proprotein convertase (PC) family. In mammals, seven members have been identified, with furin being the one first discovered and best characterized. Recently, the involvement of furin in diseases ranging from Alzheimer's disease and cancer to anthrax and Ebola fever has created additional focus on proprotein processing. We have developed a method for prediction of cleavage sites for PCs based on artificial neural networks. Two different types of neural networks have been constructed: a furin-specific network based on experimental results derived from the literature, and a general PC-specific network trained on data from the Swiss-Prot protein database. The method predicts cleavage sites in independent sequences with a sensitivity of 95% for the furin neural network and 62% for the general PC network. The ProP method is made publicly available at

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Databases as Topic
  • Furin / chemistry
  • Humans
  • Neural Networks, Computer
  • Proprotein Convertases / chemistry*
  • Protein Binding
  • Protein Engineering / methods*
  • Rats
  • Sensitivity and Specificity


  • Proprotein Convertases
  • Furin