Background: Occurring at the cysteine residue in the C-terminal of a protein, prenylation
is a special kind of post-translational modification (PTM), which may play a key role for
statin in altering immune function. Therefore, knowledge of the prenylation sites in proteins is
important for drug development as well as for in-depth understanding the biological process concerned.
Objective: Given a query protein whose C-terminal contains some cysteine residues, which one
can be of prenylation or none of them can be prenylated?
Methods: To address this problem, we have developed a new predictor, called “iPreny-PseAAC”,
by incorporating two tiers of sequence pair coupling effects into the general form of PseAAC
(pseudo amino acid composition).
Results: It has been observed by four different cross-validation approaches that all the important
indexes in reflecting its prediction quality are quite high and fully consistent to each other.
Conclusion: It is anticipated that the iPreny-PseAAC predictor holds very high potential to become
a useful high throughput tool in identifying protein C-terminal cysteine prenylation sites and
the other relevant areas. To maximize the convenience for most experimental biologists, the webserver
for the new predictor has been established at http://app.aporc.org/iPreny-PseAAC/, by
which users can easily get their desired results without needing to go through the mathematical
details involved in this paper.