Procleave_smooth webserver

Please upload a PDB file (e.g. 1AU1): (example)

Specifiy the chain name (e.g. A): (example)

Please select the protease of interest from the dropdown menu to make the prediction: (help)

select all
pepsin A (A01.001)
cathepsin D (A01.009)
cathepsin E (A01.010)
rhizopuspepsin (A01.012)
aspergillopepsin I (A01.016)
necepsin-1 (A01.053)
HIV-1 retropepsin (A02.001)
cathepsin L (C01.032)
cathepsin L1 {Fasciola} sp. (C01.033)
cathepsin S (C01.034)
falcipain-2 (C01.046)
cathepsin B (C01.060)
falcipain-3 (C01.063)
caspase-3 (C14.003)
caspase-6 (C14.005)
matrix metallopeptidase-2 (M10.003)
matrix metallopeptidase-9 (M10.004)
astacin (M12.001)
meprin alpha subunit (M12.002)
meprin beta subunit (M12.004)
LAST_MAM peptidase (M12.033)
chymotrypsin A (cattle-type) (S01.001)
granzyme B ({Homo sapiens}-type) (S01.010)
elastase-2 (S01.131)
cathepsin G (S01.133)
glutamyl peptidase I (S01.269)
lysyl peptidase (bacteria) (S01.280)


If you find Procleave useful, please kindly cite our paper:

Li et al. "Procleave: a conditional random field approach that combines sequence and structural information significantly improves the prediction of protease substrate cleavage sites", Genomics Proteomics Bioinformatics, 2020 Feb;18(1):52-64. doi: 10.1016/j.gpb.2019.08.002.


Copyright © 2019. Biomedicine Discovery Institute and School of Biomedical Sciences, Faculty of Medicine, Nursing and Health Sciences, Monash University, Australia