※ CSS-Palm INTRODUCTION:
As a special class of post-translational modifications (PTMs), numerous proteins could be covalently modified by a variety of lipids, including myristate (C14), palmitate (C16), farnesyl (C15), geranylgeranyl (C20) and glycosylphosphatidylinositol (GPI), etc (Casey, 1995; Nadolski and Linder, 2007; Resh, 2006). Although most of lipid modifications are irreversible, protein S-palmitoylation, also called as thioacylation or S-acylation, could reversibly attach 16-carbon saturated fatty acids to specific cysteine residues in protein substrates through thioester linkages (Bijlmakers and Marsh, 2003; Dietrich and Ungermann, 2004; el-Husseini Ael and Bredt, 2002; Greaves and Chamberlain, 2007; Linder and Deschenes, 2007; Nadolski and Linder, 2007; Resh, 2006; Resh, 2006; Roth, et al., 2006; Smotrys and Linder, 2004; Wan, et al., 2007). Palmitoylation will enhance the surface hydrophobicity and membrane affinity of protein substrates, and play important roles in modulating proteins' trafficking (Draper, et al., 2007; Linder and Deschenes, 2007), stability (Linder and Deschenes, 2007), and sorting (Greaves and Chamberlain, 2007), etc. Also, protein palmitoylation has been involved in numerous cellular processes, including signaling (Casey, 1995; Kurayoshi, et al., 2007; Resh, 2006), apoptosis (Chakrabandhu, et al., 2007; Feig, et al., 2007), and neuronal transmission (Roth, et al., 2006; Stowers and Isacoff, 2007), etc. Although many efforts have been made in this field, the molecular mechanism underlying protein palmitoylation still remain to be inexplicit.
This website is linked in ExPASy Proteomics Tools page.
CSS-Palm 4.0 User Interface
For publication of results please cite the following article:
CSS-Palm 2.0: an updated software for palmitoylation sites prediction
Jian Ren, Longping Wen, Xinjiao Gao, Changjiang Jin, Yu Xue and Xuebiao Yao.
Protein Engineering, Design and Selection.2008 21(11):639-644