The N-terminal domain (INCENP_N) is required for chromosomal passenger complex localization to centromeres (Ainsztein et al., 1998) and forms a three-helix bundle with borealin and survivin (Klein et al., 2006; Vader et al., 2006). Ainsztein et al. (1998) have suggested that the conserved motif encompassing amino acids 32–44 is essential for targeting INCENP to centromeres during mitosis. Since the sequence of aa 1-26 is not conserved among species, they prepared a deletion construct (INCENP 27-839) encoding a protein missing the first 26 amino acids. However, the INCENP 27-839 failed to target centromeres. Unfortunately, they did not conduct in-depth research on the aa 1-26 of INCENP, only attributing the effect to INCENP protein structure (Ainsztein et al., 1998). In our study, we suppose Cys15 as an S-palmitoylation site of INCENP. By analyzing the amino acid sequence of INCENP in silico, we found Cys15 had the highest S-palmitoylation score. Surprisingly, Cys15 is a consensus amino acid site among species (Figure 4B). Such conservation indicates that Cys15 may serve a critical biological function. Taken together, the S-palmitoylation of Cys15 may serve as a
