On 2014 Mar 05, Dale D O Martin commented:

The authors state that the protein has multiple predicted N-myristoylation sites that probably plays a role in telomere maintenance. However, myristoylation can only occur on N-terminal Glycines, hence the name N-myristoylation. I've commented on this on two other papers by these authors (here http://www.ncbi.nlm.nih.gov/pubmed/18071584 & here http://www.ncbi.nlm.nih.gov/pubmed/23007995 and the same comment I made is pasted below). I have also contacted the senior author and the editor of the journal regarding the second paper (http://www.ncbi.nlm.nih.gov/pubmed/23007995), but they have not changed it despite agreeing with me that it was incorrect. So, I am highlighting it here once again.

Previous comment: It should be noted that N-myristoylation can only occur on N-terminal Glycines, hence the name N-myristoylation. This occurs either co-translationally on the nascent polypeptide following the removal of the initiator Met or it can occur posttranslationally following proteolysis, which exposes a new N-terminal Gly. The latter has only been shown to occur in caspase-cleaved proteins. In this case, the Gly follows an Asp residue where caspase will cleave. The authors here predict internal myristoylation at very unlikely positions. Furthermore, the general consensus sequence for myristoylation is GXXXS/C/T where X is any amino acid, except for large bulky residues, and S/C/T are preferred in position 5 (counting from Gly). The first site they predict is GAAPP and is very unlikely to be myristoylated. Caution should be taken when predicting internal myristoylation sites. Unless it is predicted to be cleaved to expose an N-terminal Gly.

On 2014 Mar 05, Dale D O Martin commented:

The authors state that the protein has multiple predicted N-myristoylation sites that probably plays a role in telomere maintenance. However, myristoylation can only occur on N-terminal Glycines, hence the name N-myristoylation. I've commented on this on two other papers by these authors (here http://www.ncbi.nlm.nih.gov/pubmed/18071584 & here http://www.ncbi.nlm.nih.gov/pubmed/23007995 and the same comment I made is pasted below). I have also contacted the senior author and the editor of the journal regarding the second paper (http://www.ncbi.nlm.nih.gov/pubmed/23007995), but they have not changed it despite agreeing with me that it was incorrect. So, I am highlighting it here once again.

Previous comment: It should be noted that N-myristoylation can only occur on N-terminal Glycines, hence the name N-myristoylation. This occurs either co-translationally on the nascent polypeptide following the removal of the initiator Met or it can occur posttranslationally following proteolysis, which exposes a new N-terminal Gly. The latter has only been shown to occur in caspase-cleaved proteins. In this case, the Gly follows an Asp residue where caspase will cleave. The authors here predict internal myristoylation at very unlikely positions. Furthermore, the general consensus sequence for myristoylation is GXXXS/C/T where X is any amino acid, except for large bulky residues, and S/C/T are preferred in position 5 (counting from Gly). The first site they predict is GAAPP and is very unlikely to be myristoylated. Caution should be taken when predicting internal myristoylation sites. Unless it is predicted to be cleaved to expose an N-terminal Gly.