PROSITE documentation PDOC00008N-myristoylation site
An appreciable number of eukaryotic proteins are acylated by the covalent addition of myristate (a C14-saturated fatty acid) to their N-terminal residue via an amide linkage [1,2]. The sequence specificity of the enzyme responsible for this modification, myristoyl CoA:protein N-myristoyl transferase (NMT), has been derived from the sequence of known N-myristoylated proteins and from studies using synthetic peptides. It seems to be the following:
- The N-terminal residue must be glycine.
- In position 2, uncharged residues are allowed. Charged residues, proline and large hydrophobic residues are not allowed.
- In positions 3 and 4, most, if not all, residues are allowed.
- In position 5, small uncharged residues are allowed (Ala, Ser, Thr, Cys, Asn and Gly). Serine is favored.
- In position 6, proline is not allowed.
We deliberately include as potential myristoylated glycine residues, those which are internal to a sequence. It could well be that the sequence under study represents a viral polyprotein precursor and that subsequent proteolytic processing could expose an internal glycine as the N-terminal of a mature protein.
Last update:October 1989 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Towler D.A. Gordon J.I. Adams S.P. Glaser L. |
| Title | The biology and enzymology of eukaryotic protein acylation. | |
| Source | Annu. Rev. Biochem. 57:69-99(1988). | |
| PubMed ID | 3052287 | |
| DOI | 10.1146/annurev.bi.57.070188.000441 |
| 2 | Authors | Grand R.J.A. |
| Title | Acylation of viral and eukaryotic proteins. | |
| Source | Biochem. J. 258:625-638(1989). | |
| PubMed ID | 2658970 |
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