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PROSITE documentation PDOC00008

N-myristoylation site





Description

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.
Note:

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.

Technical section

PROSITE method (with tools and information) covered by this documentation:

MYRISTYL, PS00008; N-myristoylation site  (PATTERN with a high probability of occurrence!)


References

1AuthorsTowler D.A. Gordon J.I. Adams S.P. Glaser L.
TitleThe biology and enzymology of eukaryotic protein acylation.
SourceAnnu. Rev. Biochem. 57:69-99(1988).
PubMed ID3052287
DOI10.1146/annurev.bi.57.070188.000441

2AuthorsGrand R.J.A.
TitleAcylation of viral and eukaryotic proteins.
SourceBiochem. J. 258:625-638(1989).
PubMed ID2658970



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