Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00008N-myristoylation site
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC00008
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.
-------------------------------------------------------------------------------
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 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.