PROSITE documentation PDOC00274Eukaryotic initiation factor 5A hypusine signature
Eukaryotic initiation factor 5A (eIF-5A) (formerly known as eIF-4D) [1,2] is a small protein whose precise role in the initiation of protein synthesis is not known. It appears to promote the formation of the first peptide bond. eIF-5A seems to be the only eukaryotic protein to contain an hypusine residue. Hypusine is derived from lysine by the post-translational addition of a butylamino group (from spermidine) to the epsilon-amino group of lysine. The hypusine group is essential to the function of eIF-5A.
A hypusine-containing protein has been found in archaebacteria such as Sulfolobus acidocaldarius or Methanococcus jannaschii; this protein is highly similar to eIF-5A and could play a similar role in protein biosynthesis.
The signature we developed for eIF-5A is centered around the hypusine residue.
Last update:November 1997 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Park M.H. Wolff E.C. Folk J.E. |
| Title | Hypusine: its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation. | |
| Source | Biofactors 4:95-104(1993). | |
| PubMed ID | 8347280 |
| 2 | Authors | Schnier J. Schwelberger H.G. Smit-McBride Z. Kang H.A. Hershey J.W. |
| Title | Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae. | |
| Source | Mol. Cell. Biol. 11:3105-3114(1991). | |
| PubMed ID | 1903841 |
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