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PROSITE documentation PDOC00266
Prenyl group binding site (CAAX box)


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PURL: https://purl.expasy.org/prosite/documentation/PDOC00266

Description

A number of eukaryotic proteins are post-translationally modified by the attachment of either a farnesyl or a geranyl-geranyl group to a cysteine residue [1,2,3,4]. The modification occurs on cysteine residues that are three residues away from the C-terminal extremity; the two residues that separate this cysteine from the C-terminal residue are generally aliphatic. This Cys-Ali-Ali-X pattern is generally known as the CAAX box. Proteins known or strongly presumed to be the target of this modification are listed below.

  • Ras proteins, and ras-like proteins such as Rho, Rab, Rac, Ral, and Rap.
  • Nuclear lamins A and B.
  • Some G protein α subunits.
  • G protein γ subunits (see <PDOC01002>).
  • 2',3'-cyclic nucleotide 3'-phosphodiesterase (EC 3.1.4.37).
  • Rhodopsin-sensitive cGMP 3',5'-cyclic nucleotide phosphodiesterase α and β chains (EC 3.1.4.17).
  • Rhodopsin kinase (EC 2.7.11.14).
  • Some dnaJ-like proteins (such as yeast MAS5/YDJ1).
  • A number of fungal mating factors (such as M-factor or rhodotorucine A).
Last update:

November 1997 / Text revised.

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Technical section

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

PRENYLATION, PS00294; Prenyl group binding site (CAAX box)  (PATTERN with a high probability of occurrence!)


References

1AuthorsGlomset J.A. Gelb M.H. Farnsworth C.C.
TitlePrenyl proteins in eukaryotic cells: a new type of membrane anchor.
SourceTrends Biochem. Sci. 15:139-142(1990).
PubMed ID2187294

2AuthorsLowy D.R. Willumsen B.M.
TitleProtein modification: new clue to Ras lipid glue.
SourceNature 341:384-385(1989).
PubMed ID2677741

3AuthorsImagee A.I.
SourceBiochem. Soc. Trans. 17:875-876(1989).

4AuthorsPowers S.
TitleProtein prenylation: a modification that sticks.
SourceCurr. Biol. 1:114-116(1991).
PubMed ID15336183



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