PROSITE documentation PDOC00266Prenyl group binding site (CAAX box)
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).
November 1997 / Text revised.
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Technical section
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References
1 | Authors | Glomset J.A. Gelb M.H. Farnsworth C.C. |
Title | Prenyl proteins in eukaryotic cells: a new type of membrane anchor. | |
Source | Trends Biochem. Sci. 15:139-142(1990). | |
PubMed ID | 2187294 |
2 | Authors | Lowy D.R. Willumsen B.M. |
Title | Protein modification: new clue to Ras lipid glue. | |
Source | Nature 341:384-385(1989). | |
PubMed ID | 2677741 |
3 | Authors | Imagee A.I. |
Source | Biochem. Soc. Trans. 17:875-876(1989). |
4 | Authors | Powers S. |
Title | Protein prenylation: a modification that sticks. | |
Source | Curr. Biol. 1:114-116(1991). | |
PubMed ID | 15336183 |
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