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The hydrolysis of a peptide bond or bonds within a protein as part of protein maturation, the process leading to the attainment of the full functional capacity of a protein. Any process leading to the attainment of the full functional capacity of a protein. Any protein maturation process achieved by the cleavage of peptide bonds. A series of specific posttranslational modifications to the CAAX box region of CAAX box proteins. CAAX box proteins are eukaryotic proteins that contain a CAAX motif where the C is a cysteine, the two A residues are aliphatic amino acids and the X can be one of several amino acids. The CAAX-box proteins undergo three sequential, enzymatic, post-translational modifications essential to their targeting: First, the proteins are prenylated by one of two prenyltransferases called farnesyltransferase and geranylgeranyltransferase-I. Prenylation results in the covalent attachment of either farnesyl or geranylgeranyl isoprenoid moieties to the cysteine in the CAAX box motif. Prenylation is followed by proteolytic removal of the last three amino acids of the protein (AAX). Finally, the newly exposed carboxylate group of the isoprenylcysteine is methylated by an ER-associated prenyl-dependent carboxylmethyltransferase. The second process in a series of specific posttranslational modifications to the CAAX box region of CAAX box proteins, in which the last three amino acids of the protein (AAX) are removed by proteolysis.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: CAAX-box protein processing
Acc: GO:0071586
Aspect: Biological Process
Desc: The second process in a series of specific posttranslational modifications to the CAAX box region of CAAX box proteins, in which the last three amino acids of the protein (AAX) are removed by proteolysis.
Proteins in PDR annotated with:
   This term: 2 [Search]
   Term or descendants: 2 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0071586 - CAAX-box protein processing (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle