EC Number   |
Natural Substrates |
|---|
   3.4.99.B1 | a-factor + H2O |
- |
| 3.4.99.B1 | a-factor-CaaX + H2O |
a stands for aliphatic amino acid, X is any amino acid |
| 3.4.99.B1 | a-factor-CaaX + H2O |
removal of the last three amino acids of carboxyl-terminal sequence motif CaaX, enzyme proteolyzes a-factor with A, V, L, I, C or M at the a1 position, V, L, I, C or M at the a2 position or any amino acid at the X position |
| 3.4.99.B1 | K-Ras(farnesyl)VIM + H2O |
- |
| 3.4.99.B1 | more |
in the absence of Rce1, splenocytes and bone marrow cells expressing oncogenic KRAS yield more and larger colonies when grown in methylcellulose. The inactivation of Rce1 worsens the myeloproliferative disease caused by oncogenic K-RAS |
| 3.4.99.B1 | more |
the Trypanosoma brucei RCE1 ortholog appears to be the dominant prenyl-CaaX protease |
| 3.4.99.B1 | more |
the enzyme is responsible for one step in Ras membrane localization |
| 3.4.99.B1 | Ras + H2O |
- |
| 3.4.99.B1 | Ras-CaaX + H2O |
a stands for aliphatic amino acid, X is any amino acid |
| 3.4.99.B1 | Ras2 + H2O |
a stands for aliphatic amino acid, X is any amino acid |
