RNF187
Domain
The RING-type zinc finger domain is required for E3 ligase activity.
Function
E3 ubiquitin-protein ligase that acts as a coactivator of JUN-mediated gene activation in response to growth factor signaling via the MAP3K1 pathway, independently from MAPK8.
Pathway
Protein modification; protein ubiquitination.
Post-translational modifications
Ubiquitinated; undergoes 'Lys-48'-linked autoubiquitination in the absence of growth factors and MAP3K1-induced 'Lys-63'-linked polyubiquitination (PubMed:20852630). 'Lys-48'-autoubiquitination leads to degradation by the proteasome, while MAP3K1-induced 'Lys-63'-linked polyubiquitination results in the stabilization of the protein (PubMed:20852630). 'Lys-48'- and 'Lys-63'-linked polyubiquitinations occur most probably on the same 3 C-terminal lysine residues (Lys-195, Lys-223 and Lys-224) and are thus mutually exclusive (PubMed:20852630). Other sites of ubiquitination are not excluded (PubMed:20852630). 'Lys-63'-linked polyubiquitination by TRIM7 in response to growth factor signaling via the MEK/ERK pathway enhances protein stability (PubMed:25851810).
Arginine methylation by PRMT1 stabilizes RNF187 by facilitating K63-linked ubiquitin chain formation, and enables dimerization, c-Jun interaction and subsequent AP1 target gene expression.
Cellular localization
- Cytoplasm
- Nucleus
- Predominantly located in the cytoplasm. Shuttles between the cytoplasm and the nucleus.
Alternative names
E3 ubiquitin-protein ligase RNF187, RING domain AP1 coactivator 1, RING finger protein 187, RING-type E3 ubiquitin transferase RNF187, RACO-1, RNF187