RNF187

RNF187 (Ring Finger Protein 187) is a protein coding gene. Gene Ontology annotations related to this gene include ligase activity and ubiquitin-protein transferase activity.

Full Name

Ring Finger Protein 187

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.

Biological Process

Biological Process innate immune responseManual Assertion Based On ExperimentIBA:GO_Central
Biological Process positive regulation of cell population proliferationISS:UniProtKB
Biological Process positive regulation of transcription, DNA-templatedManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process proteasome-mediated ubiquitin-dependent protein catabolic processManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process protein autoubiquitinationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process protein K48-linked ubiquitinationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process protein ubiquitinationManual Assertion Based On ExperimentIBA:GO_Central
Biological Process regulation of gene expressionManual Assertion Based On ExperimentIBA:GO_Central

Cellular Location

Cytoplasm
Nucleus
Predominantly located in the cytoplasm. Shuttles between the cytoplasm and the nucleus.

PTM

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.