Ring Finger Protein 4 (RNF4), also known as Small Nuclear Ring Finger Protein (SNURF), is a protein encoded by the RNF4 gene in humans. This protein is characterized by the presence of a RING finger domain, which is a specialized type of zinc finger that mediates protein-protein interactions. RNF4 functions primarily as an E3 ubiquitin ligase, playing a crucial role in the ubiquitination process, which tags proteins for degradation by the proteasome .
RNF4 contains a RING finger motif and four SUMO interaction motifs (SIMs) at the N-terminal. The RING domain is located at the C-terminal. The SIM domains have a preference for binding polySUMO chains, and RNF4 functions to ubiquitinate polysumoylated proteins, including promyelocytic leukemia protein (PML) .
As a transcription regulator, RNF4 interacts with and inhibits the activity of TRPS1, a transcription suppressor of GATA-mediated transcription. Additionally, RNF4 interacts with transcription repressor ZNF278/PATZ1, reducing the enhancement of androgen receptor-dependent transcription mediated by RNF4 .
RNF4 plays a significant role in several biological processes, including:
Studies of the mouse and rat counterparts of RNF4 suggest a role in spermatogenesis .
Recombinant human RNF4 is produced in Escherichia coli (E. coli) and is available as a single, non-glycosylated polypeptide chain containing 213 amino acids. It has a molecular mass of 23.7 kDa and is fused to a 23 amino acid His-tag at the N-terminus. The recombinant protein is purified using proprietary chromatographic techniques .