Zinc finger protein RFP is a protein that in humans is encoded by the TRIM27gene.
This gene encodes a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localizes to the nuclear matrix. It interacts with the enhancer of polycomb protein and represses gene transcription. It is also thought to be involved in the differentiation of male germ cells. Fusion of the N-terminus of this protein with the truncated C-terminus of the RET gene product has been shown to result in production of the ret transforming protein.
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Shimono Y, Murakami H, Hasegawa Y, Takahashi M (2001). "RET finger protein is a transcriptional repressor and interacts with enhancer of polycomb that has dual transcriptional functions". J. Biol. Chem.275 (50): 39411–9. doi:10.1074/jbc.M006585200. PMID10976108.
Saenko V, Rogounovitch T, Shimizu-Yoshida Y, et al. (2003). "Novel tumorigenic rearrangement, Delta rfp/ret, in a papillary thyroid carcinoma from externally irradiated patient". Mutat. Res.527 (1–2): 81–90. doi:10.1016/S0027-5107(03)00056-3. PMID12787916.
Dho SH, Kwon KS (2003). "The Ret finger protein induces apoptosis via its RING finger-B box-coiled-coil motif". J. Biol. Chem.278 (34): 31902–8. doi:10.1074/jbc.M304062200. PMID12807881.
Shimono Y, Murakami H, Kawai K, et al. (2004). "Mi-2 beta associates with BRG1 and RET finger protein at the distinct regions with transcriptional activating and repressing abilities". J. Biol. Chem.278 (51): 51638–45. doi:10.1074/jbc.M309198200. PMID14530259.