Zinc finger protein RFP is a protein that in humans is encoded by the TRIM27gene.[1][2]
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.[2]
↑Vernet C, Boretto J, Mattei MG, Takahashi M, Jack LJ, Mather IH, Rouquier S, Pontarotti P (Mar 1994). "Evolutionary study of multigenic families mapping close to the human MHC class I region". J Mol Evol. 37 (6): 600–12. Bibcode:1993JMolE..37..600V. doi:10.1007/bf00182746. PMID8114113.
↑Cao, T; Duprez E; Borden K L; Freemont P S; Etkin L D (May 1998). "Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML". J. Cell Sci. ENGLAND. 111 (10): 1319–29. ISSN0021-9533. PMID9570750.
↑Morris-Desbois, C; Bochard V; Reynaud C; Jalinot P (Oct 1999). "Interaction between the Ret finger protein and the Int-6 gene product and co-localisation into nuclear bodies". J. Cell Sci. ENGLAND. 112 (19): 3331–42. ISSN0021-9533. PMID10504338.
Ishizaka Y, Ochiai M, Tahira T, et al. (1989). "Activation of the ret-II oncogene without a sequence encoding a transmembrane domain and transforming activity of two ret-II oncogene products differing in carboxy-termini due to alternative splicing". Oncogene. 4 (6): 789–94. PMID2734021.
Takahashi M, Buma Y, Iwamoto T, et al. (1990). "Cloning and expression of the ret proto-oncogene encoding a tyrosine kinase with two potential transmembrane domains". Oncogene. 3 (5): 571–8. PMID3078962.
Cao T, Borden KL, Freemont PS, Etkin LD (1997). "Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution". J. Cell Sci. 110 (14): 1563–71. PMID9247190.
Cao T, Duprez E, Borden KL, et al. (1998). "Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML". J. Cell Sci. 111 (10): 1319–29. PMID9570750.
Morris-Desbois C, Bochard V, Reynaud C, Jalinot P (1999). "Interaction between the Ret finger protein and the Int-6 gene product and co-localisation into nuclear bodies". J. Cell Sci. 112 (19): 3331–42. PMID10504338.
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.
Tezel G, Nagasaka T, Shimono Y, Takahashi M (2003). "Differential expression of RET finger protein in testicular germ cell tumors". Pathol. Int. 52 (10): 623–7. doi:10.1046/j.1440-1827.2002.01401.x. PMID12445133.
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.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID14574404.