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Gene Review

TRIM27  -  tripartite motif containing 27

Homo sapiens

Synonyms: RFP, RING finger protein 76, RNF76, Ret finger protein, Tripartite motif-containing protein 27, ...
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Disease relevance of TRIM27

  • Furthermore, ablation of RFP in U2OS osteosarcoma cells augments a transcriptional program indicative of lineage-specific differentiation in response to Rb [1].
  • Using AH7974 (rat ascites hepatoma) and Raji (human Burkitt lymphoma) cells, we demonstrated strong association of RFP with the nuclear matrix [2].
  • To further characterize the RFP protein, we developed a polyclonal antibody against the product synthesized from a fragment of the RFP cDNA expressed in Escherichia coli [2].
  • RFP immunoreactivity was seen uniformly and specifically in 12 of the 13 pure seminomas examined [3].
  • The catalytic activities of Ret tyrosine kinases as the products of oncogene RET with multiple endocrine neoplasia type 2A (Ret-MEN2A) or 2B (Ret-MEN2B) mutations and the hybrid gene from c-RET and RFP (Rfp-Ret) were higher than those of c-Ret [4].

Psychiatry related information on TRIM27

  • Extending the RFP to a matrix evaluation form allows input from all persons involved in the decision-making process and displays the information in a clear manner, making the overall decision much easier [5].

High impact information on TRIM27


Chemical compound and disease context of TRIM27


Biological context of TRIM27

  • Here we show that RFP interacts with Enhancer of Polycomb (EPC) and strongly represses the gene transcription [9].
  • Using the luciferase reporter-gene assay, we found that they repress the gene transcription activity independent of the differences of enhancers and promoters used, although the repressive activity of RFP was much stronger than that of EPC [9].
  • These results suggested that RFP may be involved in the epigenetic gene silencing mechanism cooperating with Polycomb group proteins and that EPC is a unique molecule with both repressive and transactivating activities [9].
  • These results demonstrate that the intracellular location and the transcriptional activity of RFP are modified by PIAS proteins which possess SUMO E3 ligase activities and suggest that they may play a co-operative role in spermatogenesis [10].
  • Moreover, in situ hybridization shows that RFP, butyrophilin, and MOG map to the human chromosome 6p21.3-6p22 region and are thus close to the MHC class I genes [11].

Anatomical context of TRIM27


Associations of TRIM27 with chemical compounds

  • RET finger protein (RFP) belongs to the large B-box RING finger protein family and is known to become oncogenic by fusion with RET tyrosine kinase [9].
  • When treated with retinoic acid, rfp reassociates with the NBs in a pattern similar to non APL cells [13].
  • Transcriptional repression by RFP was trichostatin A sensitive and did not involve an Id-like mechanism or ubiquitination with subsequent degradation of bHLH proteins [14].
  • However, when the host mice were pretreated with cyclophosphamide, the HCT-116-GFP-RFP cells also survived and formed colonies in the liver after portal vein injection [15].
  • Mutation of this NES or treatment with leptomycin B abrogated the nuclear export of RFP in NIH3T3 cells [16].

Co-localisations of TRIM27

  • Additionally, we found that rfp colocalizes with PML-RARA protein produced in APL patients [13].

Regulatory relationships of TRIM27

  • To obtain the dual-color cells, red fluorescent protein (RFP) was expressed in the cytoplasm of HT-1080 human fibrosarcoma cells, and green fluorescent protein (GFP) linked to histone H2B was expressed in the nucleus [17].
  • The RFP-expressing hMSCs were enriched by high-speed flow cytometry and maintained their potential to differentiate along adipogenic or osteogenic lineages [18].

Other interactions of TRIM27

  • Microspherule protein 1, Mi-2beta, and RET finger protein associate in the nucleolus and up-regulate ribosomal gene transcription [19].
  • These results suggest that rfp, along with the other known/unknown components of PML NBs, have an important role in regulating cellular growth and differentiation [13].
  • RFP functions as a transcriptional repressor and associates with Enhancer of Polycomb 1 (EPC1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex [10].
  • Co-localization and association of Mi-2, RFP, and histone deacetylase 1 suggested that these proteins cooperate in transcriptional repression [12].
  • Mi-2 beta associates with BRG1 and RET finger protein at the distinct regions with transcriptional activating and repressing abilities [12].

Analytical, diagnostic and therapeutic context of TRIM27


  1. Selective ablation of retinoblastoma protein function by the RET finger protein. Krützfeldt, M., Ellis, M., Weekes, D.B., Bull, J.J., Eilers, M., Vivanco, M.D., Sellers, W.R., Mittnacht, S. Mol. Cell (2005) [Pubmed]
  2. RFP is a DNA binding protein associated with the nuclear matrix. Isomura, T., Tamiya-Koizumi, K., Suzuki, M., Yoshida, S., Taniguchi, M., Matsuyama, M., Ishigaki, T., Sakuma, S., Takahashi, M. Nucleic Acids Res. (1992) [Pubmed]
  3. Differential expression of RET finger protein in testicular germ cell tumors. Tezel, G., Nagasaka, T., Shimono, Y., Takahashi, M. Pathol. Int. (2002) [Pubmed]
  4. Molecular mechanism of activation and superactivation of Ret tyrosine kinases by ultraviolet light irradiation. Kato, M., Iwashita, T., Akhand, A.A., Liu, W., Takeda, K., Takeuchi, K., Yoshihara, M., Hossain, K., Wu, J., Du, J., Oh, C., Kawamoto, Y., Suzuki, H., Takahashi, M., Nakashima, I. Antioxid. Redox Signal. (2000) [Pubmed]
  5. Two viewpoints: the preparation of a request for proposal. Viewpoint #2. Shanks, C.K. Journal (American Medical Record Association) (1988) [Pubmed]
  6. BDNF release from single cells elicits local dendritic growth in nearby neurons. Horch, H.W., Katz, L.C. Nat. Neurosci. (2002) [Pubmed]
  7. Assembly and trafficking of caveolar domains in the cell: caveolae as stable, cargo-triggered, vesicular transporters. Tagawa, A., Mezzacasa, A., Hayer, A., Longatti, A., Pelkmans, L., Helenius, A. J. Cell Biol. (2005) [Pubmed]
  8. Real-time whole-body imaging of an orthotopic metastatic prostate cancer model expressing red fluorescent protein. Yang, M., Jiang, P., Yamamoto, N., Li, L., Geller, J., Moossa, A.R., Hoffman, R.M. Prostate (2005) [Pubmed]
  9. RET finger protein is a transcriptional repressor and interacts with enhancer of polycomb that has dual transcriptional functions. Shimono, Y., Murakami, H., Hasegawa, Y., Takahashi, M. J. Biol. Chem. (2000) [Pubmed]
  10. PIAS proteins are involved in the SUMO-1 modification, intracellular translocation and transcriptional repressive activity of RET finger protein. Matsuura, T., Shimono, Y., Kawai, K., Murakami, H., Urano, T., Niwa, Y., Goto, H., Takahashi, M. Exp. Cell Res. (2005) [Pubmed]
  11. Evolutionary study of multigenic families mapping close to the human MHC class I region. Vernet, C., Boretto, J., Mattéi, M.G., Takahashi, M., Jack, L.J., Mather, I.H., Rouquier, S., Pontarotti, P. J. Mol. Evol. (1993) [Pubmed]
  12. Mi-2 beta associates with BRG1 and RET finger protein at the distinct regions with transcriptional activating and repressing abilities. Shimono, Y., Murakami, H., Kawai, K., Wade, P.A., Shimokata, K., Takahashi, M. J. Biol. Chem. (2003) [Pubmed]
  13. Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML. Cao, T., Duprez, E., Borden, K.L., Freemont, P.S., Etkin, L.D. J. Cell. Sci. (1998) [Pubmed]
  14. RFP represses transcriptional activation by bHLH transcription factors. Bloor, A.J., Kotsopoulou, E., Hayward, P., Champion, B.R., Green, A.R. Oncogene (2005) [Pubmed]
  15. Dual-color imaging of nuclear-cytoplasmic dynamics, viability, and proliferation of cancer cells in the portal vein area. Tsuji, K., Yamauchi, K., Yang, M., Jiang, P., Bouvet, M., Endo, H., Kanai, Y., Yamashita, K., Moossa, A.R., Hoffman, R.M. Cancer Res. (2006) [Pubmed]
  16. Intracellular localization of the Ret finger protein depends on a functional nuclear export signal and protein kinase C activation. Harbers, M., Nomura, T., Ohno, S., Ishii, S. J. Biol. Chem. (2001) [Pubmed]
  17. Cellular dynamics visualized in live cells in vitro and in vivo by differential dual-color nuclear-cytoplasmic fluorescent-protein expression. Yamamoto, N., Jiang, P., Yang, M., Xu, M., Yamauchi, K., Tsuchiya, H., Tomita, K., Wahl, G.M., Moossa, A.R., Hoffman, R.M. Cancer Res. (2004) [Pubmed]
  18. Transfer and stable transgene expression of a mammalian artificial chromosome into bone marrow-derived human mesenchymal stem cells. Vanderbyl, S., MacDonald, G.N., Sidhu, S., Gung, L., Telenius, A., Perez, C., Perkins, E. Stem Cells (2004) [Pubmed]
  19. Microspherule protein 1, Mi-2beta, and RET finger protein associate in the nucleolus and up-regulate ribosomal gene transcription. Shimono, K., Shimono, Y., Shimokata, K., Ishiguro, N., Takahashi, M. J. Biol. Chem. (2005) [Pubmed]
  20. Characterization of the Interleukin (IL)-6 Inhibitor IL-6-RFP: FUSED RECEPTOR DOMAINS ACT AS HIGH AFFINITY CYTOKINE-BINDING PROTEINS. Metz, S., Wiesinger, M., Vogt, M., Lauks, H., Schmalzing, G., Heinrich, P.C., M??ller-Newen, G. J. Biol. Chem. (2007) [Pubmed]
  21. Role for O-glycosylation of RFP in the interaction with enhancer of polycomb. Tezel, G., Shimono, Y., Murakumo, Y., Kawai, K., Fukuda, T., Iwahashi, N., Takahashi, M. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  22. Different nuclear/cytoplasmic distributions of RET finger protein in different cell types. Tezel, G., Nagasaka, T., Iwahashi, N., Asai, N., Iwashita, T., Sakata, K., Takahashi, M. Pathol. Int. (1999) [Pubmed]
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