TRIM27

From Wikipedia, the free encyclopedia

Tripartite motif-containing 27

Identifiers

TRIM27; RFP; RNF76

External IDs

OMIM: 602165 MGI: 97904 HomoloGene: 4748

Gene ontology
Molecular Function:	• DNA binding • transmembrane receptor protein tyrosine kinase activity • protein binding • zinc ion binding • metal ion binding
Cellular Component:	• intracellular • membrane fraction • nucleus • cytoplasm • integral to plasma membrane
Biological Process:	• transcription • regulation of transcription, DNA-dependent • spermatogenesis • cell proliferation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_030950 (mRNA)
NP_112212 (protein)

NM_009054 (mRNA)
NP_033080 (protein)

Location

Chr c6_COX: 29.02 - 29.04 Mb

Chr 13: 21.19 - 21.2 Mb

Pubmed search

[1]

[2]

Tripartite motif-containing 27, also known as TRIM27, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: TRIM27 tripartite motif-containing 27.

[edit] Further reading

Borden KL (1999). "RING fingers and B-boxes: zinc-binding protein-protein interaction domains.". Biochem. Cell Biol. 76 (2-3): 351–8. PMID 9923704.
Isomura T, Tamiya-Koizumi K, Suzuki M, et al. (1992). "RFP is a DNA binding protein associated with the nuclear matrix.". Nucleic Acids Res. 20 (20): 5305–10. PMID 1437549.
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. PMID 2734021.
Takahashi M, Cooper GM (1987). "ret transforming gene encodes a fusion protein homologous to tyrosine kinases.". Mol. Cell. Biol. 7 (4): 1378–85. PMID 3037315.
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. PMID 3078962.
Takahashi M, Inaguma Y, Hiai H, Hirose F (1988). "Developmentally regulated expression of a human "finger"-containing gene encoded by the 5' half of the ret transforming gene.". Mol. Cell. Biol. 8 (4): 1853–6. PMID 3380101.
Vernet C, Boretto J, Mattéi MG, et al. (1994). "Evolutionary study of multigenic families mapping close to the human MHC class I region.". J. Mol. Evol. 37 (6): 600–12. PMID 8114113.
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 ( Pt 14): 1563–71. PMID 9247190.
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 ( Pt 10): 1319–29. PMID 9570750.
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 ( Pt 19): 3331–42. PMID 10504338.
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. PMID 10976108.
Reymond A, Meroni G, Fantozzi A, et al. (2001). "The tripartite motif family identifies cell compartments.". EMBO J. 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMID 11331580.
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. PMID 12445133.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
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. PMID 12787916.
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. PMID 12807881.
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. PMID 14530259.
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. PMID 14574404.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.