TRIM27

TRIM27
Identifiers
Aliases	TRIM27, RFP, RNF76, tripartite motif containing 27
External IDs	OMIM: 602165; MGI: 97904; HomoloGene: 111010; GeneCards: TRIM27; OMA:TRIM27 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p22.1 Start 28,903,002 bp End 28,923,988 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13 A3.1|13 7.67 cM Start 21,363,615 bp End 21,378,894 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube body of pancreas right lobe of liver endometrium canal of the cervix blood spleen pituitary gland anterior pituitary granulocyte Top expressed in internal carotid artery Paneth cell external carotid artery condyle fossa primary oocyte Rostral migratory stream spermatid primitive streak lacrimal gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding zinc ion binding metal ion binding ubiquitin-protein transferase activity protein binding nucleic acid binding transmembrane receptor protein tyrosine kinase activity identical protein binding transferase activity ubiquitin protein ligase activity SUMO transferase activity Cellular component cytoplasm endosome PML body nuclear membrane membrane integral component of plasma membrane intracellular anatomical structure nucleoplasm retromer complex early endosome nucleus fibrillar center nucleolus cytosol Biological process regulation of transcription, DNA-templated negative regulation of adaptive immune response negative regulation of protein kinase activity protein K63-linked ubiquitination protein trimerization positive regulation of DNA-binding transcription factor activity transcription, DNA-templated negative regulation of calcium ion import negative regulation of gene expression, epigenetic retrograde transport, endosome to Golgi spermatogenesis Arp2/3 complex-mediated actin nucleation negative regulation of tumor necrosis factor production cell population proliferation peptidyl-tyrosine phosphorylation negative regulation of transcription by RNA polymerase II negative regulation of viral transcription innate immune response positive regulation of actin nucleation protein sumoylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5987 19720 Ensembl ENSG00000229006 ENSG00000233948 ENSG00000204713 ENSG00000215641 ENSG00000237071 ENSG00000237462 ENSG00000234495 ENSMUSG00000021326 UniProt P14373 Q62158 RefSeq (mRNA) NM_030950 NM_006510 NM_009054 RefSeq (protein) NP_006501 NP_033080 Location (UCSC) Chr 6: 28.9 – 28.92 Mb Chr 13: 21.36 – 21.38 Mb PubMed search
Wikidata
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Zinc finger protein RFP is a protein that in humans is encoded by the TRIM27 gene.

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.

Interactions

TRIM27 has been shown to interact with PRAM1 and EIF3S6.

Further reading

• Borden KL (1999). "RING fingers and B-boxes: zinc-binding protein-protein interaction domains". Biochem. Cell Biol. 76 (2–3): 351–8. doi:10.1139/bcb-76-2-3-351. 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. doi:10.1093/nar/20.20.5305. PMC 334335. 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. doi:10.1128/mcb.7.4.1378. PMC 365224. 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. doi:10.1128/mcb.8.4.1853. PMC 363354. PMID 3380101.
• 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. doi:10.1242/jcs.110.14.1563. 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 (10): 1319–29. doi:10.1242/jcs.111.10.1319. 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 (19): 3331–42. doi:10.1242/jcs.112.19.3331. 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. PMC 125245. 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. doi:10.1046/j.1440-1827.2002.01401.x. PMID 12445133. S2CID 20915447.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. doi:10.1016/S0027-5107(03)00056-3. 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. Bibcode:2003Natur.425..805M. 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. PMC 528928. PMID 15489334.