TFE3
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| Transcription factor binding to IGHM enhancer 3 | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | TFE3; RCCP2; RCCX1; TFEA; bHLHe33 | ||||||||||||
| External IDs | OMIM: 314310 MGI: 98511 HomoloGene: 4755 GeneCards: TFE3 Gene | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| More reference expression data | |||||||||||||
| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 7030 | 209446 | |||||||||||
| Ensembl | ENSG00000068323 | ENSMUSG00000000134 | |||||||||||
| UniProt | P19532 | Q64092 | |||||||||||
| RefSeq (mRNA) | NM_006521 | NM_001105196 | |||||||||||
| RefSeq (protein) | NP_006512 | NP_001098666 | |||||||||||
| Location (UCSC) | Chr HG1436_HG1432_PATCH: 48.89 – 48.9 Mb | Chr X: 7.76 – 7.78 Mb | |||||||||||
| PubMed search | |||||||||||||
Transcription factor E3 is a protein that in humans is encoded by the TFE3 gene.[1][2][3]
TFE3, a member of the helix-loop-helix family of transcription factors, binds to the mu-E3 motif of the immunoglobulin heavy-chain enhancer and is expressed in many cell types (Henthorn et al., 1991).[supplied by OMIM][3]
Interactions
TFE3 has been shown to interact with E2F3,[4] Mothers against decapentaplegic homolog 3[5][6] and Microphthalmia-associated transcription factor.[7][8]
Translocations
A proportion of renal carcinomas (RCC) that occur in young patients are associated with translocations involving the TFE3 gene at chromosome Xp11.2 PRCC
References
- ↑ Puck JM, Stewart CC, Henthorn PS (May 1991). "A high-frequency RFLP at the human TFE3 locus on the X chromosome". Nucleic Acids Res 19 (3): 684. doi:10.1093/nar/19.3.684-a. PMC 333678. PMID 1672758.
- ↑ Henthorn PS, Stewart CC, Kadesch T, Puck JM (Feb 1992). "The gene encoding human TFE3, a transcription factor that binds the immunoglobulin heavy-chain enhancer, maps to Xp11.22". Genomics 11 (2): 374–8. doi:10.1016/0888-7543(91)90145-5. PMID 1685140.
- ↑ 3.0 3.1 "Entrez Gene: TFE3 transcription factor binding to IGHM enhancer 3".
- ↑ Giangrande, Paloma H; Hallstrom Timothy C, Tunyaplin Chainarong, Calame Kathryn, Nevins Joseph R (Jun 2003). "Identification of E-box factor TFE3 as a functional partner for the E2F3 transcription factor". Mol. Cell. Biol. (United States) 23 (11): 3707–20. doi:10.1128/MCB.23.11.3707-3720.2003. ISSN 0270-7306. PMC 155231. PMID 12748276.
- ↑ Grinberg, Asya V; Kerppola Tom (Mar 2003). "Both Max and TFE3 cooperate with Smad proteins to bind the plasminogen activator inhibitor-1 promoter, but they have opposite effects on transcriptional activity". J. Biol. Chem. (United States) 278 (13): 11227–36. doi:10.1074/jbc.M211734200. ISSN 0021-9258. PMID 12551947.
- ↑ Hua, X; Miller Z A, Wu G, Shi Y, Lodish H F (Nov 1999). "Specificity in transforming growth factor beta-induced transcription of the plasminogen activator inhibitor-1 gene: interactions of promoter DNA, transcription factor muE3, and Smad proteins". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (23): 13130–5. doi:10.1073/pnas.96.23.13130. ISSN 0027-8424. PMC 23912. PMID 10557285.
- ↑ Steingrimsson, Eiríkur; Tessarollo Lino, Pathak Bhavani, Hou Ling, Arnheiter Heinz, Copeland Neal G, Jenkins Nancy A (Apr 2002). "Mitf and Tfe3, two members of the Mitf-Tfe family of bHLH-Zip transcription factors, have important but functionally redundant roles in osteoclast development". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (7): 4477–82. doi:10.1073/pnas.072071099. ISSN 0027-8424. PMC 123673. PMID 11930005.
- ↑ Mansky, Kim C; Sulzbacher Sabine, Purdom Georgia, Nelsen Lori, Hume David A, Rehli Michael, Ostrowski Michael C (Feb 2002). "The microphthalmia transcription factor and the related helix-loop-helix zipper factors TFE-3 and TFE-C collaborate to activate the tartrate-resistant acid phosphatase promoter". J. Leukoc. Biol. (United States) 71 (2): 304–10. ISSN 0741-5400. PMID 11818452.
Further reading
- Beckmann H, Kadesch T (1991). "The leucine zipper of TFE3 dictates helix-loop-helix dimerization specificity". Genes Dev. 5 (6): 1057–66. doi:10.1101/gad.5.6.1057. PMID 2044953.
- Beckmann H, Su LK, Kadesch T (1990). "TFE3: a helix-loop-helix protein that activates transcription through the immunoglobulin enhancer muE3 motif". Genes Dev. 4 (2): 167–79. doi:10.1101/gad.4.2.167. PMID 2338243.
- Zhao GQ, Zhao Q, Zhou X, et al. (1993). "TFEC, a basic helix-loop-helix protein, forms heterodimers with TFE3 and inhibits TFE3-dependent transcription activation". Mol. Cell. Biol. 13 (8): 4505–12. PMC 360062. PMID 8336698.
- Sidhar SK, Clark J, Gill S, et al. (1997). "The t(X;1)(p11.2;q21.2) translocation in papillary renal cell carcinoma fuses a novel gene PRCC to the TFE3 transcription factor gene". Hum. Mol. Genet. 5 (9): 1333–8. doi:10.1093/hmg/5.9.1333. PMID 8872474.
- Weterman MA, Wilbrink M, Geurts van Kessel A (1997). "Fusion of the transcription factor TFE3 gene to a novel gene, PRCC, in t(X;1)(p11;q21)-positive papillary renal cell carcinomas". Proc. Natl. Acad. Sci. U.S.A. 93 (26): 15294–8. doi:10.1073/pnas.93.26.15294. PMC 26398. PMID 8986805.
- Clark J, Lu YJ, Sidhar SK, et al. (1997). "Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3 gene in papillary renal cell carcinoma". Oncogene 15 (18): 2233–9. doi:10.1038/sj.onc.1201394. PMID 9393982.
- Hua X, Liu X, Ansari DO, Lodish HF (1998). "Synergistic cooperation of TFE3 and smad proteins in TGF-beta-induced transcription of the plasminogen activator inhibitor-1 gene". Genes Dev. 12 (19): 3084–95. doi:10.1101/gad.12.19.3084. PMC 317197. PMID 9765209.
- Steingrímsson E, Tessarollo L, Reid SW, et al. (1999). "The bHLH-Zip transcription factor Tfeb is essential for placental vascularization". Development 125 (23): 4607–16. PMID 9806910.
- Hua X, Miller ZA, Wu G, et al. (1999). "Specificity in transforming growth factor beta-induced transcription of the plasminogen activator inhibitor-1 gene: interactions of promoter DNA, transcription factor muE3, and Smad proteins". Proc. Natl. Acad. Sci. U.S.A. 96 (23): 13130–5. doi:10.1073/pnas.96.23.13130. PMC 23912. PMID 10557285.
- Weterman MJ, van Groningen JJ, Jansen A, van Kessel AG (2000). "Nuclear localization and transactivating capacities of the papillary renal cell carcinoma-associated TFE3 and PRCC (fusion) proteins". Oncogene 19 (1): 69–74. doi:10.1038/sj.onc.1203255. PMID 10644981.
- Hua X, Miller ZA, Benchabane H, et al. (2000). "Synergism between transcription factors TFE3 and Smad3 in transforming growth factor-beta-induced transcription of the Smad7 gene". J. Biol. Chem. 275 (43): 33205–8. doi:10.1074/jbc.C000568200. PMID 10973944.
- Ladanyi M, Lui MY, Antonescu CR, et al. (2001). "The der(17)t(X;17)(p11;q25) of human alveolar soft part sarcoma fuses the TFE3 transcription factor gene to ASPL, a novel gene at 17q25". Oncogene 20 (1): 48–57. doi:10.1038/sj.onc.1204074. PMID 11244503.
- Weterman MA, van Groningen JJ, den Hartog A, Geurts van Kessel A (2001). "Transformation capacities of the papillary renal cell carcinoma-associated PRCCTFE3 and TFE3PRCC fusion genes". Oncogene 20 (12): 1414–24. doi:10.1038/sj.onc.1204213. PMID 11313885.
- Heimann P, El Housni H, Ogur G, et al. (2001). "Fusion of a novel gene, RCC17, to the TFE3 gene in t(X;17)(p11.2;q25.3)-bearing papillary renal cell carcinomas". Cancer Res. 61 (10): 4130–5. PMID 11358836.
- Chung MC, Kim HK, Kawamoto S (2001). "TFEC can function as a transcriptional activator of the nonmuscle myosin II heavy chain-A gene in transfected cells". Biochemistry 40 (30): 8887–97. doi:10.1021/bi002847d. PMID 11467950.
- Dintilhac A, Bernués J (2002). "HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences". J. Biol. Chem. 277 (9): 7021–8. doi:10.1074/jbc.M108417200. PMID 11748221.
- Kawata Y, Suzuki H, Higaki Y, et al. (2002). "bcn-1 Element-dependent activation of the laminin gamma 1 chain gene by the cooperative action of transcription factor E3 (TFE3) and Smad proteins". J. Biol. Chem. 277 (13): 11375–84. doi:10.1074/jbc.M111284200. PMID 11801598.
- Steingrimsson E, Tessarollo L, Pathak B, et al. (2002). "Mitf and Tfe3, two members of the Mitf-Tfe family of bHLH-Zip transcription factors, have important but functionally redundant roles in osteoclast development". Proc. Natl. Acad. Sci. U.S.A. 99 (7): 4477–82. doi:10.1073/pnas.072071099. PMC 123673. PMID 11930005.
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