TFE3

Transcription factor binding to IGHM enhancer 3
Identifiers
Symbols	TFE3; RCCP2; TFEA; bHLHe33
External IDs	OMIM: 314310 MGI: 98511 HomoloGene: 4755 GeneCards: TFE3 Gene
Gene Ontology Molecular function • DNA binding • sequence-specific DNA binding transcription factor activity • protein binding • transcription regulatory region DNA binding • protein heterodimerization activity Cellular component • nucleus • nucleolus • cytoplasm Biological process • transcription, DNA-dependent • transcription, DNA-dependent • regulation of transcription, DNA-dependent • humoral immune response • regulation of osteoclast differentiation • positive regulation of transcription from RNA polymerase II promoter Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7030	209446
Ensembl	ENSG00000068323	ENSMUSG00000000134
UniProt	P19532	Q05BT8
RefSeq (mRNA)	NM_006521	NM_172472
RefSeq (protein)	NP_006512	NP_766060
Location (UCSC)	Chr X: 48.89 – 48.9 Mb	Chr X: 7.34 – 7.35 Mb
PubMed search	[1]	[2]

Transcription factor E3 is a protein that in humans is encoded by the TFE3 gene.

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]

Interactions

TFE3 has been shown to interact with E2F3, Mothers against decapentaplegic homolog 3 and Microphthalmia-associated transcription factor.

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=360062. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=26398. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=317197. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=23912. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=123673.