TFE3

From Wikipedia, the free encyclopedia

Transcription factor binding to IGHM enhancer 3

Identifiers

TFE3; RCCP2; TFEA

External IDs

OMIM: 314310 MGI: 98511 HomoloGene: 4755

Gene ontology
Molecular Function:	• transcription factor activity
Cellular Component:	• nucleus
Biological Process:	• transcription from RNA polymerase II promoter • regulation of osteoclast differentiation • positive regulation of transcription, DNA-dependent

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006521 (mRNA)
NP_006512 (protein)

NM_172472 (mRNA)
NP_766060 (protein)

Location

Chr X: 48.77 - 48.79 Mb

Chr X: 6.92 - 6.93 Mb

Pubmed search

[1]

[2]

Transcription factor binding to IGHM enhancer 3, also known as TFE3, is a human gene.^[1]

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]^[1]

[edit] References

^ ^a ^b Entrez Gene: TFE3 transcription factor binding to IGHM enhancer 3.

[edit] Further reading

Puck JM, Stewart CC, Henthorn PS (1991). "A high-frequency RFLP at the human TFE3 locus on the X chromosome.". Nucleic Acids Res. 19 (3): 684. PMID 1672758.
Henthorn PS, Stewart CC, Kadesch T, Puck JM (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. PMID 1685140.
Beckmann H, Kadesch T (1991). "The leucine zipper of TFE3 dictates helix-loop-helix dimerization specificity.". Genes Dev. 5 (6): 1057–66. 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. 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. 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. 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. 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. 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. 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. 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. PMID 11930005.