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TFEC  -  transcription factor EC

Homo sapiens

Synonyms: BHLHE34, Class E basic helix-loop-helix protein 34, TCFEC, TFE-C, TFEC-L, ...
 
 
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Disease relevance of TFEC

 

High impact information on TFEC

 

Biological context of TFEC

  • TFECL contains an acidic domain that corresponds to a transcriptional activation domain of TFE3 but its equivalent region is deleted in rat TFEC [1].
  • Furthermore, we observed that a considerable proportion of the TFEC transcripts splice out protein-coding exons, resulting in transcription factor isoforms lacking one or more functional domains, primarily the basic region and/or the AAD [4].
  • In transient transfection assays, TFE3 and TFEC could collaborate with MITF to superactivate the tartrate resistant acid phosphatase (TRAP) promoter, a target for MITF in osteoclasts [3].
  • The extracellular release of TFECP from T. foetus suggests that it is a potential virulence factor in bovine trichomoniasis [5].
 

Anatomical context of TFEC

  • A novel TFEC transcript (TFEC-C) encodes an N-terminally truncated TFEC isoform lacking the acidic activation domain (AAD), and is exclusively expressed in kidney and small intestine [4].
  • These results indicate that although different isoforms of MITF appear to be functionally similar, the TFE3 and TFEC proteins may collaborate with MITF to efficiently regulate expression of target genes in osteoclasts [3].
 

Associations of TFEC with chemical compounds

  • These results indicate that this enzyme (TFECP) is a distinct cysteine proteinase [5].
  • Bacitracin-purified T. foetus extracellular cysteine proteinase (TFECP) was separated in a denaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis gel, electroblotted, and a 31-kDa band cut out for amino acid sequencing [5].
 

Other interactions of TFEC

  • Furthermore, cDNA cloning by polymerase chain reaction yielded cDNAs for two TFEC isoforms, designated TFEC-l and TFEC-s, which are generated by alternative pre-mRNA splicing [6].
  • We found that, similar to the MiTF gene, the genes for TFEB and TFEC contain multiple alternative first exons with restricted and differential tissue distributions [4].
 

Analytical, diagnostic and therapeutic context of TFEC

References

  1. Molecular cloning of cDNA encoding a human TFEC isoform, a newly identified transcriptional regulator. Yasumoto, K., Shibahara, S. Biochim. Biophys. Acta (1997) [Pubmed]
  2. TFEC, a basic helix-loop-helix protein, forms heterodimers with TFE3 and inhibits TFE3-dependent transcription activation. Zhao, G.Q., Zhao, Q., Zhou, X., Mattei, M.G., de Crombrugghe, B. Mol. Cell. Biol. (1993) [Pubmed]
  3. 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. Mansky, K.C., Sulzbacher, S., Purdom, G., Nelsen, L., Hume, D.A., Rehli, M., Ostrowski, M.C. J. Leukoc. Biol. (2002) [Pubmed]
  4. Regulation of the MiTF/TFE bHLH-LZ transcription factors through restricted spatial expression and alternative splicing of functional domains. Kuiper, R.P., Schepens, M., Thijssen, J., Schoenmakers, E.F., van Kessel, A.G. Nucleic Acids Res. (2004) [Pubmed]
  5. Characterization of extracellular proteinases of Tritrichomonas foetus. Thomford, J.W., Talbot, J.A., Ikeda, J.S., Corbeil, L.B. J. Parasitol. (1996) [Pubmed]
  6. TFEC can function as a transcriptional activator of the nonmuscle myosin II heavy chain-A gene in transfected cells. Chung, M.C., Kim, H.K., Kawamoto, S. Biochemistry (2001) [Pubmed]
 
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