TFE3

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Transcription factor binding to IGHM enhancer 3
Identifiers
Symbols TFE3 ; RCCP2; RCCX1; TFEA; bHLHe33
External IDs OMIM314310 MGI98511 HomoloGene4755 GeneCards: TFE3 Gene
RNA expression pattern
PBB GE TFE3 206649 s at tn.png
PBB GE TFE3 212457 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 7030 209446
Ensembl ENSG00000068323 ENSMUSG00000000134
UniProt P19532 Q64092
RefSeq (mRNA) NM_001282142 NM_001105196
RefSeq (protein) NP_001269071 NP_001098666
Location (UCSC) Chr X:
49.03 – 49.04 Mb
Chr X:
7.76 – 7.78 Mb
PubMed search [1] [2]

Transcription factor E3 is a protein that in humans is encoded by the TFE3 gene.[1][2][3]

Function[edit]

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[edit]

TFE3 has been shown to interact with:

Translocations[edit]

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[edit]

  1. ^ 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. 
  2. ^ 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. ^ a b "Entrez Gene: TFE3 transcription factor binding to IGHM enhancer 3". 
  4. ^ Giangrande PH, Hallstrom TC, Tunyaplin C, Calame K, Nevins JR (Jun 2003). "Identification of E-box factor TFE3 as a functional partner for the E2F3 transcription factor". Mol. Cell. Biol. 23 (11): 3707–20. doi:10.1128/mcb.23.11.3707-3720.2003. PMC 155231. PMID 12748276. 
  5. ^ Steingrimsson E, Tessarollo L, Pathak B, Hou L, Arnheiter H, Copeland NG, Jenkins NA (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. 99 (7): 4477–82. doi:10.1073/pnas.072071099. PMC 123673. PMID 11930005. 
  6. ^ Mansky KC, Sulzbacher S, Purdom G, Nelsen L, Hume DA, Rehli M, Ostrowski MC (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. 71 (2): 304–10. PMID 11818452. 
  7. ^ Grinberg AV, Kerppola T (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. 278 (13): 11227–36. doi:10.1074/jbc.M211734200. PMID 12551947. 
  8. ^ Hua X, Miller ZA, Wu G, Shi Y, Lodish HF (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. 96 (23): 13130–5. doi:10.1073/pnas.96.23.13130. PMC 23912. PMID 10557285. 

Further reading[edit]