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TFE3

From Wikipedia, the free encyclopedia

TFE3
Identifiers
AliasesTFE3, RCCP2, RCCX1, TFEA, bHLHe33, transcription factor binding to IGHM enhancer 3, MRXSPF
External IDsOMIM: 314310; MGI: 98511; HomoloGene: 4755; GeneCards: TFE3; OMA:TFE3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001282142
NM_006521

RefSeq (protein)

NP_001269071
NP_006512

Location (UCSC)Chr X: 49.03 – 49.04 MbChr X: 7.63 – 7.64 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Transcription factor E3 is a protein that in humans is encoded by the TFE3 gene.[5][6][7]

Function

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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][7]

Interactions

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TFE3 has been shown to interact with:

Translocations

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A proportion of renal carcinomas (RCC) that occur in young patients are associated with translocations involving the TFE3 gene at chromosome Xp11.2 PRCC[citation needed]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000068323Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000000134Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ 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.
  7. ^ a b "Entrez Gene: TFE3 transcription factor binding to IGHM enhancer 3".
  8. ^ 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.
  9. ^ 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. Bibcode:2002PNAS...99.4477S. doi:10.1073/pnas.072071099. PMC 123673. PMID 11930005.
  10. ^ 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. doi:10.1189/jlb.71.2.304. PMID 11818452. S2CID 22801820.
  11. ^ 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.
  12. ^ 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. Bibcode:1999PNAS...9613130H. doi:10.1073/pnas.96.23.13130. PMC 23912. PMID 10557285.

Further reading

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