TCF3

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Transcription factor 3
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols TCF3 ; E2A; E47; ITF1; TCF-3; VDIR; bHLHb21
External IDs OMIM147141 MGI98510 HomoloGene2408 GeneCards: TCF3 Gene
RNA expression pattern
PBB GE TCF3 209151 x at tn.png
PBB GE TCF3 209152 s at tn.png
PBB GE TCF3 209153 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6929 21423
Ensembl ENSG00000071564 ENSMUSG00000020167
UniProt P15923 P15806
RefSeq (mRNA) NM_001136139 NM_001164147
RefSeq (protein) NP_001129611 NP_001157619
Location (UCSC) Chr 19:
1.61 – 1.65 Mb
Chr 10:
80.41 – 80.43 Mb
PubMed search [1] [2]

Transcription factor 3 (E2A immunoglobulin enhancer-binding factors E12/E47), also known as TCF3, is a protein that in humans is encoded by the TCF3 gene.[1][2][3] TCF3 has been shown to directly enhance Hes1 (a well-known target of Notch signaling) expression.[4]


Interactions[edit]

TCF3 has been shown to interact with ID3,[5][6] LYL1,[7] Twist transcription factor,[8] PCAF,[9] LMX1A,[10] LDB1,[11] ELK3,[12] CBFA2T3,[11] MyoD,[6][13] EP300,[9] CREB-binding protein,[9] MAPKAPK3,[14] Myogenin,[6][15] TAL1[11][16] and UBE2I.[17]

References[edit]

  1. ^ "Entrez Gene: TCF3". 
  2. ^ Henthorn P, McCarrick-Walmsley R, Kadesch T (February 1990). "Sequence of the cDNA encoding ITF-1, a positive-acting transcription factor". Nucleic Acids Res. 18 (3): 677. doi:10.1093/nar/18.3.677. PMC 333499. PMID 2308859. 
  3. ^ Kamps MP, Murre C, Sun XH, Baltimore D (February 1990). "A new homeobox gene contributes the DNA binding domain of the t(1;19) translocation protein in pre-B ALL". Cell 60 (4): 547–55. doi:10.1016/0092-8674(90)90658-2. PMID 1967983. 
  4. ^ E proteins and Notch signaling cooperate to promote T cell lineage specification and commitment
  5. ^ Deed, R W; Jasiok M, Norton J D (April 1998). "Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells". J. Biol. Chem. (UNITED STATES) 273 (14): 8278–86. doi:10.1074/jbc.273.14.8278. ISSN 0021-9258. PMID 9525934. 
  6. ^ a b c Langlands, K; Yin X, Anand G, Prochownik E V (August 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. (UNITED STATES) 272 (32): 19785–93. doi:10.1074/jbc.272.32.19785. ISSN 0021-9258. PMID 9242638. 
  7. ^ Miyamoto, A; Cui X, Naumovski L, Cleary M L (May 1996). "Helix-loop-helix proteins LYL1 and E2a form heterodimeric complexes with distinctive DNA-binding properties in hematolymphoid cells". Mol. Cell. Biol. (UNITED STATES) 16 (5): 2394–401. ISSN 0270-7306. PMC 231228. PMID 8628307. 
  8. ^ El Ghouzzi, V; Legeai-Mallet L, Aresta S, Benoist C, Munnich A, de Gunzburg J, Bonaventure J (March 2000). "Saethre-Chotzen mutations cause TWIST protein degradation or impaired nuclear location". Hum. Mol. Genet. (ENGLAND) 9 (5): 813–9. doi:10.1093/hmg/9.5.813. ISSN 0964-6906. PMID 10749989. 
  9. ^ a b c Bradney, Curtis; Hjelmeland Mark, Komatsu Yasuhiko, Yoshida Minoru, Yao Tso-Pang, Zhuang Yuan (January 2003). "Regulation of E2A activities by histone acetyltransferases in B lymphocyte development". J. Biol. Chem. (United States) 278 (4): 2370–6. doi:10.1074/jbc.M211464200. ISSN 0021-9258. PMID 12435739. 
  10. ^ Johnson, J D; Zhang W, Rudnick A, Rutter W J, German M S (July 1997). "Transcriptional synergy between LIM-homeodomain proteins and basic helix-loop-helix proteins: the LIM2 domain determines specificity". Mol. Cell. Biol. (UNITED STATES) 17 (7): 3488–96. ISSN 0270-7306. PMC 232202. PMID 9199284. 
  11. ^ a b c Goardon, Nicolas; Lambert Julie A, Rodriguez Patrick, Nissaire Philippe, Herblot Sabine, Thibault Pierre, Dumenil Dominique, Strouboulis John, Romeo Paul-Henri, Hoang Trang (January 2006). "ETO2 coordinates cellular proliferation and differentiation during erythropoiesis". EMBO J. (England) 25 (2): 357–66. doi:10.1038/sj.emboj.7600934. ISSN 0261-4189. PMC 1383517. PMID 16407974. 
  12. ^ Maira, S M; Wurtz J M, Wasylyk B (November 1996). "Net (ERP/SAP2) one of the Ras-inducible TCFs, has a novel inhibitory domain with resemblance to the helix-loop-helix motif". EMBO J. (ENGLAND) 15 (21): 5849–65. ISSN 0261-4189. PMC 452333. PMID 8918463. 
  13. ^ Maleki, S J; Royer C A, Hurlburt B K (June 1997). "MyoD-E12 heterodimers and MyoD-MyoD homodimers are equally stable". Biochemistry (UNITED STATES) 36 (22): 6762–7. doi:10.1021/bi970262m. ISSN 0006-2960. PMID 9184158. 
  14. ^ Neufeld, B; Grosse-Wilde A, Hoffmeyer A, Jordan B W, Chen P, Dinev D, Ludwig S, Rapp U R (July 2000). "Serine/Threonine kinases 3pK and MAPK-activated protein kinase 2 interact with the basic helix-loop-helix transcription factor E47 and repress its transcriptional activity". J. Biol. Chem. (UNITED STATES) 275 (27): 20239–42. doi:10.1074/jbc.C901040199. ISSN 0021-9258. PMID 10781029. 
  15. ^ Chakraborty, T; Martin J F, Olson E N (September 1992). "Analysis of the oligomerization of myogenin and E2A products in vivo using a two-hybrid assay system". J. Biol. Chem. (UNITED STATES) 267 (25): 17498–501. ISSN 0021-9258. PMID 1325437. 
  16. ^ Hsu, H L; Wadman I, Baer R (April 1994). "Formation of in vivo complexes between the TAL1 and E2A polypeptides of leukemic T cells". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 91 (8): 3181–5. doi:10.1073/pnas.91.8.3181. ISSN 0027-8424. PMC 43539. PMID 8159721. 
  17. ^ Huggins, G S; Chin M T, Sibinga N E, Lee S L, Haber E, Lee M E (October 1999). "Characterization of the mUBC9-binding sites required for E2A protein degradation". J. Biol. Chem. (UNITED STATES) 274 (40): 28690–6. doi:10.1074/jbc.274.40.28690. ISSN 0021-9258. PMID 10497239. 

Further reading[edit]

  • LeBrun DP (2004). "E2A basic helix-loop-helix transcription factors in human leukemia". Front. Biosci. 8: s206–22. doi:10.2741/1030. PMID 12700034.