Open Access Articles- Top Results for E2F1


SymbolsE2F1 ; E2F-1; RBAP1; RBBP3; RBP3
External IDsOMIM189971 MGI101941 HomoloGene3828 ChEMBL: 4382 GeneCards: E2F1 Gene
RNA expression pattern
File:PBB GE E2F1 2028 s at tn.png
File:PBB GE E2F1 204947 at tn.png
More reference expression data
RefSeq (mRNA)NM_005225NM_001291105
RefSeq (protein)NP_005216NP_001278034
Location (UCSC)Chr 20:
32.26 – 32.27 Mb
Chr 2:
154.56 – 154.57 Mb
PubMed search[1][2]

Transcription factor E2F1 is a protein that in humans is encoded by the E2F1 gene.[1]


The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. This protein binds preferentially to retinoblastoma protein pRB in a cell-cycle dependent manner. It can mediate both cell proliferation and p53-dependent/independent apoptosis.[2]


E2F1 promoter[PAX8] => E2F1 [PMID 21602887]


E2F1 has been shown to interact with:

See also


  1. Neuman E, Sellers WR, McNeil JA, Lawrence JB, Kaelin WG (December 1996). "Structure and partial genomic sequence of the human E2F1 gene". Gene 173 (2): 163–9. PMID 8964493. doi:10.1016/0378-1119(96)00184-9. 
  2. "Entrez Gene: E2F1 E2F transcription factor 1". 
  3. 3.0 3.1 Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T et al. (August 1998). "A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer". Oncogene 17 (7): 853–65. PMID 9780002. doi:10.1038/sj.onc.1202163. 
  4. 4.0 4.1 Marti A, Wirbelauer C, Scheffner M, Krek W (May 1999). "Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation". Nat. Cell Biol. 1 (1): 14–9. PMID 10559858. doi:10.1038/8984. 
  5. Yang R, Müller C, Huynh V, Fung YK, Yee AS, Koeffler HP (March 1999). "Functions of cyclin A1 in the cell cycle and its interactions with transcription factor E2F-1 and the Rb family of proteins". Mol. Cell. Biol. 19 (3): 2400–7. PMC 84032. PMID 10022926. 
  6. Xu M, Sheppard KA, Peng CY, Yee AS, Piwnica-Worms H (December 1994). "Cyclin A/CDK2 binds directly to E2F-1 and inhibits the DNA-binding activity of E2F-1/DP-1 by phosphorylation". Mol. Cell. Biol. 14 (12): 8420–31. PMC 359381. PMID 7969176. 
  7. Vandel L, Kouzarides T (August 1999). "Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase". EMBO J. 18 (15): 4280–91. PMC 1171504. PMID 10428966. doi:10.1093/emboj/18.15.4280. 
  8. Strachan GD, Jordan-Sciutto KL, Rallapalli R, Tuan RS, Hall DJ (February 2003). "The E2F-1 transcription factor is negatively regulated by its interaction with the MDMX protein". J. Cell. Biochem. 88 (3): 557–68. PMID 12532331. doi:10.1002/jcb.10318. 
  9. Kong HJ, Yu HJ, Hong S, Park MJ, Choi YH, An WG et al. (November 2003). "Interaction and functional cooperation of the cancer-amplified transcriptional coactivator activating signal cointegrator-2 and E2F-1 in cell proliferation". Mol. Cancer Res. 1 (13): 948–58. PMID 14638867. 
  10. 10.0 10.1 Taniura H, Taniguchi N, Hara M, Yoshikawa K (January 1998). "Necdin, a postmitotic neuron-specific growth suppressor, interacts with viral transforming proteins and cellular transcription factor E2F1". J. Biol. Chem. 273 (2): 720–8. PMID 9422723. doi:10.1074/jbc.273.2.720. 
  11. Kuwako K, Taniura H, Yoshikawa K (January 2004). "Necdin-related MAGE proteins differentially interact with the E2F1 transcription factor and the p75 neurotrophin receptor". J. Biol. Chem. 279 (3): 1703–12. PMID 14593116. doi:10.1074/jbc.M308454200. 
  12. Sansal I, Dupont E, Toru D, Evrard C, Rouget P (October 2000). "NPDC-1, a regulator of neural cell proliferation and differentiation, interacts with E2F-1, reduces its binding to DNA and modulates its transcriptional activity". Oncogene 19 (43): 5000–9. PMID 11042687. doi:10.1038/sj.onc.1203843. 
  13. Darbinian N, Gallia GL, Kundu M, Shcherbik N, Tretiakova A, Giordano A et al. (November 1999). "Association of Pur alpha and E2F-1 suppresses transcriptional activity of E2F-1". Oncogene 18 (46): 6398–402. PMID 10597240. doi:10.1038/sj.onc.1203011. 
  14. Joshi B, Ko D, Ordonez-Ercan D, Chellappan SP (December 2003). "A putative coiled-coil domain of prohibitin is sufficient to repress E2F1-mediated transcription and induce apoptosis". Biochem. Biophys. Res. Commun. 312 (2): 459–66. PMID 14637159. doi:10.1016/j.bbrc.2003.10.148. 
  15. Fusaro G, Dasgupta P, Rastogi S, Joshi B, Chellappan S (November 2003). "Prohibitin induces the transcriptional activity of p53 and is exported from the nucleus upon apoptotic signaling". J. Biol. Chem. 278 (48): 47853–61. PMID 14500729. doi:10.1074/jbc.M305171200. 
  16. Wang S, Zhang B, Faller DV (June 2002). "Prohibitin requires Brg-1 and Brm for the repression of E2F and cell growth". EMBO J. 21 (12): 3019–28. PMC 126057. PMID 12065415. doi:10.1093/emboj/cdf302. 
  17. Wang S, Nath N, Fusaro G, Chellappan S (November 1999). "Rb and prohibitin target distinct regions of E2F1 for repression and respond to different upstream signals". Mol. Cell. Biol. 19 (11): 7447–60. PMC 84738. PMID 10523633. 
  18. 18.0 18.1 Dyson N, Dembski M, Fattaey A, Ngwu C, Ewen M, Helin K (December 1993). "Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1". J. Virol. 67 (12): 7641–7. PMC 238233. PMID 8230483. 
  19. Nicolas E, Ait-Si-Ali S, Trouche D (August 2001). "The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein". Nucleic Acids Res. 29 (15): 3131–6. PMC 55834. PMID 11470869. doi:10.1093/nar/29.15.3131. 
  20. Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM (December 2002). "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation". J. Biol. Chem. 277 (52): 50860–6. PMID 12397079. doi:10.1074/jbc.M203839200. 
  21. 21.0 21.1 Choubey D, Li SJ, Datta B, Gutterman JU, Lengyel P (October 1996). "Inhibition of E2F-mediated transcription by p202". EMBO J. 15 (20): 5668–78. PMC 452311. PMID 8896460. 
  22. Fajas L, Paul C, Zugasti O, Le Cam L, Polanowska J, Fabbrizio E et al. (July 2000). "pRB binds to and modulates the transrepressing activity of the E1A-regulated transcription factor p120E4F". Proc. Natl. Acad. Sci. U.S.A. 97 (14): 7738–43. PMC 16614. PMID 10869426. doi:10.1073/pnas.130198397. 
  23. 23.0 23.1 Wu CL, Zukerberg LR, Ngwu C, Harlow E, Lees JA (May 1995). "In vivo association of E2F and DP family proteins". Mol. Cell. Biol. 15 (5): 2536–46. PMC 230484. PMID 7739537. 
  24. 24.0 24.1 24.2 24.3 Rotheneder H, Geymayer S, Haidweger E (November 1999). "Transcription factors of the Sp1 family: interaction with E2F and regulation of the murine thymidine kinase promoter". J. Mol. Biol. 293 (5): 1005–15. PMID 10547281. doi:10.1006/jmbi.1999.3213. 
  25. Lin SY, Black AR, Kostic D, Pajovic S, Hoover CN, Azizkhan JC (April 1996). "Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction". Mol. Cell. Biol. 16 (4): 1668–75. PMC 231153. PMID 8657142. 
  26. Karlseder J, Rotheneder H, Wintersberger E (April 1996). "Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F". Mol. Cell. Biol. 16 (4): 1659–67. PMC 231152. PMID 8657141. 
  27. Sardet C, Vidal M, Cobrinik D, Geng Y, Onufryk C, Chen A et al. (March 1995). "E2F-4 and E2F-5, two members of the E2F family, are expressed in the early phases of the cell cycle". Proc. Natl. Acad. Sci. U.S.A. 92 (6): 2403–7. PMC 42492. PMID 7892279. doi:10.1073/pnas.92.6.2403. 
  28. Helin K, Wu CL, Fattaey AR, Lees JA, Dynlacht BD, Ngwu C et al. (October 1993). "Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative trans-activation". Genes Dev. 7 (10): 1850–61. PMID 8405995. doi:10.1101/gad.7.10.1850. 
  29. Liu K, Lin FT, Ruppert JM, Lin WC (May 2003). "Regulation of E2F1 by BRCT domain-containing protein TopBP1". Mol. Cell. Biol. 23 (9): 3287–304. PMC 153207. PMID 12697828. doi:10.1128/mcb.23.9.3287-3304.2003. 
  30. Yu X, Chini CC, He M, Mer G, Chen J (October 2003). "The BRCT domain is a phospho-protein binding domain". Science 302 (5645): 639–42. PMID 14576433. doi:10.1126/science.1088753. 
  31. Zhou F, Zhang L, Wang A, Song B, Gong K, Zhang L et al. (May 2008). "The association of GSK3 beta with E2F1 facilitates nerve growth factor-induced neural cell differentiation". J. Biol. Chem. 283 (21): 14506–15. PMID 18367454. doi:10.1074/jbc.M706136200. 

Further reading

  • Dupont E, Sansal I, Toru D, Evrard C, Rouget P (1997). "[Identification of NPDC-1, gene involved in the control of proliferation and differentiation of neural and glial precursors]". C. R. Seances Soc. Biol. Fil. 191 (1): 95–104. PMID 9181131. 
  • Stevens C, La Thangue NB (2005). "The emerging role of E2F-1 in the DNA damage response and checkpoint control.". DNA Repair (Amst.) 3 (8-9): 1071–9. PMID 15279795. doi:10.1016/j.dnarep.2004.03.034. 
  • Zhang Z, Wang H, Li M, Rayburn E, Agrawal S, Zhang R (2006). "Novel MDM2 p53-independent functions identified through RNA silencing technologies.". Ann. N. Y. Acad. Sci. 1058 (1): 205–14. PMID 16394138. doi:10.1196/annals.1359.030. 
  • Schild C, Wirth M, Reichert M, Schmid RM, Saur D, Schneider G (July 2009). "PI3K signaling maintains c-myc expression to regulate transcription of E2F1 in pancreatic cancer cells". Mol. Carcinog. 48 (12): 1149–58. PMID 19603422. doi:10.1002/mc.20569. 

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.