E2F1

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E2F transcription factor 1
Protein E2F1 PDB 2aze.png
PDB rendering based on 2aze.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols E2F1 ; E2F-1; RBAP1; RBBP3; RBP3
External IDs OMIM189971 MGI101941 HomoloGene3828 ChEMBL: 4382 GeneCards: E2F1 Gene
RNA expression pattern
PBB GE E2F1 2028 s at tn.png
PBB GE E2F1 204947 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1869 13555
Ensembl ENSG00000101412 ENSMUSG00000027490
UniProt Q01094 Q61501
RefSeq (mRNA) NM_005225 NM_001291105
RefSeq (protein) NP_005216 NP_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]

Transcription[edit]

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

Interactions[edit]

E2F1 has been shown to interact with NCOA6,[3] Retinoblastoma-like protein 1,[4] Retinoblastoma protein,[4][5][6][7][8][9][10] GTF2H1,[11] SKP2,[12] PURA,[13] NPDC1,[14] Sp2 transcription factor,[15] Sp1 transcription factor,[15][16][17] CUL1,[12] ARID3A,[18] TOPBP1,[19][20] Cyclin A1,[21] TP53BP1,[7] Cyclin A2,[22] Sp4 transcription factor,[15] Sp3 transcription factor,[15] Prohibitin,[23][24][25][26] NDN,[10][27] MDM4,[28] TFDP1[9][18][29][30] and Ubiquitin C.[31]

See also[edit]

References[edit]

  1. ^ Neuman E, Sellers WR, McNeil JA, Lawrence JB, Kaelin WG Jr (December 1996). "Structure and partial genomic sequence of the human E2F1 gene". Gene 173 (2): 163–9. doi:10.1016/0378-1119(96)00184-9. PMID 8964493. 
  2. ^ "Entrez Gene: E2F1 E2F transcription factor 1". 
  3. ^ Kong, Hee Jeong; Yu Hyun Jung; Hong SunHwa; Park Min Jung; Choi Young Hyun; An Won Gun; Lee Jae Woon; Cheong JaeHun (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. (United States) 1 (13): 948–58. ISSN 1541-7786. PMID 14638867. 
  4. ^ a b 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. (UNITED STATES) 67 (12): 7641–7. ISSN 0022-538X. PMC 238233. PMID 8230483. 
  5. ^ Nicolas, E; Ait-Si-Ali S; Trouche D (August 2001). "The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein". Nucleic Acids Res. (England) 29 (15): 3131–6. doi:10.1093/nar/29.15.3131. PMC 55834. PMID 11470869. 
  6. ^ Pardo, Patricia S; Leung James K, Lucchesi John C, Pereira-Smith Olivia M (December 2002). "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation". J. Biol. Chem. (United States) 277 (52): 50860–6. doi:10.1074/jbc.M203839200. ISSN 0021-9258. PMID 12397079. 
  7. ^ a b Choubey, D; Li S J; Datta B; Gutterman J U; Lengyel P (October 1996). "Inhibition of E2F-mediated transcription by p202". EMBO J. (ENGLAND) 15 (20): 5668–78. ISSN 0261-4189. PMC 452311. PMID 8896460. 
  8. ^ Fajas, L; Paul C; Zugasti O; Le Cam L; Polanowska J; Fabbrizio E; Medema R; Vignais M L; Sardet C (July 2000). "pRB binds to and modulates the transrepressing activity of the E1A-regulated transcription factor p120E4F". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (14): 7738–43. doi:10.1073/pnas.130198397. ISSN 0027-8424. PMC 16614. PMID 10869426. 
  9. ^ a b Wu, C L; Zukerberg L R; Ngwu C; Harlow E; Lees J A (May 1995). "In vivo association of E2F and DP family proteins". Mol. Cell. Biol. (UNITED STATES) 15 (5): 2536–46. ISSN 0270-7306. PMC 230484. PMID 7739537. 
  10. ^ a b 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. (UNITED STATES) 273 (2): 720–8. doi:10.1074/jbc.273.2.720. ISSN 0021-9258. PMID 9422723. 
  11. ^ Vandel, L; Kouzarides T (August 1999). "Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase". EMBO J. (ENGLAND) 18 (15): 4280–91. doi:10.1093/emboj/18.15.4280. ISSN 0261-4189. PMC 1171504. PMID 10428966. 
  12. ^ a b 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. (ENGLAND) 1 (1): 14–9. doi:10.1038/8984. ISSN 1465-7392. PMID 10559858. 
  13. ^ Darbinian, N; Gallia G L; Kundu M; Shcherbik N; Tretiakova A; Giordano A; Khalili K (November 1999). "Association of Pur alpha and E2F-1 suppresses transcriptional activity of E2F-1". Oncogene (ENGLAND) 18 (46): 6398–402. doi:10.1038/sj.onc.1203011. ISSN 0950-9232. PMID 10597240. 
  14. ^ 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 (ENGLAND) 19 (43): 5000–9. doi:10.1038/sj.onc.1203843. ISSN 0950-9232. PMID 11042687. 
  15. ^ a b c d 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. (ENGLAND) 293 (5): 1005–15. doi:10.1006/jmbi.1999.3213. ISSN 0022-2836. PMID 10547281. 
  16. ^ Lin, S Y; Black A R; Kostic D; Pajovic S; Hoover C N; Azizkhan J C (April 1996). "Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction". Mol. Cell. Biol. (UNITED STATES) 16 (4): 1668–75. ISSN 0270-7306. PMC 231153. PMID 8657142. 
  17. ^ Karlseder, J; Rotheneder H; Wintersberger E (April 1996). "Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F". Mol. Cell. Biol. (UNITED STATES) 16 (4): 1659–67. ISSN 0270-7306. PMC 231152. PMID 8657141. 
  18. ^ a b Suzuki, M; Okuyama S; Okamoto S; Shirasuna K; Nakajima T; Hachiya T; Nojima H; Sekiya S; Oda K (August 1998). "A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer". Oncogene (ENGLAND) 17 (7): 853–65. doi:10.1038/sj.onc.1202163. ISSN 0950-9232. PMID 9780002. 
  19. ^ Liu, Kang; Lin Fang-Tsyr; Ruppert J Michael; Lin Weei-Chin (May 2003). "Regulation of E2F1 by BRCT domain-containing protein TopBP1". Mol. Cell. Biol. (United States) 23 (9): 3287–304. doi:10.1128/MCB.23.9.3287-3304.2003. ISSN 0270-7306. PMC 153207. PMID 12697828. 
  20. ^ Yu, Xiaochun; Chini Claudia Christiano Silva; He Miao; Mer Georges; Chen Junjie (October 2003). "The BRCT domain is a phospho-protein binding domain". Science (United States) 302 (5645): 639–42. doi:10.1126/science.1088753. PMID 14576433. 
  21. ^ Yang, R; Müller C; Huynh V; Fung Y K; Yee A S; Koeffler H P (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. (UNITED STATES) 19 (3): 2400–7. ISSN 0270-7306. PMC 84032. PMID 10022926. 
  22. ^ Xu, M; Sheppard K A; Peng C Y; Yee A S; 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. (UNITED STATES) 14 (12): 8420–31. ISSN 0270-7306. PMC 359381. PMID 7969176. 
  23. ^ Joshi, Bharat; Ko Danette, Ordonez-Ercan Dalia, Chellappan Srikumar P (December 2003). "A putative coiled-coil domain of prohibitin is sufficient to repress E2F1-mediated transcription and induce apoptosis". Biochem. Biophys. Res. Commun. (United States) 312 (2): 459–66. doi:10.1016/j.bbrc.2003.10.148. ISSN 0006-291X. PMID 14637159. 
  24. ^ Fusaro, Gina; Dasgupta Piyali; Rastogi Shipra; Joshi Bharat; Chellappan Srikumar (November 2003). "Prohibitin induces the transcriptional activity of p53 and is exported from the nucleus upon apoptotic signaling". J. Biol. Chem. (United States) 278 (48): 47853–61. doi:10.1074/jbc.M305171200. ISSN 0021-9258. PMID 14500729. 
  25. ^ Wang, Sheng; Zhang Baohua; Faller Douglas V (June 2002). "Prohibitin requires Brg-1 and Brm for the repression of E2F and cell growth". EMBO J. (England) 21 (12): 3019–28. doi:10.1093/emboj/cdf302. ISSN 0261-4189. PMC 126057. PMID 12065415. 
  26. ^ 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. (UNITED STATES) 19 (11): 7447–60. ISSN 0270-7306. PMC 84738. PMID 10523633. 
  27. ^ Kuwako, Ken-ichiro; Taniura Hideo; Yoshikawa Kazuaki (January 2004). "Necdin-related MAGE proteins differentially interact with the E2F1 transcription factor and the p75 neurotrophin receptor". J. Biol. Chem. (United States) 279 (3): 1703–12. doi:10.1074/jbc.M308454200. ISSN 0021-9258. PMID 14593116. 
  28. ^ Strachan, Gordon D; Jordan-Sciutto Kelly L, Rallapalli Ravikumar, Tuan Rocky S, Hall David J (February 2003). "The E2F-1 transcription factor is negatively regulated by its interaction with the MDMX protein". J. Cell. Biochem. (United States) 88 (3): 557–68. doi:10.1002/jcb.10318. ISSN 0730-2312. PMID 12532331. 
  29. ^ Sardet, C; Vidal M; Cobrinik D; Geng Y; Onufryk C; Chen A; Weinberg R A (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. (UNITED STATES) 92 (6): 2403–7. doi:10.1073/pnas.92.6.2403. ISSN 0027-8424. PMC 42492. PMID 7892279. 
  30. ^ Helin, K; Wu C L; Fattaey A R; Lees J A; Dynlacht B D; Ngwu C; Harlow E (October 1993). "Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative trans-activation". Genes Dev. (UNITED STATES) 7 (10): 1850–61. doi:10.1101/gad.7.10.1850. ISSN 0890-9369. PMID 8405995. 
  31. ^ Zhou, Fangfang; Zhang Long; Wang Aijun; Song Bo; Gong Kai; Zhang Lihai; Hu Min; Zhang Xiufang; Zhao Nanming; Gong Yandao (May 2008). "The association of GSK3 beta with E2F1 facilitates nerve growth factor-induced neural cell differentiation". J. Biol. Chem. (United States) 283 (21): 14506–15. doi:10.1074/jbc.M706136200. ISSN 0021-9258. PMID 18367454. 

PI3K signaling maintains c-myc expression to regulate transcription of E2F1 in pancreatic cancer cells.

Further reading[edit]

  • Dupont E, Sansal I, Toru D, et al. (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. doi:10.1016/j.dnarep.2004.03.034. PMID 15279795. 
  • Zhang Z, Wang H, Li M, et al. (2006). "Novel MDM2 p53-independent functions identified through RNA silencing technologies.". Ann. N. Y. Acad. Sci. 1058 (1): 205–14. doi:10.1196/annals.1359.030. PMID 16394138. 
  • 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. doi:10.1002/mc.20569. PMID 19603422. 

External links[edit]

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