E2F1

E2F1
Uygun yapılar
PDBOrtolog araması: PDBe RCSB
Tanımlayıcılar
Başka adlarE2F1
Dış kimliklerOMIM: 189971 MGI: 101941 HomoloGene: 3828 GeneCards: E2F1
Gen yerleşimi (İnsan)
20. Kromozom (insan)
Krom.20. Kromozom (insan)
20. Kromozom (insan)
E2F1 için genom yerleşimi
E2F1 için genom yerleşimi
Bant20q11.22Başlangıç33,675,477 bç
Bitiş33,686,385 bç
RNA ekspresyonu deseni


Daha çok ekspresyon verisi başvurusu
Ortologlar
TürlerİnsanFare
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005225

NM_007891
NM_001291105

RefSeq (protein)

NP_005216

NP_001278034
NP_031917

Yerleşim (UCSC)Krom. 20: 33.68 – 33.69 Mbn/a
PubMed araması
Vikiveri
İnsan'ı Gör/DüzenleFare'yi Gör/Düzenle

Transkripsiyon faktörü E2F1, insanlarda E2F1 geni tarafından kodlanan bir proteindir.

İşlevi

Bu gen tarafından kodlanan protein, E2F transkripsiyon faktörleri ailesinin bir üyesidir. E2F ailesi, hücre döngüsünün kontrolünde ve tümör baskılayıcı proteinlerin işlevlerinde kritik bir rol oynar; ayrıca küçük DNA tümör virüslerinin dönüştürücü proteinlerinin de hedefidir.

E2F proteinleri, ailenin çoğu üyesinde bulunan ve evrimsel olarak korunmuş birkaç alan içerir. Bu alanlar arasında DNA bağlanma alanı, farklılaşma tarafından düzenlenen transkripsiyon faktörü proteinleri (DP) ile etkileşimi belirleyen dimerizasyon alanı, asidik amino asitlerce zengin bir transaktivasyon alanı ve transaktivasyon alanı içine gömülü tümör baskılayıcı proteinlerle etkileşim alanı yer alır.

Bu protein ile birlikte E2F2 ve E2F3 olmak üzere iki başka aile üyesi, ek bir siklin bağlanma alanına sahiptir. Bu protein, hücre döngüsüne bağımlı bir şekilde retinoblastoma proteini (pRB)’ye tercihen bağlanır. Ayrıca hem hücre proliferasyonunu hem de p53’e bağımlı ya da bağımsız apoptozu aracılık edebilir.

Transkripsiyonu

E2F1 promoter[PAX8] => E2F1

Etkileşimleri

E2F1'in aşağıdaki proteinlerle etkileşime girdiği gösterilmiştir:

Ayrıca bakınız

Kaynakça

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000101412 - Ensembl, May 2017
  2. ↑ "İnsan PubMed Başvurusu:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ↑ "Fare PubMed Başvurusu:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑  Neuman E, Sellers WR, McNeil JA, Lawrence JB, Kaelin WG (December 1996).
  5. ↑ "Entrez Gene: E2F1 E2F transcription factor 1". 28 Ocak 2023 tarihinde kaynağından arşivlendi. Erişim tarihi: 6 Şubat 2026.
  6. ↑  Li CG, Nyman JE, Braithwaite AW, Eccles MR (December 2011).
  7. ↑ 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. 17 (7): 853–65. doi:10.1038/sj.onc.1202163. PMID 9780002.
  8. 1 2 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. doi:10.1038/8984. PMID 10559858. S2CID 8884226.
  9. ↑ 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. doi:10.1128/mcb.19.3.2400. PMC 84032. PMID 10022926.
  10. ↑ 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. doi:10.1128/MCB.14.12.8420. PMC 359381. PMID 7969176.
  11. ↑ 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. doi:10.1093/emboj/18.15.4280. PMC 1171504. PMID 10428966.
  12. ↑ 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. doi:10.1002/jcb.10318. PMID 12532331. S2CID 38805122.
  13. ↑ Kong HJ, Yu HJ, Hong S, Park MJ, Choi YH, An WG, Lee JW, Cheong J (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
  14. 1 2 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. doi:10.1074/jbc.273.2.720. PMID 9422723.
  15. ↑ 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. doi:10.1074/jbc.M308454200. PMID 14593116
  16. ↑ 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. doi:10.1038/sj.onc.1203843. PMID 11042687
  17. ↑ Darbinian N, Gallia GL, 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. 18 (46): 6398–402. doi:10.1038/sj.onc.1203011. PMID 10597240.
  18. ↑ 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. Bibcode:2003BBRC..312..459J. doi:10.1016/j.bbrc.2003.10.148. PMID 14637159
  19. ↑ 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. doi:10.1074/jbc.M305171200. PMID 14500729
  20. ↑ 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. doi:10.1093/emboj/cdf302. PMC 126057. PMID 12065415.
  21. ↑ 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. doi:10.1128/mcb.19.11.7447. PMC 84738. PMID 10523633.
  22. ↑ Walsh M, Shue G, Spidoni K, Kapoor A (March 1995). "E2F-1 and a cyclin-like DNA repair enzyme, uracil-DNA glycosylase, provide evidence for an auto-regulatory mechanisms for transcription". J. Biol. Chem. 270 (10): 5289–98. doi:10.1074/jbc.270.10.5289. PMID 7534293.
  23. ↑ 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. doi:10.1128/JVI.67.12.7641-7647.1993. PMC 238233. PMID 8230483
  24. 1 2 3 4 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. doi:10.1006/jmbi.1999.3213. PMID 10547281
  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. doi:10.1128/MCB.16.4.1668. 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. doi:10.1128/mcb.16.4.1659. PMC 231152. PMID 8657141
  27. ↑ Sardet C, Vidal M, Cobrinik D, Geng Y, Onufryk C, Chen A, Weinberg RA (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. Bibcode:1995PNAS...92.2403S. doi:10.1073/pnas.92.6.2403. PMC 42492. PMID 7892279.
  28. ↑ 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. doi:10.1128/mcb.23.9.3287-3304.2003. PMC 153207. PMID 12697828
  29. ↑ 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. Bibcode:2003Sci...302..639Y. doi:10.1126/science.1088753. PMID 14576433. S2CID 29407635.
  30. ↑ 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. doi:10.1002/j.1460-2075.1996.tb00951.x. PMC 452311. PMID 8896460
  31. ↑ Zhou F, Zhang L, Wang A, Song B, Gong K, Zhang L, Hu M, Zhang X, Zhao N, Gong Y (May 2008). "The association of GSK3 beta with E2F1 facilitates nerve growth factor-induced neural cell differentiation". J. Biol. Chem. 283 (21): 14506–15. doi:10.1074/jbc.M706136200. PMID 18367454