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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Technical|date=December 2018}}{{Infobox_gene}}
{{PBB_Controls
'''Transcription factor E2F1''' is a [[protein]] that in humans is encoded by the ''E2F1'' [[gene]].<ref name="pmid8964493">{{cite journal | vauthors = Neuman E, Sellers WR, McNeil JA, Lawrence JB, Kaelin WG | title = Structure and partial genomic sequence of the human E2F1 gene | journal = Gene | volume = 173 | issue = 2 | pages = 163–9 | date = December 1996 | pmid = 8964493 | pmc = | doi = 10.1016/0378-1119(96)00184-9 }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_E2F1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2aze.
| PDB = {{PDB2|2aze}}
| Name = E2F transcription factor 1
| HGNCid = 3113
| Symbol = E2F1
| AltSymbols =; E2F-1; RBBP3; RBP3
| OMIM = 189971
| ECnumber = 
| Homologene = 3828
| MGIid = 101941
| GeneAtlas_image1 = PBB_GE_E2F1_2028_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_E2F1_204947_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005667 |text = transcription factor complex}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0000080 |text = G1 phase of mitotic cell cycle}} {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1869
    | Hs_Ensembl = ENSG00000101412
    | Hs_RefseqProtein = NP_005216
    | Hs_RefseqmRNA = NM_005225
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 20
    | Hs_GenLoc_start = 31727147
    | Hs_GenLoc_end = 31737871
    | Hs_Uniprot = Q01094
    | Mm_EntrezGene = 13555
    | Mm_Ensembl = ENSMUSG00000027490
    | Mm_RefseqmRNA = NM_007891
    | Mm_RefseqProtein = NP_031917
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 154250848
    | Mm_GenLoc_end = 154261333
    | Mm_Uniprot = Q547J6
  }}
}}
'''E2F transcription factor 1''', also known as '''E2F1''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is a member of the E2F family of [[transcription factor]]s. 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 evolutionarily 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]].<ref>{{Cite web| title = Entrez Gene: E2F1 E2F transcription factor 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1869| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: E2F1 E2F transcription factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1869| accessdate = }}</ref>
}}


==See also==
== Transcription ==
 
E2F1 promoter[PAX8] => E2F1  {{PMID|21602887}}
 
== Interactions ==
 
E2F1 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[ARID3A]],<ref name = pmid9780002>{{cite journal | vauthors = Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K | title = A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer | journal = Oncogene | volume = 17 | issue = 7 | pages = 853–65 | date = August 1998 | pmid = 9780002 | doi = 10.1038/sj.onc.1202163 }}</ref>
* [[CUL1]],<ref name = pmid10559858/>
* [[Cyclin A1]],<ref name = pmid10022926>{{cite journal | vauthors = Yang R, Müller C, Huynh V, Fung YK, Yee AS, Koeffler HP | title = Functions of cyclin A1 in the cell cycle and its interactions with transcription factor E2F-1 and the Rb family of proteins | journal = Mol. Cell. Biol. | volume = 19 | issue = 3 | pages = 2400–7 | date = March 1999 | pmid = 10022926 | pmc = 84032 | doi =  10.1128/mcb.19.3.2400}}</ref>
* [[Cyclin A2]],<ref name = pmid7969176>{{cite journal | vauthors = Xu M, Sheppard KA, Peng CY, Yee AS, Piwnica-Worms H | title = Cyclin A/CDK2 binds directly to E2F-1 and inhibits the DNA-binding activity of E2F-1/DP-1 by phosphorylation | journal = Mol. Cell. Biol. | volume = 14 | issue = 12 | pages = 8420–31 | date = December 1994 | pmid = 7969176 | pmc = 359381 | doi =  }}</ref>
* [[GTF2H1]],<ref name = pmid10428966>{{cite journal | vauthors = Vandel L, Kouzarides T | title = Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase | journal = EMBO J. | volume = 18 | issue = 15 | pages = 4280–91 | date = August 1999 | pmid = 10428966 | pmc = 1171504 | doi = 10.1093/emboj/18.15.4280 }}</ref>
* [[MDM4]],<ref name = pmid12532331>{{cite journal | vauthors = Strachan GD, Jordan-Sciutto KL, Rallapalli R, Tuan RS, Hall DJ | title = The E2F-1 transcription factor is negatively regulated by its interaction with the MDMX protein | journal = J. Cell. Biochem. | volume = 88 | issue = 3 | pages = 557–68 | date = February 2003 | pmid = 12532331 | doi = 10.1002/jcb.10318 }}</ref>
* [[NCOA6]],<ref name = pmid14638867>{{cite journal | vauthors = Kong HJ, Yu HJ, Hong S, Park MJ, Choi YH, An WG, Lee JW, Cheong J | title = Interaction and functional cooperation of the cancer-amplified transcriptional coactivator activating signal cointegrator-2 and E2F-1 in cell proliferation | journal = Mol. Cancer Res. | volume = 1 | issue = 13 | pages = 948–58 | date = November 2003 | pmid = 14638867 | doi =  }}</ref>
* [[NDN (gene)|NDN]],<ref name = pmid9422723/><ref name = pmid14593116>{{cite journal | vauthors = Kuwako K, Taniura H, Yoshikawa K | title = Necdin-related MAGE proteins differentially interact with the E2F1 transcription factor and the p75 neurotrophin receptor | journal = J. Biol. Chem. | volume = 279 | issue = 3 | pages = 1703–12 | date = January 2004 | pmid = 14593116 | doi = 10.1074/jbc.M308454200 }}</ref>
* [[NPDC1]],<ref name = pmid11042687>{{cite journal | vauthors = Sansal I, Dupont E, Toru D, Evrard C, Rouget P | title = NPDC-1, a regulator of neural cell proliferation and differentiation, interacts with E2F-1, reduces its binding to DNA and modulates its transcriptional activity | journal = Oncogene | volume = 19 | issue = 43 | pages = 5000–9 | date = October 2000 | pmid = 11042687 | doi = 10.1038/sj.onc.1203843 }}</ref>
* [[PURA]],<ref name = pmid10597240>{{cite journal | vauthors = Darbinian N, Gallia GL, Kundu M, Shcherbik N, Tretiakova A, Giordano A, Khalili K | title = Association of Pur alpha and E2F-1 suppresses transcriptional activity of E2F-1 | journal = Oncogene | volume = 18 | issue = 46 | pages = 6398–402 | date = November 1999 | pmid = 10597240 | doi = 10.1038/sj.onc.1203011 }}</ref>
* [[Prohibitin|PHB]],<ref name = pmid14637159>{{cite journal | vauthors = Joshi B, Ko D, Ordonez-Ercan D, Chellappan SP | title = A putative coiled-coil domain of prohibitin is sufficient to repress E2F1-mediated transcription and induce apoptosis | journal = Biochem. Biophys. Res. Commun. | volume = 312 | issue = 2 | pages = 459–66 | date = December 2003 | pmid = 14637159 | doi =  10.1016/j.bbrc.2003.10.148}}</ref><ref name = pmid14500729>{{cite journal | vauthors = Fusaro G, Dasgupta P, Rastogi S, Joshi B, Chellappan S | title = Prohibitin induces the transcriptional activity of p53 and is exported from the nucleus upon apoptotic signaling | journal = J. Biol. Chem. | volume = 278 | issue = 48 | pages = 47853–61 | date = November 2003 | pmid = 14500729 | doi = 10.1074/jbc.M305171200 }}</ref><ref name = pmid12065415>{{cite journal | vauthors = Wang S, Zhang B, Faller DV | title = Prohibitin requires Brg-1 and Brm for the repression of E2F and cell growth | journal = EMBO J. | volume = 21 | issue = 12 | pages = 3019–28 | date = June 2002 | pmid = 12065415 | pmc = 126057 | doi = 10.1093/emboj/cdf302 }}</ref><ref name = pmid10523633>{{cite journal | vauthors = Wang S, Nath N, Fusaro G, Chellappan S | title = Rb and prohibitin target distinct regions of E2F1 for repression and respond to different upstream signals | journal = Mol. Cell. Biol. | volume = 19 | issue = 11 | pages = 7447–60 | date = November 1999 | pmid = 10523633 | pmc = 84738 | doi =  10.1128/mcb.19.11.7447}}</ref>
* [[Retinoblastoma protein|RB1]],<ref name = pmid9422723>{{cite journal | vauthors = Taniura H, Taniguchi N, Hara M, Yoshikawa K | title = Necdin, a postmitotic neuron-specific growth suppressor, interacts with viral transforming proteins and cellular transcription factor E2F1 | journal = J. Biol. Chem. | volume = 273 | issue = 2 | pages = 720–8 | date = January 1998 | pmid = 9422723 | doi =  10.1074/jbc.273.2.720}}</ref><ref name = pmid8230483/><ref name = pmid11470869>{{cite journal | vauthors = Nicolas E, Ait-Si-Ali S, Trouche D | title = The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein | journal = Nucleic Acids Res. | volume = 29 | issue = 15 | pages = 3131–6 | date = August 2001 | pmid = 11470869 | pmc = 55834 | doi =  10.1093/nar/29.15.3131}}</ref><ref name = pmid12397079>{{cite journal | vauthors = Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM | title = MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation | journal = J. Biol. Chem. | volume = 277 | issue = 52 | pages = 50860–6 | date = December 2002 | pmid = 12397079 | doi = 10.1074/jbc.M203839200 }}</ref><ref name = pmid8896460>{{cite journal | vauthors = Choubey D, Li SJ, Datta B, Gutterman JU, Lengyel P | title = Inhibition of E2F-mediated transcription by p202 | journal = EMBO J. | volume = 15 | issue = 20 | pages = 5668–78 | date = October 1996 | pmid = 8896460 | pmc = 452311 | doi =  }}</ref><ref name = pmid10869426>{{cite journal | vauthors = Fajas L, Paul C, Zugasti O, Le Cam L, Polanowska J, Fabbrizio E, Medema R, Vignais ML, Sardet C | title = pRB binds to and modulates the transrepressing activity of the E1A-regulated transcription factor p120E4F | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 14 | pages = 7738–43 | date = July 2000 | pmid = 10869426 | pmc = 16614 | doi = 10.1073/pnas.130198397 }}</ref><ref name = pmid7739537>{{cite journal | vauthors = Wu CL, Zukerberg LR, Ngwu C, Harlow E, Lees JA | title = In vivo association of E2F and DP family proteins | journal = Mol. Cell. Biol. | volume = 15 | issue = 5 | pages = 2536–46 | date = May 1995 | pmid = 7739537 | pmc = 230484 | doi =  10.1128/mcb.15.5.2536}}</ref>
* [[Retinoblastoma-like protein 1|RBL1]],<ref name = pmid8230483>{{cite journal | vauthors = Dyson N, Dembski M, Fattaey A, Ngwu C, Ewen M, Helin K | title = Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1 | journal = J. Virol. | volume = 67 | issue = 12 | pages = 7641–7 | date = December 1993 | pmid = 8230483 | pmc = 238233 | doi =  }}</ref>
* [[SKP2]],<ref name = pmid10559858>{{cite journal | vauthors = Marti A, Wirbelauer C, Scheffner M, Krek W | title = Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation | journal = Nat. Cell Biol. | volume = 1 | issue = 1 | pages = 14–9 | date = May 1999 | pmid = 10559858 | doi = 10.1038/8984 }}</ref>
* [[Sp1 transcription factor|SP1]],<ref name = pmid10547281/><ref name = pmid8657142>{{cite journal | vauthors = Lin SY, Black AR, Kostic D, Pajovic S, Hoover CN, Azizkhan JC | title = Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction | journal = Mol. Cell. Biol. | volume = 16 | issue = 4 | pages = 1668–75 | date = April 1996 | pmid = 8657142 | pmc = 231153 | doi =  }}</ref><ref name = pmid8657141>{{cite journal | vauthors = Karlseder J, Rotheneder H, Wintersberger E | title = Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F | journal = Mol. Cell. Biol. | volume = 16 | issue = 4 | pages = 1659–67 | date = April 1996 | pmid = 8657141 | pmc = 231152 | doi =  10.1128/mcb.16.4.1659}}</ref>
* [[Sp2 transcription factor|SP2]],<ref name = pmid10547281>{{cite journal | vauthors = Rotheneder H, Geymayer S, Haidweger E | title = Transcription factors of the Sp1 family: interaction with E2F and regulation of the murine thymidine kinase promoter | journal = J. Mol. Biol. | volume = 293 | issue = 5 | pages = 1005–15 | date = November 1999 | pmid = 10547281 | doi = 10.1006/jmbi.1999.3213 }}</ref>
* [[Sp3 transcription factor|SP3]],<ref name = pmid10547281/>
* [[Sp4 transcription factor|SP4]],<ref name = pmid10547281/>
* [[TFDP1]]<ref name = pmid9780002/><ref name = pmid7739537/><ref name = pmid7892279>{{cite journal | vauthors = Sardet C, Vidal M, Cobrinik D, Geng Y, Onufryk C, Chen A, Weinberg RA | title = E2F-4 and E2F-5, two members of the E2F family, are expressed in the early phases of the cell cycle | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 6 | pages = 2403–7 | date = March 1995 | pmid = 7892279 | pmc = 42492 | doi =  10.1073/pnas.92.6.2403}}</ref><ref name = pmid8405995>{{cite journal | vauthors = Helin K, Wu CL, Fattaey AR, Lees JA, Dynlacht BD, Ngwu C, Harlow E | title = Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative trans-activation | journal = Genes Dev. | volume = 7 | issue = 10 | pages = 1850–61 | date = October 1993 | pmid = 8405995 | doi =  10.1101/gad.7.10.1850}}</ref>
* [[TOPBP1]],<ref name = pmid12697828>{{cite journal | vauthors = Liu K, Lin FT, Ruppert JM, Lin WC | title = Regulation of E2F1 by BRCT domain-containing protein TopBP1 | journal = Mol. Cell. Biol. | volume = 23 | issue = 9 | pages = 3287–304 | date = May 2003 | pmid = 12697828 | pmc = 153207 | doi =  10.1128/mcb.23.9.3287-3304.2003}}</ref><ref name = pmid14576433>{{cite journal | vauthors = Yu X, Chini CC, He M, Mer G, Chen J | title = The BRCT domain is a phospho-protein binding domain | journal = Science | volume = 302 | issue = 5645 | pages = 639–42 | date = October 2003 | pmid = 14576433 | doi = 10.1126/science.1088753 }}</ref>
* [[TP53BP1]],<ref name = pmid8896460/>  and
* [[Ubiquitin C|UBC]].<ref name = pmid18367454>{{cite journal | vauthors = Zhou F, Zhang L, Wang A, Song B, Gong K, Zhang L, Hu M, Zhang X, Zhao N, Gong Y | title = The association of GSK3 beta with E2F1 facilitates nerve growth factor-induced neural cell differentiation | journal = J. Biol. Chem. | volume = 283 | issue = 21 | pages = 14506–15 | date = May 2008 | pmid = 18367454 | doi = 10.1074/jbc.M706136200 }}</ref>
{{Div col end}}
 
== See also ==
* [[E2F]]
* [[E2F]]
* [[Retinoblastoma protein]]
{{Clear}}


==References==
== References ==
{{reflist|2}}
{{Reflist|35em}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{Refbegin|35em}}
{{PBB_Further_reading
* {{cite journal | vauthors = Dupont E, Sansal I, Toru D, Evrard C, Rouget P | title = [Identification of NPDC-1, gene involved in the control of proliferation and differentiation of neural and glial precursors] | journal = C. R. Séances Soc. Biol. Fil. | volume = 191 | issue = 1 | pages = 95–104 | year = 1997 | pmid = 9181131 | doi =  }}
| citations =
* {{cite journal | vauthors = Stevens C, La Thangue NB | title = The emerging role of E2F-1 in the DNA damage response and checkpoint control. | journal = DNA Repair (Amst.) | volume = 3 | issue = 8-9 | pages = 1071–9 | year = 2005 | pmid = 15279795 | doi = 10.1016/j.dnarep.2004.03.034 }}
*{{cite journal | author=Dupont E, Sansal I, Toru D, ''et al.'' |title=[Identification of NPDC-1, gene involved in the control of proliferation and differentiation of neural and glial precursors] |journal=C. R. Seances Soc. Biol. Fil. |volume=191 |issue= 1 |pages= 95-104 |year= 1997 |pmid= 9181131 |doi=  }}
* {{cite journal | vauthors = Zhang Z, Wang H, Li M, Rayburn E, Agrawal S, Zhang R | title = Novel MDM2 p53-independent functions identified through RNA silencing technologies. | journal = Ann. N. Y. Acad. Sci. | volume = 1058 | issue = 1 | pages = 205–14 | year = 2006 | pmid = 16394138 | doi = 10.1196/annals.1359.030 }}
*{{cite journal | author=Stevens C, La Thangue NB |title=The emerging role of E2F-1 in the DNA damage response and checkpoint control. |journal=DNA Repair (Amst.) |volume=3 |issue= 8-9 |pages= 1071-9 |year= 2005 |pmid= 15279795 |doi= 10.1016/j.dnarep.2004.03.034 }}
* {{cite journal | vauthors = Schild C, Wirth M, Reichert M, Schmid RM, Saur D, Schneider G | title = PI3K signaling maintains c-myc expression to regulate transcription of E2F1 in pancreatic cancer cells | journal = Mol. Carcinog. | volume = 48 | issue = 12 | pages = 1149–58 | date = July 2009 | pmid = 19603422 | doi = 10.1002/mc.20569 }}
*{{cite journal | author=Zhang Z, Wang H, Li M, ''et al.'' |title=Novel MDM2 p53-independent functions identified through RNA silencing technologies. |journal=Ann. N. Y. Acad. Sci. |volume=1058 |issue= |pages= 205-14 |year= 2006 |pmid= 16394138 |doi= 10.1196/annals.1359.030 }}
{{Refend}}
}}
{{refend}}


== External links ==
== External links ==
* {{MeshName|E2F1+protein,+human}}
* {{MeshName|E2F1+protein,+human}}
* {{FactorBook|E2F1}}


{{PDB Gallery|geneid=1869}}
{{Transcription factors|g3}}
{{NLM content}}
{{NLM content}}
{{gene-20-stub}}
 
{{Transcription factors}}
{{DEFAULTSORT:E2f1}}
[[Category:Transcription factors]]
[[Category:Transcription factors]]
{{WikiDoc Sources}}

Latest revision as of 07:13, 10 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

Function

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 evolutionarily 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

E2F1 promoter[PAX8] => E2F1 PMID 21602887

Interactions

E2F1 has been shown to interact with:

See also

References

  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. doi:10.1016/0378-1119(96)00184-9. PMID 8964493.
  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, 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.
  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. doi:10.1038/8984. PMID 10559858.
  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. doi:10.1128/mcb.19.3.2400. 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. doi:10.1093/emboj/18.15.4280. PMC 1171504. PMID 10428966.
  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. doi:10.1002/jcb.10318. PMID 12532331.
  9. ↑ 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.
  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. doi:10.1074/jbc.273.2.720. PMID 9422723.
  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. doi:10.1074/jbc.M308454200. PMID 14593116.
  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. doi:10.1038/sj.onc.1203843. PMID 11042687.
  13. ↑ 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.
  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. doi:10.1016/j.bbrc.2003.10.148. PMID 14637159.
  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. doi:10.1074/jbc.M305171200. PMID 14500729.
  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. doi:10.1093/emboj/cdf302. PMC 126057. PMID 12065415.
  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. doi:10.1128/mcb.19.11.7447. PMC 84738. PMID 10523633.
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  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. doi:10.1093/nar/29.15.3131. PMC 55834. PMID 11470869.
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  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. 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. doi:10.1073/pnas.92.6.2403. PMC 42492. PMID 7892279.
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  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. doi:10.1128/mcb.23.9.3287-3304.2003. PMC 153207. PMID 12697828.
  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. doi:10.1126/science.1088753. PMID 14576433.
  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.

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. Séances 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, 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. 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.

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