E2F4: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Transcription factor E2F4''' is a [[protein]] that in humans is encoded by the ''E2F4'' [[gene]].<ref name="pmid7958924">{{cite journal | vauthors = Ginsberg D, Vairo G, Chittenden T, Xiao ZX, Xu G, Wydner KL, DeCaprio JA, Lawrence JB, Livingston DM | title = E2F-4, a new member of the E2F transcription factor family, interacts with p107 | journal = Genes Dev | volume = 8 | issue = 22 | pages = 2665–79 |date=Dec 1994 | pmid = 7958924 | pmc =  | doi =10.1101/gad.8.22.2665  }}</ref><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=Apr 1995 | pmid = 7892279 | pmc = 42492 | doi =10.1073/pnas.92.6.2403  }}</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_E2F4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cf7.
| PDB = {{PDB2|1cf7}}
| Name = E2F transcription factor 4, p107/p130-binding
| HGNCid = 3118
| Symbol = E2F4
| AltSymbols =; E2F-4
| OMIM = 600659
| ECnumber = 
| Homologene = 1471
| MGIid = 103012
| GeneAtlas_image1 = PBB_GE_E2F4_38707_r_at_tn.png
| GeneAtlas_image2 = PBB_GE_E2F4_202248_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor 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:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007049 |text = cell cycle}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1874
    | Hs_Ensembl = ENSG00000205250
    | Hs_RefseqProtein = NP_001941
    | Hs_RefseqmRNA = NM_001950
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 65783569
    | Hs_GenLoc_end = 65790322
    | Hs_Uniprot = Q16254
    | Mm_EntrezGene = 104394
    | Mm_Ensembl = ENSMUSG00000014859
    | Mm_RefseqmRNA = NM_148952
    | Mm_RefseqProtein = NP_683754
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 108186792
    | Mm_GenLoc_end = 108194499
    | Mm_Uniprot =
  }}
}}
'''E2F transcription factor 4, p107/p130-binding''', also known as '''E2F4''', 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. This protein binds to all three of the  tumor suppressor proteins pRB, p107 and p130, but with higher affinity to the last two. It plays an important role in the suppression of proliferation-associated genes, and its gene mutation and increased expression may be associated with human cancer.<ref name="entrez">{{cite web | title = Entrez Gene: E2F4 E2F transcription factor 4, p107/p130-binding| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1874| accessdate = }}</ref>
{{PBB_Summary
 
| section_title =
== Structure ==
| 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 binds to all three of the  tumor suppressor proteins pRB, p107 and p130, but with higher affinity to the last two. It plays an important role in the suppression of proliferation-associated genes, and its gene mutation and increased expression may be associated with human cancer.<ref name="entrez">{{cite web | title = Entrez Gene: E2F4 E2F transcription factor 4, p107/p130-binding| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1874| accessdate = }}</ref>
 
}}
The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a [[DNA binding domain]], a [[protein dimer|dimerization]] domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a [[transactivation]] domain enriched in acidic amino acids ([[aspartic acid|Asp]] + [[glutamic acid|Glu]]), and a tumor suppressor protein association domain which is embedded within the transactivation domain.
 
==Interactions==
E2F4 has been shown to [[Protein-protein interaction|interact]] with [[Smad3]].<ref name="pmid12150994">{{cite journal | vauthors = Chen CR, Kang Y, Siegel PM, Massagué J | title = E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression | journal = Cell | volume = 110 | issue = 1 | pages = 19–32 |date=July 2002 | pmid = 12150994 | doi = 10.1016/S0092-8674(02)00801-2 }}</ref>


==See also==
==See also==
Line 59: Line 17:


==References==
==References==
{{reflist|2}}
{{reflist}}


==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Bandyopadhyay D, Timchenko N, Suwa T |title=The human melanocyte: a model system to study the complexity of cellular aging and transformation in non-fibroblastic cells. |journal=Exp. Gerontol. |volume=36 |issue= 8 |pages= 1265–75 |year= 2001 |pmid= 11602203 |doi=10.1016/S0531-5565(01)00098-5 |display-authors=etal}}
| citations =
*{{cite journal  | vauthors=Beijersbergen RL, Kerkhoven RM, Zhu L |title=E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo. |journal=Genes Dev. |volume=8 |issue= 22 |pages= 2680–90 |year= 1994 |pmid= 7958925 |doi=10.1101/gad.8.22.2680 |display-authors=etal}}
*{{cite journal  | author=Bandyopadhyay D, Timchenko N, Suwa T, ''et al.'' |title=The human melanocyte: a model system to study the complexity of cellular aging and transformation in non-fibroblastic cells. |journal=Exp. Gerontol. |volume=36 |issue= 8 |pages= 1265-75 |year= 2001 |pmid= 11602203 |doi=  }}
*{{cite journal  | vauthors=Xiao ZX, Ginsberg D, Ewen M, Livingston DM |title=Regulation of the retinoblastoma protein-related protein p107 by G1 cyclin-associated kinases. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 10 |pages= 4633–7 |year= 1996 |pmid= 8643455 |doi=10.1073/pnas.93.10.4633  | pmc=39330  }}
*{{cite journal  | author=Sardet C, Vidal M, Cobrinik D, ''et al.'' |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 |year= 1995 |pmid= 7892279 |doi=  }}
*{{cite journal  | vauthors=Moberg K, Starz MA, Lees JA |title=E2F-4 switches from p130 to p107 and pRB in response to cell cycle reentry. |journal=Mol. Cell. Biol. |volume=16 |issue= 4 |pages= 1436–49 |year= 1996 |pmid= 8657117 |doi= | pmc=231128 }}
*{{cite journal  | author=Ginsberg D, Vairo G, Chittenden T, ''et al.'' |title=E2F-4, a new member of the E2F transcription factor family, interacts with p107. |journal=Genes Dev. |volume=8 |issue= 22 |pages= 2665-79 |year= 1994 |pmid= 7958924 |doi= }}
*{{cite journal  | vauthors=Vidal M, Brachmann RK, Fattaey A |title=Reverse two-hybrid and one-hybrid systems to detect dissociation of protein-protein and DNA-protein interactions. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 19 |pages= 10315–20 |year= 1996 |pmid= 8816797 |doi=10.1073/pnas.93.19.10315 | pmc=38381  |display-authors=etal}}
*{{cite journal  | author=Beijersbergen RL, Kerkhoven RM, Zhu L, ''et al.'' |title=E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo. |journal=Genes Dev. |volume=8 |issue= 22 |pages= 2680-90 |year= 1994 |pmid= 7958925 |doi=  }}
*{{cite journal  | vauthors=Williams CD, Linch DC, Sørensen TS |title=The predominant E2F complex in human primary haemopoietic cells and in AML blasts contains E2F-4, DP-1 and p130. |journal=Br. J. Haematol. |volume=96 |issue= 4 |pages= 688–96 |year= 1997 |pmid= 9074408 |doi=10.1046/j.1365-2141.1997.d01-2086.x |display-authors=etal}}
*{{cite journal  | author=Xiao ZX, Ginsberg D, Ewen M, Livingston DM |title=Regulation of the retinoblastoma protein-related protein p107 by G1 cyclin-associated kinases. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 10 |pages= 4633-7 |year= 1996 |pmid= 8643455 |doi=  }}
*{{cite journal  | vauthors=Lindeman GJ, Gaubatz S, Livingston DM, Ginsberg D |title=The subcellular localization of E2F-4 is cell-cycle dependent. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 10 |pages= 5095–100 |year= 1997 |pmid= 9144196 |doi=10.1073/pnas.94.10.5095  | pmc=24637  }}
*{{cite journal  | author=Moberg K, Starz MA, Lees JA |title=E2F-4 switches from p130 to p107 and pRB in response to cell cycle reentry. |journal=Mol. Cell. Biol. |volume=16 |issue= 4 |pages= 1436-49 |year= 1996 |pmid= 8657117 |doi=  }}
*{{cite journal  | vauthors=Wang H, Shao N, Ding QM |title=BRCA1 proteins are transported to the nucleus in the absence of serum and splice variants BRCA1a, BRCA1b are tyrosine phosphoproteins that associate with E2F, cyclins and cyclin dependent kinases. |journal=Oncogene |volume=15 |issue= 2 |pages= 143–57 |year= 1997 |pmid= 9244350 |doi= 10.1038/sj.onc.1201252 |display-authors=etal}}
*{{cite journal  | author=Vidal M, Brachmann RK, Fattaey A, ''et al.'' |title=Reverse two-hybrid and one-hybrid systems to detect dissociation of protein-protein and DNA-protein interactions. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 19 |pages= 10315-20 |year= 1996 |pmid= 8816797 |doi= }}
*{{cite journal  | vauthors=Müller H, Moroni MC, Vigo E |title=Induction of S-phase entry by E2F transcription factors depends on their nuclear localization. |journal=Mol. Cell. Biol. |volume=17 |issue= 9 |pages= 5508–20 |year= 1997 |pmid= 9271426 |doi=  | pmc=232399  |display-authors=etal}}
*{{cite journal  | author=Williams CD, Linch DC, Sørensen TS, ''et al.'' |title=The predominant E2F complex in human primary haemopoietic cells and in AML blasts contains E2F-4, DP-1 and p130. |journal=Br. J. Haematol. |volume=96 |issue= 4 |pages= 688-96 |year= 1997 |pmid= 9074408 |doi= }}
*{{cite journal  | vauthors=Pierce AM, Schneider-Broussard R, Philhower JL, Johnson DG |title=Differential activities of E2F family members: unique functions in regulating transcription. |journal=Mol. Carcinog. |volume=22 |issue= 3 |pages= 190–8 |year= 1998 |pmid= 9688145 |doi=10.1002/(SICI)1098-2744(199807)22:3<190::AID-MC7>3.0.CO;2-P  }}
*{{cite journal  | author=Lindeman GJ, Gaubatz S, Livingston DM, Ginsberg D |title=The subcellular localization of E2F-4 is cell-cycle dependent. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 10 |pages= 5095-100 |year= 1997 |pmid= 9144196 |doi=  }}
*{{cite journal  | vauthors=Ferreira R, Magnaghi-Jaulin L, Robin P |title=The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 18 |pages= 10493–8 |year= 1998 |pmid= 9724731 |doi=10.1073/pnas.95.18.10493 | pmc=27922  |display-authors=etal}}
*{{cite journal  | author=Wang H, Shao N, Ding QM, ''et al.'' |title=BRCA1 proteins are transported to the nucleus in the absence of serum and splice variants BRCA1a, BRCA1b are tyrosine phosphoproteins that associate with E2F, cyclins and cyclin dependent kinases. |journal=Oncogene |volume=15 |issue= 2 |pages= 143-57 |year= 1997 |pmid= 9244350 |doi= 10.1038/sj.onc.1201252 }}
*{{cite journal  | vauthors=Timchenko NA, Wilde M, Darlington GJ |title=C/EBPalpha regulates formation of S-phase-specific E2F-p107 complexes in livers of newborn mice. |journal=Mol. Cell. Biol. |volume=19 |issue= 4 |pages= 2936–45 |year= 1999 |pmid= 10082561 |doi= | pmc=84088 }}
*{{cite journal  | author=Müller H, Moroni MC, Vigo E, ''et al.'' |title=Induction of S-phase entry by E2F transcription factors depends on their nuclear localization. |journal=Mol. Cell. Biol. |volume=17 |issue= 9 |pages= 5508-20 |year= 1997 |pmid= 9271426 |doi=  }}
*{{cite journal  | vauthors=Zheng N, Fraenkel E, Pabo CO, Pavletich NP |title=Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP. |journal=Genes Dev. |volume=13 |issue= 6 |pages= 666–74 |year= 1999 |pmid= 10090723 |doi=10.1101/gad.13.6.666  | pmc=316551 }}
*{{cite journal  | author=Pierce AM, Schneider-Broussard R, Philhower JL, Johnson DG |title=Differential activities of E2F family members: unique functions in regulating transcription. |journal=Mol. Carcinog. |volume=22 |issue= 3 |pages= 190-8 |year= 1998 |pmid= 9688145 |doi=  }}
*{{cite journal  | vauthors=Furukawa Y, Iwase S, Kikuchi J |title=Transcriptional repression of the E2F-1 gene by interferon-alpha is mediated through induction of E2F-4/pRB and E2F-4/p130 complexes. |journal=Oncogene |volume=18 |issue= 11 |pages= 2003–14 |year= 1999 |pmid= 10208422 |doi= 10.1038/sj.onc.1202500 |display-authors=etal}}
*{{cite journal  | author=Ferreira R, Magnaghi-Jaulin L, Robin P, ''et al.'' |title=The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 18 |pages= 10493-8 |year= 1998 |pmid= 9724731 |doi=  }}
*{{cite journal  | vauthors=Lam EW, Glassford J, van der Sman J |title=Modulation of E2F activity in primary mouse B cells following stimulation via surface IgM and CD40 receptors. |journal=Eur. J. Immunol. |volume=29 |issue= 10 |pages= 3380–9 |year= 1999 |pmid= 10540350 |doi=10.1002/(SICI)1521-4141(199910)29:10<3380::AID-IMMU3380>3.0.CO;2-C  |display-authors=etal}}
*{{cite journal  | author=Timchenko NA, Wilde M, Darlington GJ |title=C/EBPalpha regulates formation of S-phase-specific E2F-p107 complexes in livers of newborn mice. |journal=Mol. Cell. Biol. |volume=19 |issue= 4 |pages= 2936-45 |year= 1999 |pmid= 10082561 |doi= }}
*{{cite journal  | vauthors=Zhong X, Hemmi H, Koike J |title=Various AGC repeat numbers in the coding region of the human transcription factor gene E2F-4. |journal=Hum. Mutat. |volume=15 |issue= 3 |pages= 296–7 |year= 2000 |pmid= 10679953 |doi= 10.1002/(SICI)1098-1004(200003)15:3<296::AID-HUMU18>3.0.CO;2-X |display-authors=etal}}
*{{cite journal  | author=Zheng N, Fraenkel E, Pabo CO, Pavletich NP |title=Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP. |journal=Genes Dev. |volume=13 |issue= 6 |pages= 666-74 |year= 1999 |pmid= 10090723 |doi= }}
*{{cite journal  | vauthors=Takahashi Y, Rayman JB, Dynlacht BD |title=Analysis of promoter binding by the E2F and pRB families in vivo: distinct E2F proteins mediate activation and repression. |journal=Genes Dev. |volume=14 |issue= 7 |pages= 804–16 |year= 2000 |pmid= 10766737 |doi= 10.1101/gad.14.7.804| pmc=316494 }}
*{{cite journal  | author=Furukawa Y, Iwase S, Kikuchi J, ''et al.'' |title=Transcriptional repression of the E2F-1 gene by interferon-alpha is mediated through induction of E2F-4/pRB and E2F-4/p130 complexes. |journal=Oncogene |volume=18 |issue= 11 |pages= 2003-14 |year= 1999 |pmid= 10208422 |doi= 10.1038/sj.onc.1202500 }}
*{{cite journal  | vauthors=Schwemmle S, Pfeifer GP |title=Genomic structure and mutation screening of the E2F4 gene in human tumors. |journal=Int. J. Cancer |volume=86 |issue= 5 |pages= 672–7 |year= 2000 |pmid= 10797289 |doi=10.1002/(SICI)1097-0215(20000601)86:5<672::AID-IJC11>3.0.CO;2-X  }}
*{{cite journal  | author=Lam EW, Glassford J, van der Sman J, ''et al.'' |title=Modulation of E2F activity in primary mouse B cells following stimulation via surface IgM and CD40 receptors. |journal=Eur. J. Immunol. |volume=29 |issue= 10 |pages= 3380-9 |year= 1999 |pmid= 10540350 |doi=  }}
*{{cite journal  | author=Zhong X, Hemmi H, Koike J, ''et al.'' |title=Various AGC repeat numbers in the coding region of the human transcription factor gene E2F-4. |journal=Hum. Mutat. |volume=15 |issue= 3 |pages= 296-7 |year= 2000 |pmid= 10679953 |doi= 10.1002/(SICI)1098-1004(200003)15:3<296::AID-HUMU18>3.0.CO;2-X }}
*{{cite journal | author=Takahashi Y, Rayman JB, Dynlacht BD |title=Analysis of promoter binding by the E2F and pRB families in vivo: distinct E2F proteins mediate activation and repression. |journal=Genes Dev. |volume=14 |issue= 7 |pages= 804-16 |year= 2000 |pmid= 10766737 |doi=  }}
*{{cite journal  | author=Schwemmle S, Pfeifer GP |title=Genomic structure and mutation screening of the E2F4 gene in human tumors. |journal=Int. J. Cancer |volume=86 |issue= 5 |pages= 672-7 |year= 2000 |pmid= 10797289 |doi=  }}
}}
{{refend}}
{{refend}}


== External links ==
== External links ==
* {{MeshName|E2F4+protein,+human}}
* {{MeshName|E2F4+protein,+human}}
* {{FactorBook|E2F4}}


{{NLM content}}
{{NLM content}}
{{PDB Gallery|geneid=1874}}
{{Transcription factors|g3}}
[[Category:Transcription factors]]
{{gene-16-stub}}
{{gene-16-stub}}
{{Transcription factors}}
[[Category:Transcription factors]]
{{WikiDoc Sources}}

Revision as of 00:25, 27 October 2017

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Identifiers
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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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View/Edit Human

Transcription factor E2F4 is a protein that in humans is encoded by the E2F4 gene.[1][2]

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. This protein binds to all three of the tumor suppressor proteins pRB, p107 and p130, but with higher affinity to the last two. It plays an important role in the suppression of proliferation-associated genes, and its gene mutation and increased expression may be associated with human cancer.[3]

Structure

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 (Asp + Glu), and a tumor suppressor protein association domain which is embedded within the transactivation domain.

Interactions

E2F4 has been shown to interact with Smad3.[4]

See also

References

  1. ↑ Ginsberg D, Vairo G, Chittenden T, Xiao ZX, Xu G, Wydner KL, DeCaprio JA, Lawrence JB, Livingston DM (Dec 1994). "E2F-4, a new member of the E2F transcription factor family, interacts with p107". Genes Dev. 8 (22): 2665–79. doi:10.1101/gad.8.22.2665. PMID 7958924.
  2. ↑ Sardet C, Vidal M, Cobrinik D, Geng Y, Onufryk C, Chen A, Weinberg RA (Apr 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.
  3. ↑ "Entrez Gene: E2F4 E2F transcription factor 4, p107/p130-binding".
  4. ↑ Chen CR, Kang Y, Siegel PM, Massagué J (July 2002). "E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression". Cell. 110 (1): 19–32. doi:10.1016/S0092-8674(02)00801-2. PMID 12150994.

Further reading

External links

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



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