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E2F5 - Wikipedia, the free encyclopedia

E2F5

From Wikipedia, the free encyclopedia


E2F transcription factor 5, p130-binding
PDB rendering based on 1cf7.
Available structures: 1cf7
Identifiers
Symbol(s) E2F5; E2F-5
External IDs OMIM: 600967 MGI105091 HomoloGene1472
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 1875 13559
Ensembl ENSG00000133740 ENSMUSG00000027552
Uniprot Q15329 Q99LK0
Refseq NM_001951 (mRNA)
NP_001942 (protein)
NM_007892 (mRNA)
NP_031918 (protein)
Location Chr 8: 86.28 - 86.31 Mb Chr 3: 14.56 - 14.58 Mb
Pubmed search [1] [2]

E2F transcription factor 5, p130-binding, also known as E2F5, is a human 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 evolutionarily conserved domains that are present 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 is differentially phosphorylated and is expressed in a wide variety of human tissues. It has higher identity to E2F4 than to other family members. Both this protein and E2F4 interact with tumor suppressor proteins p130 and p107, but not with pRB. Alternative splicing results in multiple variants encoding different isoforms.[1]

Contents

[edit] See also

[edit] References

[edit] Further reading

  • Hijmans EM, Voorhoeve PM, Beijersbergen RL, et al. (1995). "E2F-5, a new E2F family member that interacts with p130 in vivo.". Mol. Cell. Biol. 15 (6): 3082–9. PMID 7760804. 
  • Sardet C, Vidal M, Cobrinik D, et al. (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. PMID 7892279. 
  • Ginsberg D, Vairo G, Chittenden T, et al. (1994). "E2F-4, a new member of the E2F transcription factor family, interacts with p107.". Genes Dev. 8 (22): 2665–79. PMID 7958924. 
  • Beijersbergen RL, Kerkhoven RM, Zhu L, et al. (1994). "E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo.". Genes Dev. 8 (22): 2680–90. PMID 7958925. 
  • Itoh A, Levinson SF, Morita T, et al. (1996). "Structural characterization and specificity of expression of E2F-5: a new member of the E2F family of transcription factors.". Cell. Mol. Biol. Res. 41 (3): 147–54. PMID 8589754. 
  • Lindeman GJ, Gaubatz S, Livingston DM, Ginsberg D (1997). "The subcellular localization of E2F-4 is cell-cycle dependent.". Proc. Natl. Acad. Sci. U.S.A. 94 (10): 5095–100. PMID 9144196. 
  • Vaishnav YN, Vaishnav MY, Pant V (1998). "The molecular and functional characterization of E2F-5 transcription factor.". Biochem. Biophys. Res. Commun. 242 (3): 586–92. doi:10.1006/bbrc.1997.8010. PMID 9464260. 
  • Morris L, Allen KE, La Thangue NB (2000). "Regulation of E2F transcription by cyclin E-Cdk2 kinase mediated through p300/CBP co-activators.". Nat. Cell Biol. 2 (4): 232–9. doi:10.1038/35008660. PMID 10783242. 
  • Gaubatz S, Lindeman GJ, Ishida S, et al. (2000). "E2F4 and E2F5 play an essential role in pocket protein-mediated G1 control.". Mol. Cell 6 (3): 729–35. PMID 11030352. 
  • D'Souza SJ, Pajak A, Balazsi K, Dagnino L (2001). "Ca2+ and BMP-6 signaling regulate E2F during epidermal keratinocyte differentiation.". J. Biol. Chem. 276 (26): 23531–8. doi:10.1074/jbc.M100780200. PMID 11319226. 
  • Chestukhin A, Litovchick L, Rudich K, DeCaprio JA (2002). "Nucleocytoplasmic shuttling of p130/RBL2: novel regulatory mechanism.". Mol. Cell. Biol. 22 (2): 453–68. PMID 11756542. 
  • Apostolova MD, Ivanova IA, Dagnino C, et al. (2002). "Active nuclear import and export pathways regulate E2F-5 subcellular localization.". J. Biol. Chem. 277 (37): 34471–9. doi:10.1074/jbc.M205827200. PMID 12089160. 
  • Chen CR, Kang Y, Siegel PM, Massagué J (2002). "E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression.". Cell 110 (1): 19–32. PMID 12150994. 
  • Macaluso M, Cinti C, Russo G, et al. (2003). "pRb2/p130-E2F4/5-HDAC1-SUV39H1-p300 and pRb2/p130-E2F4/5-HDAC1-SUV39H1-DNMT1 multimolecular complexes mediate the transcription of estrogen receptor-alpha in breast cancer.". Oncogene 22 (23): 3511–7. doi:10.1038/sj.onc.1206578. PMID 12789259. 
  • Ohtani N, Brennan P, Gaubatz S, et al. (2003). "Epstein-Barr virus LMP1 blocks p16INK4a-RB pathway by promoting nuclear export of E2F4/5.". J. Cell Biol. 162 (2): 173–83. doi:10.1083/jcb.200302085. PMID 12860972. 
  • Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation.". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. 
  • Jiang Y, Saavedra HI, Holloway MP, et al. (2004). "Aberrant regulation of survivin by the RB/E2F family of proteins.". J. Biol. Chem. 279 (39): 40511–20. doi:10.1074/jbc.M404496200. PMID 15271987. 
  • Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions.". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMID 15342556. 
  • Joshi B, Ordonez-Ercan D, Dasgupta P, Chellappan S (2005). "Induction of human metallothionein 1G promoter by VEGF and heavy metals: differential involvement of E2F and metal transcription factors.". Oncogene 24 (13): 2204–17. doi:10.1038/sj.onc.1208206. PMID 15735762. 
  • Swetloff A, Ferretti P (2006). "Changes in E2F5 intracellular localization in mouse and human choroid plexus epithelium with development.". Int. J. Dev. Biol. 49 (7): 859–65. doi:10.1387/ijdb.051996as. PMID 16172982. 

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


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