E2F5

E2F transcription factor 5, p130-binding
PDB rendering based on 1cf7.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1cf7​
Identifiers
Symbols	E2F5 ; E2F-5
External IDs	OMIM: 600967 MGI: 105091 HomoloGene: 1472 GeneCards: E2F5 Gene
Gene ontology Molecular function • DNA binding • transcription factor activity, sequence-specific DNA binding • protein binding • transcription factor binding Cellular component • nucleus • nucleoplasm • transcription factor complex • nucleolus • cytoplasm Biological process • mitotic cell cycle • transcription, DNA-templated • transcription initiation from RNA polymerase II promoter • transforming growth factor beta receptor signaling pathway • organ morphogenesis • gene expression • cell projection organization • positive regulation of transcription from RNA polymerase II promoter • regulation of cell cycle Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1875	13559
Ensembl	ENSG00000133740	ENSMUSG00000027552
UniProt	Q15329	Q61502
RefSeq (mRNA)	NM_001083588	NM_007892
RefSeq (protein)	NP_001077057	NP_031918
Location (UCSC)	Chr 8: 85.18 – 85.22 Mb	Chr 3: 14.58 – 14.61 Mb
PubMed search

Transcription factor E2F5 is a protein that in humans is encoded by the E2F5 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. 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.^[2]

Interactions

E2F5 has been shown to interact with TFDP1.^[1][3]

See also

• E2F

References

1. Sardet C, Vidal M, Cobrinik D, Geng Y, Onufryk C, Chen A, Weinberg RA (Mar 1995). "E2F-4 and E2F-5, two members of the E2F family, are expressed in the early phases of the cell cycle". Proceedings of the National Academy of Sciences of the United States of America 92 (6): 2403–7. doi:10.1073/pnas.92.6.2403. PMC 42492. PMID 7892279.
2. "Entrez Gene: E2F5 E2F transcription factor 5, p130-binding".
3. Hijmans EM, Voorhoeve PM, Beijersbergen RL, van 't Veer LJ, Bernards R (Jun 1995). "E2F-5, a new E2F family member that interacts with p130 in vivo". Molecular and Cellular Biology 15 (6): 3082–9. doi:10.1128/mcb.15.6.3082. PMC 230539. PMID 7760804.

Further reading

• Hijmans EM, Voorhoeve PM, Beijersbergen RL, van 't Veer LJ, Bernards R (Jun 1995). "E2F-5, a new E2F family member that interacts with p130 in vivo". Molecular and Cellular Biology 15 (6): 3082–9. doi:10.1128/mcb.15.6.3082. PMC 230539. PMID 7760804.
• Ginsberg D, Vairo G, Chittenden T, Xiao ZX, Xu G, Wydner KL, DeCaprio JA, Lawrence JB, Livingston DM (Nov 1994). "E2F-4, a new member of the E2F transcription factor family, interacts with p107". Genes & Development 8 (22): 2665–79. doi:10.1101/gad.8.22.2665. PMID 7958924.
• Beijersbergen RL, Kerkhoven RM, Zhu L, Carlée L, Voorhoeve PM, Bernards R (Nov 1994). "E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo". Genes & Development 8 (22): 2680–90. doi:10.1101/gad.8.22.2680. PMID 7958925.
• Itoh A, Levinson SF, Morita T, Kourembanas S, Brody JS, Mitsialis SA (1996). "Structural characterization and specificity of expression of E2F-5: a new member of the E2F family of transcription factors". Cellular & Molecular Biology Research 41 (3): 147–54. PMID 8589754.
• Lindeman GJ, Gaubatz S, Livingston DM, Ginsberg D (May 1997). "The subcellular localization of E2F-4 is cell-cycle dependent". Proceedings of the National Academy of Sciences of the United States of America 94 (10): 5095–100. doi:10.1073/pnas.94.10.5095. PMC 24637. PMID 9144196.
• Vaishnav YN, Vaishnav MY, Pant V (Jan 1998). "The molecular and functional characterization of E2F-5 transcription factor". Biochemical and Biophysical Research Communications 242 (3): 586–92. doi:10.1006/bbrc.1997.8010. PMID 9464260.
• Morris L, Allen KE, La Thangue NB (Apr 2000). "Regulation of E2F transcription by cyclin E-Cdk2 kinase mediated through p300/CBP co-activators". Nature Cell Biology 2 (4): 232–9. doi:10.1038/35008660. PMID 10783242.
• Gaubatz S, Lindeman GJ, Ishida S, Jakoi L, Nevins JR, Livingston DM, Rempel RE (Sep 2000). "E2F4 and E2F5 play an essential role in pocket protein-mediated G1 control". Molecular Cell 6 (3): 729–35. doi:10.1016/S1097-2765(00)00071-X. PMID 11030352.
• D'Souza SJ, Pajak A, Balazsi K, Dagnino L (Jun 2001). "Ca2+ and BMP-6 signaling regulate E2F during epidermal keratinocyte differentiation". The Journal of Biological Chemistry 276 (26): 23531–8. doi:10.1074/jbc.M100780200. PMID 11319226.
• Chestukhin A, Litovchick L, Rudich K, DeCaprio JA (Jan 2002). "Nucleocytoplasmic shuttling of p130/RBL2: novel regulatory mechanism". Molecular and Cellular Biology 22 (2): 453–68. doi:10.1128/MCB.22.2.453-468.2002. PMC 139733. PMID 11756542.
• Apostolova MD, Ivanova IA, Dagnino C, D'Souza SJ, Dagnino L (Sep 2002). "Active nuclear import and export pathways regulate E2F-5 subcellular localization". The Journal of Biological Chemistry 277 (37): 34471–9. doi:10.1074/jbc.M205827200. PMID 12089160.
• Chen CR, Kang Y, Siegel PM, Massagué J (Jul 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.
• Macaluso M, Cinti C, Russo G, Russo A, Giordano A (Jun 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, Sanij E, Hertzog P, Wolvetang E, Ghysdael J, Rowe M, Hara E (Jul 2003). "Epstein-Barr virus LMP1 blocks p16INK4a-RB pathway by promoting nuclear export of E2F4/5". The Journal of Cell Biology 162 (2): 173–83. doi:10.1083/jcb.200302085. PMC 2172795. PMID 12860972.
• Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (Jun 2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nature Biotechnology 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
• Jiang Y, Saavedra HI, Holloway MP, Leone G, Altura RA (Sep 2004). "Aberrant regulation of survivin by the RB/E2F family of proteins". The Journal of Biological Chemistry 279 (39): 40511–20. doi:10.1074/jbc.M404496200. PMID 15271987.
• Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (Sep 2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Research 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
• Joshi B, Ordonez-Ercan D, Dasgupta P, Chellappan S (Mar 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". The International Journal of Developmental Biology 49 (7): 859–65. doi:10.1387/ijdb.051996as. PMID 16172982.

External links

• E2F5 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)

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