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E2F transcription factor 3
Identifiers
Symbols E2F3; DKFZp686C18211; E2F-3; KIAA0075; MGC104598
External IDs OMIM600427 MGI1096340 HomoloGene74413 GeneCards: E2F3 Gene
RNA expression pattern
PBB GE E2F3 203692 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1871 13557
Ensembl ENSG00000112242 ENSMUSG00000016477
UniProt O00716 Q3TMJ9
RefSeq (mRNA) NM_001949 NM_010093
RefSeq (protein) NP_001940 NP_034223
Location (UCSC) Chr 6:
20.51 - 20.6 Mb
Chr 13:
29.91 - 29.99 Mb
PubMed search [1] [2]

Transcription factor E2F3 is a protein that in humans is encoded by the E2F3 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 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, E2F1 and E2F2, have an additional cyclin binding domain. This protein binds specifically to retinoblastoma protein pRB in a cell-cycle dependent manner. Alternative gene splicing is found in the mouse homolog, but has not reported in human yet.[2]

Contents

Interactions

E2F3 has been shown to interact with TFE3[3] and RYBP.[4]

See also

References

  1. ^ Lees JA, Saito M, Vidal M, Valentine M, Look T, Harlow E, Dyson N, Helin K (Jan 1994). "The retinoblastoma protein binds to a family of E2F transcription factors". Mol Cell Biol 13 (12): 7813–25. PMID 8246996.  
  2. ^ "Entrez Gene: E2F3 E2F transcription factor 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1871.  
  3. ^ Giangrande, Paloma H; Hallstrom Timothy C, Tunyaplin Chainarong, Calame Kathryn, Nevins Joseph R (Jun. 2003). "Identification of E-box factor TFE3 as a functional partner for the E2F3 transcription factor". Mol. Cell. Biol. (United States) 23 (11): 3707–20. ISSN 0270-7306. PMID 12748276.  
  4. ^ Schlisio, Susanne; Halperin Terri, Vidal Miguel, Nevins Joseph R (Nov. 2002). "Interaction of YY1 with E2Fs, mediated by RYBP, provides a mechanism for specificity of E2F function". EMBO J. (England) 21 (21): 5775–86. ISSN 0261-4189. PMID 12411495.  

Further reading

  • Nomura N, Nagase T, Miyajima N, et al. (1995). "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1.". DNA Res. 1 (5): 223–9. doi:10.1093/dnares/1.5.223. PMID 7584044.  
  • Wu CL, Zukerberg LR, Ngwu C, et al. (1995). "In vivo association of E2F and DP family proteins.". Mol. Cell. Biol. 15 (5): 2536–46. PMID 7739537.  
  • Karlseder J, Rotheneder H, Wintersberger E (1996). "Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F.". Mol. Cell. Biol. 16 (4): 1659–67. PMID 8657141.  
  • Rogers KT, Higgins PD, Milla MM, et al. (1996). "DP-2, a heterodimeric partner of E2F: identification and characterization of DP-2 proteins expressed in vivo.". Proc. Natl. Acad. Sci. U.S.A. 93 (15): 7594–9. doi:10.1073/pnas.93.15.7594. PMID 8755520.  
  • Magae J, Wu CL, Illenye S, et al. (1997). "Nuclear localization of DP and E2F transcription factors by heterodimeric partners and retinoblastoma protein family members.". J. Cell. Sci. 109 ( Pt 7): 1717–26. PMID 8832394.  
  • Hofmann F, Livingston DM (1996). "Differential effects of cdk2 and cdk3 on the control of pRb and E2F function during G1 exit.". Genes Dev. 10 (7): 851–61. doi:10.1101/gad.10.7.851. PMID 8846921.  
  • 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. doi:10.1073/pnas.94.10.5095. PMID 9144196.  
  • Dynlacht BD, Moberg K, Lees JA, et al. (1997). "Specific regulation of E2F family members by cyclin-dependent kinases.". Mol. Cell. Biol. 17 (7): 3867–75. PMID 9199321.  
  • Pierce AM, Schneider-Broussard R, Philhower JL, Johnson DG (1998). "Differential activities of E2F family members: unique functions in regulating transcription.". Mol. Carcinog. 22 (3): 190–8. doi:10.1002/(SICI)1098-2744(199807)22:3<190::AID-MC7>3.0.CO;2-P. PMID 9688145.  
  • Humbert PO, Verona R, Trimarchi JM, et al. (2000). "E2f3 is critical for normal cellular proliferation.". Genes Dev. 14 (6): 690–703. PMID 10733529.  
  • Takahashi Y, Rayman JB, Dynlacht BD (2000). "Analysis of promoter binding by the E2F and pRB families in vivo: distinct E2F proteins mediate activation and repression.". Genes Dev. 14 (7): 804–16. PMID 10766737.  
  • Leone G, Nuckolls F, Ishida S, et al. (2000). "Identification of a novel E2F3 product suggests a mechanism for determining specificity of repression by Rb proteins.". Mol. Cell. Biol. 20 (10): 3626–32. doi:10.1128/MCB.20.10.3626-3632.2000. PMID 10779352.  
  • He Y, Armanious MK, Thomas MJ, Cress WD (2000). "Identification of E2F-3B, an alternative form of E2F-3 lacking a conserved N-terminal region.". Oncogene 19 (30): 3422–33. doi:10.1038/sj.onc.1203682. PMID 10918599.  
  • Yamochi T, Semba K, Tsuji K, et al. (2002). "ik3-1/Cables is a substrate for cyclin-dependent kinase 3 (cdk 3).". Eur. J. Biochem. 268 (23): 6076–82. doi:10.1046/j.0014-2956.2001.02555.x. PMID 11733001.  
  • Weinmann AS, Yan PS, Oberley MJ, et al. (2002). "Isolating human transcription factor targets by coupling chromatin immunoprecipitation and CpG island microarray analysis.". Genes Dev. 16 (2): 235–44. doi:10.1101/gad.943102. PMID 11799066.  
  • Ren B, Cam H, Takahashi Y, et al. (2002). "E2F integrates cell cycle progression with DNA repair, replication, and G(2)/M checkpoints.". Genes Dev. 16 (2): 245–56. doi:10.1101/gad.949802. PMID 11799067.  
  • He Y, Cress WD (2002). "E2F-3B is a physiological target of cyclin A.". J. Biol. Chem. 277 (26): 23493–9. doi:10.1074/jbc.M202629200. PMID 11980909.  
  • Schlisio S, Halperin T, Vidal M, Nevins JR (2002). "Interaction of YY1 with E2Fs, mediated by RYBP, provides a mechanism for specificity of E2F function.". Embo J. 21 (21): 5775–86. doi:10.1093/emboj/cdf577. PMID 12411495.  
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.  

External links

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

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