E2F3

E2F transcription factor 3
Identifiers
Symbols	E2F3 ; E2F-3
External IDs	OMIM: 600427 MGI: 1096340 HomoloGene: 74413 GeneCards: E2F3 Gene
Gene ontology Molecular function • core promoter binding • transcription factor activity, sequence-specific DNA binding • protein binding Cellular component • nucleus • nucleoplasm • transcription factor complex • cytoplasm • Golgi apparatus • intracellular membrane-bounded organelle Biological process • mitotic cell cycle • transcription initiation from RNA polymerase II promoter • Notch signaling pathway • positive regulation of cell proliferation • positive regulation of transcription, DNA-templated • negative regulation of fat cell proliferation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1871	13557
Ensembl	ENSG00000112242	ENSMUSG00000016477
UniProt	O00716	O35261
RefSeq (mRNA)	NM_001243076	NM_001289920
RefSeq (protein)	NP_001230005	NP_001276849
Location (UCSC)	Chr 6: 20.4 – 20.49 Mb	Chr 13: 29.91 – 29.99 Mb
PubMed search

Transcription factor E2F3 is a protein that in humans is encoded by the E2F3 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 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]

Interactions

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

See also

• E2F

References

1. Lees JA, Saito M, Vidal M, Valentine M, Look T, Harlow E, Dyson N, Helin K (Dec 1993). "The retinoblastoma protein binds to a family of E2F transcription factors". Molecular and Cellular Biology 13 (12): 7813–25. doi:10.1128/mcb.13.12.7813. PMC 364853. PMID 8246996.
2. "Entrez Gene: E2F3 E2F transcription factor 3".
3. Giangrande PH, Hallstrom TC, Tunyaplin C, Calame K, Nevins JR (Jun 2003). "Identification of E-box factor TFE3 as a functional partner for the E2F3 transcription factor". Molecular and Cellular Biology 23 (11): 3707–20. doi:10.1128/MCB.23.11.3707-3720.2003. PMC 155231. PMID 12748276.
4. Schlisio S, Halperin T, Vidal M, Nevins JR (Nov 2002). "Interaction of YY1 with E2Fs, mediated by RYBP, provides a mechanism for specificity of E2F function". The EMBO Journal 21 (21): 5775–86. doi:10.1093/emboj/cdf577. PMC 131074. PMID 12411495.

Further reading

• Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S (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 Research 1 (5): 223–9. doi:10.1093/dnares/1.5.223. PMID 7584044.
• Wu CL, Zukerberg LR, Ngwu C, Harlow E, Lees JA (May 1995). "In vivo association of E2F and DP family proteins". Molecular and Cellular Biology 15 (5): 2536–46. doi:10.1128/mcb.15.5.2536. PMC 230484. PMID 7739537.
• Karlseder J, Rotheneder H, Wintersberger E (Apr 1996). "Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F". Molecular and Cellular Biology 16 (4): 1659–67. doi:10.1128/mcb.16.4.1659. PMC 231152. PMID 8657141.
• Rogers KT, Higgins PD, Milla MM, Phillips RS, Horowitz JM (Jul 1996). "DP-2, a heterodimeric partner of E2F: identification and characterization of DP-2 proteins expressed in vivo". Proceedings of the National Academy of Sciences of the United States of America 93 (15): 7594–9. doi:10.1073/pnas.93.15.7594. PMC 38791. PMID 8755520.
• Magae J, Wu CL, Illenye S, Harlow E, Heintz NH (Jul 1996). "Nuclear localization of DP and E2F transcription factors by heterodimeric partners and retinoblastoma protein family members". Journal of Cell Science 109 (7): 1717–26. PMID 8832394.
• Hofmann F, Livingston DM (Apr 1996). "Differential effects of cdk2 and cdk3 on the control of pRb and E2F function during G1 exit". Genes & Development 10 (7): 851–61. doi:10.1101/gad.10.7.851. PMID 8846921.
• 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.
• Dynlacht BD, Moberg K, Lees JA, Harlow E, Zhu L (Jul 1997). "Specific regulation of E2F family members by cyclin-dependent kinases". Molecular and Cellular Biology 17 (7): 3867–75. doi:10.1128/mcb.17.7.3867. PMC 232239. PMID 9199321.
• Pierce AM, Schneider-Broussard R, Philhower JL, Johnson DG (Jul 1998). "Differential activities of E2F family members: unique functions in regulating transcription". Molecular Carcinogenesis 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, Rogers C, Dandapani S, Lees JA (Mar 2000). "E2f3 is critical for normal cellular proliferation". Genes & Development 14 (6): 690–703. PMC 316459. PMID 10733529.
• Takahashi Y, Rayman JB, Dynlacht BD (Apr 2000). "Analysis of promoter binding by the E2F and pRB families in vivo: distinct E2F proteins mediate activation and repression". Genes & Development 14 (7): 804–16. doi:10.1101/gad.14.7.804. PMC 316494. PMID 10766737.
• Leone G, Nuckolls F, Ishida S, Adams M, Sears R, Jakoi L, Miron A, Nevins JR (May 2000). "Identification of a novel E2F3 product suggests a mechanism for determining specificity of repression by Rb proteins". Molecular and Cellular Biology 20 (10): 3626–32. doi:10.1128/MCB.20.10.3626-3632.2000. PMC 85655. PMID 10779352.
• He Y, Armanious MK, Thomas MJ, Cress WD (Jul 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, Mizumoto K, Sato H, Matsuura Y, Nishimoto I, Matsuoka M (Dec 2001). "ik3-1/Cables is a substrate for cyclin-dependent kinase 3 (cdk 3)". European Journal of Biochemistry / FEBS 268 (23): 6076–82. doi:10.1046/j.0014-2956.2001.02555.x. PMID 11733001.
• Weinmann AS, Yan PS, Oberley MJ, Huang TH, Farnham PJ (Jan 2002). "Isolating human transcription factor targets by coupling chromatin immunoprecipitation and CpG island microarray analysis". Genes & Development 16 (2): 235–44. doi:10.1101/gad.943102. PMC 155318. PMID 11799066.
• Ren B, Cam H, Takahashi Y, Volkert T, Terragni J, Young RA, Dynlacht BD (Jan 2002). "E2F integrates cell cycle progression with DNA repair, replication, and G(2)/M checkpoints". Genes & Development 16 (2): 245–56. doi:10.1101/gad.949802. PMC 155321. PMID 11799067.
• He Y, Cress WD (Jun 2002). "E2F-3B is a physiological target of cyclin A". The Journal of Biological Chemistry 277 (26): 23493–9. doi:10.1074/jbc.M202629200. PMID 11980909.
• Schlisio S, Halperin T, Vidal M, Nevins JR (Nov 2002). "Interaction of YY1 with E2Fs, mediated by RYBP, provides a mechanism for specificity of E2F function". The EMBO Journal 21 (21): 5775–86. doi:10.1093/emboj/cdf577. PMC 131074. PMID 12411495.

External links

• E2F3 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.