E2F3

Protein-coding gene in the species Homo sapiens
E2F3
Identifiers
AliasesE2F3, E2F-3, E2F transcription factor 3
External IDsOMIM: 600427 MGI: 1096340 HomoloGene: 74413 GeneCards: E2F3
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for E2F3
Genomic location for E2F3
Band6p22.3Start20,401,879 bp[1]
End20,493,714 bp[1]
Gene location (Mouse)
Chromosome 13 (mouse)
Chr.Chromosome 13 (mouse)[2]
Chromosome 13 (mouse)
Genomic location for E2F3
Genomic location for E2F3
Band13|13 A3.2Start30,090,558 bp[2]
End30,170,046 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Brodmann area 23

  • middle temporal gyrus

  • endothelial cell

  • tibia

  • visceral pleura

  • bone marrow

  • monocyte

  • embryo

  • trabecular bone

  • blood
Top expressed in
  • primitive streak

  • maxillary prominence

  • cumulus cell

  • medullary collecting duct

  • abdominal wall

  • atrium

  • hair follicle

  • atrioventricular valve

  • renal corpuscle

  • endocardial cushion
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • DNA-binding transcription factor activity
  • DNA binding
  • protein binding
  • protein dimerization activity
  • RNA polymerase II transcription regulatory region sequence-specific DNA binding
  • DNA-binding transcription activator activity, RNA polymerase II-specific
  • sequence-specific DNA binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
  • cis-regulatory region sequence-specific DNA binding
  • DNA-binding transcription repressor activity, RNA polymerase II-specific
  • transcription factor binding
Cellular component
  • nucleus
  • transcription regulator complex
  • RNA polymerase II transcription regulator complex
  • nucleoplasm
Biological process
  • positive regulation of transcription, DNA-templated
  • negative regulation of fat cell proliferation
  • cell cycle
  • transcription initiation from RNA polymerase II promoter
  • regulation of transcription, DNA-templated
  • transcription, DNA-templated
  • positive regulation of cell population proliferation
  • positive regulation of transcription by RNA polymerase II
  • positive regulation of vascular associated smooth muscle cell apoptotic process
  • negative regulation of transcription by RNA polymerase II
  • regulation of cell cycle
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

1871

13557

Ensembl

ENSG00000112242

ENSMUSG00000016477

UniProt

O00716

O35261

RefSeq (mRNA)

NM_001243076
NM_001949

NM_001289920
NM_010093
NM_001359994

RefSeq (protein)

NP_001230005
NP_001940

NP_001276849
NP_034223
NP_001346923

Location (UCSC)Chr 6: 20.4 – 20.49 MbChr 13: 30.09 – 30.17 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Transcription factor E2F3 is a protein that in humans is encoded by the E2F3 gene.[5]

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.[6]

Interactions

E2F3 has been shown to interact with TFE3[7] and RYBP.[8]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000112242 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000016477 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ "Entrez Gene: E2F3 E2F transcription factor 3".
  7. ^ 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.
  8. ^ 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. Bibcode:1996PNAS...93.7594R. 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. doi:10.1242/jcs.109.7.1717. 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. Bibcode:1997PNAS...94.5095L. 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. S2CID 42749241.
  • 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. doi:10.1101/gad.14.6.690. 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. 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

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


  • v
  • t
  • e
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies


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