E2F4

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E2F transcription factor 4, p107/p130-binding
PDB rendering based on 1cf7.
Available structures: 1cf7
Identifiers
Symbol(s) E2F4; E2F-4
External IDs OMIM: 600659 MGI: 103012 HomoloGene: 1471
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 1874 104394
Ensembl ENSG00000205250 ENSMUSG00000014859
Uniprot Q16254 n/a
Refseq NM_001950 (mRNA)
NP_001941 (protein)		 NM_148952 (mRNA)
NP_683754 (protein)
Location Chr 16: 65.78 - 65.79 Mb Chr 8: 108.19 - 108.19 Mb
Pubmed search [1] [2]

E2F transcription factor 4, p107/p130-binding, also known as E2F4, is a human gene.

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 binds to all three of the tumor suppressor proteins pRB, p107 and p130, but with higher affinity to the last two. It plays an important role in the suppression of proliferation-associated genes, and its gene mutation and increased expression may be associated with human cancer.[1]

Contents

[edit] See also

[edit] References

  1. ^ Entrez Gene: E2F4 E2F transcription factor 4, p107/p130-binding.

[edit] Further reading

  • Bandyopadhyay D, Timchenko N, Suwa T, et al. (2001). "The human melanocyte: a model system to study the complexity of cellular aging and transformation in non-fibroblastic cells.". Exp. Gerontol. 36 (8): 1265–75. PMID 11602203. 
  • 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. 
  • Xiao ZX, Ginsberg D, Ewen M, Livingston DM (1996). "Regulation of the retinoblastoma protein-related protein p107 by G1 cyclin-associated kinases.". Proc. Natl. Acad. Sci. U.S.A. 93 (10): 4633–7. PMID 8643455. 
  • Moberg K, Starz MA, Lees JA (1996). "E2F-4 switches from p130 to p107 and pRB in response to cell cycle reentry.". Mol. Cell. Biol. 16 (4): 1436–49. PMID 8657117. 
  • Vidal M, Brachmann RK, Fattaey A, et al. (1996). "Reverse two-hybrid and one-hybrid systems to detect dissociation of protein-protein and DNA-protein interactions.". Proc. Natl. Acad. Sci. U.S.A. 93 (19): 10315–20. PMID 8816797. 
  • Williams CD, Linch DC, Sørensen TS, et al. (1997). "The predominant E2F complex in human primary haemopoietic cells and in AML blasts contains E2F-4, DP-1 and p130.". Br. J. Haematol. 96 (4): 688–96. PMID 9074408. 
  • 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. 
  • Wang H, Shao N, Ding QM, et al. (1997). "BRCA1 proteins are transported to the nucleus in the absence of serum and splice variants BRCA1a, BRCA1b are tyrosine phosphoproteins that associate with E2F, cyclins and cyclin dependent kinases.". Oncogene 15 (2): 143–57. doi:10.1038/sj.onc.1201252. PMID 9244350. 
  • Müller H, Moroni MC, Vigo E, et al. (1997). "Induction of S-phase entry by E2F transcription factors depends on their nuclear localization.". Mol. Cell. Biol. 17 (9): 5508–20. PMID 9271426. 
  • 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. PMID 9688145. 
  • Ferreira R, Magnaghi-Jaulin L, Robin P, et al. (1998). "The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase.". Proc. Natl. Acad. Sci. U.S.A. 95 (18): 10493–8. PMID 9724731. 
  • Timchenko NA, Wilde M, Darlington GJ (1999). "C/EBPalpha regulates formation of S-phase-specific E2F-p107 complexes in livers of newborn mice.". Mol. Cell. Biol. 19 (4): 2936–45. PMID 10082561. 
  • Zheng N, Fraenkel E, Pabo CO, Pavletich NP (1999). "Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP.". Genes Dev. 13 (6): 666–74. PMID 10090723. 
  • Furukawa Y, Iwase S, Kikuchi J, et al. (1999). "Transcriptional repression of the E2F-1 gene by interferon-alpha is mediated through induction of E2F-4/pRB and E2F-4/p130 complexes.". Oncogene 18 (11): 2003–14. doi:10.1038/sj.onc.1202500. PMID 10208422. 
  • Lam EW, Glassford J, van der Sman J, et al. (1999). "Modulation of E2F activity in primary mouse B cells following stimulation via surface IgM and CD40 receptors.". Eur. J. Immunol. 29 (10): 3380–9. PMID 10540350. 
  • Zhong X, Hemmi H, Koike J, et al. (2000). "Various AGC repeat numbers in the coding region of the human transcription factor gene E2F-4.". Hum. Mutat. 15 (3): 296–7. doi:10.1002/(SICI)1098-1004(200003)15:3<296::AID-HUMU18>3.0.CO;2-X. PMID 10679953. 
  • 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. 
  • Schwemmle S, Pfeifer GP (2000). "Genomic structure and mutation screening of the E2F4 gene in human tumors.". Int. J. Cancer 86 (5): 672–7. PMID 10797289. 

[edit] External links

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

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v • d • e
Transcription factors and intracellular receptors
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • BATF • BLZF1 • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3, L1) • CREM • DBP • DDIT3 • GABPA • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1
(1.2) Basic helix-loop-helix (bHLH)
ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1
(1.3) bHLH-ZIP
MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger
DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)
(2.2) Other Cys4
GATA (1, 2, 3, 4, 5, 6) • MTA (1, 2, 3)
(2.3) Cys2His2
ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • zinc finger ((3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)
(2.4) Cys6
(2.5) Alternating composition
AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B
(3) Helix-turn-helix
domains
ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1
(3.2) Paired box
PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)
E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)
HSF (1, 2, 4)
(3.5) Tryptophan clusters
ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • ETV (1, 4, 5, 6) • FLI1 • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB • MYBL2
(3.6) TEA domain
transcriptional enhancer factor 1, 2
(4) β-Scaffold factors with
minor groove contacts
(4.1) Rel homology region
NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (C1, C2, C3, C4, 5)
(4.2) STAT
STAT (1, 2, 3, 4, 5, 6)
(4.3) p53
(4.4) MADS box
Mef2 (A, B, C, D) • SRF
HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1
(4.10) Cold-shock domain
(4.11) Runt
(0) Other
transcription factors
(0.2) HMGI(Y)
HMGA (1, 2) • HBP1
Rb • RBL1 • RBL2
(0.5) AP-2/EREBP-related factors
Apetala 2 • EREBP • B3
(0.6) Miscellaneous
ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • IFI (16, 35) • MLL (2, 3, T1) • MNDA • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD