E2F2

From Wikipedia, the free encyclopedia

E2F transcription factor 2

Identifiers

E2F2; E2F-2

External IDs

OMIM: 600426 MGI: 1096341 HomoloGene: 48264

Gene ontology
Molecular Function:	• transcription factor activity • RNA polymerase II transcription factor activity • protein binding
Cellular Component:	• nucleus • transcription factor complex
Biological Process:	• regulation of progression through cell cycle • transcription • regulation of transcription, DNA-dependent • transcription initiation from RNA polymerase II promoter • cell cycle

Orthologs

Human

Mouse

Refseq

NM_004091 (mRNA)
NP_004082 (protein)

NM_177733 (mRNA)
NP_808401 (protein)

Location

Chr 1: 23.71 - 23.73 Mb

Chr 4: 135.44 - 135.47 Mb

Pubmed search

[1]

[2]

E2F transcription factor 2, also known as E2F2, 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 and another 2 members, E2F1 and E2F3, have an additional cyclin binding domain. This protein binds specifically to retinoblastoma protein pRB in a cell-cycle dependent manner, and it exhibits overall 46% amino acid identity to E2F1.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

[edit] References

^ Entrez Gene: E2F2 E2F transcription factor 2.

[edit] Further reading

Dyson N (1998). "The regulation of E2F by pRB-family proteins.". Genes Dev. 12 (15): 2245–62. PMID 9694791.
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.
Ivey-Hoyle M, Conroy R, Huber HE, et al. (1994). "Cloning and characterization of E2F-2, a novel protein with the biochemical properties of transcription factor E2F.". Mol. Cell. Biol. 13 (12): 7802–12. PMID 8246995.
Lees JA, Saito M, Vidal M, et al. (1994). "The retinoblastoma protein binds to a family of E2F transcription factors.". Mol. Cell. Biol. 13 (12): 7813–25. PMID 8246996.
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.
Lin SY, Black AR, Kostic D, et al. (1996). "Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction.". Mol. Cell. Biol. 16 (4): 1668–75. PMID 8657142.
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. 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. 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. PMID 9144196.
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.
Halaban R, Cheng E, Smicun Y, Germino J (2000). "Deregulated E2F transcriptional activity in autonomously growing melanoma cells.". J. Exp. Med. 191 (6): 1005–16. PMID 10727462.
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.
Denis GV, Vaziri C, Guo N, Faller DV (2001). "RING3 kinase transactivates promoters of cell cycle regulatory genes through E2F.". Cell Growth Differ. 11 (8): 417–24. PMID 10965846.
Wu L, Timmers C, Maiti B, et al. (2001). "The E2F1-3 transcription factors are essential for cellular proliferation.". Nature 414 (6862): 457–62. doi:10.1038/35106593. PMID 11719808.
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. 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.
Crowley TE, Kaine EM, Yoshida M, et al. (2003). "Reproductive cycle regulation of nuclear import, euchromatic localization, and association with components of Pol II mediator of a mammalian double-bromodomain protein.". Mol. Endocrinol. 16 (8): 1727–37. PMID 12145330.
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. PMID 12411495.

[edit] External links

MeSH E2F2+protein,+human

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)	AP-2

(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	HIVEP1

(2.5) Alternating composition	AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B

(3) Helix-turn-helix
domains

(3.1) Homeo domain	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)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)

(3.4) Heat Shock Factors	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	p53

(4.4) MADS box	Mef2 (A, B, C, D) • SRF

(4.7) High mobility group	HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other
transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) • HBP1

(0.3) Pocket domain	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