World Library  
Flag as Inappropriate
Email this Article

E2f2

Article Id: WHEBN0014170793
Reproduction Date:

Title: E2f2  
Author: World Heritage Encyclopedia
Language: English
Subject: Retinoblastoma protein, Transcription factors, NeuroD, EMX homeogene, HOXC8
Collection: Transcription Factors
Publisher: World Heritage Encyclopedia
Publication
Date:
 

E2f2

E2F transcription factor 2
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; E2F-2
External IDs GeneCards:
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Transcription factor E2F2 is a protein that in humans is encoded by the E2F2 gene.[1][2] 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.[3]

Contents

  • Interactions 1
  • See also 2
  • References 3
  • Further reading 4
  • External links 5

Interactions

E2F2 has been shown to interact with BRD2,[4][5] Retinoblastoma protein[6] and RYBP.[7]

See also

References

  1. ^ Ivey-Hoyle M, Conroy R, Huber HE, Goodhart PJ, Oliff A, Heimbrook DC (January 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.  
  2. ^ Lees JA, Saito M, Vidal M, Valentine M, Look T, Harlow E, Dyson N, Helin K (January 1994). "The retinoblastoma protein binds to a family of E2F transcription factors". Mol Cell Biol 13 (12): 7813–25.  
  3. ^ "Entrez Gene: E2F2 E2F transcription factor 2". 
  4. ^ Crowley, Thomas E; Kaine Emily M; Yoshida Manabu; Nandi Anindita; Wolgemuth Debra J (August 2002). "Reproductive cycle regulation of nuclear import, euchromatic localization, and association with components of Pol II mediator of a mammalian double-bromodomain protein". Mol. Endocrinol. (United States) 16 (8): 1727–37.  
  5. ^ Denis, G V; Vaziri C; Guo N; Faller D V (August 2000). "RING3 kinase transactivates promoters of cell cycle regulatory genes through E2F". Cell Growth Differ. (UNITED STATES) 11 (8): 417–24.  
  6. ^ Lee, Changwook; Chang Jeong Ho; Lee Hyun Sook; Cho Yunje (December 2002). "Structural basis for the recognition of the E2F transactivation domain by the retinoblastoma tumor suppressor". Genes Dev. (United States) 16 (24): 3199–212.  
  7. ^ Schlisio, Susanne; Halperin Terri; Vidal Miguel; Nevins Joseph R (November 2002). "Interaction of YY1 with E2Fs, mediated by RYBP, provides a mechanism for specificity of E2F function". EMBO J. (England) 21 (21): 5775–86.  

Further reading

  • Dyson N (1998). "The regulation of E2F by pRB-family proteins.". Genes Dev. 12 (15): 2245–62.  
  • Wu CL, Zukerberg LR, Ngwu C, (1995). "In vivo association of E2F and DP family proteins". Mol. Cell. Biol. 15 (5): 2536–46.  
  • 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.  
  • Lin SY, Black AR, Kostic D, (1996). "Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction". Mol. Cell. Biol. 16 (4): 1668–75.  
  • Rogers KT, Higgins PD, Milla MM, (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.  
  • Magae J, Wu CL, Illenye S, (1997). "Nuclear localization of DP and E2F transcription factors by heterodimeric partners and retinoblastoma protein family members". J. Cell. Sci. 109 (7): 1717–26.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • Wu L, Timmers C, Maiti B, (2001). "The E2F1-3 transcription factors are essential for cellular proliferation". Nature 414 (6862): 457–62.  
  • Yamochi T, Semba K, Tsuji K, (2002). "ik3-1/Cables is a substrate for cyclin-dependent kinase 3 (cdk 3)". Eur. J. Biochem. 268 (23): 6076–82.  
  • Weinmann AS, Yan PS, Oberley MJ, (2002). "Isolating human transcription factor targets by coupling chromatin immunoprecipitation and CpG island microarray analysis". Genes Dev. 16 (2): 235–44.  
  • Crowley TE, Kaine EM, Yoshida M, (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.  
  • 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.  

External links

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



This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and USA.gov, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for USA.gov and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
 
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
 
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.
 


Copyright © World Library Foundation. All rights reserved. eBooks from Project Gutenberg are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.