World Library  
Flag as Inappropriate
Email this Article


Article Id: WHEBN0014156063
Reproduction Date:

Title: Ilf3  
Author: World Heritage Encyclopedia
Language: English
Subject: FUS, NeuroD, EMX homeogene, Nur (biology), Early growth response proteins
Publisher: World Heritage Encyclopedia


Interleukin enhancer binding factor 3, 90kDa
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols  ; CBTF; DRBF; DRBP76; MMP4; MPHOSPH4; MPP4; NF-AT-90; NF110; NF110b; NF90; NF90a; NF90b; NFAR; NFAR-1; NFAR2; TCP110; TCP80
External IDs GeneCards:
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Interleukin enhancer-binding factor 3 is a protein that in humans is encoded by the ILF3 gene.[1][2] Nuclear factor of activated T-cells (NFAT) is a transcription factor required for T-cell expression of interleukin 2. NFAT binds to a sequence in the IL2 enhancer known as the antigen receptor response element 2. In addition, NFAT can bind RNA and is an essential component for encapsidation and protein priming of hepatitis B viral polymerase. NFAT is a heterodimer of 45 kDa and 90 kDa proteins, the larger of which is the product of this gene. The encoded protein, which is primarily localized to ribosomes, probably regulates transcription at the level of mRNA elongation. At least three transcript variants encoding three different isoforms have been found for this gene.[3]


ILF3 has been shown to interact with XPO5,[4] FUS,[5] Protein kinase R,[5][6][7][8] PRMT1[9][10] and DNA-PKcs.[11]


  1. ^ Kao PN, Chen L, Brock G, Ng J, Kenny J, Smith AJ, Corthesy B (September 1994). "Cloning and expression of cyclosporin A- and FK506-sensitive nuclear factor of activated T-cells: NF45 and NF90". J Biol Chem 269 (32): 20691–9.  
  2. ^ Matsumoto-Taniura N, Pirollet F, Monroe R, Gerace L, Westendorf JM (January 1997). "Identification of novel M phase phosphoproteins by expression cloning". Mol Biol Cell 7 (9): 1455–69.  
  3. ^ "Entrez Gene: ILF3 interleukin enhancer binding factor 3, 90kDa". 
  4. ^ Brownawell, Amy M; Macara Ian G (January 2002). "Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins". J. Cell Biol. (United States) 156 (1): 53–64.  
  5. ^ a b Saunders, L R; Perkins D J; Balachandran S; Michaels R; Ford R; Mayeda A; Barber G N (August 2001). "Characterization of two evolutionarily conserved, alternatively spliced nuclear phosphoproteins, NFAR-1 and -2, that function in mRNA processing and interact with the double-stranded RNA-dependent protein kinase, PKR". J. Biol. Chem. (United States) 276 (34): 32300–12.  
  6. ^ Langland, J O; Kao P N; Jacobs B L (May 1999). "Nuclear factor-90 of activated T-cells: A double-stranded RNA-binding protein and substrate for the double-stranded RNA-dependent protein kinase, PKR". Biochemistry (UNITED STATES) 38 (19): 6361–8.  
  7. ^ Parker, L M; Fierro-Monti I; Mathews M B (August 2001). "Nuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinase". J. Biol. Chem. (United States) 276 (35): 32522–30.  
  8. ^ Patel, R C; Vestal D J; Xu Z; Bandyopadhyay S; Guo W; Erme S M; Williams B R; Sen G C (July 1999). "DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR". J. Biol. Chem. (UNITED STATES) 274 (29): 20432–7.  
  9. ^ Tang, J; Kao P N; Herschman H R (June 2000). "Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3". J. Biol. Chem. (UNITED STATES) 275 (26): 19866–76.  
  10. ^ Lee, Jaeho; Bedford Mark T (March 2002). "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays". EMBO Rep. (England) 3 (3): 268–73.  
  11. ^ Ting, N S; Kao P N; Chan D W; Lintott L G; Lees-Miller S P (January 1998). "DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45". J. Biol. Chem. (UNITED STATES) 273 (4): 2136–45.  

Further reading

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, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for 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.