Gene interactions and pathways from curated databases and text-mining

◀ Back to RELA

EGR1 — RELA

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Chapman et al., J Biol Chem 2000 : In this study we demonstrate that the early growth response transcription factor Egr-1 , whose DNA binding domain shares a high degree of homology with that of Sp1, can also interact with RelA in vitro and regulate NF-kappaB transcriptional activity in vivo ... Surprisingly, and in contrast to Sp1, Egr-1 specifically represses RelA transcriptional activity through its zinc finger domain
Thyss et al., EMBO J 2005 : Furthermore, we demonstrate that Egr-1 is induced upon UVB irradiation through NF-kappaB activation and the binding of p65/RelA within the Egr-1 promoter
Ma et al., J Biol Chem 2009 (Neoplasm Invasiveness...) : Furthermore, silencing EGR-1 suppressed a synergistically functional interaction between EGR-1 and NF-kappaB
Cogswell et al., J Exp Med 1997 : Characterization of the NF-kappa B1 promoter identified an Egr-1 site which was found to be essential for both the PMA/PHA mediated induction as well as the synergistic activation observed after the expression of the RelA subunit of NF-kappa B and Egr-1 ... Furthermore, Egr-1 induction was required for endogenous NF-kappa B1 gene expression, since PMA/PHA stimulated T cell lines expressing antisense Egr-1 RNA were inhibited in their ability to upregulate NF-kappa B1 transcription