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BCL3 — HDAC1

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

Studies that report less than 10 interactions are marked with *

• IRef Bind Interaction: HDAC1 — BCL3 Viatour et al., Mol Cell 2004*
• IRef Bind_translation Interaction: HDAC1 — BCL3 (coimmunoprecipitation) Viatour et al., Mol Cell 2004*
• IRef Biogrid Interaction: HDAC1 — BCL3 (physical association, affinity chromatography technology) Jamaluddin et al., J Virol 2005*
• IRef Biogrid Interaction: HDAC1 — BCL3 (physical association, affinity chromatography technology) Viatour et al., Mol Cell 2004*
• IRef Hprd Interaction: HDAC1 — BCL3 (in vivo) Viatour et al., Mol Cell 2004*

Text-mined interactions from Literome

Rocha et al., Mol Cell Biol 2003 : p53 represses cyclin D1 transcription through down regulation of Bcl-3 and inducing increased association of the p52 NF-kappaB subunit with histone deacetylase 1
Jamaluddin et al., J Virol 2005 : Nondenaturing co-IP assays indicate that nuclear Bcl-3 associates with STAT-1 and histone deacetylase 1 (HDAC-1), increasing HDAC-1 recruitment to the IL-8 promoter