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HDAC3 — RUNX1

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: HDAC3 — RUNX1 (physical association, affinity chromatography technology) Reed-Inderbitzin et al., Oncogene 2006*
• IRef Biogrid Interaction: HDAC3 — RUNX1 (physical association, affinity chromatography technology) Guo et al., J Biol Chem 2011*
• IRef Biogrid Interaction: HDAC3 — RUNX1 (direct interaction, pull down) Guo et al., J Biol Chem 2011*

Text-mined interactions from Literome

Guo et al., J Biol Chem 2011 : Phosphorylation of RUNX1 by cyclin dependent kinase reduces direct interaction with HDAC1 and HDAC3
Lutterbach et al., Mol Cell Biol 1998 (Leukemia, Myeloid...) : Finally, AML-1/ETO associates with histone deacetylase activity and a histone deacetylase inhibitor impairs the ability of the fusion protein to repress transcription