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EMD — SMARCB1

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: EMD — SMARCB1 (physical association, affinity chromatography technology) Holaska et al., Biochemistry 2007
• MIPS CORUM Emerin complex 32: Emerin complex 32 complex (ACTB-BANF2-CHD4-DPY30-EMD-HDAC1-HDAC3-HIST1H3B-HIST1H3C-HIST1H3A-HIST1H3F-HIST1H3G-HIST1H3D-HIST1H3E-HIST1H3J-HIST1H3H-HIST1H3I-LMNB1-MED4-NMI-RBL1-RBL2-RCOR1-SAP18-SMARCB1-SMARCC1-SMARCC2-SPTAN1-TBL1XR1-TBL1Y-TRIM28) Holaska et al., Biochemistry 2007
• IRef Corum Interaction: Complex of 94 proteins (association, ion exchange chromatography) Holaska et al., Biochemistry 2007

Text-mined interactions from Literome

Lee et al., J Cell Sci 2001 (Muscular Dystrophy, Emery-Dreifuss) : We show that emerin binds directly to barrier-to-autointegration factor (BAF), a DNA bridging protein, and that this binding to BAF requires conserved residues in the LEM-motif of emerin
Holaska et al., J Biol Chem 2003 : Although GCL alone can not explain the disease mechanism, our results strongly support gene expression models for Emery-Dreifuss muscular dystrophy by showing that emerin binds directly to a transcriptional repressor, GCL, and by suggesting that emerin-repressor complexes might be regulated by BAF
Jacque et al., Nature 2006 : Barrier-to-autointegration factor (BAF) , the LEM ( LAP, emerin, MAN ) binding partner of emerin, was required for the association of viral cDNA with emerin and for the ability of emerin to support virus infection