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HDAC2 — MTA1

Pathways - manually collected, often from reviews:

• Reactome Reaction: HDAC2 → MTA1 (indirect_complex)

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: HDAC2 — MTA1 (physical association, affinity chromatography technology) Cui et al., Mol Cell Biol 2011
• IRef Biogrid Interaction: HDAC2 — MTA1 (physical association, affinity chromatography technology) Balasenthil et al., Cancer Res 2007*
• IRef Biogrid Interaction: HDAC2 — MTA1 (physical association, affinity chromatography technology) Xue et al., Mol Cell 1998
• IRef Biogrid Interaction: HDAC2 — MTA1 (physical association, affinity chromatography technology) Ohshiro et al., EMBO Rep 2010*
• IRef Biogrid Interaction: HDAC2 — MTA1 (physical association, affinity chromatography technology) Bantscheff et al., Nat Biotechnol 2011
• IRef Biogrid Interaction: HDAC2 — MTA1 (physical association, affinity chromatography technology) Joshi et al., Molecular systems biology 2013
• IRef Biogrid Interaction: HDAC2 — MTA1 (physical association, affinity chromatography technology) Yao et al., J Biol Chem 2003
• IRef Biogrid Interaction: HDAC2 — MTA1 (physical association, affinity chromatography technology) Hakimi et al., J Biol Chem 2003
• IRef Biogrid Interaction: HDAC2 — MTA1 (direct interaction, pull down) Mazumdar et al., Nat Cell Biol 2001
• IRef Biogrid Interaction: HDAC2 — MTA1 (physical association, affinity chromatography technology) Mazumdar et al., Nat Cell Biol 2001
• IRef Biogrid Interaction: HDAC2 — MTA1 (colocalization, imaging technique) Li et al., J Biol Chem 2010*
• IRef Biogrid Interaction: HDAC2 — MTA1 (physical association, affinity chromatography technology) Yan et al., J Biol Chem 2003*
• MIPS CORUM ESR1-CDK7-CCNH-MNAT1-MTA1-HDAC2 complex: ESR1-CDK7-CCNH-MNAT1-MTA1-HDAC2 complex complex (CCNH-CDK7-ESR1-HDAC2-MNAT1-MTA1) Talukder et al., J Biol Chem 2003
• MIPS CORUM SNF2h-cohesin-NuRD complex: SNF2h-cohesin-NuRD complex complex (BAZ1A-CHD3-HDAC1-HDAC2-MBD2-MBD3-MTA1-MTA2-RAD21-RBBP4-RBBP7-SMARCA5-SMC1A-SMC3-STAG1-STAG2) Hakimi et al., Nature 2002
• MIPS CORUM NuRD.1 complex: NuRD.1 complex complex (CHD4-HDAC2-MBD3-MTA1-MTA3-RBBP4-RBBP7) Xue et al., Mol Cell 1998
• MIPS CORUM NRD complex (Nucleosome remodeling and deacetylation complex): NRD complex (Nucleosome remodeling and deacetylation complex) complex (KDM1A-CHD3-CHD4-HDAC1-HDAC2-MTA1-RBBP4) Tong et al., Nature 1998
• MIPS CORUM Anti-HDAC2 complex: Anti-HDAC2 complex complex (KDM1A-CHD3-CHD4-GSE1-GTF2I-HDAC1-HDAC2-HMG20B-MTA1-MTA2-PHF21A-RBBP4-RBBP7-RCOR1-ZMYM2-ZMYM3-SIN3A-SIN3B) Hakimi et al., J Biol Chem 2003
• MIPS CORUM MTA1 complex: MTA1 complex complex (HDAC2-MBD3-MTA1-RBBP4-RBBP7) Yao et al., J Biol Chem 2003
• MIPS CORUM MTA1-HDAC core complex: MTA1-HDAC core complex complex (HDAC2-MTA1-RBBP4-RBBP7) Yao et al., J Biol Chem 2003
• IRef Corum Interaction: Complex of 33 proteins (association, ion exchange chromatography) Hakimi et al., Nature 2002
• IRef Corum Interaction: Complex of 11 proteins (association, chromatography technology) Yao et al., J Biol Chem 2003
• IRef Corum Interaction: Complex of 17 proteins (association, affinity chromatography technology) Xue et al., Mol Cell 1998
• IRef Corum Interaction: Complex of ESR1-CDK7-CCNH-MNAT1-MTA1-HDAC2 (association, coimmunoprecipitation) Talukder et al., J Biol Chem 2003
• IRef Corum Interaction: Complex of 37 proteins (association, anti bait coimmunoprecipitation) Hakimi et al., J Biol Chem 2003
• IRef Corum Interaction: Complex of 13 proteins (association, affinity chromatography technology) Yao et al., J Biol Chem 2003
• IRef Corum Interaction: Complex of HDAC2-CHD3-KDM1A-RBBP4-CHD4-MTA1-HDAC1 (association, anti bait coimmunoprecipitation) Tong et al., Nature 1998
• IRef Hprd Interaction: Complex of 257 proteins (in vivo) Hakimi et al., J Biol Chem 2003
• IRef Hprd Interaction: Complex of 50 proteins (in vivo) Yao et al., J Biol Chem 2003, Jiang et al., J Biol Chem 2004
• IRef Hprd Interaction: HDAC2 — MTA1 (in vitro) Mazumdar et al., Nat Cell Biol 2001
• IRef Hprd Interaction: HDAC2 — MTA1 (in vivo) Mazumdar et al., Nat Cell Biol 2001
• IRef Innatedb Interaction: HDAC2 — MTA1 (unknown, -) Yan et al., J Biol Chem 2003*
• IRef Intact Interaction: Complex of HDAC1-HDAC2-MTA1 (association, anti tag coimmunoprecipitation) Wang et al., EMBO Rep 2008
• IRef Intact Interaction: Complex of 30 proteins (association, tandem affinity purification) Pichlmair et al., Nature 2012
• IRef Intact Interaction: Complex of 26 proteins (association, anti bait coimmunoprecipitation) Bantscheff et al., Nat Biotechnol 2011
• IRef Intact Interaction: Complex of 40 proteins (association, anti bait coimmunoprecipitation) Bantscheff et al., Nat Biotechnol 2011
• IRef Intact Interaction: Complex of 92 proteins (association, anti tag coimmunoprecipitation) Joshi et al., Molecular systems biology 2013
• IRef Intact Interaction: Complex of 47 proteins (association, anti tag coimmunoprecipitation) Joshi et al., Molecular systems biology 2013
• IRef Intact Interaction: Complex of 11 proteins (association, anti bait coimmunoprecipitation) Opsahl et al., Proteomics 2010
• IRef Intact Interaction: Complex of 25 proteins (association, anti bait coimmunoprecipitation) Wang et al., Cell 2009
• IRef Intact Interaction: Complex of 14 proteins (association, anti bait coimmunoprecipitation) Bantscheff et al., Nat Biotechnol 2011
• IRef Intact Interaction: HDAC2 — MTA1 (physical association, anti bait coimmunoprecipitation) Ohshiro et al., EMBO Rep 2010*
• IRef Ophid Interaction: HDAC2 — MTA1 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Xiao et al., J Biol Chem 2000 : We further demonstrate that the N-terminal NRD interacts with the C-terminal region of NIK, thereby inhibiting the binding of NIK to its substrate IkappaB kinase ... Consistently, when expressed alone, the NRD potently inhibits NIK mediated NF-kappaB signaling
Van Komen et al., J Cell Biol 2006 : Our results suggest that the NRD is required for efficient t-SNARE complex formation and does not recruit necessary scaffolding factors
Manavathi et al., Proc Natl Acad Sci U S A 2007 : We discovered that MTA1 physically interacts with the Six3 chromatin in a histone deacetylase dependent manner, leading to transcriptional suppression of the Six3 gene
Molvaersmyr et al., Nucleic Acids Res 2010 : Thus, c-Myb harbours two AFs, one that is constitutively active and one in the NRD being SUMO regulated ( SRAF )
Borrmann et al., Neurochem Int 2011 (Neuroblastoma) : Here, we show that p42 ( IP4 ) enhances the enzymatic activity of NRD 3-4 times
Cong et al., J Biol Chem 2011 : SUMO conjugation on Lys-509, which is located within the SUMO consensus site, together with SIM synergistically regulates the co-repressor activity of MTA1 on PS2 transcription, probably by recruiting HDAC2 onto the PS2 promoter
Sonoda et al., Brain Res 1986 : The GSR was inhibited by electrical stimulation of the PAG/NRD
Brown et al., J Interferon Cytokine Res 1997 : The NRD ( NF-kappa B/Rel/Dorsal ) complexes induced by LPS and IFN-gamma were further characterized by addition of antisera to electrophoretic mobility shift assay ( EMSA ) reaction mixtures ... The NRD ( NF-kappa B/Rel/Dorsal ) complexes induced by LPS and IFN-gamma were further characterized by addition of antisera to electrophoretic mobility shift assay ( EMSA ) reaction mixtures
Kuhen et al., Virology 1999 : Deletion and substitution mutations indicated that the NRD negatively affected Pkr transcription by a mechanism dependent upon the KCS element