+ |
CHD4 | down-regulates quantity by repression
transcriptional regulation
|
CD79A |
0.251 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254090 |
|
|
Mus musculus |
B-lymphocyte |
pmid |
sentence |
23071088 |
However, NuRD complexes greatly reduce activation of the B cell-specific mb-1 (Cd79a) gene by the transcription factors EBF1 and Pax5|We conclude that repressive functions of MBD2-containing NuRD complexes are dependent on cooperative interactions between the major domains of CHD4 with histones and DNA and on binding of methylated DNA by MBD2. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
CHD4 | form complex
binding
|
MBD3/NuRD complex |
0.828 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263856 |
|
|
Homo sapiens |
|
pmid |
sentence |
27098840 |
The NuRD complex is a multi-protein transcriptional corepressor that couples histone deacetylase and ATP-dependent chromatin remodelling activities.In humans, an assembly of proteins called the NuRD complex makes chromatin more compact by removing acetyl groups from nucleosomes. This complex is important for early development and for the stability and repair of our genes. Three proteins make up its core: HDAC1, which removes the acetyl group from the nucleosome; MTA1, which acts as a scaffold to hold the complex together; and RBBP4, which enables the complex to interact with nucleosomes. MBD2 and MBD3 are members of the methyl cytosine-guanosine (CpG)-binding domain (MBD) family of proteins42; 43. Of the five MBD members, only MBD2 and MBD3 associate with NuRD and are required for the complex formation and gene repression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CHD4 | form complex
binding
|
MBD2/NuRD complex |
0.809 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263844 |
|
|
Homo sapiens |
|
pmid |
sentence |
27098840 |
The NuRD complex is a multi-protein transcriptional corepressor that couples histone deacetylase and ATP-dependent chromatin remodelling activities.In humans, an assembly of proteins called the NuRD complex makes chromatin more compact by removing acetyl groups from nucleosomes. This complex is important for early development and for the stability and repair of our genes. Three proteins make up its core: HDAC1, which removes the acetyl group from the nucleosome; MTA1, which acts as a scaffold to hold the complex together; and RBBP4, which enables the complex to interact with nucleosomes. MBD2 and MBD3 are members of the methyl cytosine-guanosine (CpG)-binding domain (MBD) family of proteins42; 43. Of the five MBD members, only MBD2 and MBD3 associate with NuRD and are required for the complex formation and gene repression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MBD2 | down-regulates quantity by repression
transcriptional regulation
|
CHD4 |
0.616 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254102 |
|
|
Mus musculus |
B-lymphocyte |
pmid |
sentence |
23071088 |
MBD2 and multiple domains of CHD4 are required for transcriptional repression by Mi-2/NuRD complexes |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
CHD4 | form complex
binding
|
ChAHP |
0.421 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266752 |
|
|
Mus musculus |
HM-1 ES Cell |
pmid |
sentence |
29795351 |
Here we show that ADNP interacts with the chromatin remodeller CHD4 and the chromatin architectural protein HP1 to form a stable complex, which we refer to as ChAHP. Besides mediating complex assembly, ADNP recognizes DNA motifs that specify binding of ChAHP to euchromatin. In conclusion, CHD4, ADNP and HP1β/γ form a stable protein complex, which we refer to as ChAHP. |
|
Publications: |
1 |
Organism: |
Mus Musculus |