+ |
SMARCD1 | form complex
binding
|
Embryonic stem cell-specific SWI/SNF |
0.748 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270722 |
|
|
Mus musculus |
Embryonic Stem Cell |
pmid |
sentence |
19279220 |
An embryonic stem cell chromatin remodeling complex, esBAF, is essential for embryonic stem cell self-renewal and pluripotency |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
SMARCD1 | form complex
binding
|
Muscle cell-specific SWI/SNF ARID1B variant |
0.789 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270707 |
|
|
Homo sapiens |
|
pmid |
sentence |
11073988 |
The SWI/SNF family of chromatin-remodeling complexes facilitates gene activation by assisting transcription machinery to gain access to targets in chromatin. Our data suggest that BAF250 confers specificity to the human BAF complex and may recruit the complex to its targets through either protein-DNA or protein-protein interactions. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
+ |
CHFR | down-regulates quantity by destabilization
polyubiquitination
|
SMARCD1 |
0.311 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271459 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
22285184 |
Here we report that CHFR interacts with BRG1, SNF5, and BAF60a of the SWI/SNF-like BAF complex and ubiquitinates them to target for degradation through a proteasome-mediated pathway, and that SRG3/mBAF155 stabilizes these components by blocking their interaction with CHFR. These results suggest that CHFR enhances the degradation of the components of the SWI/SNF-like BAF complex by inducing their poly-ubiquitination. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
SMARCD1 | form complex
binding
|
Muscle cell-specific SWI/SNF ARID1A variant |
0.787 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270694 |
|
|
Homo sapiens |
|
pmid |
sentence |
11073988 |
The SWI/SNF family of chromatin-remodeling complexes facilitates gene activation by assisting transcription machinery to gain access to targets in chromatin. Our data suggest that BAF250 confers specificity to the human BAF complex and may recruit the complex to its targets through either protein-DNA or protein-protein interactions. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
+ |
SMARCD1 | form complex
binding
|
Muscle cell-specific SWI/SNF SMARCA4 variant |
0.788 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270734 |
|
|
Homo sapiens |
|
pmid |
sentence |
11073988 |
We have also found that, of the two human SWI/2/SNF2 family-related ATPases, the PBAF complex contains only BRG1 but not hbrm (Xue et al., submitted). In contrast, the BAF complex isolated by BAF250 can include either BRG1 or hbrm (Fig. (Fig.4b).4b). These data underscore the distinctness of the two human complexes and suggest that BAF250 is a signature subunit that may confer specificity to the BAF complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
+ |
SMARCD1 | form complex
binding
|
GBAF |
0.673 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269785 |
|
|
Homo sapiens |
|
pmid |
sentence |
30397315 |
Mammalian SWI/SNF (mSWI/SNF) complexes are ATP-dependent chromatin remodelers that modulate genomic architecture and DNA accessibility, enabling timely and appropriate control of gene expression. They are combinatorially assembled from the products of 29 total genes into three final-form complexes: canonical BAF, PBAF (polybromo-associated BAF complexes), and a newly-defined non-canonical BAF (ncBAF), with specific subunits specifying distinct complexes, such as PBRM1, ARID2, and BRD7 in PBAF complexes, ARID1A/ARID1B and DPF2 in canonical BAF (cBAF) complexes, and GLTSCR1/GLTSCR1L and BRD9 in ncBAF complexes |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMARCD1 | form complex
binding
|
Neural progenitor-specific SWI/SNF |
0.805 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270615 |
|
|
Homo sapiens |
|
pmid |
sentence |
25195934 |
The BAF (mammalian SWI/SNF) complexes are a family of multi-subunit ATP-dependent chromatin remodelers that use ATP hydrolysis to alter chromatin structure. Distinct BAF complex compositions are possible through combinatorial assembly of homologous subunit families and can serve non-redundant functions. In mammalian neural development, developmental stage-specific BAF assemblies are found in embryonic stem cells, neural progenitors and postmitotic neurons. In particular, the neural progenitor-specific BAF complexes are essential for controlling the kinetics and mode of neural progenitor cell division, while neuronal BAF function is necessary for the maturation of postmitotic neuronal phenotypes as well as long-term memory formation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMARCD1 | form complex
binding
|
SWI/SNF ACTL6A-ARID1A-SMARCA2 variant |
0.787 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269822 |
|
|
Homo sapiens |
|
pmid |
sentence |
30397315 |
Mammalian SWI/SNF (mSWI/SNF) complexes are ATP-dependent chromatin remodelers that modulate genomic architecture and DNA accessibility, enabling timely and appropriate control of gene expression. They are combinatorially assembled from the products of 29 total genes into three final-form complexes: canonical BAF, PBAF (polybromo-associated BAF complexes), and a newly-defined non-canonical BAF (ncBAF), with specific subunits specifying distinct complexes, such as PBRM1, ARID2, and BRD7 in PBAF complexes, ARID1A/ARID1B and DPF2 in canonical BAF (cBAF) complexes, and GLTSCR1/GLTSCR1L and BRD9 in ncBAF complexes |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMARCD1 | form complex
binding
|
SWI/SNF complex |
0.881 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-132939 |
|
|
Homo sapiens |
|
pmid |
sentence |
15627498 |
We discuss recent insights in the functional differences between two evolutionary conserved subclasses of swi/snf-related chromatin remodeling factors. Onesubfamily comprises yeast swi/snf, fly bap and mammalian baf, whereas the other subfamily includes yeast rsc, fly pbap andmammalian pbaf. We review the subunit composition, conserved protein modules and biological functions of each of these subclasses ofswi/snf remodelers. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMARCD1 | form complex
binding
|
SWI/SNF ACTL6B varian |
0.811 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270604 |
|
|
Homo sapiens |
|
pmid |
sentence |
30397315 |
Mammalian SWI/SNF (mSWI/SNF) complexes are ATP-dependent chromatin remodelers that modulate genomic architecture and DNA accessibility, enabling timely and appropriate control of gene expression. They are combinatorially assembled from the products of 29 total genes into three final-form complexes: canonical BAF, PBAF (polybromo-associated BAF complexes), and a newly-defined non-canonical BAF (ncBAF), with specific subunits specifying distinct complexes, such as PBRM1, ARID2, and BRD7 in PBAF complexes, ARID1A/ARID1B and DPF2 in canonical BAF (cBAF) complexes, and GLTSCR1/GLTSCR1L and BRD9 in ncBAF complexes |
|
Publications: |
1 |
Organism: |
Homo Sapiens |