+ |
CSNK2A1 | down-regulates
phosphorylation
|
CBX1 |
0.308 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-187450 |
Thr51 |
GFSDEDNtWEPEENL |
Homo sapiens |
|
pmid |
sentence |
19657222 |
Two recent papers suggest that hp1 recruitment to damage sites, rather than its rapid mobilization, is the predominant behaviour exhibited by this protein. Our findings reconcile recent findings in a new model, wherein rapid hp1beta mobilization from dsbs is mediated by its phosphorylation on thr51 by ck2 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBX1 | up-regulates activity
binding
|
H3-4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264492 |
|
|
Homo sapiens |
|
pmid |
sentence |
19111658 |
A core characteristic of heterochromatin is its association with heterochromatin protein 1 (HP1) proteins, a highly conserved family of chromosomal proteins that bind to di- and trimethylated H3K9 via a conserved N-terminal domain called the chromodomain (CD) HP1 proteins are a highly conserved family of eukaryotic proteins that bind to methylated histone H3 lysine 9 (H3K9) and are required for heterochromatic gene silencing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EMSY | up-regulates activity
binding
|
CBX1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263917 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
14651845 |
The binding sites for HP1β and BS69 with EMSY abut each other, and are found directly adjacent to the ENT domain of EMSY. This demonstrates that EMSY has the capacity to contact directly at least two proteins which contain a Royal Family domain. Since this domain is found in proteins with a chromatin connection, we assume that EMSY functions, at least partly, in the regulation of chromatin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBX1 | up-regulates activity
binding
|
H3C1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264493 |
|
|
Homo sapiens |
|
pmid |
sentence |
19111658 |
A core characteristic of heterochromatin is its association with heterochromatin protein 1 (HP1) proteins, a highly conserved family of chromosomal proteins that bind to di- and trimethylated H3K9 via a conserved N-terminal domain called the chromodomain (CD) HP1 proteins are a highly conserved family of eukaryotic proteins that bind to methylated histone H3 lysine 9 (H3K9) and are required for heterochromatic gene silencing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBX1 | up-regulates activity
binding
|
H3-3A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264491 |
|
|
Homo sapiens |
|
pmid |
sentence |
19111658 |
A core characteristic of heterochromatin is its association with heterochromatin protein 1 (HP1) proteins, a highly conserved family of chromosomal proteins that bind to di- and trimethylated H3K9 via a conserved N-terminal domain called the chromodomain (CD) HP1 proteins are a highly conserved family of eukaryotic proteins that bind to methylated histone H3 lysine 9 (H3K9) and are required for heterochromatic gene silencing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBX1 | up-regulates activity
binding
|
Histone H3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265323 |
|
|
Homo sapiens |
|
pmid |
sentence |
19111658 |
A core characteristic of heterochromatin is its association with heterochromatin protein 1 (HP1) proteins, a highly conserved family of chromosomal proteins that bind to di- and trimethylated H3K9 via a conserved N-terminal domain called the chromodomain (CD) HP1 proteins are a highly conserved family of eukaryotic proteins that bind to methylated histone H3 lysine 9 (H3K9) and are required for heterochromatic gene silencing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF123 | down-regulates quantity by destabilization
polyubiquitination
|
CBX1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272034 |
|
|
Homo sapiens |
|
pmid |
sentence |
23077635 |
In the present study, we report that HP1α and β undergo proteasomal degradation in lamin A/C knock-down cells and show by ectopic expression, RNAi and binding studies that the RING finger ubiquitin ligase RNF123 is directly involved in HP1 degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBX1 | form complex
binding
|
ChAHP |
0.366 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266754 |
|
|
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 |