+ |
CNOT4 | form complex
binding
|
CCR4-NOT complex |
0.77 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268302 |
|
|
Homo sapiens |
|
pmid |
sentence |
19558367 |
In the present study, we examine the composition of the human Ccr4-Not complex in an in-depth proteomic approach using stable cell lines expressing tagged CNOT proteins. We find at least four different variants of the human complex, consisting of seven stable core proteins and mutually exclusive associated mRNA deadenylase subunits. Interestingly, human CNOT4 is in a separate approximately 200 kDa complex. Furthermore, analyses of associated proteins indicate involvement of Ccr4-Not complexes in splicing, transport and localization of RNA molecules. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CNOT4 | down-regulates quantity by destabilization
ubiquitination
|
KDM5C |
0.561 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271468 |
|
|
Homo sapiens |
|
pmid |
sentence |
19346402 |
In our study, we show that the protein level of the yeast histone H3 Lys 4 (H3 K4) demethylase Jhd2/Kdm5 is modulated through polyubiquitination by the E3 ubiquitin ligase Not4 and turnover by the proteasome. Finally, we show that human NOT4 can polyubiquitinate human JARID1C/SMCX, a homolog of Jhd2, suggesting that this is likely a conserved mechanism. We propose that Not4 is an E3 ubiquitin ligase that monitors and controls a precise amount of Jhd2 protein so that the proper balance between histone demethylase and histone methyltransferase activities occur in the cell, ensuring appropriate levels of H3 K4 trimethylation and gene expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
CNOT4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271004 |
|
|
Homo sapiens |
|
pmid |
sentence |
34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CNOT4 | down-regulates quantity by destabilization
ubiquitination
|
RBM15 |
0.367 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271466 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
26575292 |
We demonstrate that RBM15 is methylated by protein arginine methyltransferase 1 (PRMT1) at residue R578, leading to its degradation via ubiquitylation by an E3 ligase (CNOT4). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |