| + |
PLK1 | down-regulates quantity by destabilization 
phosphorylation
|
ZMYM2 |
0.391 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275559 |
Ser303 |
QKQPGVDsLSPVASL |
|
|
| pmid |
sentence |
| 25855382 |
PLK1 and HOTAIR Accelerate Proteasomal Degradation of SUZ12 and ZNF198 during Hepatitis B Virus-Induced Liver Carcinogenesis|Similar analyses with ZNF198 identified two clusters of putative Plk1 phosphorylation sites in vitro. A cluster of serine residues at the N-terminus of ZNF198, S303, S305, and S309, and a cluster at the C-terminus, S1056 and S1064. The triple Ser to Ala mutant, S303A/S305A/S309A, consistently exhibited the lowest level of phosphorylation in vitro, in comparison to the double S1056A/S1064A mutant |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275558 |
Ser305 |
QPGVDSLsPVASLPK |
|
|
| pmid |
sentence |
| 25855382 |
PLK1 and HOTAIR Accelerate Proteasomal Degradation of SUZ12 and ZNF198 during Hepatitis B Virus-Induced Liver Carcinogenesis|Similar analyses with ZNF198 identified two clusters of putative Plk1 phosphorylation sites in vitro. A cluster of serine residues at the N-terminus of ZNF198, S303, S305, and S309, and a cluster at the C-terminus, S1056 and S1064. The triple Ser to Ala mutant, S303A/S305A/S309A, consistently exhibited the lowest level of phosphorylation in vitro, in comparison to the double S1056A/S1064A mutant |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275560 |
Ser309 |
DSLSPVAsLPKQIFQ |
|
|
| pmid |
sentence |
| 25855382 |
PLK1 and HOTAIR Accelerate Proteasomal Degradation of SUZ12 and ZNF198 during Hepatitis B Virus-Induced Liver Carcinogenesis|Similar analyses with ZNF198 identified two clusters of putative Plk1 phosphorylation sites in vitro. A cluster of serine residues at the N-terminus of ZNF198, S303, S305, and S309, and a cluster at the C-terminus, S1056 and S1064. The triple Ser to Ala mutant, S303A/S305A/S309A, consistently exhibited the lowest level of phosphorylation in vitro, in comparison to the double S1056A/S1064A mutant |
|
| Publications: |
3 |
| + |
ZMYM2 | down-regulates activity
binding
|
NANOG |
0.304 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269802 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 31363497 |
In this work, we identified ZMYM2/ZFP198, which physically associates with NANOG as a key negative regulator of NANOG-mediated reprogramming of both epiblast stem cells and somatic cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Epiblast |
| + |
ZMYM2 | up-regulates activity 
binding
|
MYBL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269801 |
|
|
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 32439918 |
Here we have identified the zinc-finger proteins ZMYM2 and ZMYM4 as novel B-MYB binding proteins. B-MYB has been implicated in cell cycle progression at two steps, namely at the G1/S- and the G2/M-transition. ZMYM2 is required for the G1/S-transition in HepG2 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ZMYM2
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