+ |
CDK2 | up-regulates activity
phosphorylation
|
RNF138 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277831 |
Thr27 |
VCQEVLKtPVRTTAC |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
38309501 |
Altogether, our results suggest RNF138 is phosphorylated at position T27 in a CDK1- and CDK2-dependent manner.Altogether, our results suggest RNF138 is phosphorylated at position T27 in a CDK1- and CDK2-dependent manner. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK1 | up-regulates activity
phosphorylation
|
RNF138 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277832 |
Thr27 |
VCQEVLKtPVRTTAC |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
38309501 |
Altogether, our results suggest RNF138 is phosphorylated at position T27 in a CDK1- and CDK2-dependent manner.Altogether, our results suggest RNF138 is phosphorylated at position T27 in a CDK1- and CDK2-dependent manner. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF138 | down-regulates quantity by destabilization
polyubiquitination
|
TCF7L2 |
0.331 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271593 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16714285 |
Here, we show that NARF induces the ubiquitylation of TCF/LEF in vitro and in vivo, and functions as an E3 ubiquitin-ligase that specifically cooperates with the E2 conjugating enzyme E2-25K. We found that NLK augmented NARF binding and ubiquitylation of TCF/LEF, and this required NLK kinase activity. The ubiquitylated TCF/LEF was subsequently degraded by the proteasome. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF138 | down-regulates quantity by destabilization
polyubiquitination
|
LEF1 |
0.312 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271595 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16714285 |
Here, we show that NARF induces the ubiquitylation of TCF/LEF in vitro and in vivo, and functions as an E3 ubiquitin-ligase that specifically cooperates with the E2 conjugating enzyme E2-25K. We found that NLK augmented NARF binding and ubiquitylation of TCF/LEF, and this required NLK kinase activity. The ubiquitylated TCF/LEF was subsequently degraded by the proteasome. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
RNF138 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271027 |
|
|
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 |
+ |
UBE2K | up-regulates activity
binding
|
RNF138 |
0.517 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271594 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16714285 |
NARF exhibits E3 ubiquitin-ligase activity in cooperation with the ubiquitin conjugating enzyme, E2-25K. These data show that the auto-ubiquitylating activity of NARF is coordinated with E2-25K, and that the RING finger domain of NARF is indispensable for this reaction. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |