+ |
Ub:E2 | up-regulates activity
ubiquitination
|
RNF144B |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271181 |
|
|
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 |
+ |
RNF144B | down-regulates quantity by destabilization
ubiquitination
|
CDKN1A |
0.366 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271478 |
|
|
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
12853982 |
P53RFP, a p53-inducible RING-finger protein, regulates the stability of p21WAF1. Here we report the isolation of a novel transcriptional target of p53, designated p53RFP (p53-inducible RING-finger protein), whose product has E3 ubiquitin ligase activity. Its expression was negatively correlated to that of p21(WAF1) protein; p53RFP is likely to play a role in the regulation of this protein, probably through interaction with, and ubiquitination of, p21(WAF1). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF144B | down-regulates quantity by destabilization
ubiquitination
|
NPM1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271490 |
|
|
Homo sapiens |
Lymphoblast |
pmid |
sentence |
20864535 |
NPMc degradation was mediated by the ubiquitin-proteasome pathway involving the IBR-type RING-finger E3 ubiquitin ligase IBRDC2, and genetic correction of FA-A or FA-C lymphoblasts prevented NPMc ubiquitination. As shown in Fig. 4C, knockdown of IBRDC2, an IBR-type RING-finger E3 ubiquitin ligase (21), significantly reduced NPMc ubiquitination and restored NPMc stability in FA-A cells |
|
Publications: |
1 |
Organism: |
Homo Sapiens |