| + |
WWP1 | up-regulates activity 
ubiquitination
|
AMOTL2 |
0.295 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271873 |
Lys347 |
EKAGRIEkLESEIQR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 34404733 |
AMOTL2 mono-ubiquitination by WWP1 promotes contact inhibition by facilitating LATS activation|Here, we provide evidence that the E3 ligase WWP1 (WW-domain containing protein 1) mono-ubiquitinates AMOTL2 (angiomotin-like 2) at K347 and K408. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271874 |
Lys408 |
ANRRLASkTQEAQAG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 34404733 |
AMOTL2 mono-ubiquitination by WWP1 promotes contact inhibition by facilitating LATS activation|Here, we provide evidence that the E3 ligase WWP1 (WW-domain containing protein 1) mono-ubiquitinates AMOTL2 (angiomotin-like 2) at K347 and K408. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
WWP1 | up-regulates quantity by stabilization
ubiquitination
|
AMOT |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275847 |
|
|
|
|
| pmid |
sentence |
| 24101513 |
Here low serum and high LATS1 activity are found to enhance the levels of the 130-kDa isoform of angiomotin (Amot130) through phosphorylation by LATS1/2 at serine 175, which then forms a binding site for 14-3-3. Such phosphorylation, in turn, enables the ubiquitin ligase atrophin-1 interacting protein (AIP)4 to bind, ubiquitinate, and stabilize Amot130 |
|
| Publications: |
1 |
| + |
WWP1 | up-regulates
binding
|
SMAD7 |
0.72 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126128 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15221015 |
Wwp1 associated with smad7 and induced its nuclear export, and enhanced binding of smad7 to tgf-beta type i receptor to cause ubiquitination and degradation of the receptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WWP2 | up-regulates activity
binding
|
WWP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272231 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25071155 |
WWP1 in complex with WWP2 specifically regulates ΔNp73. In our study, we identified WWP2, an E3 ligase, as a novel p73-associated protein that ubiquitinates and degrades p73. In contrast, WWP2 heterodimerizes with another E3 ligase, WWP1, which specifically ubiquitinates and degrades ΔNp73. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WWP1 | up-regulates activity
ubiquitination, relocalization
|
SMAD7 |
0.72 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-227466 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15221015 |
Similar to Smurfs, WWP1 associated with Smad7 and induced its nuclear export, and enhanced binding of Smad7 to TGF-beta type I receptor to cause ubiquitination and degradation of the receptor. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126578 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15221015 |
We found that WWP1 inhibited transcriptional activities induced by TGF-beta. Similar to Smurfs, WWP1 associated with Smad7 and induced its nuclear export, and enhanced binding of Smad7 to TGF-beta type I receptor to cause ubiquitination and degradation of the receptor. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
TGIF1 | up-regulates
binding
|
WWP1 |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128854 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15359284 |
We demonstrate that tiul1 degrades not only the activated type i receptor in association with smad7 but also smad2 in association with tgif.the steady-state levels of tgif are not affected by tiul1, but the interaction of tiul1 with tgif allows this ubiquitin ligase to target smad2 for degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WWP1 | down-regulates quantity by destabilization 
polyubiquitination
|
TP73 |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272232 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25071155 |
WWP1 in complex with WWP2 specifically regulates ΔNp73. In our study, we identified WWP2, an E3 ligase, as a novel p73-associated protein that ubiquitinates and degrades p73. In contrast, WWP2 heterodimerizes with another E3 ligase, WWP1, which specifically ubiquitinates and degrades ΔNp73. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WWP1 | down-regulates
ubiquitination
|
TGFBR1 |
0.513 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126581 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15221015 |
Similar to smurfs, wwp1 associated with smad7 and induced its nuclear export, and enhanced binding of smad7 to tgf-beta type i receptor to cause ubiquitination and degradation of the receptor. Consistent with these results, wwp1 inhibited phosphorylation of smad2 induced by tgf-beta. Wwp1 thus negatively regulates tgf-beta signaling in cooperation with smad7 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SPART | up-regulates activity
binding
|
WWP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261307 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19580544 |
Cytosolic endogenous spartin is mono-ubiquitinated and we demonstrate that it interacts via a PPXY motif with the ubiquitin E3 ligases AIP4 [atrophin-interacting protein 4; ITCH (itchy E3 ubiquitin protein ligase homologue] [corrected] and AIP5 (WWP1). Surprisingly, the PPXY motif, AIP4 and AIP5 are not required for spartin's ubiquitination, and so we propose that spartin acts as an adaptor for these proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ub:E2 | up-regulates activity
ubiquitination
|
WWP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271293 |
|
|
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 |
3.0
WWP1
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