+ |
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 |
+ |
LATS2 | down-regulates activity
phosphorylation
|
AMOTL2 |
0.718 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272084 |
Ser159 |
HGHVRSLsERLLQLS |
|
|
pmid |
sentence |
24225952 |
The N-terminal regions of Amot proteins contain a conserved HXRXXS consensus site for LATS1/2-mediated phosphorylation.|Amot family members. Knockdown of LATS1 and LATS2 endogenously reduced the phosphorylation of Amots detected by the phospho-specific antibodies. Mutation of the serine to alanine within this HXRXXS site in Amot and AmotL2 established that this site was essential for Hippo core kinase-mediated phosphorylation. Wild-type and non-phosphorylated Amot (Amot-S175A) were targeted to actin filaments, whereas phospho-mimic Amot (Amot-S175D) failed to be localized with actin. |
|
Publications: |
1 |
+ |
MTOR | down-regulates activity
phosphorylation
|
AMOTL2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272086 |
Ser759 |
SSSQRAAsLDSVATS |
|
|
pmid |
sentence |
25998128 |
AMOTL2 is phosphorylated at serine 760 by mTORC2. Mutation of AMOTL2 mimicking constitutive Ser(760) phosphorylation blocks its ability to bind and repress YAP leading to increased relative expression of known YAP gene targets. |
|
Publications: |
1 |
+ |
mTORC2 | down-regulates activity
phosphorylation
|
AMOTL2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272085 |
Ser759 |
SSSQRAAsLDSVATS |
|
|
pmid |
sentence |
25998128 |
AMOTL2 is phosphorylated at serine 760 by mTORC2. Mutation of AMOTL2 mimicking constitutive Ser(760) phosphorylation blocks its ability to bind and repress YAP leading to increased relative expression of known YAP gene targets. |
|
Publications: |
1 |
+ |
FGFR1 | up-regulates activity
phosphorylation
|
AMOTL2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271869 |
Tyr107 |
KGEELPTyEEAKAHS |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21937427 |
These data support an idea that Amotl2 Tyr-103 can be phosphorylated by FGF receptor tyrosine kinase activity. We then determined whether Amotl2 Tyr-103 is required for its interaction with c-Src. |Amotl2 promotes MAPK/ERK activation via c-Src, which is dependent on phosphorylation of tyrosine residue at position 103 but independent of the C-terminal PDZ-binding domain. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AMOTL2 | up-regulates
|
Angiogenesis |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271871 |
|
|
Homo sapiens |
Endothelial Cell |
pmid |
sentence |
21937427 |
Taking together, our data indicate that Amotl2 plays a pivotal role in polarity, migration and proliferation of angiogenic endothelial cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AMOTL2 | up-regulates activity
binding
|
SRC |
0.262 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271870 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21937427 |
These data support an idea that Amotl2 Tyr-103 can be phosphorylated by FGF receptor tyrosine kinase activity. We then determined whether Amotl2 Tyr-103 is required for its interaction with c-Src. |Amotl2 promotes MAPK/ERK activation via c-Src, which is dependent on phosphorylation of tyrosine residue at position 103 but independent of the C-terminal PDZ-binding domain. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AMOTL2 | up-regulates
|
Cell_migration |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271872 |
|
|
Homo sapiens |
Endothelial Cell |
pmid |
sentence |
21937427 |
Taking together, our data indicate that Amotl2 plays a pivotal role in polarity, migration and proliferation of angiogenic endothelial cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AMOTL2 | up-regulates activity
relocalization
|
LATS2 |
0.718 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271875 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
34404733 |
Ubiquitinated AMOTL2 then serves as a physical docking site for LATS2, which phosphorylates YAP to promote its cytoplasmic retention and degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |