+ |
TRPM7 | up-regulates activity
phosphorylation
|
PLCG2 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278460 |
Ser1164 |
AVKSGFRsVPLKNGY |
Homo sapiens |
|
pmid |
sentence |
22759789 |
We present data indicating that TRPM7 phosphorylates phospholipase C\u03b32 at position Ser1164 in the C2-domain, and at position Thr1045 in the linker between the catalytic region and the C2 domain. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278459 |
Thr1045 |
LQPESMRtEKYDPMP |
Homo sapiens |
|
pmid |
sentence |
22759789 |
We present data indicating that TRPM7 phosphorylates PLCgamma2 at position Ser1164 in the C2-domain, and at position Thr1045 in the linker between the catalytic region and the C2 domain. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
TRPM7 | up-regulates
phosphorylation
|
ANXA1 |
0.559 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-202804 |
Ser5 |
sEFLKQAW |
Homo sapiens |
|
pmid |
sentence |
24103589 |
Trpm7 was responsible for phosphorylation of the serine 5 (ser5) residue [29]. In 2009, the study focused on an association between anxa1 and trpm7 confirmed the presence of a trpm7/annexin a1/mg2_+ complex, suggesting a novel pathway in bradykinin signaling, dependent on pkc and c-src [30]. Even though that pathway is not fully characterized, the same team that discovered the ser5 phosphorylation of anxa1 also reported crucial relevance of this modification for anxa1 membrane binding and especially for the interaction between annexin a1 and its known partner, the calcium binding protein s100a11 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRPM7 | up-regulates activity
phosphorylation
|
EEF2K |
0.32 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277923 |
Ser78 |
SSGSPANsFHFKEAW |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21112387 |
TRPM7 interacts with, and phosphorylates mouse eEF2-k at serine site 77 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |