+ |
PRKCA | up-regulates activity
phosphorylation
|
FERMT3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266415 |
Ser484 |
LSLQRTGsGGPGNHP |
Homo sapiens |
HEL Cell |
pmid |
sentence |
25609252 |
PKC-induced phosphorylation events, as we have shown kindlin-3 to be a PKC phosphorylation target (Fig. 6C), are often followed by rapid activation of phosphatases (38). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FERMT3 | up-regulates activity
binding
|
FBLIM1 |
0.504 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266104 |
|
|
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
24165133 |
Kindlin binds migfilin tandem LIM domains and regulates migfilin focal adhesion localization and recruitment dynamics. Two integrin-binding proteins present in FAs, kindlin-1 and kindlin-2, are important for integrin activation, FA formation, and signaling. By binding filamin, migfilin provides a link between kindlin and the actin cytoskeleton. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
FERMT3 | up-regulates activity
binding
|
ITGB3 |
0.639 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266066 |
|
|
Mus musculus |
Blood Platelet, RAW-264.7 Cell |
pmid |
sentence |
18278053 |
Mechanistically, Kindlin-3 can directly bind to regions of beta-integrin tails distinct from those of Talin and trigger integrin activation. We have therefore identified Kindlin-3 as a novel and essential element for platelet integrin activation in hemostasis and thrombosis|Kindlin-3 was also able to interact with the wild-type beta1 and beta3 integrin tails (Fig. 3c), in the presence and absence of Talin1 (Supplementary Fig. 3 online), and the F3 subdomain of Kindlin-3 was sufficient for this interaction and this interaction occurred in a direct manner |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
FERMT3 | up-regulates activity
binding
|
ITGB1 |
0.396 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266065 |
|
|
Mus musculus |
Blood Platelet, RAW-264.7 Cell |
pmid |
sentence |
18278053 |
Mechanistically, Kindlin-3 can directly bind to regions of beta-integrin tails distinct from those of Talin and trigger integrin activation. We have therefore identified Kindlin-3 as a novel and essential element for platelet integrin activation in hemostasis and thrombosis|Kindlin-3 was also able to interact with the wild-type beta1 and beta3 integrin tails (Fig. 3c), in the presence and absence of Talin1 (Supplementary Fig. 3 online), and the F3 subdomain of Kindlin-3 was sufficient for this interaction and this interaction occurred in a direct manner |
|
Publications: |
1 |
Organism: |
Mus Musculus |