| + |
AKT1 | up-regulates activity 
phosphorylation
|
PTK2 |
0.432 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276437 |
Ser695 |
EERMRMEsRRQATVS |
in vitro |
|
| pmid |
sentence |
| 23264741 |
Here we show that soluble growth factors enhance integrin signaling through Akt phosphorylation of FAK at Ser695 and Thr700. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276436 |
Thr700 |
MESRRQAtVSWDSGG |
in vitro |
|
| pmid |
sentence |
| 23264741 |
Here we show that soluble growth factors enhance integrin signaling through Akt phosphorylation of FAK at Ser695 and Thr700. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CDK5 | up-regulates
phosphorylation
|
PTK2 |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-86223 |
Ser732 |
SSEGFYPsPQHMVQT |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 12941275 |
Here, we show that fak phosphorylation by cdk5 at s732 is important for microtubule organization, nuclear movement, and neuronal migration. In cultured neurons, s732-phosphorylated fak is enriched along a centrosome-associated microtubule fork that abuts the nucleus. Overexpression of the nonphosphorylatable mutant fak s732a results in disorganization of the microtubule fork and impairment of nuclear movement in vitro, and neuronal positioning defects in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2A | up-regulates
phosphorylation
|
PTK2 |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135631 |
Ser843 |
DVRLSRGsIDREDGS |
Homo sapiens |
|
| pmid |
sentence |
| 15845548 |
Furthermore, activated camkii directly phosphorylated the recombinant cooh-terminal region of fak at a residue equivalent to ser-843. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
LRRK2 | down-regulates activity 
phosphorylation
|
PTK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278281 |
Thr474 |
KFLQEALtMRQFDHP |
Homo sapiens |
|
| pmid |
sentence |
| 26365310 |
LRRK2 inhibits FAK activation in a kinase dependent manner, meaning that the G2019S gain-of-function mutation results in the excessive inhibition of FAK activation and microglial motility.|Taken together, these results suggest that LRRK2 directly phosphorylate FAK at T474. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2 | up-regulates activity
phosphorylation
|
ATP2B4 (isoform 6) |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263194 |
Tyr1176 |
LDGEVTPyANTNNNA |
Homo sapiens |
|
| pmid |
sentence |
| 12540962 |
Results of co-immunoprecipitation, treatment with tyrosine kinase inhibitors and integrin inhibition experiments suggest that FAK is responsible for PMCA4b tyrosine phosphorylation during platelet activation. equence analysis indicates that Y(1176) is a likely substrate for focal adhesion kinase (FAK), while Y(1122) is not located in a tyrosine phosphorylation motif. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2 | up-regulates activity
phosphorylation, binding
|
PXN |
0.914 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-28243 |
Tyr118 |
VGEEEHVySFPNKQK |
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Paxillin is phosphorylated by FAK–Src on Tyr31 and Tyr118, and this can also promote SH2-mediated binding of Crk to paxillin. Overexpressing paxillin that is mutated at these phosphorylation sites inhibits the turnover of focal contacts6 and cell motility, which therefore supports the presence of multiple routes for FAK–Src-mediated signalling in modulating the dynamics of cell adhesion sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-28247 |
Tyr31 |
FLSEETPySYPTGNH |
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Paxillin is phosphorylated by FAK–Src on Tyr31 and Tyr118, and this can also promote SH2-mediated binding of Crk to paxillin. Overexpressing paxillin that is mutated at these phosphorylation sites inhibits the turnover of focal contacts6 and cell motility, which therefore supports the presence of multiple routes for FAK–Src-mediated signalling in modulating the dynamics of cell adhesion sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257732 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling, VEGF Signaling |
| + |
PTK2 | down-regulates activity
phosphorylation
|
ACTN1 |
0.57 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-108329 |
Tyr12 |
DSQQTNDyMQPEEDW |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 11369769 |
The cytoskeletal/non-muscle isoform of alpha-actinin is phosphorylated on its actin-binding domain by the focal adhesion kinase tyrosine 12 is the site of phosphorylation. The wild type recombinant protein was not phosphorylated in cells lacking the focal adhesion kinase (fak).Tyrosine phosphorylation reduced the amount of alpha-actinin that cosedimented with actin filaments. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Axon guidance |
| + |
PTK2 | down-regulates
phosphorylation
|
ACTN1 |
0.57 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192126 |
Tyr12 |
DSQQTNDyMQPEEDW |
Homo sapiens |
|
| pmid |
sentence |
| 23454549 |
Phosphorylation at y12 by fak reduces _-actinin1's affinity for actin . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
PTK2 |
phosphorylation
|
CTNNB1 |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261946 |
Tyr142 |
AVVNLINyQDDAELA |
Mus musculus |
|
| pmid |
sentence |
| 22264731 |
VEGF promotes tension-independent FAK activation, rapid FAK localization to cell-cell junctions, binding of the FAK FERM domain to the vascular endothelial cadherin (VE-cadherin) cytoplasmic tail, and direct FAK phosphorylation of β-catenin at tyrosine-142 (Y142) facilitating VE-cadherin-β-catenin dissociation and EC junctional breakdown. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PTK2 | up-regulates activity
phosphorylation
|
NANOG |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276410 |
Tyr174 |
QKASAPTyPSLYSSY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22493428 |
In addition, FAK directly phosphorylates Nanog in a dose-dependent manner by in vitro kinase assay and in cancer cells in vivo. The site-directed mutagenesis of Nanog tyrosines, Y35F and Y174F, blocked phosphorylation and binding by FAK. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276409 |
Tyr35 |
ICGPEENyPSLQMSS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22493428 |
In addition, FAK directly phosphorylates Nanog in a dose-dependent manner by in vitro kinase assay and in cancer cells in vivo. The site-directed mutagenesis of Nanog tyrosines, Y35F and Y174F, blocked phosphorylation and binding by FAK. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PDGFRB | up-regulates
phosphorylation
|
PTK2 |
0.55 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167658 |
Tyr194 |
ALEKKSNyEVLEKDV |
Homo sapiens |
|
| pmid |
sentence |
| 20802513 |
In this study, we demonstrate that growth factor receptors including hepatocyte growth factor receptor met, epidermal growth factor receptor, and platelet-derived growth factor receptor directly phosphorylate fak on tyr194 in the ferm domain collectively, this study provides the first example to explain how fak is activated by receptor tyrosine kinases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167662 |
Tyr5 |
yLDPNLNH |
Homo sapiens |
|
| pmid |
sentence |
| 20802513 |
In this study, we demonstrate that growth factor receptors including hepatocyte growth factor receptor met, epidermal growth factor receptor, and platelet-derived growth factor receptor directly phosphorylate fak on tyr194 in the ferm domain collectively, this study provides the first example to explain how fak is activated by receptor tyrosine kinases. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PDGFRA | up-regulates activity
phosphorylation
|
PTK2 |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259400 |
Tyr194 |
ALEKKSNyEVLEKDV |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 20802513 |
Focal adhesion kinase (FAK) has a crucial role in integration of signals from integrins and growth factor receptors. In this study, we demonstrate that growth factor receptors including hepatocyte growth factor receptor Met, epidermal growth factor receptor, and platelet-derived growth factor receptor directly phosphorylate FAK on Tyr194 in the FERM domain (band 4.1 and ezrin/radixin/moesin homology domain). Upon binding to Met or phosphoinositides, FAK may undergo conformational changes, which renders Tyr194 accessible for phosphorylation. Substitution of Tyr194 with Phe significantly suppresses the activation of FAK by Met. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MET | up-regulates
phosphorylation
|
PTK2 |
0.494 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147179 |
Tyr194 |
ALEKKSNyEVLEKDV |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Here we report that fak directly interacts with the hepatocyte growth factor receptor c-met. Phosphorylation of c-met at tyr-1349 and, to a lesser extent, tyr-1356 is required for its interaction with the band 4.1 and ezrin/radixin/moesin homology domain (ferm domain) of fak. met-fak interaction leads to fak activation and subsequent contribution to hepatocyte growth factor-induced cell motility and cell invasion. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167654 |
Tyr194 |
ALEKKSNyEVLEKDV |
Homo sapiens |
|
| pmid |
sentence |
| 20802513 |
In this study, we demonstrate that growth factor receptors including hepatocyte growth factor receptor met, epidermal growth factor receptor, and platelet-derived growth factor receptor directly phosphorylate fak on tyr194 in the ferm domain (band 4.1 and ezrin/radixin/moesin homology domain). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147183 |
Tyr397 |
SVSETDDyAEIIDEE |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Met-mediated fak phosphorylation could further activate fak. Indeed, we found that met phosphorylates fak at its known phosphorylation sites, including tyr-576 and tyr-577, both of which are located in the activating loop within the catalytic domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147187 |
Tyr407 |
IIDEEDTyTMPSTRD |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Met-mediated fak phosphorylation could further activate fak. Indeed, we found that met phosphorylates fak at its known phosphorylation sites, including tyr-576 and tyr-577, both of which are located in the activating loop within the catalytic domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147191 |
Tyr576 |
RYMEDSTyYKASKGK |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Met-mediated fak phosphorylation could further activate fak. Indeed, we found that met phosphorylates fak at its known phosphorylation sites, including tyr-576 and tyr-577, both of which are located in the activating loop within the catalytic domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147195 |
Tyr577 |
YMEDSTYyKASKGKL |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Met-mediated fak phosphorylation could further activate fak. Indeed, we found that met phosphorylates fak at its known phosphorylation sites, including tyr-576 and tyr-577, both of which are located in the activating loop within the catalytic domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147199 |
Tyr861 |
PIGNQHIyQPVGKPD |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Met-mediated fak phosphorylation could further activate fak. Indeed, we found that met phosphorylates fak at its known phosphorylation sites, including tyr-576 and tyr-577, both of which are located in the activating loop within the catalytic domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147203 |
Tyr925 |
DRSNDKVyENVTGLV |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Met-mediated fak phosphorylation could further activate fak. Indeed, we found that met phosphorylates fak at its known phosphorylation sites, including tyr-576 and tyr-577, both of which are located in the activating loop within the catalytic domain |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| + |
EGFR | up-regulates
phosphorylation
|
PTK2 |
0.592 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167646 |
Tyr194 |
ALEKKSNyEVLEKDV |
Homo sapiens |
|
| pmid |
sentence |
| 20802513 |
In this study, we demonstrate that growth factor receptors including hepatocyte growth factor receptor met, epidermal growth factor receptor, and platelet-derived growth factor receptor directly phosphorylate fak on tyr194 in the ferm domain collectively, this study provides the first example to explain how fak is activated by receptor tyrosine kinases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167650 |
Tyr5 |
yLDPNLNH |
Homo sapiens |
|
| pmid |
sentence |
| 20802513 |
In this study, we demonstrate that growth factor receptors including hepatocyte growth factor receptor met, epidermal growth factor receptor, and platelet-derived growth factor receptor directly phosphorylate fak on tyr194 in the ferm domain collectively, this study provides the first example to explain how fak is activated by receptor tyrosine kinases. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTK2 | up-regulates
phosphorylation
|
ACTN4 |
0.556 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192191 |
Tyr265 |
MTYVSSFyHAFSGAQ |
Homo sapiens |
|
| pmid |
sentence |
| 23454549 |
Phosphorylation at y12 by fak reduces _-actinin1's affinity for actin [25] and [27]. _-actinin4 is phosphorylated at y4, y31, and y265. Phosphorylation at y4 or y31 decreases its binding to actin [28] while phosphorylation of y265 increases its affinity for actin |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2 | up-regulates activity
phosphorylation
|
TRIO |
0.505 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249188 |
Tyr2796 |
KDNFDSFySEVAELG |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12551902 |
A FAK phosphorylation site, tyrosine residue 2737, was identified in subdomain I of the Trio kinase domain. Additionally, in vitro phosphorylation assays and in vivo co-expression studies indicated that Trio enhances FAK kinase activity. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PTK2 | down-regulates
phosphorylation
|
ACTN4 |
0.556 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192195 |
Tyr31 |
GGGSMGDyMAQEDDW |
Homo sapiens |
|
| pmid |
sentence |
| 23454549 |
Phosphorylation at y12 by fak reduces _-actinin1's affinity for actin [25] and [27]. _-actinin4 is phosphorylated at y4, y31, and y265. Phosphorylation at y4 or y31 decreases its binding to actin [28] while phosphorylation of y265 increases its affinity for actin |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192199 |
Tyr4 |
yHAANQSY |
Homo sapiens |
|
| pmid |
sentence |
| 23454549 |
Phosphorylation at y12 by fak reduces _-actinin1's affinity for actin [25] and [27]. _-actinin4 is phosphorylated at y4, y31, and y265. Phosphorylation at y4 or y31 decreases its binding to actin [28] while phosphorylation of y265 increases its affinity for actin |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTK2 |
phosphorylation
|
SH3GL1 |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139146 |
Tyr315 |
QPSCKALyDFEPEND |
Homo sapiens |
|
| pmid |
sentence |
| 16054026 |
These results identified y315 of endophilin a2 as a major phosphorylation site by fak/src complex. tyr315 phosphorylation inhibited endophilin/dynamin interactions, and blockade of tyr315 phosphorylation promoted endocytosis of mt1-mmp. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CRK | up-regulates activity
phosphorylation
|
PTK2 |
0.732 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250777 |
Tyr397 |
SVSETDDyAEIIDEE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11314030 |
Tyrosine phosphorylation FAK was strictly dependent upon c-Crk II expression | Crk-inducible FAK tyrosine phosphorylation was completely abrogated by co-expression with R38K Crk (lane 2), and decreased by co-expression with W170K Crk (lane 3), indicating that the SH2 domain of c-Crk is absolutely essential for this effect. In contrast, mutants in the C-terminus of Crk that include Y222F c-Crk, which abrogates the c-Abl phosphorylation site, and W276K Crk, which mutates the C-terminal SH3 domain, modestly increased FAK activation compared to wild-type c-Crk II. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FYN | up-regulates activity
phosphorylation
|
PTK2 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278441 |
Tyr397 |
SVSETDDyAEIIDEE |
Homo sapiens |
|
| pmid |
sentence |
| 19917775 |
Because Fyn deletion prevented FAK phosphorylation at tyrosine residues 397 and 576 (XREF_FIG), we generated a phosphorylation mimicking mutant of FAK to test whether restoring FAK phosphorylation in the fyn -/- mouse lung could restore lung vascular permeability responses to PAR1 agonist to the level seen in WT mice.|Our findings that interaction of activated FAK with p120-catenins subsequent to Fyn activation of FAK facilitates reannealing of AJ leading to reestablishment of the basal endothelial barrier suggest that the Fyn-FAK pathway plays a critical role in restoring endothelial barrier function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | up-regulates activity
phosphorylation
|
PTK2 |
0.653 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278475 |
Tyr397 |
SVSETDDyAEIIDEE |
Homo sapiens |
|
| pmid |
sentence |
| 27638858 |
HER2, EGFR, and additional RTKs directly phosphorylate FAK FERM at Y397.|To further confirm the mechanism of direct FAK activation by HER2, we performed a series of GST pull-down assays with purified recombinant proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity
dephosphorylation
|
PTK2 |
0.821 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248547 |
Tyr397 |
SVSETDDyAEIIDEE |
Homo sapiens |
Breast Cancer Cell Line |
| pmid |
sentence |
| 10400703 |
The tumor suppressor PTEN is a phosphatase with sequence homology to tensin. PTEN dephosphorylates phosphatidylinositol 3,4, 5-trisphosphate (PIP3) and focal adhesion kinase (FAK), and it can inhibit cell growth, invasion, migration, and focal adhesions. We investigated molecular interactions of PTEN and FAK in glioblastoma and breast cancer cells lacking PTEN. The PTEN trapping mutant D92A bound wild-type FAK, requiring FAK autophosphorylation site Tyr397 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2 | up-regulates
phosphorylation
|
PTK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157763 |
Tyr397 |
SVSETDDyAEIIDEE |
Homo sapiens |
|
| pmid |
sentence |
| 17828307 |
Fak y397 phosphorylation promotes src sh2 domain binding to fak, presumably leading to conformational src activation with a fak-src complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-77434 |
Tyr397 |
SVSETDDyAEIIDEE |
Homo sapiens |
|
| pmid |
sentence |
| 10816598 |
Fak autophosphorylation site, tyr397. / extracellular matrix (ecm)-induced autophosphorylation of fak on tyr397 creates a high affinity binding site for the sh2 domain of c-src, and mutation (tyr to phe) of this residue inhibits association |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133837 |
Tyr407 |
IIDEEDTyTMPSTRD |
Homo sapiens |
|
| pmid |
sentence |
| 15694384 |
Once stimulated, fak undergoes autophosphorylation at tyrosine (y) 397, followed by phosphorylation of several sites including y576/y577 which increases fak's kinase activity, as well as at y407, y861, and y925. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133841 |
Tyr576 |
RYMEDSTyYKASKGK |
Homo sapiens |
|
| pmid |
sentence |
| 15694384 |
Once stimulated, fak undergoes autophosphorylation at tyrosine (y) 397, followed by phosphorylation of several sites including y576/y577 which increases fak's kinase activity, as well as at y407, y861, and y925. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-27875 |
Tyr576 |
RYMEDSTyYKASKGK |
Homo sapiens |
|
| pmid |
sentence |
| 7529876 |
We found that maximal kinase activity of fak immune complexes requires phosphorylation of both tyrosines 576 and 577. Our results indicate that phosphorylation of fak by src (or other src family kinases) is an important step in the formation of an active signaling complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133845 |
Tyr577 |
YMEDSTYyKASKGKL |
Homo sapiens |
|
| pmid |
sentence |
| 15694384 |
Once stimulated, fak undergoes autophosphorylation at tyrosine (y) 397, followed by phosphorylation of several sites including y576/y577 which increases fak's kinase activity, as well as at y407, y861, and y925. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-27879 |
Tyr577 |
YMEDSTYyKASKGKL |
Homo sapiens |
|
| pmid |
sentence |
| 7529876 |
We found that maximal kinase activity of fak immune complexes requires phosphorylation of both tyrosines 576 and 577. Our results indicate that phosphorylation of fak by src (or other src family kinases) is an important step in the formation of an active signaling complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133849 |
Tyr861 |
PIGNQHIyQPVGKPD |
Homo sapiens |
|
| pmid |
sentence |
| 15694384 |
Once stimulated, fak undergoes autophosphorylation at tyrosine (y) 397, followed by phosphorylation of several sites including y576/y577 which increases fak's kinase activity, as well as at y407, y861, and y925. |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| Pathways: | Axon guidance, Integrin Signaling, VEGF Signaling |
| + |
PTPN12 | down-regulates activity
dephosphorylation
|
PTK2 |
0.542 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248661 |
Tyr397 |
SVSETDDyAEIIDEE |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 19595712 |
We demonstrate here that activated Ras induces tyrosine dephosphorylation and inhibition of FAK mediated by the Ras downstream Fgd1-Cdc42-PAK1-MEK-ERK signaling cascade.| PIN1 binding and prolyl isomerization of FAK cause PTP-PEST to interact with and dephosphorylate FAK Y397. Inhibition of FAK mediated by this signal relay promotes Ras-induced cell migration, invasion, and metastasis. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PTPRG | up-regulates activity
dephosphorylation
|
PTK2 |
0.244 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254717 |
Tyr397 |
SVSETDDyAEIIDEE |
in vitro |
|
| pmid |
sentence |
| 25624455 |
PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254719 |
Tyr576 |
RYMEDSTyYKASKGK |
in vitro |
|
| pmid |
sentence |
| 25624455 |
PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PTPN1 | down-regulates activity
dephosphorylation
|
PTK2 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248431 |
Tyr397 |
SVSETDDyAEIIDEE |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 16291744 |
The focal adhesion kinase (FAK) is a key regulator of cell migration. Phosphorylation at Tyr-397 activates FAK |The dephosphorylation at Tyr-397 in FAK triggered by wild-type alpha-actinin and PTP 1B caused a significant increase in cell migration. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
SRC | up-regulates
phosphorylation
|
PTK2 |
0.646 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150476 |
Tyr397 |
SVSETDDyAEIIDEE |
Homo sapiens |
|
| pmid |
sentence |
| 15735019 |
Surprisingly, we found that expression of SrcMF or Src251 resulted in increased tyrosine phosphorylation of FAK on Tyr(407), Tyr(576), Tyr(577), and Tyr(861), which are considered to be Src kinase substrates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150480 |
Tyr407 |
IIDEEDTyTMPSTRD |
Homo sapiens |
|
| pmid |
sentence |
| 15735019 |
Surprisingly, we found that expression of SrcMF or Src251 resulted in increased tyrosine phosphorylation of FAK on Tyr(407), Tyr(576), Tyr(577), and Tyr(861), which are considered to be Src kinase substrates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150484 |
Tyr576 |
RYMEDSTyYKASKGK |
Homo sapiens |
|
| pmid |
sentence |
| 15735019 |
Surprisingly, we found that expression of SrcMF or Src251 resulted in increased tyrosine phosphorylation of FAK on Tyr(407), Tyr(576), Tyr(577), and Tyr(861), which are considered to be Src kinase substrates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134212 |
Tyr577 |
YMEDSTYyKASKGKL |
Homo sapiens |
|
| pmid |
sentence |
| 15735019 |
Surprisingly, we found that expression of SrcMF or Src251 resulted in increased tyrosine phosphorylation of FAK on Tyr(407), Tyr(576), Tyr(577), and Tyr(861), which are considered to be Src kinase substrates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152967 |
Tyr742 |
HMVQTNHyQVSGYPG |
Homo sapiens |
CACO-2 Cell |
| pmid |
sentence |
| 17289681 |
We propose that fak/c-src bipartite enzyme is a sensor of cytoplasmic shrinkage, and that the phosphorylation on fak tyr-861 by src and subsequent reorganization of f-actin can initiate an anti-apoptotic signaling pathway that protects cells from hyperosmotic stress. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150492 |
Tyr861 |
PIGNQHIyQPVGKPD |
Homo sapiens |
|
| pmid |
sentence |
| 15735019 |
Surprisingly, we found that expression of SrcMF or Src251 resulted in increased tyrosine phosphorylation of FAK on Tyr(407), Tyr(576), Tyr(577), and Tyr(861), which are considered to be Src kinase substrates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152971 |
Tyr861 |
PIGNQHIyQPVGKPD |
Homo sapiens |
CACO-2 Cell |
| pmid |
sentence |
| 17289681 |
We propose that fak/c-src bipartite enzyme is a sensor of cytoplasmic shrinkage, and that the phosphorylation on fak tyr-861 by src and subsequent reorganization of f-actin can initiate an anti-apoptotic signaling pathway that protects cells from hyperosmotic stress. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157767 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17828307 |
Fak y397 phosphorylation promotes src sh2 domain binding to fak, presumably leading to conformational src activation with a fak-src complex. |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance, Integrin Signaling |
| + |
PTK2B | up-regulates
phosphorylation
|
PTK2 |
0.52 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147070 |
Tyr407 |
IIDEEDTyTMPSTRD |
Homo sapiens |
|
| pmid |
sentence |
| 16760434 |
Activated rock phosphorylates fak on ser732, which is essential for phosphorylation of tyr407 and for cell migration. We further show that pyk2 is activated by vegf-induced clustering of integrin v 3 and is responsible for the phosphorylation of tyr407. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2 | up-regulates activity
phosphorylation
|
SRC |
0.646 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278452 |
Tyr419 |
RLIEDNEyTARQGAK |
Homo sapiens |
|
| pmid |
sentence |
| 17828307 |
Cell reconstitution showed that FAK catalytic activity is required for alpha5beta1-stimulated Src activation in part through direct FAK phosphorylation of Src at Tyr-418. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance, Integrin Signaling |
| + |
PTK2 | down-regulates activity
phosphorylation
|
CTTN |
0.745 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278284 |
Tyr421 |
RLPSSPVyEDAASFK |
Homo sapiens |
|
| pmid |
sentence |
| 22952866 |
FAK can directly phosphorylate cortactin at Y421 and Y466, and these sites are also phosphorylated by Src and Abl/Arg tyrosine kinases.|GFP-FAK re-expression in FAK-/- MEFs enhances FA turnover (XREF_FIG) and cortactin knockdown slows FA turnover (XREF_FIG). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278283 |
Tyr470 |
AYATEAVyESAEAPG |
Homo sapiens |
|
| pmid |
sentence |
| 22952866 |
FAK directly phosphorylates cortactin at Y421 and Y466 and over-expression of cortactin Y421, Y466, and Y482 mutated to phenylalanine (3YF) prevented FAK-enhanced FA turnover and cell motility.|GFP-FAK re-expression in FAK-/- MEFs enhances FA turnover (XREF_FIG) and cortactin knockdown slows FA turnover (XREF_FIG). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278285 |
Tyr486 |
YPAEDSTyDEYENDL |
Homo sapiens |
|
| pmid |
sentence |
| 22952866 |
FAK directly phosphorylates cortactin at Y421 and Y466 and over-expression of cortactin Y421, Y466, and Y482 mutated to phenylalanine (3YF) prevented FAK-enhanced FA turnover and cell motility.|GFP-FAK re-expression in FAK-/- MEFs enhances FA turnover (XREF_FIG) and cortactin knockdown slows FA turnover (XREF_FIG). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PTK2 | up-regulates activity
phosphorylation
|
SHC1 |
0.672 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259854 |
Tyr427 |
ELFDDPSyVNVQNLD |
Homo sapiens |
|
| pmid |
sentence |
| 9566877 |
In vitro, FAK directly phosphorylated Shc Tyr-317 to promote Grb2 binding. FAK can associate and directly phosphorylate Shc at Tyr-317 to promote Grb2 binding and low-level signaling to ERK2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
INSR | up-regulates activity
phosphorylation
|
PTK2 |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251323 |
Tyr576 |
RYMEDSTyYKASKGK |
in vitro |
|
| pmid |
sentence |
| 9507031 |
P125(Fak) sequence comprising amino acids 568-582, which contains tyrosines 576 and 577 of the kinase domain regulatory loop, is phosphorylated by the insulin receptor. p125(Fak) phosphorylation by the receptor results in its activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251324 |
Tyr577 |
YMEDSTYyKASKGKL |
in vitro |
|
| pmid |
sentence |
| 9507031 |
P125(Fak) sequence comprising amino acids 568-582, which contains tyrosines 576 and 577 of the kinase domain regulatory loop, is phosphorylated by the insulin receptor. p125(Fak) phosphorylation by the receptor results in its activation. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
RET | up-regulates
phosphorylation
|
PTK2 |
0.635 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173013 |
Tyr576 |
RYMEDSTyYKASKGK |
Homo sapiens |
|
| pmid |
sentence |
| 21454698 |
The identification of focal adhesion kinase (fak) as a direct substrate for ret kinase revealed (i) a ret-fak transactivation mechanism consisting of direct phosphorylation of fak tyr-576/577 by ret and a reciprocal phosphorylation of ret by fak, which crucially is able to rescue the kinase-impaired ret k758m mutant and (ii) that fak binds ret via its ferm domain. Interestingly, this interaction is abolished upon ret phosphorylation, indicating that ret binding to the ferm domain of fak is a priming step for ret-fak transactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173017 |
Tyr577 |
YMEDSTYyKASKGKL |
Homo sapiens |
|
| pmid |
sentence |
| 21454698 |
The identification of focal adhesion kinase (fak) as a direct substrate for ret kinase revealed (i) a ret-fak transactivation mechanism consisting of direct phosphorylation of fak tyr-576/577 by ret and a reciprocal phosphorylation of ret by fak, which crucially is able to rescue the kinase-impaired ret k758m mutant and (ii) that fak binds ret via its ferm domain. Interestingly, this interaction is abolished upon ret phosphorylation, indicating that ret binding to the ferm domain of fak is a priming step for ret-fak transactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173021 |
Tyr925 |
DRSNDKVyENVTGLV |
Homo sapiens |
|
| pmid |
sentence |
| 21454698 |
Strikingly, when fak and ret kinases were co-incubated in the presence of atp, a marked increased in fak tyr-576/577 and tyr-925 phosphorylation was observed together with a shift in mobility of fak, indicating conversion to an activated state |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
BMX | up-regulates
phosphorylation
|
PTK2 |
0.546 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202139 |
Tyr577 |
YMEDSTYyKASKGKL |
Homo sapiens |
|
| pmid |
sentence |
| 23716717 |
Bmx phosphorylated focal adhesion kinase (fak) at tyr577 subsequent to its src-mediated phosphorylation at tyr576. Loss of bmx by rna interference or by genetic deletion in mouse embryonic fibroblasts (mefs) markedly impaired fak activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | down-regulates
dephosphorylation
|
PTK2 |
0.73 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148926 |
Tyr577 |
YMEDSTYyKASKGKL |
Homo sapiens |
|
| pmid |
sentence |
| 16920701 |
Dca concomitantly and significantly increased association of tyrosine phosphatase shp2 with fak. Incubation of immunoprecipitated fak, in vitro, with glutathione-s-transferase-shp2 fusion protein resulted in tyrosine dephosphorylation of fak in a concentration-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRG | down-regulates activity
dephosphorylation
|
PTK2 |
0.244 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254718 |
Tyr577 |
YMEDSTYyKASKGKL |
in vitro |
|
| pmid |
sentence |
| 25624455 |
PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254720 |
Tyr861 |
PIGNQHIyQPVGKPD |
in vitro |
|
| pmid |
sentence |
| 25624455 |
PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PTK2 |
phosphorylation
|
BCAR1 |
0.811 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249111 |
Tyr664 |
EGGWMEDyDYVHLQG |
|
|
| pmid |
sentence |
| 11604500 |
FAK phosphorylates CAS-SBD tyrosines 668 and/or 670, driving an SH2-mediated recruitment of Src which then phosphorylates CAS-SD. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249112 |
Tyr666 |
GWMEDYDyVHLQGKE |
|
|
| pmid |
sentence |
| 11604500 |
FAK phosphorylates CAS-SBD tyrosines 668 and/or 670, driving an SH2-mediated recruitment of Src which then phosphorylates CAS-SD. |
|
| Publications: |
2 |
| + |
PTK6 | up-regulates activity
phosphorylation
|
PTK2 |
0.265 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278428 |
Tyr861 |
PIGNQHIyQPVGKPD |
Homo sapiens |
|
| pmid |
sentence |
| 23027128 |
B. PTK6 phosphorylates FAK at tyrosine residue 861.|Knockdown of PTK6 in the PC3 human prostate cancer cell line disrupts FAK and AKT activation and promotes anoikis, which can be rescued by exogenous expression of FAK. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2 | up-regulates
phosphorylation
|
RET |
0.635 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173009 |
Tyr905 |
DVYEEDSyVKRSQGR |
Homo sapiens |
|
| pmid |
sentence |
| 21454698 |
Focal adhesion kinase (fak) binds ret kinase via its ferm domain, priming a direct and reciprocal ret-fak transactivation mechanism. following gdnf stimulation, increased phosphorylation of fak at tyr-576/577 as well as phosphorylation of ret at tyr-905 was observed. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FGR | up-regulates
phosphorylation
|
PTK2 |
0.548 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94405 |
Tyr925 |
DRSNDKVyENVTGLV |
Homo sapiens |
|
| pmid |
sentence |
| 12387730 |
Phosphorylated on tyrosine residues upon activation. Phosphorylation at tyr-925 is important for interaction with grb2 and depends on the complex formation between fak and the src-kinase fgr. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AX/b2 integrin | up-regulates activity 
|
PTK2 |
0.45 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257714 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Av/b1 integrin | up-regulates activity
|
PTK2 |
0.703 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277737 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRIM72 | down-regulates quantity by destabilization
ubiquitination
|
PTK2 |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278648 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24344130 |
Because RING disrupted MG53 mutants (C14A and DeltaR) did not induce FAK ubiquitination and degradation, the RING domain was determined to be required for MG53 induced FAK ubiquitination. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A5/b1 integrin | up-regulates activity
|
PTK2 |
0.609 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257705 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2 | up-regulates
binding
|
PI3K |
0.566 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252726 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9416004 |
Pi3-kinase has also been shown to bind fak in a cell cell adhesion-dipendent manner at the major autophosphorylation site y397. This association could live to activation of pi3-kinase and its downstream effectors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling, VEGF Signaling |
| + |
ITGB2 | up-regulates activity
|
PTK2 |
0.558 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257711 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Av/b5 integrin | up-regulates activity
|
PTK2 |
0.646 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257723 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A8/b1 integrin | up-regulates
|
PTK2 |
0.55 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253309 |
|
|
|
|
| pmid |
sentence |
| 15721307 |
We previously showed that α8β1-mediated adhesion of cells to fibronectin resulted in phosphorylation of FAK | FAK can activate PI3 kinase, either directly or indirectly through Src kinase [23]. |
|
| Publications: |
1 |
| + |
AE/b7 integrin | up-regulates activity
|
PTK2 |
0.478 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257727 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN12 | down-regulates
dephosphorylation
|
PTK2 |
0.542 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109035 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11432829 |
This function correlated with the ability of ptp-pest to induce dephosphorylation of shc, pyk2, fak and cas, and inactivate the ras pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A4/b1 integrin | up-regulates activity
|
PTK2 |
0.634 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257704 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITGB7 | up-regulates activity
|
PTK2 |
0.563 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257726 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A6/b4 integrin | up-regulates activity
|
PTK2 |
0.51 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257721 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
ITGB5 | up-regulates activity
|
PTK2 |
0.594 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257722 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AD/b2 integrin | up-regulates activity
|
PTK2 |
0.451 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257716 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A9/b1 integrin | up-regulates activity
|
PTK2 |
0.575 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257708 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-methyl-N-[3-[[[2-[(2-oxo-1,3-dihydroindol-5-yl)amino]-5-(trifluoromethyl)-4-pyrimidinyl]amino]methyl]-2-pyridinyl]methanesulfonamide | down-regulates
chemical inhibition
|
PTK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206067 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GDNF | up-regulates quantity by expression
transcriptional regulation
|
PTK2 |
0.451 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252184 |
|
|
Rattus norvegicus |
Neural Stem Cell |
| pmid |
sentence |
| 15212950 |
We characterize the network of 43 genes induced by GDNF overproduction of neuronal progenitor cells (ST14A), which mainly regulate migration and differentiation of neuronal progenitor cells.Laminin, Mpl3, Alcam, Bin1, Id1, Id2, Id3, neuregulin1, the ephrinB2-receptor, neuritin, focal adhesion kinase (FAK), Tc10, Pdpk1, clusterin, GTP-cyclooxygenase1, and follistatin are genes up-regulated by GDNF overexpression. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PTPN1 | down-regulates
dephosphorylation
|
PTK2 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141637 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16291744 |
We show that coexpression of wild-type alpha-actinin and ptp 1b causes dephosphorylation at tyr-397 in fak. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PF-03814735 | down-regulates
chemical inhibition
|
PTK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205959 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK18 | down-regulates activity 
|
PTK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264561 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 28361970 |
PCTK3/CDK18 regulates cell migration and adhesion by negatively modulating FAK activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DCC | up-regulates activity
binding
|
PTK2 |
0.717 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268371 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15494734 |
Here we show that different regions of the intracellular domain of DCC directly interacted with the tyrosine kinases Src and focal adhesion kinase (FAK). Netrin activated both FAK and Src and stimulated tyrosine phosphorylation of DCC. Inhibition of Src family kinases reduced DCC tyrosine phosphorylation and blocked both axon attraction and outgrowth of neurons in response to netrin. Mutation of the tyrosine phosphorylation residue in DCC abolished its function of mediating netrin-induced axon attraction. On the basis of our observations, we suggest a model in which DCC functions as a kinase-coupled receptor, and FAK and Src act immediately downstream of DCC in netrin signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268370 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29479476 |
The initial step of signaling inside the cell after netrin-1/DCC ligation is the binding of DCC cytoplasmic P3 motif to focal adhesion targeting (FAT) domain of focal adhesion kinase (FAK). Here we report the crystal structure of P3/FAT complex. The helical P3 peptide interacts with a helix-swapped FAT dimer in a 2:2 ratio. Dimeric FAT binding is P3-specific and stabilized by a calcium ion. We propose that netrin-1/DCC engagement creates a small cluster of P3/FAT for FAK recruitment close to the cell membrane, which exerts a concerted effect with PIP2 for FAK signaling. Axon guidance assays confirm that this DCC/FAK complex is physiologically essential for netrin-1-induced chemoattraction. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
ITGB8 | up-regulates activity
|
PTK2 |
0.465 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257729 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AL/b2 integrin | up-regulates activity
|
PTK2 |
0.456 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257712 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A6/b1 integrin | up-regulates activity
|
PTK2 |
0.574 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257706 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
ACP1 | down-regulates activity
dephosphorylation
|
PTK2 |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277064 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12815062 |
Lymphocyte function-associated antigen-1-mediated T cell adhesion is impaired by low molecular weight phosphotyrosine phosphatase-dependent inhibition of FAK activity. 4000254={CellProcess=4107155 CellType=10000184}}|Moreover, in these conditions LMW-PTP causes FAK dephosphorylation, thus preventing the activation of FAK downstream pathways. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITGB1 | up-regulates activity
|
PTK2 |
0.708 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257700 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
ACTN1 | down-regulates activity
binding
|
PTK2 |
0.57 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261799 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 16291744 |
Consistent with the results obtained with COS-7 cells, coexpression of wild-type α-actinin with PTP 1B in PTP 1B-null cells resulted in Src/α-actinin binding and limited the interaction between FAK and Src |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Axon guidance |
| + |
ZNF503 | up-regulates activity
|
PTK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261191 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 25538248 |
Zpo2-overexpressing cells demonstrated high levels of pFAK compared with the control (Fig. 6A). Additionally, Western blot analysis indicated that, in response to Zpo2 expression, both EpH4.9 and PyMT cells increase FAK activity, as demonstrated by higher levels of pFAK staining (Fig. 6B). |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ITGB4 | up-regulates activity
|
PTK2 |
0.581 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257720 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
A4/b7 integrin | up-regulates activity
|
PTK2 |
0.562 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257728 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2 | up-regulates activity
binding
|
TLN1 |
0.687 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257731 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
Av/b6 integrin | up-regulates activity
|
PTK2 |
0.592 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257725 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AIIB/b3 integrin | up-regulates activity
|
PTK2 |
0.568 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257717 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CADM2 | up-regulates activity
|
PTK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268855 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29506532 |
The results indicated that CADM2 […} modulates EMT process and migration ability via focal adhesion kinase (FAK) /AKT signaling pathway in HCC. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2 | up-regulates
binding
|
PIK3R1 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-53979 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9416004 |
Pi3-kinase has also been shown to bind fak in a cell cell adhesion-dipendent manner at the major autophosphorylation site y397. This association could live to activation of pi3-kinase and its downstream effectors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MYO1E | up-regulates activity
binding
|
PTK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265427 |
|
|
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 28348210 |
Myosin-1E (MYO1E), an actin-dependent molecular motor protein, directly interacts with FAK to induce Y397 autophosphorylation, which, in turn, causes changes in gene expression commonly observed in aggressive cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Av/b8 integrin | up-regulates activity
|
PTK2 |
0.582 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257730 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A3/b1 integrin | up-regulates activity
|
PTK2 |
0.616 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257703 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP3 | down-regulates activity
dephosphorylation
|
PTK2 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277033 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28759036 |
Deficiency in VHR/DUSP3, a suppressor of focal adhesion kinase, reveals its role in regulating cell adhesion and migration.|In vitro assays proved that recombinant VHR directly dephosphorylated FAK and paxillin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RTKs | up-regulates activity
phosphorylation
|
PTK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259030 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30889378 |
The RTKs in turn induce phosphorylation of focal adhesion kinase (FAK) or the signaling domain of the b4 integrin. These elements recruit distinct subsets of signaling enzymes and adaptors, refining the specificity of individual partner RTKs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
Av/b2 integrin | up-regulates activity
|
PTK2 |
0.628 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257715 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AM/b2 integrin | up-regulates activity
|
PTK2 |
0.469 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257713 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAP1 | down-regulates activity
|
PTK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264824 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 30894654 |
In HeLa and metastatic breast cancer cells, depletion of CAP1 leads to activation of FAK and enhanced cell adhesion |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A1/b1 integrin | up-regulates activity
|
PTK2 |
0.576 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257701 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
A2/b1 integrin | up-regulates activity
|
PTK2 |
0.6 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257702 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Av/b3 integrin | up-regulates activity
|
PTK2 |
0.681 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257719 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
ITGB6 | up-regulates activity
|
PTK2 |
0.486 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257724 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A10/b1 integrin | up-regulates activity
|
PTK2 |
0.553 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257709 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A8/b1 integrin | up-regulates activity
|
PTK2 |
0.55 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257707 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KDR | up-regulates activity
|
PTK2 |
0.493 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261945 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 22264731 |
Here we show that genetic or pharmacological FAK inhibition in ECs prevents VEGF-stimulated permeability downstream of VEGF receptor or Src tyrosine kinase activation in vivo. VEGF promotes tension-independent FAK activation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | VEGF Signaling |
| + |
ITGB3 | up-regulates activity
|
PTK2 |
0.664 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257718 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
PTK2 | up-regulates activity
binding
|
GRB2 |
0.704 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257733 |
|
|
|
|
| pmid |
sentence |
| 15688067 |
Src-mediated phosphorylation of FAK at Tyr925 creates an SH2 binding site for the growth-factor-receptor-bound protein 2 (GRB2) adaptor protein, which leads to the activation of Ras and the extracellular signal-regulated kinase-2 (ERK2) cascade. |
|
| Publications: |
1 |
| Pathways: | Integrin Signaling, VEGF Signaling |
| + |
A11/b1 integrin | up-regulates activity
|
PTK2 |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257710 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PTK2
- 
- 