| + |
PTK6 | up-regulates 
phosphorylation
|
ARHGAP5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181452 |
Tyr1109 |
KGYSDEIyVVPDDSQ |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 18829532 |
Breast tumor kinase phosphorylates p190rhogap to regulate rho and ras and promote breast carcinoma growth, migration, and invasion. Brk phosphorylates p190 at the y(1105) residue both in vitro and in vivo, thereby promoting the association of p190 with p120rasgap (p120). As a consequence, brk stimulates p190 and attenuates p120 functions, leading to rhoa inactivation and ras activation, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK6 | down-regulates quantity 
phosphorylation
|
CTNNB1 |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278286 |
Tyr142 |
AVVNLINyQDDAELA |
Homo sapiens |
|
| pmid |
sentence |
| 20026641 |
PTK6 directly phosphorylates beta-catenin on Tyr64, Tyr142, Tyr331 and/or Tyr333, with the predominant site being Tyr64.|The ability of PTK6 to negatively regulate beta-catenin and TCF transcription by modulating levels of TCF4 and TLE and Groucho could contribute to its growth-inhibitory activities in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278287 |
Tyr331 |
LVNIMRTyTYEKLLW |
Homo sapiens |
|
| pmid |
sentence |
| 20026641 |
PTK6 directly phosphorylates beta-catenin on Tyr64, Tyr142, Tyr331 and/or Tyr333, with the predominant site being Tyr64.|The ability of PTK6 to negatively regulate beta-catenin and TCF transcription by modulating levels of TCF4 and TLE and Groucho could contribute to its growth-inhibitory activities in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278289 |
Tyr333 |
NIMRTYTyEKLLWTT |
Homo sapiens |
|
| pmid |
sentence |
| 20026641 |
PTK6 directly phosphorylates beta-catenin on Tyr64, Tyr142, Tyr331 and/or Tyr333, with the predominant site being Tyr64.|The ability of PTK6 to negatively regulate beta-catenin and TCF transcription by modulating levels of TCF4 and TLE and Groucho could contribute to its growth-inhibitory activities in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278288 |
Tyr64 |
VDTSQVLyEWEQGFS |
Homo sapiens |
|
| pmid |
sentence |
| 20026641 |
PTK6 directly phosphorylates beta-catenin on Tyr64, Tyr142, Tyr331 and/or Tyr333, with the predominant site being Tyr64.|The ability of PTK6 to negatively regulate beta-catenin and TCF transcription by modulating levels of TCF4 and TLE and Groucho could contribute to its growth-inhibitory activities in vivo. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PTK6 | up-regulates activity
phosphorylation
|
BCAR1 |
0.62 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177238 |
Tyr165 |
PSPATDLyQVPPGPG |
Homo sapiens |
|
| pmid |
sentence |
| 22084245 |
Protein-tyrosine kinase 6 promotes peripheral adhesion complex formation and cell migration by phosphorylating p130 crk-associated substrate. Tyrosine residues 165 and 664 of p130cas were both phosphorylated by ptk6 in vitro |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK6 | up-regulates activity
phosphorylation
|
ARAP1 |
0.507 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263188 |
Tyr231 |
PEFDDSDyDEVPEEG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20554524 |
ARAP1 associated with PTK6 in an EGF/EGF receptor (EGFR)-dependent manner. In addition, the SH2 domain of PTK6, particularly the Arg(105) residue that contacts the phosphate group of the tyrosine residue, was essential for the association. Moreover, PTK6 phosphorylated residue Tyr(231) in the N-terminal domain of ARAP1. Expression of ARAP1, but not of the Y231F mutant, inhibited the down-regulation of EGFR in HEK293 cells expressing PTK6. These results demonstrate that PTK6 enhances EGFR signaling by inhibition of EGFR down-regulation through phosphorylation of ARAP1 in breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK6 | up-regulates activity
phosphorylation
|
STAP2 |
0.738 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247067 |
Tyr250 |
PFLLDEDyEKVLGYV |
Homo sapiens |
|
| pmid |
sentence |
| 19393627 |
Our previous studies revealed that STAP-2 binds to signal transducer and activator of transcription 3 (STAT3) and STAT5, and regulates the signaling pathways downstream of them. In the present study, we identified tyrosine-250 (Tyr250) in STAP-2 as a major site of phosphorylation by Brk, using a series of STAP-2 YF mutants and anti-phospho-STAP-2 Tyr250 antibody. Furthermore, overexpression of the STAP-2 Y250F mutant protein affected Brk-mediated STAT3 activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK6 | up-regulates
phosphorylation
|
AKT |
0.499 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138437 |
Tyr315 |
TFCGTPEyLAPEVLE |
Homo sapiens |
|
| pmid |
sentence |
| 15994200 |
These observations suggest that RET/PTC is able to phosphorylate the Y315 residue of PKB, an event that results in maximal activation of PKB for RET/PTC-induced thyroid tumorigenesis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166506 |
Tyr315 |
TFCGTPEyLAPEVLE |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20606012 |
Here we demonstrate that AKT is a direct substrate of PTK6 and that AKT tyrosine residues 315 and 326 are phosphorylated by PTK6. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166510 |
Tyr326 |
EVLEDNDyGRAVDWW |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20606012 |
Here we demonstrate that AKT is a direct substrate of PTK6 and that AKT tyrosine residues 315 and 326 are phosphorylated by PTK6. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Prostate Gland |
| + |
PTK6 | up-regulates
phosphorylation
|
AKT1 |
0.499 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252617 |
Tyr315 |
TFCGTPEyLAPEVLE |
Homo sapiens |
|
| pmid |
sentence |
| 15994200 |
These observations suggest that RET/PTC is able to phosphorylate the Y315 residue of PKB, an event that results in maximal activation of PKB for RET/PTC-induced thyroid tumorigenesis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252618 |
Tyr315 |
TFCGTPEyLAPEVLE |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20606012 |
Here we demonstrate that AKT is a direct substrate of PTK6 and that AKT tyrosine residues 315 and 326 are phosphorylated by PTK6. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252622 |
Tyr326 |
EVLEDNDyGRAVDWW |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20606012 |
Here we demonstrate that AKT is a direct substrate of PTK6 and that AKT tyrosine residues 315 and 326 are phosphorylated by PTK6. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Prostate Gland |
| + |
PTPN1 | down-regulates activity
dephosphorylation
|
PTK6 |
0.594 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277082 |
Tyr342 |
RLIKEDVyLSHDHNI |
Homo sapiens |
|
| pmid |
sentence |
| 29142193 |
Using a variety of PTEN mutant constructs, we show that protein phosphatase activity of PTEN targets PTK6, with efficiency similar to PTP1B, a phosphatase that directly dephosphorylates PTK6 Y342. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity
dephosphorylation
|
PTK6 |
0.41 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276975 |
Tyr342 |
RLIKEDVyLSHDHNI |
in vitro |
|
| pmid |
sentence |
| 29142193 |
PTEN inhibits PTK6 activity and downstream signaling in prostate cancer cells.|Using an in vitro phosphatase assay, we observed that PTEN was able to dephosphorylate PTK6 at tyrosine residue 342 in a dose dependent manner. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PTK6 | up-regulates
phosphorylation
|
PTK6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90604 |
Tyr342 |
RLIKEDVyLSHDHNI |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 12121988 |
Autophosphorylation increases enzyme activity of wild-type brk but not of a y342a mutant form of brk. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK6 | down-regulates activity
phosphorylation
|
DOK1 |
0.513 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278301 |
Tyr362 |
DPKEDPIyDEPEGLA |
Homo sapiens |
|
| pmid |
sentence |
| 24523872 |
BRK downregulates Dok1 via proteasomal degradation.|BRK phosphorylates Dok1 at tyrosine 362. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK6 |
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4.0
PTK6
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