| + |
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 | up-regulates activity
phosphorylation
|
BCAR1 |
0.584 |
| 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 |
0.463 |
| 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 |
0.714 |
| 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
|
AKT1 |
0.454 |
| 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-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-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 |
| + |
PTK6 | up-regulates
phosphorylation
|
AKT |
0.454 |
| 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 |
| + |
PTPN1 | down-regulates activity 
dephosphorylation
|
PTK6 |
0.557 |
| 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 |
0.427 |
| 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 |
phosphorylation
|
KHDRBS1 |
0.738 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249293 |
Tyr435 |
ARPVKGAyREHPYGR |
Homo sapiens |
|
| pmid |
sentence |
| 16179349 |
We show that BRK phosphorylates Sam68 on all three tyrosines in the nuclear localization signal. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249294 |
Tyr440 |
GAYREHPyGRY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16179349 |
We show that BRK phosphorylates Sam68 on all three tyrosines in the nuclear localization signal. |Tyrosine 440 was identified as a principal modulator of Sam68 localization and this site was phosphorylated in response to EGF treatment in human breast tumor cell lines. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249292 |
Tyr443 |
REHPYGRy |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16179349 |
We show that BRK phosphorylates Sam68 on all three tyrosines in the nuclear localization signal. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PTK6 | up-regulates activity
phosphorylation
|
PTK6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249152 |
Tyr447 |
RLSSFTSyENPT |
Homo sapiens |
|
| pmid |
sentence |
| 12121988 |
Mutation of a C-terminal tyrosine (Tyr-447) increases enzyme activity and SH2 domain accessibility, consistent with a role for this residue in autoinhibition. | These results suggest that the Y447F and W44A mutations disrupt the normal intramolecular regulation of Brk and increase the catalytic activity of Brk. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK6 | up-regulates activity
phosphorylation
|
EPS8 |
0.366 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263189 |
Tyr498 |
YAFSSNIyTRGSHLD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27738316 |
Eps8 which was identified by this method is phosphorylated by Myr-PTK6 in HEK293 cells. Mouse Eps8 expressed in HEK293 cells is phosphorylated by Myr-PTK6 at residues Tyr497, Tyr524, and Tyr534. These results indicate that plasma-membrane-associated PTK6 phosphorylates Eps8, which promotes cell proliferation, adhesion, and migration and, thus, tumorigenesis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263190 |
Tyr525 |
NRHIDRNyEPLKTQP |
Homo sapiens |
|
| pmid |
sentence |
| 28214294 |
Eps8 which was identified by this method is phosphorylated by Myr-PTK6 in HEK293 cells. Mouse Eps8 expressed in HEK293 cells is phosphorylated by Myr-PTK6 at residues Tyr497, Tyr524, and Tyr534. These results indicate that plasma-membrane-associated PTK6 phosphorylates Eps8, which promotes cell proliferation, adhesion, and migration and, thus, tumorigenesis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263191 |
Tyr535 |
LKTQPKKyAKSKYDF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28214294 |
Eps8 which was identified by this method is phosphorylated by Myr-PTK6 in HEK293 cells. Mouse Eps8 expressed in HEK293 cells is phosphorylated by Myr-PTK6 at residues Tyr497, Tyr524, and Tyr534. These results indicate that plasma-membrane-associated PTK6 phosphorylates Eps8, which promotes cell proliferation, adhesion, and migration and, thus, tumorigenesis. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PTK6 | up-regulates
phosphorylation
|
BCAR1 |
0.584 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177242 |
Tyr664 |
EGGWMEDyDYVHLQG |
Homo sapiens |
Prostate Gland Cancer Cell |
| 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
phosphorylation
|
STAT5B |
0.441 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159066 |
Tyr699 |
TAKAVDGyVKPQIKQ |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17997837 |
Phosphospecific antibodies, mutational analysis, and in vitro kinase assays demonstrated that brk specifically mediated stat5b phosphorylation at the activating tyrosine, y699. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK6 | up-regulates
phosphorylation
|
KHDRBS1 |
0.738 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-80020 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10913193 |
Sik/brk is the first identified tyrosine kinase that can phosphorylate sam68 and regulate its activity within the nucleus, where it resides during most of the cell cycle |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK6 | up-regulates
phosphorylation
|
STAP2 |
0.714 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81489 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10980601 |
The phosphorylation of and association with bks by brk was also dependent on the sh2-like domain present within bks.bks is a substrate for the kinase activity of brk and has the characteristics of an adaptor protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PTK6
- 
- 