+ |
PTK2B |
phosphorylation
|
SNCA |
0.32 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249151 |
Tyr125 |
VDPDNEAyEMPSEEG |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
12096713 |
The present report demonstrates that the protein tyrosine kinase Pyk2/RAFTK is involved in cell stress-induced tyrosine phosphorylation of alpha S. Hyperosmotic stress induced tyrosine phosphorylation of alpha S via Pyk2/RAFTK at tyrosine residue 125. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
PTK2B | down-regulates activity
phosphorylation
|
ASAP1 |
0.469 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263186 |
Tyr323 |
QLQGNKEyGSEKKGY |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
12771146 |
The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylation and inhibition of the Arf-GTPase-activating protein ASAP1. Pyk2 directly phosphorylates ASAP1 on tyrosine residues in vitro and increases ASAP1 tyrosine phosphorylation when co-expressed in HEK293T cells.Phosphorylation of tyrosine 308 and 782 affects the phosphoinositide binding profile of ASAP1, and fluorimetric Arf-GTPase assays with purified proteins revealed an inhibition of ASAP1 GTPase-activating protein activity by Pyk2-mediated tyrosine phosphorylation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263187 |
Tyr767 |
RDKQRLSyGAFTNQI |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
12771146 |
The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylation and inhibition of the Arf-GTPase-activating protein ASAP1. Pyk2 directly phosphorylates ASAP1 on tyrosine residues in vitro and increases ASAP1 tyrosine phosphorylation when co-expressed in HEK293T cells.Phosphorylation of tyrosine 308 and 782 affects the phosphoinositide binding profile of ASAP1, and fluorimetric Arf-GTPase assays with purified proteins revealed an inhibition of ASAP1 GTPase-activating protein activity by Pyk2-mediated tyrosine phosphorylation. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PTK2B | up-regulates
phosphorylation
|
PTK2B |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124339 |
Tyr402 |
CSIESDIyAEIPDET |
Homo sapiens |
|
pmid |
sentence |
15105428 |
Overexpression of pyk2 alone led to its spontaneous activation and tyrosine phosphorylation, resulting in activation of stat5b, indicated by the reporter gfp-stat5b. These effects were completely dependent upon tyr(402), the autophosphorylation site of pyk2, which allows recruitment of src family members for further activating phosphorylations at other sites on pyk2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN6 | down-regulates
dephosphorylation
|
PTK2B |
0.365 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-71414 |
Tyr402 |
CSIESDIyAEIPDET |
Homo sapiens |
|
pmid |
sentence |
10521452 |
Raftk binds constitutively to the protein tyrosine phosphatase shptp1.SHPTP1 Plays a negative role in pyk2/raftk signaling by dephosphorylating raftk on tyr-402, thereby inhibiting the interaction of the sh2 domain of c-src with raftk |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN12 | down-regulates activity
dephosphorylation
|
PTK2B |
0.562 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248662 |
Tyr402 |
CSIESDIyAEIPDET |
Rattus norvegicus |
|
pmid |
sentence |
11337490 |
Inhibition of the catalytic activity of cell adhesion kinase beta by protein-tyrosine phosphatase-PEST-mediated dephosphorylation|CAKbeta was found to be a substrate for PTP-PEST. Both the major autophosphorylation site of CAKbeta (Tyr(402)) and activation loop tyrosine residues, Tyr(579) and Tyr(580), were targeted for dephosphorylation by PTP-PEST. Dephosphorylation of CAKbeta by PTP-PEST dramatically inhibited CAKbeta kinase activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-107502 |
Tyr579 |
RYIEDEDyYKASVTR |
Homo sapiens |
|
pmid |
sentence |
11337490 |
Inhibition of the catalytic activity of cell adhesion kinase beta by protein-tyrosine phosphatase-pest-mediated dephosphorylation. / dephosphorylation of tyr402 and tyr579/580 by ptp-pest |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248664 |
Tyr580 |
YIEDEDYyKASVTRL |
Rattus norvegicus |
|
pmid |
sentence |
11337490 |
Inhibition of the catalytic activity of cell adhesion kinase beta by protein-tyrosine phosphatase-PEST-mediated dephosphorylation|CAKbeta was found to be a substrate for PTP-PEST. Both the major autophosphorylation site of CAKbeta (Tyr(402)) and activation loop tyrosine residues, Tyr(579) and Tyr(580), were targeted for dephosphorylation by PTP-PEST. Dephosphorylation of CAKbeta by PTP-PEST dramatically inhibited CAKbeta kinase activity. |
|
Publications: |
3 |
Organism: |
Rattus Norvegicus, Homo Sapiens |
+ |
SRC | up-regulates
phosphorylation
|
PTK2B |
0.607 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-133870 |
Tyr402 |
CSIESDIyAEIPDET |
Homo sapiens |
|
pmid |
sentence |
15695828 |
These data indicate that pyk2 activation via phosphorylation at tyr-402 requires ?V?3 Ligation and src activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTK2B | up-regulates
phosphorylation
|
PTK2 |
0.503 |
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 |
+ |
PTK2B | up-regulates activity
phosphorylation
|
TGFB1I1 |
0.734 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262876 |
Tyr60 |
SGDKDHLySTVCKPR |
Chlorocebus aethiops |
|
pmid |
sentence |
10838081 |
Hic-5 is a CAKbeta-binding protein localized at focal adhesions. Here we show that overexpression of CAKbeta or Fyn, but not FAK, enhanced the tyrosine phosphorylation of coexpressed Hic-5 in COS-7 cells. The Y60F mutant of Hic-5 was not phosphorylated, and Hic-5 phosphorylated on tyrosine 60 was bound specifically to the SH2 domain of Csk. Specific phosphorylation of Hic-5 by CAKbeta and Fyn may activate a signaling pathway mediated by Hic-5. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
PTK2B | down-regulates
phosphorylation
|
NOS3 |
0.315 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178648 |
Tyr657 |
FGLGSRAyPHFCAFA |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
18483407 |
We found that fluid shear stress induces the association of enos with the proline-rich tyrosine kinase 2 (pyk2) in endothelial cells and that the enos immunoprecipitated from enos- and pyk2-overexpressing hek293 cells was tyrosine-phosphorylated on tyr657. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-161824 |
Tyr657 |
FGLGSRAyPHFCAFA |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19934023 |
We found that fluid shear stress induces the association of enos with the proline-rich tyrosine kinase 2 (pyk2) in endothelial cells and that the enos immunoprecipitated from enos- and pyk2-overexpressing hek293 cells was tyrosine-phosphorylated on tyr657. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PTPN11 | down-regulates activity
dephosphorylation
|
PTK2B |
0.714 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277084 |
Tyr906 |
CQLPPEGyVVVVKNV |
Homo sapiens |
|
pmid |
sentence |
10880513 |
We demonstrate that RAFTK is a direct substrate of SHP2 both in vitro and in vivo, and that Tyr(906) in the C-terminal domain of RAFTK mediates its interaction with SHP2. |We demonstrate that RAFTK is a direct substrate of SHP2 both in vitro and in vivo, and that Tyr(906) in the C-terminal domain of RAFTK mediates its interaction with SHP2. Moreover, overexpression of dominant negative SHP2 blocked the protective effect of IL-6 against Dex-induced apoptosis. These findings demonstrate that SHP2 mediates the anti-apoptotic effect of IL-6 and suggest SHP2 as a novel therapeutic target in MM..... 1) RAFTK is a substrate of SHP2 in vitro and 2) dephosphorylation of RAFTK by SHP2 inhibits its kinase activity. |
|
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
|
PTK2B |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-206070 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTK2B | up-regulates activity
phosphorylation
|
STAP1 |
0.358 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261818 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10518561 |
In 293 cells expressing recombinant BRDG1 and various PTKs, Tec and Pyk2, but not Btk, Bmx, Lyn, Syk, or c-Abl, induced marked phosphorylation of BRDG1 on tyrosine residues. BRDG1 was also phosphorylated by Tec directly in vitro. Furthermore, BRDG1 was shown to participate in a positive feedback loop by increasing the activity of Tec. BRDG1 thus appears to function as a docking protein acting downstream of Tec in BCR signaling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTK2B | up-regulates activity
phosphorylation
|
ASAP2 |
0.541 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269704 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10022920 |
Tyrosine phosphorylation of Pap by Pyk2 or Src kinases. We have identified a new Pyk2 binding protein designated Pap. Pap is a multidomain protein composed of an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal SH3 domain. We demonstrate that Pap forms a stable complex with Pyk2 and that activation of Pyk2 leads to tyrosine phosphorylation of Pap in living cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |