| + |
PRKACA | up-regulates activity 
phosphorylation
|
CSK |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105229 |
Ser364 |
ALREKKFsTKSDVWS |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 11181701 |
Activation of the cooh-terminal src kinase (csk) by camp-dependent protein kinase inhibits signaling through the t cell receptor.Pka phosphorylates csk at s364 in vitro and in vivo leading to a two- to fourfold increase in csk activity that is necessary for camp-mediated inhibition of tcr-induced interleukin 2 secretion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSK | up-regulates
phosphorylation
|
PTPRC |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-26785 |
Tyr1218 |
MVSTFEQyQFLYDVI |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 7507203 |
Tyrosine phosphorylation of cd45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphatase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation |
| + |
CSK | up-regulates activity
phosphorylation
|
MDM2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279163 |
Tyr281 |
EVYQVTVyQAGESDT |
Homo sapiens |
|
| pmid |
sentence |
| 25624478 |
Here we show that activated c-Src kinase phosphorylates Y281 and Y302 of Mdm2, resulting in an increase in Mdm2 stability and its association with Ubc12, the E2 enzyme of the neddylating complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279164 |
Tyr302 |
PEISLADyWKCTSCN |
Homo sapiens |
|
| pmid |
sentence |
| 25624478 |
Here we show that activated c-Src kinase phosphorylates Y281 and Y302 of Mdm2, resulting in an increase in Mdm2 stability and its association with Ubc12, the E2 enzyme of the neddylating complex. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSK | up-regulates activity
phosphorylation
|
CSK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250778 |
Tyr304 |
DVCEAMEyLEGNNFV |
in vitro |
|
| pmid |
sentence |
| 9148770 |
Taken together these results indicate that Csk can be phosphorylated in vivo at Tyr-184 by an as yet unknown tyrosine kinase, and that autophosphorylation of Tyr-304 occurs only at abnormally high Csk concentrations in vitro. Furthermore, Tyr-304 is required for the maintenance of the structure of the Csk kinase domain. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | EBV infection, T cell activation |
| + |
CSK | down-regulates 
phosphorylation
|
LCK |
0.555 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-20371 |
Tyr505 |
FTATEGQyQPQP |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 1639064 |
P50csk tyrosine kinase phosphorylates p56lck at tyr-505 and down regulates its catalytic activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation |
| + |
CSK | down-regulates
phosphorylation
|
LYN |
0.554 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-132912 |
Tyr508 |
YTATEGQyQQQP |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 15626731 |
Lyn tyr507 kinase, csk, is recruited by pag, which targets lipid rafts by palmitoylation.Thus, our data suggest that il-6 treatment induces the translocation of cd45 to lipid rafts sequentially, followed by the association of cd45 with lyn and pag;dephosphorylation of lyn tyr507 and pag tyr314;lyn activation;and csk release from lipid rafts |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection |
| + |
CSK | down-regulates activity
phosphorylation
|
FGR |
0.553 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250779 |
Tyr523 |
FTSAEPQyQPGDQT |
in vitro |
|
| pmid |
sentence |
| 7515063 |
CSK catalyzed phosphorylation affects Tyr-511 of c-Fgr, homologous to Tyr-527 of c-Src and it prevents the autophosphorylation normally occurring at c-Fgr Tyr-400, homologous to c-Src Tyr-416. | Once phosphorylated at Tyr-511 and down-regulated by CSK, c-Fgr is no more susceptible to polylysine stimulation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CSK | down-regulates
phosphorylation
|
SRC |
0.584 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179417 |
Tyr530 |
FTSTEPQyQPGENL |
Homo sapiens |
|
| pmid |
sentence |
| 18614016 |
The catalytic activity of the src family of tyrosine kinases is suppressed by phosphorylation on a tyrosine residue located near the c terminus (tyr 527 in c-src), which is catalyzed by c-terminal src kinase (csk). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSK | up-regulates activity
phosphorylation
|
PECAM1 |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262741 |
Tyr713 |
KKDTETVySEVRKAV |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 9624175 |
We demonstrated that phosphorylation of PECAM-1 by Src or Csk family kinases was sufficient to trigger its association with SHP-2. Moreover, it was able to promote binding of PECAM-1 to SHP-1, a SHP-2-related protein-tyrosine phosphatase expressed in hemopoietic cells. Taken together, these findings indicated that the Src and Csk families of kinases are strong candidates for mediating tyrosine phosphorylation of PECAM-1 and triggering its association with SH2 domain-containing phosphatases under physiological circumstances. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
IGF1R | up-regulates 
|
CSK |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-64676 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10026153 |
The results suggest that c-src and csk are involved in igf-ir and ir signaling and that the interaction of csk with the igf-ir may play a role in the decrease in c-src activity following igf-i stimulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection |
| + |
lapatinib | down-regulates activity
chemical inhibition
|
CSK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257900 |
|
|
Homo sapiens |
HUVEC Cell |
| pmid |
sentence |
| 21443688 |
YN968D1 potently suppressed the kinase activities of VEGFR-2, c-kit and c-src, and inhibited cellular phosphorylation of VEGFR-2, c-kit and PDGFRβ. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSK | down-regulates quantity
phosphorylation
|
EEF2 |
0.261 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279698 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24648518 |
C-terminal Src kinase (Csk)-mediated phosphorylation of eukaryotic elongation factor 2 (eEF2) promotes proteolytic cleavage and nuclear translocation of eEF2.|In this report, we show that eukaryotic elongation factor 2 (eEF2) is a new protein substrate of Csk and could locate in the nucleus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSK | up-regulates
binding
|
NOTCH1 |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196824 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22479394 |
We found that the notch-1-furin interaction is regulated by the non-receptor tyrosine kinase, c-src. c-src and notch-1 are physically associated, and this association is responsible for notch-1 processing and activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSK | down-regulates activity
phosphorylation
|
ITCH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245327 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16888620 |
CISK strongly interacts and colocalizes with the E3 ubiquitin ligase AIP4, which is important for the ubiquitin-dependent lysosomal degradation of CXCR4. Moreover, the observed inhibition is both dependent on the interaction between CISK and AIP4 and on the activation status of CISK. Consistent with this, an activated form of CISK but not of the related kinase SGK1 phosphorylates specific sites of AIP4 in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CREBBP | up-regulates
binding
|
CSK |
0.55 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-77139 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10801129 |
Here we present cbp--a transmembrane phosphoprotein that is ubiquitously expressed and binds specifically to the sh2 domain of csk. Cbp is involved in the membrane localization of csk and in the csk-mediated inhibition of c-src. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
CSK
- 
- 