| + |
HCK | up-regulates activity 
phosphorylation
|
PLCG1 |
0.661 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249360 |
Tyr1253 |
EGSFESRyQQPFEDF |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249361 |
Tyr771 |
IGTAEPDyGALYEGR |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249362 |
Tyr783 |
EGRNPGFyVEANPMP |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
HCK | up-regulates
phosphorylation
|
BCR-ABL |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-53964 |
Tyr177 |
ADAEKPFyVNVEFHH |
Homo sapiens |
|
| pmid |
sentence |
| 9407116 |
The src family kinase hck interacts with bcr-abl by a kinase-independent mechanism and phosphorylates the grb2-binding site of bcr |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HCK | up-regulates
phosphorylation
|
ELMO1 |
0.588 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138142 |
Tyr18 |
AIEWPGAyPKLMEID |
Homo sapiens |
|
| pmid |
sentence |
| 15952790 |
We previously showed that elmo1 binds directly to the hck sh3 domain and is phosphorylated by hck. In this study, we used mass spectrometry to identify the following sites of elmo1 phosphorylation: tyr 18, tyr 216, tyr 511, tyr 395, and tyr 720. Mutant forms of elmo1 lacking these sites were defective in their ability to promote phagocytosis and migration in fibroblasts. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138146 |
Tyr216 |
VLNSHDLyQKVAQEI |
Homo sapiens |
|
| pmid |
sentence |
| 15952790 |
We previously showed that elmo1 binds directly to the hck sh3 domain and is phosphorylated by hck. In this study, we used mass spectrometry to identify the following sites of elmo1 phosphorylation: tyr 18, tyr 216, tyr 511, tyr 395, and tyr 720. Mutant forms of elmo1 lacking these sites were defective in their ability to promote phagocytosis and migration in fibroblasts. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138150 |
Tyr395 |
AKHHQDAyIRIVLEN |
Homo sapiens |
|
| pmid |
sentence |
| 15952790 |
We previously showed that elmo1 binds directly to the hck sh3 domain and is phosphorylated by hck. In this study, we used mass spectrometry to identify the following sites of elmo1 phosphorylation: tyr 18, tyr 216, tyr 511, tyr 395, and tyr 720. Mutant forms of elmo1 lacking these sites were defective in their ability to promote phagocytosis and migration in fibroblasts. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138154 |
Tyr511 |
SKLQNLSyTEILKIR |
Homo sapiens |
|
| pmid |
sentence |
| 15952790 |
We previously showed that elmo1 binds directly to the hck sh3 domain and is phosphorylated by hck. In this study, we used mass spectrometry to identify the following sites of elmo1 phosphorylation: tyr 18, tyr 216, tyr 511, tyr 395, and tyr 720. Mutant forms of elmo1 lacking these sites were defective in their ability to promote phagocytosis and migration in fibroblasts. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138158 |
Tyr720 |
IPKEPSNyDFVYDCN |
Homo sapiens |
|
| pmid |
sentence |
| 15952790 |
We previously showed that elmo1 binds directly to the hck sh3 domain and is phosphorylated by hck. In this study, we used mass spectrometry to identify the following sites of elmo1 phosphorylation: tyr 18, tyr 216, tyr 511, tyr 395, and tyr 720. Mutant forms of elmo1 lacking these sites were defective in their ability to promote phagocytosis and migration in fibroblasts. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
HCK | up-regulates activity
phosphorylation
|
WAS |
0.577 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273957 |
Tyr291 |
AETSKLIyDFIEDQG |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 12235133 |
Hck induces tyrosine phosphorylation of WASp. Here we show that the Src family kinase Hck induces phosphorylation of WASp-Tyr(291) independently of Cdc42 and that this causes a shift in the mobility of WASp upon SDS-PAGE. A phospho-mimicking mutant, WASp-Y291E, exhibited an enhanced ability to stimulate actin polymerization in a cell-free system and when microinjected into primary macrophages induced extensive filopodium formation with greater efficiency than wild-type WASp or a Y291F mutant. We propose that phosphorylation of Tyr(291) directly regulates WASp function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251268 |
Tyr291 |
AETSKLIyDFIEDQG |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12235133 |
Src family kinase Hck induces phosphorylation of WASp-Tyr(291). Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
HCK | up-regulates
phosphorylation
|
HCK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-80340 |
Tyr411 |
RVIEDNEyTAREGAK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10934191 |
Tyr(416) is the autophosphorylation site in the activation loop. Autophosphorylation of tyr(416) is required for hck activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HCK | up-regulates activity
phosphorylation
|
HCK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251266 |
Tyr411 |
RVIEDNEyTAREGAK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10934191 |
Hck transiently expressed in human embryonic kidney 293T cells was found to be phosphorylated at Tyr-29 and Tyr-388, proving that Hck can also undergo autophosphorylation at both sites in vivo. autophosphorylation of Tyr-29 contributes significantly to the activation of Hck. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251265 |
Tyr51 |
ASPHCPVyVPDPTST |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10934191 |
Hck transiently expressed in human embryonic kidney 293T cells was found to be phosphorylated at Tyr-29 and Tyr-388, proving that Hck can also undergo autophosphorylation at both sites in vivo. autophosphorylation of Tyr-29 contributes significantly to the activation of Hck. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
HCK | up-regulates
phosphorylation
|
RAPGEF1 |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203613 |
Tyr504 |
APIPSVPyAPFAAIL |
Homo sapiens |
|
| pmid |
sentence |
| 24396067 |
We also showed that ctla-4 receptor signaling mediates tyrosine phosphorylation in the c3g protein, and that this is required for augmented activation of rap1 and increased adhesion mediated by leukocyte function-associated antigen type 1 (lfa-1). ctla-4 signaling leads to phosphorylation of c3g tyrosine 504. the src family member hck phosphorylates c3g downstream of ctla-4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HCK | down-regulates 
phosphorylation
|
HCK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76996 |
Tyr522 |
YTATESQyQQQP |
Homo sapiens |
|
| pmid |
sentence |
| 10934191 |
We demonstrate that autophosphorylation of the recombinant src family kinase hck leads to a 20-fold increase in its specific enzymatic activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HCK | up-regulates activity
phosphorylation
|
STAT3 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251267 |
Tyr705 |
DPGSAAPyLKTKFIC |
in vitro |
|
| pmid |
sentence |
| 12244095 |
Activation of STAT3 by the Src family kinase Hck requires a functional SH3 domain. Direct Phosphorylation of STAT3 on Tyr-705 by Src Family Kinases |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HCK |
phosphorylation
|
ADAM15 |
0.362 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112927 |
Tyr715 |
LVMLGASyWYRARLH |
Homo sapiens |
|
| pmid |
sentence |
| 11741929 |
Hck, and to a lesser extent lck, phosphorylated the adam15 cytoplasmic domain in vitro in immune complex kinase assays. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HCK | up-regulates
phosphorylation
|
ADAM15 |
0.362 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112919 |
Tyr715 |
LVMLGASyWYRARLH |
Homo sapiens |
|
| pmid |
sentence |
| 11741929 |
Hck, and to a lesser extent lck, phosphorylated the adam15. Deletion and point mutation analysis of the adam15 cytoplasmic domain confirmed the importance of the proline-rich motifs for grb2 and lck binding and indicated the regulatory nature of tyr(715) and tyr(735). These data demonstrate selective, phosphorylation-dependent interactions of adam15 with src family ptks and grb2, which highlight the potential for integration of adam functions and cellular signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112923 |
Tyr735 |
LKGPTCQyRAAQSGP |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 11741929 |
Hck, and to a lesser extent lck, phosphorylated the adam15. Deletion and point mutation analysis of the adam15 cytoplasmic domain confirmed the importance of the proline-rich motifs for grb2 and lck binding and indicated the regulatory nature of tyr(715) and tyr(735). These data demonstrate selective, phosphorylation-dependent interactions of adam15 with src family ptks and grb2, which highlight the potential for integration of adam functions and cellular signaling. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
HCK | up-regulates activity
phosphorylation
|
BCR-ABL |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260810 |
Tyr730 |
PNLFVALyDFVASGD |
Homo sapiens |
|
| pmid |
sentence |
| 16912036 |
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260811 |
Tyr775 |
QGWVPSNyITPVNSL |
Homo sapiens |
|
| pmid |
sentence |
| 16912036 |
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260813 |
Tyr788 |
SLEKHSWyHGPVSRN |
Homo sapiens |
|
| pmid |
sentence |
| 16912036 |
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260812 |
Tyr798 |
VSRNAAEyLLSSGIN |
Homo sapiens |
|
| pmid |
sentence |
| 16912036 |
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260814 |
Tyr832 |
LRYEGRVyHYRINTA |
Homo sapiens |
|
| pmid |
sentence |
| 16912036 |
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260815 |
Tyr845 |
TASDGKLyVSSESRF |
Homo sapiens |
|
| pmid |
sentence |
| 16912036 |
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260816 |
Tyr875 |
GLITTLHyPAPKRNK |
Homo sapiens |
|
| pmid |
sentence |
| 16912036 |
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity. |
|
| Publications: |
7 |
Organism: |
Homo Sapiens |
| + |
HCK | up-regulates activity
phosphorylation
|
CSF3R |
0.394 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251263 |
Tyr752 |
GTSDQVLyGQLLGSP |
in vitro |
|
| pmid |
sentence |
| 9790917 |
Hck becomes activated upon G-CSF treatment and is, in turn, able to phosphorylate the G-CSF-R, indicating a clear functional and physical involvement in G-CSF signaling. the ability of Hck to phosphorylate the G-CSF-R in vitro, both Y728 and Y763 fit the Src consensus phosphorylation site |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251264 |
Tyr787 |
LTPSPKSyENLWFQA |
in vitro |
|
| pmid |
sentence |
| 9790917 |
Hck becomes activated upon G-CSF treatment and is, in turn, able to phosphorylate the G-CSF-R, indicating a clear functional and physical involvement in G-CSF signaling. the ability of Hck to phosphorylate the G-CSF-R in vitro, both Y728 and Y763 fit the Src consensus phosphorylation site. we investigated the activation of Hck by the G-CSF-R in intact cells as well as in vitro. These studies revealed recruitment of Hck to activated G-CSF-R, mediated by direct binding via its SH2 domain to multiple phosphotyrosines of the receptor. In addition, we show that Hck becomes activated upon G-CSF treatment and is, in turn, able to phosphorylate the G-CSF-R, indicating a clear functional and physical involvement in G-CSF signaling. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
HCK | up-regulates activity
phosphorylation
|
PLCG2 |
0.526 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249363 |
Tyr753 |
ERDINSLyDVSRMYV |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249364 |
Tyr759 |
LYDVSRMyVDPSEIN |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
HCK |
phosphorylation
|
CBL |
0.648 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251262 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 10092522 |
Hck is one member of the Src-family PTKs that is able to phosphorylate Cbl. Upon enzymatic activation of Hck either by pharmacological agents or genetic mutation, Cbl becomes tyrosine phosphorylated. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
GNAS | up-regulates activity
binding
|
HCK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256529 |
|
|
in vitro |
|
| pmid |
sentence |
| 11007482 |
Galphas and Galphai similarly modulate Hck, another member of Src-family tyrosine kinases. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
GNAI1 | up-regulates activity
binding
|
HCK |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256528 |
|
|
in vitro |
|
| pmid |
sentence |
| 11007482 |
Galphas and Galphai similarly modulate Hck, another member of Src-family tyrosine kinases. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
HCK
- 
- 