| + |
BMX | up-regulates quantity 
phosphorylation
|
BCAR1 |
0.52 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276384 |
Tyr12 |
NVLAKALyDNVAESP |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 21937722 |
Recombinant Bmx kinase was found to effectively phosphorylate the wt CAS SH3 domain on Tyr-12 (Figure 2B). A novel phosphorylation site on CAS, Tyr-12 (Y12) within the ligand-binding hydrophobic pocket of the CAS SH3 domain, was identified and found to be enriched in Src-transformed cells and invasive human carcinoma cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ITK | up-regulates activity
phosphorylation
|
BMX |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251331 |
Tyr216 |
SSTSLAQyDSNSKKI |
in vitro |
|
| pmid |
sentence |
| 12573241 |
Itk phosphorylated Bmx-SH3 to a low extent. pY positions correspond to the residues Y215 and Y223 in Bmx. Tec family protein tyrosine kinases (TFKs) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251332 |
Tyr224 |
DSNSKKIyGSQPNFN |
in vitro |
|
| pmid |
sentence |
| 12573241 |
Itk phosphorylated Bmx-SH3 to a low extent. pY positions correspond to the residues Y215 and Y223 in Bmx. Tec family protein tyrosine kinases (TFKs) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
TEC | up-regulates activity
phosphorylation
|
BMX |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246647 |
Tyr216 |
SSTSLAQyDSNSKKI |
Homo sapiens |
MOLT-4 Cell |
| pmid |
sentence |
| 12573241 |
Tec family protein tyrosine kinases (TFKs) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop.The major phosphorylation sites were identified as conserved tyrosines, for Itk Y180 and for Bmx Y215, both sites being homologous to the Y223 site in Btk |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTK | up-regulates
phosphorylation
|
BMX |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98028 |
Tyr216 |
SSTSLAQyDSNSKKI |
Homo sapiens |
|
| pmid |
sentence |
| 12573241 |
Tec family protein tyrosine kinases (tfks) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the sh3 domain via a transphosphorylation mechanism. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98032 |
Tyr224 |
DSNSKKIyGSQPNFN |
Homo sapiens |
|
| pmid |
sentence |
| 12573241 |
Tec family protein tyrosine kinases (tfks) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the sh3 domain via a transphosphorylation mechanism. For bmx, we obtained two phosphorylated sites, y215 and y223 (fig. 6c). The bmx-y215 is a conserved tyrosine, which is homologous to btk-y223 and itk-y180 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
TEC | up-regulates
phosphorylation
|
BMX |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98094 |
Tyr224 |
DSNSKKIyGSQPNFN |
Homo sapiens |
|
| pmid |
sentence |
| 12573241 |
Tec family protein tyrosine kinases (tfks) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the sh3 domain via a transphosphorylation mechanism. For bmx, we obtained two phosphorylated sites, y215 and y223 (fig. 6c). The bmx-y215 is a conserved tyrosine, which is homologous to btk-y223 and itk-y180 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMX | up-regulates activity
phosphorylation
|
RUFY1 |
0.619 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262678 |
Tyr389 |
TKVELETyKQTRQGL |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 11877430 |
Etk interacts with RUFY1 through its SH3 and SH2 domains. RUFY1 is tyrosine-phosphorylated and appears to be a substrate of Etk. Phosphorylation of the two tyrosine residues, Tyr-281 and Tyr-292, located in the linker region of the two coiled-coil domains by Etk seems to be critical for RUFY1 targeting to the endosomes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262679 |
Tyr400 |
RQGLDEMySDVWKQL |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 11877430 |
Etk interacts with RUFY1 through its SH3 and SH2 domains. RUFY1 is tyrosine-phosphorylated and appears to be a substrate of Etk. Phosphorylation of the two tyrosine residues, Tyr-281 and Tyr-292, located in the linker region of the two coiled-coil domains by Etk seems to be critical for RUFY1 targeting to the endosomes. |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
PTPRG | down-regulates activity 
dephosphorylation
|
BMX |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254693 |
Tyr40 |
LTKTNLSyYEYDKMK |
in vitro |
|
| pmid |
sentence |
| 25624455 |
PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SRC | up-regulates
phosphorylation
|
BMX |
0.515 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75330 |
Tyr566 |
RYVLDDQyVSSVGTK |
Homo sapiens |
|
| pmid |
sentence |
| 10688651 |
Coexpression of v-src and etk led to a transphosphorylation on tyrosine 566 of etk and subsequent autophosphorylation. These events correlated with a substantial increase in the kinase activity of etk. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMX | up-regulates
phosphorylation
|
PTK2 |
0.53 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202139 |
Tyr577 |
YMEDSTYyKASKGKL |
Homo sapiens |
|
| pmid |
sentence |
| 23716717 |
Bmx phosphorylated focal adhesion kinase (fak) at tyr577 subsequent to its src-mediated phosphorylation at tyr576. Loss of bmx by rna interference or by genetic deletion in mouse embryonic fibroblasts (mefs) markedly impaired fak activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
9-(1-Methyl-4-pyrazolyl)-1-[1-(1-oxoprop-2-enyl)-2,3-dihydroindol-6-yl]-2-benzo[h][1,6]naphthyridinone | down-regulates activity
chemical inhibition
|
BMX |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262232 |
|
|
in vitro |
|
| pmid |
sentence |
| 24556163 |
This analysis revealed that QL47 also potently inhibits BMX with an IC50 of 6.7 nM but impressively displays more than 100-fold selectivity against EGFR, HER2, JAK3, BLK, TEC, and ITK that possess an equivalently placed cysteine |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
BMX
- 
- 