| + |
PRKCA | down-regulates 
phosphorylation
|
MET |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37718 |
Ser985 |
PHLDRLVsARSVSPT |
Homo sapiens |
|
| pmid |
sentence |
| 8294430 |
These data show that phosphorylation of ser985 is a key mechanism for the negative regulation of hgf/sf receptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRG | down-regulates activity
dephosphorylation
|
MET |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254712 |
Tyr1003 |
VSNESVDyRATFPED |
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 |
| + |
PTPN1 | down-regulates
dephosphorylation
|
MET |
0.617 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145141 |
Tyr1234 |
RDMYDKEyYSVHNKT |
Homo sapiens |
|
| pmid |
sentence |
| 16537444 |
Using substrate trapping mutants of ptp1b or tcptp, we have demonstrated that both phosphatases interact with met and that these interactions require phosphorylation of twin tyrosines (tyr-1234/1235) in the activation loop of the met kinase domain. We demonstrate that phosphorylation of tyr-1234/1235 in the activation loop of the met receptor is elevated in the absence of either ptp1b or tcptp and further elevated upon loss of both phosphatases. This enhanced phosphorylation of met corresponds to enhanced biological activity and cellular invasion. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181323 |
Tyr1234 |
RDMYDKEyYSVHNKT |
Homo sapiens |
|
| pmid |
sentence |
| 18819921 |
Using substrate trapping mutants of ptp1b or tcptp, we have demonstrated that both phosphatases interact with met and that these interactions require phosphorylation of twin tyrosines (tyr-1234/1235) in the activation loop of the met kinase domain. We demonstrate that phosphorylation of tyr-1234/1235 in the activation loop of the met receptor is elevated in the absence of either ptp1b or tcptp and further elevated upon loss of both phosphatases. This enhanced phosphorylation of met corresponds to enhanced biological activity and cellular invasion. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145145 |
Tyr1235 |
DMYDKEYySVHNKTG |
Homo sapiens |
|
| pmid |
sentence |
| 16537444 |
Using substrate trapping mutants of ptp1b or tcptp, we have demonstrated that both phosphatases interact with met and that these interactions require phosphorylation of twin tyrosines (tyr-1234/1235) in the activation loop of the met kinase domain. We demonstrate that phosphorylation of tyr-1234/1235 in the activation loop of the met receptor is elevated in the absence of either ptp1b or tcptp and further elevated upon loss of both phosphatases. This enhanced phosphorylation of met corresponds to enhanced biological activity and cellular invasion. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181327 |
Tyr1235 |
DMYDKEYySVHNKTG |
Homo sapiens |
|
| pmid |
sentence |
| 18819921 |
Using substrate trapping mutants of ptp1b or tcptp, we have demonstrated that both phosphatases interact with met and that these interactions require phosphorylation of twin tyrosines (tyr-1234/1235) in the activation loop of the met kinase domain. We demonstrate that phosphorylation of tyr-1234/1235 in the activation loop of the met receptor is elevated in the absence of either ptp1b or tcptp and further elevated upon loss of both phosphatases. This enhanced phosphorylation of met corresponds to enhanced biological activity and cellular invasion. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates
dephosphorylation
|
MET |
0.473 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181331 |
Tyr1234 |
RDMYDKEyYSVHNKT |
Homo sapiens |
|
| pmid |
sentence |
| 18819921 |
We have identified ptp1b and tcptp as negative regulators of the hepatocyte growth factor receptor, the met receptor-tyrosine kinase. In vivo, loss of ptp1b or tcptp enhances hepatocyte growth factor-mediated phosphorylation of met. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181335 |
Tyr1235 |
DMYDKEYySVHNKTG |
Homo sapiens |
|
| pmid |
sentence |
| 18819921 |
We have identified ptp1b and tcptp as negative regulators of the hepatocyte growth factor receptor, the met receptor-tyrosine kinase. In vivo, loss of ptp1b or tcptp enhances hepatocyte growth factor-mediated phosphorylation of met. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN1 | down-regulates activity
dephosphorylation
|
MET |
0.617 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248411 |
Tyr1234 |
RDMYDKEyYSVHNKT |
Homo sapiens |
|
| pmid |
sentence |
| 18819921 |
Using substrate trapping mutants of PTP1B or TCPTP, we have demonstrated that both phosphatases interact with Met and that these interactions require phosphorylation of twin tyrosines (Tyr-1234/1235) in the activation loop of the Met kinase domain.|Using small interfering RNA against PTP1B and TCPTP, we demonstrate that phosphorylation of Tyr-1234/1235 in the activation loop of the Met receptor is elevated in the absence of either PTP1B or TCPTP and further elevated upon loss of both phosphatases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248412 |
Tyr1235 |
DMYDKEYySVHNKTG |
Homo sapiens |
|
| pmid |
sentence |
| 18819921 |
Using substrate trapping mutants of PTP1B or TCPTP, we have demonstrated that both phosphatases interact with Met and that these interactions require phosphorylation of twin tyrosines (Tyr-1234/1235) in the activation loop of the Met kinase domain.|Using small interfering RNA against PTP1B and TCPTP, we demonstrate that phosphorylation of Tyr-1234/1235 in the activation loop of the Met receptor is elevated in the absence of either PTP1B or TCPTP and further elevated upon loss of both phosphatases. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MET | up-regulates 
phosphorylation
|
MET |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37723 |
Tyr1234 |
RDMYDKEyYSVHNKT |
Homo sapiens |
|
| pmid |
sentence |
| 8302603 |
Previous work has shown that autophosphorylation of p190met enhances its enzymatic activity and that the major phosphorylation site is tyr1235, located in the catalytic domainonly the replacement of both tyr1234 and tyr1235 yielded a mutant which completely lost the ability to be activated by autophosphorylation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37727 |
Tyr1235 |
DMYDKEYySVHNKTG |
Homo sapiens |
|
| pmid |
sentence |
| 8302603 |
Previous work has shown that autophosphorylation of p190met enhances its enzymatic activity and that the major phosphorylation site is tyr1235, located in the catalytic domainonly the replacement of both tyr1234 and tyr1235 yielded a mutant which completely lost the ability to be activated by autophosphorylation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Hepatocellular Tumor, Prostate Cancer, Rhabdomyosarcoma |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
MET |
0.473 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248387 |
Tyr1234 |
RDMYDKEyYSVHNKT |
Homo sapiens |
|
| pmid |
sentence |
| 18819921 |
Using substrate trapping mutants of PTP1B or TCPTP, we have demonstrated that both phosphatases interact with Met and that these interactions require phosphorylation of twin tyrosines (Tyr-1234/1235) in the activation loop of the Met kinase domain.|Using small interfering RNA against PTP1B and TCPTP, we demonstrate that phosphorylation of Tyr-1234/1235 in the activation loop of the Met receptor is elevated in the absence of either PTP1B or TCPTP and further elevated upon loss of both phosphatases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248388 |
Tyr1235 |
DMYDKEYySVHNKTG |
Homo sapiens |
|
| pmid |
sentence |
| 18819921 |
Using substrate trapping mutants of PTP1B or TCPTP, we have demonstrated that both phosphatases interact with Met and that these interactions require phosphorylation of twin tyrosines (Tyr-1234/1235) in the activation loop of the Met kinase domain.|Using small interfering RNA against PTP1B and TCPTP, we demonstrate that phosphorylation of Tyr-1234/1235 in the activation loop of the Met receptor is elevated in the absence of either PTP1B or TCPTP and further elevated upon loss of both phosphatases. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
MET |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248702 |
Tyr1349 |
STFIGEHyVHVNATY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12475979 |
When co-expressed in 293 cells, the full-length substrate-trapping mutant form of DEP-1 formed a stable complex with the chimeric receptor colony stimulating factor 1 (CSF)-Met and wild type DEP-1 dephosphorylated CSF-Met. Furthermore, we observed that DEP-1 preferentially dephosphorylated a Gab1 binding site (Tyr(1349)) and a COOH-terminal tyrosine implicated in morphogenesis (Tyr(1365)), |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248703 |
Tyr1365 |
NVKCVAPyPSLLSSE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12475979 |
When co-expressed in 293 cells, the full-length substrate-trapping mutant form of DEP-1 formed a stable complex with the chimeric receptor colony stimulating factor 1 (CSF)-Met and wild type DEP-1 dephosphorylated CSF-Met. Furthermore, we observed that DEP-1 preferentially dephosphorylated a Gab1 binding site (Tyr(1349)) and a COOH-terminal tyrosine implicated in morphogenesis (Tyr(1365)), |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRB | down-regulates
dephosphorylation
|
MET |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139560 |
Tyr1356 |
YVHVNATyVNVKCVA |
Homo sapiens |
|
| pmid |
sentence |
| 16101282 |
Ptp1b and shp-2 are bound to the c-met receptor to control its activity. Although the binding of ptp1b increases when there is a decrease in c-met activation and acts as a negative regulator of the receptor, the increased binding and phosphorylation of shp-2 coincide with maximal stimulation of c-met, acting as a positive regulator. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173004 |
Tyr1356 |
YVHVNATyVNVKCVA |
Homo sapiens |
|
| pmid |
sentence |
| 21454675 |
Receptor-type protein tyrosine phosphatase beta (rptp-beta) directly dephosphorylates and regulates hepatocyte growth factor receptor (hgfr/met) function. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRB | down-regulates activity
dephosphorylation
|
MET |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248440 |
Tyr1356 |
YVHVNATyVNVKCVA |
Homo sapiens |
|
| pmid |
sentence |
| 21454675 |
Receptor-type protein tyrosine phosphatase beta (RPTP-beta) directly dephosphorylates and regulates hepatocyte growth factor receptor (HGFR/Met) function.|Expression of RPTP-β in primary human keratinocytes reduces both basal and HGF-induced Met phosphorylation at tyrosine 1356 and inhibits downstream MEK1/2 and Erk activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates
dephosphorylation
|
MET |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96347 |
Tyr1365 |
NVKCVAPyPSLLSSE |
Homo sapiens |
Breast Cancer Cell, Lung Cancer Cell |
| pmid |
sentence |
| 12475979 |
Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase dep-1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MET | up-regulates
phosphorylation
|
PTK2 |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147179 |
Tyr194 |
ALEKKSNyEVLEKDV |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Here we report that fak directly interacts with the hepatocyte growth factor receptor c-met. Phosphorylation of c-met at tyr-1349 and, to a lesser extent, tyr-1356 is required for its interaction with the band 4.1 and ezrin/radixin/moesin homology domain (ferm domain) of fak. met-fak interaction leads to fak activation and subsequent contribution to hepatocyte growth factor-induced cell motility and cell invasion. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167654 |
Tyr194 |
ALEKKSNyEVLEKDV |
Homo sapiens |
|
| pmid |
sentence |
| 20802513 |
In this study, we demonstrate that growth factor receptors including hepatocyte growth factor receptor met, epidermal growth factor receptor, and platelet-derived growth factor receptor directly phosphorylate fak on tyr194 in the ferm domain (band 4.1 and ezrin/radixin/moesin homology domain). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147183 |
Tyr397 |
SVSETDDyAEIIDEE |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Met-mediated fak phosphorylation could further activate fak. Indeed, we found that met phosphorylates fak at its known phosphorylation sites, including tyr-576 and tyr-577, both of which are located in the activating loop within the catalytic domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147187 |
Tyr407 |
IIDEEDTyTMPSTRD |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Met-mediated fak phosphorylation could further activate fak. Indeed, we found that met phosphorylates fak at its known phosphorylation sites, including tyr-576 and tyr-577, both of which are located in the activating loop within the catalytic domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147191 |
Tyr576 |
RYMEDSTyYKASKGK |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Met-mediated fak phosphorylation could further activate fak. Indeed, we found that met phosphorylates fak at its known phosphorylation sites, including tyr-576 and tyr-577, both of which are located in the activating loop within the catalytic domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147195 |
Tyr577 |
YMEDSTYyKASKGKL |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Met-mediated fak phosphorylation could further activate fak. Indeed, we found that met phosphorylates fak at its known phosphorylation sites, including tyr-576 and tyr-577, both of which are located in the activating loop within the catalytic domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147199 |
Tyr861 |
PIGNQHIyQPVGKPD |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Met-mediated fak phosphorylation could further activate fak. Indeed, we found that met phosphorylates fak at its known phosphorylation sites, including tyr-576 and tyr-577, both of which are located in the activating loop within the catalytic domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147203 |
Tyr925 |
DRSNDKVyENVTGLV |
Homo sapiens |
|
| pmid |
sentence |
| 16782899 |
Met-mediated fak phosphorylation could further activate fak. Indeed, we found that met phosphorylates fak at its known phosphorylation sites, including tyr-576 and tyr-577, both of which are located in the activating loop within the catalytic domain |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| + |
MET | up-regulates activity
phosphorylation
|
GAB1 |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250552 |
Tyr285 |
TEADGELyVFNTPSG |
Homo sapiens |
A-549 Cell |
| pmid |
sentence |
| 10734310 |
Gab-1 is phosphorylated on the same residues by HGF and EGF receptors. Among 16 peptides only nine were phosphorylated by the EGF and HGF receptors, namely peptides containing the tyrosine residues 285, 307, 373, 407, 448, 473, 590, 628 and 660. we show that in the response to HGF or EGF, Gab1 is phosphorylated in vivo on the same residues. However, a sustained activation of signaling pathways downstream to Gab1 (as a result of its sustained phosphorylation) is achieved only in response to HGF. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250288 |
Tyr589 |
SHDSEENyVPMNPNL |
Homo sapiens |
A-549 Cell |
| pmid |
sentence |
| 10734310 |
Gab-1 is phosphorylated on the same residues by HGF and EGF receptors. Among 16 peptides only nine were phosphorylated by the EGF and HGF receptors, namely peptides containing the tyrosine residues 285, 307, 373, 407, 448, 473, 590, 628 and 660. we show that in the response to HGF or EGF, Gab1 is phosphorylated in vivo on the same residues. However, a sustained activation of signaling pathways downstream to Gab1 (as a result of its sustained phosphorylation) is achieved only in response to HGF. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250289 |
Tyr627 |
KGDKQVEyLDLDLDS |
Homo sapiens |
A-549 Cell |
| pmid |
sentence |
| 10734310 |
Gab-1 is phosphorylated on the same residues by HGF and EGF receptors. Among 16 peptides only nine were phosphorylated by the EGF and HGF receptors, namely peptides containing the tyrosine residues 285, 307, 373, 407, 448, 473, 590, 628 and 660. we show that in the response to HGF or EGF, Gab1 is phosphorylated in vivo on the same residues. However, a sustained activation of signaling pathways downstream to Gab1 (as a result of its sustained phosphorylation) is achieved only in response to HGF. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250290 |
Tyr659 |
VADERVDyVVVDQQK |
Homo sapiens |
A-549 Cell |
| pmid |
sentence |
| 10734310 |
Gab-1 is phosphorylated on the same residues by HGF and EGF receptors. Among 16 peptides only nine were phosphorylated by the EGF and HGF receptors, namely peptides containing the tyrosine residues 285, 307, 373, 407, 448, 473, 590, 628 and 660. we show that in the response to HGF or EGF, Gab1 is phosphorylated in vivo on the same residues. However, a sustained activation of signaling pathways downstream to Gab1 (as a result of its sustained phosphorylation) is achieved only in response to HGF. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | Hepatocellular Tumor, Rhabdomyosarcoma |
| + |
N-[[3-fluoro-4-[[2-(1-methyl-4-imidazolyl)-7-thieno[3,2-b]pyridinyl]oxy]anilino]-sulfanylidenemethyl]-2-phenylacetamide | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194343 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MACC1 | up-regulates quantity by expression
transcriptional regulation
|
MET |
0.41 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266058 |
|
|
Homo sapiens |
SW-480 Cell |
| pmid |
sentence |
| 19098908 |
Human colon carcinoma SW480 cells express virtually no MACC1. MACC1 cDNA transfection led not only to strong increases in MACC1 mRNA expression (Fig. 3a), but also to a 40-fold upregulation of the HGF receptor MET mRNA expression (Fig. 3b). This was confirmed on the protein level |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGX-523 | down-regulates activity
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258282 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PHA-665752 | down-regulates activity
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258265 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PAX7-FOXO1 | up-regulates quantity by expression
transcriptional regulation
|
MET |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251566 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25211658 |
Several deregulated signalling pathways enhance cell growth by modulating cell-cycle regulatory factors in RMS. The most frequently affected signalling pathways include the insulin-like growth factor (IGF), fibroblast growth factor (FGF), hepatocyte growth factor, and platelet-derived growth factor. In ARMS, PAX-FOXO1 activates these pathways by transcriptional activation of receptor genes including IGFR1, FGFR4, MET (c-Met), and PDGFRA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HGF | up-regulates
binding
|
MET |
0.927 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-38429 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8380735 |
Hgf is the ligand for p190met, the receptor tyrosine kinase encoded by the met proto-oncogene. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Hepatocellular Tumor, Prostate Cancer, Rhabdomyosarcoma |
| + |
N1'-[3-fluoro-4-[[6-methoxy-7-[3-(4-morpholinyl)propoxy]-4-quinolinyl]oxy]phenyl]-N1-(4-fluorophenyl)cyclopropane-1,1-dicarboxamide | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174555 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 21697284 |
Cocrystallization of the met kinase domain in complex with nvp-bvu972 revealed a key role for y1230 in binding of nvp-bvu972, as previously reported for multiple other selective met inhibitors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SP1 | up-regulates quantity by expression
transcriptional regulation
|
MET |
0.328 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241490 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 9223667 |
Furthermore, in transient cotransfection assays, overexpression of Sp1 and/or Sp3 stimulated HGF promoter activity independently and additively through binding to the Sp1 binding site in the HGF gene promoter region. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PHA-665752 | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206088 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MET | up-regulates
binding
|
GRAP |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-42358 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8662889 |
To efficiently promote transformation met requires direct binding with grb2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MET | up-regulates 
|
Metastasis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263658 |
|
|
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 22035268 |
C-Met expression and activation appears to be one of the common mechanisms of resistance to other targeted therapies. Given these multiple roles of c-Met in prostate cancer, several c-Met inhibitors have been developed. Evidence to date suggests that aberrant activation of the HGF/c-Met axis in prostate cancer epithelial cells appears to be a relatively late event in tumor progression. C-Met expression increases in advanced stages of the disease, with the highest expression observed in bone metastases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Prostate Cancer |
| + |
MK-2461 | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194384 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
6-[difluoro-[6-(1-methyl-4-pyrazolyl)-[1,2,4]triazolo[4,3-b]pyridazin-3-yl]methyl]quinoline | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193522 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMG-208 | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189507 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HOTAIR | down-regulates 
|
MET |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272090 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32650779 |
LncRNA HOTAIR overexpression induced downregulation of c-Met signaling promotes hybrid epithelial/mesenchymal phenotype in hepatocellular carcinoma cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
cabozantinib | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207845 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGX-523 | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206905 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LSM-1131 | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189873 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NME1 | down-regulates quantity by repression
transcriptional regulation
|
MET |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255164 |
|
|
Homo sapiens |
MDA-MB-435 Cell |
| pmid |
sentence |
| 17671192 |
To elucidate the molecular mechanism of Nm23-H1 motility suppression, expression microarray analysis of an MDA-MB-435 cancer cell line overexpressing wild-type Nm23-H1 was done and cross-compared with expression profiles from lines expressing the P96S and S120G mutants. Nine genes, MET, PTN, SMO, FZD1, L1CAM, MMP2, NETO2, CTGF, and EDG2, were down-regulated by wild-type but not by mutant Nm23-H1 expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MET | up-regulates activity
binding
|
GRB2 |
0.68 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256261 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22128289 |
For activation of the mitogen-activated protein kinase (MAPK) cascades, c-MET activation stimulates the activity of the rat sarcoma viral oncogene homolog (RAS) guanine nucleotide exchanger son of sevenless (SOS) via binding with SHC and GRB2 leading to the activation of RAS. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Hepatocellular Tumor, Rhabdomyosarcoma |
| + |
MECP2 | down-regulates quantity by repression
post transcriptional regulation
|
MET |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264683 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24150225 |
MeCP2 binding enhances MET expression in the presence of the rs1858830 C allele, but MET transcription is attenuated by RTT-specific mutations in MeCP2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MET | down-regulates
relocalization
|
GLMN |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110726 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11571281 |
Significantly, nonphosphorylated hgf receptor prevents fap68 from stimulating p70s6k. fap68 binding to met requires the last 30 amino acids of the c-terminal tail, which are unique to the hgf receptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CBL | down-regulates quantity by destabilization
ubiquitination
|
MET |
0.716 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185680 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19450681 |
Tyrosine y1001, which when phosphorylated upon met activation, is involved in cbl recruitment, allowing receptor ubiquitination and down regulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAX3-FOXO1 | up-regulates quantity by expression
transcriptional regulation
|
MET |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251570 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25211658 |
Several deregulated signalling pathways enhance cell growth by modulating cell-cycle regulatory factors in RMS. The most frequently affected signalling pathways include the insulin-like growth factor (IGF), fibroblast growth factor (FGF), hepatocyte growth factor, and platelet-derived growth factor. In ARMS, PAX-FOXO1 activates these pathways by transcriptional activation of receptor genes including IGFR1, FGFR4, MET (c-Met), and PDGFRA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-[4-[(2-amino-3-chloro-4-pyridinyl)oxy]-3-fluorophenyl]-4-ethoxy-1-(4-fluorophenyl)-2-oxo-3-pyridinecarboxamide | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190404 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RELA | up-regulates quantity
transcriptional regulation
|
MET |
0.254 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241929 |
|
|
Mus musculus |
HEPA 1-6 Cell |
| pmid |
sentence |
| 19530226 |
Together, these results indicate that the Met gene is a direct target of NFkappaB and that Met participates in NFkappaB-mediated cell survival. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MET | up-regulates
binding
|
RANBP9 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91028 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12147692 |
Our data suggest that ranbpm, functioning as an adaptor protein for the met tyrosine kinase domain, can augment the hgf-met signaling pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
crizotinib | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191136 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
2-[4-[3-(6-quinolinylmethyl)-5-triazolo[4,5-b]pyrazinyl]-1-pyrazolyl]ethanol | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205968 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOXP2 | down-regulates quantity by repression
transcriptional regulation
|
MET |
0.432 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269054 |
|
|
Homo sapiens |
Neural Stem Cell |
| pmid |
sentence |
| 21832174 |
FOXP2 binds directly to the 5' regulatory region of MET, and overexpression of FOXP2 results in transcriptional repression of MET. The expression of MET in restricted human neocortical regions, and its regulation in part by FOXP2, is consistent with genetic evidence for MET contributing to ASD risk. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SU11274 | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207123 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMG 458 | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189516 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
crizotinib | down-regulates activity
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258102 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
NVP-BVU972 | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194943 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
USP8 | down-regulates quantity
destabilization
|
MET |
0.428 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266903 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16520378 |
Degradation of acutely stimulated receptor tyrosine kinases, epidermal growth factor receptor and Met, is strongly inhibited in UBPY knockdown cells suggesting that UBPY function is essential for growth factor receptor down-regulation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMS 794833 | down-regulates
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190422 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N1'-[3-fluoro-4-[[6-methoxy-7-[3-(4-morpholinyl)propoxy]-4-quinolinyl]oxy]phenyl]-N1-(4-fluorophenyl)cyclopropane-1,1-dicarboxamide | down-regulates activity
chemical inhibition
|
MET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258214 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
MET
- 
- 