| + |
NTRK1 | up-regulates activity 
phosphorylation
|
SHC3 (isoform 2) |
0.768 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273913 |
Tyr218 |
GDGSDHPyYNSIPSK |
in vitro |
|
| pmid |
sentence |
| 11791173 |
We also obtained tryptic phosphopeptide maps of N-Shc protein phosphorylated in vitro by other tyrosine kinases, TrkB, v-Src and EGFR. The overall patterns of the phosphopeptide maps generated by these tyrosine kinases were similar, although there were some differences among these maps (Figure 4a–d).We performed phosphopeptide mapping analysis using GST-fused N-Shc protein, and found that N-Shc phosphorylated by TrkA in vitro was resolved into at least seven phosphopeptides (Y1 through Y7, Figure 4a). Phosphopeptide mapping revealed that N-Shc has novel tyrosine-phosphorylation sites at Y259/Y260 and Y286; in vivo-phosphorylation of these tyrosines was demonstrated by site-specific anti-pTyr antibodies. Phosphorylated Y286 bound to several proteins, of which one was Crk. The pY221/pY222 site, corresponding to one of the Grb2-binding sites of Shc, also preferentially bound to Crk. The phosphorylation-dependent interaction between N-Shc and Crk was demonstrated in vitro and in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273915 |
Tyr219 |
DGSDHPYyNSIPSKM |
in vitro |
|
| pmid |
sentence |
| 11791173 |
We also obtained tryptic phosphopeptide maps of N-Shc protein phosphorylated in vitro by other tyrosine kinases, TrkB, v-Src and EGFR. The overall patterns of the phosphopeptide maps generated by these tyrosine kinases were similar, although there were some differences among these maps (Figure 4a–d).We performed phosphopeptide mapping analysis using GST-fused N-Shc protein, and found that N-Shc phosphorylated by TrkA in vitro was resolved into at least seven phosphopeptides (Y1 through Y7, Figure 4a). Phosphopeptide mapping revealed that N-Shc has novel tyrosine-phosphorylation sites at Y259/Y260 and Y286; in vivo-phosphorylation of these tyrosines was demonstrated by site-specific anti-pTyr antibodies. Phosphorylated Y286 bound to several proteins, of which one was Crk. The pY221/pY222 site, corresponding to one of the Grb2-binding sites of Shc, also preferentially bound to Crk. The phosphorylation-dependent interaction between N-Shc and Crk was demonstrated in vitro and in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273914 |
Tyr283 |
RQGSSDIySTPEGKL |
in vitro |
|
| pmid |
sentence |
| 11791173 |
We also obtained tryptic phosphopeptide maps of N-Shc protein phosphorylated in vitro by other tyrosine kinases, TrkB, v-Src and EGFR. The overall patterns of the phosphopeptide maps generated by these tyrosine kinases were similar, although there were some differences among these maps (Figure 4a–d).We performed phosphopeptide mapping analysis using GST-fused N-Shc protein, and found that N-Shc phosphorylated by TrkA in vitro was resolved into at least seven phosphopeptides (Y1 through Y7, Figure 4a). Phosphopeptide mapping revealed that N-Shc has novel tyrosine-phosphorylation sites at Y259/Y260 and Y286; in vivo-phosphorylation of these tyrosines was demonstrated by site-specific anti-pTyr antibodies. Phosphorylated Y286 bound to several proteins, of which one was Crk. The pY221/pY222 site, corresponding to one of the Grb2-binding sites of Shc, also preferentially bound to Crk. The phosphorylation-dependent interaction between N-Shc and Crk was demonstrated in vitro and in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273923 |
Tyr301 |
PTGEAPTyVNTQQIP |
in vitro |
|
| pmid |
sentence |
| 11791173 |
We also obtained tryptic phosphopeptide maps of N-Shc protein phosphorylated in vitro by other tyrosine kinases, TrkB, v-Src and EGFR. The overall patterns of the phosphopeptide maps generated by these tyrosine kinases were similar, although there were some differences among these maps (Figure 4a–d).We performed phosphopeptide mapping analysis using GST-fused N-Shc protein, and found that N-Shc phosphorylated by TrkA in vitro was resolved into at least seven phosphopeptides (Y1 through Y7, Figure 4a). Phosphopeptide mapping revealed that N-Shc has novel tyrosine-phosphorylation sites at Y259/Y260 and Y286; in vivo-phosphorylation of these tyrosines was demonstrated by site-specific anti-pTyr antibodies. Phosphorylated Y286 bound to several proteins, of which one was Crk. The pY221/pY222 site, corresponding to one of the Grb2-binding sites of Shc, also preferentially bound to Crk. The phosphorylation-dependent interaction between N-Shc and Crk was demonstrated in vitro and in vivo. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
NTRK1 | up-regulates
phosphorylation
|
NTRK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47167 |
Tyr496 |
HIIENPQyFSDACVH |
Homo sapiens |
|
| pmid |
sentence |
| 9099755 |
In vitro studies indicate that trka autophosphorylates at tyrosines 490, 670, 674, 675, and 785 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47171 |
Tyr676 |
FGMSRDIySTDYYRV |
Homo sapiens |
|
| pmid |
sentence |
| 9099755 |
In vitro studies indicate that trka autophosphorylates at tyrosines 490, 670, 674, 675, and 785 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47175 |
Tyr680 |
RDIYSTDyYRVGGRT |
Homo sapiens |
|
| pmid |
sentence |
| 9099755 |
In vitro studies indicate that trka autophosphorylates at tyrosines 490, 670, 674, 675, and 785 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47179 |
Tyr681 |
DIYSTDYyRVGGRTM |
Homo sapiens |
|
| pmid |
sentence |
| 9099755 |
In vitro studies indicate that trka autophosphorylates at tyrosines 490, 670, 674, 675, and 785 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47183 |
Tyr791 |
LAQAPPVyLDVLG |
Homo sapiens |
|
| pmid |
sentence |
| 9099755 |
In vitro studies indicate that trka autophosphorylates at tyrosines 490, 670, 674, 675, and 785 |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates activity 
dephosphorylation
|
NTRK1 |
0.489 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248468 |
Tyr680 |
RDIYSTDyYRVGGRT |
Rattus norvegicus |
|
| pmid |
sentence |
| 14662744 |
Here, we identify SHP-1 as a phosphotyrosine phosphatase that negatively regulates TrkA. SHP-1 formed complexes with TrkA at Y490, and dephosphorylated it at Y674/675. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248469 |
Tyr681 |
DIYSTDYyRVGGRTM |
Rattus norvegicus |
|
| pmid |
sentence |
| 14662744 |
Here, we identify SHP-1 as a phosphotyrosine phosphatase that negatively regulates TrkA. SHP-1 formed complexes with TrkA at Y490, and dephosphorylated it at Y674/675. |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
NTRK1 | up-regulates
phosphorylation
|
SH2B2 |
0.531 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-62619 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9856458 |
Two substrates of trk kinases, raps and sh2-b. raps and sh2-b mediate trk signaling in developing neurons |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
regorafenib | down-regulates activity
chemical inhibition
|
NTRK1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259212 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24756792 |
In biochemical in vitro or cell-based assays, Regorafenib or its major human active metabolites M-2 and M-5 inhibited the activity of RET,VEGFR 1-3, KIT, PDGFR-alpha, PDGFR-beta, FGFR1, FGFR2, TIE2, DDR2, TrkA, Eph2A, RAF-1, BRAF, BRAFV600E, SAPK2, PTK5, and Abl at concentrations that can be achieved clinically. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
anthra[1,9-cd]pyrazol-6(2H)-one | down-regulates
chemical inhibition
|
NTRK1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170617 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21159646 |
In comparison, in the same assay conditions, the previously reported mps1 inhibitor sp600125 (13) was 10-fold less potent than nms-p715 on mps1 and, in addition, it was highly unspecific, being more active on at least 12 kinases including mitotic kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NTRK1 | up-regulates
binding, phosphorylation
|
PLCG1 |
0.637 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75405 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 10708759 |
Autophosphorylated trka binds directly to plc?, Abl, and shc. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-38538 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8384556 |
The nerve growth factor (ngf) receptor/trk associated with and phosphorylated phospholipase c gamma (plc gamma) |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
NGF | up-regulates
binding
|
NTRK1 |
0.955 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85114 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11114882 |
Ngf is the preferred ligand for trka, bdnf and nt4/5 are preferred for trkb, and nt3 for trkc (barbacid 1994). These specificities are not absolute, and nt3 is also a ligand for trka and trkb. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NTRK1 | up-regulates
binding
|
ABL1 |
0.515 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75402 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10708759 |
Autophosphorylated trka binds directly to plc?, Abl, and shc. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NTF4 | up-regulates
binding
|
NTRK1 |
0.693 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85117 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11114882 |
Ngf is the preferred ligand for trka, bdnf and nt4/5 are preferred for trkb, and nt3 for trkc (barbacid 1994). These specificities are not absolute, and nt3 is also a ligand for trka and trkb. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NTRK1 | up-regulates
binding
|
SHC1 |
0.837 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75408 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 10708759 |
Autophosphorylated trka binds directly to plc?, Abl, and shc. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NTRK1 | up-regulates
relocalization
|
ARHGAP32 |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95809 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12446789 |
Grit translocation was regulated by receptor stimulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP26 | down-regulates activity
dephosphorylation
|
NTRK1 |
0.379 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277105 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28701747 |
NEAP and DUSP26 dephosphorylated TrkA and FGFR1 directly.|We found that NEAP, but not its phosphatase-defective mutant, suppressed nerve growth factor (NGF) receptor TrkA and fibroblast growth factor receptor 1 (FGFR1) activation in PC12 cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAB7A | down-regulates activity
binding
|
NTRK1 |
0.485 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261305 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 16306406 |
Endogenous TrkA and Rab7 form a complex. Inhibition of Rab7 potentiates the signaling of TrkA in response to brief stimulations with NGF |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PTPN1 | down-regulates activity
dephosphorylation
|
NTRK1 |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277081 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28919207 |
PTP1B inactivation prevents TrkA exit from soma and causes receptor degradation, suggesting a " gate-keeper " mechanism that ensures targeting of inactive receptors to axons to engage with ligand.|We identify a gate keeping mechanism in which TrkA receptors, destined for transcytosis, are dephosphorylated in neuronal soma by the ER-resident tyrosine phosphatase, PTP1B. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LSM-1231 | down-regulates activity
chemical inhibition
|
NTRK1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258238 |
|
|
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 |
| + |
NTRK1 | up-regulates
binding
|
SH2B1 |
0.523 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124198 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15082760 |
The adapter protein sh2-b has been shown to bind to activated nerve growth factor (ngf) receptor trka and has been implicated in ngf-induced neuronal differentiation and the survival of sympathetic neurons. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NTRK1 | up-regulates
binding
|
FRS2 |
0.769 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-65955 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10092678 |
The signaling adapter frs-2 competes with shc for binding to the nerve growth factor receptor trka:a model for discriminating proliferation and differentiation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
NTRK1
- 
- 