| + |
NTRK2 | down-regulates 
phosphorylation
|
KCNA3 |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183515 |
Tyr161 |
PSFDAILyYYQSGGR |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19166614 |
Previously we have shown that acute brain-derived neurotrophic factor (bdnf) activation of neurotrophin receptor tyrosine kinase b (trkb) suppresses the shaker voltage-gated potassium channel (kv1.3) via phosphorylation of multiple tyrosine residues in the n and c terminal aspects of the channel protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183519 |
Tyr162 |
SFDAILYyYQSGGRI |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19166614 |
Previously we have shown that acute brain-derived neurotrophic factor (bdnf) activation of neurotrophin receptor tyrosine kinase b (trkb) suppresses the shaker voltage-gated potassium channel (kv1.3) via phosphorylation of multiple tyrosine residues in the n and c terminal aspects of the channel protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183523 |
Tyr163 |
FDAILYYyQSGGRIR |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19166614 |
Previously we have shown that acute brain-derived neurotrophic factor (bdnf) activation of neurotrophin receptor tyrosine kinase b (trkb) suppresses the shaker voltage-gated potassium channel (kv1.3) via phosphorylation of multiple tyrosine residues in the n and c terminal aspects of the channel protein. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
NTRK2 | up-regulates activity 
phosphorylation
|
SHC3 (isoform 2) |
0.741 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273916 |
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-273918 |
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-273917 |
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-273924 |
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 |
| + |
NTRK2 | up-regulates activity
phosphorylation
|
FRS3 |
0.577 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250202 |
Tyr417 |
EPPRQLNyIQVELKG |
Homo sapiens |
|
| pmid |
sentence |
| 11432792 |
The tyrosine phosphoryla tion of FRS2/SNT2 was stimulated dependently on the TrkB activation. to explore the possibility that tyrosine residues 417 and 455 on FRS2/SNT2 function as the binding sites for Shp2, we coexpressed Y417F or Y455F phenylalanine mutants and the Y417/455F double phenylalanine mutant of Myc/Histagged FRS2/SNT2 with TrkB. The active TrkB induced somewhat reduced tyrosine phosphorylation of all of the phenylalanine mutants of FRS2/SNT2 in comparison with tyrosine phosphorylation of the wild type |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250203 |
Tyr455 |
PARSSDSyAVIDLKK |
Homo sapiens |
|
| pmid |
sentence |
| 11432792 |
The tyrosine phosphoryla tion of FRS2/SNT2 was stimulated dependently on the TrkB activation. to explore the possibility that tyrosine residues 417 and 455 on FRS2/SNT2 function as the binding sites for Shp2, we coexpressed Y417F or Y455F phenylalanine mutants and the Y417/455F double phenylalanine mutant of Myc/Histagged FRS2/SNT2 with TrkB. The active TrkB induced somewhat reduced tyrosine phosphorylation of all of the phenylalanine mutants of FRS2/SNT2 in comparison with tyrosine phosphorylation of the wild type |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
NTRK2 | up-regulates activity
phosphorylation
|
NTRK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250204 |
Tyr516 |
PVIENPQyFGITNSQ |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 10533983 |
TrkB autophosphorylation occurs on five cytoplasmic tyrosines: Y484, Y670, Y674, Y675, and Y785. Mutagenesis of Y484 inhibits the interaction between Shc and TrkB, and also block the E3DNF-inducible tyrosine phoslphorylation of Shc |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250205 |
Tyr702 |
FGMSRDVySTDYYRV |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 10533983 |
TrkB autophosphorylation occurs on five cytoplasmic tyrosines: Y484, Y670, Y674, Y675, and Y785. Mutagenesis of Y484 inhibits the interaction between Shc and TrkB, and also block the E3DNF-inducible tyrosine phoslphorylation of Shc |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250312 |
Tyr817 |
LAKASPVyLDILG |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 10533983 |
TrkB autophosphorylation occurs on five cytoplasmic tyrosines: Y484, Y670, Y674, Y675, and Y785. the Y785F mutation abolish the BDNF-inducible tyrosine phosphorylation of PLCy, but receptors containing this mutation are also defective in the ability to induce the tyrosine phosphorylation of the c-cbl proto-oncogene product. |
|
| Publications: |
3 |
Organism: |
Mus Musculus |
| Pathways: | Rett syndrome |
| + |
NTRK2 |
phosphorylation
|
NTRK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250206 |
Tyr706 |
RDVYSTDyYRVGGHT |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 10533983 |
TrkB autophosphorylation occurs on five cytoplasmic tyrosines: Y484, Y670, Y674, Y675, and Y785. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250207 |
Tyr707 |
DVYSTDYyRVGGHTM |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 10533983 |
TrkB autophosphorylation occurs on five cytoplasmic tyrosines: Y484, Y670, Y674, Y675, and Y785. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| Pathways: | Rett syndrome |
| + |
PTPN1 | down-regulates activity
dephosphorylation
|
NTRK2 |
0.388 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264554 |
Tyr706 |
RDVYSTDyYRVGGHT |
Homo sapiens |
SH-SY5Y Cell |
| pmid |
sentence |
| 26214522 |
Collectively, these data establish a direct enzyme-substrate interaction between PTP1B and phosphorylated Y705/706 (p-Y705/706) TRKB, the critical autophosphorylation sites that mediate BDNF-induced signaling.| Therefore, the data are consistent with a role of PTP1B as an inhibitor of BDNF/TRKB signaling |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264553 |
Tyr707 |
DVYSTDYyRVGGHTM |
Homo sapiens |
|
| pmid |
sentence |
| 26214522 |
Collectively, these data establish a direct enzyme-substrate interaction between PTP1B and phosphorylated Y705/706 (p-Y705/706) TRKB, the critical autophosphorylation sites that mediate BDNF-induced signaling.| Therefore, the data are consistent with a role of PTP1B as an inhibitor of BDNF/TRKB signaling |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Rett syndrome |
| + |
NTRK2 | up-regulates
binding
|
FYN |
0.39 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-58424 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9648856 |
All these data suggest the involvement of fyn in the neurotrophin signal transduction pathways downstream of trkb. We investigated whether fyn is involved in the trk-dependent signal transduction pathways of neurotrophin. The fyn-src homology domain 2 (sh2) was observed to associate in vitro with the intracellular domain of trkb (icd-trkb). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NTRK2 | up-regulates
binding
|
NCK2 |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89764 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12074588 |
We identified the nck2 adaptor protein as a novel interaction partner of the active form of trkb. Additionally, we identified three tyrosines in icd-trkb (y694, y695, and y771) that are crucial for this interaction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LSM-1231 | down-regulates activity
chemical inhibition
|
NTRK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258239 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259759 |
|
|
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: |
2 |
Organism: |
In Vitro |
| + |
NTF4 | up-regulates
binding
|
NTRK2 |
0.938 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-31644 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7679912 |
Its interactions with trkb can be distinguished from those of brain-derived neurotrophic factor (bdnf) with trkb. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ASH1L | up-regulates quantity by expression
transcriptional regulation
|
NTRK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269058 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 35210569 |
Depletion of ASH1L decreases neurite outgrowth and decreases expression of the gene encoding the neurotrophin receptor TrkB whose signaling pathway is linked to neuronal morphogenesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NTRK2 | up-regulates
binding
|
SHC3 |
0.741 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-55864 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9507002 |
Our present study established that n-shc and sck are expressed in a region-specific manner in the brain and that n-shc is a higher affinity adapter molecule than sck for trka and trkb receptors |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| Pathways: | Rett syndrome |
| + |
BDNF | up-regulates
binding
|
NTRK2 |
0.812 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-31597 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7679912 |
Its interactions with trkb can be distinguished from those of brain-derived neurotrophic factor (bdnf) with trkb |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Rett syndrome |
| + |
ANKRD11 | up-regulates quantity by expression
transcriptional regulation
|
NTRK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266731 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 29274743 |
Ankrd11 knockdown decreases the levels of bdnf and Trkb mRNAs. Next, we examine whether ANKRD11 accesses the Trkb promoter in cortical neurons. We performed the chromatin immunoprecipitation assay (ChIP) using an ANKRD11 antibody followed by PCR to amplify the Trkb promoter region. We found that ANKRD11 binds to the Trkb promoter (Fig. 6E). As expected, the level of ANKRD11 binding was decreased in the Ankrd11 knockdown condition. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
RORA | up-regulates quantity by expression
transcriptional regulation
|
NTRK2 |
0.271 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265137 |
|
|
|
|
| pmid |
sentence |
| 28608249 |
Some genes which are directly regulated by RORA such as NLGN1 and NTRK2 have been shown to be associated with increased susceptibility to ASD (Correia et al. 2010; Ylisaukko-oja et al. 2005). |
|
| Publications: |
1 |
3.0
NTRK2
- 
- 