| + |
PRKACA | down-regulates 
phosphorylation
|
RET |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167349 |
Ser696 |
SSGARRPsLDSMENQ |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 20682772 |
Furthermore, we find that activation of protein kinase a (pka) by forskolin reduces the recruitment of shp2 to ret and negatively affects ligand-mediated neurite outgrowth. In agreement with this, mutation of ser(696), a known pka phosphorylation site in ret, enhances shp2 binding to the receptor and eliminates the effect of forskolin on ligand-induced outgrowth. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | down-regulates quantity by destabilization
phosphorylation
|
ATF4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276448 |
Thr107 |
LGIDDLEtMPDDLLT |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25795775 |
We observed that RET physically interacted with and phosphorylated ATF4 at tyrosine and threonine residues. Indeed, RET kinase activity was required to inhibit the ATF4-dependent activation of the NOXA gene because the site-specific substitution mutations that block threonine phosphorylation increased ATF4 stability and activated its targets NOXA and PUMA. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276449 |
Thr114 |
TMPDDLLtTLDDTCD |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25795775 |
We observed that RET physically interacted with and phosphorylated ATF4 at tyrosine and threonine residues. Indeed, RET kinase activity was required to inhibit the ATF4-dependent activation of the NOXA gene because the site-specific substitution mutations that block threonine phosphorylation increased ATF4 stability and activated its targets NOXA and PUMA. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276447 |
Thr115 |
MPDDLLTtLDDTCDL |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25795775 |
We observed that RET physically interacted with and phosphorylated ATF4 at tyrosine and threonine residues. Indeed, RET kinase activity was required to inhibit the ATF4-dependent activation of the NOXA gene because the site-specific substitution mutations that block threonine phosphorylation increased ATF4 stability and activated its targets NOXA and PUMA. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276450 |
Thr119 |
LLTTLDDtCDLFAPL |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25795775 |
We observed that RET physically interacted with and phosphorylated ATF4 at tyrosine and threonine residues. Indeed, RET kinase activity was required to inhibit the ATF4-dependent activation of the NOXA gene because the site-specific substitution mutations that block threonine phosphorylation increased ATF4 stability and activated its targets NOXA and PUMA. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates 
phosphorylation
|
MAPK14 |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150875 |
Thr180 |
RHTDDEMtGYVATRW |
Homo sapiens |
|
| pmid |
sentence |
| 17126298 |
Dually phosphorylated on thr-180 and tyr-182 by the map2ks map2k3/mkk3, map2k4/mkk4 and map2k6/mkk6 in response to inflammatory citokines, environmental stress or growth factors, which activates the enzyme. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155377 |
Thr180 |
RHTDDEMtGYVATRW |
Homo sapiens |
|
| pmid |
sentence |
| 17548358 |
Dually phosphorylated on thr-180 and tyr-182 by the map2ks map2k3/mkk3, map2k4/mkk4 and map2k6/mkk6 in response to inflammatory citokines, environmental stress or growth factors, which activates the enzyme. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-40493 |
Thr180 |
RHTDDEMtGYVATRW |
Homo sapiens |
|
| pmid |
sentence |
| 8622669 |
Dually phosphorylated on thr-180 and tyr-182 by the map2ks map2k3/mkk3, map2k4/mkk4 and map2k6/mkk6 in response to inflammatory citokines, environmental stress or growth factors, which activates the enzyme. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-28059 |
Thr180 |
RHTDDEMtGYVATRW |
Homo sapiens |
|
| pmid |
sentence |
| 7535770 |
Dually phosphorylated on thr-180 and tyr-182 by the map2ks map2k3/mkk3, map2k4/mkk4 and map2k6/mkk6 in response to inflammatory citokines, environmental stress or growth factors, which activates the enzyme. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155381 |
Tyr182 |
TDDEMTGyVATRWYR |
Homo sapiens |
|
| pmid |
sentence |
| 17548358 |
Dually phosphorylated on thr-180 and tyr-182 by the map2ks map2k3/mkk3, map2k4/mkk4 and map2k6/mkk6 in response to inflammatory citokines, environmental stress or growth factors, which activates the enzyme. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-28063 |
Tyr182 |
TDDEMTGyVATRWYR |
Homo sapiens |
|
| pmid |
sentence |
| 7535770 |
Dually phosphorylated on thr-180 and tyr-182 by the map2ks map2k3/mkk3, map2k4/mkk4 and map2k6/mkk6 in response to inflammatory citokines, environmental stress or growth factors, which activates the enzyme. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150879 |
Tyr182 |
TDDEMTGyVATRWYR |
Homo sapiens |
|
| pmid |
sentence |
| 17126298 |
Dually phosphorylated on thr-180 and tyr-182 by the map2ks map2k3/mkk3, map2k4/mkk4 and map2k6/mkk6 in response to inflammatory citokines, environmental stress or growth factors, which activates the enzyme. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-40497 |
Tyr182 |
TDDEMTGyVATRWYR |
Homo sapiens |
|
| pmid |
sentence |
| 8622669 |
Dually phosphorylated on thr-180 and tyr-182 by the map2ks map2k3/mkk3, map2k4/mkk4 and map2k6/mkk6 in response to inflammatory citokines, environmental stress or growth factors, which activates the enzyme. |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
phosphorylation
|
RET |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122915 |
Tyr1015 |
MMVKRRDyLDLAAST |
Homo sapiens |
|
| pmid |
sentence |
| 14981541 |
Opn upregulation depended on the integrity of the ret/ptc kinase and tyrosines y1015 and y1062, two major ret/ptc autophosphorylation sites. ret signalling mainly depends on three key tyrosine residues: tyrosine 905, in the activation loop, whose phosphorylation stabilizes the active conformation of the catalytic domain , tyrosine 1015, a docking site for phospholipase citalic gamma and tyrosine 1062. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121141 |
Tyr1062 |
TWIENKLyGMSDPNW |
Homo sapiens |
|
| pmid |
sentence |
| 14711813 |
Mass spectrometric analysis revealed that ret tyr806, tyr809, tyr900, tyr905, tyr981, tyr1062, tyr1090, and tyr1096 were autophosphorylation sitesret short and middle isoforms contain 16 tyrosine residues in their intracellular domains, and ret long isoforms have two additional tyrosines in the c-terminal tail. Among these tyrosines, tyr905, tyr1015, tyr1062, and tyr1096 are thought to be phosphorylated to become binding sites for grb7/grb10, phospholipase c_, shc/snt(frs2)/enigma, and grb2, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121145 |
Tyr1090 |
TNTGFPRyPNDSVYA |
Homo sapiens |
|
| pmid |
sentence |
| 14711813 |
Mass spectrometric analysis revealed that ret tyr(806), tyr(809), tyr(900), tyr(905), tyr(981), tyr(1062), tyr(1090), and tyr(1096) were autophosphorylation sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121149 |
Tyr1096 |
RYPNDSVyANWMLSP |
Homo sapiens |
|
| pmid |
sentence |
| 14711813 |
Mass spectrometric analysis revealed that ret tyr(806), tyr(809), tyr(900), tyr(905), tyr(981), tyr(1062), tyr(1090), and tyr(1096) were autophosphorylation sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121153 |
Tyr806 |
PLLLIVEyAKYGSLR |
Homo sapiens |
|
| pmid |
sentence |
| 14711813 |
Mass spectrometric analysis revealed that ret tyr(806), tyr(809), tyr(900), tyr(905), tyr(981), tyr(1062), tyr(1090), and tyr(1096) were autophosphorylation sites. these facts suggest that tyr806 and tyr809, located in this unique position, play a novel supplemental role for the activation loop upon phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121157 |
Tyr809 |
LIVEYAKyGSLRGFL |
Homo sapiens |
|
| pmid |
sentence |
| 14711813 |
Mass spectrometric analysis revealed that ret tyr(806), tyr(809), tyr(900), tyr(905), tyr(981), tyr(1062), tyr(1090), and tyr(1096) were autophosphorylation sites. these facts suggest that tyr806 and tyr809, located in this unique position, play a novel supplemental role for the activation loop upon phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121161 |
Tyr900 |
FGLSRDVyEEDSYVK |
Homo sapiens |
|
| pmid |
sentence |
| 14711813 |
Mass spectrometric analysis revealed that ret tyr(900) was autophosphorylation site. Tyr900 can partially replace the function of tyr905 as a local switch for kinase activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148992 |
Tyr900 |
FGLSRDVyEEDSYVK |
Homo sapiens |
|
| pmid |
sentence |
| 16928683 |
Mass spectrometric analysis revealed that ret tyr(900) was autophosphorylation site. Tyr900 can partially replace the function of tyr905 as a local switch for kinase activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121165 |
Tyr905 |
DVYEEDSyVKRSQGR |
Homo sapiens |
|
| pmid |
sentence |
| 14711813 |
Mass spectrometric analysis revealed that ret tyr(806), tyr(809), tyr(900), tyr(905), tyr(981), tyr(1062), tyr(1090), and tyr(1096) were autophosphorylation sites. taken together, the results suggest that phosphorylation of tyr981 is not obligatorily required for the catalytic activity but plays a supplementary role in initiating autophosphorylation of tyr905, which brings about the overall kinase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121169 |
Tyr981 |
DNCSEEMyRLMLQCW |
Homo sapiens |
|
| pmid |
sentence |
| 14711813 |
Mass spectrometric analysis revealed that ret tyr806, tyr809, tyr900, tyr905, tyr981, tyr1062, tyr1090, and tyr1096 were autophosphorylation sitesthe results suggest that phosphorylation of tyr981 is not obligatorily required for the catalytic activity but plays a supplementary role in initiating autophosphorylation of tyr905, which brings about the overall kinase activity. |
|
| Publications: |
10 |
Organism: |
Homo Sapiens |
| Pathways: | Thyroid cancer |
| + |
RET |
phosphorylation
|
RET |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248940 |
Tyr1029 |
TPSDSLIyDDGLSEE |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 8621380 |
Based on the phosphopeptide maps, we can identify six tyrosine phosphorylation sites in RET: Tyr-687, Tyr-826, Tyr-1062, Tyr-1096, Tyr-1015, and Tyr-1029. By comparing the peptide map of each mutant to the wild-type receptor, we can tentatively assign each tryptic peptide containing phosphorylation sites to individual P-labeled spots on the two-dimensional map |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248941 |
Tyr687 |
AQAFPVSySSSGARR |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 8621380 |
Based on the phosphopeptide maps, we can identify six tyrosine phosphorylation sites in RET: Tyr-687, Tyr-826, Tyr-1062, Tyr-1096, Tyr-1015, and Tyr-1029. By comparing the peptide map of each mutant to the wild-type receptor, we can tentatively assign each tryptic peptide containing phosphorylation sites to individual P-labeled spots on the two-dimensional map |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248942 |
Tyr826 |
SRKVGPGyLGSGGSR |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 8621380 |
Based on the phosphopeptide maps, we can identify six tyrosine phosphorylation sites in RET: Tyr-687, Tyr-826, Tyr-1062, Tyr-1096, Tyr-1015, and Tyr-1029. By comparing the peptide map of each mutant to the wild-type receptor, we can tentatively assign each tryptic peptide containing phosphorylation sites to individual P-labeled spots on the two-dimensional map |
|
| Publications: |
3 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Thyroid cancer |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
RET |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248700 |
Tyr1062 |
TWIENKLyGMSDPNW |
Homo sapiens |
|
| pmid |
sentence |
| 16778204 |
The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins.|PTPRJ expression induces dephosphorylation of the RET(C634R) and, probably via an indirect mechanism, RET/PTC1 oncoproteins on two key RET autophosphorylation sites (Tyr1062 and Tyr905). This results in a significant decrease of RET-induced Shc and extracellular signal-regulated kinase 1/2 phosphorylation levels |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248701 |
Tyr905 |
DVYEEDSyVKRSQGR |
Homo sapiens |
|
| pmid |
sentence |
| 16778204 |
The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins.|PTPRJ expression induces dephosphorylation of the RET(C634R) and, probably via an indirect mechanism, RET/PTC1 oncoproteins on two key RET autophosphorylation sites (Tyr1062 and Tyr905). This results in a significant decrease of RET-induced Shc and extracellular signal-regulated kinase 1/2 phosphorylation levels |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates
dephosphorylation
|
RET |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147161 |
Tyr1062 |
TWIENKLyGMSDPNW |
Homo sapiens |
|
| pmid |
sentence |
| 16778204 |
Ptprj expression induces dephosphorylation of the ret(c634r) and, probably via an indirect mechanism, ret/ptc1 oncoproteins on two key ret autophosphorylation sites (tyr1062 and tyr905). in line with this finding, adoptive ptprj expression reduced the oncogenic activity of ret |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147165 |
Tyr905 |
DVYEEDSyVKRSQGR |
Homo sapiens |
|
| pmid |
sentence |
| 16778204 |
Ptprj expression induces dephosphorylation of the ret(c634r) and, probably via an indirect mechanism, ret/ptc1 oncoproteins on two key ret autophosphorylation sites (tyr1062 and tyr905). in line with this finding, adoptive ptprj expression reduced the oncogenic activity of ret |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRF | down-regulates
dephosphorylation
|
RET |
0.427 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85170 |
Tyr1062 |
TWIENKLyGMSDPNW |
Homo sapiens |
|
| pmid |
sentence |
| 11121408 |
Lar expression significantly reduced tyrosine-1062 phosphorylation in ret-men2a but not in ret-men2b |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
phosphorylation
|
MAPK1 |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140294 |
Tyr187 |
HTGFLTEyVATRWYR |
Homo sapiens |
|
| pmid |
sentence |
| 16153436 |
We hypothesized that ret could directly phosphorylate fak and erk. erk 2 could be phosphorylated at y187 (y204 in erk1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
phosphorylation
|
MAPK3 |
0.435 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140298 |
Tyr204 |
HTGFLTEyVATRWYR |
Homo sapiens |
|
| pmid |
sentence |
| 16153436 |
We hypothesized that ret could directly phosphorylate fak and erk. erk 2 could be phosphorylated at y187 (y204 in erk1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
phosphorylation
|
AKT |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166514 |
Tyr315 |
TFCGTPEyLAPEVLE |
Homo sapiens |
|
| pmid |
sentence |
| 15994200 |
The PKB Y315 residue, which is known to be phosphorylated by Src tyrosine kinase, was also a major site of phosphorylation by RET/PTC. RET/PTC-mediated tyrosine phosphorylation results in the activation of PKB kinase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244443 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12242309 |
Overexpressed rai resulted in the potentiation of the ret-dependent activation of phosphatidylinositol 3-kinase (pi3k) and akt. The ret/ptc receptor tyrosine kinase that responds to glial cell-line-derived neurotrophic factor also phosphorylated akt tyrosine residue 315 promoting activation of akt |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Thyroid cancer |
| + |
RET | up-regulates
phosphorylation
|
AKT1 |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252619 |
Tyr315 |
TFCGTPEyLAPEVLE |
Homo sapiens |
NIH-3T3 Cell |
| pmid |
sentence |
| 15994200 |
The PKB Y315 residue, which is known to be phosphorylated by Src tyrosine kinase, was also a major site of phosphorylation by RET/PTC. RET/PTC-mediated tyrosine phosphorylation results in the activation of PKB kinase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates activity
phosphorylation
|
AFAP1L2 |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263192 |
Tyr54 |
SSSSDEEyIYMNKVT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19060924 |
RET/PTC induced robust tyrosine phosphorylation of XB130, which promoted its subsequent association with the p85alpha subunit of phosphatidylinositol 3-kinase (PI 3-kinase). We identified tyrosine 54 of XB130 as the major target of RET/PTC-mediated phosphorylation and a critical binding site for the SH2 domains of p85alpha. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
phosphorylation
|
PTK2 |
0.637 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173013 |
Tyr576 |
RYMEDSTyYKASKGK |
Homo sapiens |
|
| pmid |
sentence |
| 21454698 |
The identification of focal adhesion kinase (fak) as a direct substrate for ret kinase revealed (i) a ret-fak transactivation mechanism consisting of direct phosphorylation of fak tyr-576/577 by ret and a reciprocal phosphorylation of ret by fak, which crucially is able to rescue the kinase-impaired ret k758m mutant and (ii) that fak binds ret via its ferm domain. Interestingly, this interaction is abolished upon ret phosphorylation, indicating that ret binding to the ferm domain of fak is a priming step for ret-fak transactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173017 |
Tyr577 |
YMEDSTYyKASKGKL |
Homo sapiens |
|
| pmid |
sentence |
| 21454698 |
The identification of focal adhesion kinase (fak) as a direct substrate for ret kinase revealed (i) a ret-fak transactivation mechanism consisting of direct phosphorylation of fak tyr-576/577 by ret and a reciprocal phosphorylation of ret by fak, which crucially is able to rescue the kinase-impaired ret k758m mutant and (ii) that fak binds ret via its ferm domain. Interestingly, this interaction is abolished upon ret phosphorylation, indicating that ret binding to the ferm domain of fak is a priming step for ret-fak transactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173021 |
Tyr925 |
DRSNDKVyENVTGLV |
Homo sapiens |
|
| pmid |
sentence |
| 21454698 |
Strikingly, when fak and ret kinases were co-incubated in the presence of atp, a marked increased in fak tyr-576/577 and tyr-925 phosphorylation was observed together with a shift in mobility of fak, indicating conversion to an activated state |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates activity
phosphorylation
|
PDPK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235863 |
Tyr9 |
ARTTSQLyDAVPIQS |
Cricetulus griseus |
|
| pmid |
sentence |
| 12738763 |
Ret/ptc (rearranged in transformation/papillary thyroid carcinomas) tyrosine kinase phosphorylates and activates phosphoinositide-dependent kinase 1 (pdk1) ret/ptc phosphorylates a specific tyrosine (y9) residue located in the n-terminal region of pdk1. |
|
| Publications: |
1 |
Organism: |
Cricetulus Griseus |
| Pathways: | Thyroid cancer |
| + |
PTK2 | up-regulates
phosphorylation
|
RET |
0.637 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173009 |
Tyr905 |
DVYEEDSyVKRSQGR |
Homo sapiens |
|
| pmid |
sentence |
| 21454698 |
Focal adhesion kinase (fak) binds ret kinase via its ferm domain, priming a direct and reciprocal ret-fak transactivation mechanism. following gdnf stimulation, increased phosphorylation of fak at tyr-576/577 as well as phosphorylation of ret at tyr-905 was observed. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
binding
|
GRB10 |
0.541 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-41699 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8631863 |
Grb7 and grb10, likely relay signals emanating from ret to other, as yet, unidentified targets within the cell |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
binding
|
DOK5 |
0.622 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109516 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11470823 |
Dok-4 and dok-5 enhance c-ret-dependent activation of mitogen-activated protein kinase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
phosphorylation
|
Gbeta |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269894 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16153436 |
We hypothesized that ret could directly phosphorylate fak and erk. erk 2 could be phosphorylated at y187 (y204 in erk1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
motesanib | down-regulates
chemical inhibition
|
RET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194572 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
binding
|
DOK4 |
0.574 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109513 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 11470823 |
We identified two new family members, dok-4 and dok-5, that can directly associate with y1062 of c-ret dok-4 and dok-5 enhance c-ret-dependent activation of mitogen-activated protein kinase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
binding
|
GRB7 |
0.569 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-41765 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8631863 |
Grb7 and grb10, likely relay signals emanating from ret to other, as yet, unidentified targets within the cell |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
regorafenib | down-regulates activity
chemical inhibition
|
RET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259181 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26254357 |
A novel multi-kinase inhibitor, regorafenib (Figure 1), inhibits vascular endothelial growth factor receptor (VEGFR) 1, VEGFR2, and VEGFR3, that play key roles in angiogenesis, and fibroblast growth factor receptor (FGFR) 1, platelet-derived growth factor receptor-β (PDGFR-β), tyrosine kinase with immunoglobulin and epidermal growth factor homology domain 2 (TIE2) and the mutant oncogenic kinase KIT, RET, B-RAF |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
binding
|
GFRA1 |
0.754 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-77587 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10829012 |
Gdnfr-alpha-ligand complex, together with the tyrosine kinase receptor (cret) forms a functional receptor that activates downstream signal transduction pathways |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
binding
|
SHC1 |
0.655 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36902 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8183561 |
We have shown that the sh2 domain of the adaptor protein shc coimmunoprecipitates with all the ret. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Thyroid cancer |
| + |
NRTN | up-regulates
binding
|
RET |
0.714 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-49122 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9182803 |
A receptor complex comprised of trnr1 (gdnfr alpha) and ret was recently identified and found to be capable of mediating both gdnf and ntn signaling |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
TG101209 | down-regulates
chemical inhibition
|
RET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207269 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
binding
|
DOK6 |
0.646 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-127382 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15286081 |
These data identify dok-6 as a novel dok-4/5-related adaptor molecule that may function in vivo to transduce signals that regulate ret-mediated processes such as axonal projection. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
sorafenib tosylate | down-regulates activity
chemical inhibition
|
RET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259229 |
|
|
in vitro |
|
| pmid |
sentence |
| 16757355 |
Further characterization of sorafenib revealed that this molecule was a multikinase inhibitor that targeted the vascular endothelial growth factor receptor family (VEGFR-2 and VEGFR-3) and platelet-derived growth factor receptor family (PDGFR-beta and Kit), which play key roles in tumor progression and angiogenesis. The in vitro and cellular profile of sorafenib is summarized in Table I. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
RET | up-regulates
phosphorylation
|
ERK1/2 |
0.435 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244643 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16153436 |
We hypothesized that ret could directly phosphorylate fak and erk. erk 2 could be phosphorylated at y187 (y204 in erk1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Thyroid cancer |
| + |
CBLC | down-regulates quantity by destabilization
ubiquitination
|
RET |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278674 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24466333 |
Here we show that Cbl-c binds wild-type and MEN2A isoforms of the receptor tyrosine kinase, RET, and that Cbl-c enhances ubiquitination and degradation of activated RET.|We show that Cbl-c negatively regulates RET by ubiquitinating and downregulating the activated RTK while Enigma positively regulates activated RET by preventing Cbl-c binding to RET and thus preventing RET ubiquitination and degradation while promoting RET mitogenic signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
binding
|
DOK1 |
0.612 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90158 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12087092 |
Dok proteins directly associate with tyrosine 1062 of ret and could be its substrates. Phosphorylation of dok1 is necessary for interaction with ras-gap in vitro and in vivo. Dok1 is a negative regulator for the ras/erk signaling pathway activated by ret. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
vandetanib | down-regulates activity
chemical inhibition
|
RET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258307 |
|
|
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 |
| + |
ponatinib | down-regulates activity
chemical inhibition
|
RET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259275 |
|
|
Homo sapiens |
Leukemia Cell, Medullary Thyroid Carcinoma Cell |
| pmid |
sentence |
| 23526464 |
The RET tyrosine kinase encoding gene acts as a dominantly transforming oncogene in thyroid carcinoma and other malignancies. Ponatinib (AP24534) is an oral ATP-competitive tyrosine kinase inhibitor that is in advanced clinical experimentation in leukemia.Ponatinib is a potent inhibitor of RET kinase and has promising preclinical activity in models of RET-driven medullary thyroid carcinoma. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GDNF | up-regulates
binding
|
RET |
0.91 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-49094 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9182803 |
A receptor complex comprised of trnr1 (gdnfr alpha) and ret was recently identified and found to be capable of mediating both gdnf and ntn signaling |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
lapatinib | down-regulates activity
chemical inhibition
|
RET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257899 |
|
|
Homo sapiens |
HUVEC Cell |
| pmid |
sentence |
| 21443688 |
YN968D1 potently suppressed the kinase activities of VEGFR-2, c-kit and c-src, and inhibited cellular phosphorylation of VEGFR-2, c-kit and PDGFRβ. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
cabozantinib | down-regulates activity
chemical inhibition
|
RET |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259321 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21606412 |
XL184 (cabozantinib) is a potent inhibitor of MET, vascular endothelial growth factor receptor 2 (VEGFR2), and RET, with robust antiangiogenic, antitumor, and anti-invasive effects in preclinical models. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RET | up-regulates
binding
|
FRS2 |
0.677 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-108244 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11360177 |
Tyrosine 1062 in ret provides a site for the interaction of multiple signaling molecules and that the balance of shc and snt/frs2 binding may affect the nature of the intracellular signaling for cell proliferation, differentiation and survival induced by activated ret |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
RET
- 
- 