| + |
PRKG2 | down-regulates activity 
phosphorylation
|
PDGFRB |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277577 |
Ser254 |
WTYPRKEsGRLVEPV |
Homo sapiens |
AGS Cell |
| pmid |
sentence |
| 35066967 |
Secretory PKG II inhibited PDGF‐BB ‐induced PDGFRβ activation via phosphorylating its Ser254. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277401 |
Ser712 |
SDKRRPPsAELYSNA |
Homo sapiens |
Gastric Cancer Cell |
| pmid |
sentence |
| 29935031 |
PKG II inhibited PDGFRβ activation in gastric cancer via phosphorylating Ser712 of this RTK. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN1 | down-regulates activity
dephosphorylation
|
PDGFRB |
0.679 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248416 |
Tyr1009 |
LDTSSVLyTAVQPNE |
in vitro |
|
| pmid |
sentence |
| 7545675 |
Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248417 |
Tyr1021 |
PNEGDNDyIIPLPDP |
in vitro |
|
| pmid |
sentence |
| 7545675 |
Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248413 |
Tyr740 |
TGESDGGyMDMSKDE |
in vitro |
|
| pmid |
sentence |
| 7545675 |
Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248414 |
Tyr751 |
SKDESVDyVPMLDMK |
in vitro |
|
| pmid |
sentence |
| 7545675 |
Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248415 |
Tyr771 |
ADIESSNyMAPYDNY |
in vitro |
|
| pmid |
sentence |
| 7545675 |
Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides |
|
| Publications: |
5 |
Organism: |
In Vitro |
| + |
PDGFRB | up-regulates 
phosphorylation
|
PDGFRB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-18575 |
Tyr1009 |
LDTSSVLyTAVQPNE |
Homo sapiens |
|
| pmid |
sentence |
| 1396585 |
These data show that tyrosine phosphorylation of plc-gamma is dependent on autophosphorylation of the pdgf beta-receptor at tyr1009 and tyr1021. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-18579 |
Tyr1021 |
PNEGDNDyIIPLPDP |
Homo sapiens |
|
| pmid |
sentence |
| 1396585 |
These data show that tyrosine phosphorylation of plc-gamma is dependent on autophosphorylation of the pdgf beta-receptor at tyr1009 and tyr1021. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-16892 |
Tyr771 |
ADIESSNyMAPYDNY |
Homo sapiens |
|
| pmid |
sentence |
| 1314164 |
Mutagenesis studies show that tyr740 and 751 are involved in the pdgf-stimulated binding of phosphatidylinositol (pi) 3 kinase, and tyr771 is required for efficient binding of gap, the gtpase activator of ras. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PTPN1 | down-regulates
dephosphorylation
|
PDGFRB |
0.679 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179064 |
Tyr1009 |
LDTSSVLyTAVQPNE |
Homo sapiens |
|
| pmid |
sentence |
| 18567737 |
Ptp1b blocked pdgf-induced tyr716 and tyr751 phosphorylation of the pdgfr. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179068 |
Tyr1021 |
PNEGDNDyIIPLPDP |
Homo sapiens |
|
| pmid |
sentence |
| 18567737 |
Interestingly, resveratrol increased the activity of protein tyrosine phosphatase ptp1b, which dephosphorylates pdgf-stimulated phosphorylation at tyrosine-751 and tyrosine-716 on pdgfr with concomitant reduction in akt and erk1/2 kinase activity. these results for the first time provide evidence that the stilbene resveratrol targets ptp1b to inhibit pdgfr mitogenic signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179072 |
Tyr716 |
RPPSAELySNALPVG |
Homo sapiens |
|
| pmid |
sentence |
| 18567737 |
Ptp1b blocked pdgf-induced tyr716 and tyr751 phosphorylation of the pdgfr. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179076 |
Tyr751 |
SKDESVDyVPMLDMK |
Homo sapiens |
|
| pmid |
sentence |
| 18567737 |
Ptp1b blocked pdgf-induced tyr716 and tyr751 phosphorylation of the pdgfr. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179080 |
Tyr771 |
ADIESSNyMAPYDNY |
Homo sapiens |
|
| pmid |
sentence |
| 18567737 |
Ptp1b blocked pdgf-induced tyr716 and tyr751 phosphorylation of the pdgfr. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
PDGFRB |
0.545 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248390 |
Tyr1021 |
PNEGDNDyIIPLPDP |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 14966296 |
The PDGF beta receptor is negatively regulated by protein tyrosine phosphatases (PTPs).|In summary, our findings identify TC-PTP as a previously unrecognized negative regulator of PDGF beta receptor signaling and support the general notion that PTPs display site selectivity in their action on tyrosine kinase receptors.The fact that two of the investigated PDGF β receptor sites, Y1021 and Y771, displayed a larger increase in phosphorylation than Y579 and Y751 in TC-PTP ko MEFs indicated that these two sites are preferred substrates for TC-PTP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248389 |
Tyr771 |
ADIESSNyMAPYDNY |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 14966296 |
The PDGF beta receptor is negatively regulated by protein tyrosine phosphatases (PTPs).|In summary, our findings identify TC-PTP as a previously unrecognized negative regulator of PDGF beta receptor signaling and support the general notion that PTPs display site selectivity in their action on tyrosine kinase receptors.The fact that two of the investigated PDGF β receptor sites, Y1021 and Y771, displayed a larger increase in phosphorylation than Y579 and Y751 in TC-PTP ko MEFs indicated that these two sites are preferred substrates for TC-PTP. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
PDGFRB |
0.564 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248704 |
Tyr1021 |
PNEGDNDyIIPLPDP |
Homo sapiens |
|
| pmid |
sentence |
| 12062403 |
Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1|DEP-1 dephosphorylation of original and chimeric phospho-peptides spanning the preferred pY1021 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDGFRB | up-regulates activity
phosphorylation
|
ABL2 |
0.308 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277304 |
Tyr116 |
PNLFVALyDFVASGD |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277302 |
Tyr139 |
EKLRVLGyNQNGEWS |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277306 |
Tyr161 |
QGWVPSNyITPVNSL |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277305 |
Tyr272 |
KCNKPTVyGVSPIHD |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277301 |
Tyr299 |
HKLGGGQyGEVYVGV |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277303 |
Tyr303 |
GGQYGEVyVGVWKKY |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277300 |
Tyr310 |
YVGVWKKySLTVAVK |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Publications: |
7 |
Organism: |
In Vitro |
| + |
PDGFRB | up-regulates activity
phosphorylation
|
GNAI1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277233 |
Tyr154 |
QLNDSAAyYLNDLDR |
in vitro |
|
| pmid |
sentence |
| 33139573 |
RTKs directly phosphorylate Gαi on Y154, 155, and Y320. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277232 |
Tyr155 |
LNDSAAYyLNDLDRI |
in vitro |
|
| pmid |
sentence |
| 33139573 |
RTKs directly phosphorylate Gαi on Y154, 155, and Y320. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277234 |
Tyr320 |
RKDTKEIyTHFTCAT |
in vitro |
|
| pmid |
sentence |
| 33139573 |
RTKs directly phosphorylate Gαi on Y154, 155, and Y320. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PDGFRB | up-regulates
phosphorylation
|
PTK2 |
0.537 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167658 |
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 collectively, this study provides the first example to explain how fak is activated by receptor tyrosine kinases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167662 |
Tyr5 |
yLDPNLNH |
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 collectively, this study provides the first example to explain how fak is activated by receptor tyrosine kinases. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PDGFRB | up-regulates activity
phosphorylation
|
FYN |
0.562 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250253 |
Tyr28 |
SLNQSSGyRYGTDPT |
in vitro |
|
| pmid |
sentence |
| 9425276 |
PDGF-induced phosphorylation of Tyr28 in the N-terminus of Fyn affects Fyn activation. We show here that Fyn, a member of the Src family, is phosphorylated on Tyr28 in the unique N-terminal part of the molecule after interaction with the intracellular domain of the PDGF beta-receptor. Activated Fyn furthermore undergoes autophosphorylation on Tyr30, Tyr39 and Tyr420. When Fyn mutants with Tyr28, Tyr30 or Tyr39 replaced with phenylalanine residues were transfected into NIH3T3 cells a decreased activation after PDGF stimulation was seen, suggesting a functional importance of the N-terminal tyrosine phosphorylation of Fyn. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PDGFRB | up-regulates activity
phosphorylation
|
SRC |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247979 |
Tyr419 |
RLIEDNEyTARQGAK |
Homo sapiens |
Lung Adenocarcinoma Cell |
| pmid |
sentence |
| 15489898 |
The increased Src activity is mainly due to the phosphorylation of Tyr-419, rather than the dephosphorylation of Tyr-530 of Src protein. PDGFR, not FAK or EGFR, appears to be the upstream protein tyrosine kinase responsible for the detachment-induced Src activation in the lung tumor cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDGFRB | up-regulates activity
phosphorylation
|
PTPN11 |
0.739 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250260 |
Tyr542 |
SKRKGHEyTNIKYSL |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 8041791 |
Upon PDGF stimulation, SHPTP2 binds to the PDGFR and becomes tyrosine-phosphorylated. We have identified tyrosine-542 (pY542TNI) as the major in vivo site of SHPTP2 tyrosine phosphorylation. phosphorylation of SHPTP2 couples Grb2 to PDGFR in vivo, providing a mechanism for Ras activation by PDGFR and for positive signaling via SHPTP2 and Csw. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PDGFRB | up-regulates activity
phosphorylation
|
PDGFRB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250254 |
Tyr579 |
VSSDGHEyIYVDPMQ |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 9642269 |
We used two platelet-derived growth factor beta-receptor (beta-PDGFR) mutants to identify events that are required for full engagement (autophosphorylation and activation of the kinase activity) of the beta-PDGFR kinase. The F79/81 receptor (Tyr to Phe substitution at 579 and 581 in the juxtamembrane domain of the receptor) was capable of only very modest ligand-dependent autophosphorylation and also failed to associate with numerous SH2 domain-containing proteins. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250255 |
Tyr581 |
SDGHEYIyVDPMQLP |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 9642269 |
We used two platelet-derived growth factor beta-receptor (beta-PDGFR) mutants to identify events that are required for full engagement (autophosphorylation and activation of the kinase activity) of the beta-PDGFR kinase. The F79/81 receptor (Tyr to Phe substitution at 579 and 581 in the juxtamembrane domain of the receptor) was capable of only very modest ligand-dependent autophosphorylation and also failed to associate with numerous SH2 domain-containing proteins. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250256 |
Tyr716 |
RPPSAELySNALPVG |
in vitro |
|
| pmid |
sentence |
| 8940081 |
The SH2 domain of Grb7 can directly bind to the autophosphorylated PDGF beta-receptor in vitro. Grb7 association to the PDGF beta-receptor was dramatically reduced by replacement of tyrosine residues 716 or 775 with phenylalanine residues. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250257 |
Tyr740 |
TGESDGGyMDMSKDE |
in vitro |
|
| pmid |
sentence |
| 8195171 |
Synthetic peptide analysis revealed that certain autophosphorylation sites in the PDGF beta-receptor (Tyr-579, Tyr-740, Tyr-751, and Tyr-771) were able to mediate the specific binding of the Shc SH2 domain as well as intact Shc proteins. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250258 |
Tyr763 |
DMKGDVKyADIESSN |
Sus scrofa |
|
| pmid |
sentence |
| 10391677 |
Activation of the beta-receptor for platelet-derived growth factor (PDGF) by its ligand leads to autophosphorylation on a number of tyrosine residues. Here we show that Tyr763 in the kinase insert region is a novel autophosphorylation site, which after phosphorylation binds the protein tyrosine phosphatase SHP-2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250259 |
Tyr775 |
SSNYMAPyDNYVPSA |
in vitro |
|
| pmid |
sentence |
| 8940081 |
The SH2 domain of Grb7 can directly bind to the autophosphorylated PDGF beta-receptor in vitro. Grb7 association to the PDGF beta-receptor was dramatically reduced by replacement of tyrosine residues 716 or 775 with phenylalanine residues. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens, In Vitro, Sus Scrofa |
| + |
PDGFRB | up-regulates activity
phosphorylation
|
TNK2 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276854 |
Tyr635 |
PLPPPPAyDDVAQDE |
Homo sapiens |
U-87MG Cell |
| pmid |
sentence |
| 25257795 |
Mutational analysis suggested that Y635 of ACK1 is a PDGFR-β phosphorylation site and that the ACK1 Y635F mutant abrogated the sequential activation of AKT. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABL2 | up-regulates activity
phosphorylation
|
PDGFRB |
0.308 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276140 |
Tyr686 |
IITEYCRyGDLVDYL |
in vitro |
|
| pmid |
sentence |
| 19275932 |
C-Abl phosphorylates three tyrosine residues on PDGFR-beta (Y686, Y934, Y970), while Arg only phosphorylatesY686. Y686 and Y934 reside in PDGFR-beta catalytic domains, while Y970 is in the C-terminal tail. Using site-directed mutagenesis, we show that Abl-dependent phosphorylation of PDGFR-beta activates PDGFR-beta activity, in vitro, but serves to downregulate PDGFR-mediated chemotaxis. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ABL1 | up-regulates activity
phosphorylation
|
PDGFRB |
0.507 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276142 |
Tyr686 |
IITEYCRyGDLVDYL |
in vitro |
|
| pmid |
sentence |
| 19275932 |
C-Abl phosphorylates three tyrosine residues on PDGFR-beta (Y686, Y934, Y970), while Arg only phosphorylatesY686. Y686 and Y934 reside in PDGFR-beta catalytic domains, while Y970 is in the C-terminal tail. Using site-directed mutagenesis, we show that Abl-dependent phosphorylation of PDGFR-beta activates PDGFR-beta activity, in vitro, but serves to downregulate PDGFR-mediated chemotaxis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276141 |
Tyr934 |
AHASDEIyEIMQKCW |
in vitro |
|
| pmid |
sentence |
| 19275932 |
C-Abl phosphorylates three tyrosine residues on PDGFR-beta (Y686, Y934, Y970), while Arg only phosphorylatesY686. Y686 and Y934 reside in PDGFR-beta catalytic domains, while Y970 is in the C-terminal tail. Using site-directed mutagenesis, we show that Abl-dependent phosphorylation of PDGFR-beta activates PDGFR-beta activity, in vitro, but serves to downregulate PDGFR-mediated chemotaxis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276143 |
Tyr970 |
GEGYKKKyQQVDEEF |
in vitro |
|
| pmid |
sentence |
| 19275932 |
C-Abl phosphorylates three tyrosine residues on PDGFR-beta (Y686, Y934, Y970), while Arg only phosphorylatesY686. Y686 and Y934 reside in PDGFR-beta catalytic domains, while Y970 is in the C-terminal tail. Using site-directed mutagenesis, we show that Abl-dependent phosphorylation of PDGFR-beta activates PDGFR-beta activity, in vitro, but serves to downregulate PDGFR-mediated chemotaxis. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
ABL1 | down-regulates
phosphorylation
|
PDGFRB |
0.507 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184552 |
Tyr686 |
IITEYCRyGDLVDYL |
Homo sapiens |
Breast Cancer Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19275932 |
These data are exciting as they indicate that abl kinases not only are activated by pdgfr and promote pdgfr-mediated proliferation and migration,but also act in an intricate negative feedback loop to turn-off pdgfr-mediated chemotaxis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184556 |
Tyr970 |
GEGYKKKyQQVDEEF |
Homo sapiens |
Breast Cancer Cell, Glioblastoma Cell |
| pmid |
sentence |
| 19275932 |
These data are exciting as they indicate that abl kinases not only are activated by pdgfr and promote pdgfr-mediated proliferation and migration,but also act in an intricate negative feedback loop to turn-off pdgfr-mediated chemotaxis. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRG | down-regulates activity
dephosphorylation
|
PDGFRB |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254715 |
Tyr716 |
RPPSAELySNALPVG |
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 |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
PDGFRB |
0.739 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248667 |
Tyr740 |
TGESDGGyMDMSKDE |
in vitro |
|
| pmid |
sentence |
| 7545675 |
Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248668 |
Tyr751 |
SKDESVDyVPMLDMK |
in vitro |
|
| pmid |
sentence |
| 7545675 |
Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248669 |
Tyr771 |
ADIESSNyMAPYDNY |
in vitro |
|
| pmid |
sentence |
| 7545675 |
Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PDGFRB |
phosphorylation
|
PDGFRB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-22993 |
Tyr751 |
SKDESVDyVPMLDMK |
Homo sapiens |
|
| pmid |
sentence |
| 2550144 |
We have identified two platelet-derived growth factor (pdgf)-dependent autophosphorylation sites in the beta subunit of the human pdgf receptor (pdgf-r). The major site of phosphorylation (tyr-857) corresponds to the major autophosphorylation site in many other tyrosine kinases. Tyr-751, which lies within the kinase insert region, is a second in vivo site and the major in vitro site. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-22997 |
Tyr857 |
DIMRDSNyISKGSTF |
Homo sapiens |
|
| pmid |
sentence |
| 2550144 |
We have identified two platelet-derived growth factor (pdgf)-dependent autophosphorylation sites in the beta subunit of the human pdgf receptor (pdgf-r). The major site of phosphorylation (tyr-857) corresponds to the major autophosphorylation site in many other tyrosine kinases. Tyr-751, which lies within the kinase insert region, is a second in vivo site and the major in vitro site. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ACP1 | down-regulates activity
dephosphorylation
|
PDGFRB |
0.314 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248452 |
Tyr857 |
DIMRDSNyISKGSTF |
Homo sapiens |
|
| pmid |
sentence |
| 12149261 |
Insight into the role of low molecular weight phosphotyrosine phosphatase (LMW-PTP) on platelet-derived growth factor receptor (PDGF-r) signaling. LMW-PTP controls PDGF-r kinase activity through TYR-857 dephosphorylation|On the basis of these results, we propose a key role for LMW-PTP in PDGF-r down-regulation through the dephosphorylation of the activation loop Tyr-857, thus determining a general negative regulation of all downstream signals, with the exception of those elicited by internalized receptors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABL1 | down-regulates activity
phosphorylation
|
PDGFRB |
0.507 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260931 |
Tyr934 |
PAHASDEiYEIMQKC |
Homo sapiens |
|
| pmid |
sentence |
| 19275932 |
C-Abl phosphorylates three tyrosine residues on PDGFR-β (Y686, Y934, Y970) | These data are exciting as they indicate that abl kinases not only are activated by pdgfr and promote pdgfr-mediated proliferation and migration,but also act in an intricate negative feedback loop to turn-off pdgfr-mediated chemotaxis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
sorafenib tosylate | down-regulates activity
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259227 |
|
|
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 |
| + |
PDGFRB | up-regulates
binding
|
CRK |
0.591 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185667 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19426560 |
Crk can interact directly with tyrosine kinase receptors and can transmit signals downstream |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75884 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10733900 |
Crk could bind to both pdgf alpha- and beta-receptors in vivo |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
pazopanib hydrochloride | down-regulates activity
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259167 |
|
|
in vitro |
|
| pmid |
sentence |
| 17620431 |
The present study describes an orally bioavailable, ATP-competitive, multitargeted kinase inhibitor, pazopanib (GW786034), and the drug concentration requirement for maximal in vivo activity. Pazopanib is a low nanomolar inhibitor of VEGFR, PDGFR, and c-Kit tyrosine kinases. Pazopanib inhibition of a number of kinases outside of the VEGFR family was also determined. These included Abl1; Akt3; activin-like kinase 6; cyclin-dependent kinase 1/cyclin A; cyclin-dependent kinase 2/cyclin A; c-fms; c-Kit; epidermal growth factor receptor; ErbB2; ErbB4; EphB4; focal adhesion kinase; FGF receptors (FGFR) 1, 2, and 3; Flt-3; glycogen synthase kinase 3; insulin-like growth factor type I receptor; insulin receptor; interleukin-2–inducible T-cell kinase; c-jun NH2-terminal kinases 1, 2, and 3; lymphocyte-specific protein tyrosine kinase (murine); Met; p38α; PDGFRα and PDGFRβ; protein kinase C-β1 and -β2; polo-like kinases 1 and 3; Ret; Src; Syk; Tie-2; and Wee1. All assays were conducted using purified, recombinantly expressed catalytic domains of the kinases. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PDGFRB | up-regulates
phosphorylation
|
PLCG1 |
0.853 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-28179 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7535778 |
Tyrosine phosphorylation has been shown to increase the enzymatic activity of plc-? / we show that the human pdgf ?- And ?-Receptors differ quantitatively in their abilities to associate with and phosphorylate plc-? And to stimulate inositol phosphate production. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Crenolanib | down-regulates
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191124 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
nintedanib | down-regulates activity
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257799 |
|
|
in vitro |
|
| pmid |
sentence |
| 18559524 |
In this report, we describe the preclinical profile of BIBF 1120, a combined VEGFR, FGFR, and PDGFR inhibitor currently entering phase III clinical studies in non–small cell lung carcinoma and other cancers. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
masitinib | down-regulates activity
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258246 |
|
|
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 |
| + |
5-[(Z)-(5-Fluoro-2-oxo-1H-indol-3-ylidene)methyl]-N-[(2S)-2-hydroxy-3-morpholin-4-ylpropyl]-2,4-dimethyl-3H-pyrrole-3-carboxamide | down-regulates activity
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258288 |
|
|
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-259808 |
|
|
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 |
| + |
axitinib | down-regulates activity
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258075 |
|
|
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 |
| + |
PDGFRB | up-regulates
binding
|
RASA1 |
0.561 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-115843 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11896619 |
The gtpase activating protein (gap) of ras binds only to beta-receptors / we have previously shown that the binding site for gtpase activating protein of ras (rasgap) in the pdgf beta-receptor, tyr771, is phosphorylated to a much lower extent in the heterodimeric configuration of pdgf alpha- and beta-receptors, compared to the pdgf beta-receptor homodimer. / the decreased recruitment of the rasgap to the receptor leads to prolonged activation of the ras/map kinase pathway |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDGFRB | up-regulates
binding
|
NCK2 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-64740 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10026169 |
The sh2 domains of grb2, nck, and grb4 all precipitated activated pdgf receptor with similar efficiency. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CBL | down-regulates quantity by destabilization
polyubiquitination
|
PDGFRB |
0.612 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272549 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 10347229 |
Overexpression of wild type Cbl in NIH3T3 cells led to an enhancement of the ligand-dependent ubiquitination and subsequent degradation of the PDGFRbeta, as observed with PDGFRalpha. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272553 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10514377 |
Ubiquitination of the PDGF β-receptor (Rβ) by the c-Cbl RING in an SH2-dependent manner. |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| + |
sunitinib | down-regulates
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163956 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20185585 |
The vegfr/pdgfr inhibitor sunitinib (selleck) was used at 35 mg/kg in citrate-buffered water and administered daily by oral gavage for 7 days. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172926 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21423276 |
The vegfr/pdgfr inhibitor sunitinib (selleck) was used at 35 mg/kg in citrate-buffered water and administered daily by oral gavage for 7 days. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176766 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21993628 |
The vegfr/pdgfr inhibitor sunitinib (selleck) was used at 35 mg/kg in citrate-buffered water and administered daily by oral gavage for 7 days. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
axitinib | down-regulates
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171869 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 21297102 |
Inhibitors for fgf (azd4547), vegf, or pdgf receptors (axitinib), but not that for tgf receptor (ly364947), significantly decreased the abundance of (pcna) in endothelial cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
tandutinib | down-regulates activity
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258299 |
|
|
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 |
| + |
2-Hydroxy-3-[N-[4-[methyl-[2-(4-methylpiperazin-1-yl)acetyl]amino]phenyl]-C-phenylcarbonimidoyl]-1H-indole-6-carboxylic acid | down-regulates activity
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259707 |
|
|
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-258187 |
|
|
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 |
| + |
canertinib | down-regulates activity
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258095 |
|
|
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 |
| + |
imatinib | down-regulates activity
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258227 |
|
|
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 |
| + |
pazopanib | down-regulates activity
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257737 |
|
|
Homo sapiens |
HUVEC Cell |
| pmid |
sentence |
| 18620382 |
Pyrimidine 13 showed good potency against all the human VEGFR receptors with an IC50 of 10, 30, and 47 nM for VEGFR-1, -2, and -3, respectively. Significant activity was also seen against the closely related tyrosine receptor kinases PDGFRβ, c-Kit, FGF-R1, and c-fms with IC50’s of 84, 74, 140, and 146 nM, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
regorafenib | down-regulates activity
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259180 |
|
|
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 |
| + |
PDGFB | up-regulates
binding
|
PDGFRB |
0.903 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107400 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11331882 |
Pdgf-b activates both pdgfr-alpha and pdgfr-beta |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
orantinib | down-regulates
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207441 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
nilotinib | down-regulates activity
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258259 |
|
|
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 |
| + |
Telatinib | down-regulates
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207230 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDGFRB | up-regulates
phosphorylation
|
SHC1 |
0.645 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36906 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8195171 |
In this study, we have characterized the interaction between the pdgf beta-receptor and shc. multiple autophosphorylation sites in the pdgf beta-receptor are responsible for the binding of shc. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MK-2461 | down-regulates
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194390 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDGFRB | up-regulates
binding
|
GRB2 |
0.666 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34765 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7935391 |
A pathway leading to activation of the gtp-binding protein ras involves the adaptor molecule grb2. Here we show that tyr-716, a novel autophosphorylation site in the pdgf beta-receptor kinase insert, mediates direct binding of grb2 in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
linifanib | down-regulates
chemical inhibition
|
PDGFRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193666 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDGFRB | up-regulates
binding
|
NCK1 |
0.622 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-64737 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10026169 |
Growth factor binding to receptor protein tyrosine kinases (r-ptks)1 induces their dimerization and trans-phosphorylation, creating docking sites for proteins containing sh2 and ptb protein interaction domains. Nck binds to the pdgf and egfr receptors (figure 3c). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PDGFRB
- 
- 