| + |
GRK2 | down-regulates quantity by destabilization 
phosphorylation
|
IGF1R |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276413 |
Ser1278 |
EPGFREVsFYYSEEN |
in vitro |
|
| pmid |
sentence |
| 22509025 |
GRK2 and GRK6 coimmunoprecipitate with IGF-1R and increase IGF-1R serine phosphorylation, promoting β-arrestin1 association. Using immunoprecipitation, confocal microscopy, and FRET analysis, we demonstrated β-arrestin/IGF-1R association to be transient for GRK2 and stable for GRK6. Using bioinformatic studies we identified serines 1248 and 1291 as the major serine phosphorylation sites of the IGF-1R. Targeted mutation of S1248 recapitulates GRK2 modulation, whereas S1291 mutation resembles GRK6 effects on IGF-1R signaling/degradation |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
GRK6 | down-regulates quantity by destabilization
phosphorylation
|
IGF1R |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276412 |
Ser1321 |
LPLPDRHsGHKAENG |
in vitro |
|
| pmid |
sentence |
| 22509025 |
GRK2 and GRK6 coimmunoprecipitate with IGF-1R and increase IGF-1R serine phosphorylation, promoting β-arrestin1 association. Using immunoprecipitation, confocal microscopy, and FRET analysis, we demonstrated β-arrestin/IGF-1R association to be transient for GRK2 and stable for GRK6. Using bioinformatic studies we identified serines 1248 and 1291 as the major serine phosphorylation sites of the IGF-1R. Targeted mutation of S1248 recapitulates GRK2 modulation, whereas S1291 mutation resembles GRK6 effects on IGF-1R signaling/degradation |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SRC | up-regulates 
phosphorylation
|
IGF1R |
0.564 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-45122 |
Tyr1161 |
FGMTRDIyETDYYRK |
Homo sapiens |
|
| pmid |
sentence |
| 8940173 |
Src phosphorylates the insulin-like growth factor type i receptor on the autophosphorylation sites. Requirement for transformation by srcsrc kinase can substitute for the receptor kinase in phosphorylating and activating the igf-i receptor |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-45126 |
Tyr1165 |
RDIYETDyYRKGGKG |
Homo sapiens |
|
| pmid |
sentence |
| 8940173 |
Src phosphorylates the insulin-like growth factor type i receptor on the autophosphorylation sites. Requirement for transformation by srcsrc kinase can substitute for the receptor kinase in phosphorylating and activating the igf-i receptor |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246264 |
Tyr1165 |
RDIYETDyYRKGGKG |
in vitro |
|
| pmid |
sentence |
| 7493944 |
The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-45130 |
Tyr1166 |
DIYETDYyRKGGKGL |
Homo sapiens |
|
| pmid |
sentence |
| 8940173 |
Src phosphorylates the insulin-like growth factor type i receptor on the autophosphorylation sites. Requirement for transformation by srcsrc kinase can substitute for the receptor kinase in phosphorylating and activating the igf-i receptor |
|
| Publications: |
4 |
Organism: |
Homo Sapiens, In Vitro |
| Pathways: | Rhabdomyosarcoma |
| + |
SRC | up-regulates activity
phosphorylation
|
IGF1R |
0.564 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246272 |
Tyr1161 |
FGMTRDIyETDYYRK |
in vitro |
|
| pmid |
sentence |
| 7493944 |
The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246268 |
Tyr1166 |
DIYETDYyRKGGKGL |
in vitro |
|
| pmid |
sentence |
| 7493944 |
The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246276 |
Tyr1346 |
SFDERQPyAHMNGGR |
in vitro |
|
| pmid |
sentence |
| 7493944 |
The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247193 |
Tyr973 |
RLGNGVLyASVNPEY |
in vitro |
|
| pmid |
sentence |
| 8940173 |
The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247197 |
Tyr980 |
YASVNPEyFSAADVY |
in vitro |
|
| pmid |
sentence |
| 8940173 |
The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain. |
|
| Publications: |
5 |
Organism: |
In Vitro |
| Pathways: | Rhabdomyosarcoma |
| + |
IGF1R | up-regulates activity
phosphorylation
|
IGF1R |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-26582 |
Tyr1161 |
FGMTRDIyETDYYRK |
Homo sapiens |
|
| pmid |
sentence |
| 7493944 |
Insulin and insulin-like growth factor (igf-i) receptors are heterotetrameric proteins consisting of two alpha-and two beta-subunits and members of the transmembrane tyrosine kinase receptors. Specific ligand binding to the receptor triggers a cascade of intracellular events, which begins with autophosphorylation of several tyrosine residues of the beta-subunit of the receptor. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246248 |
Tyr1161 |
FGMTRDIyETDYYRK |
in vitro |
|
| pmid |
sentence |
| 8940173 |
The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-26590 |
Tyr1166 |
DIYETDYyRKGGKGL |
Homo sapiens |
|
| pmid |
sentence |
| 7493944 |
Insulin and insulin-like growth factor (igf-i) receptors are heterotetrameric proteins consisting of two alpha-and two beta-subunits and members of the transmembrane tyrosine kinase receptors. Specific ligand binding to the receptor triggers a cascade of intracellular events, which begins with autophosphorylation of several tyrosine residues of the beta-subunit of the receptor. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246244 |
Tyr1166 |
DIYETDYyRKGGKGL |
in vitro |
|
| pmid |
sentence |
| 8940173 |
The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246260 |
Tyr1346 |
SFDERQPyAHMNGGR |
in vitro |
|
| pmid |
sentence |
| 8940173 |
The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246256 |
Tyr980 |
YASVNPEyFSAADVY |
in vitro |
|
| pmid |
sentence |
| 7493944 |
The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinase. We mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens, In Vitro |
| Pathways: | Colorectal Carcinoma, EBV infection, Hepatocellular Tumor, IGF and Myogenesis, Non-small-cell lung cancer (NSCLC), P38 Signaling and Myogenesis, Rhabdomyosarcoma |
| + |
IGF1R | up-regulates
phosphorylation
|
IGF1R |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-26586 |
Tyr1165 |
RDIYETDyYRKGGKG |
Homo sapiens |
|
| pmid |
sentence |
| 7493944 |
Insulin and insulin-like growth factor (IGF-I) receptors are heterotetrameric proteins consisting of two alpha-and two beta-subunits and members of the transmembrane tyrosine kinase receptors. Specific ligand binding to the receptor triggers a cascade of intracellular events, which begins with autophosphorylation of several tyrosine residues of the beta-subunit of the receptor. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246252 |
Tyr973 |
RLGNGVLyASVNPEY |
in vitro |
|
| pmid |
sentence |
| 7493944 |
The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinase. We mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, In Vitro |
| Pathways: | Colorectal Carcinoma, EBV infection, Hepatocellular Tumor, IGF and Myogenesis, Non-small-cell lung cancer (NSCLC), P38 Signaling and Myogenesis, Rhabdomyosarcoma |
| + |
IGF1R | up-regulates
phosphorylation
|
IRS1 |
0.864 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157730 |
Tyr1179 |
GLENGLNyIDLDLVK |
Homo sapiens |
|
| pmid |
sentence |
| 17827393 |
Furthermore, IGF-1 stimulates tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) and IRS-2 and their association with the p85 subunit of phosphoinositide-3 kinase (PI3K). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157734 |
Tyr1229 |
SSEDLSAyASISFQK |
Homo sapiens |
|
| pmid |
sentence |
| 17827393 |
Furthermore, IGF-1 stimulates tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) and IRS-2 and their association with the p85 subunit of phosphoinositide-3 kinase (PI3K). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157738 |
Tyr465 |
GEEELSNyICMGGKG |
Homo sapiens |
|
| pmid |
sentence |
| 17827393 |
Furthermore, IGF-1 stimulates tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) and IRS-2 and their association with the p85 subunit of phosphoinositide-3 kinase (PI3K). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157742 |
Tyr612 |
TLHTDDGyMPMSPGV |
Homo sapiens |
|
| pmid |
sentence |
| 17827393 |
Furthermore, IGF-1 stimulates tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) and IRS-2 and their association with the p85 subunit of phosphoinositide-3 kinase (PI3K). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157746 |
Tyr632 |
GRKGSGDyMPMSPKS |
Homo sapiens |
|
| pmid |
sentence |
| 17827393 |
Furthermore, IGF-1 stimulates tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) and IRS-2 and their association with the p85 subunit of phosphoinositide-3 kinase (PI3K). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157750 |
Tyr896 |
EPKSPGEyVNIEFGS |
Homo sapiens |
|
| pmid |
sentence |
| 17827393 |
Furthermore, IGF-1 stimulates tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) and IRS-2 and their association with the p85 subunit of phosphoinositide-3 kinase (PI3K). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157754 |
Tyr941 |
EETGTEEyMKMDLGP |
Homo sapiens |
|
| pmid |
sentence |
| 17827393 |
Furthermore, IGF-1 stimulates tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) and IRS-2 and their association with the p85 subunit of phosphoinositide-3 kinase (PI3K). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157758 |
Tyr989 |
VPSSRGDyMTMQMSC |
Homo sapiens |
|
| pmid |
sentence |
| 17827393 |
Furthermore, IGF-1 stimulates tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) and IRS-2 and their association with the p85 subunit of phosphoinositide-3 kinase (PI3K). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255104 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15829723 |
IGF-I binding to its receptor activates the kinase activity of the receptor, which then recruits the insulin response substrate-1, causing activation of phosphatidyl-inositol-3 kinase (PI3K) to phosphorylate Akt. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175665 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21798082 |
Binding of IGF1 to its receptor leads to activation of its intrinsic tyrosine kinase and autophosphorylation, thus generating docking sites for insulin receptor substrate (IRS), which is also phosphorylated by the IGF1 receptor. |
|
| Publications: |
10 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| Pathways: | IGF and Myogenesis |
| + |
IGF1R | up-regulates activity
phosphorylation
|
PCNA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277254 |
Tyr133 |
LGIPEQEySCVVKMP |
in vitro |
|
| pmid |
sentence |
| 28924044 |
In vitro MS analysis of PCNA co-incubated with the IGF-1R kinase indicated tyrosine residues 60, 133, and 250 in PCNA as IGF-1R targets, and PCNA phosphorylation was followed by mono- and polyubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277252 |
Tyr250 |
DMGHLKYyLAPKIED |
in vitro |
|
| pmid |
sentence |
| 28924044 |
In vitro MS analysis of PCNA co-incubated with the IGF-1R kinase indicated tyrosine residues 60, 133, and 250 in PCNA as IGF-1R targets, and PCNA phosphorylation was followed by mono- and polyubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277253 |
Tyr60 |
RSEGFDTyRCDRNLA |
in vitro |
|
| pmid |
sentence |
| 28924044 |
In vitro MS analysis of PCNA co-incubated with the IGF-1R kinase indicated tyrosine residues 60, 133, and 250 in PCNA as IGF-1R targets, and PCNA phosphorylation was followed by mono- and polyubiquitination. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
IGF1R | down-regulates activity
phosphorylation
|
CRK |
0.711 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251273 |
Tyr221 |
GGPEPGPyAQPSVNT |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 9480911 |
On activation of the IGF-I receptor, Crk-II binds to phosphorylated tyrosine residues, especially in the juxtamembrane region. As a result of this binding, the IGF-I receptor kinase phosphorylates Tyr-221 of Crk-II, resulting in a change in intramolecular folding and binding of the SH2 domain to the phosphorylated Tyr-221, which causes rapid disassociation of the Crk-II-IGF-I receptor complex. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
IGF1R | up-regulates
phosphorylation
|
PDPK1 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166710 |
Tyr373 |
SEDDEDCyGNYDNLL |
Homo sapiens |
|
| pmid |
sentence |
| 20643654 |
Previous studies indicate that optimal activation of PDK1 requires phosphorylation of Tyr373/376 (11, 12, 14, 17), and growth factor receptor activation leads to PDK1 recruitment to the plasma membrane, followed by sequential phosphorylation of Tyr9 and then Tyr373/376 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236548 |
Tyr373 |
SEDDEDCyGNYDNLL |
in vitro |
|
| pmid |
sentence |
| 20044479 |
IGF-1R Directly Interacts with and Phosphorylates PDK1 in Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166714 |
Tyr376 |
DEDCYGNyDNLLSQF |
Homo sapiens |
|
| pmid |
sentence |
| 20643654 |
Previous studies indicate that optimal activation of PDK1 requires phosphorylation of Tyr373/376, and growth factor receptor activation leads to PDK1 recruitment to the plasma membrane, followed by sequential phosphorylation of Tyr9 and then Tyr373/376 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236544 |
Tyr376 |
DEDCYGNyDNLLSQF |
Homo sapiens |
|
| pmid |
sentence |
| 20044479 |
We have described that upon ligand binding, igf-1r directly interacts with and phosphorylates pdk1 at tyr373/376 |
|
| Publications: |
4 |
Organism: |
Homo Sapiens, In Vitro |
| Pathways: | Hepatocellular Tumor, IGF and Myogenesis, Non-small-cell lung cancer (NSCLC), Rhabdomyosarcoma |
| + |
NVP-ADW742 | down-regulates
chemical inhibition
|
IGF1R |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194883 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SNX5 | down-regulates quantity
binding
|
IGF1R |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269444 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 32150533 |
Here, we discovered that the binding between SNX-BARs and CI-MPR or IGF1R is mediated by the phox-homology (PX) domain of SNX5 or SNX6 and a bipartite motif, termed SNX-BAR-binding motif (SBM), in the cargoes. our studies establish that SNX-BARs function as a direct cargo-selecting module for a large set of transmembrane proteins transiting the endosome, in addition to their roles in phospholipid recognition and biogenesis of tubular structures. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IGF1 | up-regulates activity
binding
|
IGF1R |
0.955 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175662 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21798082 |
Binding of IGF1 to its receptor leads to activation of its intrinsic tyrosine kinase and autophosphorylation, thus generating docking sites for insulin receptor substrate (IRS), which is also phosphorylated by the IGF1 receptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection, IGF and Myogenesis, P38 Signaling and Myogenesis, Rhabdomyosarcoma |
| + |
IGF1R | up-regulates activity 
|
AKT1 |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235373 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 11715022 |
We show that IGF-1 unexpectedly acts via Akt to antagonize calcineurin signalling during myotube hypertrophy. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | IGF and Myogenesis, P38 Signaling and Myogenesis |
| + |
SNX6 | down-regulates quantity
binding
|
IGF1R |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269445 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 32150533 |
Here, we discovered that the binding between SNX-BARs and CI-MPR or IGF1R is mediated by the phox-homology (PX) domain of SNX5 or SNX6 and a bipartite motif, termed SNX-BAR-binding motif (SBM), in the cargoes. our studies establish that SNX-BARs function as a direct cargo-selecting module for a large set of transmembrane proteins transiting the endosome, in addition to their roles in phospholipid recognition and biogenesis of tubular structures. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IGF1R | up-regulates
binding
|
PIK3R1 |
0.706 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179386 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18595745 |
Igf-1 activated both the pi3k and the extracellular signal-regulated kinase [?] (erk [?]) Pathways as evidenced by phosphorylation of either akt or erk1 [?]/2 (respectively) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IGF and Myogenesis |
| + |
NVP-AEW541 | down-regulates
chemical inhibition
|
IGF1R |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194892 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
mir-133a1 | down-regulates quantity 
post transcriptional regulation
|
IGF1R |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261973 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17996649 |
Here, we show that miR-223 is a direct transcriptional target of AML1/ETO. By recruiting chromatin remodeling enzymes at an AML1-binding site on the pre-miR-223 gene, AML1/ETO induces heterochromatic silencing of miR-223. Ectopic miR-223 expression, RNAi against AML1/ETO, or demethylating treatment enhances miR-223 levels and restores cell differentiation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GRB10 | down-regulates
binding
|
IGF1R |
0.728 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174062 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21659604 |
Grb10 negatively regulates growth factor signaling. It binds the insulinand insulin-like growth factor 1 (igf-1) receptors, and mice without grb10 are larger and exhibit enhanced insulin sensitivity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IGF1R | up-regulates
|
calcium(2+) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255100 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15829723 |
Mechanical loading increases IGF-I release, and IGF-I can stimulate Ca2+ influx and thereby activate calcineurin |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IGF1R | up-regulates
phosphorylation
|
IRS4 |
0.643 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-56604 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9553137 |
Insulin-like growth factor i acting through its receptor was as effective as insulin in eliciting tyrosine phosphorylation of irs-4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
2-[[2-[[1-[2-(dimethylamino)-1-oxoethyl]-5-methoxy-2,3-dihydroindol-6-yl]amino]-7H-pyrrolo[2,3-d]pyrimidin-4-yl]amino]-6-fluoro-N-methylbenzamide | down-regulates activity
chemical inhibition
|
IGF1R |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258116 |
|
|
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 |
| + |
IGF1R | up-regulates activity
|
AKT |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244403 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 11715022 |
we show that IGF-1 unexpectedly acts via Akt to antagonize calcineurin signalling during myotube hypertrophy. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | EBV infection, Hepatocellular Tumor, Non-small-cell lung cancer (NSCLC), Rhabdomyosarcoma |
| + |
IGF1R | up-regulates
phosphorylation
|
PIK3C2A |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-32076 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7692086 |
Analysis of the ability of the full-length igfr and its mutant receptors described above to associate with phosphatidylinositol 3 kinase indicated that the association required ptk activity and tyrosine [?] Phosphorylation of the receptors and correlated well with their transforming activities |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-(2,6-difluorophenyl)-5-[3-[2-[5-ethyl-2-methoxy-4-[4-(4-methylsulfonyl-1-piperazinyl)-1-piperidinyl]anilino]-4-pyrimidinyl]-2-imidazo[1,2-a]pyridinyl]-2-methoxybenzamide | down-regulates
chemical inhibition
|
IGF1R |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192880 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Linsitinib | down-regulates activity
chemical inhibition
|
IGF1R |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262028 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 24712877 |
Effects of the antitumor drug OSI-906, a dual inhibitor of IGF-1 receptor and insulin receptor, on the glycemic control, β-cell functions, and β-cell proliferation in male mice |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
IGF1R | up-regulates activity
binding
|
SHC1 |
0.726 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262587 |
|
|
in vitro |
|
| pmid |
sentence |
| 7541045 |
In our present work, we show that both IRS-1 and SHC interact directly with the juxtamembrane region of the IGFIR in a phosphotyrosine-dependent manner. |We propose a model in which IGFIR autophosphorylation of Tyr-950 forms a direct binding site for the amino-terminal receptor binding domains of SHC and IRS-1. This interaction is presumed to facilitate tyrosine phosphorylation of SHC on Tyr-317 leading to GRB2/SOS interaction |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PTPN1 | down-regulates activity
dephosphorylation
|
IGF1R |
0.855 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-115709 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11884589 |
Ptp-1b can regulate igf-ir kinase activity and function and that loss of ptp-1b can enhance igf-i-mediated cell survival, growth, and motility in transformed cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMS-754807 | down-regulates
chemical inhibition
|
IGF1R |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190497 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IGF1R | up-regulates quantity by expression
transcriptional regulation
|
FBN1 |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251863 |
|
|
Rattus norvegicus |
NRK Cell |
| pmid |
sentence |
| 17200203 |
Decorin and IGF-I induce fibrillin-1 protein synthesis in normal rat kidney fibroblasts |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
IGF1 | up-regulates
binding
|
IGF1R |
0.955 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182484 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19029956 |
At the cellular level, the ligands IGF1, IGF2 and insulin bind to various members of the insulin receptor (IR) - IGF1 receptor (IGF1R) family. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection, IGF and Myogenesis, P38 Signaling and Myogenesis, Rhabdomyosarcoma |
| + |
PAX7-FOXO1 | up-regulates quantity by expression
transcriptional regulation
|
IGF1R |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249595 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20663909 |
We also provide the first direct evidence that FGFR4 and IGF1R are the targets for PAX3-FKHR. The map of PAX3-FKHR binding sites provides a framework for understanding the pathogenic roles of PAX3-FKHR, as well as its molecular targets to allow a systematic evaluation of agents against this aggressive rhabdomyosarcoma. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
4-[[(2S)-2-(3-chlorophenyl)-2-hydroxyethyl]amino]-3-[4-methyl-6-(4-morpholinyl)-1,3-dihydrobenzimidazol-2-ylidene]-2-pyridinone | down-regulates
chemical inhibition
|
IGF1R |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190443 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
2-[(3-bromo-5-tert-butyl-4-hydroxyphenyl)methylidene]propanedinitrile | down-regulates
chemical inhibition
|
IGF1R |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189368 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IGF2 | up-regulates activity
binding
|
IGF1R |
0.816 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251495 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22810696 |
These results strongly suggest that the IGF2–IGF1R–IRS2 axis signals to PI3K in CRC and imply that therapeutic targeting of the pathway could act to block PI3K activity in this subset of patients. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Colorectal Carcinoma, Hepatocellular Tumor, Rhabdomyosarcoma |
| + |
PAX3-FOXO1 | up-regulates quantity by expression
transcriptional regulation
|
IGF1R |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251568 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25211658 |
Several deregulated signalling pathways enhance cell growth by modulating cell-cycle regulatory factors in RMS. The most frequently affected signalling pathways include the insulin-like growth factor (IGF), fibroblast growth factor (FGF), hepatocyte growth factor, and platelet-derived growth factor. In ARMS, PAX-FOXO1 activates these pathways by transcriptional activation of receptor genes including IGFR1, FGFR4, MET (c-Met), and PDGFRA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IGF1R | up-regulates
|
SIRPA |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113640 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11779860 |
These studies indicate that igf-ir stimulates phosphorylation of shps-1 which is critical for shp-2 recruitment to the plasma membrane and for its recruitment to the igf-ir |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
3-[8-amino-1-(2-phenyl-7-quinolinyl)-3-imidazo[1,5-a]pyrazinyl]-1-methyl-1-cyclobutanol | down-regulates
chemical inhibition
|
IGF1R |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193675 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
2-[[2-[[1-[2-(dimethylamino)-1-oxoethyl]-5-methoxy-2,3-dihydroindol-6-yl]amino]-7H-pyrrolo[2,3-d]pyrimidin-4-yl]amino]-6-fluoro-N-methylbenzamide | down-regulates
chemical inhibition
|
IGF1R |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192868 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BMS-754807 | down-regulates activity
chemical inhibition
|
IGF1R |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262027 |
|
|
Homo sapiens |
Rhabdomyosarcoma Cell |
| pmid |
sentence |
| 19996272 |
BMS-754807, a small molecule inhibitor of insulin-like growth factor-1R/IR |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IGF1R | up-regulates
phosphorylation
|
IRS2 |
0.795 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-70477 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10471495 |
Our results reveal that igf-1 receptors promote beta-cell development and survival through the irs-2 signalling pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Colorectal Carcinoma |
| + |
BMS-554417 | down-regulates
chemical inhibition
|
IGF1R |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190455 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IGF1R | up-regulates
binding
|
PI3K |
0.686 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252690 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18595745 |
Igf-1 activated both the pi3k and the extracellular signal-regulated kinase [?] (erk [?]) Pathways as evidenced by phosphorylation of either akt or erk1 [?]/2 (respectively) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection, Hepatocellular Tumor, Non-small-cell lung cancer (NSCLC) |
| + |
IGF1R | up-regulates
binding
|
PIK3R3 |
0.804 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52683 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9415396 |
Moreover, we found that the insulin-like growth factor-1 receptor (igf-ir) bound to p55pik;the interaction occurred at the receptor tyrosine 1316 and involved both p55pik sh2 domains. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
INS | up-regulates
binding
|
IGF1R |
0.891 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-22083 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1851182 |
Because of the sequence homology and tertiary structure similarities between proinsulin (pi) and insulin-like growth factor-i (igf-i), it is possible that pi interacts with the igf-i receptor with higher affinity than insulin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
IGF1R | up-regulates
|
CSK |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-64676 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10026153 |
The results suggest that c-src and csk are involved in igf-ir and ir signaling and that the interaction of csk with the igf-ir may play a role in the decrease in c-src activity following igf-i stimulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection |
3.0
IGF1R
- 
- 